{"ComplexID":1,"ComplexName":"BCL6-HDAC4 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P41182;P56524","subunits.Entrez.IDs.":"604;9759","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0051276;GO:0030183;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;chromosome organization;B cell differentiation;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;42.10.03;43.03.07.02.01.01;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;organization of chromosome structure;B-cell;nucleus","PubMed.ID":11929873,"subunits.Protein.name.":"B-cell lymphoma 6 protein ;Histone deacetylase 4","subunits.Gene.name.":"BCL6;HDAC4","subunits.Gene.name.syn.":"BCL5 LAZ3 ZBTB27 ZNF51;KIAA0288","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Transcriptional repression by BCL6 is thought to be achieved in part by recruiting a repressor complex containing histone deacetylases.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2,"ComplexName":"BCL6-HDAC5 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P41182;Q9UQL6","subunits.Entrez.IDs.":"604;10014","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0051276;GO:0030183;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;chromosome organization;B cell differentiation;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;42.10.03;43.03.07.02.01.01;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;organization of chromosome structure;B-cell;nucleus","PubMed.ID":11929873,"subunits.Protein.name.":"B-cell lymphoma 6 protein ;Histone deacetylase 5","subunits.Gene.name.":"BCL6;HDAC5","subunits.Gene.name.syn.":"BCL5 LAZ3 ZBTB27 ZNF51;KIAA0600","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Transcriptional repression by BCL6 is thought to be achieved in part by recruiting a repressor complex containing histone deacetylases.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3,"ComplexName":"BCL6-HDAC7 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P41182;Q8WUI4","subunits.Entrez.IDs.":"604;51564","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0051276;GO:0030183;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;chromosome organization;B cell differentiation;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;42.10.03;43.03.07.02.01.01;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;organization of chromosome structure;B-cell;nucleus","PubMed.ID":11929873,"subunits.Protein.name.":"B-cell lymphoma 6 protein ;Histone deacetylase 7","subunits.Gene.name.":"BCL6;HDAC7","subunits.Gene.name.syn.":"BCL5 LAZ3 ZBTB27 ZNF51;HDAC7A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Transcriptional repression by BCL6 is thought to be achieved in part by recruiting a repressor complex containing histone deacetylases.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":4,"ComplexName":"Multisubunit ACTR coactivator complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q09472;Q92793;Q92831;Q9Y6Q9","subunits.Entrez.IDs.":"2033;1387;8850;8202","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies;MI:0018-two hybrid","GO.ID":"GO:0045893;GO:0023052;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;signaling;nucleus","FunCat.ID":"11.02.03.04.01;30.01;70.10","FunCat.description":"transcription activation;cellular signalling;nucleus","PubMed.ID":9267036,"subunits.Protein.name.":"Histone acetyltransferase p300;CREB-binding protein;Histone acetyltransferase KAT2B;Nuclear receptor coactivator 3","subunits.Gene.name.":"EP300;CREBBP;KAT2B;NCOA3","subunits.Gene.name.syn.":"P300;CBP;PCAF;AIB1, BHLHE42, RAC3, TRAM1, ACTR","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cofactor ACTR binds directly nuclear receptors and stimulates their transcriptional activities in a hormone-dependent fashion.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":9,"ComplexName":"6S-nuclear aryl hydrocarbon (Ah) receptor ligand-activated complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P30561;P53762","subunits.Entrez.IDs.":"11622;11863","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0023052;GO:0009593;GO:0042221;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;signaling;detection of chemical stimulus;response to chemical;nucleus","FunCat.ID":"11.02.03.04;16.03.01;30.01;34.11.03;70.10","FunCat.description":"transcriptional control;DNA binding;cellular signalling;chemoperception and response;nucleus","PubMed.ID":1317062,"subunits.Protein.name.":"Aryl hydrocarbon receptor ;Aryl hydrocarbon receptor nuclear translocator","subunits.Gene.name.":"Ahr;Arnt","subunits.Gene.name.syn.":";None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Arnt contains a basic helix-loop-helix motif, which may be responsible for interacting with both the XRE (xenobiotic responsive element) and the ligand-binding subunit.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":10,"ComplexName":"13S condensin complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95347;Q15003;Q15021;Q9BPX3;Q9NTJ3","subunits.Entrez.IDs.":"10592;23397;9918;64151;10051","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0019- coimmunoprecipitation","GO.ID":"GO:0000279;GO:0007067;GO:0030261;GO:0007059;GO:0051276;GO:0005694","GO.description":"M phase;mitotic nuclear division;chromosome condensation;chromosome segregation;chromosome organization;chromosome","FunCat.ID":"10.03.01.01.11;10.03.04.03;10.03.04.05;42.10.03;70.10.03","FunCat.description":"M phase;chromosome condensation;chromosome segregation/division;organization of chromosome structure;chromosome","PubMed.ID":11136719,"subunits.Protein.name.":"Structural maintenance of chromosomes protein 2 ;Condensin complex subunit 2 ;Condensin complex subunit 1 ;Condensin complex subunit 3 ;Structural maintenance of chromosomes protein 4","subunits.Gene.name.":"SMC2;NCAPH;NCAPD2;NCAPG;SMC4","subunits.Gene.name.syn.":"CAPE SMC2L1;BRRN BRRN1 CAPH KIAA0074;CAPD2 CNAP1 KIAA0159;CAPG NYMEL3;CAPC SMC4L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":11,"ComplexName":"BLOC-3 (biogenesis of lysosome-related organelles complex 3)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q92902;Q9NQG7","subunits.Entrez.IDs.":"3257;89781","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0007032;GO:0007040;GO:0007033","GO.description":"endosome organization;lysosome organization;vacuole organization","FunCat.ID":"42.22;42.25","FunCat.description":"endosome;vacuole or lysosome","PubMed.ID":12847290,"subunits.Protein.name.":"Hermansky-Pudlak syndrome 1 protein;Hermansky-Pudlak syndrome 4 protein","subunits.Gene.name.":"HPS1;HPS4","subunits.Gene.name.syn.":"HPS;KIAA1667","Disease.comment":"HPS1-7 are involved in Hermansky-Pudlak syndrome (HPS), which  comprises at least seven different autosomal recessive disorders (referred to as HPS-1 through -7) that share the clinical manifestations of oculocutaneous albinism combined with platelet storage pool deficiency and do not present with the severe immunodeficiency and giant intracellular granules characteristic of Chediak-Higashi syndrome (PMID:15030569).","Subunits.comment":"None","Complex.comment":"The results suggest that HPS1 and HPS4 are components of a protein complex that regulates the intracellular localization of lysosomes and late endosomes and may function in a BLOC-1-dependent pathway for melanosome biogenesis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":12,"ComplexName":"BLOC-2 (biogenesis of lysosome-related organelles complex 2)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q86YV9;Q969F9;Q9UPZ3","subunits.Entrez.IDs.":"79803;84343;11234","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0029- cosedimentation through density gradients; MI:0071- molecular sieving","GO.ID":"GO:0007032;GO:0007040;GO:0007033","GO.description":"endosome organization;lysosome organization;vacuole organization","FunCat.ID":"42.22;42.25","FunCat.description":"endosome;vacuole or lysosome","PubMed.ID":15030569,"subunits.Protein.name.":"Hermansky-Pudlak syndrome 6 protein ;Hermansky-Pudlak syndrome 3 protein;Hermansky-Pudlak syndrome 5 protein","subunits.Gene.name.":"HPS6;HPS3;HPS5","subunits.Gene.name.syn.":";;AIBP63 KIAA1017","Disease.comment":"HPS1-7 are involved in Hermansky-Pudlak syndrome (HPS), which  comprises at least seven different autosomal recessive disorders (referred to as HPS-1 through -7) that share the clinical manifestations of oculocutaneous albinism combined with platelet storage pool deficiency and do not present with the severe immunodeficiency and giant intracellular granules characteristic of Chediak-Higashi syndrome.","Subunits.comment":"None","Complex.comment":"The results suggest that BLOC-2 is not critical for basal levels of secretion of lysosomal enzymes by fibroblasts.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":13,"ComplexName":"MUS81-CDS1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q92903;Q96NY9","subunits.Entrez.IDs.":"1040;80198","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006281;GO:0006310","GO.description":"DNA repair;DNA recombination","FunCat.ID":"10.01.05.01;10.01.05.03","FunCat.description":"DNA repair;DNA recombination","PubMed.ID":11741546,"subunits.Protein.name.":"Phosphatidate cytidylyltransferase 1 ;Crossover junction endonuclease MUS81","subunits.Gene.name.":"CDS1;MUS81","subunits.Gene.name.syn.":"CDS;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":14,"ComplexName":"BLOC-2 (biogenesis of lysosome-related organelles complex 2)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P59438;Q8BLY7;Q91VB4","subunits.Entrez.IDs.":"246694;20170;12807","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0029- cosedimentation through density gradients; MI:0071- molecular sieving","GO.ID":"GO:0007032;GO:0007040;GO:0007033","GO.description":"endosome organization;lysosome organization;vacuole organization","FunCat.ID":"42.22;42.25","FunCat.description":"endosome;vacuole or lysosome","PubMed.ID":14718540,"subunits.Protein.name.":"Hermansky-Pudlak syndrome 5 protein homolog ;Hermansky-Pudlak syndrome 6 protein homolog ;Hermansky-Pudlak syndrome 3 protein homolog","subunits.Gene.name.":"Hps5;Hps6;Hps3","subunits.Gene.name.syn.":"Ru2;Ru;Coa","Disease.comment":"HPS1-7 are involved in Hermansky-Pudlak syndrome (HPS), which  comprises at least seven different autosomal recessive disorders (referred to as HPS-1 through -7) that share the clinical manifestations of oculocutaneous albinism combined with platelet storage pool deficiency and do not present with the severe immunodeficiency and giant intracellular granules characteristic of Chediak-Higashi syndrome (PMID:15030569).","Subunits.comment":"None","Complex.comment":"The results indicate that the Hps3, Hps5, and Hps6 proteins regulate vesicle trafficking to lysosome-related organelles at the physiological level as components of the BLOC-2 complex.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":15,"ComplexName":"NCOR complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15379;O60907;O75376;Q13227;Q92828;Q9BZK7","subunits.Entrez.IDs.":"8841;6907;9611;2874;7464;79718","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies;MI:0019-coimmunoprecipitation;MI:0069-mass spectrometry studies of complexes","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;organization of chromosome structure;nucleus","PubMed.ID":12628926,"subunits.Protein.name.":"Histone deacetylase 3;F-box-like/WD repeat-containing protein TBL1X;Nuclear receptor corepressor 1;G protein pathway suppressor 2;Coronin-2A;F-box-like/WD repeat-containing protein TBL1XR1","subunits.Gene.name.":"HDAC3;TBL1X;NCOR1;GPS2;CORO2A;TBL1XR1","subunits.Gene.name.syn.":"None;TBL1;KIAA1047;None;IR10 WDR2;IRA1 TBLR1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"By using specific small interference RNAs (siRNAs), the authors demonstrate that HDAC3 is essential, whereas TBL1 and TBLR1 are functionally redundant but essential for repression by unliganded thyroid hormone receptor.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":23,"ComplexName":"BLOC-1 (biogenesis of lysosome-related organelles complex 1)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95295;P78537;Q6QNY0;Q6QNY1;Q8TDH9;Q96EV8;Q9NUP1;Q9UL45","subunits.Entrez.IDs.":"23557;2647;388552;282991;63915;84062;55330;26258","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":15102850,"subunits.Protein.name.":"SNARE-associated protein Snapin;Biogenesis of lysosome-related organelles complex 1 subunit 1;Biogenesis of lysosome-related organelles complex 1 subunit 3 ;Biogenesis of lysosome-related organelles complex 1 subunit 2;Biogenesis of lysosome-related organelles complex 1 subunit 5 ;Dysbindin;Biogenesis of lysosome-related organelles complex 1 subunit 4;Biogenesis of lysosome-related organelles complex 1 subunit 6","subunits.Gene.name.":"SNAPIN;BLOC1S1;BLOC1S3;BLOC1S2;BLOC1S5;DTNBP1;BLOC1S4;BLOC1S6","subunits.Gene.name.syn.":"BLOC1S7 SNAP25BP SNAPAP;BLOS1 GCN5L1 RT14;BLOS3;BLOS2 CEAP;MUTED;BLOC1S8;CNO;PA, PLDN","Disease.comment":"PLDN, MUTED, CNO and DTNBP1 are involved in Hermansky-Pudlak syndrome (HPS), a genetic disorder characterized by hypopigmentation and platelet storage pool deficiency.","Subunits.comment":"None","Complex.comment":"The authors identified Snapin, BLOS1, BLOS2, and BLOS3 as subunits of BLOC-1 and found that the HPS mouse model strain, reduced pigmentation, carries a nonsense mutation in BLOS3. The genes encoding these proteins may underlie the pathogenesis of novel forms of HPS in patients having no detectable mutation in any of the genes that cause HPS types 1-7.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":24,"ComplexName":"BLOC-1 (biogenesis of lysosome-related organelles complex 1)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O55102;Q5U5M8;Q8R015;Q8VED2;Q91WZ8;Q9CWG9;Q9R0C0;Q9Z266","subunits.Entrez.IDs.":"14533;232946;17828;117197;94245;73689;18457;20615","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0071- molecular sieving","GO.ID":"GO:0007032;GO:0007040;GO:0007033","GO.description":"endosome organization;lysosome organization;vacuole organization","FunCat.ID":"42.22;42.25","FunCat.description":"endosome;vacuole or lysosome","PubMed.ID":15102850,"subunits.Protein.name.":"Biogenesis of lysosome-related organelles complex 1 subunit 1 ;Biogenesis of lysosome-related organelles complex 1 subunit 3 ;Biogenesis of lysosome-related organelles complex 1 subunit 5;Biogenesis of lysosome-related organelles complex 1 subunit 4 ;Dysbindin ;Biogenesis of lysosome-related organelles complex 1 subunit 2 ;Biogenesis of lysosome-related organelles complex 1 subunit 6;SNARE-associated protein Snapin","subunits.Gene.name.":"Bloc1s1;Bloc1s3;Bloc1s5;Bloc1s4;Dtnbp1;Bloc1s2;Bloc1s6;Snapin","subunits.Gene.name.syn.":"Gcn5l1;Blos3 Rp;Mu Muted;Cno;Bloc1s8 Sdy;Blos2;P2 Pa Pldn;Bloc1s7 Snap25bp Snapap","Disease.comment":"PLDN, MUTED, CNO and DTNBP1 are involved in Hermansky-Pudlak syndrome (HPS), a genetic disorder characterized by hypopigmentation and platelet storage pool deficiency.","Subunits.comment":"None","Complex.comment":"The authors identified Snapin, BLOS1, BLOS2, and BLOS3 as subunits of BLOC-1 and found that the HPS mouse model strain, reduced pigmentation, carries a nonsense mutation in BLOS3. The genes encoding these proteins may underlie the pathogenesis of novel forms of HPS in patients having no detectable mutation in any of the genes that cause HPS types 1-7.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":25,"ComplexName":"9S-cytosolic aryl hydrocarbon (Ah) receptor non-ligand activated complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O08915;P07901;P11499;P30561","subunits.Entrez.IDs.":"11632;15519;15516;11622","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0030- cross-linking studies","GO.ID":"GO:0006950;GO:0009593;GO:0042221;GO:0005737","GO.description":"response to stress;detection of chemical stimulus;response to chemical;cytoplasm","FunCat.ID":"32.01;34.11.03;70.03","FunCat.description":"stress response;chemoperception and response;cytoplasm","PubMed.ID":1310021,"subunits.Protein.name.":"AH receptor-interacting protein ;Heat shock protein HSP 90-alpha ;Heat shock protein HSP 90-beta ;Aryl hydrocarbon receptor","subunits.Gene.name.":"Aip;Hsp90aa1;Hsp90ab1;Ahr","subunits.Gene.name.syn.":";Hsp86 Hsp86-1 Hspca;Hsp84 Hsp84-1 Hspcb;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors propose that the AhR exists in cytosol as a tetrameric species, while in the nucleus the AhR exists as a heterodimer.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":26,"ComplexName":"Bestrophin-protein phosphatase 2A complex","Organism":"Pig","Synonyms":"None","Cell.line":"eye","subunits.UniProt.IDs.":"P54612;P67776;Q8WMR7","subunits.Entrez.IDs.":"397088;397656;397169","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies;MI:0019-coimmunoprecipitation","GO.ID":"GO:0006821;GO:0005216;GO:0023052;GO:0009583;GO:0009416;GO:0007601","GO.description":"chloride transport;ion channel activity;signaling;detection of light stimulus;response to light stimulus;visual perception","FunCat.ID":"20.01.01.07.09;20.03.01.01;30.01;34.11.01;34.11.01.03","FunCat.description":"chloride transport;ion channels;cellular signalling;photoperception and response;visual transduction","PubMed.ID":12058047,"subunits.Protein.name.":"Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform;Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform;Bestrophin-1","subunits.Gene.name.":"PPP2R1A;PPP2CA;BEST1","subunits.Gene.name.syn.":"None;None;VMD2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The interaction of bestrophin and PP2A suggests that phosphorylation or dephosphorylation of bestrophin may act as the on/off switch for the light peak or modulate its amplitude or timing.","SWISSPROT.organism":"Sus scrofa (Pig);Sus scrofa (Pig);Sus scrofa (Pig)"}
{"ComplexID":27,"ComplexName":"Arp2/3 complex","Organism":"Human","Synonyms":"ARP2/3 protein complex","Cell.line":"None","subunits.UniProt.IDs.":"O15143;O15144;O15145;O15511;P59998;P61158;P61160","subunits.Entrez.IDs.":"10095;10109;10094;10092;10093;10096;10097","Protein.complex.purification.method":"MI:0027-cosedimentation;MI:0071-molecular sieving","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":9359840,"subunits.Protein.name.":"Actin-related protein 2/3 complex subunit 1B;Actin-related protein 2/3 complex subunit 2;Actin-related protein 2/3 complex subunit 3;Actin-related protein 2/3 complex subunit 5;Actin-related protein 2/3 complex subunit 4;Actin-related protein 3;Actin-related protein 2","subunits.Gene.name.":"ARPC1B;ARPC2;ARPC3;ARPC5;ARPC4;ACTR3;ACTR2","subunits.Gene.name.syn.":"ARC41;ARC34;ARC21;ARC16;ARC20;ARP3;ARP2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":28,"ComplexName":"Modulator","Organism":"Bovine","Synonyms":"PA700-dependent proteasome activator","Cell.line":"None","subunits.UniProt.IDs.":"Q2KIW6;Q3SZ19;Q3SZ81","subunits.Entrez.IDs.":"518637;513315;508448","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0226- ion exchange chromatography","GO.ID":"GO:0043161;GO:0006511;GO:0005524;GO:0051098;GO:0005515;GO:0016504;GO:0005737;GO:0005634","GO.description":"proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;ATP binding;regulation of binding;protein binding;peptidase activator activity;cytoplasm;nucleus","FunCat.ID":"14.13.01.01;16.19.03;18.01.07;16.01;18.02.01.01.03;70.03;70.10","FunCat.description":"proteasomal degradation (ubiquitin/proteasomal pathway);ATP binding;regulation by binding / dissociation;protein binding;protease activator;cytoplasm;nucleus","PubMed.ID":8621709,"subunits.Protein.name.":"26S protease regulatory subunit 10B ;26S proteasome non-ATPase regulatory subunit 9 ;PSMC3 protein","subunits.Gene.name.":"PSMC6;PSMD9;PSMC3","subunits.Gene.name.syn.":";;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The modulator has no direct effect on the activity of the proteasome, but enhances PA700 activation of the proteasome by up to 8-fold. This activation is associated with the formation of a proteasome/PA700-containing complex that is significantly larger than that formed in its absence. Two of its proteins, p50 and p42, were also identified as components of PA700.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":29,"ComplexName":"PA28gamma complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P61289","subunits.Entrez.IDs.":"10197","Protein.complex.purification.method":"MI:0226- ion exchange chromatography; MI:0071- molecular sieving","GO.ID":"GO:0043161;GO:0006511;GO:0005515;GO:0051098;GO:0016504;GO:0005737;GO:0005634","GO.description":"proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;protein binding;regulation of binding;peptidase activator activity;cytoplasm;nucleus","FunCat.ID":"14.13.01.01;16.01;18.01.07;18.02.01.01.03;70.03;70.10","FunCat.description":"proteasomal degradation (ubiquitin/proteasomal pathway);protein binding;regulation by binding / dissociation;protease activator;cytoplasm;nucleus","PubMed.ID":9325261,"subunits.Protein.name.":"Proteasome activator complex subunit 3","subunits.Gene.name.":"PSME3","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"According to gel filtration chromatography experiments, the protein complex probably consists of seven identical subunits.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":30,"ComplexName":"PA28 complex","Organism":"Human","Synonyms":"11S REG","Cell.line":"None","subunits.UniProt.IDs.":"Q06323;Q9UL46","subunits.Entrez.IDs.":"5720;5721","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0226- ion exchange chromatography","GO.ID":"GO:0043161;GO:0006511;GO:0051098;GO:0005515;GO:0016504;GO:0005737","GO.description":"proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;regulation of binding;protein binding;peptidase activator activity;cytoplasm","FunCat.ID":"14.13.01.01;18.01.07;16.01;18.02.01.01.03;70.03","FunCat.description":"proteasomal degradation (ubiquitin/proteasomal pathway);regulation by binding / dissociation;protein binding;protease activator;cytoplasm","PubMed.ID":9325261,"subunits.Protein.name.":"Proteasome activator complex subunit 1 ;Proteasome activator complex subunit 2","subunits.Gene.name.":"PSME1;PSME2","subunits.Gene.name.syn.":"IFI5111;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"PA28 is a regulatory complex of the 20S proteasome. It acts as proteasome activator and stimulates cleavage after basic, acidic, and most hydrophobic residues in many peptides.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":31,"ComplexName":"PA28 complex","Organism":"Bovine","Synonyms":"11S REG","Cell.line":"None","subunits.UniProt.IDs.":"Q2KJE7;Q5E9G3","subunits.Entrez.IDs.":"510041;509857","Protein.complex.purification.method":"MI:0226- ion exchange chromatography","GO.ID":"GO:0043161;GO:0006511;GO:0051098;GO:0005515;GO:0016504;GO:0005737","GO.description":"proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;regulation of binding;protein binding;peptidase activator activity;cytoplasm","FunCat.ID":"14.13.01.01;18.01.07;16.01;18.02.01.01.03;70.03","FunCat.description":"proteasomal degradation (ubiquitin/proteasomal pathway);regulation by binding / dissociation;protein binding;protease activator;cytoplasm","PubMed.ID":7989312,"subunits.Protein.name.":"Proteasome ;Proteasome activator complex subunit 2","subunits.Gene.name.":"PSME1;PSME2","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"PA28 is a regulatory complex of the 20S proteasome. It acts as proteasome activator and stimulates cleavage after basic, acidic, and most hydrophobic residues in many peptides.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":32,"ComplexName":"PA700 complex","Organism":"Human","Synonyms":"19S complex","Cell.line":"None","subunits.UniProt.IDs.":"O00231;O00232;O00233;O00487;O43242;O75832;P17980;P35998;P43686;P48556;P51665;P55036;P62191;P62195;P62333;Q13200;Q15008;Q16401;Q99460;Q9UNM6","subunits.Entrez.IDs.":"5717;5718;5715;10213;5709;5716;5702;5701;5704;5714;5713;5710;5700;5705;5706;5708;9861;5711;5707;5719","Protein.complex.purification.method":"MI:0226- ion exchange chromatography; MI:0071- molecular sieving","GO.ID":"GO:0043161;GO:0006511;GO:0005515;GO:0051098;GO:0016504;GO:0005737","GO.description":"proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;protein binding;regulation of binding;peptidase activator activity;cytoplasm","FunCat.ID":"14.13.01.01;16.01;18.01.07;18.02.01.01.03;70.03","FunCat.description":"proteasomal degradation (ubiquitin/proteasomal pathway);protein binding;regulation by binding / dissociation;protease activator;cytoplasm","PubMed.ID":9148964,"subunits.Protein.name.":"26S proteasome non-ATPase regulatory subunit 11 ;26S proteasome non-ATPase regulatory subunit 12 ;26S proteasome non-ATPase regulatory subunit 9 ;26S proteasome non-ATPase regulatory subunit 14 ;26S proteasome non-ATPase regulatory subunit 3 ;26S proteasome non-ATPase regulatory subunit 10 ;26S protease regulatory subunit 6A ;26S protease regulatory subunit 7 ;26S protease regulatory subunit 6B ;26S proteasome non-ATPase regulatory subunit 8 ;26S proteasome non-ATPase regulatory subunit 7 ;26S proteasome non-ATPase regulatory subunit 4 ;26S protease regulatory subunit 4 ;26S protease regulatory subunit 8 ;26S protease regulatory subunit 10B ;26S proteasome non-ATPase regulatory subunit 2 ;26S proteasome non-ATPase regulatory subunit 6 ;26S proteasome non-ATPase regulatory subunit 5 ;26S proteasome non-ATPase regulatory subunit 1 ;26S proteasome non-ATPase regulatory subunit 13","subunits.Gene.name.":"PSMD11;PSMD12;PSMD9;PSMD14;PSMD3;PSMD10;PSMC3;PSMC2;PSMC4;PSMD8;PSMD7;PSMD4;PSMC1;PSMC5;PSMC6;PSMD2;PSMD6;PSMD5;PSMD1;PSMD13","subunits.Gene.name.syn.":";;;POH1;;;TBP1;MSS1;MIP224 TBP7;;MOV34L;MCB1;;SUG1;SUG2;TRAP2;KIAA0107 PFAAP4;KIAA0072;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The proteasome is an essential component of the ATP-dependent proteolytic pathway in eukaryotic cells and is responsible for the degradation of most cellular proteins (for reviews see PMID:8811196 and PMID:10872471). It contains a barrel-shaped proteolytic core complex (the 20S proteasome), and is capped at one or both ends by regulatory complexes like the 19S complex (PMID:11812135), modulator (PMID:8621709), PA28 (PMID:9325261) and PA28gamma (PMID:9325261). Interferon-gamma (IFN-gamma) alters the peptide-degrading specificity of proteasomes and produces an immunoproteasome responsible for accelerated processing of nonself endogenous antigens by inducing the replacement of subunits Psmb5, Psmb6 and Psmb7 by Psmb8, Psmb9 and Psmb10, respectively.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":33,"ComplexName":"Prefoldin","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15212;O60925;P61758;Q99471;Q9NQP4;Q9UHV9","subunits.Entrez.IDs.":"10471;5201;7411;5204;5203;5202","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0050821;GO:0006457;GO:0005515;GO:0030036;GO:0000226;GO:0005737","GO.description":"protein stabilization;protein folding;protein binding;actin cytoskeleton organization;microtubule cytoskeleton organization;cytoplasm","FunCat.ID":"14.01;16.01;42.04.03;42.04.05;70.03","FunCat.description":"protein folding and stabilization;protein binding;actin cytoskeleton;microtubule cytoskeleton;cytoplasm","PubMed.ID":14634002,"subunits.Protein.name.":"Prefoldin subunit 6;Prefoldin subunit 1;Prefoldin subunit 3;Prefoldin subunit 5;Prefoldin subunit 4;Prefoldin subunit 2","subunits.Gene.name.":"PFDN6;PFDN1;VBP1;PFDN5;PFDN4;PFDN2","subunits.Gene.name.syn.":"HKE2 PFD6;PFD1;PFDN3;MM1 PFD5;PFD4;PFD2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":34,"ComplexName":"Aqp4-Dag1-Dmd-Snta1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"cerebellum homogenate","subunits.UniProt.IDs.":"P11530;P47863;Q498T0;Q91XP6","subunits.Entrez.IDs.":"24907;25293;362242;114489","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0015267;GO:0005886","GO.description":"channel activity;plasma membrane","FunCat.ID":"20.03.01;70.02","FunCat.description":"channel / pore class transport;eukaryotic plasma membrane / membrane attached","PubMed.ID":11717465,"subunits.Protein.name.":"Dystrophin;Aquaporin-4;Snta1 protein;Dystroglycan 1","subunits.Gene.name.":"Dmd;Aqp4;Snta1;Dag1","subunits.Gene.name.syn.":"None;None;None;None","Disease.comment":"None","Subunits.comment":"Dystrophin has been described as the astrocyte isoform of dystrophin, Dp71.","Complex.comment":"The authors show that expression and subcellular localization of AQP4 depend on association with the dystrophin complex through a tSSV-PDZ-mediated interaction with alpha -syntrophin.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":36,"ComplexName":"AP1 adaptor complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43747;O75843;P56377;P61966;Q10567;Q96PC3;Q9BXS5;Q9Y6Q5","subunits.Entrez.IDs.":"164;8906;8905;1174;162;130340;8907;10053","Protein.complex.purification.method":"MI:0018- two hybrid","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0016192;GO:0006900;GO:0016050;GO:0006897;GO:0030133","GO.description":"intracellular protein transport;protein targeting;protein transport;vesicle-mediated transport;membrane budding;vesicle organization;endocytosis;transport vesicle","FunCat.ID":"14.04;20.01.10;20.09.07;20.09.07.25;20.09.18.09.01;70.09","FunCat.description":"protein targeting, sorting and translocation;protein transport;vesicular transport (Golgi network, etc.);vesicle formation;endocytosis;intracellular transport vesicles","PubMed.ID":9733768,"subunits.Protein.name.":"AP-1 complex subunit gamma-1;AP-1 complex subunit gamma-like 2 ;AP-1 complex subunit sigma-2 ;AP-1 complex subunit sigma-1A ;AP-1 complex subunit beta-1 ;AP-1 complex subunit sigma-3 ;AP-1 complex subunit mu-1 ;AP-1 complex subunit mu-2","subunits.Gene.name.":"AP1G1;AP1G2;AP1S2;AP1S1;AP1B1;AP1S3;AP1M1;AP1M2","subunits.Gene.name.syn.":"ADTG CLAPG1;;;AP19 CLAPS1;ADTB1 BAM22 CLAPB2;;CLTNM;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This adaptor-related complex participates in a transport step different from that of AP-1. It may function at some trafficking step in the complex pathways between the TGN and the cell surface.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":37,"ComplexName":"Harmonin-CAD23 complex","Organism":"Mouse","Synonyms":"CDH23-harmonin transmembrane complex","Cell.line":"ear","subunits.UniProt.IDs.":"Q99PF4;Q9ES64","subunits.Entrez.IDs.":"22295;72088","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0096-pull down;MI:0018-two hybrid","GO.ID":"GO:0007605;GO:0030154","GO.description":"sensory perception of sound;cell differentiation","FunCat.ID":"36.25.01.03;40.02","FunCat.description":"hearing;cell differentiation","PubMed.ID":12407180,"subunits.Protein.name.":"Cadherin-23;Harmonin","subunits.Gene.name.":"Cdh23;Ush1c","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":38,"ComplexName":"20S proteasome","Organism":"Mouse","Synonyms":"proteasome","Cell.line":"None","subunits.UniProt.IDs.":"O09061;O55234;O70435;P49722;P70195;P99026;Q60692;Q9QUM9;Q9R1P0;Q9R1P1;Q9R1P3;Q9R1P4;Q9Z2U0;Q9Z2U1","subunits.Entrez.IDs.":"19170;19173;19167;19166;19177;19172;19175;26443;26441;26446;26445;26440;26444;26442","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016485;GO:0043161;GO:0006511;GO:0006950;GO:0005737;GO:0005634","GO.description":"protein processing;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;response to stress;cytoplasm;nucleus","FunCat.ID":"14.07.11;14.13.01.01;32.01;70.03;70.10","FunCat.description":"protein processing (proteolytic);proteasomal degradation (ubiquitin/proteasomal pathway);stress response;cytoplasm;nucleus","PubMed.ID":10436176,"subunits.Protein.name.":"Proteasome subunit beta type-1 ;Proteasome subunit beta type-5 ;Proteasome subunit alpha type-3 ;Proteasome subunit alpha type-2 ;Proteasome subunit beta type-7 ;Proteasome subunit beta type-4 ;Proteasome subunit beta type-6 ;Proteasome subunit alpha type-6 ;Proteasome subunit alpha type-4 ;Proteasome subunit beta type-3 ;Proteasome subunit beta type-2 ;Proteasome subunit alpha type-1 ;Proteasome subunit alpha type-7 ;Proteasome subunit alpha type-5","subunits.Gene.name.":"Psmb1;Psmb5;Psma3;Psma2;Psmb7;Psmb4;Psmb6;Psma6;Psma4;Psmb3;Psmb2;Psma1;Psma7;Psma5","subunits.Gene.name.syn.":";;;Lmpc3;Mmc14;Lmp3;Lmp19;;;;;;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The proteasome is an essential component of the ATP-dependent proteolytic pathway in eukaryotic cells and is responsible for the degradation of most cellular proteins (for reviews see PMID:8811196 and PMID:10872471). It contains a barrel-shaped proteolytic core complex (the 20S proteasome), and is capped at one or both ends by regulatory complexes like the 19S complex (PMID:11812135), modulator (PMID:8621709), PA28 (PMID:9325261) and PA28gamma (PMID:9325261). Interferon-gamma (IFN-gamma) alters the peptide-degrading specificity of proteasomes and produces an immunoproteasome responsible for accelerated processing of nonself endogenous antigens by inducing the replacement of subunits Psmb5, Psmb6 and Psmb7 by Psmb8, Psmb9 and Psmb10, respectively.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":39,"ComplexName":"immunoproteasome","Organism":"Mouse","Synonyms":"20S proteasome; proteasome","Cell.line":"None","subunits.UniProt.IDs.":"O09061;O35955;O70435;P28063;P28076;P49722;P99026;Q9QUM9;Q9R1P0;Q9R1P1;Q9R1P3;Q9R1P4;Q9Z2U0;Q9Z2U1","subunits.Entrez.IDs.":"19170;19171;19167;16913;16912;19166;19172;26443;26441;26446;26445;26440;26444;26442","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016485;GO:0043161;GO:0006511;GO:0006950;GO:0019882;GO:0005737;GO:0005634","GO.description":"protein processing;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;response to stress;antigen processing and presentation;cytoplasm;nucleus","FunCat.ID":"14.07.11;14.13.01.01;32.01;36.25.16.03.05;70.03;70.10","FunCat.description":"protein processing (proteolytic);proteasomal degradation (ubiquitin/proteasomal pathway);stress response;antigen presentation / processing;cytoplasm;nucleus","PubMed.ID":10436176,"subunits.Protein.name.":"Proteasome subunit beta type-1 ;Proteasome subunit beta type-10 ;Proteasome subunit alpha type-3 ;Proteasome subunit beta type-8 ;Proteasome subunit beta type-9 ;Proteasome subunit alpha type-2 ;Proteasome subunit beta type-4 ;Proteasome subunit alpha type-6 ;Proteasome subunit alpha type-4 ;Proteasome subunit beta type-3 ;Proteasome subunit beta type-2 ;Proteasome subunit alpha type-1 ;Proteasome subunit alpha type-7 ;Proteasome subunit alpha type-5","subunits.Gene.name.":"Psmb1;Psmb10;Psma3;Psmb8;Psmb9;Psma2;Psmb4;Psma6;Psma4;Psmb3;Psmb2;Psma1;Psma7;Psma5","subunits.Gene.name.syn.":";Lmp10 Mecl1;;Lmp7 Mc13;Lmp2 Ring12;Lmpc3;Lmp3;;;;;;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The proteasome is an essential component of the ATP-dependent proteolytic pathway in eukaryotic cells and is responsible for the degradation of most cellular proteins (for reviews see PMID:8811196 and PMID:10872471). It contains a barrel-shaped proteolytic core complex (the 20S proteasome), and is capped at one or both ends by regulatory complexes like the 19S complex (PMID:11812135), modulator (PMID:8621709), PA28 (PMID:9325261) and PA28gamma (PMID:9325261). Interferon-gamma (IFN-gamma) alters the peptide-degrading specificity of proteasomes and produces an immunoproteasome responsible for accelerated processing of nonself endogenous antigens by inducing the replacement of subunits Psmb5, Psmb6 and Psmb7 by Psmb8, Psmb9 and Psmb10, respectively.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":40,"ComplexName":"COP9 signalosome complex (Gps1, Cops1, Cops2, Cops3, Cops4, Cops5, Cops6, Cops7a, Cops8)","Organism":"Mouse","Synonyms":"signalosome; COP9 complex; CSN complex","Cell.line":"brain","subunits.UniProt.IDs.":"O35864;O88543;O88544;O88545;P61202;Q8VBV7;Q99LD4;Q9CZ04","subunits.Entrez.IDs.":"26754;26572;26891;26893;12848;108679;209318;26894","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":9707402,"subunits.Protein.name.":"COP9 signalosome complex subunit 5;COP9 signalosome complex subunit 3;COP9 signalosome complex subunit 4;COP9 signalosome complex subunit 6;COP9 signalosome complex subunit 2;COP9 signalosome complex subunit 8;COP9 signalosome complex subunit 1;COP9 signalosome complex subunit 7a","subunits.Gene.name.":"Cops5;Cops3;Cops4;Cops6;Cops2;Cops8;Gps1;Cops7a","subunits.Gene.name.syn.":"Csn5, Jab1, Kic2;Csn3;Csn4;Csn6;Csn2, Trip15;Csn8;Cops1, Csn1;Csn7a","Disease.comment":"None","Subunits.comment":"Since the authors did not specify Csn7, we used isoform Csn7a.","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":41,"ComplexName":"Mi-2/NuRD-MTA2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O94776;O95983;P41182;Q13547;Q9BTC8","subunits.Entrez.IDs.":"9219;53615;604;3065;57504","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0051276;GO:0030183;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;chromosome organization;B cell differentiation;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;42.10.03;43.03.07.02.01.01;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;organization of chromosome structure;B-cell;nucleus","PubMed.ID":15454082,"subunits.Protein.name.":"Metastasis-associated protein MTA2;Methyl-CpG-binding domain protein 3;B-cell lymphoma 6 protein ;Histone deacetylase 1;Metastasis-associated protein MTA3","subunits.Gene.name.":"MTA2;MBD3;BCL6;HDAC1;MTA3","subunits.Gene.name.syn.":"MTA1L1 PID;None;BCL5 LAZ3 ZBTB27 ZNF51;RPD3L1;KIAA1266","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":42,"ComplexName":"CASK-MINT-VELI tripartite complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"O35430;Q62915;Q9Z250","subunits.Entrez.IDs.":"83589;29647;85327","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0096-pull down","GO.ID":"GO:0006461;GO:0048489;GO:0016079;GO:0007268;GO:0007155;GO:0030054","GO.description":"protein complex assembly;synaptic vesicle transport;synaptic vesicle exocytosis;synaptic transmission;cell adhesion;cell junction","FunCat.ID":"14.10;20.09.16.09.05;34.03.01;34.07;70.06","FunCat.description":"assembly of protein complexes;synaptic vesicle exocytosis;synaptic transmission;cell adhesion;cell junction","PubMed.ID":9753324,"subunits.Protein.name.":"Amyloid beta A4 precursor protein-binding family A member 1;Peripheral plasma membrane protein CASK;Protein lin-7 homolog A","subunits.Gene.name.":"Apba1;Cask;Lin7a","subunits.Gene.name.syn.":"Mint1 X11;None;Mals1 Veli1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex acts as a nucleation site for the assembly of proteins involved in synaptic vesicle exocytosis and synaptic junctions.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":43,"ComplexName":"Gamma-secretase complex (APH1A, PSEN1, PSENEN, NCSTN variant)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P49768;Q92542;Q96BI3;Q9NZ42","subunits.Entrez.IDs.":"5663;23385;51107;55851","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016485;GO:0016485;GO:0051090;GO:0023052;GO:0007219;GO:0005886;GO:0005794","GO.description":"protein processing;protein processing;regulation of sequence-specific DNA binding transcription factor activity;signaling;Notch signaling pathway;plasma membrane;Golgi apparatus","FunCat.ID":"14.07.11;18.02.09;30.01;30.05.02.14;70.02;70.08","FunCat.description":"protein processing (proteolytic);regulator of transcription factor;cellular signalling;Notch-receptor signalling pathway;eukaryotic plasma membrane / membrane attached;Golgi","PubMed.ID":12740439,"subunits.Protein.name.":"Presenilin-1;Nicastrin;Gamma-secretase subunit APH-1A;Gamma-secretase subunit PEN-2","subunits.Gene.name.":"PSEN1;NCSTN;APH1A;PSENEN","subunits.Gene.name.syn.":"AD3 PS1 PSNL1;KIAA0253;PSF;PEN2","Disease.comment":"Gamma-secretase is causally implicated in Alzheimer's disease.","Subunits.comment":"None","Complex.comment":"Proteolytic cleavage within the hydrophobic transmembrane domains of Notch and APP are intimately associated with a multimeric gamma-secretase complex that contains the presenilin-1 or presenilin-2 and the membrane glycoprotein nicastrin. Three variants of APH1 (APH1A short, APH1A long and APH1B) as well as two presenillin variants (PSEN1 and PSEN2) allow the formation of six different gamma-secretase complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":44,"ComplexName":"CASK-MINT complex","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"B2RUJ5;O70589","subunits.Entrez.IDs.":"319924;12361","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0096- pull down","GO.ID":"GO:0006461;GO:0048489;GO:0016079","GO.description":"protein complex assembly;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"14.10;20.09.16.09.05","FunCat.description":"assembly of protein complexes;synaptic vesicle exocytosis","PubMed.ID":9753324,"subunits.Protein.name.":"Amyloid beta A4 precursor protein-binding family A member 1;Peripheral plasma membrane protein CASK","subunits.Gene.name.":"Apba1;Cask","subunits.Gene.name.syn.":"Mint1, X11, Lin-10;mLin-2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The interaction between CASK and Mint1 was resistant to salt concentrations of up to 3 M NaCl, indicating that binding is not purely electrostatic (PMID:9753324).","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":45,"ComplexName":"Gamma-secretase complex (APH1A, PSEN1, PSENEN, NCSTN variant)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P49768;Q92542;Q96BI3;Q9NZ42","subunits.Entrez.IDs.":"5663;23385;51107;55851","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016485;GO:0016485;GO:0051090;GO:0023052;GO:0007219;GO:0005886;GO:0005794","GO.description":"protein processing;protein processing;regulation of sequence-specific DNA binding transcription factor activity;signaling;Notch signaling pathway;plasma membrane;Golgi apparatus","FunCat.ID":"14.07.11;18.02.09;30.01;30.05.02.14;70.02;70.08","FunCat.description":"protein processing (proteolytic);regulator of transcription factor;cellular signalling;Notch-receptor signalling pathway;eukaryotic plasma membrane / membrane attached;Golgi","PubMed.ID":15274632,"subunits.Protein.name.":"Presenilin-1;Nicastrin;Gamma-secretase subunit APH-1A;Gamma-secretase subunit PEN-2","subunits.Gene.name.":"PSEN1;NCSTN;APH1A;PSENEN","subunits.Gene.name.syn.":"AD3 PS1 PSNL1;KIAA0253;PSF;PEN2","Disease.comment":"Gamma-secretase is causally implicated in Alzheimer's disease.","Subunits.comment":"None","Complex.comment":"Proteolytic cleavage within the hydrophobic transmembrane domains of Notch and APP are intimately associated with a multimeric gamma-secretase complex that contains the presenilin-1 or presenilin-2 and the membrane glycoprotein nicastrin. Three variants of APH1 (APH1A short, APH1A long and APH1B) as well as two presenillin variants (PSEN1 and PSEN2) allow the formation of six different gamma-secretase complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":46,"ComplexName":"AP2 adaptor complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P17427;P62743;P63010;P84092","subunits.Entrez.IDs.":"11772;232910;163;116563","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0114- x-ray crystallography","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0006461;GO:0016192;GO:0006897;GO:0030133","GO.description":"intracellular protein transport;protein targeting;protein transport;protein complex assembly;vesicle-mediated transport;endocytosis;transport vesicle","FunCat.ID":"14.04;20.01.10;14.10;20.09.07;20.09.18.09.01;70.09","FunCat.description":"protein targeting, sorting and translocation;protein transport;assembly of protein complexes;vesicular transport (Golgi network, etc.);endocytosis;intracellular transport vesicles","PubMed.ID":12086608,"subunits.Protein.name.":"AP-2 complex subunit alpha-2 ;AP-2 complex subunit sigma ;AP-2 complex subunit beta ;AP-2 complex subunit mu","subunits.Gene.name.":"Ap2a2;Ap2s1;AP2B1;Ap2m1","subunits.Gene.name.syn.":"Adtab;Ap17 Claps2;ADTB2 CLAPB1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Homo sapiens (Human);Rattus norvegicus (Rat)"}
{"ComplexID":47,"ComplexName":"DNA polymerase alpha-primase complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P20664;P33609;P33610;P33611","subunits.Entrez.IDs.":"19075;18968;19076;18969","Protein.complex.purification.method":"MI:0027- cosedimentation","GO.ID":"GO:0006260;GO:0005634","GO.description":"DNA replication;nucleus","FunCat.ID":"10.01.03;70.10","FunCat.description":"DNA synthesis and replication;nucleus","PubMed.ID":8463324,"subunits.Protein.name.":"DNA primase small subunit;DNA polymerase alpha catalytic subunit;DNA primase large subunit;DNA polymerase alpha subunit B","subunits.Gene.name.":"Prim1;Pola1;Prim2;Pola2","subunits.Gene.name.syn.":"None;Pola;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In growing mouse FM3A cells, the transcripts of the four subunits are present throughout the cell cycle and increase slightly prior to the S phase.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":48,"ComplexName":"RGS7-Gbeta5-Galphaq complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O46470;P21279;P62881","subunits.Entrez.IDs.":"281452;14682;14697","Protein.complex.purification.method":"MI:0055- fluorescent resonance energy transfer","GO.ID":"GO:0007186","GO.description":"G-protein coupled receptor signaling pathway","FunCat.ID":"30.05.02.24","FunCat.description":"G-protein coupled receptor signalling pathway","PubMed.ID":12670932,"subunits.Protein.name.":"Regulator of G-protein signaling 7 ;Guanine nucleotide-binding protein G;Guanine nucleotide-binding protein subunit beta-5","subunits.Gene.name.":"RGS7;Gnaq;Gnb5","subunits.Gene.name.syn.":";;","Disease.comment":"None","Subunits.comment":"For the FRET experiments the authors used murine Gbeta5, bovine RGS7, and murine Galphaq.","Complex.comment":"None","SWISSPROT.organism":"Bos taurus (Bovine);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":49,"ComplexName":"DNMT3B complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60264;O95239;O95347;Q13547;Q96ST3;Q9NTJ3;Q9UBC3","subunits.Entrez.IDs.":"8467;24137;10592;3065;25942;10051;1789","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006306;GO:0006265;GO:0000279;GO:0007067;GO:0007059;GO:0051276;GO:0005694","GO.description":"DNA methylation;DNA topological change;M phase;mitotic nuclear division;chromosome segregation;chromosome organization;chromosome","FunCat.ID":"10.01.09.01;10.01.09.05;10.03.01.01.11;10.03.04.05;42.10.03;70.10.03","FunCat.description":"DNA methylation;DNA conformation modification (e.g. chromatin);M phase;chromosome segregation/division;organization of chromosome structure;chromosome","PubMed.ID":15148359,"subunits.Protein.name.":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5;Chromosome-associated kinesin KIF4A ;Structural maintenance of chromosomes protein 2 ;Histone deacetylase 1;Paired amphipathic helix protein Sin3a;Structural maintenance of chromosomes protein 4 ;DNA","subunits.Gene.name.":"SMARCA5;KIF4A;SMC2;HDAC1;SIN3A;SMC4;DNMT3B","subunits.Gene.name.syn.":"SNF2H WCRF135;KIF4;CAPE SMC2L1;RPD3L1;None;CAPC SMC4L1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":50,"ComplexName":"Rab5 GDP/GTP exchange factor complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O35551;Q9JM13","subunits.Entrez.IDs.":"54189;56715","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006897","GO.description":"endocytosis","FunCat.ID":"20.09.18.09.01","FunCat.description":"endocytosis","PubMed.ID":9323142,"subunits.Protein.name.":"Rab GTPase-binding effector protein 1 ;Rab5 GDP/GTP exchange factor","subunits.Gene.name.":"Rabep1;Rabgef1","subunits.Gene.name.syn.":"Rab5ep Rabpt5 Rabpt5a;Rabex5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex is essential for endocytic membrane fusion.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":51,"ComplexName":"CCT micro-complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P11983;P42932;P80313;P80314;P80315;P80316;P80317;P80318","subunits.Entrez.IDs.":"21454;12469;12468;12461;12464;12465;None;12462","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0050821;GO:0006457;GO:0005515;GO:0005524;GO:0005737","GO.description":"protein stabilization;protein folding;protein binding;ATP binding;cytoplasm","FunCat.ID":"14.01;16.01;16.19.03;70.03","FunCat.description":"protein folding and stabilization;protein binding;ATP binding;cytoplasm","PubMed.ID":9250675,"subunits.Protein.name.":"T-complex protein 1 subunit alpha;T-complex protein 1 subunit theta;T-complex protein 1 subunit eta;T-complex protein 1 subunit beta;T-complex protein 1 subunit delta;T-complex protein 1 subunit epsilon;T-complex protein 1 subunit zeta;T-complex protein 1 subunit gamma","subunits.Gene.name.":"Tcp1;Cct8;Cct7;Cct2;Cct4;Cct5;Cct6a;Cct3","subunits.Gene.name.syn.":"Cct1 Ccta;Cctq;Ccth;Cctb;Cctd;Ccte Kiaa0098;Cct6 Cctz Cctz1;Cctg","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The chaperonins are a family of molecular chaperones involved in protein folding, assembly and transport. The chaperonin-containing TCP-1 (CCT) is abundant in eukaryotic cytosol. CCT micro-complexes have mol. wts ranging from 120 to 250 kDa and are present in cells at lower abundance (<5%) as compared with intact CCT. Sequence analysis of the TriC subunits was shown in PMID:2377466, PMID:7953530 and PMID:7890169.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":52,"ComplexName":"CCT complex (chaperonin containing TCP1 complex)","Organism":"Mouse","Synonyms":"TRiC","Cell.line":"None","subunits.UniProt.IDs.":"P11983;P42932;P80313;P80314;P80315;P80316;P80317;P80318","subunits.Entrez.IDs.":"21454;12469;12468;12461;12464;12465;None;12462","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0091- chromatography technologies","GO.ID":"GO:0050821;GO:0006457;GO:0005515;GO:0005524;GO:0005737","GO.description":"protein stabilization;protein folding;protein binding;ATP binding;cytoplasm","FunCat.ID":"14.01;16.01;16.19.03;70.03","FunCat.description":"protein folding and stabilization;protein binding;ATP binding;cytoplasm","PubMed.ID":9013858,"subunits.Protein.name.":"T-complex protein 1 subunit alpha;T-complex protein 1 subunit theta;T-complex protein 1 subunit eta;T-complex protein 1 subunit beta;T-complex protein 1 subunit delta;T-complex protein 1 subunit epsilon;T-complex protein 1 subunit zeta;T-complex protein 1 subunit gamma","subunits.Gene.name.":"Tcp1;Cct8;Cct7;Cct2;Cct4;Cct5;Cct6a;Cct3","subunits.Gene.name.syn.":"Cct1 Ccta;Cctq;Ccth;Cctb;Cctd;Ccte Kiaa0098;Cct6 Cctz Cctz1;Cctg","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The chaperonins are a family of molecular chaperones involved in protein folding, assembly and transport. The chaperonin-containing TCP-1 (CCT) is abundant in eukaryotic cytosol. The gene product of Cct6b has only been detected in testis, whereas the other Cctz gene, Cctz-1, is expressed in all tissues investigated. Sequence analysis of the TriC subunits was shown in PMID:9013858, PMID:2377466, PMID:7953530 and PMID:7890169.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":53,"ComplexName":"Gbeta5-rgs7 complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P49803;P62882","subunits.Entrez.IDs.":"54296;83579","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0007186","GO.description":"G-protein coupled receptor signaling pathway","FunCat.ID":"30.05.02.24","FunCat.description":"G-protein coupled receptor signalling pathway","PubMed.ID":10723068,"subunits.Protein.name.":"Regulator of G-protein signaling 7 ;Guanine nucleotide-binding protein subunit beta-5","subunits.Gene.name.":"Rgs7;Gnb5","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors demonstrated the presence of the heterodimeric RGS7/Gb5 complex throughout many areas of the adult rat brain, with a role as yet undefined on the dynamics of typical Gbg-mediated neuronal pathway activation/desensitization mechanisms.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":54,"ComplexName":"SIN3 complex","Organism":"Human","Synonyms":"Histone deacetylase complex","Cell.line":"None","subunits.UniProt.IDs.":"O00422;O75446;Q09028;Q13547;Q16576;Q92769;Q96ST3","subunits.Entrez.IDs.":"10284;8819;5928;3065;5931;3066;25942","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0005515;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;protein binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;16.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;protein binding;organization of chromosome structure;nucleus","PubMed.ID":9150135,"subunits.Protein.name.":"Histone deacetylase complex subunit SAP18;Histone deacetylase complex subunit SAP30;Histone-binding protein RBBP4;Histone deacetylase 1;Histone-binding protein RBBP7;Histone deacetylase 2;Paired amphipathic helix protein Sin3a","subunits.Gene.name.":"SAP18;SAP30;RBBP4;HDAC1;RBBP7;HDAC2;SIN3A","subunits.Gene.name.syn.":"None;None;RBAP48;RPD3L1;RBAP46;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":55,"ComplexName":"HDAC4-ERK1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P27361;P56524","subunits.Entrez.IDs.":"5595;9759","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:2001141;GO:0006355;GO:0000165;GO:0051276;GO:0005634","GO.description":"DNA topological change;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;MAPK cascade;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04;30.01.05.01.03;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcriptional control;MAPKKK cascade;organization of chromosome structure;nucleus","PubMed.ID":11114188,"subunits.Protein.name.":"Mitogen-activated protein kinase 3;Histone deacetylase 4","subunits.Gene.name.":"MAPK3;HDAC4","subunits.Gene.name.syn.":"ERK1, PRKM3;KIAA0288","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"ERK1 activity links the Ras-MAPK signal transduction pathway to a mechanism for chromatin remodeling (i.e., histone deacetylation).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":56,"ComplexName":"Elongin (SIII) complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62870;P83941;Q63187","subunits.Entrez.IDs.":"81807;64525;25562","Protein.complex.purification.method":"MI:0227- reverse phase chromatography","GO.ID":"GO:0006354;GO:0045893;GO:0051098;GO:0005515;GO:0043085;GO:0008047;GO:0005634","GO.description":"DNA-templated transcription, elongation;positive regulation of transcription, DNA-templated;regulation of binding;protein binding;positive regulation of catalytic activity;enzyme activator activity;nucleus","FunCat.ID":"11.02.03.01.04;11.02.03.04.01;18.01.07;16.01;18.02.01.01;70.10","FunCat.description":"transcription elongation;transcription activation;regulation by binding / dissociation;protein binding;enzyme activator;nucleus","PubMed.ID":8244996,"subunits.Protein.name.":"Transcription elongation factor B polypeptide 2 ;Transcription elongation factor B polypeptide 1 ;Transcription elongation factor B polypeptide 3","subunits.Gene.name.":"Tceb2;Tceb1;Tceb3","subunits.Gene.name.syn.":";;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The elongin (SIII) complex strongly stimulates the rate of elongation by RNA polymerase II by suppressing transient pausing by polymerase at many sites along the DNA. In mammals, elongin is a trimeric complex. Elongin A is the catalytic subunit. Elongins B and C form a binary complex that is capable of enhancing the transcriptional activity of elongin A.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":57,"ComplexName":"HDAC4-ERK2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P28482;P56524","subunits.Entrez.IDs.":"5594;9759","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:2001141;GO:0006355;GO:0000165;GO:0051276;GO:0005634","GO.description":"DNA topological change;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;MAPK cascade;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04;30.01.05.01.03;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcriptional control;MAPKKK cascade;organization of chromosome structure;nucleus","PubMed.ID":11114188,"subunits.Protein.name.":"Mitogen-activated protein kinase 1;Histone deacetylase 4","subunits.Gene.name.":"MAPK1;HDAC4","subunits.Gene.name.syn.":"ERK2, PRKM1, PRKM2;KIAA0288","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":58,"ComplexName":"SMRT complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15379;O60907;Q13227;Q9BZK7;Q9Y618","subunits.Entrez.IDs.":"8841;6907;2874;79718;9612","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0004-affinity chromatography technologies","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;organization of chromosome structure;nucleus","PubMed.ID":12628926,"subunits.Protein.name.":"Histone deacetylase 3;F-box-like/WD repeat-containing protein TBL1X;G protein pathway suppressor 2;F-box-like/WD repeat-containing protein TBL1XR1;Nuclear receptor corepressor 2","subunits.Gene.name.":"HDAC3;TBL1X;GPS2;TBL1XR1;NCOR2","subunits.Gene.name.syn.":"None;TBL1;None;IRA1 TBLR1;CTG26","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"IR10, a subunit of the N-CoR complex, does not associate with SMRT (NCOR2).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":59,"ComplexName":"AP3 adaptor complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00203;O14617;P53677;P59780;Q13367;Q92572;Q9Y2T2","subunits.Entrez.IDs.":"8546;8943;10947;10239;8120;1176;26985","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0006892;GO:0006897;GO:0005773;GO:0005764","GO.description":"intracellular protein transport;protein targeting;protein transport;post-Golgi vesicle-mediated transport;endocytosis;vacuole;lysosome","FunCat.ID":"14.04;20.01.10;20.09.07.06;20.09.18.09.01;70.25","FunCat.description":"protein targeting, sorting and translocation;protein transport;post Golgi transport;endocytosis;vacuole or lysosome","PubMed.ID":9151686,"subunits.Protein.name.":"AP-3 complex subunit beta-1;AP-3 complex subunit delta-1;AP-3 complex subunit mu-2;AP-3 complex subunit sigma-2;AP-3 complex subunit beta-2;AP-3 complex subunit sigma-1;AP-3 complex subunit mu-1","subunits.Gene.name.":"AP3B1;AP3D1;AP3M2;AP3S2;AP3B2;AP3S1;AP3M1","subunits.Gene.name.syn.":"ADTB3A;None;None;None;None;CLAPS3;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":60,"ComplexName":"Interferon-stimulated gene factor 3 transcription complex ISGF3","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P42224;P52630;Q00978","subunits.Entrez.IDs.":"6772;6773;10379","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:2001141;GO:0006355;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;nucleus","FunCat.ID":"11.02.03.04;70.10","FunCat.description":"transcriptional control;nucleus","PubMed.ID":8943351,"subunits.Protein.name.":"Signal transducer and activator of transcription 1-alpha/beta ;Signal transducer and activator of transcription 2 ;Interferon regulatory factor 9","subunits.Gene.name.":"STAT1;STAT2;IRF9","subunits.Gene.name.syn.":";;ISGF3G","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The p48 and Stat1:2 heterodimer do not associate stably in the absence of DNA.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":61,"ComplexName":"Mi2/NuRD complex","Organism":"Human","Synonyms":"Mi2-beta-histone deacetylase complex","Cell.line":"None","subunits.UniProt.IDs.":"O94776;O95983;Q09028;Q13547;Q14839;Q16576;Q92769","subunits.Entrez.IDs.":"9219;53615;5928;3065;1108;5931;3066","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006265;GO:0045892;GO:0032774;GO:0006473;GO:0006476;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;RNA biosynthetic process;protein acetylation;protein deacetylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;11.02;14.07.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;RNA synthesis;modification by acetylation, deacetylation;organization of chromosome structure;nucleus","PubMed.ID":9790534,"subunits.Protein.name.":"Metastasis-associated protein MTA2;Methyl-CpG-binding domain protein 3;Histone-binding protein RBBP4;Histone deacetylase 1;Chromodomain-helicase-DNA-binding protein 4;Histone-binding protein RBBP7;Histone deacetylase 2","subunits.Gene.name.":"MTA2;MBD3;RBBP4;HDAC1;CHD4;RBBP7;HDAC2","subunits.Gene.name.syn.":"MTA1L1 PID;None;RBAP48;RPD3L1;None;RBAP46;None","Disease.comment":"Dermatomyositis, cancer (PMID:9790534)","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":62,"ComplexName":"MeCP1 complex","Organism":"Human","Synonyms":"Mi2/NuRD-MBD2 complex","Cell.line":"None","subunits.UniProt.IDs.":"O94776;O95983;Q09028;Q13547;Q14839;Q16576;Q92769;Q9UBB5","subunits.Entrez.IDs.":"9219;53615;5928;3065;1108;5931;3066;8932","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006265;GO:0045892;GO:0032774;GO:0006473;GO:0006476;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;RNA biosynthetic process;protein acetylation;protein deacetylation;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;11.02;14.07.04;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;RNA synthesis;modification by acetylation, deacetylation;DNA binding;organization of chromosome structure;nucleus","PubMed.ID":10444591,"subunits.Protein.name.":"Metastasis-associated protein MTA2;Methyl-CpG-binding domain protein 3;Histone-binding protein RBBP4;Histone deacetylase 1;Chromodomain-helicase-DNA-binding protein 4;Histone-binding protein RBBP7;Histone deacetylase 2;Methyl-CpG-binding domain protein 2","subunits.Gene.name.":"MTA2;MBD3;RBBP4;HDAC1;CHD4;RBBP7;HDAC2;MBD2","subunits.Gene.name.syn.":"MTA1L1 PID;None;RBAP48;RPD3L1;None;RBAP46;None;None","Disease.comment":"CHD4 is involved in dermatomyositis (PMID:9790534).","Subunits.comment":"None","Complex.comment":"MeCP1 protein complex represses transcription through preferential binding, remodeling, and deacetylation of methylated nucleosomes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":63,"ComplexName":"Mitotic 14S cohesin 1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60216;Q14683;Q8WVM7;Q9UQE7","subunits.Entrez.IDs.":"5885;8243;10274;9126","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000279;GO:0007067;GO:0007059;GO:0051276;GO:0005694","GO.description":"M phase;mitotic nuclear division;chromosome segregation;chromosome organization;chromosome","FunCat.ID":"10.03.01.01.11;10.03.04.05;42.10.03;70.10.03","FunCat.description":"M phase;chromosome segregation/division;organization of chromosome structure;chromosome","PubMed.ID":11076961,"subunits.Protein.name.":"Double-strand-break repair protein rad21 homolog ;Structural maintenance of chromosomes protein 1A ;Cohesin subunit SA-1 ;Structural maintenance of chromosomes protein 3","subunits.Gene.name.":"RAD21;SMC1A;STAG1;SMC3","subunits.Gene.name.syn.":"HR21 KIAA0078 NXP1;DXS423E KIAA0178 SB1.8 SMC1 SMC1L1;SA1;BAM BMH CSPG6 SMC3L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results suggest that vertebrate cohesins are regulated by a novel prophase pathway which is distinct from the APC pathway that controls cohesins in yeast.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":64,"ComplexName":"Mitotic 14S cohesin 2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60216;Q14683;Q8N3U4;Q9UQE7","subunits.Entrez.IDs.":"5885;8243;10735;9126","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000279;GO:0007067;GO:0051276;GO:0005634","GO.description":"M phase;mitotic nuclear division;chromosome organization;nucleus","FunCat.ID":"10.03.01.01.11;42.10.03;70.10","FunCat.description":"M phase;organization of chromosome structure;nucleus","PubMed.ID":11076961,"subunits.Protein.name.":"Double-strand-break repair protein rad21 homolog ;Structural maintenance of chromosomes protein 1A ;Cohesin subunit SA-2 ;Structural maintenance of chromosomes protein 3","subunits.Gene.name.":"RAD21;SMC1A;STAG2;SMC3","subunits.Gene.name.syn.":"HR21 KIAA0078 NXP1;DXS423E KIAA0178 SB1.8 SMC1 SMC1L1;SA2;BAM BMH CSPG6 SMC3L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":65,"ComplexName":"Multiprotein trafficking complex","Organism":"Rat","Synonyms":"SAP97-CASK-VELI-MINT1 complex","Cell.line":"brain","subunits.UniProt.IDs.":"O35430;P52188;Q62696;Q62915;Q792I0","subunits.Entrez.IDs.":"83589;117052;25252;29647;60442","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0096- pull down","GO.ID":"GO:0008324;GO:0006812;GO:0015267;GO:0050896","GO.description":"cation transmembrane transporter activity;cation transport;channel activity;response to stimulus","FunCat.ID":"20.01.01.01;20.03.01;36.25","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);channel / pore class transport;animal specific systemic sensing and response","PubMed.ID":14960569,"subunits.Protein.name.":"Amyloid beta A4 precursor protein-binding family A member 1;ATP-sensitive inward rectifier potassium channel 12 ;Disks large homolog 1;Peripheral plasma membrane protein CASK;Protein lin-7 homolog C","subunits.Gene.name.":"Apba1;Kcnj12;Dlg1;Cask;Lin7c","subunits.Gene.name.syn.":"Mint1 X11;Irk2;Dlgh1;None;Mals3 Veli3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This macromolecular complex participates in trafficking and plasma membrane localization of Kir2 channels (PMID:14960569).","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":66,"ComplexName":"TRAP complex","Organism":"Human","Synonyms":"thyroid hormone receptor-associated protein complex","Cell.line":"None","subunits.UniProt.IDs.":"O60244;O75448;P10827;Q15648;Q93074;Q9NVC6;Q9Y2W1;Q9Y2X0","subunits.Entrez.IDs.":"9282;9862;7067;5469;9968;9440;9967;10025","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies;MI:0047-far western blotting","GO.ID":"GO:0045893;GO:0030545;GO:0009755;GO:0023052;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;receptor regulator activity;hormone-mediated signaling pathway;signaling;nucleus","FunCat.ID":"11.02.03.04.01;18.02.07;30.01.09.08;30.01;70.10","FunCat.description":"transcription activation;regulator of receptor activity;hormone mediated signal transduction;cellular signalling;nucleus","PubMed.ID":8710870,"subunits.Protein.name.":"Mediator of RNA polymerase II transcription subunit 14;Mediator of RNA polymerase II transcription subunit 24;Thyroid hormone receptor alpha;Mediator of RNA polymerase II transcription subunit 1;Mediator of RNA polymerase II transcription subunit 12;Mediator of RNA polymerase II transcription subunit 17;Thyroid hormone receptor-associated protein 3;Mediator of RNA polymerase II transcription subunit 16","subunits.Gene.name.":"MED14;MED24;THRA;MED1;MED12;MED17;THRAP3;MED16","subunits.Gene.name.syn.":"ARC150 CRSP2 CXorf4 DRIP150 EXLM1 RGR1 TRAP170;ARC100 CRSP4 DRIP100 KIAA0130 THRAP4 TRAP100;EAR7 ERBA1 NR1A1 THRA1 THRA2;ARC205 CRSP1 CRSP200 DRIP205 DRIP230 PBP PPARBP PPARGBP RB18A TRAP220 TRIP2;ARC240 CAGH45 HOPA KIAA0192 TNRC11 TRAP230;ARC77 CRSP6 DRIP77 DRIP80 TRAP80;TRAP150;DRIP92 THRAP5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The human thyroid hormone receptor-associated protein (TRAP) complex is a coactivator for nuclear receptors. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":67,"ComplexName":"AP4 adaptor complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00189;Q9UPM8;Q9Y587;Q9Y6B7","subunits.Entrez.IDs.":"9179;23431;11154;10717","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0005515;GO:0006892;GO:0006897;GO:0030133;GO:0005794","GO.description":"intracellular protein transport;protein targeting;protein transport;protein binding;post-Golgi vesicle-mediated transport;endocytosis;transport vesicle;Golgi apparatus","FunCat.ID":"14.04;20.01.10;16.01;20.09.07.06;20.09.18.09.01;70.09;70.08","FunCat.description":"protein targeting, sorting and translocation;protein transport;protein binding;post Golgi transport;endocytosis;intracellular transport vesicles;Golgi","PubMed.ID":10436028,"subunits.Protein.name.":"AP-4 complex subunit mu-1 ;AP-4 complex subunit epsilon-1 ;AP-4 complex subunit sigma-1 ;AP-4 complex subunit beta-1","subunits.Gene.name.":"AP4M1;AP4E1;AP4S1;AP4B1","subunits.Gene.name.syn.":"MUARP2;;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Adaptor protein complexes (APs) function as vesicle coat components in different membrane traffic pathways.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":68,"ComplexName":"BCDX2 complex","Organism":"Human","Synonyms":"RAD51B-RAD51C-RAD51D-XRCC2 complex","Cell.line":"None","subunits.UniProt.IDs.":"O15315;O43502;O43543;O75771","subunits.Entrez.IDs.":"5890;5889;7516;5892","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0019- coimmunoprecipitation; MI:0027- cosedimentation","GO.ID":"GO:0006281;GO:0006310;GO:0003677;GO:0005524;GO:0006974;GO:0005634","GO.description":"DNA repair;DNA recombination;DNA binding;ATP binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;10.01.05.03;16.03.01;16.19.03;32.01.09;70.10","FunCat.description":"DNA repair;DNA recombination;DNA binding;ATP binding;DNA damage response;nucleus","PubMed.ID":15141025,"subunits.Protein.name.":"DNA repair protein RAD51 homolog 2 ;DNA repair protein RAD51 homolog 3 ;DNA repair protein XRCC2 ;DNA repair protein RAD51 homolog 4","subunits.Gene.name.":"RAD51B;RAD51C;XRCC2;RAD51D","subunits.Gene.name.syn.":"RAD51L1 REC2;RAD51L2;;RAD51L3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":69,"ComplexName":"ApoB RNA editing enzyme complex","Organism":"Rat","Synonyms":"None","Cell.line":"liver","subunits.UniProt.IDs.":"P38483;Q923K9;Q99PF5","subunits.Entrez.IDs.":"25383;170912;171137","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0016556;GO:0003723","GO.description":"mRNA modification;RNA binding","FunCat.ID":"11.06.03;16.03.03","FunCat.description":"mRNA modification;RNA binding","PubMed.ID":10781591,"subunits.Protein.name.":"C->U-editing enzyme APOBEC-1;APOBEC1 complementation factor;Far upstream element-binding protein 2","subunits.Gene.name.":"Apobec1;A1cf;Khsrp","subunits.Gene.name.syn.":"None;Acf Asp;Fubp2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In rat liver, ASP is apparently associated with KSRP, which may confer stability to the editing enzyme-complex with its substrate apoB RNA serving as an additional auxiliary component.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":70,"ComplexName":"CLIC4 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P07335;P39052;P60711;P62260;P63102;P68370;Q9Z0W7","subunits.Entrez.IDs.":"24264;25751;81822;29753;25578;64158;83718","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0004- affinity chromatography technologies; MI:0069- mass spectrometry studies of complexes; MI:0096- pull down","GO.ID":"GO:0008509;GO:0006820;GO:0005216;GO:0050801;GO:0006873;GO:0019898;GO:0005618","GO.description":"anion transmembrane transporter activity;anion transport;ion channel activity;ion homeostasis;cellular ion homeostasis;extrinsic component of membrane;cell wall","FunCat.ID":"20.01.01.07;20.03.01.01;34.01;42.27.03;70.01","FunCat.description":"anion transport ;ion channels;homeostasis;cell membrane or cell wall attached;cell wall","PubMed.ID":11563969,"subunits.Protein.name.":"Creatine kinase B-type ;Dynamin-2 ;Actin, cytoplasmic 1;14-3-3 protein epsilon ;14-3-3 protein zeta/delta ;Tubulin alpha-1A chain;Chloride intracellular channel protein 4","subunits.Gene.name.":"Ckb;Dnm2;Actb;Ywhae;Ywhaz;Tuba1a;Clic4","subunits.Gene.name.syn.":"Ckbb;Dyn2;None;;Msfs1;Tuba1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":71,"ComplexName":"MRN complex (MRE11-RAD50-NBS1 complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60934;P49959;Q92878","subunits.Entrez.IDs.":"4683;4361;10111","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006308;GO:0006281;GO:0000075;GO:0006974;GO:0005634","GO.description":"DNA catabolic process;DNA repair;cell cycle checkpoint;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"01.03.16.03;10.01.05.01;10.03.01.03;32.01.09;70.10","FunCat.description":"DNA degradation;DNA repair;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA damage response;nucleus","PubMed.ID":10612394,"subunits.Protein.name.":"Nibrin ;Double-strand break repair protein MRE11A ;DNA repair protein RAD50","subunits.Gene.name.":"NBN;MRE11A;RAD50","subunits.Gene.name.syn.":"NBS NBS1 P95;HNGS1 MRE11;","Disease.comment":"Rad50-MRE11-p95 protein complex is involved in Nijmegen breakage syndrome.","Subunits.comment":"None","Complex.comment":"The implication of hMre11/hRad50/p95 protein complex in NBS reveals a direct molecular link between DSB repair and cell cycle checkpoint functions.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":72,"ComplexName":"R/M complex (RAD50-MRE11 complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P49959;Q92878","subunits.Entrez.IDs.":"4361;10111","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0006308;GO:0006281;GO:0003677;GO:0006974;GO:0051276;GO:0005634","GO.description":"DNA catabolic process;DNA repair;DNA binding;cellular response to DNA damage stimulus;chromosome organization;nucleus","FunCat.ID":"01.03.16.03;10.01.05.01;16.03.01;32.01.09;42.10.03;70.10","FunCat.description":"DNA degradation;DNA repair;DNA binding;DNA damage response;organization of chromosome structure;nucleus","PubMed.ID":9651580,"subunits.Protein.name.":"Double-strand break repair protein MRE11A ;DNA repair protein RAD50","subunits.Gene.name.":"MRE11A;RAD50","subunits.Gene.name.syn.":"HNGS1 MRE11;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Mre11 by itself has 3' to 5' exonuclease activity that is increased when Mre11 is in a complex with Rad50.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":73,"ComplexName":"MRN complex (MRE11-RAD50-NBN complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60934;P49959;Q92878","subunits.Entrez.IDs.":"4683;4361;10111","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0413- electrophoretic mobility shift assay","GO.ID":"GO:0006308;GO:0006281;GO:0000075;GO:0003677;GO:0006974;GO:0005634","GO.description":"DNA catabolic process;DNA repair;cell cycle checkpoint;DNA binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"01.03.16.03;10.01.05.01;10.03.01.03;16.03.01;32.01.09;70.10","FunCat.description":"DNA degradation;DNA repair;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA binding;DNA damage response;nucleus","PubMed.ID":10346816,"subunits.Protein.name.":"Nibrin ;Double-strand break repair protein MRE11A ;DNA repair protein RAD50","subunits.Gene.name.":"NBN;MRE11A;RAD50","subunits.Gene.name.syn.":"NBS NBS1 P95;HNGS1 MRE11;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"On nonhairpin DNA ends, ATP controls a switch in endonuclease specificity that allows Mre11/Rad50/Nbs1 to cleave a 3'-protruding strand at a double-/single-strand transition.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":74,"ComplexName":"TRPC1-Homer3-IP3R complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"P48995;Q14643;Q9Z2X5","subunits.Entrez.IDs.":"7220;3708;29548","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0023052","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;signaling","FunCat.ID":"20.01.01.01;20.03.01.01;30.01","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;cellular signalling","PubMed.ID":14505576,"subunits.Protein.name.":"Short transient receptor potential channel 1 ;Inositol 1,4,5-trisphosphate receptor type 1 ;Homer protein homolog 3","subunits.Gene.name.":"TRPC1;ITPR1;Homer3","subunits.Gene.name.syn.":"TRP1;INSP3R1;Vesl3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors demonstrate that the adaptor protein, termed Homer, facilitates a physical association between TRPC1 and the IP(3)R that is required for the TRP channel to respond to signals.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Rattus norvegicus (Rat)"}
{"ComplexID":75,"ComplexName":"TSC1-TSC2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P49815;Q92574","subunits.Entrez.IDs.":"7249;7248","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006417;GO:0006468;GO:0006470;GO:0046777","GO.description":"regulation of translation;protein phosphorylation;protein dephosphorylation;protein autophosphorylation","FunCat.ID":"12.07;14.07.03","FunCat.description":"translational control;modification by phosphorylation, dephosphorylation, autophosphorylation","PubMed.ID":14651849,"subunits.Protein.name.":"Tuberin;Hamartin","subunits.Gene.name.":"TSC2;TSC1","subunits.Gene.name.syn.":"TSC4;KIAA0243 TSC","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TSC1 and TSC2 form a functional complex and inhibit the phosphorylation of S6K and 4EBP1, two key regulators of translation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":76,"ComplexName":"Cytoplasmic dynein complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P38650;P62628;P63036;P63170;Q62871;Q63100;Q9JJ79;Q9QXU8;Q9Z336","subunits.Entrez.IDs.":"29489;170714;65028;58945;116659;29564;65209;252902;83462","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0027- cosedimentation; MI:0019- coimmunoprecipitation","GO.ID":"GO:0040011;GO:0006928;GO:0050879;GO:0005515;GO:0030705;GO:0006897","GO.description":"locomotion;movement of cell or subcellular component;multicellular organismal movement;protein binding;cytoskeleton-dependent intracellular transport;endocytosis","FunCat.ID":"02.45.11;34.05;16.01;20.09.14;20.09.18.09.01","FunCat.description":"conversion to kinetic energy (e.g. movement);cell motility;protein binding;cytoskeleton-dependent transport;endocytosis","PubMed.ID":9790665,"subunits.Protein.name.":"Cytoplasmic dynein 1 heavy chain 1 ;Dynein light chain roadblock-type 1 ;DnaJ homolog subfamily A member 1 ;Dynein light chain 1, cytoplasmic ;Cytoplasmic dynein 1 intermediate chain 2 ;Cytoplasmic dynein 1 intermediate chain 1 ;Cytoplasmic dynein 2 heavy chain 1 ;Cytoplasmic dynein 1 light intermediate chain 1 ;Dynein light chain Tctex-type 1","subunits.Gene.name.":"Dync1h1;Dynlrb1;Dnaja1;Dynll1;Dync1i2;Dync1i1;Dync2h1;Dync1li1;Dynlt1","subunits.Gene.name.syn.":"Dhc1 Dnch1 Dnchc1 Dnec1 Dyhc Map1c;Dncl2a Dnlc2a;Hsj2 Rdj1;Dncl1 Dnclc1 Pin;Dnci2 Dncic2;Dnci1 Dncic1;Dhc1b Dlp4 Dnch2 Dnchc2;Dncli1;Tctel1 Tctex-1 Tctex1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cytoplasmic dynein  is involved in functions as diverse as spindle-pole organization and nuclear migration during mitosis, the positioning and functioning of the endoplasmic reticulum, the Golgi apparatus, and the nucleus, and also the minus-end-directed transport of vesicles, including endosomes and lysosomes, along microtubules and retrograde axonal transport in neurons (PMID:16440056).","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":77,"ComplexName":"nNos-Capon-Dexras1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"O35626;Q9D3A8;Q9Z0J4","subunits.Entrez.IDs.":"19416;70729;18125","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0007263;GO:0005737","GO.description":"nitric oxide mediated signal transduction;cytoplasm","FunCat.ID":"30.01.09.01;70.03","FunCat.description":"NO mediated signal transduction;cytoplasm","PubMed.ID":11086993,"subunits.Protein.name.":"Dexamethasone-induced Ras-related protein 1;Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein ;Nitric oxide synthase, brain","subunits.Gene.name.":"Rasd1;Nos1ap;Nos1","subunits.Gene.name.syn.":"Dexras1;Capon Kiaa0464;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors describe that CAPON enhances nNOS-mediated activation of Dexras1 through the ternary complex whereby CAPON links nNOS to Dexras1.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":78,"ComplexName":"nNos-Capon-Dexras1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"O54960;P29476;Q9JKF8","subunits.Entrez.IDs.":"192363;24598;64455","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0007263;GO:0005737","GO.description":"nitric oxide mediated signal transduction;cytoplasm","FunCat.ID":"30.01.09.01;70.03","FunCat.description":"NO mediated signal transduction;cytoplasm","PubMed.ID":11086993,"subunits.Protein.name.":"Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein ;Nitric oxide synthase, brain ;Dexamethasone-induced Ras-related protein 1","subunits.Gene.name.":"Nos1ap;Nos1;Rasd1","subunits.Gene.name.syn.":"Capon;Bnos;Dexras1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors describe that CAPON enhances nNOS-mediated activation of Dexras1 through the ternary complex whereby CAPON links nNOS to Dexras1.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":79,"ComplexName":"nNos-Capon-Syn1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"O54960;P09951;P29476","subunits.Entrez.IDs.":"192363;24949;24598","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0007263","GO.description":"nitric oxide mediated signal transduction","FunCat.ID":"30.01.09.01","FunCat.description":"NO mediated signal transduction","PubMed.ID":11867766,"subunits.Protein.name.":"Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein ;Synapsin-1 ;Nitric oxide synthase, brain","subunits.Gene.name.":"Nos1ap;Syn1;Nos1","subunits.Gene.name.syn.":"Capon;;Bnos","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"CAPON has  been found to function as an adapter protein linking nNOS to specific targets such as Dexras1 and synapsins. The results suggest a mechanism for specific actions of NO at presynaptic sites.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":80,"ComplexName":"Ubiquitin E3 ligase (Skp1A, Skp2, Cul1, Rbx1)","Organism":"Human","Synonyms":"Cul1-Rbx1-Skp1-Fbox protein Skp2 SCF ubiquitin ligase complex","Cell.line":"None","subunits.UniProt.IDs.":"P62877;P63208;Q13309;Q13616","subunits.Entrez.IDs.":"9978;6500;6502;8454","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0016567;GO:0016579;GO:0005634","GO.description":"protein ubiquitination;protein deubiquitination;nucleus","FunCat.ID":"14.07.05;70.10","FunCat.description":"modification by ubiquitination, deubiquitination;nucleus","PubMed.ID":11961546,"subunits.Protein.name.":"E3 ubiquitin-protein ligase RBX1;S-phase kinase-associated protein 1;S-phase kinase-associated protein 2;Cullin-1","subunits.Gene.name.":"RBX1;SKP1;SKP2;CUL1","subunits.Gene.name.syn.":"RNF75, ROC1;EMC19, OCP2, SKP1A, TCEB1L;FBXL1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on target proteins. The ubiquitin ligase is referred to as an E3 and operates in conjunction with an E1 ubiquitin-activating enzyme and an E2 ubiquitin-conjugating enzyme. Polyubiquitination marks proteins for degradation by the proteasome.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":81,"ComplexName":"Ubiquitin E3 ligase (SKP1A, FBXW8, CUL7, RBX1)","Organism":"Human","Synonyms":"Cul7-Rbx1-Skp1-F-Fbx29 complex","Cell.line":"None","subunits.UniProt.IDs.":"P62877;P63208;Q14999;Q8N3Y1","subunits.Entrez.IDs.":"9978;6500;9820;26259","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0016567;GO:0016579","GO.description":"protein ubiquitination;protein deubiquitination","FunCat.ID":"14.07.05","FunCat.description":"modification by ubiquitination, deubiquitination","PubMed.ID":12481031,"subunits.Protein.name.":"E3 ubiquitin-protein ligase RBX1;S-phase kinase-associated protein 1;Cullin-7;F-box/WD repeat-containing protein 8","subunits.Gene.name.":"RBX1;SKP1;CUL7;FBXW8","subunits.Gene.name.syn.":"RNF75, ROC1;EMC19, OCP2, SKP1A, TCEB1L;KIAA0076;FBW6 FBW8 FBX29 FBXO29 FBXW6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":82,"ComplexName":"Ubiquitin E3 ligase (Vhl, Tceb1, Tceb2, Cul2, Rbx1)","Organism":"Rat","Synonyms":"VHL tumor suppressor complex","Cell.line":"None","subunits.UniProt.IDs.":"P62870;P83941;Q498D8;Q64259;Q9D4H8","subunits.Entrez.IDs.":"81807;64525;300084;24874;71745","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0091- chromatography technologies","GO.ID":"GO:0016567;GO:0016579;GO:0005515","GO.description":"protein ubiquitination;protein deubiquitination;protein binding","FunCat.ID":"14.07.05;16.01","FunCat.description":"modification by ubiquitination, deubiquitination;protein binding","PubMed.ID":10213691,"subunits.Protein.name.":"Transcription elongation factor B polypeptide 2 ;Transcription elongation factor B polypeptide 1 ;Protein Rbx1 ;Von Hippel-Lindau disease tumor suppressor ;Cullin-2","subunits.Gene.name.":"Tceb2;Tceb1;Rbx1;Vhl;Cul2","subunits.Gene.name.syn.":";;;;","Disease.comment":"None","Subunits.comment":"Since Cul2 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on target proteins. The ubiquitin ligase is referred to as an E3 and operates in conjunction with an E1 ubiquitin-activating enzyme and an E2 ubiquitin-conjugating enzyme. Polyubiquitination marks proteins for degradation by the proteasome.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Mus musculus (Mouse)"}
{"ComplexID":83,"ComplexName":"Tubulin:stathmin complex","Organism":"Bovine","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P81948;Q3T0C7;Q6B856","subunits.Entrez.IDs.":"None;616317;281555","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0007049;GO:0000226","GO.description":"cell cycle;microtubule cytoskeleton organization","FunCat.ID":"10.03;42.04.05","FunCat.description":"cell cycle;microtubule cytoskeleton","PubMed.ID":11030624,"subunits.Protein.name.":"Tubulin alpha-4A chain ;Stathmin;Tubulin beta-2B chain","subunits.Gene.name.":"TUBA4A;STMN1;TUBB2B","subunits.Gene.name.syn.":"TUBA1;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":84,"ComplexName":"Nucleic acid channel complex","Organism":"Rat","Synonyms":"NACh","Cell.line":"None","subunits.UniProt.IDs.":"O88989;P70581","subunits.Entrez.IDs.":"24551;245922","Protein.complex.purification.method":"MI:0091- chromatography technologies","GO.ID":"GO:0005337;GO:0015931;GO:0006862;GO:0015215;GO:0015858;GO:0015267;GO:0005886","GO.description":"nucleoside transmembrane transporter activity;nucleobase-containing compound transport;nucleotide transport;nucleotide transmembrane transporter activity;nucleoside transport;channel activity;plasma membrane","FunCat.ID":"20.01.17;20.03.01;70.02","FunCat.description":"nucleotide/nucleoside/nucleobase transport;channel / pore class transport;eukaryotic plasma membrane / membrane attached","PubMed.ID":11805283,"subunits.Protein.name.":"Malate dehydrogenase, cytoplasmic ;Nucleoporin p58/p45","subunits.Gene.name.":"Mdh1;Nup58","subunits.Gene.name.syn.":"Mdh;Nupl1","Disease.comment":"None","Subunits.comment":"NACh is a heteromultimeric complex of at least two proteins.","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":85,"ComplexName":"Tubulin:stathmin complex","Organism":"Bovine","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P81948;Q3T0C7;Q6B856","subunits.Entrez.IDs.":"None;616317;281555","Protein.complex.purification.method":"MI:0107- surface plasmon resonance; MI:0071- molecular sieving","GO.ID":"GO:0007049;GO:0000226","GO.description":"cell cycle;microtubule cytoskeleton organization","FunCat.ID":"10.03;42.04.05","FunCat.description":"cell cycle;microtubule cytoskeleton","PubMed.ID":9312110,"subunits.Protein.name.":"Tubulin alpha-4A chain ;Stathmin;Tubulin beta-2B chain","subunits.Gene.name.":"TUBA4A;STMN1;TUBB2B","subunits.Gene.name.syn.":"TUBA1;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The stathmin interacts directly with tubulin, with a maximum affinity of 0.5 \\u00b5M around pH 6.5. This interaction leads to formation of a 217-kDa complex consisting of the association of one stathmin with two tubulin heterodimer molecules.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":86,"ComplexName":"NUMAC complex (nucleosomal methylation activator complex)","Organism":"Human","Synonyms":"CARM1-associated complex","Cell.line":"None","subunits.UniProt.IDs.":"O14497;P51532;P60709;Q12824;Q86X55;Q8TAQ2;Q92922;Q969G3;Q96GM5;Q96KG9","subunits.Entrez.IDs.":"8289;6597;60;6598;10498;6601;6599;6605;6602;57410","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006265;GO:0045893;GO:0018126;GO:0006479;GO:0003677;GO:0009755;GO:0023052;GO:0051276;GO:0005634","GO.description":"DNA topological change;positive regulation of transcription, DNA-templated;protein hydroxylation;protein methylation;DNA binding;hormone-mediated signaling pathway;signaling;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.01;14.07.09;16.03.01;30.01.09.08;30.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription activation;posttranslational modification of amino acids (e.g. hydroxylation, methylation);DNA binding;hormone mediated signal transduction;cellular signalling;organization of chromosome structure;nucleus","PubMed.ID":14729568,"subunits.Protein.name.":"AT-rich interactive domain-containing protein 1A;Transcription activator BRG1;Actin, cytoplasmic 1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;Histone-arginine methyltransferase CARM1 ;SWI/SNF complex subunit SMARCC2;SWI/SNF complex subunit SMARCC1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1;N-terminal kinase-like protein","subunits.Gene.name.":"ARID1A;SMARCA4;ACTB;SMARCB1;CARM1;SMARCC2;SMARCC1;SMARCE1;SMARCD1;SCYL1","subunits.Gene.name.syn.":"BAF250 BAF250A C1orf4 OSA1 SMARCF1;BAF190A BRG1 SNF2B SNF2L4;None;BAF47, INI1, SNF5L1;PRMT4;BAF170;BAF155;BAF57;BAF60A;CVAK90 GKLP NTKL TAPK TEIF TRAP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In the NUMAC complex, the methylase, CARM1, acquires the ability to covalently modify nucleosomal histones.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":87,"ComplexName":"Nup 107-160 subcomplex","Organism":"Human","Synonyms":"NPC subcomplex","Cell.line":"None","subunits.UniProt.IDs.":"P52948;P55735;P57740;Q12769;Q8NFH3;Q8NFH4;Q8WUM0;Q96EE3;Q9BW27","subunits.Entrez.IDs.":"4928;6396;57122;23279;348995;79023;55746;81929;79902","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0015031;GO:0008565;GO:0006810;GO:0051169;GO:0000775","GO.description":"protein transport;protein transporter activity;transport;nuclear transport;chromosome, centromeric region","FunCat.ID":"20.01.10;20;20.09.01;70.10.04","FunCat.description":"protein transport;CELLULAR TRANSPORT, TRANSPORT FACILITIES AND TRANSPORT ROUTES;nuclear transport;centromere / kinetochore","PubMed.ID":15146057,"subunits.Protein.name.":"Nuclear pore complex protein Nup98-Nup96 [Cleaved into: Nuclear pore complex protein Nup98;Protein SEC13 homolog;Nuclear pore complex protein Nup107;Nuclear pore complex protein Nup160;Nucleoporin Nup43 ;Nucleoporin Nup37 ;Nuclear pore complex protein Nup133;Nucleoporin SEH1;Nuclear pore complex protein Nup85","subunits.Gene.name.":"NUP98;SEC13;NUP107;NUP160;NUP43;NUP37;NUP133;SEH1L;NUP85","subunits.Gene.name.syn.":"ADAR2;D3S1231E SEC13L1 SEC13R;None;KIAA0197 NUP120;;;None;SEC13L SEH1;NUP75 PCNT1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"All trafficking of macromolecules between the cytoplasm and the nucleus occurs through nuclear pore complexes (NPCs), which are supramolecular assemblies at points of fusion between the inner and outer nuclear membranes. NPCs are composed of an eightfold symmetric spoke-ring complex, cytoplasmic fibers, and a nuclear basket.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":88,"ComplexName":"SNARE complex (Scfd1, Sec22b, Stx5, Bet1, Gosr2, Gosr1)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O35165;Q08851;Q4KM74;Q62896;Q62931;Q62991","subunits.Entrez.IDs.":"64154;65134;310710;29631;94189;54350","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0027- cosedimentation","GO.ID":"GO:0006888;GO:0006891;GO:0006900;GO:0016050;GO:0006906;GO:0048489;GO:0016079;GO:0005783;GO:0005794","GO.description":"ER to Golgi vesicle-mediated transport;intra-Golgi vesicle-mediated transport;membrane budding;vesicle organization;vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis;endoplasmic reticulum;Golgi apparatus","FunCat.ID":"20.09.07.03;20.09.07.05;20.09.07.25;20.09.07.27;20.09.16.09.05;70.07;70.08","FunCat.description":"ER to Golgi transport;intra Golgi transport;vesicle formation;vesicle fusion;synaptic vesicle exocytosis;endoplasmic reticulum;Golgi","PubMed.ID":9094723,"subunits.Protein.name.":"Golgi SNAP receptor complex member 2 ;Syntaxin-5;Vesicle-trafficking protein SEC22b ;BET1 homolog;Golgi SNAP receptor complex member 1;Sec1 family domain-containing protein 1","subunits.Gene.name.":"Gosr2;Stx5;Sec22b;Bet1;Gosr1;Scfd1","subunits.Gene.name.syn.":"Gs27;Stx5a;Sec22l1;None;Gs28;Ra410 Sly1 Stxbp1l2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":89,"ComplexName":"Exocyst Sec6/8 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00471;O60645;Q8IYI6;Q8TAG9;Q96A65;Q96KP1;Q9NV70;Q9UPT5","subunits.Entrez.IDs.":"10640;11336;149371;54536;60412;55770;55763;23265","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0015031;GO:0008565;GO:0006887","GO.description":"protein transport;protein transporter activity;exocytosis","FunCat.ID":"20.01.10;20.09.16.09.03","FunCat.description":"protein transport;exocytosis","PubMed.ID":11493706,"subunits.Protein.name.":"Exocyst complex component 5;Exocyst complex component 3;Exocyst complex component 8;Exocyst complex component 6;Exocyst complex component 4;Exocyst complex component 2;Exocyst complex component 1;Exocyst complex component 7","subunits.Gene.name.":"EXOC5;EXOC3;EXOC8;EXOC6;EXOC4;EXOC2;EXOC1;EXOC7","subunits.Gene.name.syn.":"SEC10 SEC10L1;SEC6 SEC6L1;None;SEC15A SEC15L SEC15L1;KIAA1699 SEC8 SEC8L1;SEC5 SEC5L1;SEC3 SEC3L1;EXO70 KIAA1067","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":91,"ComplexName":"FA complex (Fanconi anemia complex), cytoplasmic","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15287;O15360;Q00597;Q9NPI8","subunits.Entrez.IDs.":"2189;2175;2176;2188","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0016567;GO:0016579;GO:0006974;GO:0005737","GO.description":"protein ubiquitination;protein deubiquitination;cellular response to DNA damage stimulus;cytoplasm","FunCat.ID":"14.07.05;32.01.09;70.03","FunCat.description":"modification by ubiquitination, deubiquitination;DNA damage response;cytoplasm","PubMed.ID":15082718,"subunits.Protein.name.":"Fanconi anemia group G protein ;Fanconi anemia group A protein ;Fanconi anemia group C protein ;Fanconi anemia group F protein","subunits.Gene.name.":"FANCG;FANCA;FANCC;FANCF","subunits.Gene.name.syn.":"XRCC9;FAA FACA FANCH;FAC FACC;","Disease.comment":"FA complex is involved in Fanconi anemia (FA) disease.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":92,"ComplexName":"CD28-transactivation complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P10747;P19338","subunits.Entrez.IDs.":"940;4691","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006352;GO:2001141;GO:0006355;GO:0005634","GO.description":"DNA-templated transcription, initiation;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;nucleus","FunCat.ID":"11.02.03.01.01;11.02.03.04;70.10","FunCat.description":"transcription initiation;transcriptional control;nucleus","PubMed.ID":12324461,"subunits.Protein.name.":"T-cell-specific surface glycoprotein CD28 ;Nucleolin","subunits.Gene.name.":"CD28;NCL","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":93,"ComplexName":"Anaphase-promoting complex","Organism":"Human","Synonyms":"APC; cyclosome","Cell.line":"None","subunits.UniProt.IDs.":"P30260;Q13042;Q9H1A4;Q9UJX2;Q9UJX3;Q9UJX4;Q9UJX5;Q9UJX6","subunits.Entrez.IDs.":"996;8881;64682;8697;51434;51433;29945;29882","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000278;GO:0051726;GO:0016567;GO:0016579;GO:0005515;GO:0005634","GO.description":"mitotic cell cycle;regulation of cell cycle;protein ubiquitination;protein deubiquitination;protein binding;nucleus","FunCat.ID":"10.03.01.01;10.03.01;14.07.05;16.01;70.10","FunCat.description":"mitotic cell cycle;mitotic cell cycle and cell cycle control;modification by ubiquitination, deubiquitination;protein binding;nucleus","PubMed.ID":9469815,"subunits.Protein.name.":"Cell division cycle protein 27 homolog ;Cell division cycle protein 16 homolog ;Anaphase-promoting complex subunit 1 ;Cell division cycle protein 23 homolog ;Anaphase-promoting complex subunit 7 ;Anaphase-promoting complex subunit 5 ;Anaphase-promoting complex subunit 4 ;Anaphase-promoting complex subunit 2","subunits.Gene.name.":"CDC27;CDC16;ANAPC1;CDC23;ANAPC7;ANAPC5;ANAPC4;ANAPC2","subunits.Gene.name.syn.":"ANAPC3 D0S1430E D17S978E;ANAPC6;TSG24;ANAPC8;APC7;APC5;APC4;APC2 KIAA1406","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The initiation of anaphase and exit from mitosis depend on a multi-subunit ubiquitination complex called the anaphase-promoting complex (APC)1 or cyclosome. The APC ubiquitinates proteins such as Pds1 in budding yeast and Cut2 in fission yeast whose subsequent degradation by the 26 S proteasome is essential for the initiation of sister chromatid separation at the metaphase-anaphase transition. Later in anaphase and telophase the APC promotes the inactivation of the mitotic cyclin-dependent protein kinase 1 by ubiquitinating its activating subunit cyclin B.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":94,"ComplexName":"ATP-utilizing chromatin assembly and remodeling factor (hACF) complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60264;Q9NRL2","subunits.Entrez.IDs.":"8467;11177","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0004- affinity chromatography technologies","GO.ID":"GO:0006265;GO:2001141;GO:0006355;GO:0051276;GO:0005634","GO.description":"DNA topological change;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcriptional control;organization of chromosome structure;nucleus","PubMed.ID":10747848,"subunits.Protein.name.":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5;Bromodomain adjacent to zinc finger domain protein 1A","subunits.Gene.name.":"SMARCA5;BAZ1A","subunits.Gene.name.syn.":"SNF2H WCRF135;ACF1 WCRF180","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The hACF complex also possesses ATP-dependent nucleosome remodeling and spacing activities.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":95,"ComplexName":"Ku antigen-NARG1 complex","Organism":"Human","Synonyms":"OCFRE-binding complex","Cell.line":"MC3T3-E1 cells","subunits.UniProt.IDs.":"P12956;P13010;Q9BXJ9","subunits.Entrez.IDs.":"2547;7520;80155","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:2001141;GO:0006355;GO:0003677","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding","FunCat.ID":"11.02.03.04;16.03.01","FunCat.description":"transcriptional control;DNA binding","PubMed.ID":12145306,"subunits.Protein.name.":"X-ray repair cross-complementing protein 6 ;X-ray repair cross-complementing protein 5 ;N-alpha-acetyltransferase 15, NatA auxiliary subunit","subunits.Gene.name.":"XRCC6;XRCC5;NAA15","subunits.Gene.name.syn.":"G22P1;G22P2;GA19 NARG1 NATH TBDN100","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex regulates osteocalcin gene expression.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":96,"ComplexName":"Anaphase-promoting complex","Organism":"Human","Synonyms":"APC; cyclosome","Cell.line":"None","subunits.UniProt.IDs.":"P30260;Q13042;Q9H1A4;Q9UJX2;Q9UJX3;Q9UJX4;Q9UJX5;Q9UJX6;Q9UM13","subunits.Entrez.IDs.":"996;8881;64682;8697;51434;51433;29945;29882;10393","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000278;GO:0051726;GO:0016567;GO:0016579;GO:0005515;GO:0005634","GO.description":"mitotic cell cycle;regulation of cell cycle;protein ubiquitination;protein deubiquitination;protein binding;nucleus","FunCat.ID":"10.03.01.01;10.03.01;14.07.05;16.01;70.10","FunCat.description":"mitotic cell cycle;mitotic cell cycle and cell cycle control;modification by ubiquitination, deubiquitination;protein binding;nucleus","PubMed.ID":10318877,"subunits.Protein.name.":"Cell division cycle protein 27 homolog ;Cell division cycle protein 16 homolog ;Anaphase-promoting complex subunit 1 ;Cell division cycle protein 23 homolog ;Anaphase-promoting complex subunit 7 ;Anaphase-promoting complex subunit 5 ;Anaphase-promoting complex subunit 4 ;Anaphase-promoting complex subunit 2 ;Anaphase-promoting complex subunit 10","subunits.Gene.name.":"CDC27;CDC16;ANAPC1;CDC23;ANAPC7;ANAPC5;ANAPC4;ANAPC2;ANAPC10","subunits.Gene.name.syn.":"ANAPC3 D0S1430E D17S978E;ANAPC6;TSG24;ANAPC8;APC7;APC5;APC4;APC2 KIAA1406;APC10","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The initiation of anaphase and exit from mitosis depend on a multi-subunit ubiquitination complex called the anaphase-promoting complex (APC)1 or cyclosome. The APC ubiquitinates proteins such as Pds1 in budding yeast and Cut2 in fission yeast whose subsequent degradation by the 26 S proteasome is essential for the initiation of sister chromatid separation at the metaphase-anaphase transition. Later in anaphase and telophase the APC promotes the inactivation of the mitotic cyclin-dependent protein kinase 1 by ubiquitinating its activating subunit cyclin B.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":97,"ComplexName":"Anaphase-promoting complex","Organism":"Mouse","Synonyms":"APC; cyclosome","Cell.line":"None","subunits.UniProt.IDs.":"P53995;Q3V036;Q8BGZ4;Q8BTZ4;Q8BZQ7;Q8K2H6;Q8R349;Q91W96;Q9WVM3","subunits.Entrez.IDs.":"17222;381580;52563;59008;99152;68999;69957;52206;56317","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000278;GO:0051726;GO:0016567;GO:0016579;GO:0005515;GO:0005634","GO.description":"mitotic cell cycle;regulation of cell cycle;protein ubiquitination;protein deubiquitination;protein binding;nucleus","FunCat.ID":"10.03.01.01;10.03.01;14.07.05;16.01;70.10","FunCat.description":"mitotic cell cycle;mitotic cell cycle and cell cycle control;modification by ubiquitination, deubiquitination;protein binding;nucleus","PubMed.ID":10318877,"subunits.Protein.name.":"Anaphase-promoting complex subunit 1 ;Coiled-coil domain-containing protein 27;Cell division cycle protein 23 homolog ;Anaphase-promoting complex subunit 5 ;Anaphase-promoting complex subunit 2 ;Anaphase-promoting complex subunit 10 ;Cell division cycle protein 16 homolog ;Anaphase-promoting complex subunit 4 ;Anaphase-promoting complex subunit 7","subunits.Gene.name.":"Anapc1;Ccdc27;Cdc23;Anapc5;Anapc2;Anapc10;Cdc16;Anapc4;Anapc7","subunits.Gene.name.syn.":"Mcpr Tsg24;Gm1035;Anapc8;;;Apc10;Anapc6;D5Ertd249e;Apc7","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The initiation of anaphase and exit from mitosis depend on a multi-subunit ubiquitination complex called the anaphase-promoting complex (APC)1 or cyclosome. The APC ubiquitinates proteins such as Pds1 in budding yeast and Cut2 in fission yeast whose subsequent degradation by the 26 S proteasome is essential for the initiation of sister chromatid separation at the metaphase-anaphase transition. Later in anaphase and telophase the APC promotes the inactivation of the mitotic cyclin-dependent protein kinase 1 by ubiquitinating its activating subunit cyclin B.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":98,"ComplexName":"p300-MDM2-p53 protein complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04637;Q00987;Q09472","subunits.Entrez.IDs.":"7157;4193;2033","Protein.complex.purification.method":"MI:0091- chromatography technologies","GO.ID":"GO:2001141;GO:0006355;GO:0030234;GO:0050790;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;enzyme regulator activity;regulation of catalytic activity;nucleus","FunCat.ID":"11.02.03.04;18.02.01;70.10","FunCat.description":"transcriptional control;enzymatic activity regulation / enzyme regulator;nucleus","PubMed.ID":11070080,"subunits.Protein.name.":"Cellular tumor antigen p53;E3 ubiquitin-protein ligase Mdm2 ;Histone acetyltransferase p300","subunits.Gene.name.":"TP53;MDM2;EP300","subunits.Gene.name.syn.":"P53;;P300","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":100,"ComplexName":"hNURF complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P28370;Q09028;Q12830;Q16576","subunits.Entrez.IDs.":"6594;5928;2186;5931","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0226- ion exchange chromatography","GO.ID":"GO:0006265;GO:2001141;GO:0006355;GO:0022008;GO:0048699;GO:0051276;GO:0030182;GO:0005634","GO.description":"DNA topological change;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;neurogenesis;generation of neurons;chromosome organization;neuron differentiation;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04;41.05.13;42.10.03;43.03.13;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcriptional control;neurogenesis;organization of chromosome structure;neuron;nucleus","PubMed.ID":14609955,"subunits.Protein.name.":"Probable global transcription activator SNF2L1 ;Histone-binding protein RBBP4;Nucleosome-remodeling factor subunit BPTF ;Histone-binding protein RBBP7","subunits.Gene.name.":"SMARCA1;RBBP4;BPTF;RBBP7","subunits.Gene.name.syn.":"SNF2L SNF2L1;RBAP48;FAC1 FALZ;RBAP46","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"NURF is a member of the ISWI-containing chromatin remodeling complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":101,"ComplexName":"Nucleolar remodeling complex (NoRC complex)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q91YE5;Q91ZW3","subunits.Entrez.IDs.":"116848;93762","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006265;GO:0009303;GO:0051276;GO:0005634","GO.description":"DNA topological change;rRNA transcription;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);rRNA synthesis;organization of chromosome structure;nucleus","PubMed.ID":11532953,"subunits.Protein.name.":"Bromodomain adjacent to zinc finger domain protein 2A ;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5","subunits.Gene.name.":"Baz2a;Smarca5","subunits.Gene.name.syn.":"Kiaa0314 Tip5;Snf2h","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"NoRC induces nucleosome sliding in an ATP- and histone H4 tail-dependent fashion. This complex may serve a role in the regulation of the rDNA locus.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":102,"ComplexName":"Meiotic cohesin complex","Organism":"Mouse","Synonyms":"None","Cell.line":"male gonad (testis)","subunits.UniProt.IDs.":"P70281;Q8C5S7;Q920F6;Q9CW03","subunits.Entrez.IDs.":"20962;56739;140557;13006","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007127;GO:0007135;GO:0051276;GO:0005634","GO.description":"meiosis I;meiosis II;chromosome organization;nucleus","FunCat.ID":"10.03.02.01;10.03.02.03;42.10.03;70.10","FunCat.description":"meiosis I;meiosis II;organization of chromosome structure;nucleus","PubMed.ID":12759374,"subunits.Protein.name.":"Synaptonemal complex protein 3;Meiotic recombination protein REC8 homolog;Structural maintenance of chromosomes protein 1B;Structural maintenance of chromosomes protein 3","subunits.Gene.name.":"Sycp3;Rec8;Smc1b;Smc3","subunits.Gene.name.syn.":"Scp3;Mei8 Rec8L1;Smc1l2;Bam Bmh Cspg6 Mmip1 Smc3l1 Smcd","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":103,"ComplexName":"RNA polymerase II holoenzyme complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15514;P13984;P18074;P19387;P19388;P19447;P20226;P24928;P29083;P29084;P30876;P32780;P35269;P36954;P52434;P52435;P53803;P61218;P62487;P62875;Q00403;Q13888;Q13889;Q92759","subunits.Entrez.IDs.":"5433;2963;2068;5432;5434;2071;6908;5430;2960;2961;5431;2965;2962;5438;5437;5439;5440;5435;5436;5441;2959;2966;2967;2968","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006351;GO:0003677;GO:0005634","GO.description":"transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11;16.03.01;70.10","FunCat.description":"TRANSCRIPTION;DNA binding;nucleus","PubMed.ID":9305922,"subunits.Protein.name.":"DNA-directed RNA polymerase II subunit RPB4 ;General transcription factor IIF subunit 2 ;TFIIH basal transcription factor complex helicase XPD subunit ;DNA-directed RNA polymerase II subunit RPB3 ;DNA-directed RNA polymerases I, II, and III subunit RPABC1 ;TFIIH basal transcription factor complex helicase XPB subunit ;TATA-box-binding protein;DNA-directed RNA polymerase II subunit RPB1;General transcription factor IIE subunit 1;Transcription initiation factor IIE subunit beta ;DNA-directed RNA polymerase II subunit RPB2 ;General transcription factor IIH subunit 1;General transcription factor IIF subunit 1;DNA-directed RNA polymerase II subunit RPB9 ;DNA-directed RNA polymerases I, II, and III subunit RPABC3 ;DNA-directed RNA polymerase II subunit RPB11-a ;DNA-directed RNA polymerases I, II, and III subunit RPABC4 ;DNA-directed RNA polymerases I, II, and III subunit RPABC2 ;DNA-directed RNA polymerase II subunit RPB7 ;DNA-directed RNA polymerases I, II, and III subunit RPABC5 ;Transcription initiation factor IIB;General transcription factor IIH subunit 2 ;General transcription factor IIH subunit 3 ;General transcription factor IIH subunit 4","subunits.Gene.name.":"POLR2D;GTF2F2;ERCC2;POLR2C;POLR2E;ERCC3;TBP;POLR2A;GTF2E1;GTF2E2;POLR2B;GTF2H1;GTF2F1;POLR2I;POLR2H;POLR2J;POLR2K;POLR2F;POLR2G;POLR2L;GTF2B;GTF2H2;GTF2H3;GTF2H4","subunits.Gene.name.syn.":";RAP30;XPD XPDC;;;XPB XPBC;GTF2D1 TF2D TFIID;POLR2;TF2E1;TF2E2;;BTF2;RAP74;;;POLR2J1;;POLRF;RPB7;;TF2B TFIIB;BTF2P44;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":104,"ComplexName":"RNA polymerase II core complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15514;P19387;P19388;P24928;P30876;P36954;P52434;P52435;P53803;P61218;P62487;P62875","subunits.Entrez.IDs.":"5433;5432;5434;5430;5431;5438;5437;5439;5440;5435;5436;5441","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006351;GO:0003677;GO:0005634","GO.description":"transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11;16.03.01;70.10","FunCat.description":"TRANSCRIPTION;DNA binding;nucleus","PubMed.ID":9852112,"subunits.Protein.name.":"DNA-directed RNA polymerase II subunit RPB4 ;DNA-directed RNA polymerase II subunit RPB3 ;DNA-directed RNA polymerases I, II, and III subunit RPABC1 ;DNA-directed RNA polymerase II subunit RPB1;DNA-directed RNA polymerase II subunit RPB2 ;DNA-directed RNA polymerase II subunit RPB9 ;DNA-directed RNA polymerases I, II, and III subunit RPABC3 ;DNA-directed RNA polymerase II subunit RPB11-a ;DNA-directed RNA polymerases I, II, and III subunit RPABC4 ;DNA-directed RNA polymerases I, II, and III subunit RPABC2 ;DNA-directed RNA polymerase II subunit RPB7 ;DNA-directed RNA polymerases I, II, and III subunit RPABC5","subunits.Gene.name.":"POLR2D;POLR2C;POLR2E;POLR2A;POLR2B;POLR2I;POLR2H;POLR2J;POLR2K;POLR2F;POLR2G;POLR2L","subunits.Gene.name.syn.":";;;POLR2;;;;POLR2J1;;POLRF;RPB7;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":105,"ComplexName":"Polycomb repressive complex 2 (PRC 2)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75530;Q09028;Q15022;Q15910;Q16576","subunits.Entrez.IDs.":"8726;5928;23512;2146;5931","Protein.complex.purification.method":"MI:0096- pull down; MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0006265;GO:0045892;GO:0032774;GO:0018126;GO:0006479;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;RNA biosynthetic process;protein hydroxylation;protein methylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;11.02;14.07.09;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;RNA synthesis;posttranslational modification of amino acids (e.g. hydroxylation, methylation);organization of chromosome structure;nucleus","PubMed.ID":12435631,"subunits.Protein.name.":"Polycomb protein EED;Histone-binding protein RBBP4;Polycomb protein SUZ12;Histone-lysine N-methyltransferase EZH2;Histone-binding protein RBBP7","subunits.Gene.name.":"EED;RBBP4;SUZ12;EZH2;RBBP7","subunits.Gene.name.syn.":"None;RBAP48;CHET9 JJAZ1 KIAA0160;KMT6;RBAP46","Disease.comment":"PRC complexes are overexpressed in breast, colon, and prostate cancers.","Subunits.comment":"None","Complex.comment":"Polycomb repressive complexes are required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. They are methylating histones at lysine residues. PRC4 methylates preferentially the histone H1b isoform, whereas PRC2 methylated preferentially the histone H1d isoform. The PRC3 complex exclusively targets methylation of histone H3-K27, and the activity is repressed in the presence of histone H1. PRC2 also methylates histone H3-K27 but in the presence of histone H1, PRC2 methylates both H3-K27 and H1-K26.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":106,"ComplexName":"Srf-myogenin-E12 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12979;P15806;Q9JM73","subunits.Entrez.IDs.":"17928;21423;20807","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0437- protein tri hybrid","GO.ID":"GO:2001141;GO:0006355;GO:0030154;GO:0007517","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;cell differentiation;muscle organ development","FunCat.ID":"11.02.03.04;40.02;45.03.12","FunCat.description":"transcriptional control;cell differentiation;muscle","PubMed.ID":8617811,"subunits.Protein.name.":"Myogenin ;Transcription factor E2-alpha ;Serum response factor","subunits.Gene.name.":"Myog;Tcf3;Srf","subunits.Gene.name.syn.":";Alf2 Me2 Tcfe2a;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The formation of this complex could be one of the means by which SRF activity is deviated from proliferative to differentiating genes upon muscle cell terminal differentiation.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":107,"ComplexName":"TFIIH transcription factor complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P18074;P19447;P32780;P50613;P51946;P51948;Q13888;Q13889;Q92759","subunits.Entrez.IDs.":"2068;2071;2965;1022;902;4331;2966;2967;2968","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006794;GO:0006796;GO:0006281;GO:0007049;GO:0006351;GO:2001141;GO:0006355;GO:0006464;GO:0030234;GO:0050790;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;DNA repair;cell cycle;transcription, DNA-templated;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;cellular protein modification process;enzyme regulator activity;regulation of catalytic activity;nucleus","FunCat.ID":"01.04;10.01.05.01;10.03;11;11.02.03.04;14.07;18.02.01;70.10","FunCat.description":"phosphate metabolism;DNA repair;cell cycle;TRANSCRIPTION;transcriptional control;protein modification;enzymatic activity regulation / enzyme regulator;nucleus","PubMed.ID":9852112,"subunits.Protein.name.":"TFIIH basal transcription factor complex helicase XPD subunit ;TFIIH basal transcription factor complex helicase XPB subunit ;General transcription factor IIH subunit 1;Cyclin-dependent kinase 7 ;Cyclin-H ;CDK-activating kinase assembly factor MAT1 ;General transcription factor IIH subunit 2 ;General transcription factor IIH subunit 3 ;General transcription factor IIH subunit 4","subunits.Gene.name.":"ERCC2;ERCC3;GTF2H1;CDK7;CCNH;MNAT1;GTF2H2;GTF2H3;GTF2H4","subunits.Gene.name.syn.":"XPD XPDC;XPB XPBC;BTF2;CAK CAK1 CDKN7 MO15 STK1;;CAP35 MAT1 RNF66;BTF2P44;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Transcription factor IIH (TFIIH) is a multisubunit complex required for transcription and for DNA nucleotide excision repair.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":108,"ComplexName":"ApoB mRNA editing enzyme complex","Organism":"Rat","Synonyms":"None","Cell.line":"liver","subunits.UniProt.IDs.":"P38483;Q923K9;Q99PF5","subunits.Entrez.IDs.":"25383;170912;171137","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0016556;GO:0003723","GO.description":"mRNA modification;RNA binding","FunCat.ID":"11.06.03;16.03.03","FunCat.description":"mRNA modification;RNA binding","PubMed.ID":10781591,"subunits.Protein.name.":"C->U-editing enzyme APOBEC-1;APOBEC1 complementation factor;Far upstream element-binding protein 2","subunits.Gene.name.":"Apobec1;A1cf;Khsrp","subunits.Gene.name.syn.":"None;Acf Asp;Fubp2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":109,"ComplexName":"Fertilin complex (Adam1b, Adam2)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q60718;Q8R534","subunits.Entrez.IDs.":"11495;280667","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0015031;GO:0008565","GO.description":"protein transport;protein transporter activity","FunCat.ID":"20.01.10","FunCat.description":"protein transport","PubMed.ID":15194697,"subunits.Protein.name.":"Disintegrin and metalloproteinase domain-containing protein 2 ;Disintegrin and metalloproteinase domain-containing protein 1b","subunits.Gene.name.":"Adam2;Adam1b","subunits.Gene.name.syn.":"Ftnb;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The formation of the heterodimeric protein complex between the ADAM1b and ADAM2 precursors in TGC may be essential for the localization of the mature forms of these two ADAMs on the sperm surface.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":112,"ComplexName":"Prefoldin complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15212;O60925;P61758;Q99471;Q9NQP4;Q9UHV9","subunits.Entrez.IDs.":"10471;5201;7411;5204;5203;5202","Protein.complex.purification.method":"MI:0413-electrophoretic mobility shift assay;MI:0040-electron microscopy;MI:0071-molecular sieving","GO.ID":"GO:0050821;GO:0006457;GO:0007010","GO.description":"protein stabilization;protein folding;cytoskeleton organization","FunCat.ID":"14.01;42.04","FunCat.description":"protein folding and stabilization;cytoskeleton/structural proteins","PubMed.ID":12456645,"subunits.Protein.name.":"Prefoldin subunit 6;Prefoldin subunit 1;Prefoldin subunit 3;Prefoldin subunit 5;Prefoldin subunit 4;Prefoldin subunit 2","subunits.Gene.name.":"PFDN6;PFDN1;VBP1;PFDN5;PFDN4;PFDN2","subunits.Gene.name.syn.":"HKE2 PFD6;PFD1;PFDN3;MM1 PFD5;PFD4;PFD2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":114,"ComplexName":"SNAPc (small nuclear RNA-activating protein) complex","Organism":"Human","Synonyms":"PTF","Cell.line":"None","subunits.UniProt.IDs.":"O75971;Q13487;Q16533;Q5SXM2;Q92966","subunits.Entrez.IDs.":"10302;6618;6617;6621;6619","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0005515;GO:0003677;GO:0051098;GO:0005515;GO:0051090;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein binding;DNA binding;regulation of binding;protein binding;regulation of sequence-specific DNA binding transcription factor activity;nucleus","FunCat.ID":"11.02.03.04;16.01;16.03.01;18.01.07;18.02.09;70.10","FunCat.description":"transcriptional control;protein binding;DNA binding;regulation by binding / dissociation;regulator of transcription factor;nucleus","PubMed.ID":11056176,"subunits.Protein.name.":"snRNA-activating protein complex subunit 5 ;snRNA-activating protein complex subunit 2 ;snRNA-activating protein complex subunit 1 ;snRNA-activating protein complex subunit 4 ;snRNA-activating protein complex subunit 3","subunits.Gene.name.":"SNAPC5;SNAPC2;SNAPC1;SNAPC4;SNAPC3","subunits.Gene.name.syn.":"SNAP19;SNAP45;SNAP43;SNAP190;SNAP50","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Additional information about the constituents of the SNAPc complex is given in PMID:7715707 and PMID:9732265.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":115,"ComplexName":"Polycomb repressive complex 1 (PRC1, hPRC-H)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00257;O60264;P0DMV8;P35226;P78364;Q06587;Q14781;Q8IXK0;Q8NDX5;Q96GD3;Q99496;Q9HC52","subunits.Entrez.IDs.":"8535;8467;3303;648;1911;6015;84733;1912;80012;22955;6045;57332","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0006265;GO:0045892;GO:0032774;GO:0018126;GO:0006479;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;RNA biosynthetic process;protein hydroxylation;protein methylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;11.02;14.07.09;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;RNA synthesis;posttranslational modification of amino acids (e.g. hydroxylation, methylation);organization of chromosome structure;nucleus","PubMed.ID":12167701,"subunits.Protein.name.":"E3 SUMO-protein ligase CBX4;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5;Heat shock 70 kDa protein 1A;Polycomb complex protein BMI-1;Polyhomeotic-like protein 1;E3 ubiquitin-protein ligase RING1;Chromobox protein homolog 2;Polyhomeotic-like protein 2;Polyhomeotic-like protein 3;Polycomb protein SCMH1;E3 ubiquitin-protein ligase RING2;Chromobox protein homolog 8","subunits.Gene.name.":"CBX4;SMARCA5;HSPA1A;BMI1;PHC1;RING1;CBX2;PHC2;PHC3;SCMH1;RNF2;CBX8","subunits.Gene.name.syn.":"None;SNF2H WCRF135;HSPA1, HSX70, HSP70-1A;PCGF4 RNF51;EDR1 PH1;RNF1;None;EDR2 PH2;EDR3 PH3;None;BAP1 DING HIPI3 RING1B;PC3 RC1","Disease.comment":"None","Subunits.comment":"Since the authors did not specify HSP70, we used isoform HSPA1A.","Complex.comment":"Polycomb repressive complexes are required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones. hPRC-H apparently represents not a single complex but rather a mixture of highly related complexes, here exemplified by the M33F and Bmi1F M2 eluates. The identified beta-tubulin may be a contaminant, it needs more characterization.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":116,"ComplexName":"Polycomb repressive complex 1 (PRC1, hPRC-H)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00257;O60264;P0DMV8;P25490;P35226;P78364;Q06587;Q14781;Q8IXK0;Q8NDX5;Q96GD3;Q99496;Q9HC52","subunits.Entrez.IDs.":"8535;8467;3303;7528;648;1911;6015;84733;1912;80012;22955;6045;57332","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0006265;GO:0045892;GO:0032774;GO:0018126;GO:0006479;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;RNA biosynthetic process;protein hydroxylation;protein methylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;11.02;14.07.09;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;RNA synthesis;posttranslational modification of amino acids (e.g. hydroxylation, methylation);organization of chromosome structure;nucleus","PubMed.ID":12167701,"subunits.Protein.name.":"E3 SUMO-protein ligase CBX4;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5;Heat shock 70 kDa protein 1A;Transcriptional repressor protein YY1;Polycomb complex protein BMI-1;Polyhomeotic-like protein 1;E3 ubiquitin-protein ligase RING1;Chromobox protein homolog 2;Polyhomeotic-like protein 2;Polyhomeotic-like protein 3;Polycomb protein SCMH1;E3 ubiquitin-protein ligase RING2;Chromobox protein homolog 8","subunits.Gene.name.":"CBX4;SMARCA5;HSPA1A;YY1;BMI1;PHC1;RING1;CBX2;PHC2;PHC3;SCMH1;RNF2;CBX8","subunits.Gene.name.syn.":"None;SNF2H WCRF135;HSPA1, HSX70, HSP70-1A;INO80S;PCGF4 RNF51;EDR1 PH1;RNF1;None;EDR2 PH2;EDR3 PH3;None;BAP1 DING HIPI3 RING1B;PC3 RC1","Disease.comment":"None","Subunits.comment":"Since the authors did not specify HSP70, we used isoform HSPA1A","Complex.comment":"Polycomb repressive complexes are required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones. hPRC-H apparently represents not a single complex but rather a mixture of highly related complexes, here exemplified by the Hi-Trap S eluate. The identified beta-tubulin may be a contaminant, it needs more characterization.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":117,"ComplexName":"GPR56-CD81-Galpha(q/11)-Gbeta complex","Organism":"Human","Synonyms":"None","Cell.line":"Brij 96 lysate of HEK 293 cells","subunits.UniProt.IDs.":"P29992;P50148;P60033;P62873;Q9Y653","subunits.Entrez.IDs.":"2767;2776;975;2782;9289","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":15004227,"subunits.Protein.name.":"Guanine nucleotide-binding protein subunit alpha-11;Guanine nucleotide-binding protein G;CD81 antigen;Guanine nucleotide-binding protein G;Adhesion G-protein coupled receptor G1","subunits.Gene.name.":"GNA11;GNAQ;CD81;GNB1;ADGRG1","subunits.Gene.name.syn.":"GA11;GAQ;TAPA1, TSPAN28;None;GPR56, TM7LN4, TM7XN1","Disease.comment":"None","Subunits.comment":"The Gbeta peptide identi?ed by mass spectrometry is a sequence common to beta subunits 1? 4, and the anti-Gbeta antiserum recognizes all four subunits. Since the authors did not specify Gbeta peptide, we used isoform GNB1.","Complex.comment":"The central role of CD81 (and CD9 when present) suggests possible scaffolding functions for CD81 and CD9 in GPR56 signaling.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":118,"ComplexName":"GPI-GnT activity complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P37287;Q14442;Q92535;Q9BRB3","subunits.Entrez.IDs.":"5277;5283;5279;9091","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006644;GO:0008654;GO:0009395;GO:0005783","GO.description":"phospholipid metabolic process;phospholipid biosynthetic process;phospholipid catabolic process;endoplasmic reticulum","FunCat.ID":"01.06.02.01;70.07","FunCat.description":"phospholipid metabolism;endoplasmic reticulum","PubMed.ID":9463366,"subunits.Protein.name.":"Phosphatidylinositol N-acetylglucosaminyltransferase subunit A ;Phosphatidylinositol N-acetylglucosaminyltransferase subunit H ;Phosphatidylinositol N-acetylglucosaminyltransferase subunit C ;Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q","subunits.Gene.name.":"PIGA;PIGH;PIGC;PIGQ","subunits.Gene.name.syn.":";;GPI2;GPI1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This protein complex has GPI-GlcNAc transferase (GPI-GnT) activity in vitro.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":120,"ComplexName":"Lymphotoxin beta receptor complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P01374;P36941;Q06643","subunits.Entrez.IDs.":"4049;4055;4050","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007166;GO:0006915","GO.description":"cell surface receptor signaling pathway;apoptotic process","FunCat.ID":"30.05;40.10.02","FunCat.description":"transmembrane signal transduction;apoptosis (type I programmed cell death)","PubMed.ID":9122217,"subunits.Protein.name.":"Lymphotoxin-alpha ;Tumor necrosis factor receptor superfamily member 3 ;Lymphotoxin-beta","subunits.Gene.name.":"LTA;LTBR;LTB","subunits.Gene.name.syn.":"TNFB TNFSF1;D12S370 TNFCR TNFR3 TNFRSF3;TNFC TNFSF3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The binding of heterotrimeric lymphotoxin, LT alpha1 beta2, to the LTbeta receptor (LTbeta R), a member of the tumor necrosis factor receptor (TNFR) superfamily, induces nuclear factor kappaB (NF-kappaB) activation and cell death in HT29 adenocarcinoma cells.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":122,"ComplexName":"MCM complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P25206;P49717;P49718;P97310;P97311;Q61881","subunits.Entrez.IDs.":"17215;17217;17218;17216;17219;17220","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0018- two hybrid","GO.ID":"GO:0006260;GO:0007126;GO:0005524;GO:0005694","GO.description":"DNA replication;meiotic nuclear division;ATP binding;chromosome","FunCat.ID":"10.01.03;10.03.02;16.19.03;70.10.03","FunCat.description":"DNA synthesis and replication;meiosis;ATP binding;chromosome","PubMed.ID":12614612,"subunits.Protein.name.":"DNA replication licensing factor MCM3 ;DNA replication licensing factor MCM4 ;DNA replication licensing factor MCM5 ;DNA replication licensing factor MCM2 ;DNA replication licensing factor MCM6 ;DNA replication licensing factor MCM7","subunits.Gene.name.":"Mcm3;Mcm4;Mcm5;Mcm2;Mcm6;Mcm7","subunits.Gene.name.syn.":"Mcmd Mcmd3;Cdc21 Mcmd4;Cdc46 Mcmd5;Bm28 Cdcl1 Kiaa0030 Mcmd2;Mcmd6 Mis5;Cdc47 Mcmd7","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":123,"ComplexName":"Rnase/Mrp complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75817;O75818;O95059;O95707;P78345;P78346;Q969H6;Q99575;Q9BUL9;Q9H633","subunits.Entrez.IDs.":"10248;10799;11102;10775;10557;10556;51367;10940;54913;79897","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006401;GO:0006364;GO:0003723;GO:0005634","GO.description":"RNA catabolic process;rRNA processing;RNA binding;nucleus","FunCat.ID":"01.03.16.01;11.04.01;16.03.03;70.10","FunCat.description":"RNA degradation;rRNA processing;RNA binding;nucleus","PubMed.ID":15096576,"subunits.Protein.name.":"Ribonuclease P protein subunit p20 ;Ribonuclease P protein subunit p40 ;Ribonuclease P protein subunit p14 ;Ribonuclease P protein subunit p29 ;Ribonuclease P protein subunit p38 ;Ribonuclease P protein subunit p30 ;Ribonuclease P/MRP protein subunit POP5 ;Ribonucleases P/MRP protein subunit POP1 ;Ribonuclease P protein subunit p25 ;Ribonuclease P protein subunit p21","subunits.Gene.name.":"POP7;RPP40;RPP14;POP4;RPP38;RPP30;POP5;POP1;RPP25;RPP21","subunits.Gene.name.syn.":"RPP20;RNASEP1;;RPP29;;RNASEP2;;KIAA0061;;C6orf135 CAT60","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"RNase MRP is involved in the processing of pre-rRNA and the generation of RNA primers for mitochondrial DNA replication.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":124,"ComplexName":"RGS9-GNB5-GNAT1-R9AP complex","Organism":"Bovine","Synonyms":"None","Cell.line":"eye","subunits.UniProt.IDs.":"O46469;P04695;Q8MJG0","subunits.Entrez.IDs.":"281453;281794;282338","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0007186;GO:0009583;GO:0009416;GO:0005886","GO.description":"G-protein coupled receptor signaling pathway;detection of light stimulus;response to light stimulus;plasma membrane","FunCat.ID":"30.05.02.24;34.11.01;70.02","FunCat.description":"G-protein coupled receptor signalling pathway;photoperception and response;eukaryotic plasma membrane / membrane attached","PubMed.ID":12119397,"subunits.Protein.name.":"Regulator of G-protein signaling 9;Guanine nucleotide-binding protein G;Regulator of G-protein signaling 9-binding protein","subunits.Gene.name.":"RGS9;GNAT1;RGS9BP","subunits.Gene.name.syn.":"None;None;R9AP","Disease.comment":"None","Subunits.comment":"At the time of annotation, the additional member  GNB5 (Gbeta5) of the protein complex was not found in the UniProt database.","Complex.comment":"None","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":126,"ComplexName":"CCT micro-complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P17987;P40227;P48643;P49368;P50990;P50991;P78371;Q99832","subunits.Entrez.IDs.":"6950;908;22948;7203;10694;10575;10576;10574","Protein.complex.purification.method":"MI:0029-cosedimentation through density gradients;MI:0047-far western blotting","GO.ID":"GO:0050821;GO:0006457;GO:0005515;GO:0005524;GO:0005737","GO.description":"protein stabilization;protein folding;protein binding;ATP binding;cytoplasm","FunCat.ID":"14.01;16.01;16.19.03;70.03","FunCat.description":"protein folding and stabilization;protein binding;ATP binding;cytoplasm","PubMed.ID":9250675,"subunits.Protein.name.":"T-complex protein 1 subunit alpha;T-complex protein 1 subunit zeta;T-complex protein 1 subunit epsilon;T-complex protein 1 subunit gamma;T-complex protein 1 subunit theta;T-complex protein 1 subunit delta;T-complex protein 1 subunit beta;T-complex protein 1 subunit eta","subunits.Gene.name.":"TCP1;CCT6A;CCT5;CCT3;CCT8;CCT4;CCT2;CCT7","subunits.Gene.name.syn.":"CCT1 CCTA;CCT6 CCTZ;CCTE KIAA0098;CCTG TRIC5;C21orf112 CCTQ KIAA0002;CCTD SRB;99D8.1 CCTB;CCTH NIP7-1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The chaperonins are a family of molecular chaperones involved in protein folding, assembly and transport. The chaperonin-containing TCP-1 (CCT) is abundant in eukaryotic cytosol. CCT micro-complexes have mol. wts ranging from 120 to 250 kDa and are present in cells at lower abundance (<5%) as compared with intact CCT.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":127,"ComplexName":"NDC80 kinetochore complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14777;Q8NBT2;Q9BZD4;Q9HBM1","subunits.Entrez.IDs.":"10403;147841;83540;57405","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000278;GO:0007059;GO:0000775","GO.description":"mitotic cell cycle;chromosome segregation;chromosome, centromeric region","FunCat.ID":"10.03.01.01;10.03.04.05;70.10.04","FunCat.description":"mitotic cell cycle;chromosome segregation/division;centromere / kinetochore","PubMed.ID":14699129,"subunits.Protein.name.":"Kinetochore protein NDC80 homolog ;Kinetochore protein Spc24 ;Kinetochore protein Nuf2 ;Kinetochore protein Spc25","subunits.Gene.name.":"NDC80;SPC24;NUF2;SPC25","subunits.Gene.name.syn.":"HEC HEC1 KNTC2;SPBC24;CDCA1 NUF2R;SPBC25","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Components of the conserved NDC80 complex are required for chromosome congression, and their disruption results in mitotic arrest accompanied by multiple spindle aberrations. hSPC25 is an essential kinetochore component that plays a significant role in proper execution of mitotic events.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":128,"ComplexName":"ORC complex (origin recognition complex)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O88708;Q60862;Q9JK30;Q9WUJ8;Q9WUV0;Q9Z1N2","subunits.Entrez.IDs.":"26428;18393;50793;56452;26429;18392","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0018- two hybrid","GO.ID":"GO:0006267;GO:0003688;GO:0005524;GO:0005694","GO.description":"pre-replicative complex assembly involved in nuclear cell cycle DNA replication;DNA replication origin binding;ATP binding;chromosome","FunCat.ID":"10.01.03.03;16.19.03;70.10.03","FunCat.description":"ori recognition and priming complex formation;ATP binding;chromosome","PubMed.ID":12614612,"subunits.Protein.name.":"Origin recognition complex subunit 4;Origin recognition complex subunit 2;Origin recognition complex subunit 3 ;Origin recognition complex subunit 6;Origin recognition complex subunit 5;Origin recognition complex subunit 1","subunits.Gene.name.":"Orc4;Orc2;Orc3;Orc6;Orc5;Orc1","subunits.Gene.name.syn.":"Orc4l;Orc2l;Orc3l;Orc6l;Orc5l;Orc1l","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":129,"ComplexName":"PIDDsome complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P42575;P78560;Q9HB75","subunits.Entrez.IDs.":"835;8738;55367","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006919;GO:0006915","GO.description":"activation of cysteine-type endopeptidase activity involved in apoptotic process;apoptotic process","FunCat.ID":"40.10.02.02.02;40.10.02","FunCat.description":"caspase activation;apoptosis (type I programmed cell death)","PubMed.ID":15073321,"subunits.Protein.name.":"Caspase-2 ;Death domain-containing protein CRADD ;p53-induced death domain-containing protein 1","subunits.Gene.name.":"CASP2;CRADD;PIDD1","subunits.Gene.name.syn.":"ICH1 NEDD2;RAIDD;LRDD PIDD","Disease.comment":"PIDDsome is involved in caspase-2 dependent TSA-induced cell death in prostate cancer cell lines (PMID:17110788).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":130,"ComplexName":"Gamma-secretase complex (Aph1a, Psen1, Psenen, Ncstn)","Organism":"Mouse","Synonyms":"presenilin complex","Cell.line":"None","subunits.UniProt.IDs.":"P49769;P57716;Q8BVF7;Q9CQR7","subunits.Entrez.IDs.":"19164;59287;226548;66340","Protein.complex.purification.method":"MI:0413- electrophoretic mobility shift assay","GO.ID":"GO:0016485;GO:0051090;GO:0023052;GO:0007219;GO:0006928;GO:0043066;GO:0005886;GO:0005794","GO.description":"protein processing;regulation of sequence-specific DNA binding transcription factor activity;signaling;Notch signaling pathway;movement of cell or subcellular component;negative regulation of apoptotic process;plasma membrane;Golgi apparatus","FunCat.ID":"14.07.11;18.02.09;30.01;30.05.02.14;34.05;40.10.02.01;70.02;70.08","FunCat.description":"protein processing (proteolytic);regulator of transcription factor;cellular signalling;Notch-receptor signalling pathway;cell motility;anti-apoptosis;eukaryotic plasma membrane / membrane attached;Golgi","PubMed.ID":14717705,"subunits.Protein.name.":"Presenilin-1 ;Nicastrin;Gamma-secretase subunit APH-1A ;Gamma-secretase subunit PEN-2","subunits.Gene.name.":"Psen1;Ncstn;Aph1a;Psenen","subunits.Gene.name.syn.":"Ad3h Psnl1;;;Pen2","Disease.comment":"None","Subunits.comment":"Three variants of APH1 (APH1A short, APH1A long and APH1B) as well as two presenillin variants (PSEN1 and PSEN2) allow the formation of six different gamma-secretase complexes.","Complex.comment":"Proteolytic cleavage within the hydrophobic transmembrane domains of Notch and APP are intimately associated with a multimeric gamma-secretase complex that contains the presenilin-1 or presenilin-2 and the membrane glycoprotein nicastrin.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":131,"ComplexName":"Skeletal muscle sarcoglycan complex SGC, alpha-beta-gamma-delta","Organism":"Mouse","Synonyms":"None","Cell.line":"striated muscle","subunits.UniProt.IDs.":"P82347;P82348;P82349;P82350","subunits.Entrez.IDs.":"24052;24053;24051;20391","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0030-cross-linking studies","GO.ID":"GO:0006461;GO:0006941;GO:0007519;GO:0014706;GO:0005886","GO.description":"protein complex assembly;striated muscle contraction;skeletal muscle tissue development;striated muscle tissue development;plasma membrane","FunCat.ID":"14.10;36.25.09.03;41.05.15;45.03.12.01;70.02","FunCat.description":"assembly of protein complexes;striated muscle contraction;myogenesis;striated muscle;eukaryotic plasma membrane / membrane attached","PubMed.ID":9864373,"subunits.Protein.name.":"Delta-sarcoglycan;Gamma-sarcoglycan;Beta-sarcoglycan;Alpha-sarcoglycan","subunits.Gene.name.":"Sgcd;Sgcg;Sgcb;Sgca","subunits.Gene.name.syn.":"None;None;None;None","Disease.comment":"Sarcoglycan complex (SGC) is involved in muscular dystrophy and cardiomyopathy (PMID:15117830).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":132,"ComplexName":"CCT complex (chaperonin containing TCP1 complex)","Organism":"Mouse","Synonyms":"TRiC","Cell.line":"None","subunits.UniProt.IDs.":"P11983;P42932;P80313;P80314;P80315;P80316;P80317;P80318","subunits.Entrez.IDs.":"21454;12469;12468;12461;12464;12465;None;12462","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0047-far western blotting;MI:0040-electron microscopy","GO.ID":"GO:0050821;GO:0006457;GO:0005515;GO:0005524;GO:0005737","GO.description":"protein stabilization;protein folding;protein binding;ATP binding;cytoplasm","FunCat.ID":"14.01;16.01;16.19.03;70.03","FunCat.description":"protein folding and stabilization;protein binding;ATP binding;cytoplasm","PubMed.ID":10604479,"subunits.Protein.name.":"T-complex protein 1 subunit alpha;T-complex protein 1 subunit theta;T-complex protein 1 subunit eta;T-complex protein 1 subunit beta;T-complex protein 1 subunit delta;T-complex protein 1 subunit epsilon;T-complex protein 1 subunit zeta;T-complex protein 1 subunit gamma","subunits.Gene.name.":"Tcp1;Cct8;Cct7;Cct2;Cct4;Cct5;Cct6a;Cct3","subunits.Gene.name.syn.":"Cct1 Ccta;Cctq;Ccth;Cctb;Cctd;Ccte Kiaa0098;Cct6 Cctz Cctz1;Cctg","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The chaperonins are a family of molecular chaperones involved in protein folding, assembly and transport. The chaperonin-containing TCP-1 (CCT) is abundant in eukaryotic cytosol.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":136,"ComplexName":"Troponin complex","Organism":"Rabbit","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P02586;P02641;P02643","subunits.Entrez.IDs.":"100009341;None;100009581","Protein.complex.purification.method":"MI:0091- chromatography technologies","GO.ID":"GO:0005509;GO:0006936;GO:0007517;GO:0015629","GO.description":"calcium ion binding;muscle contraction;muscle organ development;actin cytoskeleton","FunCat.ID":"16.17.01;36.25.09;45.03.12;70.04.03","FunCat.description":"calcium binding;muscle contraction;muscle;actin cytoskeleton","PubMed.ID":12395950,"subunits.Protein.name.":"Troponin C, skeletal muscle;Troponin T, fast skeletal muscle ;Troponin I, fast skeletal muscle","subunits.Gene.name.":"TNNC2;TNNT3;TNNI2","subunits.Gene.name.syn.":";;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Oryctolagus cuniculus (Rabbit);Oryctolagus cuniculus (Rabbit);Oryctolagus cuniculus (Rabbit)"}
{"ComplexID":138,"ComplexName":"Telosome complex","Organism":"Human","Synonyms":"telomere-associated protein complex","Cell.line":"None","subunits.UniProt.IDs.":"P54274;Q15554;Q96AP0;Q9BSI4;Q9NUX5;Q9NYB0","subunits.Entrez.IDs.":"7013;7014;65057;26277;25913;54386","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0006461;GO:0003677;GO:0051276;GO:0005634","GO.description":"protein complex assembly;DNA binding;chromosome organization;nucleus","FunCat.ID":"14.10;16.03.01;42.10.03;70.10","FunCat.description":"assembly of protein complexes;DNA binding;organization of chromosome structure;nucleus","PubMed.ID":15383534,"subunits.Protein.name.":"Telomeric repeat-binding factor 1 ;Telomeric repeat-binding factor 2 ;Adrenocortical dysplasia protein homolog ;TERF1-interacting nuclear factor 2 ;Protection of telomeres protein 1 ;Telomeric repeat-binding factor 2-interacting protein 1","subunits.Gene.name.":"TERF1;TERF2;ACD;TINF2;POT1;TERF2IP","subunits.Gene.name.syn.":"PIN2 TRBF1 TRF TRF1;TRBF2 TRF2;PIP1 PTOP TINT1 TPP1;TIN2;;DRIP5 RAP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TIN2 binds TRF2 directly, thereby tethering TRF2 to the TRF1 complex. This complex is responsible for telomere maintenance.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":139,"ComplexName":"SDH-mABC1-PIC-ANT-ATPase complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P15999;P16036;P21913;Q05962;Q5RKI8;Q920L2","subunits.Entrez.IDs.":"65262;245959;298596;85333;362302;157074","Protein.complex.purification.method":"MI:0027-cosedimentation;MI:0019-coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0005743","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;mitochondrial inner membrane","FunCat.ID":"20.01.01.01;20.03.01.01;70.16.05","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;mitochondrial inner membrane","PubMed.ID":15284438,"subunits.Protein.name.":"ATP synthase subunit alpha, mitochondrial;Phosphate carrier protein, mitochondrial;Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial;ADP/ATP translocase 1;ATP-binding cassette sub-family B member 8, mitochondrial;Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial","subunits.Gene.name.":"Atp5a1;Slc25a3;Sdhb;Slc25a4;Abcb8;Sdha","subunits.Gene.name.syn.":"None;Phc;Sdh1;Ant1;None;None","Disease.comment":"None","Subunits.comment":"Since the authors did not specify ADP/ATP translocase, we used isoform Ant1.","Complex.comment":"The complex constitutes the mitochondrial ATP-sensitive K(+) channel.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":140,"ComplexName":"E-box sequence-binding complex","Organism":"Human","Synonyms":"Bex2 protein complex","Cell.line":"None","subunits.UniProt.IDs.":"P25791;Q02577;Q86U70;Q9BXY8","subunits.Entrez.IDs.":"4005;4808;8861;None","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0022008;GO:0048699;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;neurogenesis;generation of neurons;nucleus","FunCat.ID":"11.02.03.04;41.05.13;70.10","FunCat.description":"transcriptional control;neurogenesis;nucleus","PubMed.ID":16314316,"subunits.Protein.name.":"Rhombotin-2 ;Helix-loop-helix protein 2 ;LIM domain-binding protein 1 ;Protein BEX2","subunits.Gene.name.":"LMO2;NHLH2;LDB1;BEX2","subunits.Gene.name.syn.":"RBTN2 RBTNL1 RHOM2 TTG2;BHLHA34 HEN2 KIAA0490;CLIM2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex may help to understand the molecular mechanisms by which hBex2 plays a role in transcriptional regulation in the brain during neurodevelopment.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":141,"ComplexName":"Sos1-Abi1-Eps8 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q08509;Q62245;Q8CBW3","subunits.Entrez.IDs.":"13860;20662;11308","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007264","GO.description":"small GTPase mediated signal transduction","FunCat.ID":"30.01.05.05.01","FunCat.description":"small GTPase mediated signal transduction","PubMed.ID":10499589,"subunits.Protein.name.":"Epidermal growth factor receptor kinase substrate 8;Son of sevenless homolog 1;Abl interactor 1","subunits.Gene.name.":"Eps8;Sos1;Abi1","subunits.Gene.name.syn.":"None;None;Ssh3bp1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors  propose a model in which Eps8 mediates the transfer of signals between Ras and Rac, by forming a complex with E3b1 and Sos1.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":142,"ComplexName":"CD147-gamma-secretase complex (APH-1a, PS-1, PEN-2, NCT variant)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P35613;P49768;Q92542;Q96BI3;Q9NZ42","subunits.Entrez.IDs.":"682;5663;23385;51107;55851","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016485;GO:0023052;GO:0005886;GO:0005794","GO.description":"protein processing;signaling;plasma membrane;Golgi apparatus","FunCat.ID":"14.07.11;30.01;70.02;70.08","FunCat.description":"protein processing (proteolytic);cellular signalling;eukaryotic plasma membrane / membrane attached;Golgi","PubMed.ID":15890777,"subunits.Protein.name.":"Basigin ;Presenilin-1;Nicastrin;Gamma-secretase subunit APH-1A;Gamma-secretase subunit PEN-2","subunits.Gene.name.":"BSG;PSEN1;NCSTN;APH1A;PSENEN","subunits.Gene.name.syn.":";AD3 PS1 PSNL1;KIAA0253;PSF;PEN2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"CD147 in gamma-secretase complex down-modulates the production of amyloid beta-peptides.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":143,"ComplexName":"APP-FE65-LRP complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00213;P05067;Q07954","subunits.Entrez.IDs.":"322;351;4035","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0016485","GO.description":"protein processing","FunCat.ID":"14.07.11","FunCat.description":"protein processing (proteolytic)","PubMed.ID":15115822,"subunits.Protein.name.":"Amyloid beta A4 precursor protein-binding family B member 1 ;Amyloid beta A4 protein;Prolow-density lipoprotein receptor-related protein 1","subunits.Gene.name.":"APBB1;APP;LRP1","subunits.Gene.name.syn.":"FE65 RIR;A4 AD1;A2MR APR","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":144,"ComplexName":"Gamma-BAR-AP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43747;O75843;P56377;P61966;Q10567;Q63HQ0;Q96PC3;Q9BXS5;Q9Y6Q5","subunits.Entrez.IDs.":"164;8906;8905;1174;162;55435;130340;8907;10053","Protein.complex.purification.method":"MI:0018- two hybrid; MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0050789;GO:0016192;GO:0006900;GO:0016050;GO:0006897;GO:0030133","GO.description":"intracellular protein transport;protein targeting;protein transport;regulation of biological process;vesicle-mediated transport;membrane budding;vesicle organization;endocytosis;transport vesicle","FunCat.ID":"14.04;20.01.10;18;20.09.07;20.09.07.25;20.09.18.09.01;70.09","FunCat.description":"protein targeting, sorting and translocation;protein transport;REGULATION OF METABOLISM AND PROTEIN FUNCTION;vesicular transport (Golgi network, etc.);vesicle formation;endocytosis;intracellular transport vesicles","PubMed.ID":15775984,"subunits.Protein.name.":"AP-1 complex subunit gamma-1;AP-1 complex subunit gamma-like 2 ;AP-1 complex subunit sigma-2 ;AP-1 complex subunit sigma-1A ;AP-1 complex subunit beta-1 ;AP-1 complex-associated regulatory protein ;AP-1 complex subunit sigma-3 ;AP-1 complex subunit mu-1 ;AP-1 complex subunit mu-2","subunits.Gene.name.":"AP1G1;AP1G2;AP1S2;AP1S1;AP1B1;AP1AR;AP1S3;AP1M1;AP1M2","subunits.Gene.name.syn.":"ADTG CLAPG1;;;AP19 CLAPS1;ADTB1 BAM22 CLAPB2;C4orf16;;CLTNM;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The isolation of AP1 adaptor complex was described in PMID:9733768.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":145,"ComplexName":"CCT:PFD complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15212;O60925;P61758;Q2NKZ1;Q2T9X2;Q32L40;Q3MHL7;Q3T0K2;Q3T115;Q3ZBH0;Q3ZCI9;Q99471;Q9NQP4;Q9UHV9","subunits.Entrez.IDs.":"10471;5201;7411;514355;613336;512043;521540;504735;533784;505313;281047;5204;5203;5202","Protein.complex.purification.method":"MI:0040-electron microscopy;MI:0028-cosedimentation in solution;MI:0226-ion exchange chromatography","GO.ID":"GO:0050821;GO:0006457;GO:0005515;GO:0005524;GO:0005737","GO.description":"protein stabilization;protein folding;protein binding;ATP binding;cytoplasm","FunCat.ID":"14.01;16.01;16.19.03;70.03","FunCat.description":"protein folding and stabilization;protein binding;ATP binding;cytoplasm","PubMed.ID":12456645,"subunits.Protein.name.":"Prefoldin subunit 6;Prefoldin subunit 1;Prefoldin subunit 3;T-complex protein 1 subunit eta;T-complex protein 1 subunit delta;T-complex protein 1 subunit alpha;T-complex protein 1 subunit zeta;T-complex protein 1 subunit gamma;Chaperonin containing TCP1, subunit 5;T-complex protein 1 subunit beta;T-complex protein 1 subunit theta;Prefoldin subunit 5;Prefoldin subunit 4;Prefoldin subunit 2","subunits.Gene.name.":"PFDN6;PFDN1;VBP1;CCT7;CCT4;TCP1;CCT6A;CCT3;CCT5;CCT2;CCT8;PFDN5;PFDN4;PFDN2","subunits.Gene.name.syn.":"HKE2 PFD6;PFD1;PFDN3;None;None;CCT1;None;None;None;None;None;MM1 PFD5;PFD4;PFD2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The biogenesis of the cytoskeletal proteins actin and tubulin involves interaction of nascent chains of each of the two proteins with the oligomeric protein prefoldin (PFD) and their subsequent transfer to the cytosolic chaperonin CCT (chaperonin containing TCP-1). Three-dimensional reconstruction of the CCT:PFD complex based on cryoelectron microscopy reveals that PFD binds to each of the two CCT rings.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":146,"ComplexName":"Src-dynamin-synapsin complex","Organism":"Mouse","Synonyms":"None","Cell.line":"brain synaptosomes; PC12 cells","subunits.UniProt.IDs.":"O88935;P05480;P39053","subunits.Entrez.IDs.":"20964;20779;13429","Protein.complex.purification.method":"MI:0047-far western blotting;MI:0019-coimmunoprecipitation","GO.ID":"GO:0016079","GO.description":"synaptic vesicle exocytosis","FunCat.ID":"20.09.16.09.05","FunCat.description":"synaptic vesicle exocytosis","PubMed.ID":9539797,"subunits.Protein.name.":"Synapsin-1;Neuronal proto-oncogene tyrosine-protein kinase Src;Dynamin-1","subunits.Gene.name.":"Syn1;Src;Dnm1","subunits.Gene.name.syn.":"Syn-1;pp60c-src;Dnm, Kiaa4093","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The SH3 domain of Src, but not that of the splice variant N-Src, bound to three proteins from mouse synaptosomes or PC12 cells: dynamin, synapsin Ia, and synapsin Ib. Src may play a regulatory role in membrane traffic events that are particularly critical in the neuron.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":147,"ComplexName":"Src-dynamin-synapsin complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P09951;P21575;Q9WUD9","subunits.Entrez.IDs.":"24949;140694;83805","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0048489;GO:0016079","GO.description":"synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.16.09.05","FunCat.description":"synaptic vesicle exocytosis","PubMed.ID":9539797,"subunits.Protein.name.":"Synapsin-1 ;Dynamin-1 ;Proto-oncogene tyrosine-protein kinase Src","subunits.Gene.name.":"Syn1;Dnm1;Src","subunits.Gene.name.syn.":";Dnm;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The SH3 domain of Src, but not that of the splice variant N-Src, bound to three proteins from mouse synaptosomes or PC12 cells: dynamin, synapsin Ia, and synapsin Ib. Src may play a regulatory role in membrane traffic events that are particularly critical in the neuron.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":148,"ComplexName":"Src-dynamin-synapsin-alpha-adaptin complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P09951;P18484;P21575;Q9WUD9","subunits.Entrez.IDs.":"24949;81637;140694;83805","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0048489;GO:0016079","GO.description":"synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.16.09.05","FunCat.description":"synaptic vesicle exocytosis","PubMed.ID":9539797,"subunits.Protein.name.":"Synapsin-1 ;AP-2 complex subunit alpha-2 ;Dynamin-1 ;Proto-oncogene tyrosine-protein kinase Src","subunits.Gene.name.":"Syn1;Ap2a2;Dnm1;Src","subunits.Gene.name.syn.":";Adtab;Dnm;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The identification of a complex containing Src, dynamin, and alpha-adaptin indicates that Src may play a more general role in membrane traffic as well.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":149,"ComplexName":"PBAF complex (Polybromo- and BAF containing complex)","Organism":"Human","Synonyms":"SWI/SNF complex B","Cell.line":"None","subunits.UniProt.IDs.":"O96019;P51532;P60709;Q12824;Q68CP9;Q86U86;Q8TAQ2;Q92922;Q969G3;Q96GM5","subunits.Entrez.IDs.":"86;6597;60;6598;196528;55193;6601;6599;6605;6602","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies;MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":11078522,"subunits.Protein.name.":"Actin-like protein 6A;Transcription activator BRG1;Actin, cytoplasmic 1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;AT-rich interactive domain-containing protein 2;Protein polybromo-1;SWI/SNF complex subunit SMARCC2;SWI/SNF complex subunit SMARCC1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","subunits.Gene.name.":"ACTL6A;SMARCA4;ACTB;SMARCB1;ARID2;PBRM1;SMARCC2;SMARCC1;SMARCE1;SMARCD1","subunits.Gene.name.syn.":"BAF53 BAF53A INO80K;BAF190A BRG1 SNF2B SNF2L4;None;BAF47, INI1, SNF5L1;KIAA1557;BAF180 PB1;BAF170;BAF155;BAF57;BAF60A","Disease.comment":"None","Subunits.comment":"Since the authors did not specify Actin as well as Actin-like protein 6, we used isoform ACTB and isoform ACTL6A, respectively. At the time of annotation, the additional member BAF240 of the protein complex was not found in the UniProt database.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":150,"ComplexName":"CCT complex (chaperonin containing TCP1 complex), testis specific","Organism":"Bovine","Synonyms":"TRiC","Cell.line":"None","subunits.UniProt.IDs.":"Q2NKZ1;Q2T9X2;Q32L40;Q3T084;Q3T0K2;Q3T115;Q3ZBH0;Q3ZCI9","subunits.Entrez.IDs.":"514355;613336;512043;538090;504735;533784;505313;281047","Protein.complex.purification.method":"MI:0027-cosedimentation;MI:0091-chromatography technologies","GO.ID":"GO:0050821;GO:0006457;GO:0005515;GO:0005524;GO:0005737","GO.description":"protein stabilization;protein folding;protein binding;ATP binding;cytoplasm","FunCat.ID":"14.01;16.01;16.19.03;70.03","FunCat.description":"protein folding and stabilization;protein binding;ATP binding;cytoplasm","PubMed.ID":12456645,"subunits.Protein.name.":"T-complex protein 1 subunit eta;T-complex protein 1 subunit delta;T-complex protein 1 subunit alpha;T-complex protein 1 subunit zeta-2;T-complex protein 1 subunit gamma;Chaperonin containing TCP1, subunit 5;T-complex protein 1 subunit beta;T-complex protein 1 subunit theta","subunits.Gene.name.":"CCT7;CCT4;TCP1;CCT6B;CCT3;CCT5;CCT2;CCT8","subunits.Gene.name.syn.":"None;None;CCT1;None;None;None;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The chaperonins are a family of molecular chaperones involved in protein folding, assembly and transport. The chaperonin-containing TCP-1 (CCT) is abundant in eukaryotic cytosol. The gene product of Cct6b has only been detected in testis, whereas the other Cctz gene, Cctz-1, is expressed in all tissues investigated.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":152,"ComplexName":"TFIIE complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P29083;P29084","subunits.Entrez.IDs.":"2960;2961","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006352;GO:2001141;GO:0006355;GO:0005634","GO.description":"DNA-templated transcription, initiation;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;nucleus","FunCat.ID":"11.02.03.01.01;11.02.03.04;70.10","FunCat.description":"transcription initiation;transcriptional control;nucleus","PubMed.ID":9836642,"subunits.Protein.name.":"General transcription factor IIE subunit 1;Transcription initiation factor IIE subunit beta","subunits.Gene.name.":"GTF2E1;GTF2E2","subunits.Gene.name.syn.":"TF2E1;TF2E2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":153,"ComplexName":"TFIIF complex (transcription factor IIF)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P13984;P35269","subunits.Entrez.IDs.":"2963;2962","Protein.complex.purification.method":"MI:0027- cosedimentation","GO.ID":"GO:0006352;GO:0000287;GO:0005524;GO:0005634","GO.description":"DNA-templated transcription, initiation;magnesium ion binding;ATP binding;nucleus","FunCat.ID":"11.02.03.01.01;16.17.07;16.19.03;70.10","FunCat.description":"transcription initiation;magnesium binding;ATP binding;nucleus","PubMed.ID":9836642,"subunits.Protein.name.":"General transcription factor IIF subunit 2 ;General transcription factor IIF subunit 1","subunits.Gene.name.":"GTF2F2;GTF2F1","subunits.Gene.name.syn.":"RAP30;RAP74","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TFIIF facilitates activator-dependent transcription initiation on chromatin templates.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":154,"ComplexName":"Src1-Ep300-Crebbp complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P45481;P70365;Q8BJ14","subunits.Entrez.IDs.":"12914;17977;328572","Protein.complex.purification.method":"MI:0018- two hybrid; MI:0019- coimmunoprecipitation; MI:0004- affinity chromatography technologies","GO.ID":"GO:0045893;GO:0030545;GO:0023052","GO.description":"positive regulation of transcription, DNA-templated;receptor regulator activity;signaling","FunCat.ID":"11.02.03.04.01;18.02.07;30.01","FunCat.description":"transcription activation;regulator of receptor activity;cellular signalling","PubMed.ID":8855229,"subunits.Protein.name.":"CREB-binding protein ;Nuclear receptor coactivator 1 ;Putative uncharacterized protein","subunits.Gene.name.":"Crebbp;Ncoa1;Ep300","subunits.Gene.name.syn.":"Cbp;Src1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":155,"ComplexName":"TFIID complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00268;P20226;P21675;P49848;Q12962;Q15542;Q15544;Q16594;Q6P1X5","subunits.Entrez.IDs.":"6874;6908;6872;6878;6881;6877;6882;6880;6873","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006352;GO:2001141;GO:0006355;GO:0003677;GO:0005634","GO.description":"DNA-templated transcription, initiation;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.01.01;11.02.03.04;16.03.01;70.10","FunCat.description":"transcription initiation;transcriptional control;DNA binding;nucleus","PubMed.ID":9836642,"subunits.Protein.name.":"Transcription initiation factor TFIID subunit 4;TATA-box-binding protein;Transcription initiation factor TFIID subunit 1;Transcription initiation factor TFIID subunit 6;Transcription initiation factor TFIID subunit 10;Transcription initiation factor TFIID subunit 5;Transcription initiation factor TFIID subunit 11;Transcription initiation factor TFIID subunit 9;Transcription initiation factor TFIID subunit 2","subunits.Gene.name.":"TAF4;TBP;TAF1;TAF6;TAF10;TAF5;TAF11;TAF9;TAF2","subunits.Gene.name.syn.":"TAF2C TAF2C1 TAF4A TAFII130 TAFII135;GTF2D1 TF2D TFIID;BA2R CCG1 CCGS TAF2A;TAF2E TAFII70;TAF2A TAF2H TAFII30;TAF2D;TAF2I;TAF2G TAFII31;CIF150 TAF2B","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":156,"ComplexName":"Retrotranslocation complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P57678;Q86TM6;Q9BUN8","subunits.Entrez.IDs.":"50628;84447;79139","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0015031;GO:0008565","GO.description":"protein transport;protein transporter activity","FunCat.ID":"20.01.10","FunCat.description":"protein transport","PubMed.ID":16186510,"subunits.Protein.name.":"Gem-associated protein 4 ;E3 ubiquitin-protein ligase synoviolin ;Derlin-1","subunits.Gene.name.":"GEMIN4;SYVN1;DERL1","subunits.Gene.name.syn.":";HRD1 KIAA1810;DER1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":157,"ComplexName":"Condensin I complex","Organism":"Human","Synonyms":"canonical condensin complex","Cell.line":"None","subunits.UniProt.IDs.":"O95347;Q15003;Q15021;Q9BPX3;Q9NTJ3","subunits.Entrez.IDs.":"10592;23397;9918;64151;10051","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000278;GO:0030261;GO:0051276;GO:0005634","GO.description":"mitotic cell cycle;chromosome condensation;chromosome organization;nucleus","FunCat.ID":"10.03.01.01;10.03.04.03;42.10.03;70.10","FunCat.description":"mitotic cell cycle;chromosome condensation;organization of chromosome structure;nucleus","PubMed.ID":10958694,"subunits.Protein.name.":"Structural maintenance of chromosomes protein 2 ;Condensin complex subunit 2 ;Condensin complex subunit 1 ;Condensin complex subunit 3 ;Structural maintenance of chromosomes protein 4","subunits.Gene.name.":"SMC2;NCAPH;NCAPD2;NCAPG;SMC4","subunits.Gene.name.syn.":"CAPE SMC2L1;BRRN BRRN1 CAPH KIAA0074;CAPD2 CNAP1 KIAA0159;CAPG NYMEL3;CAPC SMC4L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":158,"ComplexName":"ATP synthasome","Organism":"Rat","Synonyms":"ATP synthase-PIC-ANC complex","Cell.line":"None","subunits.UniProt.IDs.":"P05504;P10719;P11608;P15999;P16036;P19511;P21571;P29418;P29419;P31399;P35434;P35435;Q06645;Q06646;Q06647;Q09073;Q71S46","subunits.Entrez.IDs.":"26197;171374;26196;65262;245959;171375;94271;245958;140608;641434;245965;116550;29754;171082;192241;25176;114630","Protein.complex.purification.method":"MI:0047-far western blotting;MI:0027-cosedimentation;MI:0020-transmission electron microscopy;MI:0410-electron tomography","GO.ID":"GO:0006091;GO:0009060","GO.description":"generation of precursor metabolites and energy;aerobic respiration","FunCat.ID":"01;02.13.03","FunCat.description":"METABOLISM;aerobic respiration","PubMed.ID":12560333,"subunits.Protein.name.":"ATP synthase subunit a;ATP synthase subunit beta, mitochondrial;ATP synthase protein 8;ATP synthase subunit alpha, mitochondrial;Phosphate carrier protein, mitochondrial;ATP synthase F;ATP synthase-coupling factor 6, mitochondrial;ATP synthase subunit epsilon, mitochondrial;ATP synthase subunit e, mitochondrial;ATP synthase subunit d, mitochondrial;ATP synthase subunit delta, mitochondrial;ATP synthase subunit gamma, mitochondrial;ATP synthase F;ATP synthase F;ATP synthase subunit O, mitochondrial;ADP/ATP translocase 2;ATP synthase F","subunits.Gene.name.":"Mt-atp6;Atp5b;Mt-atp8;Atp5a1;Slc25a3;Atp5f1;Atp5j;Atp5e;Atp5i;Atp5h;Atp5d;Atp5c1;Atp5g1;Atp5g2;Atp5o;Slc25a5;Atp5g3","subunits.Gene.name.syn.":"Atp6 Atpase6 Mtatp6;None;Atp8 Atpase8 Mtatp8;None;Phc;Atp5f;None;None;None;Atp5jd;None;Atp5c;None;None;None;Ant2;None","Disease.comment":"None","Subunits.comment":"Two additional members of complex have been described as ATP synthase g chain and ATP synthase f chain.","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":159,"ComplexName":"Condensin I-PARP-1-XRCC1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95347;P09874;P18887;Q15003;Q15021;Q9BPX3;Q9NTJ3","subunits.Entrez.IDs.":"10592;142;7515;23397;9918;64151;10051","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0006974;GO:0005634","GO.description":"DNA repair;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;32.01.09;70.10","FunCat.description":"DNA repair;DNA damage response;nucleus","PubMed.ID":16543152,"subunits.Protein.name.":"Structural maintenance of chromosomes protein 2 ;Poly [ADP-ribose] polymerase 1;DNA repair protein XRCC1 ;Condensin complex subunit 2 ;Condensin complex subunit 1 ;Condensin complex subunit 3 ;Structural maintenance of chromosomes protein 4","subunits.Gene.name.":"SMC2;PARP1;XRCC1;NCAPH;NCAPD2;NCAPG;SMC4","subunits.Gene.name.syn.":"CAPE SMC2L1;ADPRT PPOL;;BRRN BRRN1 CAPH KIAA0074;CAPD2 CNAP1 KIAA0159;CAPG NYMEL3;CAPC SMC4L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The association between PARP-1 and XRCC1 was enhanced in response to DNA damage.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":160,"ComplexName":"Condensin II","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95347;P42695;Q6IBW4;Q86XI2;Q9NTJ3","subunits.Entrez.IDs.":"10592;23310;29781;54892;10051","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0000278;GO:0030261;GO:0051276;GO:0005634","GO.description":"mitotic cell cycle;chromosome condensation;chromosome organization;nucleus","FunCat.ID":"10.03.01.01;10.03.04.03;42.10.03;70.10","FunCat.description":"mitotic cell cycle;chromosome condensation;organization of chromosome structure;nucleus","PubMed.ID":14532007,"subunits.Protein.name.":"Structural maintenance of chromosomes protein 2 ;Condensin-2 complex subunit D3 ;Condensin-2 complex subunit H2 ;Condensin-2 complex subunit G2 ;Structural maintenance of chromosomes protein 4","subunits.Gene.name.":"SMC2;NCAPD3;NCAPH2;NCAPG2;SMC4","subunits.Gene.name.syn.":"CAPE SMC2L1;CAPD3 KIAA0056;CAPH2;LUZP5;CAPC SMC4L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":161,"ComplexName":"SWAP complex","Organism":"Mouse","Synonyms":"None","Cell.line":"B-cell","subunits.UniProt.IDs.":"P09405;P11103;Q61937;Q6A028","subunits.Entrez.IDs.":"17975;11545;18148;20947","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0006312;GO:0019724;GO:0005634","GO.description":"mitotic recombination;B cell mediated immunity;nucleus","FunCat.ID":"10.01.05.03.03;36.25.16.03.01;70.10","FunCat.description":"somatic / mitotic recombination;humoral response (B-cells);nucleus","PubMed.ID":9642267,"subunits.Protein.name.":"Nucleolin;Poly [ADP-ribose] polymerase 1;Nucleophosmin;Switch-associated protein 70","subunits.Gene.name.":"Ncl;Parp1;Npm1;Swap70","subunits.Gene.name.syn.":"Nuc;Adprp Adprt Adprt1;None;Kiaa0640","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SWAP complex has recombination activity and is specific for switching B-cells and prefers S-region substrates.S regions, several kilobase pairs in length, contain short, G-rich repetitive sequence elements, often arranged in tandem arrays (PMID:9642267).","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":162,"ComplexName":"Conserved oligomeric Golgi (COG) complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P83436;Q14746;Q8WTW3;Q96JB2;Q96MW5;Q9H9E3;Q9UP83;Q9Y2V7","subunits.Entrez.IDs.":"91949;22796;9382;83548;84342;25839;10466;57511","Protein.complex.purification.method":"MI:0040- electron microscopy; MI:0047- far western blotting; MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0006486;GO:0042125;GO:0006891;GO:0007030;GO:0005794","GO.description":"protein glycosylation;protein galactosylation;intra-Golgi vesicle-mediated transport;Golgi organization;Golgi apparatus","FunCat.ID":"14.07.02;20.09.07.05;42.08;70.08","FunCat.description":"modification with sugar residues (e.g. glycosylation, deglycosylation);intra Golgi transport;Golgi;Golgi","PubMed.ID":11980916,"subunits.Protein.name.":"Conserved oligomeric Golgi complex subunit 7;Conserved oligomeric Golgi complex subunit 2 ;Conserved oligomeric Golgi complex subunit 1 ;Conserved oligomeric Golgi complex subunit 3 ;Conserved oligomeric Golgi complex subunit 8;Conserved oligomeric Golgi complex subunit 4 ;Conserved oligomeric Golgi complex subunit 5;Conserved oligomeric Golgi complex subunit 6","subunits.Gene.name.":"COG7;COG2;COG1;COG3;COG8;COG4;COG5;COG6","subunits.Gene.name.syn.":"None;LDLC;KIAA1381 LDLB;SEC34;None;;GOLTC1 GTC90;KIAA1134","Disease.comment":"Deficiencies in COG1, COG7, COG8 cause a novel group of Cogenital Disorders of Glycosylation II (PMID:17904886).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":163,"ComplexName":"Cohesin-SA2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60216;Q14683;Q8N3U4;Q9UQE7","subunits.Entrez.IDs.":"5885;8243;10735;9126","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0004- affinity chromatography technologies","GO.ID":"GO:0000279;GO:0007067;GO:0007059;GO:0003677;GO:0051276;GO:0005694","GO.description":"M phase;mitotic nuclear division;chromosome segregation;DNA binding;chromosome organization;chromosome","FunCat.ID":"10.03.01.01.11;10.03.04.05;16.03.01;42.10.03;70.10.03","FunCat.description":"M phase;chromosome segregation/division;DNA binding;organization of chromosome structure;chromosome","PubMed.ID":10931856,"subunits.Protein.name.":"Double-strand-break repair protein rad21 homolog ;Structural maintenance of chromosomes protein 1A ;Cohesin subunit SA-2 ;Structural maintenance of chromosomes protein 3","subunits.Gene.name.":"RAD21;SMC1A;STAG2;SMC3","subunits.Gene.name.syn.":"HR21 KIAA0078 NXP1;DXS423E KIAA0178 SB1.8 SMC1 SMC1L1;SA2;BAM BMH CSPG6 SMC3L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":164,"ComplexName":"Cohesin-SA1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60216;Q14683;Q8WVM7;Q9UQE7","subunits.Entrez.IDs.":"5885;8243;10274;9126","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0004- affinity chromatography technologies","GO.ID":"GO:0000279;GO:0007067;GO:0007059;GO:0003677;GO:0051276;GO:0005694","GO.description":"M phase;mitotic nuclear division;chromosome segregation;DNA binding;chromosome organization;chromosome","FunCat.ID":"10.03.01.01.11;10.03.04.05;16.03.01;42.10.03;70.10.03","FunCat.description":"M phase;chromosome segregation/division;DNA binding;organization of chromosome structure;chromosome","PubMed.ID":10931856,"subunits.Protein.name.":"Double-strand-break repair protein rad21 homolog ;Structural maintenance of chromosomes protein 1A ;Cohesin subunit SA-1 ;Structural maintenance of chromosomes protein 3","subunits.Gene.name.":"RAD21;SMC1A;STAG1;SMC3","subunits.Gene.name.syn.":"HR21 KIAA0078 NXP1;DXS423E KIAA0178 SB1.8 SMC1 SMC1L1;SA1;BAM BMH CSPG6 SMC3L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In HeLa cell extracts, the ratio between the hSA1-containing complex (h-cohesin SA1) and the hSA2-containing complex (h-cohesin SA2) is about 1:3.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":165,"ComplexName":"Cohesin-SA1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60216;Q14683;Q8WVM7;Q9UQE7","subunits.Entrez.IDs.":"5885;8243;10274;9126","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0000279;GO:0007067;GO:0007059;GO:0003677;GO:0051276;GO:0005694","GO.description":"M phase;mitotic nuclear division;chromosome segregation;DNA binding;chromosome organization;chromosome","FunCat.ID":"10.03.01.01.11;10.03.04.05;16.03.01;42.10.03;70.10.03","FunCat.description":"M phase;chromosome segregation/division;DNA binding;organization of chromosome structure;chromosome","PubMed.ID":11250156,"subunits.Protein.name.":"Double-strand-break repair protein rad21 homolog ;Structural maintenance of chromosomes protein 1A ;Cohesin subunit SA-1 ;Structural maintenance of chromosomes protein 3","subunits.Gene.name.":"RAD21;SMC1A;STAG1;SMC3","subunits.Gene.name.syn.":"HR21 KIAA0078 NXP1;DXS423E KIAA0178 SB1.8 SMC1 SMC1L1;SA1;BAM BMH CSPG6 SMC3L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The cohesin complex binds directly to double-stranded DNA and induces the formation of large protein-DNA aggregates.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":166,"ComplexName":"Cohesin-SA2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60216;Q14683;Q8N3U4;Q9UQE7","subunits.Entrez.IDs.":"5885;8243;10735;9126","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0000279;GO:0007067;GO:0007059;GO:0003677;GO:0051276;GO:0005694","GO.description":"M phase;mitotic nuclear division;chromosome segregation;DNA binding;chromosome organization;chromosome","FunCat.ID":"10.03.01.01.11;10.03.04.05;16.03.01;42.10.03;70.10.03","FunCat.description":"M phase;chromosome segregation/division;DNA binding;organization of chromosome structure;chromosome","PubMed.ID":11250156,"subunits.Protein.name.":"Double-strand-break repair protein rad21 homolog ;Structural maintenance of chromosomes protein 1A ;Cohesin subunit SA-2 ;Structural maintenance of chromosomes protein 3","subunits.Gene.name.":"RAD21;SMC1A;STAG2;SMC3","subunits.Gene.name.syn.":"HR21 KIAA0078 NXP1;DXS423E KIAA0178 SB1.8 SMC1 SMC1L1;SA2;BAM BMH CSPG6 SMC3L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The cohesin complex binds directly to double-stranded DNA and induces the formation of large protein-DNA aggregates.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":167,"ComplexName":"Condensin I complex","Organism":"Human","Synonyms":"canonical condensin complex","Cell.line":"None","subunits.UniProt.IDs.":"O95347;Q15003;Q15021;Q9BPX3;Q9NTJ3","subunits.Entrez.IDs.":"10592;23397;9918;64151;10051","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0000278;GO:0030261;GO:0051276;GO:0005634","GO.description":"mitotic cell cycle;chromosome condensation;chromosome organization;nucleus","FunCat.ID":"10.03.01.01;10.03.04.03;42.10.03;70.10","FunCat.description":"mitotic cell cycle;chromosome condensation;organization of chromosome structure;nucleus","PubMed.ID":11250156,"subunits.Protein.name.":"Structural maintenance of chromosomes protein 2 ;Condensin complex subunit 2 ;Condensin complex subunit 1 ;Condensin complex subunit 3 ;Structural maintenance of chromosomes protein 4","subunits.Gene.name.":"SMC2;NCAPH;NCAPD2;NCAPG;SMC4","subunits.Gene.name.syn.":"CAPE SMC2L1;BRRN BRRN1 CAPH KIAA0074;CAPD2 CNAP1 KIAA0159;CAPG NYMEL3;CAPC SMC4L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":168,"ComplexName":"Protein-sorting complex (Stam2, Hgs, Eps15)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O88811;P42567;Q99LI8","subunits.Entrez.IDs.":"56324;13858;15239","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031","GO.description":"intracellular protein transport;protein targeting;protein transport","FunCat.ID":"14.04;20.01.10","FunCat.description":"protein targeting, sorting and translocation;protein transport","PubMed.ID":12551915,"subunits.Protein.name.":"Signal transducing adapter molecule 2 ;Epidermal growth factor receptor substrate 15 ;Hepatocyte growth factor-regulated tyrosine kinase substrate","subunits.Gene.name.":"Stam2;Eps15;Hgs","subunits.Gene.name.syn.":"Hbp;;Hrs","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Hrs, Eps15, and STAM proteins function in a multivalent complex that sorts ubiquitinated proteins into the multivesicular body pathway.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":169,"ComplexName":"Protein-sorting complex (Stam1, Hgs, Eps15)","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P42567;Q92783;Q99LI8","subunits.Entrez.IDs.":"13858;8027;15239","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031","GO.description":"intracellular protein transport;protein targeting;protein transport","FunCat.ID":"14.04;20.01.10","FunCat.description":"protein targeting, sorting and translocation;protein transport","PubMed.ID":12551915,"subunits.Protein.name.":"Epidermal growth factor receptor substrate 15 ;Signal transducing adapter molecule 1 ;Hepatocyte growth factor-regulated tyrosine kinase substrate","subunits.Gene.name.":"Eps15;STAM;Hgs","subunits.Gene.name.syn.":";STAM1;Hrs","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Hrs, Eps15, and STAM proteins function in a multivalent complex that sorts ubiquitinated proteins into the multivesicular body pathway.","SWISSPROT.organism":"Mus musculus (Mouse);Homo sapiens (Human);Mus musculus (Mouse)"}
{"ComplexID":170,"ComplexName":"Ric-8A G(i) alpha-1 subunit complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P10824;Q80ZG1","subunits.Entrez.IDs.":"25686;293614","Protein.complex.purification.method":"MI:0018-two hybrid;MI:0027-cosedimentation","GO.ID":"GO:0005085","GO.description":"guanyl-nucleotide exchange factor activity","FunCat.ID":"18.02.03","FunCat.description":"guanyl-nucleotide exchange factor (GEF)","PubMed.ID":12509430,"subunits.Protein.name.":"Guanine nucleotide-binding protein G;Synembryn-A","subunits.Gene.name.":"Gnai1;Ric8a","subunits.Gene.name.syn.":"Gnai-1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":171,"ComplexName":"Ric-8A G(i) alpha-2 subunit complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04897;Q80ZG1","subunits.Entrez.IDs.":"81664;293614","Protein.complex.purification.method":"MI:0018-two hybrid;MI:0027-cosedimentation","GO.ID":"GO:0005085","GO.description":"guanyl-nucleotide exchange factor activity","FunCat.ID":"18.02.03","FunCat.description":"guanyl-nucleotide exchange factor (GEF)","PubMed.ID":12509430,"subunits.Protein.name.":"Guanine nucleotide-binding protein G;Synembryn-A","subunits.Gene.name.":"Gnai2;Ric8a","subunits.Gene.name.syn.":"Gnai-2;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":172,"ComplexName":"Ric-8A G(o) alpha-1 subunit complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P59215;Q80ZG1","subunits.Entrez.IDs.":"50664;293614","Protein.complex.purification.method":"MI:0018-two hybrid;MI:0027-cosedimentation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":12509430,"subunits.Protein.name.":"Guanine nucleotide-binding protein G;Synembryn-A","subunits.Gene.name.":"Gnao1;Ric8a","subunits.Gene.name.syn.":"Gna0 Gnao;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":173,"ComplexName":"MRN complex (MRE11-RAD50-NBN complex)","Organism":"Human","Synonyms":"RAD50-MRE11-p95 complex","Cell.line":"Raji cells","subunits.UniProt.IDs.":"O60934;P49959;Q92878","subunits.Entrez.IDs.":"4683;4361;10111","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006308;GO:0006281;GO:0000075;GO:0003677;GO:0006974;GO:0005634","GO.description":"DNA catabolic process;DNA repair;cell cycle checkpoint;DNA binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"01.03.16.03;10.01.05.01;10.03.01.03;16.03.01;32.01.09;70.10","FunCat.description":"DNA degradation;DNA repair;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA binding;DNA damage response;nucleus","PubMed.ID":9705271,"subunits.Protein.name.":"Nibrin ;Double-strand break repair protein MRE11A ;DNA repair protein RAD50","subunits.Gene.name.":"NBN;MRE11A;RAD50","subunits.Gene.name.syn.":"NBS NBS1 P95;HNGS1 MRE11;","Disease.comment":"Nibrin is mutated in Nijmegen breakage syndrome.","Subunits.comment":"None","Complex.comment":"MRN complex possesses manganese-dependent single-stranded DNA endonuclease and 3' to 5' exonuclease activities, important for recombination, repair, and genomic stability.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":174,"ComplexName":"Ric-8A G(o) alpha-2 subunit complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P59215;Q80ZG1","subunits.Entrez.IDs.":"50664;293614","Protein.complex.purification.method":"MI:0018-two hybrid;MI:0027-cosedimentation","GO.ID":"GO:0005085","GO.description":"guanyl-nucleotide exchange factor activity","FunCat.ID":"18.02.03","FunCat.description":"guanyl-nucleotide exchange factor (GEF)","PubMed.ID":12509430,"subunits.Protein.name.":"Guanine nucleotide-binding protein G;Synembryn-A","subunits.Gene.name.":"Gnao1;Ric8a","subunits.Gene.name.syn.":"Gna0 Gnao;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":175,"ComplexName":"Ric-8A G(q) alpha subunit complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P82471;Q80ZG1","subunits.Entrez.IDs.":"81666;293614","Protein.complex.purification.method":"MI:0018-two hybrid;MI:0027-cosedimentation","GO.ID":"GO:0005085","GO.description":"guanyl-nucleotide exchange factor activity","FunCat.ID":"18.02.03","FunCat.description":"guanyl-nucleotide exchange factor (GEF)","PubMed.ID":12509430,"subunits.Protein.name.":"Guanine nucleotide-binding protein G;Synembryn-A","subunits.Gene.name.":"Gnaq;Ric8a","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":176,"ComplexName":"Ric-8A G alpha 13 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q6Q7Y5;Q80ZG1","subunits.Entrez.IDs.":"303634;293614","Protein.complex.purification.method":"MI:0018-two hybrid;MI:0027-cosedimentation","GO.ID":"GO:0005085","GO.description":"guanyl-nucleotide exchange factor activity","FunCat.ID":"18.02.03","FunCat.description":"guanyl-nucleotide exchange factor (GEF)","PubMed.ID":12509430,"subunits.Protein.name.":"Guanine nucleotide-binding protein subunit alpha-13;Synembryn-A","subunits.Gene.name.":"Gna13;Ric8a","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":177,"ComplexName":"OGT-TRAK1-TRAK2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15294;O60296;Q9UPV9","subunits.Entrez.IDs.":"8473;66008;22906","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0018-two hybrid","GO.ID":"GO:0018126;GO:0006479;GO:0007214","GO.description":"protein hydroxylation;protein methylation;gamma-aminobutyric acid signaling pathway","FunCat.ID":"14.07.09;30.05.02.24.04","FunCat.description":"posttranslational modification of amino acids (e.g. hydroxylation, methylation);gamma-aminobutyric acid signalling pathway","PubMed.ID":12435728,"subunits.Protein.name.":"UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit;Trafficking kinesin-binding protein 2;Trafficking kinesin-binding protein 1","subunits.Gene.name.":"OGT;TRAK2;TRAK1","subunits.Gene.name.syn.":"None;ALS2CR3 KIAA0549;KIAA1042 OIP106","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"O-GlcNAc, OGT, and GRIF-1 could be involved in GABA signaling. GRIF-1 would function as an adaptor/scaffolding protein, bridging OGT to GABAA receptor in this model.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":178,"ComplexName":"Respiratory chain complex I (holoenzyme), mitochondrial","Organism":"Human","Synonyms":"NADH:ubiquinone oxidoreductase (EC 1.6.5.3)","Cell.line":"None","subunits.UniProt.IDs.":"O00217;O00483;O14561;O15239;O43181;O43674;O43676;O43677;O43678;O43920;O75251;O75306;O75380;O75438;O75489;O95139;O95167;O95168;O95169;O95178;O95182;O95298;O95299;O96000;P03886;P03891;P03897;P03901;P03915;P03923;P17568;P19404;P28331;P49821;P51970;P56181;P56556;Q16718;Q16795;Q86Y39;Q9NX14;Q9P0J0;Q9UI09;Q9Y6M9","subunits.Entrez.IDs.":"4728;4697;4706;4694;4724;4711;4709;4717;4695;4725;374291;4720;4726;4707;4722;4712;4696;4710;4714;4708;4701;4718;4705;4716;4535;4536;4537;4539;4540;4541;4713;4729;4719;4723;4702;4731;4700;4698;4704;126328;54539;51079;55967;4715","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0006091;GO:0009060;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":12611891,"subunits.Protein.name.":"NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial;Cytochrome c oxidase subunit NDUFA4;Acyl carrier protein, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1;NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3;NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2;NADH dehydrogenase [ubiquinone] iron-sulfur protein 5;NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1;NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7;NADH dehydrogenase [ubiquinone] 1 subunit C2;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10;NADH-ubiquinone oxidoreductase chain 1;NADH-ubiquinone oxidoreductase chain 2;NADH-ubiquinone oxidoreductase chain 3;NADH-ubiquinone oxidoreductase chain 4L;NADH-ubiquinone oxidoreductase chain 5;NADH-ubiquinone oxidoreductase chain 6;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7;NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial;NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial;NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8;NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9","subunits.Gene.name.":"NDUFS8;NDUFA4;NDUFAB1;NDUFA1;NDUFS4;NDUFB5;NDUFB3;NDUFC1;NDUFA2;NDUFS5;NDUFS7;NDUFS2;NDUFS6;NDUFB1;NDUFS3;NDUFB6;NDUFA3;NDUFB4;NDUFB8;NDUFB2;NDUFA7;NDUFC2;NDUFA10;NDUFB10;MT-ND1;MT-ND2;MT-ND3;MT-ND4L;MT-ND5;MT-ND6;NDUFB7;NDUFV2;NDUFS1;NDUFV1;NDUFA8;NDUFV3;NDUFA6;NDUFA5;NDUFA9;NDUFA11;NDUFB11;NDUFA13;NDUFA12;NDUFB9","subunits.Gene.name.syn.":"None;None;None;None;None;None;None;None;None;None;None;None;None;None;None;None;None;None;None;None;None;None;None;None;MTND1 NADH1 ND1;MTND2 NADH2 ND2;MTND3 NADH3 ND3;MTND4L NADH4L ND4L;MTND5 NADH5 ND5;MTND6 NADH6 ND6;None;None;None;UQOR1;None;None;LYRM6 NADHB14;None;NDUFS2L;None;None;GRIM19;DAP13;LYRM3 UQOR22","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":179,"ComplexName":"Nephrin multiprotein complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"B5DFH1;O88382;P16086;Q62915;Q9R044;Q9WUX0;Q9Z1P2","subunits.Entrez.IDs.":"361598;113970;64159;29647;64563;305614;81634","Protein.complex.purification.method":"MI:0096-pull down;MI:0051-fluorescence technologies;MI:0069-mass spectrometry studies of complexes","GO.ID":"GO:0016337;GO:0007043;GO:0030154","GO.description":"single organismal cell-cell adhesion;cell-cell junction assembly;cell differentiation","FunCat.ID":"34.07.01;42.06.04;40.02","FunCat.description":"cell-cell adhesion;intercellular junction (gap junction/adherens junction);cell differentiation","PubMed.ID":15994232,"subunits.Protein.name.":"Iqgap1 protein;Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2;Spectrin alpha chain, non-erythrocytic 1;Peripheral plasma membrane protein CASK;Nephrin;Beta II spectrin;Alpha-actinin-1","subunits.Gene.name.":"Iqgap1;Magi2;Sptan1;Cask;Nphs1;Sptbn1;Actn1","subunits.Gene.name.syn.":"None;Acvrinp1, Aip1, Sscam;Spna2 Spta2;None;Nphn;Spnb1 sptbn1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":180,"ComplexName":"PNUTS-PP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62136;Q96QC0","subunits.Entrez.IDs.":"5499;5514","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0004857","GO.description":"enzyme inhibitor activity","FunCat.ID":"18.02.01.02","FunCat.description":"enzyme inhibitor","PubMed.ID":12574161,"subunits.Protein.name.":"Serine/threonine-protein phosphatase PP1-alpha catalytic subunit;Serine/threonine-protein phosphatase 1 regulatory subunit 10","subunits.Gene.name.":"PPP1CA;PPP1R10","subunits.Gene.name.syn.":"PPP1A;CAT53 FB19 PNUTS","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":181,"ComplexName":"26S proteasome","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14818;P17980;P20618;P25786;P25787;P25788;P25789;P28066;P28070;P28072;P28074;P35998;P43686;P49720;P49721;P55036;P60900;P62191;P62195;P62333;Q99436;Q9UNM6","subunits.Entrez.IDs.":"5688;5702;5689;5682;5683;5684;5685;5686;5692;5694;5693;5701;5704;5691;5690;5710;5687;5700;5705;5706;5695;5719","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0043161;GO:0006511;GO:0005515;GO:0006950;GO:0005737;GO:0005634","GO.description":"proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;protein binding;response to stress;cytoplasm;nucleus","FunCat.ID":"14.13.01.01;16.01;32.01;70.03;70.10","FunCat.description":"proteasomal degradation (ubiquitin/proteasomal pathway);protein binding;stress response;cytoplasm;nucleus","PubMed.ID":11812135,"subunits.Protein.name.":"Proteasome subunit alpha type-7 ;26S protease regulatory subunit 6A ;Proteasome subunit beta type-1 ;Proteasome subunit alpha type-1 ;Proteasome subunit alpha type-2 ;Proteasome subunit alpha type-3 ;Proteasome subunit alpha type-4 ;Proteasome subunit alpha type-5 ;Proteasome subunit beta type-4 ;Proteasome subunit beta type-6 ;Proteasome subunit beta type-5 ;26S protease regulatory subunit 7 ;26S protease regulatory subunit 6B ;Proteasome subunit beta type-3 ;Proteasome subunit beta type-2 ;26S proteasome non-ATPase regulatory subunit 4 ;Proteasome subunit alpha type-6 ;26S protease regulatory subunit 4 ;26S protease regulatory subunit 8 ;26S protease regulatory subunit 10B ;Proteasome subunit beta type-7 ;26S proteasome non-ATPase regulatory subunit 13","subunits.Gene.name.":"PSMA7;PSMC3;PSMB1;PSMA1;PSMA2;PSMA3;PSMA4;PSMA5;PSMB4;PSMB6;PSMB5;PSMC2;PSMC4;PSMB3;PSMB2;PSMD4;PSMA6;PSMC1;PSMC5;PSMC6;PSMB7;PSMD13","subunits.Gene.name.syn.":"HSPC;TBP1;PSC5;HC2 NU PROS30 PSC2;HC3 PSC3;HC8 PSC8;HC9 PSC9;;PROS26;LMPY Y;LMPX MB1 X;MSS1;MIP224 TBP7;;;MCB1;PROS27;;SUG1;SUG2;Z;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The proteasome is an essential component of the ATP-dependent proteolytic pathway in eukaryotic cells and is responsible for the degradation of most cellular proteins (for reviews see PMID:8811196 and PMID:10872471). It contains a barrel-shaped proteolytic core complex (the 20S proteasome), and is capped at one or both ends by regulatory complexes like the 19S complex (PMID:11812135), modulator (PMID:8621709), PA28 (PMID:9325261) and PA28gamma (PMID:9325261). Interferon-gamma (IFN-gamma) alters the peptide-degrading specificity of proteasomes and produces an immunoproteasome responsible for accelerated processing of nonself endogenous antigens by inducing the replacement of subunits Psmb5, Psmb6 and Psmb7 by Psmb8, Psmb9 and Psmb10, respectively.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":182,"ComplexName":"Synaptotagmin-sodium channel complex (Syt1-Scn1a-Scn1b)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04774;P21707;Q00954","subunits.Entrez.IDs.":"81574;25716;29686","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0006887;GO:0050896;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;exocytosis;response to stimulus;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;20.09.16.09.03;36.25;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;exocytosis;animal specific systemic sensing and response;eukaryotic plasma membrane / membrane attached","PubMed.ID":10737807,"subunits.Protein.name.":"Sodium channel protein type 1 subunit alpha ;Synaptotagmin-1 ;Sodium channel subunit beta-1","subunits.Gene.name.":"Scn1a;Syt1;Scn1b","subunits.Gene.name.syn.":";;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results imply that synaptotagmin can associate with voltage-gated ion channels dependent on and independently of SNARE protein interactions.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":183,"ComplexName":"Synaptotagmin-sodium channel complex (Syt2-Scn1a-Scn1b)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04774;P29101;Q00954","subunits.Entrez.IDs.":"81574;24805;29686","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0006887;GO:0050896;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;exocytosis;response to stimulus;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;20.09.16.09.03;36.25;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;exocytosis;animal specific systemic sensing and response;eukaryotic plasma membrane / membrane attached","PubMed.ID":10737807,"subunits.Protein.name.":"Sodium channel protein type 1 subunit alpha ;Synaptotagmin-2 ;Sodium channel subunit beta-1","subunits.Gene.name.":"Scn1a;Syt2;Scn1b","subunits.Gene.name.syn.":";;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results imply that synaptotagmin can associate with voltage-gated ion channels dependent on and independently of SNARE protein interactions.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":184,"ComplexName":"Synaptotagmin-sodium channel complex  (Syt1-Scn2a-Scn1b)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04775;P21707;Q00954","subunits.Entrez.IDs.":"24766;25716;29686","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0006887;GO:0050896;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;exocytosis;response to stimulus;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;20.09.16.09.03;36.25;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;exocytosis;animal specific systemic sensing and response;eukaryotic plasma membrane / membrane attached","PubMed.ID":10737807,"subunits.Protein.name.":"Sodium channel protein type 2 subunit alpha;Synaptotagmin-1 ;Sodium channel subunit beta-1","subunits.Gene.name.":"Scn2a;Syt1;Scn1b","subunits.Gene.name.syn.":"Scn2a1, Nav1.2;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results imply that synaptotagmin can associate with voltage-gated ion channels dependent on and independently of SNARE protein interactions.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":185,"ComplexName":"Synaptotagmin-sodium channel complex (Syt2-Scn2a-Scn1b)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04775;P29101;Q00954","subunits.Entrez.IDs.":"24766;24805;29686","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0006887;GO:0050896;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;exocytosis;response to stimulus;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;20.09.16.09.03;36.25;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;exocytosis;animal specific systemic sensing and response;eukaryotic plasma membrane / membrane attached","PubMed.ID":10737807,"subunits.Protein.name.":"Sodium channel protein type 2 subunit alpha;Synaptotagmin-2 ;Sodium channel subunit beta-1","subunits.Gene.name.":"Scn2a;Syt2;Scn1b","subunits.Gene.name.syn.":"Scn2a1, Nav1.2;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results imply that synaptotagmin can associate with voltage-gated ion channels dependent on and independently of SNARE protein interactions.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":186,"ComplexName":"Wave-2 complex","Organism":"Human","Synonyms":"WAVE complex; WAVE regulatory complex (WRC)","Cell.line":"None","subunits.UniProt.IDs.":"Q7L576;Q8IZP0;Q8WUW1;Q9Y2A7;Q9Y6W5","subunits.Entrez.IDs.":"23191;10006;55845;10787;10163","Protein.complex.purification.method":"MI:0029-cosedimentation through density gradients;MI:0091-chromatography technologies","GO.ID":"GO:0007264;GO:0016477;GO:0030036;GO:0015629","GO.description":"small GTPase mediated signal transduction;cell migration;actin cytoskeleton organization;actin cytoskeleton","FunCat.ID":"30.01.05.05.01;34.05.01;42.04.03;70.04.03","FunCat.description":"small GTPase mediated signal transduction;cell migration;actin cytoskeleton;actin cytoskeleton","PubMed.ID":15070726,"subunits.Protein.name.":"Cytoplasmic FMR1-interacting protein 1;Abl interactor 1;Protein BRICK1;Nck-associated protein 1;Wiskott-Aldrich syndrome protein family member 2","subunits.Gene.name.":"CYFIP1;ABI1;BRK1;NCKAP1;WASF2","subunits.Gene.name.syn.":"KIAA0068;SSH3BP1;C3orf10;HEM2 KIAA0587 NAP1;WAVE2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Proteins are only present in the complexed form, with the exception of Hspc (C3orf10). The complex is organized around a core of Nap and Abi. Sra is a peripheral subunit recruited on the Nap side, whereas the Wave and Hspc subunits are recruited on the Abi side of the core.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":187,"ComplexName":"Wave-2 complex (Rac-activated)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P28660;Q7TMB8;Q8BH43;Q8BPG5;Q8CBW3","subunits.Entrez.IDs.":"50884;20430;242687;19353;11308","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0007264;GO:0006928;GO:0030036;GO:0015629","GO.description":"small GTPase mediated signal transduction;movement of cell or subcellular component;actin cytoskeleton organization;actin cytoskeleton","FunCat.ID":"30.01.05.05.01;34.05;42.04.03;70.04.03","FunCat.description":"small GTPase mediated signal transduction;cell motility;actin cytoskeleton;actin cytoskeleton","PubMed.ID":14765121,"subunits.Protein.name.":"Nck-associated protein 1 ;Cytoplasmic FMR1-interacting protein 1 ;Wiskott-Aldrich syndrome protein family member 2 ;Putative uncharacterized protein;Abl interactor 1","subunits.Gene.name.":"Nckap1;Cyfip1;Wasf2;Rac1;Abi1","subunits.Gene.name.syn.":"Hem2 Kiaa0587 Nap1;Kiaa0068 Shyc Sra1;Wave2;;Ssh3bp1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The complex is constitutively assembled in the presence and absence of active Rac in vivo. The authors show that Sra-1 and Nap1 colocalize with Abi-1 and WAVE2 at the interface between the lamellipodial actin meshwork and the membrane. These proteins form stable complexes in vivo that can be immunoprecipitated from resting cells, upon Rac activation by AlF treatment and upon overexpression of constitutively active Rac.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":188,"ComplexName":"Wave-2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P28660;Q7TMB8;Q8BH43;Q8CBW3","subunits.Entrez.IDs.":"50884;20430;242687;11308","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0007264;GO:0006928;GO:0030036;GO:0015629","GO.description":"small GTPase mediated signal transduction;movement of cell or subcellular component;actin cytoskeleton organization;actin cytoskeleton","FunCat.ID":"30.01.05.05.01;34.05;42.04.03;70.04.03","FunCat.description":"small GTPase mediated signal transduction;cell motility;actin cytoskeleton;actin cytoskeleton","PubMed.ID":14765121,"subunits.Protein.name.":"Nck-associated protein 1 ;Cytoplasmic FMR1-interacting protein 1 ;Wiskott-Aldrich syndrome protein family member 2 ;Abl interactor 1","subunits.Gene.name.":"Nckap1;Cyfip1;Wasf2;Abi1","subunits.Gene.name.syn.":"Hem2 Kiaa0587 Nap1;Kiaa0068 Shyc Sra1;Wave2;Ssh3bp1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The complex is constitutively assembled in the presence and absence of active Rac in vivo. The authors show that Sra-1 and Nap1 colocalize with Abi-1 and WAVE2 at the interface between the lamellipodial actin meshwork and the membrane. These proteins form stable complexes in vivo that can be immunoprecipitated from resting cells, upon Rac activation by AlF treatment and upon overexpression of constitutively active Rac.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":189,"ComplexName":"BAF complex","Organism":"Human","Synonyms":"SWI/SNF complex A","Cell.line":"None","subunits.UniProt.IDs.":"O14497;O94805;O96019;P51531;P51532;P60709;P63261;Q12824;Q8NFD5;Q8TAQ2;Q92922;Q969G3;Q96GM5","subunits.Entrez.IDs.":"8289;51412;86;6595;6597;60;71;6598;57492;6601;6599;6605;6602","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies;MI:0019-coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045893;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;positive regulation of transcription, DNA-templated;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.01;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription activation;DNA binding;organization of chromosome structure;nucleus","PubMed.ID":11078522,"subunits.Protein.name.":"AT-rich interactive domain-containing protein 1A;Actin-like protein 6B;Actin-like protein 6A;Probable global transcription activator SNF2L2;Transcription activator BRG1;Actin, cytoplasmic 1;Actin, cytoplasmic 2;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;AT-rich interactive domain-containing protein 1B;SWI/SNF complex subunit SMARCC2;SWI/SNF complex subunit SMARCC1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","subunits.Gene.name.":"ARID1A;ACTL6B;ACTL6A;SMARCA2;SMARCA4;ACTB;ACTG1;SMARCB1;ARID1B;SMARCC2;SMARCC1;SMARCE1;SMARCD1","subunits.Gene.name.syn.":"BAF250 BAF250A C1orf4 OSA1 SMARCF1;ACTL6 BAF53B;BAF53 BAF53A INO80K;BAF190B, BRM, SNF2A, SNF2L2;BAF190A BRG1 SNF2B SNF2L4;None;ACTG;BAF47, INI1, SNF5L1;BAF250B DAN15 KIAA1235 OSA2;BAF170;BAF155;BAF57;BAF60A","Disease.comment":"None","Subunits.comment":"Since the authors did not specify Actin as well as Actin-like protein 6 and ARID1, we used isoform ACTB, isoform ACTL6A or isoform ARID1A, respectively. At the time of annotation, the additional member BAF110 of the protein complex was not found in the UniProt database.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":190,"ComplexName":"Mitotic checkpoint complex (MCC)","Organism":"Human","Synonyms":"APC/C inhibitory factor","Cell.line":"None","subunits.UniProt.IDs.":"O43684;O60566;Q12834;Q13257","subunits.Entrez.IDs.":"9184;701;991;4085","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0006- anti bait coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0000075","GO.description":"cell cycle checkpoint","FunCat.ID":"10.03.01.03","FunCat.description":"cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle)","PubMed.ID":11535616,"subunits.Protein.name.":"Mitotic checkpoint protein BUB3;Mitotic checkpoint serine/threonine-protein kinase BUB1 beta ;Cell division cycle protein 20 homolog ;Mitotic spindle assembly checkpoint protein MAD2A","subunits.Gene.name.":"BUB3;BUB1B;CDC20;MAD2L1","subunits.Gene.name.syn.":";BUBR1 MAD3L SSK1;;MAD2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"MCC inhibitory activity is 3,000-fold greater than that of recombinant MAD2, MCC is not generated from kinetochores, as it is also present and active in interphase cells.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":191,"ComplexName":"20S proteasome","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14818;P20618;P25786;P25787;P25788;P25789;P28066;P28070;P28072;P28074;P49720;P49721;P60900;Q99436","subunits.Entrez.IDs.":"5688;5689;5682;5683;5684;5685;5686;5692;5694;5693;5691;5690;5687;5695","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0016485;GO:0043161;GO:0006511;GO:0006950;GO:0005737;GO:0005634","GO.description":"protein processing;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;response to stress;cytoplasm;nucleus","FunCat.ID":"14.07.11;14.13.01.01;32.01;70.03;70.10","FunCat.description":"protein processing (proteolytic);proteasomal degradation (ubiquitin/proteasomal pathway);stress response;cytoplasm;nucleus","PubMed.ID":7811265,"subunits.Protein.name.":"Proteasome subunit alpha type-7 ;Proteasome subunit beta type-1 ;Proteasome subunit alpha type-1 ;Proteasome subunit alpha type-2 ;Proteasome subunit alpha type-3 ;Proteasome subunit alpha type-4 ;Proteasome subunit alpha type-5 ;Proteasome subunit beta type-4 ;Proteasome subunit beta type-6 ;Proteasome subunit beta type-5 ;Proteasome subunit beta type-3 ;Proteasome subunit beta type-2 ;Proteasome subunit alpha type-6 ;Proteasome subunit beta type-7","subunits.Gene.name.":"PSMA7;PSMB1;PSMA1;PSMA2;PSMA3;PSMA4;PSMA5;PSMB4;PSMB6;PSMB5;PSMB3;PSMB2;PSMA6;PSMB7","subunits.Gene.name.syn.":"HSPC;PSC5;HC2 NU PROS30 PSC2;HC3 PSC3;HC8 PSC8;HC9 PSC9;;PROS26;LMPY Y;LMPX MB1 X;;;PROS27;Z","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The proteasome is an essential component of the ATP-dependent proteolytic pathway in eukaryotic cells and is responsible for the degradation of most cellular proteins (for reviews see PMID:8811196 and PMID:10872471). It contains a barrel-shaped proteolytic core complex (the 20S proteasome), and is capped at one or both ends by regulatory complexes like the 19S complex (PMID:11812135), modulator (PMID:8621709), PA28 (PMID:9325261) and PA28gamma (PMID:9325261). Interferon-gamma (IFN-gamma) alters the peptide-degrading specificity of proteasomes and produces an immunoproteasome responsible for accelerated processing of nonself endogenous antigens by inducing the replacement of subunits Psmb5, Psmb6 and Psmb7 by Psmb8, Psmb9 and Psmb10, respectively.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":192,"ComplexName":"PA28-20S proteasome","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14818;P20618;P25786;P25787;P25788;P25789;P28066;P28070;P28072;P28074;P49720;P49721;P60900;Q06323;Q99436;Q9UL46","subunits.Entrez.IDs.":"5688;5689;5682;5683;5684;5685;5686;5692;5694;5693;5691;5690;5687;5720;5695;5721","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0016485;GO:0043161;GO:0006511;GO:0006950;GO:0005737;GO:0005634","GO.description":"protein processing;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;response to stress;cytoplasm;nucleus","FunCat.ID":"14.07.11;14.13.01.01;32.01;70.03;70.10","FunCat.description":"protein processing (proteolytic);proteasomal degradation (ubiquitin/proteasomal pathway);stress response;cytoplasm;nucleus","PubMed.ID":11676531,"subunits.Protein.name.":"Proteasome subunit alpha type-7 ;Proteasome subunit beta type-1 ;Proteasome subunit alpha type-1 ;Proteasome subunit alpha type-2 ;Proteasome subunit alpha type-3 ;Proteasome subunit alpha type-4 ;Proteasome subunit alpha type-5 ;Proteasome subunit beta type-4 ;Proteasome subunit beta type-6 ;Proteasome subunit beta type-5 ;Proteasome subunit beta type-3 ;Proteasome subunit beta type-2 ;Proteasome subunit alpha type-6 ;Proteasome activator complex subunit 1 ;Proteasome subunit beta type-7 ;Proteasome activator complex subunit 2","subunits.Gene.name.":"PSMA7;PSMB1;PSMA1;PSMA2;PSMA3;PSMA4;PSMA5;PSMB4;PSMB6;PSMB5;PSMB3;PSMB2;PSMA6;PSME1;PSMB7;PSME2","subunits.Gene.name.syn.":"HSPC;PSC5;HC2 NU PROS30 PSC2;HC3 PSC3;HC8 PSC8;HC9 PSC9;;PROS26;LMPY Y;LMPX MB1 X;;;PROS27;IFI5111;Z;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The proteasome is an essential component of the ATP-dependent proteolytic pathway in eukaryotic cells and is responsible for the degradation of most cellular proteins (for reviews see PMID:8811196 and PMID:10872471). It contains a barrel-shaped proteolytic core complex (the 20S proteasome), and is capped at one or both ends by regulatory complexes like the 19S complex (PMID:11812135), modulator (PMID:8621709), PA28 (PMID:9325261) and PA28gamma (PMID:9325261). Interferon-gamma (IFN-gamma) alters the peptide-degrading specificity of proteasomes and produces an immunoproteasome responsible for accelerated processing of nonself endogenous antigens by inducing the replacement of subunits Psmb5, Psmb6 and Psmb7 by Psmb8, Psmb9 and Psmb10, respectively.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":193,"ComplexName":"PA700-20S-PA28 complex","Organism":"Human","Synonyms":"proteasome","Cell.line":"None","subunits.UniProt.IDs.":"O00231;O00232;O00233;O00487;O14818;O43242;O75832;P17980;P20618;P25786;P25787;P25788;P25789;P28066;P28070;P28072;P28074;P35998;P43686;P48556;P49720;P49721;P51665;P55036;P60900;P62191;P62195;P62333;Q06323;Q13200;Q15008;Q16401;Q99436;Q99460;Q9UL46;Q9UNM6","subunits.Entrez.IDs.":"5717;5718;5715;10213;5688;5709;5716;5702;5689;5682;5683;5684;5685;5686;5692;5694;5693;5701;5704;5714;5691;5690;5713;5710;5687;5700;5705;5706;5720;5708;9861;5711;5695;5707;5721;5719","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0043161;GO:0006511;GO:0005515;GO:0051098;GO:0016504","GO.description":"proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;protein binding;regulation of binding;peptidase activator activity","FunCat.ID":"14.13.01.01;16.01;18.01.07;18.02.01.01.03","FunCat.description":"proteasomal degradation (ubiquitin/proteasomal pathway);protein binding;regulation by binding / dissociation;protease activator","PubMed.ID":11676531,"subunits.Protein.name.":"26S proteasome non-ATPase regulatory subunit 11 ;26S proteasome non-ATPase regulatory subunit 12 ;26S proteasome non-ATPase regulatory subunit 9 ;26S proteasome non-ATPase regulatory subunit 14 ;Proteasome subunit alpha type-7 ;26S proteasome non-ATPase regulatory subunit 3 ;26S proteasome non-ATPase regulatory subunit 10 ;26S protease regulatory subunit 6A ;Proteasome subunit beta type-1 ;Proteasome subunit alpha type-1 ;Proteasome subunit alpha type-2 ;Proteasome subunit alpha type-3 ;Proteasome subunit alpha type-4 ;Proteasome subunit alpha type-5 ;Proteasome subunit beta type-4 ;Proteasome subunit beta type-6 ;Proteasome subunit beta type-5 ;26S protease regulatory subunit 7 ;26S protease regulatory subunit 6B ;26S proteasome non-ATPase regulatory subunit 8 ;Proteasome subunit beta type-3 ;Proteasome subunit beta type-2 ;26S proteasome non-ATPase regulatory subunit 7 ;26S proteasome non-ATPase regulatory subunit 4 ;Proteasome subunit alpha type-6 ;26S protease regulatory subunit 4 ;26S protease regulatory subunit 8 ;26S protease regulatory subunit 10B ;Proteasome activator complex subunit 1 ;26S proteasome non-ATPase regulatory subunit 2 ;26S proteasome non-ATPase regulatory subunit 6 ;26S proteasome non-ATPase regulatory subunit 5 ;Proteasome subunit beta type-7 ;26S proteasome non-ATPase regulatory subunit 1 ;Proteasome activator complex subunit 2 ;26S proteasome non-ATPase regulatory subunit 13","subunits.Gene.name.":"PSMD11;PSMD12;PSMD9;PSMD14;PSMA7;PSMD3;PSMD10;PSMC3;PSMB1;PSMA1;PSMA2;PSMA3;PSMA4;PSMA5;PSMB4;PSMB6;PSMB5;PSMC2;PSMC4;PSMD8;PSMB3;PSMB2;PSMD7;PSMD4;PSMA6;PSMC1;PSMC5;PSMC6;PSME1;PSMD2;PSMD6;PSMD5;PSMB7;PSMD1;PSME2;PSMD13","subunits.Gene.name.syn.":";;;POH1;HSPC;;;TBP1;PSC5;HC2 NU PROS30 PSC2;HC3 PSC3;HC8 PSC8;HC9 PSC9;;PROS26;LMPY Y;LMPX MB1 X;MSS1;MIP224 TBP7;;;;MOV34L;MCB1;PROS27;;SUG1;SUG2;IFI5111;TRAP2;KIAA0107 PFAAP4;KIAA0072;Z;;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The proteasome is an essential component of the ATP-dependent proteolytic pathway in eukaryotic cells and is responsible for the degradation of most cellular proteins (for reviews see PMID:8811196 and PMID:10872471). It contains a barrel-shaped proteolytic core complex (the 20S proteasome), and is capped at one or both ends by regulatory complexes like the 19S complex (PMID:11812135), modulator (PMID:8621709), PA28 (PMID:9325261) and PA28gamma (PMID:9325261). Interferon-gamma (IFN-gamma) alters the peptide-degrading specificity of proteasomes and produces an immunoproteasome responsible for accelerated processing of nonself endogenous antigens by inducing the replacement of subunits Psmb5, Psmb6 and Psmb7 by Psmb8, Psmb9 and Psmb10, respectively.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":194,"ComplexName":"PA28gamma-20S proteasome","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14818;P20618;P25786;P25787;P25788;P25789;P28066;P28070;P28072;P28074;P49720;P49721;P60900;P61289;Q99436","subunits.Entrez.IDs.":"5688;5689;5682;5683;5684;5685;5686;5692;5694;5693;5691;5690;5687;10197;5695","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0016485;GO:0043161;GO:0006511;GO:0006950;GO:0005737;GO:0005634","GO.description":"protein processing;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;response to stress;cytoplasm;nucleus","FunCat.ID":"14.07.11;14.13.01.01;32.01;70.03;70.10","FunCat.description":"protein processing (proteolytic);proteasomal degradation (ubiquitin/proteasomal pathway);stress response;cytoplasm;nucleus","PubMed.ID":7811265,"subunits.Protein.name.":"Proteasome subunit alpha type-7 ;Proteasome subunit beta type-1 ;Proteasome subunit alpha type-1 ;Proteasome subunit alpha type-2 ;Proteasome subunit alpha type-3 ;Proteasome subunit alpha type-4 ;Proteasome subunit alpha type-5 ;Proteasome subunit beta type-4 ;Proteasome subunit beta type-6 ;Proteasome subunit beta type-5 ;Proteasome subunit beta type-3 ;Proteasome subunit beta type-2 ;Proteasome subunit alpha type-6 ;Proteasome activator complex subunit 3 ;Proteasome subunit beta type-7","subunits.Gene.name.":"PSMA7;PSMB1;PSMA1;PSMA2;PSMA3;PSMA4;PSMA5;PSMB4;PSMB6;PSMB5;PSMB3;PSMB2;PSMA6;PSME3;PSMB7","subunits.Gene.name.syn.":"HSPC;PSC5;HC2 NU PROS30 PSC2;HC3 PSC3;HC8 PSC8;HC9 PSC9;;PROS26;LMPY Y;LMPX MB1 X;;;PROS27;;Z","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The proteasome is an essential component of the ATP-dependent proteolytic pathway in eukaryotic cells and is responsible for the degradation of most cellular proteins (for reviews see PMID:8811196 and PMID:10872471). It contains a barrel-shaped proteolytic core complex (the 20S proteasome), and is capped at one or both ends by regulatory complexes like the 19S complex (PMID:11812135), modulator (PMID:8621709), PA28 (PMID:9325261) and PA28gamma (PMID:9325261). Interferon-gamma (IFN-gamma) alters the peptide-degrading specificity of proteasomes and produces an immunoproteasome responsible for accelerated processing of nonself endogenous antigens by inducing the replacement of subunits Psmb5, Psmb6 and Psmb7 by Psmb8, Psmb9 and Psmb10, respectively.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":195,"ComplexName":"Ubiquitin E3 ligase (Lrrc41, Tceb1, Tceb2, Cul5, Rbx1)","Organism":"Rat","Synonyms":"Muf1-Elongin BC-Cul5-Rbx1 complex","Cell.line":"None","subunits.UniProt.IDs.":"P62870;P83941;Q498D8;Q5M9H1;Q9JJ31","subunits.Entrez.IDs.":"81807;64525;300084;362566;64624","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0005634","GO.description":"protein ubiquitination;protein deubiquitination;nucleus","FunCat.ID":"14.07.05;70.10","FunCat.description":"modification by ubiquitination, deubiquitination;nucleus","PubMed.ID":11384984,"subunits.Protein.name.":"Transcription elongation factor B polypeptide 2 ;Transcription elongation factor B polypeptide 1 ;Protein Rbx1 ;Leucine-rich repeat-containing protein 41;Cullin-5","subunits.Gene.name.":"Tceb2;Tceb1;Rbx1;Lrrc41;Cul5","subunits.Gene.name.syn.":";;;;Vacm1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on target proteins. The ubiquitin ligase is referred to as an E3 and operates in conjunction with an E1 ubiquitin-activating enzyme and an E2 ubiquitin-conjugating enzyme. Polyubiquitination marks proteins for degradation by the proteasome.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":196,"ComplexName":"Ubiquitin E3 ligase (Vhl, Tceb1, Tceb2, Cul5, Rbx1)","Organism":"Rat","Synonyms":"VHL-Elongin BC-Cul5-Rbx1 complex","Cell.line":"None","subunits.UniProt.IDs.":"P62870;P83941;Q498D8;Q64259;Q9JJ31","subunits.Entrez.IDs.":"81807;64525;300084;24874;64624","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579","GO.description":"protein ubiquitination;protein deubiquitination","FunCat.ID":"14.07.05","FunCat.description":"modification by ubiquitination, deubiquitination","PubMed.ID":11384984,"subunits.Protein.name.":"Transcription elongation factor B polypeptide 2 ;Transcription elongation factor B polypeptide 1 ;Protein Rbx1 ;Von Hippel-Lindau disease tumor suppressor ;Cullin-5","subunits.Gene.name.":"Tceb2;Tceb1;Rbx1;Vhl;Cul5","subunits.Gene.name.syn.":";;;;Vacm1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on target proteins. The ubiquitin ligase is referred to as an E3 and operates in conjunction with an E1 ubiquitin-activating enzyme and an E2 ubiquitin-conjugating enzyme. Polyubiquitination marks proteins for degradation by the proteasome.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":197,"ComplexName":"Ubiquitin E3 ligase (Vhl, Tceb1, Tceb2, Cul2, Rbx1)","Organism":"Rat","Synonyms":"VHL-Elongin BC-Cul2-Rbx1 complex","Cell.line":"None","subunits.UniProt.IDs.":"P62870;P83941;Q498D8;Q64259;Q9D4H8","subunits.Entrez.IDs.":"81807;64525;300084;24874;71745","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579","GO.description":"protein ubiquitination;protein deubiquitination","FunCat.ID":"14.07.05","FunCat.description":"modification by ubiquitination, deubiquitination","PubMed.ID":11384984,"subunits.Protein.name.":"Transcription elongation factor B polypeptide 2 ;Transcription elongation factor B polypeptide 1 ;Protein Rbx1 ;Von Hippel-Lindau disease tumor suppressor ;Cullin-2","subunits.Gene.name.":"Tceb2;Tceb1;Rbx1;Vhl;Cul2","subunits.Gene.name.syn.":";;;;","Disease.comment":"None","Subunits.comment":"Since Cul2 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on target proteins. The ubiquitin ligase is referred to as an E3 and operates in conjunction with an E1 ubiquitin-activating enzyme and an E2 ubiquitin-conjugating enzyme. Polyubiquitination marks proteins for degradation by the proteasome.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Mus musculus (Mouse)"}
{"ComplexID":198,"ComplexName":"Ubiquitin E3 ligase (Tceb1, Tceb2, Tceb3, Cul5, Rbx1)","Organism":"Rat","Synonyms":"Elongin A-Elongin BC-Cul5-Rbx1 complex","Cell.line":"None","subunits.UniProt.IDs.":"P62870;P83941;Q498D8;Q63187;Q9JJ31","subunits.Entrez.IDs.":"81807;64525;300084;25562;64624","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579","GO.description":"protein ubiquitination;protein deubiquitination","FunCat.ID":"14.07.05","FunCat.description":"modification by ubiquitination, deubiquitination","PubMed.ID":11384984,"subunits.Protein.name.":"Transcription elongation factor B polypeptide 2 ;Transcription elongation factor B polypeptide 1 ;Protein Rbx1 ;Transcription elongation factor B polypeptide 3 ;Cullin-5","subunits.Gene.name.":"Tceb2;Tceb1;Rbx1;Tceb3;Cul5","subunits.Gene.name.syn.":";;;;Vacm1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on target proteins. The ubiquitin ligase is referred to as an E3 and operates in conjunction with an E1 ubiquitin-activating enzyme and an E2 ubiquitin-conjugating enzyme. Polyubiquitination marks proteins for degradation by the proteasome.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":199,"ComplexName":"Ubiquitin E3 ligase (Socs1, Tceb1, Tceb2, Cul5, Rbx1)","Organism":"Rat","Synonyms":"Socs1-Elongin BC-Cul5-Rbx1 complex","Cell.line":"None","subunits.UniProt.IDs.":"P62870;P83941;Q498D8;Q9JJ31;Q9QX78","subunits.Entrez.IDs.":"81807;64525;300084;64624;252971","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579","GO.description":"protein ubiquitination;protein deubiquitination","FunCat.ID":"14.07.05","FunCat.description":"modification by ubiquitination, deubiquitination","PubMed.ID":11384984,"subunits.Protein.name.":"Transcription elongation factor B polypeptide 2 ;Transcription elongation factor B polypeptide 1 ;Protein Rbx1 ;Cullin-5 ;Suppressor of cytokine signaling 1","subunits.Gene.name.":"Tceb2;Tceb1;Rbx1;Cul5;Socs1","subunits.Gene.name.syn.":";;;Vacm1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on target proteins. The ubiquitin ligase is referred to as an E3 and operates in conjunction with an E1 ubiquitin-activating enzyme and an E2 ubiquitin-conjugating enzyme. Polyubiquitination marks proteins for degradation by the proteasome.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":200,"ComplexName":"Ubiquitin E3 ligase (Wsb1, Tceb1, Tceb2, Cul5, Rbx1)","Organism":"Rat","Synonyms":"Wsb1-Elongin BC-Cul5-Rbx1 complex","Cell.line":"None","subunits.UniProt.IDs.":"P62870;P83941;Q498D8;Q4KM78;Q9JJ31","subunits.Entrez.IDs.":"81807;64525;300084;303336;64624","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511;GO:0005515;GO:0007224;GO:0005783","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;protein binding;smoothened signaling pathway;endoplasmic reticulum","FunCat.ID":"14.07.05;14.13.01.01;16.01;30.05.02.16;70.07","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway);protein binding;hedgehog-dependent signalling pathway;endoplasmic reticulum","PubMed.ID":11384984,"subunits.Protein.name.":"Transcription elongation factor B polypeptide 2 ;Transcription elongation factor B polypeptide 1 ;Protein Rbx1 ;WD repeat and SOCS box-containing 1;Cullin-5","subunits.Gene.name.":"Tceb2;Tceb1;Rbx1;Wsb1;Cul5","subunits.Gene.name.syn.":";;;;Vacm1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on target proteins. The ubiquitin ligase is referred to as an E3 and operates in conjunction with an E1 ubiquitin-activating enzyme and an E2 ubiquitin-conjugating enzyme. Polyubiquitination marks proteins for degradation by the proteasome.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":201,"ComplexName":"HUIC complex","Organism":"Human","Synonyms":"BRCA1-BARD1 complex","Cell.line":"None","subunits.UniProt.IDs.":"P38398;Q99728","subunits.Entrez.IDs.":"672;580","Protein.complex.purification.method":"MI:0226- ion exchange chromatography; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0007050;GO:0000075;GO:0005634","GO.description":"cell cycle arrest;cell cycle checkpoint;nucleus","FunCat.ID":"10.03.01.02;10.03.01.03;70.10","FunCat.description":"cell cycle arrest;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);nucleus","PubMed.ID":11504724,"subunits.Protein.name.":"Breast cancer type 1 susceptibility protein;BRCA1-associated RING domain protein 1","subunits.Gene.name.":"BRCA1;BARD1","subunits.Gene.name.syn.":"RNF53;","Disease.comment":"BRCA1 is involved in breast cancer.","Subunits.comment":"None","Complex.comment":"The HUIC complex has been isolated after treating cells with hydroxyurea.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":202,"ComplexName":"BRCA1-RAD50-MRE11-NBS1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60934;P38398;P49959;Q92878","subunits.Entrez.IDs.":"4683;672;4361;10111","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006281;GO:0006974;GO:0005634","GO.description":"DNA repair;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;32.01.09;70.10","FunCat.description":"DNA repair;DNA damage response;nucleus","PubMed.ID":11504724,"subunits.Protein.name.":"Nibrin ;Breast cancer type 1 susceptibility protein;Double-strand break repair protein MRE11A ;DNA repair protein RAD50","subunits.Gene.name.":"NBN;BRCA1;MRE11A;RAD50","subunits.Gene.name.syn.":"NBS NBS1 P95;RNF53;HNGS1 MRE11;","Disease.comment":"BRCA1 is involved in breast cancer.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":203,"ComplexName":"Ubiquitin E3 ligase (Med8, Tceb1, Tceb2, Cul2, Rbx1)","Organism":"Rat","Synonyms":"Med8-Elongin BC-Cul2-Rbx1 complex","Cell.line":"None","subunits.UniProt.IDs.":"P62870;P83941;Q498D8;Q9D4H8;Q9D7W5","subunits.Entrez.IDs.":"81807;64525;300084;71745;80509","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0005515;GO:0005634","GO.description":"protein ubiquitination;protein deubiquitination;protein binding;nucleus","FunCat.ID":"14.07.05;16.01;70.10","FunCat.description":"modification by ubiquitination, deubiquitination;protein binding;nucleus","PubMed.ID":12149480,"subunits.Protein.name.":"Transcription elongation factor B polypeptide 2 ;Transcription elongation factor B polypeptide 1 ;Protein Rbx1 ;Cullin-2 ;Mediator of RNA polymerase II transcription subunit 8","subunits.Gene.name.":"Tceb2;Tceb1;Rbx1;Cul2;Med8","subunits.Gene.name.syn.":";;;;","Disease.comment":"None","Subunits.comment":"Since Cul2 and Med8 from rat were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":204,"ComplexName":"Ubiquitin E3 ligase (Asb2, Tceb1, Tceb2, Cul5, Rbx1)","Organism":"Rat","Synonyms":"Asb2-Elongin BC-Cul5-Rbx1 complex","Cell.line":"None","subunits.UniProt.IDs.":"P62870;P83941;Q498D8;Q5U2S6;Q9JJ31","subunits.Entrez.IDs.":"81807;64525;300084;299266;64624","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0005515","GO.description":"protein ubiquitination;protein deubiquitination;protein binding","FunCat.ID":"14.07.05;16.01","FunCat.description":"modification by ubiquitination, deubiquitination;protein binding","PubMed.ID":15590664,"subunits.Protein.name.":"Transcription elongation factor B polypeptide 2 ;Transcription elongation factor B polypeptide 1 ;Protein Rbx1 ;Ankyrin repeat and SOCS box protein 2 ;Cullin-5","subunits.Gene.name.":"Tceb2;Tceb1;Rbx1;Asb2;Cul5","subunits.Gene.name.syn.":";;;;Vacm1","Disease.comment":"Results suggest that Asb2 targets specific proteins to destruction by the proteasome in leukemia cells that have been induced to differentiate.","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":205,"ComplexName":"Ubiquitin E3 ligase (VHL, TCEB1, TCEB2, CUL2, RBX1)","Organism":"Human","Synonyms":"VHL-Elongin BC-CUL2-RBX1 complex","Cell.line":"None","subunits.UniProt.IDs.":"P40337;P62877;Q13617;Q15369;Q15370","subunits.Entrez.IDs.":"7428;9978;8453;6921;6923","Protein.complex.purification.method":"MI:0028- cosedimentation in solution","GO.ID":"GO:0016567;GO:0016579;GO:0005515","GO.description":"protein ubiquitination;protein deubiquitination;protein binding","FunCat.ID":"14.07.05;16.01","FunCat.description":"modification by ubiquitination, deubiquitination;protein binding","PubMed.ID":10535940,"subunits.Protein.name.":"Von Hippel-Lindau disease tumor suppressor;E3 ubiquitin-protein ligase RBX1;Cullin-2;Transcription elongation factor B polypeptide 1;Transcription elongation factor B polypeptide 2","subunits.Gene.name.":"VHL;RBX1;CUL2;TCEB1;TCEB2","subunits.Gene.name.syn.":"None;RNF75, ROC1;None;elongin c;elongin b","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":206,"ComplexName":"DNA ligase IV-XRCC4 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P49917;Q13426","subunits.Entrez.IDs.":"3981;7518","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0004- affinity chromatography technologies","GO.ID":"GO:0006281;GO:0006312;GO:0003677;GO:0005694","GO.description":"DNA repair;mitotic recombination;DNA binding;chromosome","FunCat.ID":"10.01.05.01;10.01.05.03.03;16.03.01;70.10.03","FunCat.description":"DNA repair;somatic / mitotic recombination;DNA binding;chromosome","PubMed.ID":9259561,"subunits.Protein.name.":"DNA ligase 4 ;DNA repair protein XRCC4","subunits.Gene.name.":"LIG4;XRCC4","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"XRCC4 serves as a molecular bridge to target DNA ligase IV to a DNA double-strand break.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":207,"ComplexName":"Ubiquitin E3 ligase (ASB2, TCEB1, TCEB2, CUL5, RNF7)","Organism":"Human","Synonyms":"Asb2-Elongin BC-Cul5-Rbx2 complex","Cell.line":"None","subunits.UniProt.IDs.":"Q15369;Q15370;Q93034;Q96Q27;Q9UBF6","subunits.Entrez.IDs.":"6921;6923;8065;51676;9616","Protein.complex.purification.method":"MI:0028- cosedimentation in solution","GO.ID":"GO:0016567;GO:0016579;GO:0005515","GO.description":"protein ubiquitination;protein deubiquitination;protein binding","FunCat.ID":"14.07.05;16.01","FunCat.description":"modification by ubiquitination, deubiquitination;protein binding","PubMed.ID":16325183,"subunits.Protein.name.":"Transcription elongation factor B polypeptide 1;Transcription elongation factor B polypeptide 2;Cullin-5;Ankyrin repeat and SOCS box protein 2 ;RING-box protein 2","subunits.Gene.name.":"TCEB1;TCEB2;CUL5;ASB2;RNF7","subunits.Gene.name.syn.":"elongin c;elongin b;VACM1;;RBX2 ROC2 SAG","Disease.comment":"None","Subunits.comment":"The presence of Elongin BC was predicted by the authors but has not been shown experimentally.","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":208,"ComplexName":"Ubiquitin E3 ligase (ASB1, TCEB1, TCEB2, CUL5, RNF7)","Organism":"Human","Synonyms":"Asb1-Elongin BC-Cul5-Rbx2 complex","Cell.line":"None","subunits.UniProt.IDs.":"Q15369;Q15370;Q93034;Q9UBF6;Q9Y576","subunits.Entrez.IDs.":"6921;6923;8065;9616;51665","Protein.complex.purification.method":"MI:0028- cosedimentation in solution","GO.ID":"GO:0016567;GO:0016579;GO:0005515","GO.description":"protein ubiquitination;protein deubiquitination;protein binding","FunCat.ID":"14.07.05;16.01","FunCat.description":"modification by ubiquitination, deubiquitination;protein binding","PubMed.ID":16325183,"subunits.Protein.name.":"Transcription elongation factor B polypeptide 1;Transcription elongation factor B polypeptide 2;Cullin-5;RING-box protein 2 ;Ankyrin repeat and SOCS box protein 1","subunits.Gene.name.":"TCEB1;TCEB2;CUL5;RNF7;ASB1","subunits.Gene.name.syn.":"elongin c;elongin b;VACM1;RBX2 ROC2 SAG;KIAA1146","Disease.comment":"None","Subunits.comment":"The presence of Elongin BC was predicted by the authors but has not been shown experimentally.","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":209,"ComplexName":"Ubiquitin E3 ligase (ASB6, TCEB1, TCEB2, CUL5, RNF7)","Organism":"Human","Synonyms":"Asb6-Elongin BC-Cul5-Rbx2 complex","Cell.line":"None","subunits.UniProt.IDs.":"Q15369;Q15370;Q93034;Q9NWX5;Q9UBF6","subunits.Entrez.IDs.":"6921;6923;8065;140459;9616","Protein.complex.purification.method":"MI:0028- cosedimentation in solution","GO.ID":"GO:0016567;GO:0016579;GO:0005515","GO.description":"protein ubiquitination;protein deubiquitination;protein binding","FunCat.ID":"14.07.05;16.01","FunCat.description":"modification by ubiquitination, deubiquitination;protein binding","PubMed.ID":16325183,"subunits.Protein.name.":"Transcription elongation factor B polypeptide 1;Transcription elongation factor B polypeptide 2;Cullin-5;Ankyrin repeat and SOCS box protein 6 ;RING-box protein 2","subunits.Gene.name.":"TCEB1;TCEB2;CUL5;ASB6;RNF7","subunits.Gene.name.syn.":"elongin c;elongin b;VACM1;;RBX2 ROC2 SAG","Disease.comment":"None","Subunits.comment":"The presence of Elongin BC was predicted by the authors but has not been shown experimentally.","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":210,"ComplexName":"Ubiquitin E3 ligase (ASB7, TCEB1, TCEB2, CUL5, RNF7)","Organism":"Human","Synonyms":"Asb7-Elongin BC-Cul5-Rbx2 complex","Cell.line":"None","subunits.UniProt.IDs.":"Q15369;Q15370;Q93034;Q9H672;Q9UBF6","subunits.Entrez.IDs.":"6921;6923;8065;140460;9616","Protein.complex.purification.method":"MI:0028- cosedimentation in solution","GO.ID":"GO:0016567;GO:0016579;GO:0005515","GO.description":"protein ubiquitination;protein deubiquitination;protein binding","FunCat.ID":"14.07.05;16.01","FunCat.description":"modification by ubiquitination, deubiquitination;protein binding","PubMed.ID":16325183,"subunits.Protein.name.":"Transcription elongation factor B polypeptide 1;Transcription elongation factor B polypeptide 2;Cullin-5;Ankyrin repeat and SOCS box protein 7 ;RING-box protein 2","subunits.Gene.name.":"TCEB1;TCEB2;CUL5;ASB7;RNF7","subunits.Gene.name.syn.":"elongin c;elongin b;VACM1;;RBX2 ROC2 SAG","Disease.comment":"None","Subunits.comment":"The presence of Elongin BC was predicted by the authors but has not been shown experimentally.","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":211,"ComplexName":"Ubiquitin E3 ligase (ASB12, TCEB1, TCEB2, CUL5, RNF7)","Organism":"Human","Synonyms":"Asb12-Elongin BC-Cul5-Rbx2 complex","Cell.line":"None","subunits.UniProt.IDs.":"Q15369;Q15370;Q8WXK4;Q93034;Q9UBF6","subunits.Entrez.IDs.":"6921;6923;142689;8065;9616","Protein.complex.purification.method":"MI:0028- cosedimentation in solution","GO.ID":"GO:0016567;GO:0016579;GO:0005515","GO.description":"protein ubiquitination;protein deubiquitination;protein binding","FunCat.ID":"14.07.05;16.01","FunCat.description":"modification by ubiquitination, deubiquitination;protein binding","PubMed.ID":16325183,"subunits.Protein.name.":"Transcription elongation factor B polypeptide 1;Transcription elongation factor B polypeptide 2;Ankyrin repeat and SOCS box protein 12 ;Cullin-5;RING-box protein 2","subunits.Gene.name.":"TCEB1;TCEB2;ASB12;CUL5;RNF7","subunits.Gene.name.syn.":"elongin c;elongin b;;VACM1;RBX2 ROC2 SAG","Disease.comment":"None","Subunits.comment":"The presence of Elongin BC was predicted by the authors but has not been shown experimentally.","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":212,"ComplexName":"DNA ligase III-XRCC1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P18887;P49916","subunits.Entrez.IDs.":"7515;3980","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006281;GO:0005634","GO.description":"DNA repair;nucleus","FunCat.ID":"10.01.05.01;70.10","FunCat.description":"DNA repair;nucleus","PubMed.ID":7760816,"subunits.Protein.name.":"DNA repair protein XRCC1 ;DNA ligase 3","subunits.Gene.name.":"XRCC1;LIG3","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":213,"ComplexName":"DNA ligase IV-XRCC1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P18887;P49917","subunits.Entrez.IDs.":"7515;3981","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006281;GO:0005634","GO.description":"DNA repair;nucleus","FunCat.ID":"10.01.05.01;70.10","FunCat.description":"DNA repair;nucleus","PubMed.ID":7760816,"subunits.Protein.name.":"DNA repair protein XRCC1 ;DNA ligase 4","subunits.Gene.name.":"XRCC1;LIG4","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":214,"ComplexName":"Ubiquitin E3 ligase (WSB1, TCEB1, TCEB2, CUL5, RBX1)","Organism":"Human","Synonyms":"WSB1-Elongin BC-CUL5-RBX1 complex","Cell.line":"None","subunits.UniProt.IDs.":"P62877;Q15369;Q15370;Q93034;Q9Y6I7","subunits.Entrez.IDs.":"9978;6921;6923;8065;26118","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511;GO:0005515;GO:0007224;GO:0005783","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;protein binding;smoothened signaling pathway;endoplasmic reticulum","FunCat.ID":"14.07.05;14.13.01.01;16.01;30.05.02.16;70.07","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway);protein binding;hedgehog-dependent signalling pathway;endoplasmic reticulum","PubMed.ID":15965468,"subunits.Protein.name.":"E3 ubiquitin-protein ligase RBX1;Transcription elongation factor B polypeptide 1;Transcription elongation factor B polypeptide 2;Cullin-5;WD repeat and SOCS box-containing protein 1","subunits.Gene.name.":"RBX1;TCEB1;TCEB2;CUL5;WSB1","subunits.Gene.name.syn.":"RNF75, ROC1;elongin c;elongin b;VACM1;SWIP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. WSB-1 is a Hedgehog-inducible ubiquitin ligase that modulates thyroid hormone activation and PTHrP secretion in the developing growth plate.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":216,"ComplexName":"PDZK1-NaPiIIa-MAP17 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q60825;Q9CQH0;Q9JIL4","subunits.Entrez.IDs.":"20505;67182;59020","Protein.complex.purification.method":"MI:0018-two hybrid","GO.ID":"GO:0006811","GO.description":"ion transport","FunCat.ID":"20.01.01","FunCat.description":"ion transport","PubMed.ID":12837682,"subunits.Protein.name.":"Sodium-dependent phosphate transport protein 2A;PDZK1-interacting protein 1;Na(+)/H(+) exchange regulatory cofactor NHE-RF3","subunits.Gene.name.":"Slc34a1;Pdzk1ip1;Pdzk1","subunits.Gene.name.syn.":"Npt2 Slc17a2;Map17;Cap70 Nherf3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":217,"ComplexName":"CRSP complex","Organism":"Human","Synonyms":"cofactor required for Sp1","Cell.line":"None","subunits.UniProt.IDs.":"O43513;O60244;O75448;O95402;Q15648;Q6P2C8;Q9NVC6;Q9ULK4","subunits.Entrez.IDs.":"9443;9282;9862;9441;5469;9442;9440;9439","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0226- ion exchange chromatography","GO.ID":"GO:0045893;GO:0005515;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;protein binding;nucleus","FunCat.ID":"11.02.03.04.01;16.01;70.10","FunCat.description":"transcription activation;protein binding;nucleus","PubMed.ID":10377381,"subunits.Protein.name.":"Mediator of RNA polymerase II transcription subunit 7 ;Mediator of RNA polymerase II transcription subunit 14;Mediator of RNA polymerase II transcription subunit 24;Mediator of RNA polymerase II transcription subunit 26 ;Mediator of RNA polymerase II transcription subunit 1;Mediator of RNA polymerase II transcription subunit 27 ;Mediator of RNA polymerase II transcription subunit 17;Mediator of RNA polymerase II transcription subunit 23","subunits.Gene.name.":"MED7;MED14;MED24;MED26;MED1;MED27;MED17;MED23","subunits.Gene.name.syn.":"ARC34 CRSP9;ARC150 CRSP2 CXorf4 DRIP150 EXLM1 RGR1 TRAP170;ARC100 CRSP4 DRIP100 KIAA0130 THRAP4 TRAP100;ARC70 CRSP7;ARC205 CRSP1 CRSP200 DRIP205 DRIP230 PBP PPARBP PPARGBP RB18A TRAP220 TRIP2;CRSP34 CRSP8;ARC77 CRSP6 DRIP77 DRIP80 TRAP80;ARC130 CRSP3 DRIP130 KIAA1216 SUR2","Disease.comment":"None","Subunits.comment":"Information about the 85kD component CRSP5 of the protein complex is not available in databases.","Complex.comment":"Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":218,"ComplexName":"CRSP complex","Organism":"Human","Synonyms":"cofactor required for Sp1","Cell.line":"None","subunits.UniProt.IDs.":"O43513;O60244;O75448;O95402;Q15648;Q6P2C8;Q9NVC6;Q9ULK4","subunits.Entrez.IDs.":"9443;9282;9862;9441;5469;9442;9440;9439","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0226- ion exchange chromatography","GO.ID":"GO:0045893;GO:0005515;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;protein binding;nucleus","FunCat.ID":"11.02.03.04.01;16.01;70.10","FunCat.description":"transcription activation;protein binding;nucleus","PubMed.ID":9989412,"subunits.Protein.name.":"Mediator of RNA polymerase II transcription subunit 7 ;Mediator of RNA polymerase II transcription subunit 14;Mediator of RNA polymerase II transcription subunit 24;Mediator of RNA polymerase II transcription subunit 26 ;Mediator of RNA polymerase II transcription subunit 1;Mediator of RNA polymerase II transcription subunit 27 ;Mediator of RNA polymerase II transcription subunit 17;Mediator of RNA polymerase II transcription subunit 23","subunits.Gene.name.":"MED7;MED14;MED24;MED26;MED1;MED27;MED17;MED23","subunits.Gene.name.syn.":"ARC34 CRSP9;ARC150 CRSP2 CXorf4 DRIP150 EXLM1 RGR1 TRAP170;ARC100 CRSP4 DRIP100 KIAA0130 THRAP4 TRAP100;ARC70 CRSP7;ARC205 CRSP1 CRSP200 DRIP205 DRIP230 PBP PPARBP PPARGBP RB18A TRAP220 TRIP2;CRSP34 CRSP8;ARC77 CRSP6 DRIP77 DRIP80 TRAP80;ARC130 CRSP3 DRIP130 KIAA1216 SUR2","Disease.comment":"None","Subunits.comment":"At the time of annotation, the additional 85kD component CRSP5 of the protein complex was not found in the UniProt database.","Complex.comment":"Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":219,"ComplexName":"CAND1-CUL1-RBX1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62877;Q13616;Q86VP6","subunits.Entrez.IDs.":"9978;8454;55832","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0005515;GO:0051098;GO:0030234;GO:0050790","GO.description":"protein binding;regulation of binding;enzyme regulator activity;regulation of catalytic activity","FunCat.ID":"16.01;18.01.07;18.02.01","FunCat.description":"protein binding;regulation by binding / dissociation;enzymatic activity regulation / enzyme regulator","PubMed.ID":15537541,"subunits.Protein.name.":"E3 ubiquitin-protein ligase RBX1;Cullin-1;Cullin-associated NEDD8-dissociated protein 1","subunits.Gene.name.":"RBX1;CUL1;CAND1","subunits.Gene.name.syn.":"RNF75, ROC1;None;KIAA0829 TIP120 TIP120A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cand1 forms a tight complex with the Cul1-Roc1 SCF catalytic core, inhibiting the assembly of the multisubunit E3 protein-ubiquitin ligase complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":220,"ComplexName":"ARF-Mule complex","Organism":"Human","Synonyms":"ARF-BP1-ARF-NPM1 complex","Cell.line":"None","subunits.UniProt.IDs.":"P06748;Q7Z6Z7;Q8N726","subunits.Entrez.IDs.":"4869;10075;1029","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0005515;GO:0005634","GO.description":"protein binding;nucleus","FunCat.ID":"16.01;70.10","FunCat.description":"protein binding;nucleus","PubMed.ID":15989956,"subunits.Protein.name.":"Nucleophosmin ;E3 ubiquitin-protein ligase HUWE1 ;Tumor suppressor ARF","subunits.Gene.name.":"NPM1;HUWE1;CDKN2A","subunits.Gene.name.syn.":"NPM;KIAA0312 KIAA1578 UREB1;CDKN2 MLM","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"ARF is an inhibitor of the ARF-BP1 protein-ubiquitin ligase.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":221,"ComplexName":"CAND1-CUL2-RBX1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62877;Q13617;Q86VP6","subunits.Entrez.IDs.":"9978;8453;55832","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0005515;GO:0051098;GO:0005515;GO:0030234;GO:0050790","GO.description":"protein binding;regulation of binding;protein binding;enzyme regulator activity;regulation of catalytic activity","FunCat.ID":"16.01;18.01.07;18.02.01","FunCat.description":"protein binding;regulation by binding / dissociation;enzymatic activity regulation / enzyme regulator","PubMed.ID":12609982,"subunits.Protein.name.":"E3 ubiquitin-protein ligase RBX1;Cullin-2;Cullin-associated NEDD8-dissociated protein 1","subunits.Gene.name.":"RBX1;CUL2;CAND1","subunits.Gene.name.syn.":"RNF75, ROC1;None;KIAA0829 TIP120 TIP120A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Binding of Cand1 to cullins inhibits the formation of E3 protein-ubiquitin ligases.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":222,"ComplexName":"CAND1-CUL3-RBX1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62877;Q13618;Q86VP6","subunits.Entrez.IDs.":"9978;8452;55832","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0005515;GO:0051098;GO:0005515;GO:0030234;GO:0050790","GO.description":"protein binding;regulation of binding;protein binding;enzyme regulator activity;regulation of catalytic activity","FunCat.ID":"16.01;18.01.07;18.02.01","FunCat.description":"protein binding;regulation by binding / dissociation;enzymatic activity regulation / enzyme regulator","PubMed.ID":12609982,"subunits.Protein.name.":"E3 ubiquitin-protein ligase RBX1;Cullin-3;Cullin-associated NEDD8-dissociated protein 1","subunits.Gene.name.":"RBX1;CUL3;CAND1","subunits.Gene.name.syn.":"RNF75, ROC1;KIAA0617;KIAA0829 TIP120 TIP120A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Binding of Cand1 to cullins inhibits the formation of E3 protein-ubiquitin ligases.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":223,"ComplexName":"CAND1-CUL4A-RBX1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62877;Q13619;Q86VP6","subunits.Entrez.IDs.":"9978;8451;55832","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0005515;GO:0051098;GO:0005515;GO:0030234;GO:0050790","GO.description":"protein binding;regulation of binding;protein binding;enzyme regulator activity;regulation of catalytic activity","FunCat.ID":"16.01;18.01.07;18.02.01","FunCat.description":"protein binding;regulation by binding / dissociation;enzymatic activity regulation / enzyme regulator","PubMed.ID":12609982,"subunits.Protein.name.":"E3 ubiquitin-protein ligase RBX1;Cullin-4A;Cullin-associated NEDD8-dissociated protein 1","subunits.Gene.name.":"RBX1;CUL4A;CAND1","subunits.Gene.name.syn.":"RNF75, ROC1;None;KIAA0829 TIP120 TIP120A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Binding of Cand1 to cullins inhibits the formation of E3 protein-ubiquitin ligases.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":224,"ComplexName":"CAND1-CUL4B-RBX1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62877;Q13620;Q86VP6","subunits.Entrez.IDs.":"9978;8450;55832","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0005515;GO:0051098;GO:0005515;GO:0030234;GO:0050790","GO.description":"protein binding;regulation of binding;protein binding;enzyme regulator activity;regulation of catalytic activity","FunCat.ID":"16.01;18.01.07;18.02.01","FunCat.description":"protein binding;regulation by binding / dissociation;enzymatic activity regulation / enzyme regulator","PubMed.ID":12609982,"subunits.Protein.name.":"E3 ubiquitin-protein ligase RBX1;Cullin-4B;Cullin-associated NEDD8-dissociated protein 1","subunits.Gene.name.":"RBX1;CUL4B;CAND1","subunits.Gene.name.syn.":"RNF75, ROC1;KIAA0695;KIAA0829 TIP120 TIP120A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Binding of Cand1 to cullins inhibits the formation of E3 protein-ubiquitin ligases.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":226,"ComplexName":"Ubiquitin E3 ligase (SKP1A, SKP2, CUL1)","Organism":"Human","Synonyms":"SKP1-SKP2-CUL1 complex","Cell.line":"None","subunits.UniProt.IDs.":"P63208;Q13309;Q13616","subunits.Entrez.IDs.":"6500;6502;8454","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0005515","GO.description":"protein ubiquitination;protein deubiquitination;protein binding","FunCat.ID":"14.07.05;16.01","FunCat.description":"modification by ubiquitination, deubiquitination;protein binding","PubMed.ID":12609982,"subunits.Protein.name.":"S-phase kinase-associated protein 1;S-phase kinase-associated protein 2;Cullin-1","subunits.Gene.name.":"SKP1;SKP2;CUL1","subunits.Gene.name.syn.":"EMC19, OCP2, SKP1A, TCEB1L;FBXL1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":227,"ComplexName":"Ubiquitin E3 ligase (SKP1A, BTRC, CUL1)","Organism":"Human","Synonyms":"Skp1-Btrc-Cul1 complex","Cell.line":"None","subunits.UniProt.IDs.":"P63208;Q13616;Q9Y297","subunits.Entrez.IDs.":"6500;8454;8945","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511;GO:0005515","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;protein binding","FunCat.ID":"14.07.05;14.13.01.01;16.01","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway);protein binding","PubMed.ID":9990852,"subunits.Protein.name.":"S-phase kinase-associated protein 1;Cullin-1;F-box/WD repeat-containing protein 1A","subunits.Gene.name.":"SKP1;CUL1;BTRC","subunits.Gene.name.syn.":"EMC19, OCP2, SKP1A, TCEB1L;None;BTRCP FBW1A FBXW1A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":228,"ComplexName":"SMCC complex","Organism":"Human","Synonyms":"SRB/MED-containing cofactor complex","Cell.line":"None","subunits.UniProt.IDs.":"O60244;O75448;O75586;P24863;P49336;Q13503;Q15648;Q9Y3C7","subunits.Entrez.IDs.":"9282;9862;10001;892;1024;9412;5469;51003","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045893;GO:0045892;GO:0005515;GO:0051098;GO:0051090;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;negative regulation of transcription, DNA-templated;protein binding;regulation of binding;regulation of sequence-specific DNA binding transcription factor activity;nucleus","FunCat.ID":"11.02.03.04.01;11.02.03.04.03;16.01;18.01.07;18.02.09;70.10","FunCat.description":"transcription activation;transcription repression;protein binding;regulation by binding / dissociation;regulator of transcription factor;nucleus","PubMed.ID":10024883,"subunits.Protein.name.":"Mediator of RNA polymerase II transcription subunit 14;Mediator of RNA polymerase II transcription subunit 24;Mediator of RNA polymerase II transcription subunit 6 ;Cyclin-C;Cyclin-dependent kinase 8;Mediator of RNA polymerase II transcription subunit 21;Mediator of RNA polymerase II transcription subunit 1;Mediator of RNA polymerase II transcription subunit 31","subunits.Gene.name.":"MED14;MED24;MED6;CCNC;CDK8;MED21;MED1;MED31","subunits.Gene.name.syn.":"ARC150 CRSP2 CXorf4 DRIP150 EXLM1 RGR1 TRAP170;ARC100 CRSP4 DRIP100 KIAA0130 THRAP4 TRAP100;ARC33;None;None;SRB7 SURB7;ARC205 CRSP1 CRSP200 DRIP205 DRIP230 PBP PPARBP PPARGBP RB18A TRAP220 TRIP2;SOH1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":229,"ComplexName":"NAT complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60244;O75586;P24863;P49336;Q13503;Q9BTT4;Q9ULK4","subunits.Entrez.IDs.":"9282;10001;892;1024;9412;84246;9439","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0045892;GO:0005515;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;protein binding;nucleus","FunCat.ID":"11.02.03.04.03;16.01;70.10","FunCat.description":"transcription repression;protein binding;nucleus","PubMed.ID":9734358,"subunits.Protein.name.":"Mediator of RNA polymerase II transcription subunit 14;Mediator of RNA polymerase II transcription subunit 6 ;Cyclin-C;Cyclin-dependent kinase 8;Mediator of RNA polymerase II transcription subunit 21;Mediator of RNA polymerase II transcription subunit 10 ;Mediator of RNA polymerase II transcription subunit 23","subunits.Gene.name.":"MED14;MED6;CCNC;CDK8;MED21;MED10;MED23","subunits.Gene.name.syn.":"ARC150 CRSP2 CXorf4 DRIP150 EXLM1 RGR1 TRAP170;ARC33;None;None;SRB7 SURB7;;ARC130 CRSP3 DRIP130 KIAA1216 SUR2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"A complex, NAT, that represses activation of transcription by RNAPII has been isolated. The NAT complex is composed of approximately 20 polypeptides and includes a subset of the Srb polypeptides, hSrb7, hSrb10, and hSrb11, as well as hRgr1 and hMed6. The presence of hSrb10, hSrb11, and hRgr1 in a complex that functions to down-regulate transcription is consistent with studies in yeast demonstrating that Srb8-Srb11, as well as Rgr1, function as negative regulators of transcription in vivo. It has been suggested that the NAT complex is a subcomplex of the RNAPII holoenzyme and its function and regulation is through the RNAPII holoenzyme. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":230,"ComplexName":"Mediator complex","Organism":"Human","Synonyms":"Mediator of transcriptional regulation","Cell.line":"None","subunits.UniProt.IDs.":"A0JLT2;O43513;O60244;O75448;O75586;O95402;P24863;P49336;Q13503;Q15528;Q15648;Q6P2C8;Q71F56;Q71SY5;Q93074;Q96G25;Q96HR3;Q96RN5;Q9BTT4;Q9BUE0;Q9BWU1;Q9H204;Q9H944;Q9NPJ6;Q9NVC6;Q9NWA0;Q9NX70;Q9P086;Q9UHV7;Q9ULK4;Q9Y2X0;Q9Y3C7","subunits.Entrez.IDs.":"219541;9443;9282;9862;10001;9441;892;1024;9412;6837;5469;9442;23389;81857;9968;112950;90390;51586;84246;54797;23097;80306;9477;29079;9440;55090;55588;400569;9969;9439;10025;51003","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation; MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0045893;GO:0005515;GO:0051098;GO:0005515;GO:0051090;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;protein binding;regulation of binding;protein binding;regulation of sequence-specific DNA binding transcription factor activity;nucleus","FunCat.ID":"11.02.03.04.01;16.01;18.01.07;18.02.09;70.10","FunCat.description":"transcription activation;protein binding;regulation by binding / dissociation;regulator of transcription factor;nucleus","PubMed.ID":15175163,"subunits.Protein.name.":"Mediator of RNA polymerase II transcription subunit 19 ;Mediator of RNA polymerase II transcription subunit 7 ;Mediator of RNA polymerase II transcription subunit 14;Mediator of RNA polymerase II transcription subunit 24;Mediator of RNA polymerase II transcription subunit 6 ;Mediator of RNA polymerase II transcription subunit 26 ;Cyclin-C;Cyclin-dependent kinase 8;Mediator of RNA polymerase II transcription subunit 21;Mediator of RNA polymerase II transcription subunit 22 ;Mediator of RNA polymerase II transcription subunit 1;Mediator of RNA polymerase II transcription subunit 27 ;Mediator of RNA polymerase II transcription subunit 13-like ;Mediator of RNA polymerase II transcription subunit 25 ;Mediator of RNA polymerase II transcription subunit 12;Mediator of RNA polymerase II transcription subunit 8 ;Mediator of RNA polymerase II transcription subunit 30 ;Mediator of RNA polymerase II transcription subunit 15;Mediator of RNA polymerase II transcription subunit 10 ;Mediator of RNA polymerase II transcription subunit 18 ;Cyclin-dependent kinase 19 ;Mediator of RNA polymerase II transcription subunit 28 ;Mediator of RNA polymerase II transcription subunit 20 ;Mediator of RNA polymerase II transcription subunit 4 ;Mediator of RNA polymerase II transcription subunit 17;Mediator of RNA polymerase II transcription subunit 9 ;Mediator of RNA polymerase II transcription subunit 29 ;Mediator of RNA polymerase II transcription subunit 11 ;Mediator of RNA polymerase II transcription subunit 13 ;Mediator of RNA polymerase II transcription subunit 23 ;Mediator of RNA polymerase II transcription subunit 16;Mediator of RNA polymerase II transcription subunit 31","subunits.Gene.name.":"MED19;MED7;MED14;MED24;MED6;MED26;CCNC;CDK8;MED21;MED22;MED1;MED27;MED13L;MED25;MED12;MED8;MED30;MED15;MED10;MED18;CDK19;MED28;MED20;MED4;MED17;MED9;MED29;MED11;MED13;MED23;MED16;MED31","subunits.Gene.name.syn.":"LCMR1;ARC34 CRSP9;ARC150 CRSP2 CXorf4 DRIP150 EXLM1 RGR1 TRAP170;ARC100 CRSP4 DRIP100 KIAA0130 THRAP4 TRAP100;ARC33;ARC70 CRSP7;None;None;SRB7 SURB7;SURF5;ARC205 CRSP1 CRSP200 DRIP205 DRIP230 PBP PPARBP PPARGBP RB18A TRAP220 TRIP2;CRSP34 CRSP8;KIAA1025 PROSIT240 THRAP2 TRAP240L;ACID1 ARC92 PTOV2;ARC240 CAGH45 HOPA KIAA0192 TNRC11 TRAP230;;THRAP6 TRAP25;ARC105 CTG7A PCQAP TIG1 TNRC7;;;CDC2L6 CDK11 KIAA1028;EG1;TRFP;ARC36 DRIP36 VDRIP;ARC77 CRSP6 DRIP77 DRIP80 TRAP80;MED25;IXL;;ARC250 KIAA0593 THRAP1 TRAP240;ARC130 CRSP3 DRIP130 KIAA1216 SUR2;DRIP92 THRAP5;SOH1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Regulation of transcription by RNA polymerase II (Pol II) is controlled by specific combinations of sequence-specific, DNA binding regulatory transcription factors (TFs) bound to a gene's promoter and enhancer regions. These TFs interact with several multiprotein complexes that remodel the chromatin context of the promoter, integrate signals from multiple TFs to control the frequency of transcription initiation, and regulate the efficiency of transcription elongation. One such complex is the Mediator, an ~2-megadalton complex of 20 to 30 subunits that is believed to function as a molecular bridge by simultaneously interacting with both DNA-bound TFs and Pol II. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":232,"ComplexName":"ARC complex","Organism":"Human","Synonyms":"activator-recruited cofactor","Cell.line":"None","subunits.UniProt.IDs.":"O43513;O60244;O75448;O75586;O95402;Q15648;Q71SY5;Q93074;Q96G25;Q96RN5;Q9NPJ6;Q9NVC6;Q9UHV7;Q9UKU7;Q9ULK4","subunits.Entrez.IDs.":"9443;9282;9862;10001;9441;5469;81857;9968;112950;51586;29079;9440;9969;27034;9439","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0045893;GO:0005515;GO:0051098;GO:0005515;GO:0051090;GO:0035556;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;protein binding;regulation of binding;protein binding;regulation of sequence-specific DNA binding transcription factor activity;intracellular signal transduction;nucleus","FunCat.ID":"11.02.03.04.01;16.01;18.01.07;18.02.09;30.01;70.10","FunCat.description":"transcription activation;protein binding;regulation by binding / dissociation;regulator of transcription factor;cellular signalling;nucleus","PubMed.ID":10235267,"subunits.Protein.name.":"Mediator of RNA polymerase II transcription subunit 7 ;Mediator of RNA polymerase II transcription subunit 14;Mediator of RNA polymerase II transcription subunit 24;Mediator of RNA polymerase II transcription subunit 6 ;Mediator of RNA polymerase II transcription subunit 26 ;Mediator of RNA polymerase II transcription subunit 1;Mediator of RNA polymerase II transcription subunit 25 ;Mediator of RNA polymerase II transcription subunit 12;Mediator of RNA polymerase II transcription subunit 8 ;Mediator of RNA polymerase II transcription subunit 15;Mediator of RNA polymerase II transcription subunit 4 ;Mediator of RNA polymerase II transcription subunit 17;Mediator of RNA polymerase II transcription subunit 13 ;Isobutyryl-CoA dehydrogenase, mitochondrial ;Mediator of RNA polymerase II transcription subunit 23","subunits.Gene.name.":"MED7;MED14;MED24;MED6;MED26;MED1;MED25;MED12;MED8;MED15;MED4;MED17;MED13;ACAD8;MED23","subunits.Gene.name.syn.":"ARC34 CRSP9;ARC150 CRSP2 CXorf4 DRIP150 EXLM1 RGR1 TRAP170;ARC100 CRSP4 DRIP100 KIAA0130 THRAP4 TRAP100;ARC33;ARC70 CRSP7;ARC205 CRSP1 CRSP200 DRIP205 DRIP230 PBP PPARBP PPARGBP RB18A TRAP220 TRIP2;ACID1 ARC92 PTOV2;ARC240 CAGH45 HOPA KIAA0192 TNRC11 TRAP230;;ARC105 CTG7A PCQAP TIG1 TNRC7;ARC36 DRIP36 VDRIP;ARC77 CRSP6 DRIP77 DRIP80 TRAP80;ARC250 KIAA0593 THRAP1 TRAP240;ARC42 IBD;ARC130 CRSP3 DRIP130 KIAA1216 SUR2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Experiemts show that the transcription coactivator ARC is required for SREBP (sterol regulatory element binding protein) control of cholesterol and lipid homeostasis. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors. According to authors, the ARC complex is probably identical to the DRIP complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":234,"ComplexName":"HuCHRAC complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60264;Q9NRF9;Q9NRG0;Q9NRL2","subunits.Entrez.IDs.":"8467;54107;54108;11177","Protein.complex.purification.method":"MI:0226- ion exchange chromatography","GO.ID":"GO:0006265;GO:0005515;GO:0003677;GO:0005524;GO:0005634","GO.description":"DNA topological change;protein binding;DNA binding;ATP binding;nucleus","FunCat.ID":"10.01.09.05;16.01;16.03.01;16.19.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);protein binding;DNA binding;ATP binding;nucleus","PubMed.ID":10880450,"subunits.Protein.name.":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5;DNA polymerase epsilon subunit 3;Chromatin accessibility complex protein 1 ;Bromodomain adjacent to zinc finger domain protein 1A","subunits.Gene.name.":"SMARCA5;POLE3;CHRAC1;BAZ1A","subunits.Gene.name.syn.":"SNF2H WCRF135;CHRAC17;CHRAC15;ACF1 WCRF180","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"HuCHRAC is a member of the ISWI-containing chromatin remodelling complexes. The polyclonal antibodies against ISWI do not discriminate between hSNF2L and hSNF2H.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":235,"ComplexName":"WICH complex","Organism":"Mouse","Synonyms":"WSTF-ISWI chromatin remodeling complex","Cell.line":"None","subunits.UniProt.IDs.":"Q91ZW3;Q9Z277","subunits.Entrez.IDs.":"93762;22385","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006265;GO:0005515;GO:0003677;GO:0005694","GO.description":"DNA topological change;protein binding;DNA binding;chromosome","FunCat.ID":"10.01.09.05;16.01;16.03.01;70.10.03","FunCat.description":"DNA conformation modification (e.g. chromatin);protein binding;DNA binding;chromosome","PubMed.ID":11980720,"subunits.Protein.name.":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5 ;Tyrosine-protein kinase BAZ1B","subunits.Gene.name.":"Smarca5;Baz1b","subunits.Gene.name.syn.":"Snf2h;Wbscr9 Wstf","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"WICH is a member of the ISWI-containing chromatin remodelling complexes.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":236,"ComplexName":"WICH complex","Organism":"Human","Synonyms":"WSTF-ISWI chromatin remodeling complex","Cell.line":"None","subunits.UniProt.IDs.":"O60264;Q9UIG0","subunits.Entrez.IDs.":"8467;9031","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006265;GO:0005515;GO:0003677;GO:0005524;GO:0005694","GO.description":"DNA topological change;protein binding;DNA binding;ATP binding;chromosome","FunCat.ID":"10.01.09.05;16.01;16.03.01;16.19.03;70.10.03","FunCat.description":"DNA conformation modification (e.g. chromatin);protein binding;DNA binding;ATP binding;chromosome","PubMed.ID":11980720,"subunits.Protein.name.":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5;Tyrosine-protein kinase BAZ1B","subunits.Gene.name.":"SMARCA5;BAZ1B","subunits.Gene.name.syn.":"SNF2H WCRF135;WBSC10 WBSCR10 WBSCR9 WSTF","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"WICH is a member of the ISWI-containing chromatin remodelling complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":237,"ComplexName":"Ags3-Lkb1-Gnai3 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P08753;Q9R080","subunits.Entrez.IDs.":"25643;246254","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0007186","GO.description":"G-protein coupled receptor signaling pathway","FunCat.ID":"30.05.02.24","FunCat.description":"G-protein coupled receptor signalling pathway","PubMed.ID":12719437,"subunits.Protein.name.":"Guanine nucleotide-binding protein G;G-protein-signaling modulator 1","subunits.Gene.name.":"Gnai3;Gpsm1","subunits.Gene.name.syn.":"Gnai-3;Ags3","Disease.comment":"None","Subunits.comment":"At the time of annotation, the additional member Lkb1 (Stk11) of the protein complex was not found in the UniProt database.","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":238,"ComplexName":"SWI-SNF chromatin remodeling-related-BRCA1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14497;O96019;P38398;P51531;P51532;Q12824;Q8TAQ2;Q92922;Q92925;Q969G3","subunits.Entrez.IDs.":"8289;86;672;6595;6597;6598;6601;6599;6603;6605","Protein.complex.purification.method":"MI:0071-molecular sieving;MI:0004-affinity chromatography technologies","GO.ID":"GO:0006265;GO:2001141;GO:0006355;GO:0051276;GO:0005634","GO.description":"DNA topological change;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcriptional control;organization of chromosome structure;nucleus","PubMed.ID":10943845,"subunits.Protein.name.":"AT-rich interactive domain-containing protein 1A;Actin-like protein 6A;Breast cancer type 1 susceptibility protein;Probable global transcription activator SNF2L2;Transcription activator BRG1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;SWI/SNF complex subunit SMARCC2;SWI/SNF complex subunit SMARCC1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","subunits.Gene.name.":"ARID1A;ACTL6A;BRCA1;SMARCA2;SMARCA4;SMARCB1;SMARCC2;SMARCC1;SMARCD2;SMARCE1","subunits.Gene.name.syn.":"BAF250 BAF250A C1orf4 OSA1 SMARCF1;BAF53 BAF53A INO80K;RNF53;BAF190B, BRM, SNF2A, SNF2L2;BAF190A BRG1 SNF2B SNF2L4;BAF47, INI1, SNF5L1;BAF170;BAF155;BAF60B;BAF57","Disease.comment":"BRCA1 gene is involved in breast and ovarian cancers.","Subunits.comment":"Since the authors did not specify Actin-like protein 6, we used isoform ACTL6A.","Complex.comment":"BRCA1 interacts directly with BRG1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":239,"ComplexName":"Sin3-Hdac1-Sds3 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O09106;Q62141;Q8BR65","subunits.Entrez.IDs.":"433759;20467;71954","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0032774;GO:0006473;GO:0006476;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;RNA biosynthetic process;protein acetylation;protein deacetylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;11.02;14.07.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;RNA synthesis;modification by acetylation, deacetylation;organization of chromosome structure;nucleus","PubMed.ID":11909966,"subunits.Protein.name.":"Histone deacetylase 1;Paired amphipathic helix protein Sin3b ;Sin3 histone deacetylase corepressor complex component SDS3","subunits.Gene.name.":"Hdac1;Sin3b;Suds3","subunits.Gene.name.syn.":"None;Kiaa0700;Sds3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":240,"ComplexName":"BRCA1-CTIP-ZBRK1 repressor complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P38398;Q99708;Q9GZX5","subunits.Entrez.IDs.":"672;5932;59348","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0045892;GO:0003677;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04.03;16.03.01;70.10","FunCat.description":"transcription repression;DNA binding;nucleus","PubMed.ID":16843262,"subunits.Protein.name.":"Breast cancer type 1 susceptibility protein;DNA endonuclease RBBP8 ;Zinc finger protein 350","subunits.Gene.name.":"BRCA1;RBBP8;ZNF350","subunits.Gene.name.syn.":"RNF53;CTIP;ZBRK1","Disease.comment":"BRCA1 is involved in breast cancer.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":241,"ComplexName":"BLOC-3 (biogenesis of lysosome-related organelles complex 3)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q92902;Q9NQG7","subunits.Entrez.IDs.":"3257;89781","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0029- cosedimentation through density gradients; MI:0071- molecular sieving","GO.ID":"GO:0007032;GO:0007040;GO:0007033","GO.description":"endosome organization;lysosome organization;vacuole organization","FunCat.ID":"42.22;42.25","FunCat.description":"endosome;vacuole or lysosome","PubMed.ID":12756248,"subunits.Protein.name.":"Hermansky-Pudlak syndrome 1 protein;Hermansky-Pudlak syndrome 4 protein","subunits.Gene.name.":"HPS1;HPS4","subunits.Gene.name.syn.":"HPS;KIAA1667","Disease.comment":"HPS1-7 are involved in Hermansky-Pudlak syndrome (HPS), which  comprises at least seven different autosomal recessive disorders (referred to as HPS-1 through -7) that share the clinical manifestations of oculocutaneous albinism combined with platelet storage pool deficiency and do not present with the severe immunodeficiency and giant intracellular granules characteristic of Chediak-Higashi syndrome (PMID:15030569).","Subunits.comment":"None","Complex.comment":"The results demonstrate that the HPS1 and HPS4 proteins are components of a cytosolic complex that is involved in the biogenesis of lysosomal-related organelles by a mechanism distinct from that operated by AP-3 complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":242,"ComplexName":"BRCA1-BACH1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P38398;Q9BX63","subunits.Entrez.IDs.":"672;83990","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0005634","GO.description":"DNA repair;nucleus","FunCat.ID":"10.01.05.01;70.10","FunCat.description":"DNA repair;nucleus","PubMed.ID":11301010,"subunits.Protein.name.":"Breast cancer type 1 susceptibility protein;Fanconi anemia group J protein","subunits.Gene.name.":"BRCA1;BRIP1","subunits.Gene.name.syn.":"RNF53;BACH1 FANCJ","Disease.comment":"BRCA1 is involved in breast cancer.","Subunits.comment":"None","Complex.comment":"An intact BRCA1 C-terminal region is necessary for the interaction with BACH1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":243,"ComplexName":"RalBP1-CDC2-CCNB1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06493;P14635;Q15311","subunits.Entrez.IDs.":"983;891;10928","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0000278;GO:0006468;GO:0006470;GO:0046777;GO:0006464;GO:0050789;GO:0005634","GO.description":"mitotic cell cycle;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;cellular protein modification process;regulation of biological process;nucleus","FunCat.ID":"10.03.01.01;14.07.03;14.07;18;70.10","FunCat.description":"mitotic cell cycle;modification by phosphorylation, dephosphorylation, autophosphorylation;protein modification;REGULATION OF METABOLISM AND PROTEIN FUNCTION;nucleus","PubMed.ID":12775724,"subunits.Protein.name.":"Cyclin-dependent kinase 1 ;G2/mitotic-specific cyclin-B1;RalA-binding protein 1","subunits.Gene.name.":"CDK1;CCNB1;RALBP1","subunits.Gene.name.syn.":"CDC2 CDC28A CDKN1 P34CDC2;CCNB;RLIP1 RLIP76","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The complex was only detected in mitotic cell extracts. The authors show that RLIP76 associates with a catalytically active cyclinB\\u00b7p34cdc2(cdk1) complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":244,"ComplexName":"BRAFT complex","Organism":"Human","Synonyms":"BLM complex I","Cell.line":"None","subunits.UniProt.IDs.":"O15287;O15360;P15927;P27694;P35244;P40692;P54132;Q00597;Q13472;Q9H9A7;Q9HB96;Q9NPI8;Q9NW38","subunits.Entrez.IDs.":"2189;2175;6118;6117;6119;4292;641;2176;7156;80010;2178;2188;55120","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0051276;GO:0006281;GO:0006974;GO:0005634","GO.description":"chromosome organization;DNA repair;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"42.10.03;10.01.05.01;32.01.09;70.10","FunCat.description":"organization of chromosome structure;DNA repair;DNA damage response;nucleus","PubMed.ID":12724401,"subunits.Protein.name.":"Fanconi anemia group G protein ;Fanconi anemia group A protein ;Replication protein A 32 kDa subunit ;Replication protein A 70 kDa DNA-binding subunit;Replication protein A 14 kDa subunit ;DNA mismatch repair protein Mlh1 ;Bloom syndrome protein ;Fanconi anemia group C protein ;DNA topoisomerase 3-alpha ;RecQ-mediated genome instability protein 1 ;Fanconi anemia group E protein ;Fanconi anemia group F protein ;E3 ubiquitin-protein ligase FANCL","subunits.Gene.name.":"FANCG;FANCA;RPA2;RPA1;RPA3;MLH1;BLM;FANCC;TOP3A;RMI1;FANCE;FANCF;FANCL","subunits.Gene.name.syn.":"XRCC9;FAA FACA FANCH;REPA2 RPA32 RPA34;REPA1 RPA70;REPA3 RPA14;COCA2;RECQ2 RECQL3;FAC FACC;TOP3;C9orf76;FACE;;PHF9","Disease.comment":"BRAFT complex is involved in Fanconi Anemia (FA) and Bloom Syndrome (BS).","Subunits.comment":"The BRAFT complex contains several other proteins of unknown function, called FAAPs or BLAPs. FAAP 43 has been identified as FANCL/PHF9 in a following paper (PMID:12973351).","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":245,"ComplexName":"FA core complex (Fanconi anemia core complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15287;O15360;Q00597;Q0VG06;Q8NB91;Q9H9A7;Q9HB96;Q9NPI8;Q9NW38","subunits.Entrez.IDs.":"2189;2175;2176;80233;2187;80010;2178;2188;55120","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0006974;GO:0005634","GO.description":"protein ubiquitination;protein deubiquitination;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"14.07.05;32.01.09;70.10","FunCat.description":"modification by ubiquitination, deubiquitination;DNA damage response;nucleus","PubMed.ID":12724401,"subunits.Protein.name.":"Fanconi anemia group G protein ;Fanconi anemia group A protein ;Fanconi anemia group C protein ;Fanconi anemia core complex-associated protein 100 ;Fanconi anemia group B protein ;RecQ-mediated genome instability protein 1 ;Fanconi anemia group E protein ;Fanconi anemia group F protein ;E3 ubiquitin-protein ligase FANCL","subunits.Gene.name.":"FANCG;FANCA;FANCC;FAAP100;FANCB;RMI1;FANCE;FANCF;FANCL","subunits.Gene.name.syn.":"XRCC9;FAA FACA FANCH;FAC FACC;C17orf70;;C9orf76;FACE;;PHF9","Disease.comment":"FA complex is involved in Fanconi anemia (FA) disease.","Subunits.comment":"FANCB and FANCL have been designated as FAAP90 and FAAP43. RMI1 has been designated as FAAP75.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":246,"ComplexName":"BLM complex III","Organism":"Human","Synonyms":"BLM-CIII complex","Cell.line":"None","subunits.UniProt.IDs.":"P40692;P54132;Q13472;Q9H9A7","subunits.Entrez.IDs.":"4292;641;7156;80010","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0051276;GO:0006281;GO:0006974;GO:0005634","GO.description":"chromosome organization;DNA repair;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"42.10.03;10.01.05.01;32.01.09;70.10","FunCat.description":"organization of chromosome structure;DNA repair;DNA damage response;nucleus","PubMed.ID":12724401,"subunits.Protein.name.":"DNA mismatch repair protein Mlh1 ;Bloom syndrome protein ;DNA topoisomerase 3-alpha ;RecQ-mediated genome instability protein 1","subunits.Gene.name.":"MLH1;BLM;TOP3A;RMI1","subunits.Gene.name.syn.":"COCA2;RECQ2 RECQL3;TOP3;C9orf76","Disease.comment":"BLM complex III is involved in Bloom syndrome (BS).","Subunits.comment":"Another subunit of the complex was found in the analysis, which has not been further characterized: BLAPp100.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":247,"ComplexName":"RalBP1-CCNB1-AP2A-NUMB-EPN1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95782;P14635;P49757;Q15311;Q9Y6I3","subunits.Entrez.IDs.":"160;891;8650;10928;29924","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0000278;GO:0006897;GO:0005634","GO.description":"mitotic cell cycle;endocytosis;nucleus","FunCat.ID":"10.03.01.01;20.09.18.09.01;70.10","FunCat.description":"mitotic cell cycle;endocytosis;nucleus","PubMed.ID":12775724,"subunits.Protein.name.":"AP-2 complex subunit alpha-1;G2/mitotic-specific cyclin-B1;Protein numb homolog;RalA-binding protein 1;Epsin-1","subunits.Gene.name.":"AP2A1;CCNB1;NUMB;RALBP1;EPN1","subunits.Gene.name.syn.":"ADTAA CLAPA1;CCNB;None;RLIP1 RLIP76;None","Disease.comment":"None","Subunits.comment":"Since the authors did not specify AP2A, we used isoform AP2A1.","Complex.comment":"RLIP, an effector of the RAL GTPases, is important for the mitotic cdk1 to facilitate the phosphorylation of Epsin.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":248,"ComplexName":"BRAFT complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15287;O15360;P15927;P27694;P35244;P54132;Q00597;Q13472;Q9HB96;Q9NPI8;Q9NW38","subunits.Entrez.IDs.":"2189;2175;6118;6117;6119;641;2176;7156;2178;2188;55120","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0051276;GO:0006281;GO:0016567;GO:0016579;GO:0006974;GO:0005634","GO.description":"chromosome organization;DNA repair;protein ubiquitination;protein deubiquitination;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"42.10.03;10.01.05.01;14.07.05;32.01.09;70.10","FunCat.description":"organization of chromosome structure;DNA repair;modification by ubiquitination, deubiquitination;DNA damage response;nucleus","PubMed.ID":12973351,"subunits.Protein.name.":"Fanconi anemia group G protein ;Fanconi anemia group A protein ;Replication protein A 32 kDa subunit ;Replication protein A 70 kDa DNA-binding subunit;Replication protein A 14 kDa subunit ;Bloom syndrome protein ;Fanconi anemia group C protein ;DNA topoisomerase 3-alpha ;Fanconi anemia group E protein ;Fanconi anemia group F protein ;E3 ubiquitin-protein ligase FANCL","subunits.Gene.name.":"FANCG;FANCA;RPA2;RPA1;RPA3;BLM;FANCC;TOP3A;FANCE;FANCF;FANCL","subunits.Gene.name.syn.":"XRCC9;FAA FACA FANCH;REPA2 RPA32 RPA34;REPA1 RPA70;REPA3 RPA14;RECQ2 RECQL3;FAC FACC;TOP3;FACE;;PHF9","Disease.comment":"None","Subunits.comment":"FANCL/PHF9 (formerly called FAAP 43) is a newly identified component of the BRAFT complex.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":249,"ComplexName":"Caspase-2-TRAF2-RIP1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P29594;P39429;Q62172","subunits.Entrez.IDs.":"12366;22030;19765","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation; MI:0071- molecular sieving","GO.ID":"GO:0000165;GO:0007249","GO.description":"MAPK cascade;I-kappaB kinase/NF-kappaB signaling","FunCat.ID":"30.01.05.01.03;30.01.05.01.04","FunCat.description":"MAPKKK cascade;NIK-I-kappaB/NF-kappaB cascade","PubMed.ID":15590671,"subunits.Protein.name.":"Caspase-2 ;TNF receptor-associated factor 2;RalA-binding protein 1","subunits.Gene.name.":"Casp2;Traf2;Ralbp1","subunits.Gene.name.syn.":"Ich1 Nedd-2 Nedd2;None;Rip1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex activates NF-kappaB and p38 MAPK through the caspase recruitment domain of caspase-2 independently of its proteolytic activity.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":251,"ComplexName":"BCDX2 complex","Organism":"Human","Synonyms":"RAD51B-RAD51C-RAD51D-XRCC2 complex","Cell.line":"None","subunits.UniProt.IDs.":"O15315;O43502;O43543;O75771","subunits.Entrez.IDs.":"5890;5889;7516;5892","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0006310;GO:0003677;GO:0005524;GO:0006974;GO:0005634","GO.description":"DNA repair;DNA recombination;DNA binding;ATP binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;10.01.05.03;16.03.01;16.19.03;32.01.09;70.10","FunCat.description":"DNA repair;DNA recombination;DNA binding;ATP binding;DNA damage response;nucleus","PubMed.ID":11751635,"subunits.Protein.name.":"DNA repair protein RAD51 homolog 2 ;DNA repair protein RAD51 homolog 3 ;DNA repair protein XRCC2 ;DNA repair protein RAD51 homolog 4","subunits.Gene.name.":"RAD51B;RAD51C;XRCC2;RAD51D","subunits.Gene.name.syn.":"RAD51L1 REC2;RAD51L2;;RAD51L3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"BCDX2 binds specifically to nicks in duplex DNA (PMID:11751635).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":252,"ComplexName":"RAD51C-XRCC3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43502;O43542","subunits.Entrez.IDs.":"5889;7517","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0004- affinity chromatography technologies","GO.ID":"GO:0006794;GO:0006796;GO:0006281;GO:0006310;GO:0006310;GO:0003677;GO:0005524;GO:0006974;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;DNA repair;DNA recombination;DNA recombination;DNA binding;ATP binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"01.04;10.01.05.01;10.01.05.03;16.03.01;16.19.03;32.01.09;70.10","FunCat.description":"phosphate metabolism;DNA repair;DNA recombination;DNA binding;ATP binding;DNA damage response;nucleus","PubMed.ID":11751635,"subunits.Protein.name.":"DNA repair protein RAD51 homolog 3 ;DNA repair protein XRCC3","subunits.Gene.name.":"RAD51C;XRCC3","subunits.Gene.name.syn.":"RAD51L2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":253,"ComplexName":"RAD51C-XRCC3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43502;O43542","subunits.Entrez.IDs.":"5889;7517","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006281;GO:0006310;GO:0003677;GO:0005524;GO:0006974;GO:0005634","GO.description":"DNA repair;DNA recombination;DNA binding;ATP binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;10.01.05.03;16.03.01;16.19.03;32.01.09;70.10","FunCat.description":"DNA repair;DNA recombination;DNA binding;ATP binding;DNA damage response;nucleus","PubMed.ID":15037616,"subunits.Protein.name.":"DNA repair protein RAD51 homolog 3 ;DNA repair protein XRCC3","subunits.Gene.name.":"RAD51C;XRCC3","subunits.Gene.name.syn.":"RAD51L2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors postulate that XRCC3 regulates the dissociation and formation of Rad51C-XRCC3 complex through ATP binding and hydrolysis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":254,"ComplexName":"TBPIP/HOP2-MND1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q9BWT6;Q9P2W1","subunits.Entrez.IDs.":"84057;29893","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0007131;GO:0007126;GO:0000280;GO:0007059;GO:0003677;GO:0051098;GO:0005515;GO:0030234;GO:0050790;GO:0005634","GO.description":"reciprocal meiotic recombination;meiotic nuclear division;nuclear division;chromosome segregation;DNA binding;regulation of binding;protein binding;enzyme regulator activity;regulation of catalytic activity;nucleus","FunCat.ID":"10.01.05.03.01;10.03.02;10.03.04.07;10.03.04.05;16.03.01;18.01.07;16.01;18.02.01;70.10","FunCat.description":"meiotic recombination;meiosis;nuclear division;chromosome segregation/division;DNA binding;regulation by binding / dissociation;protein binding;enzymatic activity regulation / enzyme regulator;nucleus","PubMed.ID":16407260,"subunits.Protein.name.":"Meiotic nuclear division protein 1 homolog;Homologous-pairing protein 2 homolog","subunits.Gene.name.":"MND1;PSMC3IP","subunits.Gene.name.syn.":"GAJ;HOP2 TBPIP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The complex ensures proper pairing between homologous chromosomes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":255,"ComplexName":"TBPIP/HOP2-Mnd1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O35047;Q8K396","subunits.Entrez.IDs.":"19183;76915","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0007131;GO:0007126;GO:0000280;GO:0007059;GO:0005515;GO:0003677;GO:0051098;GO:0030234;GO:0050790;GO:0005634","GO.description":"reciprocal meiotic recombination;meiotic nuclear division;nuclear division;chromosome segregation;protein binding;DNA binding;regulation of binding;enzyme regulator activity;regulation of catalytic activity;nucleus","FunCat.ID":"10.01.05.03.01;10.03.02;10.03.04.07;10.03.04.05;16.01;16.03.01;18.01.07;18.02.01;70.10","FunCat.description":"meiotic recombination;meiosis;nuclear division;chromosome segregation/division;protein binding;DNA binding;regulation by binding / dissociation;enzymatic activity regulation / enzyme regulator;nucleus","PubMed.ID":15834424,"subunits.Protein.name.":"Homologous-pairing protein 2 homolog ;Meiotic nuclear division protein 1 homolog","subunits.Gene.name.":"Psmc3ip;Mnd1","subunits.Gene.name.syn.":"Hop2 Tbpip;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The complex ensures proper pairing between homologous chromosomes.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":256,"ComplexName":"RAD51B-RAD51C complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15315;O43502","subunits.Entrez.IDs.":"5890;5889","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0006310;GO:0003677;GO:0005524;GO:0005634","GO.description":"DNA repair;DNA recombination;DNA binding;ATP binding;nucleus","FunCat.ID":"10.01.05.01;10.01.05.03;16.03.01;16.19.03;70.10","FunCat.description":"DNA repair;DNA recombination;DNA binding;ATP binding;nucleus","PubMed.ID":11751636,"subunits.Protein.name.":"DNA repair protein RAD51 homolog 2 ;DNA repair protein RAD51 homolog 3","subunits.Gene.name.":"RAD51B;RAD51C","subunits.Gene.name.syn.":"RAD51L1 REC2;RAD51L2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":257,"ComplexName":"Hop2-Mnd1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O35047;Q8K396","subunits.Entrez.IDs.":"19183;76915","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0004- affinity chromatography technologies","GO.ID":"GO:0007131;GO:0007127;GO:0005515;GO:0003677;GO:0051098;GO:0030234;GO:0050790;GO:0005634","GO.description":"reciprocal meiotic recombination;meiosis I;protein binding;DNA binding;regulation of binding;enzyme regulator activity;regulation of catalytic activity;nucleus","FunCat.ID":"10.01.05.03.01;10.03.02.01;16.01;16.03.01;18.01.07;18.02.01;70.10","FunCat.description":"meiotic recombination;meiosis I;protein binding;DNA binding;regulation by binding / dissociation;enzymatic activity regulation / enzyme regulator;nucleus","PubMed.ID":16675459,"subunits.Protein.name.":"Homologous-pairing protein 2 homolog ;Meiotic nuclear division protein 1 homolog","subunits.Gene.name.":"Psmc3ip;Mnd1","subunits.Gene.name.syn.":"Hop2 Tbpip;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Only the heterodimeric complex, but not the individual proteins, can stimulate strand invasion by Dmc1.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":258,"ComplexName":"BCDX2 complex","Organism":"Human","Synonyms":"RAD51B-RAD51C-RAD51D-XRCC2 complex","Cell.line":"None","subunits.UniProt.IDs.":"O15315;O43502;O43543;O75771","subunits.Entrez.IDs.":"5890;5889;7516;5892","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006281;GO:0006310;GO:0003677;GO:0005524;GO:0006974;GO:0005634","GO.description":"DNA repair;DNA recombination;DNA binding;ATP binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;10.01.05.03;16.03.01;16.19.03;32.01.09;70.10","FunCat.description":"DNA repair;DNA recombination;DNA binding;ATP binding;DNA damage response;nucleus","PubMed.ID":11842113,"subunits.Protein.name.":"DNA repair protein RAD51 homolog 2 ;DNA repair protein RAD51 homolog 3 ;DNA repair protein XRCC2 ;DNA repair protein RAD51 homolog 4","subunits.Gene.name.":"RAD51B;RAD51C;XRCC2;RAD51D","subunits.Gene.name.syn.":"RAD51L1 REC2;RAD51L2;;RAD51L3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":259,"ComplexName":"RAD51C-XRCC3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43502;O43542","subunits.Entrez.IDs.":"5889;7517","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006281;GO:0006310;GO:0003677;GO:0005524;GO:0006974;GO:0005634","GO.description":"DNA repair;DNA recombination;DNA binding;ATP binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;10.01.05.03;16.03.01;16.19.03;32.01.09;70.10","FunCat.description":"DNA repair;DNA recombination;DNA binding;ATP binding;DNA damage response;nucleus","PubMed.ID":11842113,"subunits.Protein.name.":"DNA repair protein RAD51 homolog 3 ;DNA repair protein XRCC3","subunits.Gene.name.":"RAD51C;XRCC3","subunits.Gene.name.syn.":"RAD51L2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":260,"ComplexName":"RAD51B-RAD51C complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15315;O43502","subunits.Entrez.IDs.":"5890;5889","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0006310;GO:0003677;GO:0005524;GO:0006974;GO:0005634","GO.description":"DNA repair;DNA recombination;DNA binding;ATP binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;10.01.05.03;16.03.01;16.19.03;32.01.09;70.10","FunCat.description":"DNA repair;DNA recombination;DNA binding;ATP binding;DNA damage response;nucleus","PubMed.ID":11744692,"subunits.Protein.name.":"DNA repair protein RAD51 homolog 2 ;DNA repair protein RAD51 homolog 3","subunits.Gene.name.":"RAD51B;RAD51C","subunits.Gene.name.syn.":"RAD51L1 REC2;RAD51L2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":261,"ComplexName":"RAD51B-RAD51C-RAD51D-XRCC2-XRCC3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15315;O43502;O43542;O43543;O75771","subunits.Entrez.IDs.":"5890;5889;7517;7516;5892","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0006310;GO:0003677;GO:0005524;GO:0006974;GO:0005634","GO.description":"DNA repair;DNA recombination;DNA binding;ATP binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;10.01.05.03;16.03.01;16.19.03;32.01.09;70.10","FunCat.description":"DNA repair;DNA recombination;DNA binding;ATP binding;DNA damage response;nucleus","PubMed.ID":11744692,"subunits.Protein.name.":"DNA repair protein RAD51 homolog 2 ;DNA repair protein RAD51 homolog 3 ;DNA repair protein XRCC3 ;DNA repair protein XRCC2 ;DNA repair protein RAD51 homolog 4","subunits.Gene.name.":"RAD51B;RAD51C;XRCC3;XRCC2;RAD51D","subunits.Gene.name.syn.":"RAD51L1 REC2;RAD51L2;;;RAD51L3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":262,"ComplexName":"RAD51L3-XRCC2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43543;O75771","subunits.Entrez.IDs.":"7516;5892","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006281;GO:0006310;GO:0003677;GO:0005524;GO:0006974;GO:0005634","GO.description":"DNA repair;DNA recombination;DNA binding;ATP binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;10.01.05.03;16.03.01;16.19.03;32.01.09;70.10","FunCat.description":"DNA repair;DNA recombination;DNA binding;ATP binding;DNA damage response;nucleus","PubMed.ID":10871607,"subunits.Protein.name.":"DNA repair protein XRCC2 ;DNA repair protein RAD51 homolog 4","subunits.Gene.name.":"XRCC2;RAD51D","subunits.Gene.name.syn.":";RAD51L3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":263,"ComplexName":"R/M complex (RAD50-MRE11 complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P49959;Q92878","subunits.Entrez.IDs.":"4361;10111","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0428- imaging techniques","GO.ID":"GO:0006308;GO:0006281;GO:0003677;GO:0006974;GO:0051276;GO:0005634","GO.description":"DNA catabolic process;DNA repair;DNA binding;cellular response to DNA damage stimulus;chromosome organization;nucleus","FunCat.ID":"01.03.16.03;10.01.05.01;16.03.01;32.01.09;42.10.03;70.10","FunCat.description":"DNA degradation;DNA repair;DNA binding;DNA damage response;organization of chromosome structure;nucleus","PubMed.ID":11741547,"subunits.Protein.name.":"Double-strand break repair protein MRE11A ;DNA repair protein RAD50","subunits.Gene.name.":"MRE11A;RAD50","subunits.Gene.name.syn.":"HNGS1 MRE11;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"R/M consists of two highly flexible intramolecular coiled coils emanating from a central globular DNA binding domain.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":264,"ComplexName":"R/M complex (RAD50-MRE11 complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P49959;Q92878","subunits.Entrez.IDs.":"4361;10111","Protein.complex.purification.method":"MI:0428- imaging techniques","GO.ID":"GO:0006308;GO:0006281;GO:0003677;GO:0006974;GO:0051276;GO:0005634","GO.description":"DNA catabolic process;DNA repair;DNA binding;cellular response to DNA damage stimulus;chromosome organization;nucleus","FunCat.ID":"01.03.16.03;10.01.05.01;16.03.01;32.01.09;42.10.03;70.10","FunCat.description":"DNA degradation;DNA repair;DNA binding;DNA damage response;organization of chromosome structure;nucleus","PubMed.ID":15165861,"subunits.Protein.name.":"Double-strand break repair protein MRE11A ;DNA repair protein RAD50","subunits.Gene.name.":"MRE11A;RAD50","subunits.Gene.name.syn.":"HNGS1 MRE11;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Human Rad50-Mre11 complexes are predominantly heterotetramers.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":265,"ComplexName":"ATR-ATRIP complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q13535;Q8WXE1","subunits.Entrez.IDs.":"545;84126","Protein.complex.purification.method":"MI:0091- chromatography technologies; MI:0071- molecular sieving","GO.ID":"GO:0000075;GO:0003677;GO:0006974;GO:0005634","GO.description":"cell cycle checkpoint;DNA binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.03.01.03;16.03.01;32.01.09;70.10","FunCat.description":"cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA binding;DNA damage response;nucleus","PubMed.ID":14724280,"subunits.Protein.name.":"Serine/threonine-protein kinase ATR ;ATR-interacting protein","subunits.Gene.name.":"ATR;ATRIP","subunits.Gene.name.syn.":"FRP1;AGS1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"ATR and ATRIP associate with chromatin in vivo, and they exist as a large molecular weight complex that can bind single-stranded (ss)DNA cellulose in vitro. Neither ATR nor ATRIP are able to bind DNA individually, nor do they bind DNA in a cooperative manner.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":266,"ComplexName":"RAD17-RFC complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75943;P35249;P35250;P40937;P40938","subunits.Entrez.IDs.":"5884;5984;5982;5985;5983","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006794;GO:0006796;GO:0000075;GO:0003677;GO:0005524;GO:0006974;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;cell cycle checkpoint;DNA binding;ATP binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"01.04;10.03.01.03;16.03.01;16.19.03;32.01.09;70.10","FunCat.description":"phosphate metabolism;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA binding;ATP binding;DNA damage response;nucleus","PubMed.ID":11572977,"subunits.Protein.name.":"Cell cycle checkpoint protein RAD17;Replication factor C subunit 4;Replication factor C subunit 2;Replication factor C subunit 5;Replication factor C subunit 3","subunits.Gene.name.":"RAD17;RFC4;RFC2;RFC5;RFC3","subunits.Gene.name.syn.":"R24L;None;None;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"RFCp38 is necessary for the association of RAD17 with the core complex RFCp36-p37-p40 to form the RAD17-RFC complex. The ATPase activity of RAD17-RFC complex is stimulated by DNA.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":267,"ComplexName":"9-1-1 complex","Organism":"Human","Synonyms":"Checkpoint 9-1-1 complex","Cell.line":"None","subunits.UniProt.IDs.":"O60671;O60921;Q99638","subunits.Entrez.IDs.":"5810;3364;5883","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0006281;GO:0000075;GO:0006974;GO:0005634","GO.description":"DNA repair;cell cycle checkpoint;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;10.03.01.03;32.01.09;70.10","FunCat.description":"DNA repair;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA damage response;nucleus","PubMed.ID":11572977,"subunits.Protein.name.":"Cell cycle checkpoint protein RAD1;Checkpoint protein HUS1;Cell cycle checkpoint control protein RAD9A","subunits.Gene.name.":"RAD1;HUS1;RAD9A","subunits.Gene.name.syn.":"REC1;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":268,"ComplexName":"9-1-1-RAD17-RFC complex","Organism":"Human","Synonyms":"Checkpoint Rad complex","Cell.line":"None","subunits.UniProt.IDs.":"O60671;O60921;O75943;P35249;P35250;P40937;P40938;Q99638","subunits.Entrez.IDs.":"5810;3364;5884;5984;5982;5985;5983;5883","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies;MI:0071-molecular sieving","GO.ID":"GO:0000075;GO:0006974;GO:0005634","GO.description":"cell cycle checkpoint;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.03.01.03;32.01.09;70.10","FunCat.description":"cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA damage response;nucleus","PubMed.ID":11572977,"subunits.Protein.name.":"Cell cycle checkpoint protein RAD1;Checkpoint protein HUS1;Cell cycle checkpoint protein RAD17;Replication factor C subunit 4;Replication factor C subunit 2;Replication factor C subunit 5;Replication factor C subunit 3;Cell cycle checkpoint control protein RAD9A","subunits.Gene.name.":"RAD1;HUS1;RAD17;RFC4;RFC2;RFC5;RFC3;RAD9A","subunits.Gene.name.syn.":"REC1;None;R24L;None;None;None;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Checkpoint Rad complex has been detected in an in vitro system.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":270,"ComplexName":"RAD17-RFC complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75943;P35249;P35250;P40937;P40938","subunits.Entrez.IDs.":"5884;5984;5982;5985;5983","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0040- electron microscopy","GO.ID":"GO:0006794;GO:0006796;GO:0000075;GO:0003677;GO:0005524;GO:0006974;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;cell cycle checkpoint;DNA binding;ATP binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"01.04;10.03.01.03;16.03.01;16.19.03;32.01.09;70.10","FunCat.description":"phosphate metabolism;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA binding;ATP binding;DNA damage response;nucleus","PubMed.ID":11907025,"subunits.Protein.name.":"Cell cycle checkpoint protein RAD17;Replication factor C subunit 4;Replication factor C subunit 2;Replication factor C subunit 5;Replication factor C subunit 3","subunits.Gene.name.":"RAD17;RFC4;RFC2;RFC5;RFC3","subunits.Gene.name.syn.":"R24L;None;None;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"RAD17 makes a heteropentameric complex with the four RFC subunits with a deep groove or cleft and is similar to the RFC clamp loader.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":271,"ComplexName":"9-1-1 complex","Organism":"Human","Synonyms":"Checkpoint 9-1-1 complex","Cell.line":"None","subunits.UniProt.IDs.":"O60671;O60921;Q99638","subunits.Entrez.IDs.":"5810;3364;5883","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies;MI:0040-electron microscopy","GO.ID":"GO:0006281;GO:0000075;GO:0006974;GO:0005634","GO.description":"DNA repair;cell cycle checkpoint;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;10.03.01.03;32.01.09;70.10","FunCat.description":"DNA repair;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA damage response;nucleus","PubMed.ID":11907025,"subunits.Protein.name.":"Cell cycle checkpoint protein RAD1;Checkpoint protein HUS1;Cell cycle checkpoint control protein RAD9A","subunits.Gene.name.":"RAD1;HUS1;RAD9A","subunits.Gene.name.syn.":"REC1;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The checkpoint 9-1-1 complex makes a trimeric ring structure reminiscent of the PCNA ring.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":272,"ComplexName":"Dysbindin-pallidin-muted-beta-dystrobrevin complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O70585;Q8R015;Q91WZ8;Q9R0C0","subunits.Entrez.IDs.":"13528;17828;94245;18457","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007040;GO:0007033","GO.description":"lysosome organization;vacuole organization","FunCat.ID":"42.25","FunCat.description":"vacuole or lysosome","PubMed.ID":12923531,"subunits.Protein.name.":"Dystrobrevin beta;Biogenesis of lysosome-related organelles complex 1 subunit 5;Dysbindin ;Biogenesis of lysosome-related organelles complex 1 subunit 6","subunits.Gene.name.":"Dtnb;Bloc1s5;Dtnbp1;Bloc1s6","subunits.Gene.name.syn.":"None;Mu Muted;Bloc1s8 Sdy;P2 Pa Pldn","Disease.comment":"Dtnbp1 is involved in Hermansky-Pudlak syndrome type 7 (HPS-7).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":274,"ComplexName":"9-1-1-RAD17-RFC supercomplex","Organism":"Human","Synonyms":"RAD17-RFC-9-1-1 checkpoint supercomplex","Cell.line":"None","subunits.UniProt.IDs.":"O60671;O60921;O75943;P35249;P35250;P40937;P40938;Q99638","subunits.Entrez.IDs.":"5810;3364;5884;5984;5982;5985;5983;5883","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies;MI:0029-cosedimentation through density gradients;MI:0040-electron microscopy","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":12578958,"subunits.Protein.name.":"Cell cycle checkpoint protein RAD1;Checkpoint protein HUS1;Cell cycle checkpoint protein RAD17;Replication factor C subunit 4;Replication factor C subunit 2;Replication factor C subunit 5;Replication factor C subunit 3;Cell cycle checkpoint control protein RAD9A","subunits.Gene.name.":"RAD1;HUS1;RAD17;RFC4;RFC2;RFC5;RFC3;RAD9A","subunits.Gene.name.syn.":"REC1;None;R24L;None;None;None;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Rad17-RFC complex binds to nicked circular, gapped and primed DNA and recruits the 9-1-1 complex in an ATP-dependent manner. The interaction is mediated mainly by binding of Rad9 to Rad17.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":275,"ComplexName":"9-1-1 complex","Organism":"Human","Synonyms":"Checkpoint 9-1-1 complex","Cell.line":"None","subunits.UniProt.IDs.":"O60671;O60921;Q99638","subunits.Entrez.IDs.":"5810;3364;5883","Protein.complex.purification.method":"MI:0071-molecular sieving","GO.ID":"GO:0006281;GO:0000075;GO:0006974;GO:0005634","GO.description":"DNA repair;cell cycle checkpoint;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;10.03.01.03;32.01.09;70.10","FunCat.description":"DNA repair;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA damage response;nucleus","PubMed.ID":11340080,"subunits.Protein.name.":"Cell cycle checkpoint protein RAD1;Checkpoint protein HUS1;Cell cycle checkpoint control protein RAD9A","subunits.Gene.name.":"RAD1;HUS1;RAD9A","subunits.Gene.name.syn.":"REC1;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":276,"ComplexName":"9-1-1 complex","Organism":"Human","Synonyms":"Checkpoint 9-1-1 complex","Cell.line":"None","subunits.UniProt.IDs.":"O60671;O60921;Q99638","subunits.Entrez.IDs.":"5810;3364;5883","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0000075;GO:0006974;GO:0005634","GO.description":"DNA repair;cell cycle checkpoint;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;10.03.01.03;32.01.09;70.10","FunCat.description":"DNA repair;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA damage response;nucleus","PubMed.ID":9872989,"subunits.Protein.name.":"Cell cycle checkpoint protein RAD1;Checkpoint protein HUS1;Cell cycle checkpoint control protein RAD9A","subunits.Gene.name.":"RAD1;HUS1;RAD9A","subunits.Gene.name.syn.":"REC1;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":277,"ComplexName":"RFC complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P35249;P35250;P35251;P40937;P40938","subunits.Entrez.IDs.":"5984;5982;5981;5985;5983","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006794;GO:0006796;GO:0006260;GO:0003677;GO:0005524;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;DNA replication;DNA binding;ATP binding;nucleus","FunCat.ID":"01.04;10.01.03;16.03.01;16.19.03;70.10","FunCat.description":"phosphate metabolism;DNA synthesis and replication;DNA binding;ATP binding;nucleus","PubMed.ID":8692848,"subunits.Protein.name.":"Replication factor C subunit 4;Replication factor C subunit 2;Replication factor C subunit 1;Replication factor C subunit 5;Replication factor C subunit 3","subunits.Gene.name.":"RFC4;RFC2;RFC1;RFC5;RFC3","subunits.Gene.name.syn.":"None;None;RFC140;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The subunits of the RFC complex have been reconstituted in an in vitro experiment. The Rfc complex works as a clamp loader.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":278,"ComplexName":"RFC core complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P35249;P35250;P40937","subunits.Entrez.IDs.":"5984;5982;5985","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006794;GO:0006796;GO:0006260;GO:0003677;GO:0005524;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;DNA replication;DNA binding;ATP binding;nucleus","FunCat.ID":"01.04;10.01.03;16.03.01;16.19.03;70.10","FunCat.description":"phosphate metabolism;DNA synthesis and replication;DNA binding;ATP binding;nucleus","PubMed.ID":8692848,"subunits.Protein.name.":"Replication factor C subunit 4;Replication factor C subunit 2;Replication factor C subunit 5","subunits.Gene.name.":"RFC4;RFC2;RFC5","subunits.Gene.name.syn.":"None;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The subunits of the RFC complex have been reconstituted in an in vitro experiment.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":279,"ComplexName":"RFC complex (activator A 1 complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P35249;P35250;P35251;P40937;P40938","subunits.Entrez.IDs.":"5984;5982;5981;5985;5983","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006794;GO:0006796;GO:0006260;GO:0003677;GO:0005524;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;DNA replication;DNA binding;ATP binding;nucleus","FunCat.ID":"01.04;10.01.03;16.03.01;16.19.03;70.10","FunCat.description":"phosphate metabolism;DNA synthesis and replication;DNA binding;ATP binding;nucleus","PubMed.ID":1670772,"subunits.Protein.name.":"Replication factor C subunit 4;Replication factor C subunit 2;Replication factor C subunit 1;Replication factor C subunit 5;Replication factor C subunit 3","subunits.Gene.name.":"RFC4;RFC2;RFC1;RFC5;RFC3","subunits.Gene.name.syn.":"None;None;RFC140;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Activator 1 (A1) is a multiprotein complex which is essential for proliferating cell nuclear antigen (PCNA)-dependent DNA polymerase delta (pol delta) activity and efficient in vitro DNA synthesis in the SV40 dipolymerase replication system (PMID:1670772).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":280,"ComplexName":"HMGB1-HMGB2-HSC70-ERP60-GAPDH complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04406;P09429;P11142;P26583;P30101","subunits.Entrez.IDs.":"2597;3146;3312;3148;2923","Protein.complex.purification.method":"MI:0413- electrophoretic mobility shift assay","GO.ID":"GO:0006281;GO:0003677;GO:0006974;GO:0005634","GO.description":"DNA repair;DNA binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;16.03.01;32.01.09;70.10","FunCat.description":"DNA repair;DNA binding;DNA damage response;nucleus","PubMed.ID":12517784,"subunits.Protein.name.":"Glyceraldehyde-3-phosphate dehydrogenase;High mobility group protein B1 ;Heat shock cognate 71 kDa protein;High mobility group protein B2 ;Protein disulfide-isomerase A3","subunits.Gene.name.":"GAPDH;HMGB1;HSPA8;HMGB2;PDIA3","subunits.Gene.name.syn.":"GAPD;HMG1;HSC70, HSP73, HSPA10;HMG2;ERP57 ERP60 GRP58","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The protein/DNA complex was isolated from human leukemia cells deficient in components of the mismatch repair system (Nalm6). This complex detects changes in DNA structure caused by incorporation of nonnatural nucleosides and is a determinant of cell sensitivity to such DNA modifying chemotherapy. The authors show that murine fibroblasts deficient in one component of the complex, Hmgb1, are 10-fold more resistant to thiopurine treatment than their wild-type counterparts.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":281,"ComplexName":"NELF complex (Negative elongation factor complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P18615;Q8IXH7;Q8WX92;Q9H3P2","subunits.Entrez.IDs.":"7936;51497;25920;7469","Protein.complex.purification.method":"MI:0226- ion exchange chromatography; MI:0029- cosedimentation through density gradients; MI:0071- molecular sieving","GO.ID":"GO:0006354;GO:0045892;GO:0003723;GO:0051098;GO:0005515;GO:0051090;GO:0005634","GO.description":"DNA-templated transcription, elongation;negative regulation of transcription, DNA-templated;RNA binding;regulation of binding;protein binding;regulation of sequence-specific DNA binding transcription factor activity;nucleus","FunCat.ID":"11.02.03.01.04;11.02.03.04.03;16.03.03;18.01.07;16.01;18.02.09;70.10","FunCat.description":"transcription elongation;transcription repression;RNA binding;regulation by binding / dissociation;protein binding;regulator of transcription factor;nucleus","PubMed.ID":10199401,"subunits.Protein.name.":"Negative elongation factor E ;Negative elongation factor C/D ;Negative elongation factor B ;Negative elongation factor A","subunits.Gene.name.":"NELFE;NELFCD;NELFB;NELFA","subunits.Gene.name.syn.":"RD RDBP;NELFD TH1 TH1L;COBRA1 KIAA1182;WHSC2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"NELF cooperates with DSIF and strongly represses POLII elongation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":282,"ComplexName":"SNF2h-cohesin-NuRD complex","Organism":"Human","Synonyms":"ISWI (SNF2h)-containing chromatin remodeling complex","Cell.line":"None","subunits.UniProt.IDs.":"O60216;O60264;O94776;O95983;Q09028;Q12873;Q13330;Q13547;Q14683;Q16576;Q8N3U4;Q8WVM7;Q92769;Q9NRL2;Q9UBB5;Q9UQE7","subunits.Entrez.IDs.":"5885;8467;9219;53615;5928;1107;9112;3065;8243;5931;10735;10274;3066;11177;8932;9126","Protein.complex.purification.method":"MI:0226- ion exchange chromatography; MI:0071- molecular sieving","GO.ID":"GO:0006265;GO:0003677;GO:0051276;GO:0005694","GO.description":"DNA topological change;DNA binding;chromosome organization;chromosome","FunCat.ID":"10.01.09.05;16.03.01;42.10.03;70.10.03","FunCat.description":"DNA conformation modification (e.g. chromatin);DNA binding;organization of chromosome structure;chromosome","PubMed.ID":12198550,"subunits.Protein.name.":"Double-strand-break repair protein rad21 homolog ;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5;Metastasis-associated protein MTA2;Methyl-CpG-binding domain protein 3;Histone-binding protein RBBP4;Chromodomain-helicase-DNA-binding protein 3;Metastasis-associated protein MTA1;Histone deacetylase 1;Structural maintenance of chromosomes protein 1A ;Histone-binding protein RBBP7;Cohesin subunit SA-2 ;Cohesin subunit SA-1 ;Histone deacetylase 2;Bromodomain adjacent to zinc finger domain protein 1A ;Methyl-CpG-binding domain protein 2;Structural maintenance of chromosomes protein 3","subunits.Gene.name.":"RAD21;SMARCA5;MTA2;MBD3;RBBP4;CHD3;MTA1;HDAC1;SMC1A;RBBP7;STAG2;STAG1;HDAC2;BAZ1A;MBD2;SMC3","subunits.Gene.name.syn.":"HR21 KIAA0078 NXP1;SNF2H WCRF135;MTA1L1 PID;None;RBAP48;None;None;RPD3L1;DXS423E KIAA0178 SB1.8 SMC1 SMC1L1;RBAP46;SA2;SA1;None;ACF1 WCRF180;None;BAM BMH CSPG6 SMC3L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The association of the complex with chromatin can be regulated by the state of DNA methylation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":283,"ComplexName":"Sin3 complex","Organism":"Human","Synonyms":"Histone deacetylase complex","Cell.line":"None","subunits.UniProt.IDs.":"O00422;O75446;Q09028;Q13547;Q16576;Q92769;Q96ST3","subunits.Entrez.IDs.":"10284;8819;5928;3065;5931;3066;25942","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0005515;GO:0051276","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;protein binding;chromosome organization","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;16.01;42.10.03","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;protein binding;organization of chromosome structure","PubMed.ID":9651585,"subunits.Protein.name.":"Histone deacetylase complex subunit SAP18;Histone deacetylase complex subunit SAP30;Histone-binding protein RBBP4;Histone deacetylase 1;Histone-binding protein RBBP7;Histone deacetylase 2;Paired amphipathic helix protein Sin3a","subunits.Gene.name.":"SAP18;SAP30;RBBP4;HDAC1;RBBP7;HDAC2;SIN3A","subunits.Gene.name.syn.":"None;None;RBAP48;RPD3L1;RBAP46;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":284,"ComplexName":"CRSP complex","Organism":"Human","Synonyms":"Cofactor required for Sp1","Cell.line":"None","subunits.UniProt.IDs.":"O43513;O60244;O75448;O75586;O95402;Q13503;Q15648;Q71SY5;Q96RN5;Q9NVC6;Q9ULK4","subunits.Entrez.IDs.":"9443;9282;9862;10001;9441;9412;5469;81857;51586;9440;9439","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0004- affinity chromatography technologies","GO.ID":"GO:0045893;GO:0005515;GO:0005694","GO.description":"positive regulation of transcription, DNA-templated;protein binding;chromosome","FunCat.ID":"11.02.03.04.01;16.01;70.10.03","FunCat.description":"transcription activation;protein binding;chromosome","PubMed.ID":11834832,"subunits.Protein.name.":"Mediator of RNA polymerase II transcription subunit 7 ;Mediator of RNA polymerase II transcription subunit 14;Mediator of RNA polymerase II transcription subunit 24;Mediator of RNA polymerase II transcription subunit 6 ;Mediator of RNA polymerase II transcription subunit 26 ;Mediator of RNA polymerase II transcription subunit 21;Mediator of RNA polymerase II transcription subunit 1;Mediator of RNA polymerase II transcription subunit 25 ;Mediator of RNA polymerase II transcription subunit 15;Mediator of RNA polymerase II transcription subunit 17;Mediator of RNA polymerase II transcription subunit 23","subunits.Gene.name.":"MED7;MED14;MED24;MED6;MED26;MED21;MED1;MED25;MED15;MED17;MED23","subunits.Gene.name.syn.":"ARC34 CRSP9;ARC150 CRSP2 CXorf4 DRIP150 EXLM1 RGR1 TRAP170;ARC100 CRSP4 DRIP100 KIAA0130 THRAP4 TRAP100;ARC33;ARC70 CRSP7;SRB7 SURB7;ARC205 CRSP1 CRSP200 DRIP205 DRIP230 PBP PPARBP PPARGBP RB18A TRAP220 TRIP2;ACID1 ARC92 PTOV2;ARC105 CTG7A PCQAP TIG1 TNRC7;ARC77 CRSP6 DRIP77 DRIP80 TRAP80;ARC130 CRSP3 DRIP130 KIAA1216 SUR2","Disease.comment":"None","Subunits.comment":"Information about four small protein subunits of the protein complex was not available in the article.","Complex.comment":"The activator-recruited cofactor ARC consists of the two distinct multisubunit complexes ARC-L and CRSP. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":285,"ComplexName":"PCNA-MLH1-PMS1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12004;P40692;P54277","subunits.Entrez.IDs.":"5111;4292;5378","Protein.complex.purification.method":"MI:0107- surface plasmon resonance","GO.ID":"GO:0006260;GO:0006281;GO:0005634","GO.description":"DNA replication;DNA repair;nucleus","FunCat.ID":"10.01.03;10.01.05.01;70.10","FunCat.description":"DNA synthesis and replication;DNA repair;nucleus","PubMed.ID":16303135,"subunits.Protein.name.":"Proliferating cell nuclear antigen;DNA mismatch repair protein Mlh1 ;PMS1 protein homolog 1","subunits.Gene.name.":"PCNA;MLH1;PMS1","subunits.Gene.name.syn.":"None;COCA2;PMSL1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors show that PCNA interacts with MSH2-MSH6 with a higher affinity than with MLH1-PMS1. PCNA acts as a scaffold for consecutive protein-protein interactions.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":286,"ComplexName":"PCNA-MSH2-MSH6 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12004;P43246;P52701","subunits.Entrez.IDs.":"5111;4436;2956","Protein.complex.purification.method":"MI:0107- surface plasmon resonance","GO.ID":"GO:0006260;GO:0006281;GO:0005634","GO.description":"DNA replication;DNA repair;nucleus","FunCat.ID":"10.01.03;10.01.05.01;70.10","FunCat.description":"DNA synthesis and replication;DNA repair;nucleus","PubMed.ID":16303135,"subunits.Protein.name.":"Proliferating cell nuclear antigen;DNA mismatch repair protein Msh2 ;DNA mismatch repair protein Msh6","subunits.Gene.name.":"PCNA;MSH2;MSH6","subunits.Gene.name.syn.":"None;;GTBP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors show that PCNA interacts with MSH2-MSH6 with a higher affinity than with MLH1-PMS1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":287,"ComplexName":"ARC-L complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43513;O60244;O75448;O75586;P24863;P49336;Q13503;Q15648;Q71SY5;Q93074;Q96RN5;Q9NVC6;Q9UHV7;Q9ULK4","subunits.Entrez.IDs.":"9443;9282;9862;10001;892;1024;9412;5469;81857;9968;51586;9440;9969;9439","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0004- affinity chromatography technologies","GO.ID":"GO:0005515;GO:0051098;GO:0005515;GO:0051090;GO:0005694","GO.description":"protein binding;regulation of binding;protein binding;regulation of sequence-specific DNA binding transcription factor activity;chromosome","FunCat.ID":"16.01;18.01.07;18.02.09;70.10.03","FunCat.description":"protein binding;regulation by binding / dissociation;regulator of transcription factor;chromosome","PubMed.ID":11834832,"subunits.Protein.name.":"Mediator of RNA polymerase II transcription subunit 7 ;Mediator of RNA polymerase II transcription subunit 14;Mediator of RNA polymerase II transcription subunit 24;Mediator of RNA polymerase II transcription subunit 6 ;Cyclin-C;Cyclin-dependent kinase 8;Mediator of RNA polymerase II transcription subunit 21;Mediator of RNA polymerase II transcription subunit 1;Mediator of RNA polymerase II transcription subunit 25 ;Mediator of RNA polymerase II transcription subunit 12;Mediator of RNA polymerase II transcription subunit 15;Mediator of RNA polymerase II transcription subunit 17;Mediator of RNA polymerase II transcription subunit 13 ;Mediator of RNA polymerase II transcription subunit 23","subunits.Gene.name.":"MED7;MED14;MED24;MED6;CCNC;CDK8;MED21;MED1;MED25;MED12;MED15;MED17;MED13;MED23","subunits.Gene.name.syn.":"ARC34 CRSP9;ARC150 CRSP2 CXorf4 DRIP150 EXLM1 RGR1 TRAP170;ARC100 CRSP4 DRIP100 KIAA0130 THRAP4 TRAP100;ARC33;None;None;SRB7 SURB7;ARC205 CRSP1 CRSP200 DRIP205 DRIP230 PBP PPARBP PPARGBP RB18A TRAP220 TRIP2;ACID1 ARC92 PTOV2;ARC240 CAGH45 HOPA KIAA0192 TNRC11 TRAP230;ARC105 CTG7A PCQAP TIG1 TNRC7;ARC77 CRSP6 DRIP77 DRIP80 TRAP80;ARC250 KIAA0593 THRAP1 TRAP240;ARC130 CRSP3 DRIP130 KIAA1216 SUR2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Experiemts show that the transcription coactivator ARC is required for SREBP (sterol regulatory element binding protein) control of cholesterol and lipid homeostasis. The activator-recruited cofactor ARC consists of the two distinct multisubunit complexes ARC-L and CRSP; Information about four small components of the protein complex is not available in the article. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":288,"ComplexName":"ARC complex","Organism":"Human","Synonyms":"activator-recruited cofactor","Cell.line":"None","subunits.UniProt.IDs.":"O43513;O60244;O75448;O75586;O95402;P24863;P49336;Q13503;Q15648;Q71SY5;Q93074;Q96RN5;Q9NVC6;Q9UHV7;Q9ULK4","subunits.Entrez.IDs.":"9443;9282;9862;10001;9441;892;1024;9412;5469;81857;9968;51586;9440;9969;9439","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0004- affinity chromatography technologies","GO.ID":"GO:0045893;GO:0005515;GO:0051098;GO:0005515;GO:0051090;GO:0005694","GO.description":"positive regulation of transcription, DNA-templated;protein binding;regulation of binding;protein binding;regulation of sequence-specific DNA binding transcription factor activity;chromosome","FunCat.ID":"11.02.03.04.01;16.01;18.01.07;18.02.09;70.10.03","FunCat.description":"transcription activation;protein binding;regulation by binding / dissociation;regulator of transcription factor;chromosome","PubMed.ID":11834832,"subunits.Protein.name.":"Mediator of RNA polymerase II transcription subunit 7 ;Mediator of RNA polymerase II transcription subunit 14;Mediator of RNA polymerase II transcription subunit 24;Mediator of RNA polymerase II transcription subunit 6 ;Mediator of RNA polymerase II transcription subunit 26 ;Cyclin-C;Cyclin-dependent kinase 8;Mediator of RNA polymerase II transcription subunit 21;Mediator of RNA polymerase II transcription subunit 1;Mediator of RNA polymerase II transcription subunit 25 ;Mediator of RNA polymerase II transcription subunit 12;Mediator of RNA polymerase II transcription subunit 15;Mediator of RNA polymerase II transcription subunit 17;Mediator of RNA polymerase II transcription subunit 13 ;Mediator of RNA polymerase II transcription subunit 23","subunits.Gene.name.":"MED7;MED14;MED24;MED6;MED26;CCNC;CDK8;MED21;MED1;MED25;MED12;MED15;MED17;MED13;MED23","subunits.Gene.name.syn.":"ARC34 CRSP9;ARC150 CRSP2 CXorf4 DRIP150 EXLM1 RGR1 TRAP170;ARC100 CRSP4 DRIP100 KIAA0130 THRAP4 TRAP100;ARC33;ARC70 CRSP7;None;None;SRB7 SURB7;ARC205 CRSP1 CRSP200 DRIP205 DRIP230 PBP PPARBP PPARGBP RB18A TRAP220 TRIP2;ACID1 ARC92 PTOV2;ARC240 CAGH45 HOPA KIAA0192 TNRC11 TRAP230;ARC105 CTG7A PCQAP TIG1 TNRC7;ARC77 CRSP6 DRIP77 DRIP80 TRAP80;ARC250 KIAA0593 THRAP1 TRAP240;ARC130 CRSP3 DRIP130 KIAA1216 SUR2","Disease.comment":"None","Subunits.comment":"Information about four small components of the protein complex is not available in the article.","Complex.comment":"Experiemts show that the transcription coactivator ARC is required for SREBP (sterol regulatory element binding protein) control of cholesterol and lipid homeostasis. The activator-recruited cofactor ARC consists of the two distinct multisubunit complexes ARC-L and CRSP. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":289,"ComplexName":"PCNA-MSH2-MSH6 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12004;P43246;P52701","subunits.Entrez.IDs.":"5111;4436;2956","Protein.complex.purification.method":"MI:0096- pull down; MI:0004- affinity chromatography technologies","GO.ID":"GO:0006281;GO:0005634","GO.description":"DNA repair;nucleus","FunCat.ID":"10.01.05.01;70.10","FunCat.description":"DNA repair;nucleus","PubMed.ID":11005803,"subunits.Protein.name.":"Proliferating cell nuclear antigen;DNA mismatch repair protein Msh2 ;DNA mismatch repair protein Msh6","subunits.Gene.name.":"PCNA;MSH2;MSH6","subunits.Gene.name.syn.":"None;;GTBP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"PCNA binds to MSH2-MSH6 complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":290,"ComplexName":"MSH2-MLH1-PMS2-PCNA DNA-repair initiation complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12004;P40692;P43246;P54278","subunits.Entrez.IDs.":"5111;4292;4436;5395","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0003677;GO:0006974;GO:0005634","GO.description":"DNA repair;DNA binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;16.03.01;32.01.09;70.10","FunCat.description":"DNA repair;DNA binding;DNA damage response;nucleus","PubMed.ID":9469823,"subunits.Protein.name.":"Proliferating cell nuclear antigen;DNA mismatch repair protein Mlh1 ;DNA mismatch repair protein Msh2 ;Mismatch repair endonuclease PMS2","subunits.Gene.name.":"PCNA;MLH1;MSH2;PMS2","subunits.Gene.name.syn.":"None;COCA2;;PMSL2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Formation of the initiation complex is ATP-dependent.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":291,"ComplexName":"MSH2-MLH1-PMS2 DNA-repair initiation complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P40692;P43246;P54278","subunits.Entrez.IDs.":"4292;4436;5395","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0003677;GO:0005634","GO.description":"DNA repair;DNA binding;nucleus","FunCat.ID":"10.01.05.01;16.03.01;70.10","FunCat.description":"DNA repair;DNA binding;nucleus","PubMed.ID":9469823,"subunits.Protein.name.":"DNA mismatch repair protein Mlh1 ;DNA mismatch repair protein Msh2 ;Mismatch repair endonuclease PMS2","subunits.Gene.name.":"MLH1;MSH2;PMS2","subunits.Gene.name.syn.":"COCA2;;PMSL2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Formation of the initiation complex is ATP-dependent.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":292,"ComplexName":"MutL-alpha complex","Organism":"Human","Synonyms":"MLH1-PMS2 complex","Cell.line":"None","subunits.UniProt.IDs.":"P40692;P54278","subunits.Entrez.IDs.":"4292;5395","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006281;GO:0003677;GO:0006974;GO:0005634","GO.description":"DNA repair;DNA binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;16.03.01;32.01.09;70.10","FunCat.description":"DNA repair;DNA binding;DNA damage response;nucleus","PubMed.ID":7892206,"subunits.Protein.name.":"DNA mismatch repair protein Mlh1 ;Mismatch repair endonuclease PMS2","subunits.Gene.name.":"MLH1;PMS2","subunits.Gene.name.syn.":"COCA2;PMSL2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":293,"ComplexName":"PCNA-DNA polymerase delta complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O35654;P17918;P52431;Q9CWP8;Q9EQ28","subunits.Entrez.IDs.":"18972;18538;18971;69745;67967","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006260;GO:0006281;GO:0005634","GO.description":"DNA replication;DNA repair;nucleus","FunCat.ID":"10.01.03;10.01.05.01;70.10","FunCat.description":"DNA synthesis and replication;DNA repair;nucleus","PubMed.ID":10219083,"subunits.Protein.name.":"DNA polymerase delta subunit 2;Proliferating cell nuclear antigen;DNA polymerase delta catalytic subunit;DNA polymerase delta subunit 4;DNA polymerase delta subunit 3","subunits.Gene.name.":"Pold2;Pcna;Pold1;Pold4;Pold3","subunits.Gene.name.syn.":"None;None;None;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Pold4 (=p66) is not absolutely necessary for polymerase activity.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":294,"ComplexName":"DNA polymerase delta complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O35654;P52431;Q9CWP8;Q9EQ28","subunits.Entrez.IDs.":"18972;18971;69745;67967","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006260;GO:0005634","GO.description":"DNA replication;nucleus","FunCat.ID":"10.01.03;70.10","FunCat.description":"DNA synthesis and replication;nucleus","PubMed.ID":10219083,"subunits.Protein.name.":"DNA polymerase delta subunit 2;DNA polymerase delta catalytic subunit;DNA polymerase delta subunit 4;DNA polymerase delta subunit 3","subunits.Gene.name.":"Pold2;Pold1;Pold4;Pold3","subunits.Gene.name.syn.":"None;None;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Pold4 (=p66) is not absolutely necessary for polymerase activity.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":295,"ComplexName":"PCNA-DNA ligase complex","Organism":"Mouse","Synonyms":"None","Cell.line":"FM3A cells","subunits.UniProt.IDs.":"O35654;P17918;P37913;Q9EQ28","subunits.Entrez.IDs.":"18972;18538;16881;67967","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006260;GO:0006281;GO:0005634","GO.description":"DNA replication;DNA repair;nucleus","FunCat.ID":"10.01.03;10.01.05.01;70.10","FunCat.description":"DNA synthesis and replication;DNA repair;nucleus","PubMed.ID":10219083,"subunits.Protein.name.":"DNA polymerase delta subunit 2;Proliferating cell nuclear antigen;DNA ligase 1;DNA polymerase delta subunit 3","subunits.Gene.name.":"Pold2;Pcna;Lig1;Pold3","subunits.Gene.name.syn.":"None;None;Lig-1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":296,"ComplexName":"Pcna-Msh2-Msh6 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P17918;P43247;P54276","subunits.Entrez.IDs.":"18538;17685;17688","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006281;GO:0005634","GO.description":"DNA repair;nucleus","FunCat.ID":"10.01.05.01;70.10","FunCat.description":"DNA repair;nucleus","PubMed.ID":10219083,"subunits.Protein.name.":"Proliferating cell nuclear antigen;DNA mismatch repair protein Msh2;DNA mismatch repair protein Msh6","subunits.Gene.name.":"Pcna;Msh2;Msh6","subunits.Gene.name.syn.":"None;None;Gtmbp","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":297,"ComplexName":"PCNA-DNA polymerase delta complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12004;P28340;P49005;Q15054;Q9HCU8","subunits.Entrez.IDs.":"5111;5424;5425;10714;57804","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0006- anti bait coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0006260;GO:0006281;GO:0005634","GO.description":"DNA replication;DNA repair;nucleus","FunCat.ID":"10.01.03;10.01.05.01;70.10","FunCat.description":"DNA synthesis and replication;DNA repair;nucleus","PubMed.ID":11328591,"subunits.Protein.name.":"Proliferating cell nuclear antigen;DNA polymerase delta catalytic subunit;DNA polymerase delta subunit 2;DNA polymerase delta subunit 3;DNA polymerase delta subunit 4","subunits.Gene.name.":"PCNA;POLD1;POLD2;POLD3;POLD4","subunits.Gene.name.syn.":"None;POLD;None;KIAA0039;POLDS","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"PPLD3 stabilizes the polymerase delta complex and increases the affinity of polymerase delta for PCNA.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":298,"ComplexName":"VEGF transcriptional complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P27695;P40763;Q16665;Q99966","subunits.Entrez.IDs.":"328;6774;3091;4435","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;nucleus","FunCat.ID":"11.02.03.04;70.10","FunCat.description":"transcriptional control;nucleus","PubMed.ID":15735682,"subunits.Protein.name.":"DNA-;Signal transducer and activator of transcription 3;Hypoxia-inducible factor 1-alpha;Cbp/p300-interacting transactivator 1","subunits.Gene.name.":"APEX1;STAT3;HIF1A;CITED1","subunits.Gene.name.syn.":"APE APE1 APEX APX HAP1 REF1;APRF;BHLHE78 MOP1 PASD8;MSG1","Disease.comment":"This complex regulates Src-dependent hypoxia-induced expression of VEGF in pancreatic and prostate carcinomas.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":299,"ComplexName":"IRF3-CBP complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q14653;Q99966","subunits.Entrez.IDs.":"3661;4435","Protein.complex.purification.method":"MI:0114-x-ray crystallography;MI:0019-coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0051090","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;regulation of sequence-specific DNA binding transcription factor activity","FunCat.ID":"11.02.03.04;18.02.09","FunCat.description":"transcriptional control;regulator of transcription factor","PubMed.ID":16154084,"subunits.Protein.name.":"Interferon regulatory factor 3;Cbp/p300-interacting transactivator 1","subunits.Gene.name.":"IRF3;CITED1","subunits.Gene.name.syn.":"None;MSG1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The crystal structure of IRF-3 in complex with CBP reveals that CBP interacts with a hydrophobic surface on IRF-3, which in latent IRF-3 is covered by its autoinhibitory elements.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":300,"ComplexName":"PC2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43513;O60244;O75448;O75586;Q13503;Q6P2C8;Q9BTT4;Q9H944;Q9NVC6;Q9Y2W1;Q9Y2X0;Q9Y3C7","subunits.Entrez.IDs.":"9443;9282;9862;10001;9412;9442;84246;9477;9440;9967;10025;51003","Protein.complex.purification.method":"MI:0226- ion exchange chromatography; MI:0071- molecular sieving","GO.ID":"GO:0045893;GO:0005515;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;protein binding;nucleus","FunCat.ID":"11.02.03.04.01;16.01;70.10","FunCat.description":"transcription activation;protein binding;nucleus","PubMed.ID":10882111,"subunits.Protein.name.":"Mediator of RNA polymerase II transcription subunit 7 ;Mediator of RNA polymerase II transcription subunit 14;Mediator of RNA polymerase II transcription subunit 24;Mediator of RNA polymerase II transcription subunit 6 ;Mediator of RNA polymerase II transcription subunit 21;Mediator of RNA polymerase II transcription subunit 27 ;Mediator of RNA polymerase II transcription subunit 10 ;Mediator of RNA polymerase II transcription subunit 20 ;Mediator of RNA polymerase II transcription subunit 17;Thyroid hormone receptor-associated protein 3;Mediator of RNA polymerase II transcription subunit 16;Mediator of RNA polymerase II transcription subunit 31","subunits.Gene.name.":"MED7;MED14;MED24;MED6;MED21;MED27;MED10;MED20;MED17;THRAP3;MED16;MED31","subunits.Gene.name.syn.":"ARC34 CRSP9;ARC150 CRSP2 CXorf4 DRIP150 EXLM1 RGR1 TRAP170;ARC100 CRSP4 DRIP100 KIAA0130 THRAP4 TRAP100;ARC33;SRB7 SURB7;CRSP34 CRSP8;;TRFP;ARC77 CRSP6 DRIP77 DRIP80 TRAP80;TRAP150;DRIP92 THRAP5;SOH1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"According to the authors, PC2 is a submodule of TRAP/SMCC. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":301,"ComplexName":"SMCC complex","Organism":"Human","Synonyms":"SRB/MED-containing cofactor complex","Cell.line":"None","subunits.UniProt.IDs.":"O43513;O60244;O75448;O75586;P24863;P49336;Q13503;Q15648;Q6P2C8;Q93074;Q9BTT4;Q9H944;Q9NVC6;Q9UHV7;Q9Y2W1;Q9Y2X0;Q9Y3C7","subunits.Entrez.IDs.":"9443;9282;9862;10001;892;1024;9412;5469;9442;9968;84246;9477;9440;9969;9967;10025;51003","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0005515;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein binding;nucleus","FunCat.ID":"11.02.03.04;16.01;70.10","FunCat.description":"transcriptional control;protein binding;nucleus","PubMed.ID":10882111,"subunits.Protein.name.":"Mediator of RNA polymerase II transcription subunit 7 ;Mediator of RNA polymerase II transcription subunit 14;Mediator of RNA polymerase II transcription subunit 24;Mediator of RNA polymerase II transcription subunit 6 ;Cyclin-C;Cyclin-dependent kinase 8;Mediator of RNA polymerase II transcription subunit 21;Mediator of RNA polymerase II transcription subunit 1;Mediator of RNA polymerase II transcription subunit 27 ;Mediator of RNA polymerase II transcription subunit 12;Mediator of RNA polymerase II transcription subunit 10 ;Mediator of RNA polymerase II transcription subunit 20 ;Mediator of RNA polymerase II transcription subunit 17;Mediator of RNA polymerase II transcription subunit 13 ;Thyroid hormone receptor-associated protein 3;Mediator of RNA polymerase II transcription subunit 16;Mediator of RNA polymerase II transcription subunit 31","subunits.Gene.name.":"MED7;MED14;MED24;MED6;CCNC;CDK8;MED21;MED1;MED27;MED12;MED10;MED20;MED17;MED13;THRAP3;MED16;MED31","subunits.Gene.name.syn.":"ARC34 CRSP9;ARC150 CRSP2 CXorf4 DRIP150 EXLM1 RGR1 TRAP170;ARC100 CRSP4 DRIP100 KIAA0130 THRAP4 TRAP100;ARC33;None;None;SRB7 SURB7;ARC205 CRSP1 CRSP200 DRIP205 DRIP230 PBP PPARBP PPARGBP RB18A TRAP220 TRIP2;CRSP34 CRSP8;ARC240 CAGH45 HOPA KIAA0192 TNRC11 TRAP230;;TRFP;ARC77 CRSP6 DRIP77 DRIP80 TRAP80;ARC250 KIAA0593 THRAP1 TRAP240;TRAP150;DRIP92 THRAP5;SOH1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":302,"ComplexName":"INO80 chromatin remodeling complex","Organism":"Human","Synonyms":"INO80 complex","Cell.line":"None","subunits.UniProt.IDs.":"O96019;P15923;Q53TQ3;Q6P4R8;Q6PI98;Q8NBZ0;Q96EZ8;Q9C086;Q9H981;Q9H9F9;Q9ULG1;Q9Y230;Q9Y265","subunits.Entrez.IDs.":"86;6929;54891;4798;125476;283899;10445;83444;93973;79913;54617;10856;8607","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0003677;GO:0005524;GO:0051276;GO:0005694","GO.description":"DNA topological change;DNA binding;ATP binding;chromosome organization;chromosome","FunCat.ID":"10.01.09.05;16.03.01;16.19.03;42.10.03;70.10.03","FunCat.description":"DNA conformation modification (e.g. chromatin);DNA binding;ATP binding;organization of chromosome structure;chromosome","PubMed.ID":16230350,"subunits.Protein.name.":"Actin-like protein 6A;Transcription factor E2-alpha ;INO80 complex subunit D;Nuclear factor related to kappa-B-binding protein ;INO80 complex subunit C ;INO80 complex subunit E ;Microspherule protein 1 ;INO80 complex subunit B ;Actin-related protein 8 ;Actin-related protein 5 ;DNA helicase INO80 ;RuvB-like 2;RuvB-like 1","subunits.Gene.name.":"ACTL6A;TCF3;INO80D;NFRKB;INO80C;INO80E;MCRS1;INO80B;ACTR8;ACTR5;INO80;RUVBL2;RUVBL1","subunits.Gene.name.syn.":"BAF53 BAF53A INO80K;BHLHB21 E2A ITF1;;INO80G;C18orf37;CCDC95;INO80Q MSP58;HMGA1L4 PAPA1 ZNHIT4;ARP8 INO80N;ARP5;INO80A INOC1 KIAA1259;INO80J TIP48 TIP49B;INO80H NMP238 TIP49 TIP49A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"INO80 complex exhibits DNA- and nucleosome-activated ATPase activity and catalyzes ATP-dependent nucleosome sliding.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":304,"ComplexName":"SRCAP-associated chromatin remodeling complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43257;O95619;O96019;P0C0S5;Q15906;Q6ZRS2;Q96CJ1;Q9GZN1;Q9Y230;Q9Y265","subunits.Entrez.IDs.":"10467;8089;86;3015;6944;10847;55840;64431;10856;8607","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045893;GO:0051276;GO:0005634","GO.description":"DNA topological change;positive regulation of transcription, DNA-templated;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription activation;organization of chromosome structure;nucleus","PubMed.ID":15647280,"subunits.Protein.name.":"Zinc finger HIT domain-containing protein 1 ;YEATS domain-containing protein 4;Actin-like protein 6A;Histone H2A.Z ;Vacuolar protein sorting-associated protein 72 homolog ;Helicase SRCAP ;ELL-associated factor 2 ;Actin-related protein 6 ;RuvB-like 2;RuvB-like 1","subunits.Gene.name.":"ZNHIT1;YEATS4;ACTL6A;H2AFZ;VPS72;SRCAP;EAF2;ACTR6;RUVBL2;RUVBL1","subunits.Gene.name.syn.":"CGBP1 ZNFN4A1;GAS41;BAF53 BAF53A INO80K;H2AZ;TCFL1 YL1;KIAA0309;TRAITS;;INO80J TIP48 TIP49B;INO80H NMP238 TIP49 TIP49A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":305,"ComplexName":"40S ribosomal subunit, cytoplasmic","Organism":"Human","Synonyms":"small ribosomal subunit, cytoplasmic","Cell.line":"None","subunits.UniProt.IDs.":"P08708;P08865;P15880;P22090;P23396;P25398;P39019;P42677;P46781;P46782;P46783;P60866;P61247;P62081;P62241;P62244;P62249;P62263;P62266;P62269;P62273;P62277;P62280;P62701;P62753;P62841;P62847;P62851;P62854;P62857;P62861;P62979;P63220","subunits.Entrez.IDs.":"6218;3921;6187;6192;6188;6206;6223;6232;6203;6193;6204;6224;6189;6201;6202;6210;6217;6208;6228;6222;6235;6207;6205;6191;6194;6209;6229;6230;6231;6234;2197;6233;6227","Protein.complex.purification.method":"MI:0363-inferred by author","GO.ID":"GO:0006412;GO:0005737","GO.description":"translation;cytoplasm","FunCat.ID":"12.04;70.03","FunCat.description":"translation;cytoplasm","PubMed.ID":14681386,"subunits.Protein.name.":"40S ribosomal protein S17;40S ribosomal protein SA;40S ribosomal protein S2;40S ribosomal protein S4, Y isoform 1;40S ribosomal protein S3;40S ribosomal protein S12;40S ribosomal protein S19;40S ribosomal protein S27;40S ribosomal protein S9;40S ribosomal protein S5 [Cleaved into: 40S ribosomal protein S5, N-terminally processed];40S ribosomal protein S10;40S ribosomal protein S20;40S ribosomal protein S3a;40S ribosomal protein S7;40S ribosomal protein S8;40S ribosomal protein S15a;40S ribosomal protein S16;40S ribosomal protein S14;40S ribosomal protein S23;40S ribosomal protein S18;40S ribosomal protein S29;40S ribosomal protein S13;40S ribosomal protein S11;40S ribosomal protein S4, X isoform;40S ribosomal protein S6;40S ribosomal protein S15;40S ribosomal protein S24;40S ribosomal protein S25;40S ribosomal protein S26;40S ribosomal protein S28;40S ribosomal protein S30;Ubiquitin-40S ribosomal protein S27a;40S ribosomal protein S21","subunits.Gene.name.":"RPS17;RPSA;RPS2;RPS4Y1;RPS3;RPS12;RPS19;RPS27;RPS9;RPS5;RPS10;RPS20;RPS3A;RPS7;RPS8;RPS15A;RPS16;RPS14;RPS23;RPS18;RPS29;RPS13;RPS11;RPS4X;RPS6;RPS15;RPS24;RPS25;RPS26;RPS28;FAU;RPS27A;RPS21","subunits.Gene.name.syn.":"RPS17L;LAMBR LAMR1;RPS4;RPS4Y;None;None;None;MPS1;None;None;None;None;FTE1 MFTL;None;None;None;None;None;None;D6S218E;None;None;None;CCG2 RPS4 SCAR;None;RIG;None;None;None;None;None;UBA80 UBCEP1;None","Disease.comment":"None","Subunits.comment":"Since the authors did not specify RPS4Y, we used isoform RPS4Y1","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":306,"ComplexName":"Ribosome, cytoplasmic","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P05386;P05387;P05388;P08708;P08865;P15880;P18077;P18124;P18621;P22090;P23396;P25398;P26373;P27635;P30050;P32969;P35268;P36578;P39019;P39023;P40429;P42677;P42766;P46776;P46777;P46778;P46779;P46781;P46782;P46783;P47914;P49207;P50914;P60866;P61247;P61254;P61313;P61353;P61513;P61927;P62081;P62241;P62244;P62249;P62263;P62266;P62269;P62273;P62277;P62280;P62424;P62701;P62750;P62753;P62829;P62841;P62847;P62851;P62854;P62857;P62861;P62888;P62891;P62899;P62906;P62910;P62913;P62917;P62945;P62979;P62987;P63173;P63220;P83731;P83881;P84098;Q02543;Q02878;Q07020;Q9Y3U8","subunits.Entrez.IDs.":"6176;6181;6175;6218;3921;6187;6165;6129;6139;6192;6188;6206;6137;6134;6136;6133;6146;6124;6223;6122;23521;6232;11224;6157;6125;6144;6158;6203;6193;6204;6159;6164;9045;6224;6189;6154;6138;6155;6168;6167;6201;6202;6210;6217;6208;6228;6222;6235;6207;6205;6130;6191;6147;6194;9349;6209;6229;6230;6231;6234;2197;6156;6170;6160;4736;6161;6135;6132;6171;6233;7311;6169;6227;6152;6173;6143;6142;6128;6141;25873","Protein.complex.purification.method":"MI:0363-inferred by author","GO.ID":"GO:0006412;GO:0005737","GO.description":"translation;cytoplasm","FunCat.ID":"12.04;70.03","FunCat.description":"translation;cytoplasm","PubMed.ID":14681386,"subunits.Protein.name.":"60S acidic ribosomal protein P1;60S acidic ribosomal protein P2;60S acidic ribosomal protein P0;40S ribosomal protein S17;40S ribosomal protein SA;40S ribosomal protein S2;60S ribosomal protein L35a;60S ribosomal protein L7;60S ribosomal protein L17;40S ribosomal protein S4, Y isoform 1;40S ribosomal protein S3;40S ribosomal protein S12;60S ribosomal protein L13;60S ribosomal protein L10;60S ribosomal protein L12;60S ribosomal protein L9;60S ribosomal protein L22;60S ribosomal protein L4;40S ribosomal protein S19;60S ribosomal protein L3;60S ribosomal protein L13a;40S ribosomal protein S27;60S ribosomal protein L35;60S ribosomal protein L27a;60S ribosomal protein L5;60S ribosomal protein L21;60S ribosomal protein L28;40S ribosomal protein S9;40S ribosomal protein S5 [Cleaved into: 40S ribosomal protein S5, N-terminally processed];40S ribosomal protein S10;60S ribosomal protein L29;60S ribosomal protein L34;60S ribosomal protein L14;40S ribosomal protein S20;40S ribosomal protein S3a;60S ribosomal protein L26;60S ribosomal protein L15;60S ribosomal protein L27;60S ribosomal protein L37a;60S ribosomal protein L37;40S ribosomal protein S7;40S ribosomal protein S8;40S ribosomal protein S15a;40S ribosomal protein S16;40S ribosomal protein S14;40S ribosomal protein S23;40S ribosomal protein S18;40S ribosomal protein S29;40S ribosomal protein S13;40S ribosomal protein S11;60S ribosomal protein L7a;40S ribosomal protein S4, X isoform;60S ribosomal protein L23a;40S ribosomal protein S6;60S ribosomal protein L23;40S ribosomal protein S15;40S ribosomal protein S24;40S ribosomal protein S25;40S ribosomal protein S26;40S ribosomal protein S28;40S ribosomal protein S30;60S ribosomal protein L30;60S ribosomal protein L39;60S ribosomal protein L31;60S ribosomal protein L10a;60S ribosomal protein L32;60S ribosomal protein L11;60S ribosomal protein L8;60S ribosomal protein L41;Ubiquitin-40S ribosomal protein S27a;Ubiquitin-60S ribosomal protein L40;60S ribosomal protein L38;40S ribosomal protein S21;60S ribosomal protein L24;60S ribosomal protein L36a;60S ribosomal protein L19;60S ribosomal protein L18a;60S ribosomal protein L6;60S ribosomal protein L18;60S ribosomal protein L36","subunits.Gene.name.":"RPLP1;RPLP2;RPLP0;RPS17;RPSA;RPS2;RPL35A;RPL7;RPL17;RPS4Y1;RPS3;RPS12;RPL13;RPL10;RPL12;RPL9; RPL9;RPL22;RPL4;RPS19;RPL3;RPL13A;RPS27;RPL35;RPL27A;RPL5;RPL21;RPL28;RPS9;RPS5;RPS10;RPL29;RPL34;RPL14;RPS20;RPS3A;RPL26;RPL15;RPL27;RPL37A;RPL37;RPS7;RPS8;RPS15A;RPS16;RPS14;RPS23;RPS18;RPS29;RPS13;RPS11;RPL7A;RPS4X;RPL23A;RPS6;RPL23;RPS15;RPS24;RPS25;RPS26;RPS28;FAU;RPL30;RPL39;RPL31;RPL10A;RPL32;RPL11;RPL8;RPL41;RPS27A;UBA52;RPL38;RPS21;RPL24;RPL36A;RPL19;RPL18A;RPL6;RPL18;RPL36","subunits.Gene.name.syn.":"RRP1;D11S2243E RPP2;None;RPS17L;LAMBR LAMR1;RPS4;None;None;None;RPS4Y;None;None;BBC1;DXS648E QM;None;; ; ;;None;RPL1;None;None;None;MPS1;None;None;None;None;None;None;None;None;None;None;None;None;FTE1 MFTL;None;EC45;None;None;None;None;None;None;None;None;None;D6S218E;None;None;None;SURF-3 SURF3;CCG2 RPS4 SCAR;None;None;None;RIG;None;None;None;None;None;None;None;None;NEDD6;None;None;None;None;UBA80 UBCEP1;UBCEP2;None;None;None;RPL44;None;None;TXREB1;None;None","Disease.comment":"None","Subunits.comment":"Since the authors did not specify RPS4Y, we used isoform RPS4Y1","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":307,"ComplexName":"Epithelial utrophin-associated protein complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"MDCK cells, epithelium","subunits.UniProt.IDs.":"O08614;O70585;Q61235","subunits.Entrez.IDs.":"22288;13528;20650","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005886","GO.description":"plasma membrane","FunCat.ID":"70.02","FunCat.description":"eukaryotic plasma membrane / membrane attached","PubMed.ID":10209032,"subunits.Protein.name.":"Cytoskeletal protein;Dystrobrevin beta;Beta-2-syntrophin","subunits.Gene.name.":"Utrn;Dtnb;Sntb2","subunits.Gene.name.syn.":"utrophin;None;Snt2b2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The complex is restricted to the basolateral cell surface of epithelial cells. The authors suggest that this complex in the MDCK cell line may be involved in the generation or maintenance of cell polarity and the formation of signaling complexes in epithelia.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":308,"ComplexName":"60S ribosomal subunit, cytoplasmic","Organism":"Human","Synonyms":"large ribosomal subunit, cytoplasmic","Cell.line":"None","subunits.UniProt.IDs.":"P05386;P05387;P05388;P18077;P18124;P18621;P26373;P27635;P30050;P32969;P35268;P36578;P39023;P40429;P42766;P46776;P46777;P46778;P46779;P47914;P49207;P50914;P61254;P61313;P61353;P61513;P61927;P62424;P62750;P62829;P62888;P62891;P62899;P62906;P62910;P62913;P62917;P62945;P62987;P63173;P83731;P83881;P84098;Q02543;Q02878;Q07020;Q9Y3U8","subunits.Entrez.IDs.":"6176;6181;6175;6165;6129;6139;6137;6134;6136;6133;6146;6124;6122;23521;11224;6157;6125;6144;6158;6159;6164;9045;6154;6138;6155;6168;6167;6130;6147;9349;6156;6170;6160;4736;6161;6135;6132;6171;7311;6169;6152;6173;6143;6142;6128;6141;25873","Protein.complex.purification.method":"MI:0363- inferred by author","GO.ID":"GO:0006412;GO:0005737","GO.description":"translation;cytoplasm","FunCat.ID":"12.04;70.03","FunCat.description":"translation;cytoplasm","PubMed.ID":14681386,"subunits.Protein.name.":"60S acidic ribosomal protein P1;60S acidic ribosomal protein P2;60S acidic ribosomal protein P0;60S ribosomal protein L35a;60S ribosomal protein L7;60S ribosomal protein L17;60S ribosomal protein L13;60S ribosomal protein L10;60S ribosomal protein L12;60S ribosomal protein L9;60S ribosomal protein L22;60S ribosomal protein L4;60S ribosomal protein L3;60S ribosomal protein L13a;60S ribosomal protein L35;60S ribosomal protein L27a;60S ribosomal protein L5;60S ribosomal protein L21;60S ribosomal protein L28;60S ribosomal protein L29;60S ribosomal protein L34;60S ribosomal protein L14;60S ribosomal protein L26;60S ribosomal protein L15;60S ribosomal protein L27;60S ribosomal protein L37a;60S ribosomal protein L37;60S ribosomal protein L7a;60S ribosomal protein L23a;60S ribosomal protein L23;60S ribosomal protein L30;60S ribosomal protein L39;60S ribosomal protein L31;60S ribosomal protein L10a;60S ribosomal protein L32;60S ribosomal protein L11;60S ribosomal protein L8;60S ribosomal protein L41;Ubiquitin-60S ribosomal protein L40;60S ribosomal protein L38;60S ribosomal protein L24;60S ribosomal protein L36a;60S ribosomal protein L19;60S ribosomal protein L18a;60S ribosomal protein L6;60S ribosomal protein L18;60S ribosomal protein L36","subunits.Gene.name.":"RPLP1;RPLP2;RPLP0;RPL35A;RPL7;RPL17;RPL13;RPL10;RPL12;RPL9; RPL9;RPL22;RPL4;RPL3;RPL13A;RPL35;RPL27A;RPL5;RPL21;RPL28;RPL29;RPL34;RPL14;RPL26;RPL15;RPL27;RPL37A;RPL37;RPL7A;RPL23A;RPL23;RPL30;RPL39;RPL31;RPL10A;RPL32;RPL11;RPL8;RPL41;UBA52;RPL38;RPL24;RPL36A;RPL19;RPL18A;RPL6;RPL18;RPL36","subunits.Gene.name.syn.":"RRP1;D11S2243E RPP2;None;None;None;None;BBC1;DXS648E QM;None;; ; ;;None;RPL1;None;None;None;None;None;None;None;None;None;None;None;EC45;None;None;None;SURF-3 SURF3;None;None;None;None;None;NEDD6;None;None;None;None;UBCEP2;None;None;RPL44;None;None;TXREB1;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":309,"ComplexName":"RC complex","Organism":"Bovine","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P20664;P28339;P33609;P33610;P35601;P49004;Q2TBV1;Q3UI84;Q58D13;Q9D0F6;Q9WUK4","subunits.Entrez.IDs.":"19075;281990;18968;19076;19687;281991;515602;106344;514793;72151;19718","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0071- molecular sieving; MI:0226- ion exchange chromatography","GO.ID":"GO:0006267;GO:0003688;GO:0006271;GO:0003677;GO:0005634","GO.description":"pre-replicative complex assembly involved in nuclear cell cycle DNA replication;DNA replication origin binding;DNA strand elongation involved in DNA replication;DNA binding;nucleus","FunCat.ID":"10.01.03.03;10.01.03.05;16.03.01;70.10","FunCat.description":"ori recognition and priming complex formation;extension/ polymerization activity;DNA binding;nucleus","PubMed.ID":8639537,"subunits.Protein.name.":"DNA primase small subunit;DNA polymerase delta catalytic subunit ;DNA polymerase alpha catalytic subunit;DNA primase large subunit;Replication factor C subunit 1 ;DNA polymerase delta subunit 2 ;Replication factor C subunit 3 ;Replication factor C subunit 4;DNA polymerase alpha subunit B ;Replication factor C subunit 5 ;Replication factor C subunit 2","subunits.Gene.name.":"Prim1;POLD1;Pola1;Prim2;Rfc1;POLD2;RFC3;Rfc4;POLA2;Rfc5;Rfc2","subunits.Gene.name.syn.":"None;;Pola;None;Ibf-1 Recc1;;;;;;","Disease.comment":"None","Subunits.comment":"Since several bovine proteins were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were taken.","Complex.comment":"ATP is required for the stability of the RC complex. PCNA is required to stabilize the RC complex to a DNA primer-end.","SWISSPROT.organism":"Mus musculus (Mouse);Bos taurus (Bovine);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Bos taurus (Bovine);Bos taurus (Bovine);Mus musculus (Mouse);Bos taurus (Bovine);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":310,"ComplexName":"Cell cycle kinase complex CDC2","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95067;P06493;P12004;P14635;P24385;P38936","subunits.Entrez.IDs.":"9133;983;5111;891;595;1026","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0000278","GO.description":"mitotic cell cycle","FunCat.ID":"10.03.01.01","FunCat.description":"mitotic cell cycle","PubMed.ID":7903056,"subunits.Protein.name.":"G2/mitotic-specific cyclin-B2;Cyclin-dependent kinase 1 ;Proliferating cell nuclear antigen;G2/mitotic-specific cyclin-B1;G1/S-specific cyclin-D1;Cyclin-dependent kinase inhibitor 1","subunits.Gene.name.":"CCNB2;CDK1;PCNA;CCNB1;CCND1;CDKN1A","subunits.Gene.name.syn.":";CDC2 CDC28A CDKN1 P34CDC2;None;CCNB;BCL1 PRAD1;CAP20 CDKN1 CIP1 MDA6 PIC1 SDI1 WAF1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":311,"ComplexName":"Cell cycle kinase complex CDK2","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12004;P24385;P24941;P38936","subunits.Entrez.IDs.":"5111;595;1017;1026","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0000278","GO.description":"mitotic cell cycle","FunCat.ID":"10.03.01.01","FunCat.description":"mitotic cell cycle","PubMed.ID":7903056,"subunits.Protein.name.":"Proliferating cell nuclear antigen;G1/S-specific cyclin-D1;Cyclin-dependent kinase 2;Cyclin-dependent kinase inhibitor 1","subunits.Gene.name.":"PCNA;CCND1;CDK2;CDKN1A","subunits.Gene.name.syn.":"None;BCL1 PRAD1;CDKN2;CAP20 CDKN1 CIP1 MDA6 PIC1 SDI1 WAF1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":312,"ComplexName":"Cell cycle kinase complex CDK4","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P11802;P12004;P24385;P38936","subunits.Entrez.IDs.":"1019;5111;595;1026","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0000278","GO.description":"mitotic cell cycle","FunCat.ID":"10.03.01.01","FunCat.description":"mitotic cell cycle","PubMed.ID":7903056,"subunits.Protein.name.":"Cyclin-dependent kinase 4 ;Proliferating cell nuclear antigen;G1/S-specific cyclin-D1;Cyclin-dependent kinase inhibitor 1","subunits.Gene.name.":"CDK4;PCNA;CCND1;CDKN1A","subunits.Gene.name.syn.":";None;BCL1 PRAD1;CAP20 CDKN1 CIP1 MDA6 PIC1 SDI1 WAF1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":313,"ComplexName":"Cell cycle kinase complex CDK5","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12004;P24385;P30281;P38936;Q00535","subunits.Entrez.IDs.":"5111;595;896;1026;1020","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0000278;GO:0006468;GO:0006470;GO:0046777","GO.description":"mitotic cell cycle;protein phosphorylation;protein dephosphorylation;protein autophosphorylation","FunCat.ID":"10.03.01.01;14.07.03","FunCat.description":"mitotic cell cycle;modification by phosphorylation, dephosphorylation, autophosphorylation","PubMed.ID":7903056,"subunits.Protein.name.":"Proliferating cell nuclear antigen;G1/S-specific cyclin-D1;G1/S-specific cyclin-D3;Cyclin-dependent kinase inhibitor 1 ;Cyclin-dependent-like kinase 5","subunits.Gene.name.":"PCNA;CCND1;CCND3;CDKN1A;CDK5","subunits.Gene.name.syn.":"None;BCL1 PRAD1;;CAP20 CDKN1 CIP1 MDA6 PIC1 SDI1 WAF1;CDKN5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":314,"ComplexName":"PCNA-p21 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12004;P38936","subunits.Entrez.IDs.":"5111;1026","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0000075;GO:0005634","GO.description":"cell cycle checkpoint;nucleus","FunCat.ID":"10.03.01.03;70.10","FunCat.description":"cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);nucleus","PubMed.ID":8861913,"subunits.Protein.name.":"Proliferating cell nuclear antigen;Cyclin-dependent kinase inhibitor 1","subunits.Gene.name.":"PCNA;CDKN1A","subunits.Gene.name.syn.":"None;CAP20 CDKN1 CIP1 MDA6 PIC1 SDI1 WAF1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":315,"ComplexName":"28S ribosomal subunit, mitochondrial","Organism":"Human","Synonyms":"Small ribosomal subunit, mitochondrial","Cell.line":"None","subunits.UniProt.IDs.":"O15235;O60783;P51398;P82650;P82663;P82664;P82673;P82675;P82909;P82912;P82914;P82921;P82930;P82932;P82933;Q92552;Q92665;Q96EL2;Q9BYN8;Q9NP92;Q9NVS2;Q9Y291;Q9Y2Q9;Q9Y2R5;Q9Y2R9;Q9Y399;Q9Y3D3;Q9Y3D5;Q9Y3D9;Q9Y676","subunits.Entrez.IDs.":"6183;63931;7818;56945;64432;55173;None;64969;92259;64963;64960;54460;65993;64968;64965;23107;10240;64951;64949;10884;55168;51650;28957;51373;51081;51116;51021;51023;51649;28973","Protein.complex.purification.method":"MI:0363- inferred by author","GO.ID":"GO:0006412;GO:0005759","GO.description":"translation;mitochondrial matrix","FunCat.ID":"12.04;70.16.07","FunCat.description":"translation;mitochondrial matrix","PubMed.ID":14681386,"subunits.Protein.name.":"28S ribosomal protein S12, mitochondrial ;28S ribosomal protein S14, mitochondrial ;28S ribosomal protein S29, mitochondrial ;28S ribosomal protein S22, mitochondrial ;28S ribosomal protein S25, mitochondrial ;28S ribosomal protein S10, mitochondrial ;28S ribosomal protein S35, mitochondrial ;28S ribosomal protein S5, mitochondrial ;28S ribosomal protein S36, mitochondrial ;28S ribosomal protein S11, mitochondrial ;28S ribosomal protein S15, mitochondrial ;28S ribosomal protein S21, mitochondrial ;28S ribosomal protein S34, mitochondrial ;28S ribosomal protein S6, mitochondrial ;28S ribosomal protein S9, mitochondrial ;28S ribosomal protein S27, mitochondrial ;28S ribosomal protein S31, mitochondrial ;28S ribosomal protein S24, mitochondrial ;28S ribosomal protein S26, mitochondrial ;28S ribosomal protein S30, mitochondrial ;28S ribosomal protein S18a, mitochondrial ;28S ribosomal protein S33, mitochondrial ;28S ribosomal protein S28, mitochondrial ;28S ribosomal protein S17, mitochondrial ;28S ribosomal protein S7, mitochondrial ;28S ribosomal protein S2, mitochondrial ;28S ribosomal protein S16, mitochondrial ;28S ribosomal protein S18c, mitochondrial ;28S ribosomal protein S23, mitochondrial ;28S ribosomal protein S18b, mitochondrial","subunits.Gene.name.":"MRPS12;MRPS14;DAP3;MRPS22;MRPS25;MRPS10;MRPS35;MRPS5;MRPS36;MRPS11;MRPS15;MRPS21;MRPS34;MRPS6;MRPS9;MRPS27;MRPS31;MRPS24;MRPS26;MRPS30;MRPS18A;MRPS33;MRPS28;MRPS17;MRPS7;MRPS2;MRPS16;MRPS18C;MRPS23;MRPS18B","subunits.Gene.name.syn.":"RPMS12 RPSM12;;MRPS29;C3orf5 RPMS22;RPMS25;;MRPS28;;;RPMS11;RPMS15;RPMS21;;C21orf101 RPMS6;RPMS9;KIAA0264;IMOGN38;;C20orf193 RPMS13;PDCD9;;;MRPS35;RPMS17;;;RPMS16;;;C6orf14","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"With the exception of MRPS12, all proteins of the small ribosomal subunit from ribosomes of Bos taurus were identified in a proteomic approach (PMID:11279123).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":316,"ComplexName":"Dystrophin associated complex DPC (Dmd, Dtnb), brain-derived","Organism":"Rat","Synonyms":"None","Cell.line":"brain neurons","subunits.UniProt.IDs.":"P11530;P84060","subunits.Entrez.IDs.":"24907;362715","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007268;GO:0007043","GO.description":"synaptic transmission;cell-cell junction assembly","FunCat.ID":"34.03.01;42.06.04","FunCat.description":"synaptic transmission;intercellular junction (gap junction/adherens junction)","PubMed.ID":10545507,"subunits.Protein.name.":"Dystrophin;Dystrobrevin beta","subunits.Gene.name.":"Dmd;Dtnb","subunits.Gene.name.syn.":"None;None","Disease.comment":"Dmd is involved in DUCHENNE muscular dystrophy (DMD).","Subunits.comment":"None","Complex.comment":"The authors demonstrate that beta-dystrobrevin is part of a neuronal DPC-like complex and suggest that it may be involved in the compound phenotype of cognitive dysfunction in DMD patients.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":317,"ComplexName":"Dystrobrevin-syntrophin complex, brain-derived","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"O70585;P11531;Q61234;Q9D2N4","subunits.Entrez.IDs.":"13528;13405;20648;13527","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007268;GO:0005886","GO.description":"synaptic transmission;plasma membrane","FunCat.ID":"34.03.01;70.02","FunCat.description":"synaptic transmission;eukaryotic plasma membrane / membrane attached","PubMed.ID":10545507,"subunits.Protein.name.":"Dystrobrevin beta;Dystrophin;Alpha-1-syntrophin;Dystrobrevin alpha","subunits.Gene.name.":"Dtnb;Dmd;Snta1;Dtna","subunits.Gene.name.syn.":"None;None;Snt1;Dtn","Disease.comment":"None","Subunits.comment":"The mouse dystrophin was described as Dp71, the authors differentiate between alpha-dystrobrevin 1 and alpha-dystrobrevin 2.Since the authors did not specify syntrophin, we used Snta1.","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":318,"ComplexName":"Muscle-derived dystrobrevin-syntrophin complex","Organism":"Mouse","Synonyms":"None","Cell.line":"muscle","subunits.UniProt.IDs.":"Q61234;Q9D2N4","subunits.Entrez.IDs.":"20648;13527","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006936","GO.description":"muscle contraction","FunCat.ID":"36.25.09","FunCat.description":"muscle contraction","PubMed.ID":10545507,"subunits.Protein.name.":"Alpha-1-syntrophin;Dystrobrevin alpha","subunits.Gene.name.":"Snta1;Dtna","subunits.Gene.name.syn.":"Snt1;Dtn","Disease.comment":"None","Subunits.comment":"The authors differentiate between alpha-dystrobrevin 1 and alpha-dystrobrevin 2.Since the authors did not specify syntrophin, we used Snta1.","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":320,"ComplexName":"55S ribosome, mitochondrial","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15235;O60783;O75394;P09001;P49406;P51398;P52815;P82650;P82663;P82664;P82673;P82675;P82909;P82912;P82914;P82921;P82930;P82932;P82933;P83111;Q13084;Q13405;Q16540;Q4U2R6;Q5T653;Q6P161;Q6P1L8;Q7Z2W9;Q7Z7F7;Q7Z7H8;Q86TS9;Q8IXM3;Q8N5N7;Q8N983;Q8TCC3;Q92552;Q92665;Q96A35;Q96DV4;Q96EL2;Q96EL3;Q96GC5;Q9BQ48;Q9BRJ2;Q9BYC8;Q9BYC9;Q9BYD1;Q9BYD2;Q9BYD3;Q9BYD6;Q9BYN8;Q9BZE1;Q9H0U6;Q9H2W6;Q9H9J2;Q9HD33;Q9NP92;Q9NQ50;Q9NRX2;Q9NVS2;Q9NWU5;Q9NX20;Q9NYK5;Q9NZE8;Q9P015;Q9P0J6;Q9P0M9;Q9Y291;Q9Y2Q9;Q9Y2R5;Q9Y2R9;Q9Y399;Q9Y3B7;Q9Y3D3;Q9Y3D5;Q9Y3D9;Q9Y676;Q9Y6G3","subunits.Entrez.IDs.":"6183;63931;9553;11222;9801;7818;6182;56945;64432;55173;None;64969;92259;64963;64960;54460;65993;64968;64965;114294;10573;740;6150;51258;51069;116541;64928;219927;128308;124995;122704;64975;54534;84545;51263;23107;10240;79590;64978;64951;116540;51642;64981;84311;64983;55052;28998;65005;51073;65008;64949;51253;29074;26589;65080;57129;10884;64976;63875;55168;29093;54948;54148;51318;29088;64979;51264;51650;28957;51373;51081;51116;65003;51021;51023;51649;28973;28977","Protein.complex.purification.method":"MI:0363- inferred by author","GO.ID":"GO:0006412;GO:0005759","GO.description":"translation;mitochondrial matrix","FunCat.ID":"12.04;70.16.07","FunCat.description":"translation;mitochondrial matrix","PubMed.ID":14681386,"subunits.Protein.name.":"28S ribosomal protein S12, mitochondrial ;28S ribosomal protein S14, mitochondrial ;39S ribosomal protein L33, mitochondrial ;39S ribosomal protein L3, mitochondrial ;39S ribosomal protein L19, mitochondrial ;28S ribosomal protein S29, mitochondrial ;39S ribosomal protein L12, mitochondrial ;28S ribosomal protein S22, mitochondrial ;28S ribosomal protein S25, mitochondrial ;28S ribosomal protein S10, mitochondrial ;28S ribosomal protein S35, mitochondrial ;28S ribosomal protein S5, mitochondrial ;28S ribosomal protein S36, mitochondrial ;28S ribosomal protein S11, mitochondrial ;28S ribosomal protein S15, mitochondrial ;28S ribosomal protein S21, mitochondrial ;28S ribosomal protein S34, mitochondrial ;28S ribosomal protein S6, mitochondrial ;28S ribosomal protein S9, mitochondrial ;Serine beta-lactamase-like protein LACTB, mitochondrial ;39S ribosomal protein L28, mitochondrial ;39S ribosomal protein L49, mitochondrial ;39S ribosomal protein L23, mitochondrial ;39S ribosomal protein L51, mitochondrial ;39S ribosomal protein L2, mitochondrial ;39S ribosomal protein L54, mitochondrial ;39S ribosomal protein L14, mitochondrial ;39S ribosomal protein L21, mitochondrial ;39S ribosomal protein L55, mitochondrial ;39S ribosomal protein L10, mitochondrial ;39S ribosomal protein L52, mitochondrial ;39S ribosomal protein L41, mitochondrial ;39S ribosomal protein L50, mitochondrial ;39S ribosomal protein L43, mitochondrial ;39S ribosomal protein L30, mitochondrial ;28S ribosomal protein S27, mitochondrial ;28S ribosomal protein S31, mitochondrial ;39S ribosomal protein L24, mitochondrial ;39S ribosomal protein L38, mitochondrial ;28S ribosomal protein S24, mitochondrial ;39S ribosomal protein L53, mitochondrial ;39S ribosomal protein L48, mitochondrial ;39S ribosomal protein L34, mitochondrial ;39S ribosomal protein L45, mitochondrial ;39S ribosomal protein L32, mitochondrial ;39S ribosomal protein L20, mitochondrial ;39S ribosomal protein L13, mitochondrial ;39S ribosomal protein L9, mitochondrial ;39S ribosomal protein L4, mitochondrial ;39S ribosomal protein L1, mitochondrial ;28S ribosomal protein S26, mitochondrial ;39S ribosomal protein L37, mitochondrial ;39S ribosomal protein L18, mitochondrial ;39S ribosomal protein L46, mitochondrial ;39S ribosomal protein L44, mitochondrial ;39S ribosomal protein L47, mitochondrial ;28S ribosomal protein S30, mitochondrial ;39S ribosomal protein L40, mitochondrial ;39S ribosomal protein L17, mitochondrial ;28S ribosomal protein S18a, mitochondrial ;39S ribosomal protein L22, mitochondrial ;39S ribosomal protein L16, mitochondrial ;39S ribosomal protein L39, mitochondrial ;39S ribosomal protein L35, mitochondrial ;39S ribosomal protein L15, mitochondrial ;39S ribosomal protein L36, mitochondrial ;39S ribosomal protein L27, mitochondrial ;28S ribosomal protein S33, mitochondrial ;28S ribosomal protein S28, mitochondrial ;28S ribosomal protein S17, mitochondrial ;28S ribosomal protein S7, mitochondrial ;28S ribosomal protein S2, mitochondrial ;39S ribosomal protein L11, mitochondrial ;28S ribosomal protein S16, mitochondrial ;28S ribosomal protein S18c, mitochondrial ;28S ribosomal protein S23, mitochondrial ;28S ribosomal protein S18b, mitochondrial ;39S ribosomal protein L42, mitochondrial","subunits.Gene.name.":"MRPS12;MRPS14;MRPL33;MRPL3;MRPL19;DAP3;MRPL12;MRPS22;MRPS25;MRPS10;MRPS35;MRPS5;MRPS36;MRPS11;MRPS15;MRPS21;MRPS34;MRPS6;MRPS9;LACTB;MRPL28;MRPL49;MRPL23;MRPL51;MRPL2;MRPL54;MRPL14;MRPL21;MRPL55;MRPL10;MRPL52;MRPL41;MRPL50;MRPL43;MRPL30;MRPS27;MRPS31;MRPL24;MRPL38;MRPS24;MRPL53;MRPL48;MRPL34;MRPL45;MRPL32;MRPL20;MRPL13;MRPL9;MRPL4;MRPL1;MRPS26;MRPL37;MRPL18;MRPL46;MRPL44;MRPL47;MRPS30;MRPL40;MRPL17;MRPS18A;MRPL22;MRPL16;MRPL39;MRPL35;MRPL15;MRPL36;MRPL27;MRPS33;MRPS28;MRPS17;MRPS7;MRPS2;MRPL11;MRPS16;MRPS18C;MRPS23;MRPS18B;MRPL42","subunits.Gene.name.syn.":"RPMS12 RPSM12;;C2orf1;MRL3 RPML3;KIAA0104 MRPL15;MRPS29;RPML12;C3orf5 RPMS22;RPMS25;;MRPS28;;;RPMS11;RPMS15;RPMS21;;C21orf101 RPMS6;RPMS9;MRPL56;MAAT1;C11orf4 NOF1;L23MRP RPL23L;MRP64;;;MRPL32 RPML32;;;MRPL8 RPML8;;BMRP MRPL27 RPML27;;;MRPL28 RPML28;KIAA0264;IMOGN38;;;;;;;;;;;;;;C20orf193 RPMS13;MRPL2 RPML2;;C15orf4 LIECG2;;NCM1;PDCD9;NLVCF URIM;LIP2;;MRPL25 RPML25;;C21orf92 MRPL5 RPML5;;;BRIP1;;;MRPS35;RPMS17;;;;RPMS16;;;C6orf14;MRPL31 MRPS32 RPML31","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":321,"ComplexName":"p27-cyclinD2-Cdk4 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P30280;P30285;P46529","subunits.Entrez.IDs.":"12444;12567;None","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0007050;GO:0050789;GO:0005634","GO.description":"cell cycle arrest;regulation of biological process;nucleus","FunCat.ID":"10.03.01.02;18;70.10","FunCat.description":"cell cycle arrest;REGULATION OF METABOLISM AND PROTEIN FUNCTION;nucleus","PubMed.ID":9325318,"subunits.Protein.name.":"G1/S-specific cyclin-D2;Cyclin-dependent kinase 4 ;Cyclin-dependent kinase inhibitor 1B","subunits.Gene.name.":"Ccnd2;Cdk4;CDKN1B","subunits.Gene.name.syn.":"Cyl-2;Crk3;","Disease.comment":"None","Subunits.comment":"Since Ccnd2 and Cdk4 from mink were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were taken.","Complex.comment":"p27 inhibits kinase activity of cyclinD2-CDK4.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Neovison vison (American mink) (Mustela vison)"}
{"ComplexID":322,"ComplexName":"DNA-PK-Ku complex","Organism":"Human","Synonyms":"DNA-PK-Ku70-Ku80 complex","Cell.line":"None","subunits.UniProt.IDs.":"P12956;P13010;P78527","subunits.Entrez.IDs.":"2547;7520;5591","Protein.complex.purification.method":"MI:0040- electron microscopy; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0009299;GO:0006468;GO:0006470;GO:0046777;GO:0003677;GO:0006464;GO:0043085;GO:0008047;GO:0005634","GO.description":"mRNA transcription;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;DNA binding;cellular protein modification process;positive regulation of catalytic activity;enzyme activator activity;nucleus","FunCat.ID":"11.02.03;14.07.03;16.03.01;14.07;18.02.01.01;70.10","FunCat.description":"mRNA synthesis;modification by phosphorylation, dephosphorylation, autophosphorylation;DNA binding;protein modification;enzyme activator;nucleus","PubMed.ID":16713581,"subunits.Protein.name.":"X-ray repair cross-complementing protein 6 ;X-ray repair cross-complementing protein 5 ;DNA-dependent protein kinase catalytic subunit","subunits.Gene.name.":"XRCC6;XRCC5;PRKDC","subunits.Gene.name.syn.":"G22P1;G22P2;HYRC HYRC1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"For assembly of the DNA-PK-Ku70-Ku80 complex presence of DNA is necessary. DNA-bound Ku directs the recruitment of the catalytic subunit DNA-Pk via a small helical domain at the C-terminus of Ku80.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":323,"ComplexName":"28S ribosomal subunit, mitochondrial","Organism":"Bovine","Synonyms":"Small ribosomal subunit, mitochondrial","Cell.line":"None","subunits.UniProt.IDs.":"P82649;P82669;P82670;P82908;P82911;P82913;P82915;P82916;P82917;P82918;P82919;P82920;P82922;P82923;P82924;P82925;P82926;P82927;P82928;P82929;P82931;Q2KID9;Q2M2T7;Q2NL27;Q2YDF6;Q32PI8;Q3SZ86;Q3T040;Q58DQ5;Q6B860","subunits.Entrez.IDs.":"532044;533011;515885;613835;509816;508928;510899;None;613561;None;614102;614343;504320;505681;516084;534185;523435;614148;535290;618357;615431;512469;None;515228;513438;514740;516004;509115;519302;445421","Protein.complex.purification.method":"MI:0028- cosedimentation in solution; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006412;GO:0005759","GO.description":"translation;mitochondrial matrix","FunCat.ID":"12.04;70.16.07","FunCat.description":"translation;mitochondrial matrix","PubMed.ID":11279123,"subunits.Protein.name.":"28S ribosomal protein S22, mitochondrial ;28S ribosomal protein S25, mitochondrial ;28S ribosomal protein S10, mitochondrial ;28S ribosomal protein S36, mitochondrial ;28S ribosomal protein S11, mitochondrial ;28S ribosomal protein S15, mitochondrial ;28S ribosomal protein S16, mitochondrial ;28S ribosomal protein S17, mitochondrial ;28S ribosomal protein S18c, mitochondrial ;28S ribosomal protein S18b, mitochondrial ;28S ribosomal protein S18a, mitochondrial ;28S ribosomal protein S21, mitochondrial ;28S ribosomal protein S29, mitochondrial ;28S ribosomal protein S2, mitochondrial ;28S ribosomal protein S30, mitochondrial ;28S ribosomal protein S31, mitochondrial ;28S ribosomal protein S33, mitochondrial ;39S ribosomal protein L42, mitochondrial ;28S ribosomal protein S28, mitochondrial ;28S ribosomal protein S34, mitochondrial ;28S ribosomal protein S6, mitochondrial ;28S ribosomal protein S5, mitochondrial ;28S ribosomal protein S24, mitochondrial ;28S ribosomal protein S23, mitochondrial ;28S ribosomal protein S35, mitochondrial ;28S ribosomal protein S27, mitochondrial ;28S ribosomal protein S26, mitochondrial ;28S ribosomal protein S7, mitochondrial ;28S ribosomal protein S9, mitochondrial ;28S ribosomal protein S14, mitochondrial","subunits.Gene.name.":"MRPS22;MRPS25;MRPS10;MRPS36;MRPS11;MRPS15;MRPS16;MRPS17;MRPS18C;MRPS18B;MRPS18A;MRPS21;DAP3;MRPS2;MRPS30;MRPS31;MRPS33;MRPL42;MRPS28;MRPS34;MRPS6;MRPS5;MRPS24;MRPS23;MRPS35;MRPS27;MRPS26;MRPS7;MRPS9;MRPS14","subunits.Gene.name.syn.":";RPMS25;;;;RPMS15;RPMS16;RPMS17;;;;RPMS21;MRPS29;;;;;MRPS32;;;RPMS6;;;;MRPS28;;;;;","Disease.comment":"None","Subunits.comment":"MRPS12 could not be identified in this study.","Complex.comment":"None","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":324,"ComplexName":"39S ribosomal subunit, mitochondrial","Organism":"Human","Synonyms":"Large ribosomal subunit, mitochondrial","Cell.line":"None","subunits.UniProt.IDs.":"O75394;P09001;P49406;P52815;P83111;Q13084;Q13405;Q16540;Q4U2R6;Q5T653;Q6P161;Q6P1L8;Q7Z2W9;Q7Z7F7;Q7Z7H8;Q86TS9;Q8IXM3;Q8N5N7;Q8N983;Q8TCC3;Q96A35;Q96DV4;Q96EL3;Q96GC5;Q9BQ48;Q9BRJ2;Q9BYC8;Q9BYC9;Q9BYD1;Q9BYD2;Q9BYD3;Q9BYD6;Q9BZE1;Q9H0U6;Q9H2W6;Q9H9J2;Q9HD33;Q9NQ50;Q9NRX2;Q9NWU5;Q9NX20;Q9NYK5;Q9NZE8;Q9P015;Q9P0J6;Q9P0M9;Q9Y3B7;Q9Y6G3","subunits.Entrez.IDs.":"9553;11222;9801;6182;114294;10573;740;6150;51258;51069;116541;64928;219927;128308;124995;122704;64975;54534;84545;51263;79590;64978;116540;51642;64981;84311;64983;55052;28998;65005;51073;65008;51253;29074;26589;65080;57129;64976;63875;29093;54948;54148;51318;29088;64979;51264;65003;28977","Protein.complex.purification.method":"MI:0363- inferred by author","GO.ID":"GO:0006412;GO:0005759","GO.description":"translation;mitochondrial matrix","FunCat.ID":"12.04;70.16.07","FunCat.description":"translation;mitochondrial matrix","PubMed.ID":14681386,"subunits.Protein.name.":"39S ribosomal protein L33, mitochondrial ;39S ribosomal protein L3, mitochondrial ;39S ribosomal protein L19, mitochondrial ;39S ribosomal protein L12, mitochondrial ;Serine beta-lactamase-like protein LACTB, mitochondrial ;39S ribosomal protein L28, mitochondrial ;39S ribosomal protein L49, mitochondrial ;39S ribosomal protein L23, mitochondrial ;39S ribosomal protein L51, mitochondrial ;39S ribosomal protein L2, mitochondrial ;39S ribosomal protein L54, mitochondrial ;39S ribosomal protein L14, mitochondrial ;39S ribosomal protein L21, mitochondrial ;39S ribosomal protein L55, mitochondrial ;39S ribosomal protein L10, mitochondrial ;39S ribosomal protein L52, mitochondrial ;39S ribosomal protein L41, mitochondrial ;39S ribosomal protein L50, mitochondrial ;39S ribosomal protein L43, mitochondrial ;39S ribosomal protein L30, mitochondrial ;39S ribosomal protein L24, mitochondrial ;39S ribosomal protein L38, mitochondrial ;39S ribosomal protein L53, mitochondrial ;39S ribosomal protein L48, mitochondrial ;39S ribosomal protein L34, mitochondrial ;39S ribosomal protein L45, mitochondrial ;39S ribosomal protein L32, mitochondrial ;39S ribosomal protein L20, mitochondrial ;39S ribosomal protein L13, mitochondrial ;39S ribosomal protein L9, mitochondrial ;39S ribosomal protein L4, mitochondrial ;39S ribosomal protein L1, mitochondrial ;39S ribosomal protein L37, mitochondrial ;39S ribosomal protein L18, mitochondrial ;39S ribosomal protein L46, mitochondrial ;39S ribosomal protein L44, mitochondrial ;39S ribosomal protein L47, mitochondrial ;39S ribosomal protein L40, mitochondrial ;39S ribosomal protein L17, mitochondrial ;39S ribosomal protein L22, mitochondrial ;39S ribosomal protein L16, mitochondrial ;39S ribosomal protein L39, mitochondrial ;39S ribosomal protein L35, mitochondrial ;39S ribosomal protein L15, mitochondrial ;39S ribosomal protein L36, mitochondrial ;39S ribosomal protein L27, mitochondrial ;39S ribosomal protein L11, mitochondrial ;39S ribosomal protein L42, mitochondrial","subunits.Gene.name.":"MRPL33;MRPL3;MRPL19;MRPL12;LACTB;MRPL28;MRPL49;MRPL23;MRPL51;MRPL2;MRPL54;MRPL14;MRPL21;MRPL55;MRPL10;MRPL52;MRPL41;MRPL50;MRPL43;MRPL30;MRPL24;MRPL38;MRPL53;MRPL48;MRPL34;MRPL45;MRPL32;MRPL20;MRPL13;MRPL9;MRPL4;MRPL1;MRPL37;MRPL18;MRPL46;MRPL44;MRPL47;MRPL40;MRPL17;MRPL22;MRPL16;MRPL39;MRPL35;MRPL15;MRPL36;MRPL27;MRPL11;MRPL42","subunits.Gene.name.syn.":"C2orf1;MRL3 RPML3;KIAA0104 MRPL15;RPML12;MRPL56;MAAT1;C11orf4 NOF1;L23MRP RPL23L;MRP64;;;MRPL32 RPML32;;;MRPL8 RPML8;;BMRP MRPL27 RPML27;;;MRPL28 RPML28;;;;;;;;;;;;;MRPL2 RPML2;;C15orf4 LIECG2;;NCM1;NLVCF URIM;LIP2;MRPL25 RPML25;;C21orf92 MRPL5 RPML5;;;BRIP1;;;MRPL31 MRPS32 RPML31","Disease.comment":"None","Subunits.comment":"At the time of annotation, about half of the bovine subunits were not found in the UniProt database.","Complex.comment":"With the exception of MRPL36 and MRPL42, all proteins of the large ribosomal subunit from ribosomes of Bos taurus were identified in a proteomic approach (PMID:11551941).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":325,"ComplexName":"Skeletal muscle sarcoglycan complex SGC, beta-gamma-delta-zeta","Organism":"Mouse","Synonyms":"None","Cell.line":"striated muscle","subunits.UniProt.IDs.":"P82347;P82348;P82349;Q8BX51","subunits.Entrez.IDs.":"24052;24053;24051;244431","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006941;GO:0007519;GO:0014706","GO.description":"striated muscle contraction;skeletal muscle tissue development;striated muscle tissue development","FunCat.ID":"36.25.09.03;41.05.15;45.03.12.01","FunCat.description":"striated muscle contraction;myogenesis;striated muscle","PubMed.ID":12189167,"subunits.Protein.name.":"Delta-sarcoglycan;Gamma-sarcoglycan;Beta-sarcoglycan;Zeta-sarcoglycan","subunits.Gene.name.":"Sgcd;Sgcg;Sgcb;Sgcz","subunits.Gene.name.syn.":"None;None;None;None","Disease.comment":"Sarcoglycan complex (SGC) is involved in muscular dystrophy and cardiomyopathy (PMID:15117830).","Subunits.comment":"None","Complex.comment":"The authors demonstrate that zeta-sarcoglycan is an integral component of the sarcoglycan complex and, as such, is important in the pathogenesis of muscular dystrophy.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":326,"ComplexName":"Smooth muscle sarcoglycan complex SGC, beta-delta-zeta","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P82347;P82349;Q8BX51","subunits.Entrez.IDs.":"24052;24051;244431","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006939;GO:0048745;GO:0005886","GO.description":"smooth muscle contraction;smooth muscle tissue development;plasma membrane","FunCat.ID":"36.25.09.01;45.03.12.02;70.02","FunCat.description":"smooth muscle contraction;smooth muscle;eukaryotic plasma membrane / membrane attached","PubMed.ID":12189167,"subunits.Protein.name.":"Delta-sarcoglycan;Beta-sarcoglycan;Zeta-sarcoglycan","subunits.Gene.name.":"Sgcd;Sgcb;Sgcz","subunits.Gene.name.syn.":"None;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors demonstrate that zeta-sarcoglycan was found as a component of the vascular smooth muscle sarcoglycan complex. They propose that vasospasm, as it occurs in sarcoglycan-deficient muscle, may not be related to disruption of the vascular smooth muscle sarcoglycan complex.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":328,"ComplexName":"Ku antigen complex","Organism":"Human","Synonyms":"Ku70-Ku80 complex; Ku complex","Cell.line":"None","subunits.UniProt.IDs.":"P12956;P13010","subunits.Entrez.IDs.":"2547;7520","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0091- chromatography technologies","GO.ID":"GO:0006281;GO:0003677;GO:0006974;GO:0005634","GO.description":"DNA repair;DNA binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;16.03.01;32.01.09;70.10","FunCat.description":"DNA repair;DNA binding;DNA damage response;nucleus","PubMed.ID":16713581,"subunits.Protein.name.":"X-ray repair cross-complementing protein 6 ;X-ray repair cross-complementing protein 5","subunits.Gene.name.":"XRCC6;XRCC5","subunits.Gene.name.syn.":"G22P1;G22P2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In the absence of added DNA Ku70-Ku80 copurify without DNA-PKcs.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":329,"ComplexName":"Skeletal muscle sarcoglycan complex SGC, alpha-beta-gamma-delta","Organism":"Mouse","Synonyms":"None","Cell.line":"striated muscle","subunits.UniProt.IDs.":"P82347;P82348;P82349;P82350","subunits.Entrez.IDs.":"24052;24053;24051;20391","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006941;GO:0007519;GO:0014706;GO:0005886","GO.description":"striated muscle contraction;skeletal muscle tissue development;striated muscle tissue development;plasma membrane","FunCat.ID":"36.25.09.03;41.05.15;45.03.12.01;70.02","FunCat.description":"striated muscle contraction;myogenesis;striated muscle;eukaryotic plasma membrane / membrane attached","PubMed.ID":10862711,"subunits.Protein.name.":"Delta-sarcoglycan;Gamma-sarcoglycan;Beta-sarcoglycan;Alpha-sarcoglycan","subunits.Gene.name.":"Sgcd;Sgcg;Sgcb;Sgca","subunits.Gene.name.syn.":"None;None;None;None","Disease.comment":"Sarcoglycan complex (SGC) is involved in muscular dystrophy and cardiomyopathy (PMID:15117830).","Subunits.comment":"None","Complex.comment":"The authors show that mice lacking delta-sarcoglycan developed muscular dystrophy and cardiomyopathy similar to mice lacking gamma-sarcoglycan.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":330,"ComplexName":"PSF-p54(nrb) complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P23246;Q15233","subunits.Entrez.IDs.":"6421;4841","Protein.complex.purification.method":"MI:0091- chromatography technologies","GO.ID":"GO:0006281;GO:0005515;GO:0003677;GO:0006974;GO:0005634","GO.description":"DNA repair;protein binding;DNA binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;16.01;16.03.01;32.01.09;70.10","FunCat.description":"DNA repair;protein binding;DNA binding;DNA damage response;nucleus","PubMed.ID":15590677,"subunits.Protein.name.":"Splicing factor, proline- and glutamine-rich ;Non-POU domain-containing octamer-binding protein","subunits.Gene.name.":"SFPQ;NONO","subunits.Gene.name.syn.":"PSF;NRB54","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"PSF-p54(nrb) complex probably works as a dimeric complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":331,"ComplexName":"MRN complex (MRE11-RAD50-NBN complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60934;P49959;Q92878","subunits.Entrez.IDs.":"4683;4361;10111","Protein.complex.purification.method":"MI:0091- chromatography technologies","GO.ID":"GO:0006308;GO:0006281;GO:0000075;GO:0003677;GO:0006974;GO:0005634","GO.description":"DNA catabolic process;DNA repair;cell cycle checkpoint;DNA binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"01.03.16.03;10.01.05.01;10.03.01.03;16.03.01;32.01.09;70.10","FunCat.description":"DNA degradation;DNA repair;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA binding;DNA damage response;nucleus","PubMed.ID":12917393,"subunits.Protein.name.":"Nibrin ;Double-strand break repair protein MRE11A ;DNA repair protein RAD50","subunits.Gene.name.":"NBN;MRE11A;RAD50","subunits.Gene.name.syn.":"NBS NBS1 P95;HNGS1 MRE11;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":332,"ComplexName":"Skeletal muscle sarcoglycan complex SGC, alpha-beta-epsilon-gamma","Organism":"Mouse","Synonyms":"None","Cell.line":"striated muscle","subunits.UniProt.IDs.":"O70258;P82348;P82349;P82350","subunits.Entrez.IDs.":"20392;24053;24051;20391","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006941;GO:0007519;GO:0014706;GO:0005886","GO.description":"striated muscle contraction;skeletal muscle tissue development;striated muscle tissue development;plasma membrane","FunCat.ID":"36.25.09.03;41.05.15;45.03.12.01;70.02","FunCat.description":"striated muscle contraction;myogenesis;striated muscle;eukaryotic plasma membrane / membrane attached","PubMed.ID":10608889,"subunits.Protein.name.":"Epsilon-sarcoglycan;Gamma-sarcoglycan;Beta-sarcoglycan;Alpha-sarcoglycan","subunits.Gene.name.":"Sgce;Sgcg;Sgcb;Sgca","subunits.Gene.name.syn.":"None;None;None;None","Disease.comment":"Sarcoglycan complex (SGC) is involved in muscular dystrophy and cardiomyopathy (PMID:15117830).","Subunits.comment":"None","Complex.comment":"Mutations in any of the four genes encoding sarcoglycans cause a deficiency in all sarcoglycans in the sarcolemma and produce one of four types of limb-girdle muscular dystrophy.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":333,"ComplexName":"Skeletal muscle sarcoglycan complex SGC, alpha-beta-gamma-delta","Organism":"Mouse","Synonyms":"None","Cell.line":"striated muscle","subunits.UniProt.IDs.":"P82347;P82348;P82349;P82350","subunits.Entrez.IDs.":"24052;24053;24051;20391","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006941;GO:0007519;GO:0014706;GO:0005886","GO.description":"striated muscle contraction;skeletal muscle tissue development;striated muscle tissue development;plasma membrane","FunCat.ID":"36.25.09.03;41.05.15;45.03.12.01;70.02","FunCat.description":"striated muscle contraction;myogenesis;striated muscle;eukaryotic plasma membrane / membrane attached","PubMed.ID":10608889,"subunits.Protein.name.":"Delta-sarcoglycan;Gamma-sarcoglycan;Beta-sarcoglycan;Alpha-sarcoglycan","subunits.Gene.name.":"Sgcd;Sgcg;Sgcb;Sgca","subunits.Gene.name.syn.":"None;None;None;None","Disease.comment":"Sarcoglycan complex (SGC) is involved in muscular dystrophy and cardiomyopathy (PMID:15117830).","Subunits.comment":"None","Complex.comment":"Complex also isolated in C2C12 cells; epsilon-sarcoglycan was undetectable in anti-alpha-sarcoglycan isolates and vice versa. Mutations in any of the four genes encoding sarcoglycans cause a deficiency in all sarcoglycans in the sarcolemma and produce one of four types of limb-girdle muscular dystrophy.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":334,"ComplexName":"Skeletal muscle sarcoglycan complex SGC, epsilon-beta-gamma-delta","Organism":"Mouse","Synonyms":"None","Cell.line":"striated muscle","subunits.UniProt.IDs.":"O70258;P82347;P82348;P82349","subunits.Entrez.IDs.":"20392;24052;24053;24051","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006941;GO:0007519;GO:0014706;GO:0005886","GO.description":"striated muscle contraction;skeletal muscle tissue development;striated muscle tissue development;plasma membrane","FunCat.ID":"36.25.09.03;41.05.15;45.03.12.01;70.02","FunCat.description":"striated muscle contraction;myogenesis;striated muscle;eukaryotic plasma membrane / membrane attached","PubMed.ID":10608889,"subunits.Protein.name.":"Epsilon-sarcoglycan;Delta-sarcoglycan;Gamma-sarcoglycan;Beta-sarcoglycan","subunits.Gene.name.":"Sgce;Sgcd;Sgcg;Sgcb","subunits.Gene.name.syn.":"None;None;None;None","Disease.comment":"Sarcoglycan complex (SGC) is involved in muscular dystrophy and cardiomyopathy (PMID:15117830).","Subunits.comment":"None","Complex.comment":"Complex also isolated in C2C12 cells; epsilon-sarcoglycan was undetectable in anti-alpha-sarcoglycan isolates and vice versa. Mutations in any of the four genes encoding sarcoglycans cause a deficiency in all sarcoglycans in the sarcolemma and produce one of four types of limb-girdle muscular dystrophy.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":335,"ComplexName":"p54(nrb)-PSF-matrin3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P23246;P43243;Q15233","subunits.Entrez.IDs.":"6421;9782;4841","Protein.complex.purification.method":"MI:0030- cross-linking studies","GO.ID":"GO:0003723;GO:0050658;GO:0051033;GO:0005634","GO.description":"RNA binding;RNA transport;RNA transmembrane transporter activity;nucleus","FunCat.ID":"16.03.03;20.01.21;70.10","FunCat.description":"RNA binding;RNA transport;nucleus","PubMed.ID":11525732,"subunits.Protein.name.":"Splicing factor, proline- and glutamine-rich ;Matrin-3;Non-POU domain-containing octamer-binding protein","subunits.Gene.name.":"SFPQ;MATR3;NONO","subunits.Gene.name.syn.":"PSF;KIAA0723;NRB54","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex binds specifically to inosine-containing RNAs and anchors hyperedited RNAs to the nuclear matrix.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":336,"ComplexName":"DNA ligase IV-XRCC4-AHNK complex","Organism":"Human","Synonyms":"AHNAK-LX complex","Cell.line":"None","subunits.UniProt.IDs.":"P49917;Q09666;Q13426","subunits.Entrez.IDs.":"3981;79026;7518","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0006312;GO:0003677;GO:0005634","GO.description":"DNA repair;mitotic recombination;DNA binding;nucleus","FunCat.ID":"10.01.05.01;10.01.05.03.03;16.03.01;70.10","FunCat.description":"DNA repair;somatic / mitotic recombination;DNA binding;nucleus","PubMed.ID":15177040,"subunits.Protein.name.":"DNA ligase 4 ;Neuroblast differentiation-associated protein AHNAK ;DNA repair protein XRCC4","subunits.Gene.name.":"LIG4;AHNAK;XRCC4","subunits.Gene.name.syn.":";PM227;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"AHNAK stimulates the double-stranded ligation activity of DNA ligase IV-XRCC4 complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":337,"ComplexName":"Dystrophin-sarcoglycan-syntrophin complex, skeletal muscle","Organism":"Mouse","Synonyms":"None","Cell.line":"striated muscle","subunits.UniProt.IDs.":"P11531;P82347;P82348;P82349;P82350;Q61234","subunits.Entrez.IDs.":"13405;24052;24053;24051;20391;20648","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006941;GO:0007519;GO:0014706;GO:0005886","GO.description":"striated muscle contraction;skeletal muscle tissue development;striated muscle tissue development;plasma membrane","FunCat.ID":"36.25.09.03;41.05.15;45.03.12.01;70.02","FunCat.description":"striated muscle contraction;myogenesis;striated muscle;eukaryotic plasma membrane / membrane attached","PubMed.ID":9864373,"subunits.Protein.name.":"Dystrophin;Delta-sarcoglycan;Gamma-sarcoglycan;Beta-sarcoglycan;Alpha-sarcoglycan;Alpha-1-syntrophin","subunits.Gene.name.":"Dmd;Sgcd;Sgcg;Sgcb;Sgca;Snta1","subunits.Gene.name.syn.":"None;None;None;None;None;Snt1","Disease.comment":"DMD, SGCB, SGCG and SGCD are involved in muscular dystrophy  and cardiomyopathy (PMID:15117830).","Subunits.comment":"Since the authors did not specify syntrophin, we used Snta1.","Complex.comment":"The authors show  that delta -sarcoglycan can be cross-linked to the dystroglycan complex and of the four sarcoglycans, only beta -, gamma -, and delta -sarcoglycan contain intramolecular disulfide bonds.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":338,"ComplexName":"40S ribosomal subunit, cytoplasmic","Organism":"Human","Synonyms":"small ribosomal subunit, cytoplasmic","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"P08708;P08865;P15880;P23396;P25398;P39019;P46781;P46782;P46783;P60866;P61247;P62081;P62241;P62244;P62249;P62263;P62266;P62269;P62273;P62277;P62280;P62701;P62753;P62841;P62847;P62851;P62854;P62857;P62861;P62979;P63220","subunits.Entrez.IDs.":"6218;3921;6187;6188;6206;6223;6203;6193;6204;6224;6189;6201;6202;6210;6217;6208;6228;6222;6235;6207;6205;6191;6194;6209;6229;6230;6231;6234;2197;6233;6227","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0004- affinity chromatography technologies","GO.ID":"GO:0006412;GO:0005737","GO.description":"translation;cytoplasm","FunCat.ID":"12.04;70.03","FunCat.description":"translation;cytoplasm","PubMed.ID":15883184,"subunits.Protein.name.":"40S ribosomal protein S17;40S ribosomal protein SA;40S ribosomal protein S2;40S ribosomal protein S3;40S ribosomal protein S12;40S ribosomal protein S19;40S ribosomal protein S9;40S ribosomal protein S5 [Cleaved into: 40S ribosomal protein S5, N-terminally processed];40S ribosomal protein S10;40S ribosomal protein S20;40S ribosomal protein S3a;40S ribosomal protein S7;40S ribosomal protein S8;40S ribosomal protein S15a;40S ribosomal protein S16;40S ribosomal protein S14;40S ribosomal protein S23;40S ribosomal protein S18;40S ribosomal protein S29;40S ribosomal protein S13;40S ribosomal protein S11;40S ribosomal protein S4, X isoform;40S ribosomal protein S6;40S ribosomal protein S15;40S ribosomal protein S24;40S ribosomal protein S25;40S ribosomal protein S26;40S ribosomal protein S28;40S ribosomal protein S30;Ubiquitin-40S ribosomal protein S27a;40S ribosomal protein S21","subunits.Gene.name.":"RPS17;RPSA;RPS2;RPS3;RPS12;RPS19;RPS9;RPS5;RPS10;RPS20;RPS3A;RPS7;RPS8;RPS15A;RPS16;RPS14;RPS23;RPS18;RPS29;RPS13;RPS11;RPS4X;RPS6;RPS15;RPS24;RPS25;RPS26;RPS28;FAU;RPS27A;RPS21","subunits.Gene.name.syn.":"RPS17L;LAMBR LAMR1;RPS4;None;None;None;None;None;None;None;FTE1 MFTL;None;None;None;None;None;None;D6S218E;None;None;None;CCG2 RPS4 SCAR;None;RIG;None;None;None;None;None;UBA80 UBCEP1;None","Disease.comment":"None","Subunits.comment":"RPS27 was not detected in this study. RPS4Y1 and RPSY2 could not be detected, since HeLa cells were used, which contain no Y chromosome.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":339,"ComplexName":"Smooth muscle dystroglycan complex","Organism":"Rabbit","Synonyms":"None","Cell.line":"lung","subunits.UniProt.IDs.":"O08614;O70258;P82347;P82352;Q28635;Q28646;Q28685","subunits.Entrez.IDs.":"22288;20392;24052;100008714;100009208;100009214;100009278","Protein.complex.purification.method":"MI:0029-cosedimentation through density gradients","GO.ID":"GO:0006939;GO:0048745;GO:0005886","GO.description":"smooth muscle contraction;smooth muscle tissue development;plasma membrane","FunCat.ID":"36.25.09.01;45.03.12.02;70.02","FunCat.description":"smooth muscle contraction;smooth muscle;eukaryotic plasma membrane / membrane attached","PubMed.ID":10473626,"subunits.Protein.name.":"Cytoskeletal protein;Epsilon-sarcoglycan;Delta-sarcoglycan;Sarcospan;Beta-sarcoglycan;Gamma-sarcoglycan;Dystroglycan","subunits.Gene.name.":"Utrn;Sgce;Sgcd;SSPN;SGCB;SGCG;DAG1","subunits.Gene.name.syn.":"utrophin;None;None;None;None;None;None","Disease.comment":"DAG1, SGCB, SGCG and SGCD are involved in muscular dystrophy (Duchenne muscular dystrophy DMD, the milder Becker muscular dystrophy BMD) and cardiomyopathy (PMID:15117830).","Subunits.comment":"Since Sgce, Sgcd and Utrn from rabbit were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.","Complex.comment":"The authors demonstrate that the presence of the sarcoglycans and sarcospan in lung reflects association with dystroglycan in the smooth muscle within lung, and they show that epithelial dystroglycan is not associated with any of the known sarcoglycans and can be separated from the smooth muscle dystroglycan complex.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Oryctolagus cuniculus (Rabbit);Oryctolagus cuniculus (Rabbit);Oryctolagus cuniculus (Rabbit);Oryctolagus cuniculus (Rabbit)"}
{"ComplexID":340,"ComplexName":"Dystrophin-glycoprotein complex DGC, skeletal muscle","Organism":"Rabbit","Synonyms":"None","Cell.line":"striated muscle","subunits.UniProt.IDs.":"P11531;P82347;P82352;Q28626;Q28635;Q28646;Q28685;Q28686","subunits.Entrez.IDs.":"13405;24052;100008714;100009179;100009208;100009214;100009278;100009178","Protein.complex.purification.method":"MI:0226-ion exchange chromatography","GO.ID":"GO:0006941;GO:0007519;GO:0014706;GO:0005886","GO.description":"striated muscle contraction;skeletal muscle tissue development;striated muscle tissue development;plasma membrane","FunCat.ID":"36.25.09.03;41.05.15;45.03.12.01;70.02","FunCat.description":"striated muscle contraction;myogenesis;striated muscle;eukaryotic plasma membrane / membrane attached","PubMed.ID":9395445,"subunits.Protein.name.":"Dystrophin;Delta-sarcoglycan;Sarcospan;Alpha-1-syntrophin;Beta-sarcoglycan;Gamma-sarcoglycan;Dystroglycan;Alpha-sarcoglycan","subunits.Gene.name.":"Dmd;Sgcd;SSPN;SNTA1;SGCB;SGCG;DAG1;SGCA","subunits.Gene.name.syn.":"None;None;None;SNT1;None;None;None;ADL DAG2","Disease.comment":"DGC complex is involved in several forms of muscular dystrophy (Duchenne muscular dystrophy DMD, the milder Becker muscular dystrophy BMD) and cardiomyopathy (PMID:15117830).","Subunits.comment":"Since Sgcd and Dmd from rabbit were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.","Complex.comment":"These proteins provide a physical connection between the extracellular matrix and the intracellular cytoskeleton of muscle cells.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Oryctolagus cuniculus (Rabbit);Oryctolagus cuniculus (Rabbit);Oryctolagus cuniculus (Rabbit);Oryctolagus cuniculus (Rabbit);Oryctolagus cuniculus (Rabbit);Oryctolagus cuniculus (Rabbit)"}
{"ComplexID":341,"ComplexName":"Dystrophin-glycoprotein complex DGC, skeletal muscle","Organism":"Rabbit","Synonyms":"None","Cell.line":"striated muscle","subunits.UniProt.IDs.":"P11531;P82347;P82352;Q28635;Q28646;Q28685;Q28686","subunits.Entrez.IDs.":"13405;24052;100008714;100009208;100009214;100009278;100009178","Protein.complex.purification.method":"MI:0029-cosedimentation through density gradients","GO.ID":"GO:0006941;GO:0007519;GO:0014706;GO:0005886","GO.description":"striated muscle contraction;skeletal muscle tissue development;striated muscle tissue development;plasma membrane","FunCat.ID":"36.25.09.03;41.05.15;45.03.12.01;70.02","FunCat.description":"striated muscle contraction;myogenesis;striated muscle;eukaryotic plasma membrane / membrane attached","PubMed.ID":10189375,"subunits.Protein.name.":"Dystrophin;Delta-sarcoglycan;Sarcospan;Beta-sarcoglycan;Gamma-sarcoglycan;Dystroglycan;Alpha-sarcoglycan","subunits.Gene.name.":"Dmd;Sgcd;SSPN;SGCB;SGCG;DAG1;SGCA","subunits.Gene.name.syn.":"None;None;None;None;None;None;ADL DAG2","Disease.comment":"DMD, DAG1, SGCB, SGCG and SGCD are involved in muscular dystrophy (Duchenne muscular dystrophy DMD, the milder Becker muscular dystrophy BMD)  and cardiomyopathy (PMID:15117830).","Subunits.comment":"Since Sgcd and Dmd from rabbit were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Oryctolagus cuniculus (Rabbit);Oryctolagus cuniculus (Rabbit);Oryctolagus cuniculus (Rabbit);Oryctolagus cuniculus (Rabbit);Oryctolagus cuniculus (Rabbit)"}
{"ComplexID":342,"ComplexName":"Skeletal muscle sarcoglycan-sarcospan complex SG-SPN","Organism":"Rabbit","Synonyms":"None","Cell.line":"striated muscle","subunits.UniProt.IDs.":"P82347;P82352;Q28635;Q28646;Q28686","subunits.Entrez.IDs.":"24052;100008714;100009208;100009214;100009178","Protein.complex.purification.method":"MI:0029-cosedimentation through density gradients","GO.ID":"GO:0006941;GO:0007519;GO:0014706;GO:0005886","GO.description":"striated muscle contraction;skeletal muscle tissue development;striated muscle tissue development;plasma membrane","FunCat.ID":"36.25.09.03;41.05.15;45.03.12.01;70.02","FunCat.description":"striated muscle contraction;myogenesis;striated muscle;eukaryotic plasma membrane / membrane attached","PubMed.ID":10189375,"subunits.Protein.name.":"Delta-sarcoglycan;Sarcospan;Beta-sarcoglycan;Gamma-sarcoglycan;Alpha-sarcoglycan","subunits.Gene.name.":"Sgcd;SSPN;SGCB;SGCG;SGCA","subunits.Gene.name.syn.":"None;None;None;None;ADL DAG2","Disease.comment":"SGCB, SGCG and SGCD are involved in muscular dystrophy and cardiomyopathy (PMID:15117830).","Subunits.comment":"Since Sgcd from rabbit was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"The authors demonstrate that assembly of the SG subcomplex is a prerequisite for targeting SPN to the sarcolemma and that the SG- SPN subcomplex functions to stabilize alpha -dystroglycan to the muscle plasma membrane.","SWISSPROT.organism":"Mus musculus (Mouse);Oryctolagus cuniculus (Rabbit);Oryctolagus cuniculus (Rabbit);Oryctolagus cuniculus (Rabbit);Oryctolagus cuniculus (Rabbit)"}
{"ComplexID":343,"ComplexName":"Sarcoglycan-sarcospan complex SG-SPN","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q13326;Q14714;Q16585;Q16586;Q92629","subunits.Entrez.IDs.":"6445;8082;6443;6442;6444","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006941;GO:0007517;GO:0005886","GO.description":"striated muscle contraction;muscle organ development;plasma membrane","FunCat.ID":"36.25.09.03;45.03.12;70.02","FunCat.description":"striated muscle contraction;muscle;eukaryotic plasma membrane / membrane attached","PubMed.ID":10189375,"subunits.Protein.name.":"Gamma-sarcoglycan ;Sarcospan ;Beta-sarcoglycan ;Alpha-sarcoglycan ;Delta-sarcoglycan","subunits.Gene.name.":"SGCG;SSPN;SGCB;SGCA;SGCD","subunits.Gene.name.syn.":";KRAG;;ADL DAG2;","Disease.comment":"SGCB, SGCG and SGCD are involved in muscular dystrophy and cardiomyopathy (PMID:15117830).","Subunits.comment":"None","Complex.comment":"The authors demonstrate that assembly of the SG subcomplex is a prerequisite for targeting SPN to the sarcolemma and that the SG- SPN subcomplex functions to stabilize alpha -dystroglycan to the muscle plasma membrane.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":344,"ComplexName":"DNA ligase IV-XRCC4 complex (LX complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P49917;Q13426","subunits.Entrez.IDs.":"3981;7518","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0006281;GO:0006312;GO:0003677;GO:0005634","GO.description":"DNA repair;mitotic recombination;DNA binding;nucleus","FunCat.ID":"10.01.05.01;10.01.05.03.03;16.03.01;70.10","FunCat.description":"DNA repair;somatic / mitotic recombination;DNA binding;nucleus","PubMed.ID":11702069,"subunits.Protein.name.":"DNA ligase 4 ;DNA repair protein XRCC4","subunits.Gene.name.":"LIG4;XRCC4","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":345,"ComplexName":"DNA ligase IV-XRCC4 complex (LX complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P49917;Q13426","subunits.Entrez.IDs.":"3981;7518","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006281;GO:0006312;GO:0003677;GO:0005694","GO.description":"DNA repair;mitotic recombination;DNA binding;chromosome","FunCat.ID":"10.01.05.01;10.01.05.03.03;16.03.01;70.10.03","FunCat.description":"DNA repair;somatic / mitotic recombination;DNA binding;chromosome","PubMed.ID":9242410,"subunits.Protein.name.":"DNA ligase 4 ;DNA repair protein XRCC4","subunits.Gene.name.":"LIG4;XRCC4","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":346,"ComplexName":"Sarcoglycan-sarcospan-dystroglycan complex","Organism":"Mouse","Synonyms":"None","Cell.line":"muscle","subunits.UniProt.IDs.":"P82347;P82348;P82349;P82350;Q62147;Q62165","subunits.Entrez.IDs.":"24052;24053;24051;20391;16651;13138","Protein.complex.purification.method":"MI:0091- chromatography technologies","GO.ID":"GO:0006936;GO:0007517","GO.description":"muscle contraction;muscle organ development","FunCat.ID":"36.25.09;45.03.12","FunCat.description":"muscle contraction;muscle","PubMed.ID":10767327,"subunits.Protein.name.":"Delta-sarcoglycan;Gamma-sarcoglycan;Beta-sarcoglycan;Alpha-sarcoglycan;Sarcospan;Dystroglycan","subunits.Gene.name.":"Sgcd;Sgcg;Sgcb;Sgca;Sspn;Dag1","subunits.Gene.name.syn.":"None;None;None;None;Krag;Dag-1","Disease.comment":"Sarcoglycan complex (SGC) is involved in muscular dystrophy and cardiomyopathy (PMID:15117830).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":347,"ComplexName":"Sarcoglycan-sarcospan-complex SG-SPN","Organism":"Mouse","Synonyms":"None","Cell.line":"muscle","subunits.UniProt.IDs.":"P82347;P82348;P82349;P82350;Q62147","subunits.Entrez.IDs.":"24052;24053;24051;20391;16651","Protein.complex.purification.method":"MI:0091- chromatography technologies","GO.ID":"GO:0006936;GO:0007517;GO:0005886","GO.description":"muscle contraction;muscle organ development;plasma membrane","FunCat.ID":"36.25.09;45.03.12;70.02","FunCat.description":"muscle contraction;muscle;eukaryotic plasma membrane / membrane attached","PubMed.ID":10767327,"subunits.Protein.name.":"Delta-sarcoglycan;Gamma-sarcoglycan;Beta-sarcoglycan;Alpha-sarcoglycan;Sarcospan","subunits.Gene.name.":"Sgcd;Sgcg;Sgcb;Sgca;Sspn","subunits.Gene.name.syn.":"None;None;None;None;Krag","Disease.comment":"Sarcoglycan complex (SGC) is involved in muscular dystrophy and cardiomyopathy (PMID:15117830).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":348,"ComplexName":"DNA ligase IV-XRCC4 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P49917;Q13426","subunits.Entrez.IDs.":"3981;7518","Protein.complex.purification.method":"MI:0404- comigration in non denaturing gel electrophoresis; MI:0007- anti tag coimmunoprecipitation; MI:0030- cross-linking studies; MI:0071- molecular sieving","GO.ID":"GO:0006281;GO:0006312;GO:0003677;GO:0005634","GO.description":"DNA repair;mitotic recombination;DNA binding;nucleus","FunCat.ID":"10.01.05.01;10.01.05.03.03;16.03.01;70.10","FunCat.description":"DNA repair;somatic / mitotic recombination;DNA binding;nucleus","PubMed.ID":10945980,"subunits.Protein.name.":"DNA ligase 4 ;DNA repair protein XRCC4","subunits.Gene.name.":"LIG4;XRCC4","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cross-linking experiments suggest that an XRCC4\\u00b7XRCC4 dimer interface forms the core of the tetramer, and that the DNL IV polypeptides are in contact with XRCC4 but not with one another.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":349,"ComplexName":"Sarcoglycan-sarcospan-syntrophin-dystrobrevin complex","Organism":"Mouse","Synonyms":"None","Cell.line":"muscle","subunits.UniProt.IDs.":"P82347;P82348;P82349;P82350;Q61234;Q62147;Q99L88;Q9D2N4","subunits.Entrez.IDs.":"24052;24053;24051;20391;20648;16651;20649;13527","Protein.complex.purification.method":"MI:0091-chromatography technologies;MI:0019-coimmunoprecipitation","GO.ID":"GO:0006936;GO:0007517;GO:0005886","GO.description":"muscle contraction;muscle organ development;plasma membrane","FunCat.ID":"36.25.09;45.03.12;70.02","FunCat.description":"muscle contraction;muscle;eukaryotic plasma membrane / membrane attached","PubMed.ID":10767327,"subunits.Protein.name.":"Delta-sarcoglycan;Gamma-sarcoglycan;Beta-sarcoglycan;Alpha-sarcoglycan;Alpha-1-syntrophin;Sarcospan;Beta-1-syntrophin;Dystrobrevin alpha","subunits.Gene.name.":"Sgcd;Sgcg;Sgcb;Sgca;Snta1;Sspn;Sntb1;Dtna","subunits.Gene.name.syn.":"None;None;None;None;Snt1;Krag;Snt2b1;Dtn","Disease.comment":"Sarcoglycan complex (SGC) is involved in muscular dystrophy and cardiomyopathy (PMID:15117830).","Subunits.comment":"None","Complex.comment":"The authors consider that the sarcoglycan-sarcospan complex is linked to the signaling protein neuronal nitric oxide synthase via alpha-syntrophin associated with dystrobrevin.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":350,"ComplexName":"DNA ligase IV-XRCC4-PNK complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P49917;Q13426;Q96T60","subunits.Entrez.IDs.":"3981;7518;11284","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006281;GO:0005694","GO.description":"DNA repair;chromosome","FunCat.ID":"10.01.05.01;70.10.03","FunCat.description":"DNA repair;chromosome","PubMed.ID":15385968,"subunits.Protein.name.":"DNA ligase 4 ;DNA repair protein XRCC4 ;Bifunctional polynucleotide phosphatase/kinase","subunits.Gene.name.":"LIG4;XRCC4;PNKP","subunits.Gene.name.syn.":";;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Interaction of PNK with XRCC4 is dependent on the phosphothreonine-binding activity of the FHA domain.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":351,"ComplexName":"Spliceosome","Organism":"Human","Synonyms":"U2-type spliceosome","Cell.line":"None","subunits.UniProt.IDs.":"O00425;O00571;O14776;O15042;O15355;O43143;O43172;O43290;O43395;O43447;O43660;O43670;O43719;O43809;O60231;O60306;O60508;O75400;O75533;O75643;O75934;O75937;O75940;O94906;O95232;O95391;O95400;O95926;P08579;P08621;P09012;P09234;P09661;P11940;P14678;P17844;P26368;P38919;P41223;P42285;P49756;P52298;P55081;P55769;P61326;P62304;P62306;P62308;P62310;P62312;P62314;P62316;P62318;P62995;P83876;P84103;Q01081;Q01130;Q05519;Q07955;Q08170;Q08211;Q09161;Q12874;Q13123;Q13242;Q13243;Q13247;Q13356;Q13435;Q13523;Q13573;Q13769;Q13838;Q14011;Q14498;Q14562;Q15007;Q15029;Q15287;Q15393;Q15427;Q15428;Q15459;Q15637;Q16629;Q16630;Q2TAY7;Q4ZG51;Q53GS9;Q69YN4;Q6I9Y2;Q6P2Q9;Q7L014;Q86V81;Q86W42;Q8IYB3;Q8NI27;Q8WUQ7;Q8WVK2;Q8WWY3;Q8WYA6;Q92620;Q92841;Q96BP3;Q96DF8;Q96DI7;Q96FV9;Q96I25;Q96J01;Q96T37;Q96T58;Q99459;Q99633;Q9BQ61;Q9BRD0;Q9BUQ8;Q9BXP5;Q9BZJ0;Q9H2H8;Q9HCE1;Q9HCG8;Q9HCS7;Q9NW64;Q9NYV4;Q9P013;Q9UBB9;Q9UHX1;Q9UJV9;Q9UK45;Q9UKV3;Q9ULR0;Q9UMS4;Q9UNP9;Q9UQ35;Q9Y2W2;Q9Y333;Q9Y3B4;Q9Y3C6;Q9Y4Z0;Q9Y5B6;Q9Y5S9;Q9Y6A4","subunits.Entrez.IDs.":"10643;1654;10915;23350;5496;1665;9128;9092;9129;10465;5356;7756;27336;11051;8449;9716;51362;55660;23451;23020;10286;22826;10285;24148;51747;10569;10421;25949;6629;6625;6626;6631;6627;26986;6628;1655;11338;9775;8896;23517;58517;22916;4236;4809;4116;6635;6636;6637;27258;11157;6632;6633;6634;6434;10907;6428;7307;6427;9295;6426;6429;1660;4686;10946;3550;8683;6430;6431;23759;10992;8899;22938;8563;7919;1153;9584;1659;9589;9343;10921;23450;10262;8175;10291;7536;6432;11052;55234;55660;10713;25962;80145;10594;9879;10189;79228;10250;57187;58509;11017;26121;56259;9785;10521;23398;8220;9410;9984;84991;84321;64783;23013;988;8559;79002;84811;9416;51593;51340;53938;4343;57703;56949;55696;51755;51503;None;22827;51428;51690;22985;57461;27339;10450;23524;51729;57819;51639;51645;25804;94104;9939;29105","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation; MI:0071- molecular sieving; MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0008380;GO:0003723;GO:0005634","GO.description":"RNA splicing;RNA binding;nucleus","FunCat.ID":"11.04.03.01;16.03.03;70.10","FunCat.description":"splicing;RNA binding;nucleus","PubMed.ID":12226669,"subunits.Protein.name.":"Insulin-like growth factor 2 mRNA-binding protein 3 ;ATP-dependent RNA helicase DDX3X ;Transcription elongation regulator 1 ;U2 snRNP-associated SURP motif-containing protein ;Protein phosphatase 1G ;Pre-mRNA-splicing factor ATP-dependent RNA helicase DHX15 ;U4/U6 small nuclear ribonucleoprotein Prp4 ;U4/U6.U5 tri-snRNP-associated protein 1 ;U4/U6 small nuclear ribonucleoprotein Prp3 ;Peptidyl-prolyl cis-trans isomerase H ;Pleiotropic regulator 1;BUB3-interacting and GLEBS motif-containing protein ZNF207 ;HIV Tat-specific factor 1 ;Cleavage and polyadenylation specificity factor subunit 5 ;Putative pre-mRNA-splicing factor ATP-dependent RNA helicase DHX16 ;Intron-binding protein aquarius ;Pre-mRNA-processing factor 17 ;Pre-mRNA-processing factor 40 homolog A ;Splicing factor 3B subunit 1 ;U5 small nuclear ribonucleoprotein 200 kDa helicase ;Pre-mRNA-splicing factor SPF27 ;DnaJ homolog subfamily C member 8 ;Survival of motor neuron-related-splicing factor 30 ;Pre-mRNA-processing factor 6 ;Luc7-like protein 3 ;Pre-mRNA-splicing factor SLU7 ;CD2 antigen cytoplasmic tail-binding protein 2 ;Pre-mRNA-splicing factor SYF2 ;U2 small nuclear ribonucleoprotein B'' ;U1 small nuclear ribonucleoprotein 70 kDa ;U1 small nuclear ribonucleoprotein A ;U1 small nuclear ribonucleoprotein C ;U2 small nuclear ribonucleoprotein A' ;Polyadenylate-binding protein 1;Small nuclear ribonucleoprotein-associated proteins B and B' ;Probable ATP-dependent RNA helicase DDX5 ;Splicing factor U2AF 65 kDa subunit ;Eukaryotic initiation factor 4A-III;Protein BUD31 homolog ;Superkiller viralicidic activity 2-like 2 ;RNA-binding protein 25 ;Nuclear cap-binding protein subunit 2;Microfibrillar-associated protein 1;NHP2-like protein 1 ;Protein mago nashi homolog;Small nuclear ribonucleoprotein E ;Small nuclear ribonucleoprotein F ;Small nuclear ribonucleoprotein G ;U6 snRNA-associated Sm-like protein LSm3;U6 snRNA-associated Sm-like protein LSm6;Small nuclear ribonucleoprotein Sm D1 ;Small nuclear ribonucleoprotein Sm D2 ;Small nuclear ribonucleoprotein Sm D3 ;Transformer-2 protein homolog beta;Thioredoxin-like protein 4A ;Serine/arginine-rich splicing factor 3 ;Splicing factor U2AF 35 kDa subunit ;Serine/arginine-rich splicing factor 2 ;Serine/arginine-rich splicing factor 11 ;Serine/arginine-rich splicing factor 1 ;Serine/arginine-rich splicing factor 4 ;ATP-dependent RNA helicase A ;Nuclear cap-binding protein subunit 1;Splicing factor 3A subunit 3 ;Protein Red ;Serine/arginine-rich splicing factor 9;Serine/arginine-rich splicing factor 5 ;Serine/arginine-rich splicing factor 6;Peptidyl-prolyl cis-trans isomerase-like 2 ;Splicing factor 3B subunit 2 ;Serine/threonine-protein kinase PRP4 homolog ;SNW domain-containing protein 1 ;THO complex subunit 5 homolog;Spliceosome RNA helicase DDX39B ;Cold-inducible RNA-binding protein ;RNA-binding protein 39 ;ATP-dependent RNA helicase DHX8 ;Pre-mRNA-splicing regulator WTAP ;116 kDa U5 small nuclear ribonucleoprotein component ;RNA-binding protein with serine-rich domain 1 ;Splicing factor 3B subunit 3;Splicing factor 3B subunit 4 ;Splicing factor 3A subunit 2 ;Splicing factor 3A subunit 1 ;Splicing factor 1 ;Serine/arginine-rich splicing factor 7 ;Cleavage and polyadenylation specificity factor subunit 6 ;WD40 repeat-containing protein SMU1 ;Putative uncharacterized protein FNBP3 ;U4/U6.U5 tri-snRNP-associated protein 2 ;Protein virilizer homolog;THO complex subunit 7 homolog;Pre-mRNA-processing-splicing factor 8 ;Probable ATP-dependent RNA helicase DDX46 ;THO complex subunit 4 ;THO complex subunit 6 homolog;Serine/arginine repetitive matrix protein 1 ;THO complex subunit 2;Cactin ;U4/U6.U5 small nuclear ribonucleoprotein 27 kDa protein ;U4/U6 small nuclear ribonucleoprotein Prp31 ;Beta-catenin-like protein 1 ;Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16 ;Probable ATP-dependent RNA helicase DDX17 ;Peptidylprolyl isomerase domain and WD repeat-containing protein 1 ;Protein DGCR14 ;U5 small nuclear ribonucleoprotein 40 kDa protein;THO complex subunit 1;Splicing factor 45 ;THO complex subunit 3;Putative RNA-binding protein 15 ;Msx2-interacting protein ;Cell division cycle 5-like protein ;Pre-mRNA-splicing factor 18 ;Uncharacterized protein C19orf43;BUD13 homolog;Probable ATP-dependent RNA helicase DDX23 ;Serrate RNA effector molecule homolog ;Crooked neck-like protein 1 ;Peptidyl-prolyl cis-trans isomerase-like 3 ;Putative helicase MOV-10 ;Pre-mRNA-splicing factor CWC22 homolog ;Pre-mRNA-splicing factor SYF1 ;Pre-mRNA-splicing factor RBM22 ;Cyclin-dependent kinase 12 ;Spliceosome-associated protein CWC15 homolog;Tuftelin-interacting protein 11 ;Poly;Probable ATP-dependent RNA helicase DDX41 ;U6 snRNA-associated Sm-like protein LSm7;Apoptotic chromatin condensation inducer in the nucleus ;Pre-mRNA-splicing factor ISY1 homolog;Pre-mRNA-processing factor 19 ;Peptidyl-prolyl cis-trans isomerase E ;Serine/arginine repetitive matrix protein 2 ;WW domain-binding protein 11 ;U6 snRNA-associated Sm-like protein LSm2 ;Splicing factor 3B subunit 6 ;Peptidyl-prolyl cis-trans isomerase-like 1 ;U6 snRNA-associated Sm-like protein LSm4 ;PAX3- and PAX7-binding protein 1 ;RNA-binding protein 8A;Cilia- and flagella-associated protein 20","subunits.Gene.name.":"IGF2BP3;DDX3X;TCERG1;U2SURP;PPM1G;DHX15;PRPF4;SART1;PRPF3;PPIH;PLRG1;ZNF207;HTATSF1;NUDT21;DHX16;AQR;CDC40;PRPF40A;SF3B1;SNRNP200;BCAS2;DNAJC8;SMNDC1;PRPF6;LUC7L3;SLU7;CD2BP2;SYF2;SNRPB2;SNRNP70;SNRPA;SNRPC;SNRPA1;PABPC1;SNRPB;DDX5;U2AF2;EIF4A3;BUD31;SKIV2L2;RBM25;NCBP2;MFAP1;SNU13;MAGOH;SNRPE;SNRPF;SNRPG;LSM3;LSM6;SNRPD1;SNRPD2;SNRPD3;TRA2B;TXNL4A;SRSF3;U2AF1;SRSF2;SRSF11;SRSF1;SRSF4;DHX9;NCBP1;SF3A3;IK;SRSF9;SRSF5;SRSF6;PPIL2;SF3B2;PRPF4B;SNW1;THOC5;DDX39B;CIRBP;RBM39;DHX8;WTAP;EFTUD2;RNPS1;SF3B3;SF3B4;SF3A2;SF3A1;SF1;SRSF7;CPSF6;SMU1;FNBP3;USP39;KIAA1429;THOC7;PRPF8;DDX46;ALYREF;THOC6;SRRM1;THOC2;CACTIN;SNRNP27;PRPF31;CTNNBL1;DHX38;DDX17;PPWD1;DGCR14;SNRNP40;THOC1;RBM17;THOC3;RBM15;SPEN;CDC5L;PRPF18;C19orf43;BUD13;DDX23;SRRT;CRNKL1;PPIL3;MOV10;CWC22;XAB2;RBM22;CDK12;CWC15;TFIP11;PUF60;DDX41;LSM7;ACIN1;ISY1;PRPF19;PPIE;SRRM2;WBP11;LSM2;SF3B6;PPIL1;LSM4;PAXBP1;RBM8A;CFAP20","subunits.Gene.name.syn.":"IMP3 KOC1 VICKZ3;DBX DDX3;CA150 TAF2S;KIAA0332 SR140;PPM1C;DBP1 DDX15;PRP4;;HPRP3 PRP3;CYP20 CYPH;;BUGZ;;CFIM25 CPSF25 CPSF5;DBP2 DDX16 KIAA0577;KIAA0560;EHB3 PRP17 PRPF17;FBP11 FLAF1 FNBP3 HIP10 HYPA;SAP155;ASCC3L1 HELIC2 KIAA0788;DAM1;SPF31;SMNR SPF30;C20orf14;CREAP1 CROP O48;;KIAA1178;CBPIN GCIPIP;;RNPU1Z RPU1 SNRP70 U1AP1;;;;PAB1 PABP1 PABPC2;COD SNRPB1;G17P1 HELR HLR1;U2AF65;DDX48, KIAA0111;EDG2;DOB1 KIAA0052 Mtr4;RNPC7;CBP20;;NHP2L1;MAGOHA;;PBSCF;PBSCG;;;;SNRPD1;;SFRS10;DIM1 TXNL4;SFRS3 SRP20;U2AF35 U2AFBP;SFRS2;SFRS11;ASF SF2 SF2P33 SFRS1;SFRS4 SRP75;DDX9 LKP NDH2;CBP80 NCBP;SAP61;RED RER;SFRS9 SRP30C;HRS SFRS5 SRP40;SFRS6 SRP55;;SAP145;KIAA0536 PRP4 PRP4H PRP4K;SKIIP SKIP;C22orf19, KIAA0983;BAT1 UAP56;A18HNRNP CIRP;HCC1 RNPC2;DDX8;KIAA0105;KIAA0031 SNRP116;LDC2;KIAA0017 SAP130;SAP49;SAP62;SAP114;ZFM1 ZNF162;SFRS7;CFIM68;;;;;NIF3L1BP1;PRPC8;KIAA0801;ALY BEF THOC4;WDR58;SRM160;CXorf3;C19orf29;;PRP31;C20orf33;DDX38 KIAA0224 PRP16;;KIAA0073;DGCR13 DGSH DGSI ES2;PRP8BP SFP38 WDR57;HPR1;SPF45;None;OTT OTT1;KIAA0929 MINT SHARP;KIAA0432 PCDC5RP;HPRP18;;;;ARS2 ASR2;CRN;;KIAA1631;KIAA1604 NCM;HCNP KIAA1177 SYF1;ZC3H16;CRK7 CRKRS KIAA0904;C11orf5;STIP;FIR ROBPI SIAHBP1;ABS;;ACINUS KIAA0670;KIAA1160;NMP200 PRP19 SNEV;CYP33;KIAA0324 SRL300 SRM300;NPWBP SIPP1 SNP70;C6orf28 G7B;SAP14 SF3B14 SF3B14A;CYPL1;;C21orf66 GCFC GCFC1;RBM8, Y14;BUG22 C16orf80","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In eukaryotes, the removal of introns from nascent transcripts is mediated by a highly dynamic, macromolecular machine called the spliceosome.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":352,"ComplexName":"DNA ligase IV-XRCC4 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P49917;Q13426","subunits.Entrez.IDs.":"3981;7518","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006281;GO:0006312;GO:0003677;GO:0005694","GO.description":"DNA repair;mitotic recombination;DNA binding;chromosome","FunCat.ID":"10.01.05.01;10.01.05.03.03;16.03.01;70.10.03","FunCat.description":"DNA repair;somatic / mitotic recombination;DNA binding;chromosome","PubMed.ID":10854421,"subunits.Protein.name.":"DNA ligase 4 ;DNA repair protein XRCC4","subunits.Gene.name.":"LIG4;XRCC4","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":353,"ComplexName":"DNA ligase IV-condensin complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95347;P49917;Q9NTJ3","subunits.Entrez.IDs.":"10592;3981;10051","Protein.complex.purification.method":"MI:0428- imaging techniques; MI:0402- chromatin immunoprecipitation assays; MI:0019- coimmunoprecipitation","GO.ID":"GO:0006281;GO:0007049;GO:0005694","GO.description":"DNA repair;cell cycle;chromosome","FunCat.ID":"10.01.05.01;10.03;70.10.03","FunCat.description":"DNA repair;cell cycle;chromosome","PubMed.ID":12589063,"subunits.Protein.name.":"Structural maintenance of chromosomes protein 2 ;DNA ligase 4 ;Structural maintenance of chromosomes protein 4","subunits.Gene.name.":"SMC2;LIG4;SMC4","subunits.Gene.name.syn.":"CAPE SMC2L1;;CAPC SMC4L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"DNA ligase IV interacts with SMC2L1 protein.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":354,"ComplexName":"DNA ligase IV-XRCC4 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P49917;Q13426","subunits.Entrez.IDs.":"3981;7518","Protein.complex.purification.method":"MI:0428- imaging techniques; MI:0402- chromatin immunoprecipitation assays","GO.ID":"GO:0006281;GO:0006312;GO:0003677;GO:0005694","GO.description":"DNA repair;mitotic recombination;DNA binding;chromosome","FunCat.ID":"10.01.05.01;10.01.05.03.03;16.03.01;70.10.03","FunCat.description":"DNA repair;somatic / mitotic recombination;DNA binding;chromosome","PubMed.ID":12589063,"subunits.Protein.name.":"DNA ligase 4 ;DNA repair protein XRCC4","subunits.Gene.name.":"LIG4;XRCC4","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"XRCC4 and DNA ligase IV do not colocalize during mitosis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":355,"ComplexName":"DNA-PK-Ku antigen complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12956;P13010;P78527","subunits.Entrez.IDs.":"2547;7520;5591","Protein.complex.purification.method":"MI:0091- chromatography technologies","GO.ID":"GO:0009299;GO:0006468;GO:0006470;GO:0046777;GO:0003677;GO:0006464;GO:0043085;GO:0008047;GO:0005634","GO.description":"mRNA transcription;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;DNA binding;cellular protein modification process;positive regulation of catalytic activity;enzyme activator activity;nucleus","FunCat.ID":"11.02.03;14.07.03;16.03.01;14.07;18.02.01.01;70.10","FunCat.description":"mRNA synthesis;modification by phosphorylation, dephosphorylation, autophosphorylation;DNA binding;protein modification;enzyme activator;nucleus","PubMed.ID":1465419,"subunits.Protein.name.":"X-ray repair cross-complementing protein 6 ;X-ray repair cross-complementing protein 5 ;DNA-dependent protein kinase catalytic subunit","subunits.Gene.name.":"XRCC6;XRCC5;PRKDC","subunits.Gene.name.syn.":"G22P1;G22P2;HYRC HYRC1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ku antigen activates DNA-PK that phosphorylates the C-terminal domain of RNA polymerase II.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":356,"ComplexName":"DNA-PK-Ku antigen complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12956;P13010;P78527","subunits.Entrez.IDs.":"2547;7520;5591","Protein.complex.purification.method":"MI:0030- cross-linking studies; MI:0019- coimmunoprecipitation","GO.ID":"GO:0009299;GO:0006468;GO:0006470;GO:0046777;GO:0003677;GO:0006464;GO:0043085;GO:0008047;GO:0005634","GO.description":"mRNA transcription;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;DNA binding;cellular protein modification process;positive regulation of catalytic activity;enzyme activator activity;nucleus","FunCat.ID":"11.02.03;14.07.03;16.03.01;14.07;18.02.01.01;70.10","FunCat.description":"mRNA synthesis;modification by phosphorylation, dephosphorylation, autophosphorylation;DNA binding;protein modification;enzyme activator;nucleus","PubMed.ID":8422676,"subunits.Protein.name.":"X-ray repair cross-complementing protein 6 ;X-ray repair cross-complementing protein 5 ;DNA-dependent protein kinase catalytic subunit","subunits.Gene.name.":"XRCC6;XRCC5;PRKDC","subunits.Gene.name.syn.":"G22P1;G22P2;HYRC HYRC1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"DNA-PK is directed to the DNA by interaction with Ku antigen.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":357,"ComplexName":"DNA-PK-Ku antigen complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12956;P13010;P78527","subunits.Entrez.IDs.":"2547;7520;5591","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0009299;GO:0006468;GO:0006470;GO:0046777;GO:0003677;GO:0006464;GO:0043085;GO:0008047;GO:0005634","GO.description":"mRNA transcription;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;DNA binding;cellular protein modification process;positive regulation of catalytic activity;enzyme activator activity;nucleus","FunCat.ID":"11.02.03;14.07.03;16.03.01;14.07;18.02.01.01;70.10","FunCat.description":"mRNA synthesis;modification by phosphorylation, dephosphorylation, autophosphorylation;DNA binding;protein modification;enzyme activator;nucleus","PubMed.ID":8486698,"subunits.Protein.name.":"X-ray repair cross-complementing protein 6 ;X-ray repair cross-complementing protein 5 ;DNA-dependent protein kinase catalytic subunit","subunits.Gene.name.":"XRCC6;XRCC5;PRKDC","subunits.Gene.name.syn.":"G22P1;G22P2;HYRC HYRC1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ku antigen activates DNA-PK that phosphorylates the C-terminal domain of RNA polymerase II.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":358,"ComplexName":"DNA ligase IV-Xrcc4-DNA-protein kinase complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P97313;Q8BTF7;Q924T3","subunits.Entrez.IDs.":"19090;319583;108138","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006281;GO:0006312;GO:0006468;GO:0006470;GO:0046777;GO:0005694","GO.description":"DNA repair;mitotic recombination;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;chromosome","FunCat.ID":"10.01.05.01;10.01.05.03.03;14.07.03;70.10.03","FunCat.description":"DNA repair;somatic / mitotic recombination;modification by phosphorylation, dephosphorylation, autophosphorylation;chromosome","PubMed.ID":15194694,"subunits.Protein.name.":"DNA-dependent protein kinase catalytic subunit ;DNA ligase 4 ;DNA repair protein XRCC4","subunits.Gene.name.":"Prkdc;Lig4;Xrcc4","subunits.Gene.name.syn.":"Xrcc7;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"DNA ligase IV in complex with XRCC4 can be phosphorylated by DNA-protein kinase.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":359,"ComplexName":"DNA ligase IV-XRCC4-XLF complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P49917;Q13426;Q9H9Q4","subunits.Entrez.IDs.":"3981;7518;79840","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006281;GO:0005634","GO.description":"DNA repair;nucleus","FunCat.ID":"10.01.05.01;70.10","FunCat.description":"DNA repair;nucleus","PubMed.ID":16439205,"subunits.Protein.name.":"DNA ligase 4 ;DNA repair protein XRCC4 ;Non-homologous end-joining factor 1","subunits.Gene.name.":"LIG4;XRCC4;NHEJ1","subunits.Gene.name.syn.":";;XLF","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":360,"ComplexName":"Artemis-DNA-PK complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P78527;Q96SD1","subunits.Entrez.IDs.":"5591;64421","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006308;GO:0006281;GO:0006312;GO:0003677;GO:0006974;GO:0005634","GO.description":"DNA catabolic process;DNA repair;mitotic recombination;DNA binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"01.03.16.03;10.01.05.01;10.01.05.03.03;16.03.01;32.01.09;70.10","FunCat.description":"DNA degradation;DNA repair;somatic / mitotic recombination;DNA binding;DNA damage response;nucleus","PubMed.ID":16857680,"subunits.Protein.name.":"DNA-dependent protein kinase catalytic subunit ;Protein artemis","subunits.Gene.name.":"PRKDC;DCLRE1C","subunits.Gene.name.syn.":"HYRC HYRC1;ARTEMIS ASCID SCIDA SNM1C","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"DNA-PKcs is necessary for the loading of Artemis on damaged chromatin. Ku-mediated assembly of DNA-PK on DNA ends is responsible for a dissociation of the DNA-PKcs\\u00b7Artemis complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":361,"ComplexName":"Artemis-DNA-PK complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P78527;Q96SD1","subunits.Entrez.IDs.":"5591;64421","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006163;GO:0006144;GO:0006281;GO:0006312;GO:0003677;GO:0006974;GO:0005634","GO.description":"purine nucleotide metabolic process;purine nucleobase metabolic process;DNA repair;mitotic recombination;DNA binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"01.03.01;10.01.05.01;10.01.05.03.03;16.03.01;32.01.09;70.10","FunCat.description":"purin nucleotide/nucleoside/nucleobase metabolism;DNA repair;somatic / mitotic recombination;DNA binding;DNA damage response;nucleus","PubMed.ID":11955432,"subunits.Protein.name.":"DNA-dependent protein kinase catalytic subunit ;Protein artemis","subunits.Gene.name.":"PRKDC;DCLRE1C","subunits.Gene.name.syn.":"HYRC HYRC1;ARTEMIS ASCID SCIDA SNM1C","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Upon complex formation, DNA-PKcs phosphorylates Artemis, and Artemis acquires endonucleolytic activity on 5' and 3' overhangs, as well as hairpins. Finally, the Artemis:DNA-PKcs complex can open hairpins generated by the RAG complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":362,"ComplexName":"DNA ligase III-XRCC1-PNK-DNA-pol III multiprotein complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06746;P18887;P49916;Q96T60","subunits.Entrez.IDs.":"5423;7515;3980;11284","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0006974;GO:0005634","GO.description":"DNA repair;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;32.01.09;70.10","FunCat.description":"DNA repair;DNA damage response;nucleus","PubMed.ID":11163244,"subunits.Protein.name.":"DNA polymerase beta;DNA repair protein XRCC1 ;DNA ligase 3 ;Bifunctional polynucleotide phosphatase/kinase","subunits.Gene.name.":"POLB;XRCC1;LIG3;PNKP","subunits.Gene.name.syn.":"None;;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":363,"ComplexName":"DNA ligase III-XRCC1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P18887;P49916","subunits.Entrez.IDs.":"7515;3980","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006281;GO:0005634","GO.description":"DNA repair;nucleus","FunCat.ID":"10.01.05.01;70.10","FunCat.description":"DNA repair;nucleus","PubMed.ID":15141024,"subunits.Protein.name.":"DNA repair protein XRCC1 ;DNA ligase 3","subunits.Gene.name.":"XRCC1;LIG3","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":364,"ComplexName":"RC-1 complex (recombination complex 1)","Organism":"Bovine","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O54956;O97593;P97386;Q8CG48;Q9WVF7","subunits.Entrez.IDs.":"18974;282370;16882;14211;18973","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0006308;GO:0006281;GO:0006310;GO:0005634","GO.description":"DNA catabolic process;DNA repair;DNA recombination;nucleus","FunCat.ID":"01.03.16.03;10.01.05.01;10.01.05.03;70.10","FunCat.description":"DNA degradation;DNA repair;DNA recombination;nucleus","PubMed.ID":8392064,"subunits.Protein.name.":"DNA polymerase epsilon subunit 2 ;Structural maintenance of chromosomes protein 1A ;DNA ligase 3 ;Structural maintenance of chromosomes protein 2 ;DNA polymerase epsilon catalytic subunit A","subunits.Gene.name.":"Pole2;SMC1A;Lig3;Smc2;Pole","subunits.Gene.name.syn.":";SMC1 SMC1L1;;Cape Fin16 Smc2l1;Pole1","Disease.comment":"None","Subunits.comment":"Since several bovine proteins were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Bos taurus (Bovine);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":365,"ComplexName":"DNA ligase III-XRCC1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P18887;P49916","subunits.Entrez.IDs.":"7515;3980","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0006281;GO:0005634","GO.description":"DNA repair;nucleus","FunCat.ID":"10.01.05.01;70.10","FunCat.description":"DNA repair;nucleus","PubMed.ID":16060670,"subunits.Protein.name.":"DNA repair protein XRCC1 ;DNA ligase 3","subunits.Gene.name.":"XRCC1;LIG3","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"DNA polymerase beta promotes recruitment of the XRCC1-Lig3 complex to sites of base excision repair. However Pol-beta is not stably complexed with the XRCC1-Lig3 heterodimer.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":366,"ComplexName":"Rag1-Rag2 protein-DNA complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P15919;P21784","subunits.Entrez.IDs.":"19373;19374","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006312;GO:0003677;GO:0005634","GO.description":"mitotic recombination;DNA binding;nucleus","FunCat.ID":"10.01.05.03.03;16.03.01;70.10","FunCat.description":"somatic / mitotic recombination;DNA binding;nucleus","PubMed.ID":9094713,"subunits.Protein.name.":"V;V","subunits.Gene.name.":"Rag1;Rag2","subunits.Gene.name.syn.":";Rag-2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Rag1 and Rag2 proteins form a stable complex only in presence of DNA.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":367,"ComplexName":"Rag1-Rag2-Ku70-Ku80 protein-DNA complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P15919;P21784;P23475;P27641;P63158","subunits.Entrez.IDs.":"19373;19374;14375;22596;15289","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006312;GO:0003677;GO:0005634","GO.description":"mitotic recombination;DNA binding;nucleus","FunCat.ID":"10.01.05.03.03;16.03.01;70.10","FunCat.description":"somatic / mitotic recombination;DNA binding;nucleus","PubMed.ID":9094713,"subunits.Protein.name.":"V;V;X-ray repair cross-complementing protein 6 ;X-ray repair cross-complementing protein 5 ;High mobility group protein B1","subunits.Gene.name.":"Rag1;Rag2;Xrcc6;Xrcc5;Hmgb1","subunits.Gene.name.syn.":";Rag-2;G22p1 Ku70;G22p2;Hmg-1 Hmg1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"A stable complex is formed only in the presence of DNA and Rag1/2.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":368,"ComplexName":"ERCC1-ERCC4-MSH2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P07992;P43246;Q92889","subunits.Entrez.IDs.":"2067;4436;2072","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006308;GO:0006281;GO:0006974;GO:0005634","GO.description":"DNA catabolic process;DNA repair;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"01.03.16.03;10.01.05.01;32.01.09;70.10","FunCat.description":"DNA degradation;DNA repair;DNA damage response;nucleus","PubMed.ID":14706347,"subunits.Protein.name.":"DNA excision repair protein ERCC-1;DNA mismatch repair protein Msh2 ;DNA repair endonuclease XPF","subunits.Gene.name.":"ERCC1;MSH2;ERCC4","subunits.Gene.name.syn.":";;ERCC11 XPF","Disease.comment":"ERCC4 is involved in xeroderma pigmentosum group F.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":369,"ComplexName":"MSH2-MSH6-PMS2-MLH1 complex","Organism":"Human","Synonyms":"MMR complex 2","Cell.line":"None","subunits.UniProt.IDs.":"P40692;P43246;P52701;P54278","subunits.Entrez.IDs.":"4292;4436;2956;5395","Protein.complex.purification.method":"MI:0031- protein cross-linking with a bifunctional reagent; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0003677;GO:0006974;GO:0005634","GO.description":"DNA repair;DNA binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;16.03.01;32.01.09;70.10","FunCat.description":"DNA repair;DNA binding;DNA damage response;nucleus","PubMed.ID":10748159,"subunits.Protein.name.":"DNA mismatch repair protein Mlh1 ;DNA mismatch repair protein Msh2 ;DNA mismatch repair protein Msh6 ;Mismatch repair endonuclease PMS2","subunits.Gene.name.":"MLH1;MSH2;MSH6;PMS2","subunits.Gene.name.syn.":"COCA2;;GTBP;PMSL2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The protein complex specifically binds to mismatched DNA. Interactions occur without addition of ATP.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":370,"ComplexName":"MSH2-MSH6-PMS1-MLH1 complex","Organism":"Human","Synonyms":"MMR complex 1","Cell.line":"None","subunits.UniProt.IDs.":"P40692;P43246;P52701;P54277","subunits.Entrez.IDs.":"4292;4436;2956;5378","Protein.complex.purification.method":"MI:0031- protein cross-linking with a bifunctional reagent; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0003677;GO:0006974;GO:0005634","GO.description":"DNA repair;DNA binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;16.03.01;32.01.09;70.10","FunCat.description":"DNA repair;DNA binding;DNA damage response;nucleus","PubMed.ID":10748159,"subunits.Protein.name.":"DNA mismatch repair protein Mlh1 ;DNA mismatch repair protein Msh2 ;DNA mismatch repair protein Msh6 ;PMS1 protein homolog 1","subunits.Gene.name.":"MLH1;MSH2;MSH6;PMS1","subunits.Gene.name.syn.":"COCA2;;GTBP;PMSL1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The protein complex specifically binds to mismatched DNA. Interactions occur without addition of ATP.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":371,"ComplexName":"Structure-specific endonulease complex","Organism":"Mammalia","Synonyms":"ERCC1-XPF complex","Cell.line":"None","subunits.UniProt.IDs.":"P07992;Q9QYM7","subunits.Entrez.IDs.":"2067;None","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0071- molecular sieving; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006281;GO:0006974;GO:0005634","GO.description":"DNA repair;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;32.01.09;70.10","FunCat.description":"DNA repair;DNA damage response;nucleus","PubMed.ID":8797827,"subunits.Protein.name.":"DNA excision repair protein ERCC-1;DNA repair endonuclease XPF","subunits.Gene.name.":"ERCC1;ERCC4","subunits.Gene.name.syn.":";","Disease.comment":"ERCC4 is involved in xeroderma pigmentosum group F.","Subunits.comment":"None","Complex.comment":"This complex is a structure-specific endonuclease responsible for the 5' incision during repair.","SWISSPROT.organism":"Homo sapiens (Human);Cricetulus griseus (Chinese hamster) (Cricetulus b"}
{"ComplexID":372,"ComplexName":"F0F1 ATP synthase, mitochondrial","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P05504;P10719;P11608;P15999;P19511;P21571;P29418;P29419;P31399;P35434;P35435;P56135;Q03344;Q06645;Q6PDU7","subunits.Entrez.IDs.":"26197;171374;26196;65262;171375;94271;245958;140608;641434;245965;116550;57423;25392;29754;300677","Protein.complex.purification.method":"MI:0028-cosedimentation in solution","GO.ID":"GO:0006163;GO:0006144;GO:0006796;GO:0005515;GO:0005743","GO.description":"purine nucleotide metabolic process;purine nucleobase metabolic process;phosphate-containing compound metabolic process;protein binding;mitochondrial inner membrane","FunCat.ID":"01.03.01;01.04;16.01;70.16.05","FunCat.description":"purin nucleotide/nucleoside/nucleobase metabolism;phosphate metabolism;protein binding;mitochondrial inner membrane","PubMed.ID":10887193,"subunits.Protein.name.":"ATP synthase subunit a;ATP synthase subunit beta, mitochondrial;ATP synthase protein 8;ATP synthase subunit alpha, mitochondrial;ATP synthase F;ATP synthase-coupling factor 6, mitochondrial;ATP synthase subunit epsilon, mitochondrial;ATP synthase subunit e, mitochondrial;ATP synthase subunit d, mitochondrial;ATP synthase subunit delta, mitochondrial;ATP synthase subunit gamma, mitochondrial;ATP synthase subunit f, mitochondrial;ATPase inhibitor, mitochondrial;ATP synthase F;ATP synthase subunit g, mitochondrial","subunits.Gene.name.":"Mt-atp6;Atp5b;Mt-atp8;Atp5a1;Atp5f1;Atp5j;Atp5e;Atp5i;Atp5h;Atp5d;Atp5c1;Atp5j2;Atpif1;Atp5g1;Atp5l","subunits.Gene.name.syn.":"Atp6 Atpase6 Mtatp6;None;Atp8 Atpase8 Mtatp8;None;Atp5f;None;None;None;Atp5jd;None;Atp5c;None;Atpi If1;None;None","Disease.comment":"None","Subunits.comment":"Since Atp5j2 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.Since the authors did not specify Atp5g, we used isoform Atp5g1.","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Mus musculus (Mouse);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":373,"ComplexName":"Vacuolar ATPase","Organism":"Bovine","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P11019;P21282;P23956;P31404;P31407;P39942;P40682;P61420;P79251;P81103;P81134;Q28029;Q29466","subunits.Entrez.IDs.":"287017;338089;550622;282147;338059;404152;327687;282148;281641;338075;513520;282405;286768","Protein.complex.purification.method":"MI:0028-cosedimentation in solution;MI:0276-blue native page","GO.ID":"GO:0006195;GO:0006145;GO:0005515;GO:0008324;GO:0006812;GO:0042626;GO:0016192;GO:0005886","GO.description":"purine nucleotide catabolic process;purine nucleobase catabolic process;protein binding;cation transmembrane transporter activity;cation transport;ATPase activity, coupled to transmembrane movement of substances;vesicle-mediated transport;plasma membrane","FunCat.ID":"01.03.01.01;16.01;20.01.01.01;20.03.22;20.09.07;70.02","FunCat.description":"purine nucleotide /nucleoside/nucleobase catabolism;protein binding;cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);transport ATPases;vesicular transport (Golgi network, etc.);eukaryotic plasma membrane / membrane attached","PubMed.ID":9556572,"subunits.Protein.name.":"V-type proton ATPase subunit E 1;V-type proton ATPase subunit C 1;V-type proton ATPase 16 kDa proteolipid subunit;V-type proton ATPase catalytic subunit A;V-type proton ATPase subunit B, kidney isoform;V-type proton ATPase subunit D;V-type proton ATPase subunit S1;V-type proton ATPase subunit d 1;V-type proton ATPase subunit G 1;V-type proton ATPase subunit e 1;Renin receptor;V-type proton ATPase subunit F;V-type proton ATPase 116 kDa subunit a isoform 1","subunits.Gene.name.":"ATP6V1E1;ATP6V1C1;ATP6V0C;ATP6V1A;ATP6V1B1;ATP6V1D;ATP6AP1;ATP6V0D1;ATP6V1G1;ATP6V0E1;ATP6AP2;ATP6V1F;ATP6V0A1","subunits.Gene.name.syn.":"ATP6E;ATP6C VATC;ATP6C ATP6L;ATP6A1 ATP6V1A1;ATP6B1;ATP6M VATD;ATP6IP1 ATP6S1;ATP6D VPATPD;ATP6G ATP6G1;ATP6H ATP6V0E;ATP6IP2;ATP6S14 VATF;ATP6N1 VPP1","Disease.comment":"None","Subunits.comment":"Since the authors did not specify ATP6B, we used isoform ATP6B1","Complex.comment":"This ATPase was isolated from bovine chromaffin granules.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":374,"ComplexName":"MSH2-MSH6 complex","Organism":"Human","Synonyms":"MutS-alpha complex","Cell.line":"None","subunits.UniProt.IDs.":"P43246;P52701","subunits.Entrez.IDs.":"4436;2956","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0031- protein cross-linking with a bifunctional reagent","GO.ID":"GO:0006281;GO:0003677;GO:0006974;GO:0005634","GO.description":"DNA repair;DNA binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;16.03.01;32.01.09;70.10","FunCat.description":"DNA repair;DNA binding;DNA damage response;nucleus","PubMed.ID":8942985,"subunits.Protein.name.":"DNA mismatch repair protein Msh2 ;DNA mismatch repair protein Msh6","subunits.Gene.name.":"MSH2;MSH6","subunits.Gene.name.syn.":";GTBP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":375,"ComplexName":"MSH2-MSH3 complex","Organism":"Human","Synonyms":"MutS-beta complex","Cell.line":"None","subunits.UniProt.IDs.":"P20585;P43246","subunits.Entrez.IDs.":"4437;4436","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0031- protein cross-linking with a bifunctional reagent","GO.ID":"GO:0006281;GO:0003677;GO:0006974;GO:0005634","GO.description":"DNA repair;DNA binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;16.03.01;32.01.09;70.10","FunCat.description":"DNA repair;DNA binding;DNA damage response;nucleus","PubMed.ID":8942985,"subunits.Protein.name.":"DNA mismatch repair protein Msh3 ;DNA mismatch repair protein Msh2","subunits.Gene.name.":"MSH3;MSH2","subunits.Gene.name.syn.":"DUC1 DUG;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":376,"ComplexName":"PCNA-MutS-alpha-MutL-alpha-DNA complex","Organism":"Human","Synonyms":"PCNA-MSH2-MSH6-MLH1-PMS2 complex","Cell.line":"None","subunits.UniProt.IDs.":"P12004;P40692;P43246;P52701;P54278","subunits.Entrez.IDs.":"5111;4292;4436;2956;5395","Protein.complex.purification.method":"MI:0031- protein cross-linking with a bifunctional reagent; MI:0019- coimmunoprecipitation","GO.ID":"GO:0006281;GO:0003677;GO:0006974;GO:0005634","GO.description":"DNA repair;DNA binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;16.03.01;32.01.09;70.10","FunCat.description":"DNA repair;DNA binding;DNA damage response;nucleus","PubMed.ID":16204460,"subunits.Protein.name.":"Proliferating cell nuclear antigen;DNA mismatch repair protein Mlh1 ;DNA mismatch repair protein Msh2 ;DNA mismatch repair protein Msh6 ;Mismatch repair endonuclease PMS2","subunits.Gene.name.":"PCNA;MLH1;MSH2;MSH6;PMS2","subunits.Gene.name.syn.":"None;COCA2;;GTBP;PMSL2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"MutS-alpha, consisting of MSH2 and MSH6 proteins, and PCNA bind to DNA to form an initial complex. MutL-alpha, consisting of MLH1 and PMS2, binds to the complex when the DNA is damaged.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":377,"ComplexName":"PCNA-MutS-alpha-DNA initial complex","Organism":"Human","Synonyms":"PCNA-MSH2-MSH6 complex","Cell.line":"None","subunits.UniProt.IDs.":"P12004;P43246;P52701","subunits.Entrez.IDs.":"5111;4436;2956","Protein.complex.purification.method":"MI:0031- protein cross-linking with a bifunctional reagent; MI:0019- coimmunoprecipitation","GO.ID":"GO:0006281;GO:0003677;GO:0005634","GO.description":"DNA repair;DNA binding;nucleus","FunCat.ID":"10.01.05.01;16.03.01;70.10","FunCat.description":"DNA repair;DNA binding;nucleus","PubMed.ID":16204460,"subunits.Protein.name.":"Proliferating cell nuclear antigen;DNA mismatch repair protein Msh2 ;DNA mismatch repair protein Msh6","subunits.Gene.name.":"PCNA;MSH2;MSH6","subunits.Gene.name.syn.":"None;;GTBP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"MutS-alpha, consisting of MSH2 and MSH6 proteins, and PCNA bind to DNA to form an initial complex. MutL-alpha, consisting of MLH1 and PMS2, binds to the complex when the DNA is damaged.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":378,"ComplexName":"MutS-beta complex","Organism":"Human","Synonyms":"MSH2-MSH3 complex","Cell.line":"None","subunits.UniProt.IDs.":"P20585;P43246","subunits.Entrez.IDs.":"4437;4436","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006281;GO:0003677;GO:0006974;GO:0005634","GO.description":"DNA repair;DNA binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;16.03.01;32.01.09;70.10","FunCat.description":"DNA repair;DNA binding;DNA damage response;nucleus","PubMed.ID":8805365,"subunits.Protein.name.":"DNA mismatch repair protein Msh3 ;DNA mismatch repair protein Msh2","subunits.Gene.name.":"MSH3;MSH2","subunits.Gene.name.syn.":"DUC1 DUG;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":379,"ComplexName":"MutL-alpha complex","Organism":"Human","Synonyms":"MLH1-PMS2 complex","Cell.line":"None","subunits.UniProt.IDs.":"P40692;P54278","subunits.Entrez.IDs.":"4292;5395","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0003677;GO:0006974;GO:0005634","GO.description":"DNA repair;DNA binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;16.03.01;32.01.09;70.10","FunCat.description":"DNA repair;DNA binding;DNA damage response;nucleus","PubMed.ID":10748105,"subunits.Protein.name.":"DNA mismatch repair protein Mlh1 ;Mismatch repair endonuclease PMS2","subunits.Gene.name.":"MLH1;PMS2","subunits.Gene.name.syn.":"COCA2;PMSL2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Normal levels of hMLH1 protein appear to be important in maintaining normal levels of hPMS1 and hPMS2 proteins, suggesting that PMS proteins are unstable in the absence of hMLH1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":380,"ComplexName":"MutL-beta complex","Organism":"Human","Synonyms":"MLH1-PMS1 complex","Cell.line":"None","subunits.UniProt.IDs.":"P40692;P54277","subunits.Entrez.IDs.":"4292;5378","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0003677;GO:0006974;GO:0005634","GO.description":"DNA repair;DNA binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;16.03.01;32.01.09;70.10","FunCat.description":"DNA repair;DNA binding;DNA damage response;nucleus","PubMed.ID":10748105,"subunits.Protein.name.":"DNA mismatch repair protein Mlh1 ;PMS1 protein homolog 1","subunits.Gene.name.":"MLH1;PMS1","subunits.Gene.name.syn.":"COCA2;PMSL1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results provide evidence for the association of hPMS1 with hMLH1 as a heterodimer in human epithelial cancer cells. Normal levels of hMLH1 protein appear to be important in maintaining normal levels of hPMS1 and hPMS2 proteins, suggesting that PMS proteins are unstable in the absence of hMLH1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":381,"ComplexName":"Respiratory chain complex I, mitochondrial","Organism":"Mouse","Synonyms":"NADH dehydrogenase (EC 1.6.5.3)","Cell.line":"brain","subunits.UniProt.IDs.":"O09111;P03888;P03911;P52503;Q3UIU2;Q62425;Q7TMF3;Q8K3J1;Q91VD9;Q91WD5;Q91WP8;Q91YT0;Q99LC3;Q99LY9;Q9CPP6;Q9CQ54;Q9CQ75;Q9CQ91;Q9CQC7;Q9CQH3;Q9CQJ8;Q9CQZ5;Q9CQZ6;Q9CR21;Q9CR61;Q9CXZ1;Q9D6J5;Q9D6J6;Q9DC69;Q9DC70;Q9DCJ5;Q9DCS9;Q9DCT2;Q9ERS2;Q9MD59;Q9MD82;Q9Z1P6","subunits.Entrez.IDs.":"104130;17716;17719;407785;230075;17992;66414;225887;227197;226646;78330;17995;67273;595136;68202;68197;17991;66091;68194;66046;66218;67130;66495;70316;66916;17993;67264;72900;66108;75406;68375;68342;68349;67184;17717;17721;66416","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006091;GO:0009060;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":15591592,"subunits.Protein.name.":"NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial ;NADH-ubiquinone oxidoreductase chain 1 ;NADH-ubiquinone oxidoreductase chain 4 ;NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial ;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6 ;Cytochrome c oxidase subunit NDUFA4;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 ;NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial ;NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial ;NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial ;NADH dehydrogenase ;NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial ;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial ;NADH dehydrogenase [ubiquinone] iron-sulfur protein 5 ;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 ;NADH dehydrogenase [ubiquinone] 1 subunit C2 ;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2 ;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3 ;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4 ;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial ;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 ;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 ;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3 ;Acyl carrier protein, mitochondrial ;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7 ;NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial ;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial ;NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial ;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial ;NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial ;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8 ;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10 ;NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial ;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13 ;NADH-ubiquinone oxidoreductase chain 2 ;NADH-ubiquinone oxidoreductase chain 5 ;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7","subunits.Gene.name.":"Ndufb11;Mtnd1;Mtnd4;Ndufs6;Ndufb6;Ndufa4;Ndufa12;Ndufs8;Ndufs1;Ndufs2;Ndufv3;Ndufv1;Ndufa10;Ndufs5;Ndufa5;Ndufc2;Ndufa2;Ndufa3;Ndufb4;Ndufb5;Ndufb9;Ndufa6;Ndufb3;Ndufab1;Ndufb7;Ndufs4;Ndufb8;Ndufv2;Ndufa9;Ndufs7;Ndufa8;Ndufb10;Ndufs3;Ndufa13;mt-Nd2;mt-Nd5;Ndufa7","subunits.Gene.name.syn.":"Np15;mt-Nd1 Nd1;mt-Nd4 Nd4;Ip13;Gm137;;;;;;;;;;;;;;;;;;;;;;;;;;;;;Grim19;ND2 Nd2;mt-Nd6 ND5 Nd5;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":382,"ComplexName":"Respiratory chain complex I, mitochondrial","Organism":"Mouse","Synonyms":"NADH dehydrogenase (EC 1.6.5.3)","Cell.line":"brain","subunits.UniProt.IDs.":"O09111;O35683;P03888;P03899;P03911;P52503;Q3UIU2;Q62425;Q7TMF3;Q8K3J1;Q91VD9;Q91WD5;Q91WP8;Q91YT0;Q99LC3;Q99LY9;Q9CPP6;Q9CPU2;Q9CQ54;Q9CQ75;Q9CQ91;Q9CQC7;Q9CQH3;Q9CQJ8;Q9CQZ5;Q9CQZ6;Q9CR21;Q9CR61;Q9CXZ1;Q9D6J5;Q9D6J6;Q9D8B4;Q9DC69;Q9DC70;Q9DCJ5;Q9DCS9;Q9DCT2;Q9ERS2;Q9MD82;Q9Z1P6","subunits.Entrez.IDs.":"104130;54405;17716;17718;17719;407785;230075;17992;66414;225887;227197;226646;78330;17995;67273;595136;68202;68198;68197;17991;66091;68194;66046;66218;67130;66495;70316;66916;17993;67264;72900;69875;66108;75406;68375;68342;68349;67184;17721;66416","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006091;GO:0009060;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":15591592,"subunits.Protein.name.":"NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial ;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1 ;NADH-ubiquinone oxidoreductase chain 1 ;NADH-ubiquinone oxidoreductase chain 3 ;NADH-ubiquinone oxidoreductase chain 4 ;NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial ;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6 ;Cytochrome c oxidase subunit NDUFA4;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 ;NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial ;NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial ;NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial ;NADH dehydrogenase ;NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial ;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial ;NADH dehydrogenase [ubiquinone] iron-sulfur protein 5 ;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 ;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial ;NADH dehydrogenase [ubiquinone] 1 subunit C2 ;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2 ;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3 ;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4 ;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial ;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 ;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 ;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3 ;Acyl carrier protein, mitochondrial ;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7 ;NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial ;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial ;NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial ;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11 ;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial ;NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial ;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8 ;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10 ;NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial ;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13 ;NADH-ubiquinone oxidoreductase chain 5 ;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7","subunits.Gene.name.":"Ndufb11;Ndufa1;Mtnd1;Mtnd3;Mtnd4;Ndufs6;Ndufb6;Ndufa4;Ndufa12;Ndufs8;Ndufs1;Ndufs2;Ndufv3;Ndufv1;Ndufa10;Ndufs5;Ndufa5;Ndufb2;Ndufc2;Ndufa2;Ndufa3;Ndufb4;Ndufb5;Ndufb9;Ndufa6;Ndufb3;Ndufab1;Ndufb7;Ndufs4;Ndufb8;Ndufv2;Ndufa11;Ndufa9;Ndufs7;Ndufa8;Ndufb10;Ndufs3;Ndufa13;mt-Nd5;Ndufa7","subunits.Gene.name.syn.":"Np15;;mt-Nd1 Nd1;mt-Nd3 Nd3;mt-Nd4 Nd4;Ip13;Gm137;;;;;;;;;;;;;;;;;;;;;;;;;;;;;;;Grim19;mt-Nd6 ND5 Nd5;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":384,"ComplexName":"Caveolar macromolecular signaling complex","Organism":"Mouse","Synonyms":"None","Cell.line":"heart muscle","subunits.UniProt.IDs.":"P18762;P31324;P51637;P63094;P97490;Q01815;Q76MZ3","subunits.Entrez.IDs.":"11555;19088;12391;14683;11514;12288;51792","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0007186;GO:0006941;GO:0005886","GO.description":"G-protein coupled receptor signaling pathway;striated muscle contraction;plasma membrane","FunCat.ID":"30.05.02.24;36.25.09.03;70.02","FunCat.description":"G-protein coupled receptor signalling pathway;striated muscle contraction;eukaryotic plasma membrane / membrane attached","PubMed.ID":16648270,"subunits.Protein.name.":"Beta-2 adrenergic receptor;cAMP-dependent protein kinase type II-beta regulatory subunit;Caveolin-3;Guanine nucleotide-binding protein G;Adenylate cyclase type 8;Voltage-dependent L-type calcium channel subunit alpha-1C;Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform","subunits.Gene.name.":"Adrb2;Prkar2b;Cav3;Gnas;Adcy8;Cacna1c;Ppp2r1a","subunits.Gene.name.syn.":"Adrb2r;None;None;Gnas1;None;Cach2 Cacn2 Cacnl1a1 Cchl1a1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Anti-Ca(v)1.2 used for coimmunoprecipitation. The authors didn't differentiate between the different types of adenylate cyclases, Adcy8 was chosen due to its molecular weight, complex isolated from ventricular myocytes.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":385,"ComplexName":"Caveolar macromolecular signaling complex, using anti-Cav-3","Organism":"Mouse","Synonyms":"None","Cell.line":"heart muscle","subunits.UniProt.IDs.":"P18762;P31324;P51637;P63094;P97490;Q01815;Q61018;Q76MZ3","subunits.Entrez.IDs.":"11555;19088;12391;14683;11514;12288;14677;51792","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0007186;GO:0006941;GO:0005886","GO.description":"G-protein coupled receptor signaling pathway;striated muscle contraction;plasma membrane","FunCat.ID":"30.05.02.24;36.25.09.03;70.02","FunCat.description":"G-protein coupled receptor signalling pathway;striated muscle contraction;eukaryotic plasma membrane / membrane attached","PubMed.ID":16648270,"subunits.Protein.name.":"Beta-2 adrenergic receptor;cAMP-dependent protein kinase type II-beta regulatory subunit;Caveolin-3;Guanine nucleotide-binding protein G;Adenylate cyclase type 8;Voltage-dependent L-type calcium channel subunit alpha-1C;G protein alpha i1 subunit;Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform","subunits.Gene.name.":"Adrb2;Prkar2b;Cav3;Gnas;Adcy8;Cacna1c;Gnai1;Ppp2r1a","subunits.Gene.name.syn.":"Adrb2r;None;None;Gnas1;None;Cach2 Cacn2 Cacnl1a1 Cchl1a1;None;None","Disease.comment":"None","Subunits.comment":"The authors didn't differentiate between the different types of adenylate cyclases, Adcy8 was chosen due to its molecular weight, complex isolated from ventricular myocytes.","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":386,"ComplexName":"Ubiquitin E3 ligase (UBADC1, RNF123)","Organism":"Human","Synonyms":"KPC complex;KPC1-KPC2 ubiquitin-protein ligase","Cell.line":"None","subunits.UniProt.IDs.":"Q5XPI4;Q9BSL1","subunits.Entrez.IDs.":"63891;10422","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511;GO:0005515;GO:0005737","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;protein binding;cytoplasm","FunCat.ID":"14.07.05;14.13.01.01;16.01;70.03","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway);protein binding;cytoplasm","PubMed.ID":15531880,"subunits.Protein.name.":"E3 ubiquitin-protein ligase RNF123 ;Ubiquitin-associated domain-containing protein 1","subunits.Gene.name.":"RNF123;UBAC1","subunits.Gene.name.syn.":"KPC1;GBDR1 KPC2 UBADC1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. The cyclin-dependent kinase inhibitor p27(Kip1) is degraded at the G0-G1 transition of the cell cycle by the ubiquitin-proteasome pathway. Overexpression of KPC promoted the degradation of p27(Kip1), whereas a dominant-negative mutant of KPC1 delayed p27(Kip1) degradation. The nuclear export of p27(Kip1) by CRM1 seems to be necessary for KPC-mediated proteolysis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":387,"ComplexName":"MCM complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P25205;P33991;P33992;P33993;P49736;Q14566","subunits.Entrez.IDs.":"4172;4173;4174;4176;4171;4175","Protein.complex.purification.method":"MI:0226- ion exchange chromatography","GO.ID":"GO:0051276;GO:0006260;GO:0005524;GO:0005694","GO.description":"chromosome organization;DNA replication;ATP binding;chromosome","FunCat.ID":"42.10.03;10.01.03;16.19.03;70.10.03","FunCat.description":"organization of chromosome structure;DNA synthesis and replication;ATP binding;chromosome","PubMed.ID":8798650,"subunits.Protein.name.":"DNA replication licensing factor MCM3 ;DNA replication licensing factor MCM4 ;DNA replication licensing factor MCM5 ;DNA replication licensing factor MCM7 ;DNA replication licensing factor MCM2 ;DNA replication licensing factor MCM6","subunits.Gene.name.":"MCM3;MCM4;MCM5;MCM7;MCM2;MCM6","subunits.Gene.name.syn.":";CDC21;CDC46;CDC47 MCM2;BM28 CCNL1 CDCL1 KIAA0030;","Disease.comment":"The MCM proteins are highly expressed in malignant human cancer cells and pre-cancerous cells undergoing malignant transformation (PMID:16101384).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":388,"ComplexName":"Respiratory chain complex I, mitochondrial","Organism":"Bovine","Synonyms":"NADH dehydrogenase (EC 1.6.5.3)","Cell.line":"heart muscle","subunits.UniProt.IDs.":"O97725;P03887;P03892;P03898;P03902;P03910;P03920;P03924;P04394;P15690;P17694;P23709;P23934;P23935;P25708;P25712;P34942;P34943;P42026;P42028;P42029;P48305;P52505;Q01321;Q02365;Q02366;Q02367;Q02368;Q02369;Q02370;Q02371;Q02372;Q02373;Q02374;Q02375;Q02376;Q02377;Q02378;Q02379;Q02380;Q02827;Q05752;Q8HXG5;Q8HXG6;Q95KV7","subunits.Entrez.IDs.":"281742;None;None;3283884;3283885;3283886;None;3283888;None;288380;327697;287327;327691;327714;287014;327717;338060;404188;338079;287027;327710;None;327702;327704;338073;327670;327665;338065;327660;None;338064;282517;327701;327713;327680;282289;None;327690;338057;338061;338046;338063;404161;326346;338084","Protein.complex.purification.method":"MI:0227-reverse phase chromatography","GO.ID":"GO:0006091;GO:0009060;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":12381726,"subunits.Protein.name.":"NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12;NADH-ubiquinone oxidoreductase chain 1;NADH-ubiquinone oxidoreductase chain 2;NADH-ubiquinone oxidoreductase chain 3;NADH-ubiquinone oxidoreductase chain 4L;NADH-ubiquinone oxidoreductase chain 4;NADH-ubiquinone oxidoreductase chain 5;NADH-ubiquinone oxidoreductase chain 6;NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial;NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5;NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial;NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4;Acyl carrier protein, mitochondrial;Cytochrome c oxidase subunit NDUFA4;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial;NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1;NADH dehydrogenase [ubiquinone] iron-sulfur protein 5;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial;NADH dehydrogenase [ubiquinone] 1 subunit C2;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13","subunits.Gene.name.":"NDUFA12;MT-ND1;MT-ND2;MT-ND3;MT-ND4L;MT-ND4;MT-ND5;MT-ND6;NDUFV2;NDUFS1;NDUFS2;NDUFS3;NDUFS6;NDUFA5;NDUFV1;NDUFV3;NDUFA10;NDUFA9;NDUFS7;NDUFS8;NDUFA8;NDUFB4;NDUFAB1;NDUFA4;NDUFB3;NDUFA6;NDUFB6;NDUFB7;NDUFB9;NDUFA2;NDUFA3;NDUFB8;NDUFB10;NDUFB2;NDUFS4;NDUFC1;NDUFA1;NDUFB1;NDUFS5;NDUFB5;NDUFC2;NDUFA7;NDUFB11;NDUFA11;NDUFA13","subunits.Gene.name.syn.":"None;MTND1 NADH1 ND1;MTND2 NADH2 ND2;MTND3 NADH3 ND3;MTND4L NADH4L ND4L;MTND4 NADH4 ND4;MTND5 NADH5 ND5;MTND6 NADH6 ND6;None;None;None;None;None;None;UQOR1;None;None;None;None;None;None;None;None;None;None;None;None;None;UQOR22;None;None;None;None;None;None;None;None;None;None;None;None;CI-B14-5A;None;None;GRIM19","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":389,"ComplexName":"ORC complex (origin recognition complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43913;O43929;Q13415;Q13416;Q9UBD5;Q9Y5N6","subunits.Entrez.IDs.":"5001;5000;4998;4999;23595;23594","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006267;GO:0003688;GO:0005524;GO:0005694","GO.description":"pre-replicative complex assembly involved in nuclear cell cycle DNA replication;DNA replication origin binding;ATP binding;chromosome","FunCat.ID":"10.01.03.03;16.19.03;70.10.03","FunCat.description":"ori recognition and priming complex formation;ATP binding;chromosome","PubMed.ID":16549788,"subunits.Protein.name.":"Origin recognition complex subunit 5;Origin recognition complex subunit 4;Origin recognition complex subunit 1 ;Origin recognition complex subunit 2;Origin recognition complex subunit 3 ;Origin recognition complex subunit 6","subunits.Gene.name.":"ORC5;ORC4;ORC1;ORC2;ORC3;ORC6","subunits.Gene.name.syn.":"ORC5L;ORC4L;ORC1L PARC1;ORC2L;LATHEO ORC3L;ORC6L","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Orc6 is only weakly associated with the ORC complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":390,"ComplexName":"Ubiquitin E3 ligase (SKP1A, FBXW2, CUL1)","Organism":"Human","Synonyms":"SCF(hFBW2) E3 complex","Cell.line":"None","subunits.UniProt.IDs.":"P63208;Q13616;Q9UKT8","subunits.Entrez.IDs.":"6500;8454;26190","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511;GO:0005515;GO:0030878;GO:0005737","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;protein binding;thyroid gland development;cytoplasm","FunCat.ID":"14.07.05;14.13.01.01;16.01;47.03.21.03.06;70.03","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway);protein binding;thyroid gland;cytoplasm","PubMed.ID":15640526,"subunits.Protein.name.":"S-phase kinase-associated protein 1;Cullin-1;F-box/WD repeat-containing protein 2","subunits.Gene.name.":"SKP1;CUL1;FBXW2","subunits.Gene.name.syn.":"EMC19, OCP2, SKP1A, TCEB1L;None;FBW2 FWD2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The GCM proteins GCMa/1 and GCMb/2 are novel zinc-containing transcription factors critical for glial cell differentiation in fly and for placental as well as parathyroid gland development in mouse. Experiments identify the SCF(hFBW2) E3 complex as the key machinery that targets hGCMa to the ubiquitin-proteasome degradation system.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":391,"ComplexName":"Ubiquitin E3 ligase (DDB1, CUL4A, RBX1)","Organism":"Human","Synonyms":"Ddb1-Cul4a-Roc1 complex","Cell.line":"None","subunits.UniProt.IDs.":"P62877;Q13619;Q16531","subunits.Entrez.IDs.":"9978;8451;1642","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0005515;GO:0006974;GO:0005634","GO.description":"protein ubiquitination;protein deubiquitination;protein binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"14.07.05;16.01;32.01.09;70.10","FunCat.description":"modification by ubiquitination, deubiquitination;protein binding;DNA damage response;nucleus","PubMed.ID":16964240,"subunits.Protein.name.":"E3 ubiquitin-protein ligase RBX1;Cullin-4A;DNA damage-binding protein 1","subunits.Gene.name.":"RBX1;CUL4A;DDB1","subunits.Gene.name.syn.":"RNF75, ROC1;None;XAP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":392,"ComplexName":"Succinyl-CoA synthetase, GDP-forming","Organism":"Pig","Synonyms":"succinyl-CoA ligase","Cell.line":"None","subunits.UniProt.IDs.":"O19069;P53590","subunits.Entrez.IDs.":"399539;397026","Protein.complex.purification.method":"MI:0027- cosedimentation","GO.ID":"GO:0006163;GO:0006144;GO:0008152;GO:0005515;GO:0005525;GO:0005739","GO.description":"purine nucleotide metabolic process;purine nucleobase metabolic process;metabolic process;protein binding;GTP binding;mitochondrion","FunCat.ID":"01.03.01;01;16.01;16.19.05;70.16","FunCat.description":"purin nucleotide/nucleoside/nucleobase metabolism;METABOLISM;protein binding;GTP binding;mitochondrion","PubMed.ID":8401211,"subunits.Protein.name.":"Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial ;Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial","subunits.Gene.name.":"SUCLG1;SUCLG2","subunits.Gene.name.syn.":";","Disease.comment":"A deletion in SUCLG1, a gene that encodes the alpha subunit of the Krebs-cycle enzyme succinate-coenzyme A ligase (SUCL) causes fatal infantile lactic acidosis(PMID:17668387).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Sus scrofa (Pig);Sus scrofa (Pig)"}
{"ComplexID":393,"ComplexName":"Succinyl-CoA synthetase, GDP-forming","Organism":"Human","Synonyms":"succinyl-CoA ligase","Cell.line":"None","subunits.UniProt.IDs.":"P53597;Q96I99","subunits.Entrez.IDs.":"8802;8801","Protein.complex.purification.method":"MI:0027- cosedimentation","GO.ID":"GO:0006163;GO:0006144;GO:0008152;GO:0005515;GO:0005525;GO:0005739","GO.description":"purine nucleotide metabolic process;purine nucleobase metabolic process;metabolic process;protein binding;GTP binding;mitochondrion","FunCat.ID":"01.03.01;01;16.01;16.19.05;70.16","FunCat.description":"purin nucleotide/nucleoside/nucleobase metabolism;METABOLISM;protein binding;GTP binding;mitochondrion","PubMed.ID":15234968,"subunits.Protein.name.":"Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial ;Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial","subunits.Gene.name.":"SUCLG1;SUCLG2","subunits.Gene.name.syn.":";","Disease.comment":"A deletion in SUCLG1, a gene that encodes the alpha subunit of the Krebs-cycle  enzyme succinate-coenzyme A ligase (SUCL) causes fatal infantile lactic acidosis (PMID:17668387).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":394,"ComplexName":"Succinyl-CoA synthetase, ADP-forming","Organism":"Human","Synonyms":"succinyl-CoA ligase","Cell.line":"None","subunits.UniProt.IDs.":"P53597;Q9P2R7","subunits.Entrez.IDs.":"8802;8803","Protein.complex.purification.method":"MI:0027- cosedimentation","GO.ID":"GO:0006163;GO:0006144;GO:0008152;GO:0005515;GO:0005524;GO:0005739","GO.description":"purine nucleotide metabolic process;purine nucleobase metabolic process;metabolic process;protein binding;ATP binding;mitochondrion","FunCat.ID":"01.03.01;01;16.01;16.19.03;70.16","FunCat.description":"purin nucleotide/nucleoside/nucleobase metabolism;METABOLISM;protein binding;ATP binding;mitochondrion","PubMed.ID":15234968,"subunits.Protein.name.":"Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial ;Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial","subunits.Gene.name.":"SUCLG1;SUCLA2","subunits.Gene.name.syn.":";","Disease.comment":"A deletion in SUCLG1, a gene that encodes the alpha subunit of the Krebs-cycle  enzyme succinate-coenzyme A ligase (SUCL) causes fatal infantile lactic acidosis (PMID:17668387).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":395,"ComplexName":"Succinyl-CoA synthetase, ADP-forming","Organism":"Mouse","Synonyms":"succinyl-CoA ligase","Cell.line":"None","subunits.UniProt.IDs.":"Q9WUM5;Q9Z2I9","subunits.Entrez.IDs.":"56451;20916","Protein.complex.purification.method":"MI:0027- cosedimentation","GO.ID":"GO:0006163;GO:0006144;GO:0008152;GO:0005515;GO:0005524;GO:0005739","GO.description":"purine nucleotide metabolic process;purine nucleobase metabolic process;metabolic process;protein binding;ATP binding;mitochondrion","FunCat.ID":"01.03.01;01;16.01;16.19.03;70.16","FunCat.description":"purin nucleotide/nucleoside/nucleobase metabolism;METABOLISM;protein binding;ATP binding;mitochondrion","PubMed.ID":15234968,"subunits.Protein.name.":"Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial ;Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial","subunits.Gene.name.":"Suclg1;Sucla2","subunits.Gene.name.syn.":";","Disease.comment":"A deletion in SUCLG1, a gene that encodes the alpha subunit of the Krebs-cycle  enzyme succinate-coenzyme A ligase (SUCL) causes fatal infantile lactic acidosis (PMID:17668387).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":396,"ComplexName":"Succinyl-CoA synthetase, GDP-forming","Organism":"Mouse","Synonyms":"succinyl-CoA ligase","Cell.line":"None","subunits.UniProt.IDs.":"Q9WUM5;Q9Z2I8","subunits.Entrez.IDs.":"56451;20917","Protein.complex.purification.method":"MI:0027- cosedimentation","GO.ID":"GO:0006163;GO:0006144;GO:0008152;GO:0005515;GO:0005525;GO:0005739","GO.description":"purine nucleotide metabolic process;purine nucleobase metabolic process;metabolic process;protein binding;GTP binding;mitochondrion","FunCat.ID":"01.03.01;01;16.01;16.19.05;70.16","FunCat.description":"purin nucleotide/nucleoside/nucleobase metabolism;METABOLISM;protein binding;GTP binding;mitochondrion","PubMed.ID":15234968,"subunits.Protein.name.":"Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial ;Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial","subunits.Gene.name.":"Suclg1;Suclg2","subunits.Gene.name.syn.":";","Disease.comment":"A deletion in SUCLG1, a gene that encodes the alpha subunit of the Krebs-cycle  enzyme succinate-coenzyme A ligase (SUCL) causes fatal infantile lactic acidosis (PMID:17668387).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":397,"ComplexName":"Succinyl-CoA synthetase, ADP-forming","Organism":"Rat","Synonyms":"succinyl-CoA ligase","Cell.line":"None","subunits.UniProt.IDs.":"P13086;Q499V7","subunits.Entrez.IDs.":"114597;362404","Protein.complex.purification.method":"MI:0027- cosedimentation","GO.ID":"GO:0006163;GO:0006144;GO:0008152;GO:0005515;GO:0005524;GO:0005739","GO.description":"purine nucleotide metabolic process;purine nucleobase metabolic process;metabolic process;protein binding;ATP binding;mitochondrion","FunCat.ID":"01.03.01;01;16.01;16.19.03;70.16","FunCat.description":"purin nucleotide/nucleoside/nucleobase metabolism;METABOLISM;protein binding;ATP binding;mitochondrion","PubMed.ID":15234968,"subunits.Protein.name.":"Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial ;Succinate-CoA ligase subunit beta","subunits.Gene.name.":"Suclg1;Suclg2","subunits.Gene.name.syn.":";","Disease.comment":"A deletion in SUCLG1, a gene that encodes the alpha subunit of the Krebs-cycle  enzyme succinate-coenzyme A ligase (SUCL) causes fatal infantile lactic acidosis (PMID:17668387).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":398,"ComplexName":"Egasyn-glucuronidase complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12265;Q64176","subunits.Entrez.IDs.":"110006;13897","Protein.complex.purification.method":"MI:0404- comigration in non denaturing gel electrophoresis","GO.ID":"GO:0005783","GO.description":"endoplasmic reticulum","FunCat.ID":"70.07","FunCat.description":"endoplasmic reticulum","PubMed.ID":7744842,"subunits.Protein.name.":"Beta-glucuronidase ;Carboxylesterase 1E","subunits.Gene.name.":"Gusb;Ces1e","subunits.Gene.name.syn.":"Gus Gus-s;Es22","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"A region including the serpin-like sequence in the glucuronidase propeptide is essential for complex formation with egasyn and ER retention of glucuronidase.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":399,"ComplexName":"Respiratory chain complex I, mitochondrial","Organism":"Bovine","Synonyms":"NADH:ubiquinone oxidoreductase (EC 1.6.5.3)","Cell.line":"heart muscle","subunits.UniProt.IDs.":"O97725;P03887;P03892;P03898;P03902;P03910;P03920;P03924;P04394;P15690;P17694;P23709;P23934;P23935;P25708;P25712;P34942;P34943;P42026;P42028;P42029;P48305;P52505;Q01321;Q02365;Q02366;Q02367;Q02368;Q02369;Q02370;Q02371;Q02372;Q02373;Q02374;Q02375;Q02376;Q02377;Q02378;Q02379;Q02380;Q02827;Q05752;Q8HXG5;Q8HXG6;Q95KV7","subunits.Entrez.IDs.":"281742;None;None;3283884;3283885;3283886;None;3283888;None;288380;327697;287327;327691;327714;287014;327717;338060;404188;338079;287027;327710;None;327702;327704;338073;327670;327665;338065;327660;None;338064;282517;327701;327713;327680;282289;None;327690;338057;338061;338046;338063;404161;326346;338084","Protein.complex.purification.method":"MI:0091-chromatography technologies;MI:0071-molecular sieving","GO.ID":"GO:0006091;GO:0009060;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":12644575,"subunits.Protein.name.":"NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12;NADH-ubiquinone oxidoreductase chain 1;NADH-ubiquinone oxidoreductase chain 2;NADH-ubiquinone oxidoreductase chain 3;NADH-ubiquinone oxidoreductase chain 4L;NADH-ubiquinone oxidoreductase chain 4;NADH-ubiquinone oxidoreductase chain 5;NADH-ubiquinone oxidoreductase chain 6;NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial;NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5;NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial;NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4;Acyl carrier protein, mitochondrial;Cytochrome c oxidase subunit NDUFA4;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial;NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1;NADH dehydrogenase [ubiquinone] iron-sulfur protein 5;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial;NADH dehydrogenase [ubiquinone] 1 subunit C2;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13","subunits.Gene.name.":"NDUFA12;MT-ND1;MT-ND2;MT-ND3;MT-ND4L;MT-ND4;MT-ND5;MT-ND6;NDUFV2;NDUFS1;NDUFS2;NDUFS3;NDUFS6;NDUFA5;NDUFV1;NDUFV3;NDUFA10;NDUFA9;NDUFS7;NDUFS8;NDUFA8;NDUFB4;NDUFAB1;NDUFA4;NDUFB3;NDUFA6;NDUFB6;NDUFB7;NDUFB9;NDUFA2;NDUFA3;NDUFB8;NDUFB10;NDUFB2;NDUFS4;NDUFC1;NDUFA1;NDUFB1;NDUFS5;NDUFB5;NDUFC2;NDUFA7;NDUFB11;NDUFA11;NDUFA13","subunits.Gene.name.syn.":"None;MTND1 NADH1 ND1;MTND2 NADH2 ND2;MTND3 NADH3 ND3;MTND4L NADH4L ND4L;MTND4 NADH4 ND4;MTND5 NADH5 ND5;MTND6 NADH6 ND6;None;None;None;None;None;None;UQOR1;None;None;None;None;None;None;None;None;None;None;None;None;None;UQOR22;None;None;None;None;None;None;None;None;None;None;None;None;CI-B14-5A;None;None;GRIM19","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":400,"ComplexName":"Respiratory chain complex I (subcomplex I alpha), mitochondrial","Organism":"Bovine","Synonyms":"NADH:ubiqinone dehydrogenase (EC 1.6.5.3) subcomplex I alpha","Cell.line":"heart muscle","subunits.UniProt.IDs.":"O97725;P03924;P04394;P15690;P17694;P23709;P23934;P23935;P25708;P25712;P34942;P34943;P42026;P42028;P42029;P48305;P52505;Q02366;Q02368;Q02370;Q02371;Q02377;Q05752;Q8HXG6;Q95KV7","subunits.Entrez.IDs.":"281742;3283888;None;288380;327697;287327;327691;327714;287014;327717;338060;404188;338079;287027;327710;None;327702;327670;338065;None;338064;None;338063;326346;338084","Protein.complex.purification.method":"MI:0091-chromatography technologies;MI:0071-molecular sieving;MI:0029-cosedimentation through density gradients","GO.ID":"GO:0006091;GO:0009060;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":12644575,"subunits.Protein.name.":"NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12;NADH-ubiquinone oxidoreductase chain 6;NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial;NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5;NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial;NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4;Acyl carrier protein, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13","subunits.Gene.name.":"NDUFA12;MT-ND6;NDUFV2;NDUFS1;NDUFS2;NDUFS3;NDUFS6;NDUFA5;NDUFV1;NDUFV3;NDUFA10;NDUFA9;NDUFS7;NDUFS8;NDUFA8;NDUFB4;NDUFAB1;NDUFA6;NDUFB7;NDUFA2;NDUFA3;NDUFA1;NDUFA7;NDUFA11;NDUFA13","subunits.Gene.name.syn.":"None;MTND6 NADH6 ND6;None;None;None;None;None;None;UQOR1;None;None;None;None;None;None;None;None;None;None;None;None;None;CI-B14-5A;None;GRIM19","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":401,"ComplexName":"Respiratory chain complex I (subcomplex I lambda), mitochondrial","Organism":"Bovine","Synonyms":"NADH:ubiquinone oxidoreductase (EC 1.6.5.3) subcomplex I lambda","Cell.line":"heart muscle","subunits.UniProt.IDs.":"O97725;P04394;P15690;P17694;P23709;P23934;P23935;P25708;P25712;P42026;P42028;Q02368;Q02370;Q05752;Q95KV7","subunits.Entrez.IDs.":"281742;None;288380;327697;287327;327691;327714;287014;327717;338079;287027;338065;None;338063;338084","Protein.complex.purification.method":"MI:0091-chromatography technologies;MI:0071-molecular sieving;MI:0029-cosedimentation through density gradients","GO.ID":"GO:0006091;GO:0009060;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":12644575,"subunits.Protein.name.":"NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12;NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial;NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5;NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial;NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13","subunits.Gene.name.":"NDUFA12;NDUFV2;NDUFS1;NDUFS2;NDUFS3;NDUFS6;NDUFA5;NDUFV1;NDUFV3;NDUFS7;NDUFS8;NDUFB7;NDUFA2;NDUFA7;NDUFA13","subunits.Gene.name.syn.":"None;None;None;None;None;None;None;UQOR1;None;None;None;None;None;CI-B14-5A;GRIM19","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Subcomplex I lambda is a fraction of subcomplex I alpha.Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":402,"ComplexName":"Respiratory chain complex I (subcomplex I beta), mitochondrial","Organism":"Bovine","Synonyms":"NADH:ubiquinone oxidoreductase (EC 1.6.5.3) subcomplex I beta","Cell.line":"heart muscle","subunits.UniProt.IDs.":"P03910;P03920;P48305;P52505;Q02365;Q02367;Q02368;Q02369;Q02372;Q02373;Q02374;Q02378;Q02380;Q8HXG5","subunits.Entrez.IDs.":"3283886;None;None;327702;338073;327665;338065;327660;282517;327701;327713;327690;338061;404161","Protein.complex.purification.method":"MI:0091-chromatography technologies;MI:0071-molecular sieving;MI:0029-cosedimentation through density gradients","GO.ID":"GO:0006091;GO:0009060;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":12644575,"subunits.Protein.name.":"NADH-ubiquinone oxidoreductase chain 4;NADH-ubiquinone oxidoreductase chain 5;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4;Acyl carrier protein, mitochondrial;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial","subunits.Gene.name.":"MT-ND4;MT-ND5;NDUFB4;NDUFAB1;NDUFB3;NDUFB6;NDUFB7;NDUFB9;NDUFB8;NDUFB10;NDUFB2;NDUFB1;NDUFB5;NDUFB11","subunits.Gene.name.syn.":"MTND4 NADH4 ND4;MTND5 NADH5 ND5;None;None;None;None;None;UQOR22;None;None;None;None;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":403,"ComplexName":"Cytochrome bc1-complex (EC 1.10.2.2), mitochondrial","Organism":"Bovine","Synonyms":"Complex III; Cytochrome reductase; Ubiquinol:cytochrome c oxidoreductase","Cell.line":"heart muscle","subunits.UniProt.IDs.":"P00125;P00126;P00129;P00130;P00157;P07552;P13271;P13272;P23004;P31800","subunits.Entrez.IDs.":"512500;613899;616871;616109;3283889;281570;286885;287020;282394;282393","Protein.complex.purification.method":"MI:0114-x-ray crystallography","GO.ID":"GO:0009060;GO:0015031;GO:0008565;GO:0006818;GO:0022904;GO:0006839;GO:0005743","GO.description":"aerobic respiration;protein transport;protein transporter activity;hydrogen transport;respiratory electron transport chain;mitochondrial transport;mitochondrial inner membrane","FunCat.ID":"02.13.03;20.01.10;20.01.15;02.11.07;20.09.04;70.16.05","FunCat.description":"aerobic respiration;protein transport;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial transport;mitochondrial inner membrane","PubMed.ID":9651245,"subunits.Protein.name.":"Cytochrome c1, heme protein, mitochondrial;Cytochrome b-c1 complex subunit 6, mitochondrial;Cytochrome b-c1 complex subunit 7;Cytochrome b-c1 complex subunit 9;Cytochrome b;Cytochrome b-c1 complex subunit 10;Cytochrome b-c1 complex subunit 8;Cytochrome b-c1 complex subunit Rieske, mitochondrial;Cytochrome b-c1 complex subunit 2, mitochondrial;Cytochrome b-c1 complex subunit 1, mitochondrial","subunits.Gene.name.":"CYC1;UQCRH;UQCRB;UQCR10;MT-CYB;UQCR11;UQCRQ;UQCRFS1;UQCRC2;UQCRC1","subunits.Gene.name.syn.":"None;None;None;None;COB CYTB MTCYB;UQCR;None;None;None;None","Disease.comment":"None","Subunits.comment":"The bovine heart mitochondrial cytochrome bc1 complex is a dimer, with each monomer consisting of 11 different subunits.Only 10 subunits are displayed, since subunit V (Rieske iron sulfur protein = P13272) contains subunit IX (=precursor of subunit V, compare PMID:8386158).","Complex.comment":"None","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":404,"ComplexName":"Isocitrate dehydrogenase, cytoplasmic","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75874","subunits.Entrez.IDs.":"3417","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0008152;GO:0051287;GO:0050661;GO:0005737;GO:0005777","GO.description":"metabolic process;NAD binding;NADP binding;cytoplasm;peroxisome","FunCat.ID":"01;16.21.07;70.03;70.19","FunCat.description":"METABOLISM;NAD/NADP binding;cytoplasm;peroxisome","PubMed.ID":15173171,"subunits.Protein.name.":"Isocitrate dehydrogenase [NADP] cytoplasmic","subunits.Gene.name.":"IDH1","subunits.Gene.name.syn.":"PICD","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Isocitrate dehydrogenases (IDHs) catalyze the oxidative decarboxylation of isocitrate to alpha-ketoglutarate. The isocitrate dehydrogenase complex appears as homodimer.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":405,"ComplexName":"Glucosidase 2","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P14314;Q14697","subunits.Entrez.IDs.":"5589;23193","Protein.complex.purification.method":"MI:0028- cosedimentation in solution; MI:0226- ion exchange chromatography; MI:0071- molecular sieving","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0006464;GO:0005515;GO:0005783","GO.description":"intracellular protein transport;protein targeting;protein transport;cellular protein modification process;protein binding;endoplasmic reticulum","FunCat.ID":"14.04;20.01.10;14.07;16.01;70.07","FunCat.description":"protein targeting, sorting and translocation;protein transport;protein modification;protein binding;endoplasmic reticulum","PubMed.ID":8910335,"subunits.Protein.name.":"Glucosidase 2 subunit beta ;Neutral alpha-glucosidase AB","subunits.Gene.name.":"PRKCSH;GANAB","subunits.Gene.name.syn.":"G19P1;G2AN KIAA0088","Disease.comment":"None","Subunits.comment":"Since Ganab and Prkcsh from rat were not available in the UniProt database at the time of annotation, the orthologous human proteins were used.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":406,"ComplexName":"N-acetylglucosamine-1-phosphotransferase","Organism":"Bovine","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q3T906;Q58CS8","subunits.Entrez.IDs.":"79158;508713","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0226- ion exchange chromatography; MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0006468;GO:0006470;GO:0046777;GO:0005515;GO:0005773;GO:0005764","GO.description":"intracellular protein transport;protein targeting;protein transport;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;protein binding;vacuole;lysosome","FunCat.ID":"14.04;20.01.10;14.07.03;16.01;70.25","FunCat.description":"protein targeting, sorting and translocation;protein transport;modification by phosphorylation, dephosphorylation, autophosphorylation;protein binding;vacuole or lysosome","PubMed.ID":8940155,"subunits.Protein.name.":"N-acetylglucosamine-1-phosphotransferase subunits alpha/beta ;N-acetylglucosamine-1-phosphotransferase subunit gamma","subunits.Gene.name.":"GNPTAB;GNPTG","subunits.Gene.name.syn.":"GNPTA KIAA1208;","Disease.comment":"None","Subunits.comment":"Since bovine GNPTAB was not available in the UniProt database at the time of annotation, the orthologous human protein was used.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Bos taurus (Bovine)"}
{"ComplexID":407,"ComplexName":"Guanylyl cyclase, soluble (GUCY1A2, GUCY1B3)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P33402;Q02153","subunits.Entrez.IDs.":"2977;2983","Protein.complex.purification.method":"MI:0028- cosedimentation in solution","GO.ID":"GO:0009187;GO:0005515;GO:0005737","GO.description":"cyclic nucleotide metabolic process;protein binding;cytoplasm","FunCat.ID":"01.03.10;16.01;70.03","FunCat.description":"metabolism of cyclic and unusual nucleotides;protein binding;cytoplasm","PubMed.ID":1683630,"subunits.Protein.name.":"Guanylate cyclase soluble subunit alpha-2 ;Guanylate cyclase soluble subunit beta-1","subunits.Gene.name.":"GUCY1A2;GUCY1B3","subunits.Gene.name.syn.":"GUC1A2 GUCSA2;GUC1B3 GUCSB3 GUCY1B1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Two soluble guanylyl cyclase complexes were found in mammals.  The GUCY1A3-GUCY1B3 complex exhibits higher guanylyl cyclase activity than the GUCY1A2-GUCY1B3 complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":408,"ComplexName":"Guanylyl cyclase, soluble (GUCY1A3, GUCY1B3)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q02108;Q02153","subunits.Entrez.IDs.":"2982;2983","Protein.complex.purification.method":"MI:0028- cosedimentation in solution","GO.ID":"GO:0009187;GO:0005515;GO:0005737","GO.description":"cyclic nucleotide metabolic process;protein binding;cytoplasm","FunCat.ID":"01.03.10;16.01;70.03","FunCat.description":"metabolism of cyclic and unusual nucleotides;protein binding;cytoplasm","PubMed.ID":1683630,"subunits.Protein.name.":"Guanylate cyclase soluble subunit alpha-3 ;Guanylate cyclase soluble subunit beta-1","subunits.Gene.name.":"GUCY1A3;GUCY1B3","subunits.Gene.name.syn.":"GUC1A3 GUCSA3 GUCY1A1;GUC1B3 GUCSB3 GUCY1B1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Two soluble guanylyl cyclase complexes were found in mammals.  The GUCY1A3-GUCY1B3 complex exhibits higher guanylyl cyclase activity than the GUCY1A2-GUCY1B3 complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":409,"ComplexName":"Gamma-glutamylcysteine synthetase","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P19468;P48508","subunits.Entrez.IDs.":"25283;29739","Protein.complex.purification.method":"MI:0028- cosedimentation in solution","GO.ID":"GO:0006536;GO:0006534;GO:0006163;GO:0006144;GO:0005515","GO.description":"glutamate metabolic process;cysteine metabolic process;purine nucleotide metabolic process;purine nucleobase metabolic process;protein binding","FunCat.ID":"01.01.03.02;01.01.09.03;01.03.01;16.01","FunCat.description":"metabolism of glutamate;metabolism of cysteine;purin nucleotide/nucleoside/nucleobase metabolism;protein binding","PubMed.ID":1967255,"subunits.Protein.name.":"Glutamate--cysteine ligase catalytic subunit ;Glutamate--cysteine ligase regulatory subunit","subunits.Gene.name.":"Gclc;Gclm","subunits.Gene.name.syn.":"Glclc;Glclr","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":413,"ComplexName":"(ER)-localized multiprotein complex, Ig heavy chains associated","Organism":"Mouse","Synonyms":"None","Cell.line":"AG8 cell line","subunits.UniProt.IDs.":"P08003;P08113;P09103;P20029;P24369;Q6P5E4;Q99KV1;Q9ESP1;Q9JKR6;Q9JLK7","subunits.Entrez.IDs.":"12304;22027;18453;14828;19035;320011;67838;64136;12282;29867","Protein.complex.purification.method":"MI:0031- protein cross-linking with a bifunctional reagent; MI:0096- pull down","GO.ID":"GO:0050821;GO:0006457;GO:0030968;GO:0005783","GO.description":"protein stabilization;protein folding;endoplasmic reticulum unfolded protein response;endoplasmic reticulum","FunCat.ID":"14.01;32.01.07;70.07","FunCat.description":"protein folding and stabilization;unfolded protein response (e.g. ER quality control);endoplasmic reticulum","PubMed.ID":12475965,"subunits.Protein.name.":"Protein disulfide-isomerase A4 ;Endoplasmin ;Protein disulfide-isomerase ;78 kDa glucose-regulated protein ;Peptidyl-prolyl cis-trans isomerase B ;UDP-glucose:glycoprotein glucosyltransferase 1 ;DnaJ homolog subfamily B member 11 ;Stromal cell-derived factor 2-like protein 1 ;Hypoxia up-regulated protein 1 ;Calcium-binding protein 1","subunits.Gene.name.":"Pdia4;Hsp90b1;P4hb;Hspa5;Ppib;Uggt1;Dnajb11;Sdf2l1;Hyou1;Cabp1","subunits.Gene.name.syn.":"Cai Erp72;Grp94 Tra-1 Tra1;Pdia1;Grp78;;Gt Ugcgl1 Uggt Ugt1 Ugtr;;;Grp170;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex isolated in mouse lymphoma cell lines Ag8(8). The assembly of the chaperones with each other is not dependent on the presence of unassembled, unfolded heavy chains but rather that unassembled heavy chains may bind to this preformed ER chaperone network.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":414,"ComplexName":"(ER)-localized multiprotein complex, in absence of Ig heavy chains","Organism":"Mouse","Synonyms":"None","Cell.line":"Ag8.653 cells","subunits.UniProt.IDs.":"P08003;P08113;P09103;P20029;P24369;Q6P5E4;Q9ESP1;Q9JKR6;Q9JLK7","subunits.Entrez.IDs.":"12304;22027;18453;14828;19035;320011;64136;12282;29867","Protein.complex.purification.method":"MI:0031- protein cross-linking with a bifunctional reagent; MI:0096- pull down; MI:0019- coimmunoprecipitation","GO.ID":"GO:0050821;GO:0006457;GO:0030968;GO:0005783","GO.description":"protein stabilization;protein folding;endoplasmic reticulum unfolded protein response;endoplasmic reticulum","FunCat.ID":"14.01;32.01.07;70.07","FunCat.description":"protein folding and stabilization;unfolded protein response (e.g. ER quality control);endoplasmic reticulum","PubMed.ID":12475965,"subunits.Protein.name.":"Protein disulfide-isomerase A4 ;Endoplasmin ;Protein disulfide-isomerase ;78 kDa glucose-regulated protein ;Peptidyl-prolyl cis-trans isomerase B ;UDP-glucose:glycoprotein glucosyltransferase 1 ;Stromal cell-derived factor 2-like protein 1 ;Hypoxia up-regulated protein 1 ;Calcium-binding protein 1","subunits.Gene.name.":"Pdia4;Hsp90b1;P4hb;Hspa5;Ppib;Uggt1;Sdf2l1;Hyou1;Cabp1","subunits.Gene.name.syn.":"Cai Erp72;Grp94 Tra-1 Tra1;Pdia1;Grp78;;Gt Ugcgl1 Uggt Ugt1 Ugtr;;Grp170;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The assembly of the chaperones with each other is not dependent on the presence of unassembled, unfolded heavy chains but rather that unassembled heavy chains may bind to this preformed ER chaperone network.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":415,"ComplexName":"EXO1-MLH1-PMS2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P40692;P54278;Q9UQ84","subunits.Entrez.IDs.":"4292;5395;9156","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006308;GO:0006401;GO:0006281;GO:0006974;GO:0005634","GO.description":"DNA catabolic process;RNA catabolic process;DNA repair;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"01.03.16.03;01.03.16.01;10.01.05.01;32.01.09;70.10","FunCat.description":"DNA degradation;RNA degradation;DNA repair;DNA damage response;nucleus","PubMed.ID":11427529,"subunits.Protein.name.":"DNA mismatch repair protein Mlh1 ;Mismatch repair endonuclease PMS2 ;Exonuclease 1","subunits.Gene.name.":"MLH1;PMS2;EXO1","subunits.Gene.name.syn.":"COCA2;PMSL2;EXOI HEX1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors propose  the involvement of hExoI as a downstream effector in MMR (DNA mismatch repair) and/or DNA recombination.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":416,"ComplexName":"Nitric oxide synthase-dystrophin complex, skeletal muscle","Organism":"Mouse","Synonyms":"None","Cell.line":"striated muscle","subunits.UniProt.IDs.":"P11531;Q9Z0J4","subunits.Entrez.IDs.":"13405;18125","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies;MI:0096-pull down;MI:0019-coimmunoprecipitation","GO.ID":"GO:0007263;GO:0006936;GO:0005886","GO.description":"nitric oxide mediated signal transduction;muscle contraction;plasma membrane","FunCat.ID":"30.01.09.01;36.25.09;70.02","FunCat.description":"NO mediated signal transduction;muscle contraction;eukaryotic plasma membrane / membrane attached","PubMed.ID":7545544,"subunits.Protein.name.":"Dystrophin;Nitric oxide synthase, brain","subunits.Gene.name.":"Dmd;Nos1","subunits.Gene.name.syn.":"None;None","Disease.comment":"DMD is  involved in muscular dystrophy (Duchenne muscular dystrophy).","Subunits.comment":"None","Complex.comment":"The authors describe that  aberrant regulation of nNOS may contribute to preferential degeneration of fast-twitch muscle fibers in DMD.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":417,"ComplexName":"COX-2-Cav-3 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P35355;P51638","subunits.Entrez.IDs.":"29527;29161","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0030234;GO:0050790;GO:0005886","GO.description":"enzyme regulator activity;regulation of catalytic activity;plasma membrane","FunCat.ID":"18.02.01;70.02","FunCat.description":"enzymatic activity regulation / enzyme regulator;eukaryotic plasma membrane / membrane attached","PubMed.ID":16479074,"subunits.Protein.name.":"Prostaglandin G/H synthase 2 ;Caveolin-3","subunits.Gene.name.":"Ptgs2;Cav3","subunits.Gene.name.syn.":"Cox-2 Cox2;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Chondrocytes were stimulated with Cd.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":418,"ComplexName":"H/ACA ribonucleoprotein complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P40615;Q6AYA1;Q9CQS2;Q9CRB2","subunits.Entrez.IDs.":"170944;499709;66181;52530","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0071- molecular sieving","GO.ID":"GO:0009187;GO:0000154;GO:0005515;GO:0005730","GO.description":"cyclic nucleotide metabolic process;rRNA modification;protein binding;nucleolus","FunCat.ID":"01.03.10;11.06.01;16.01;70.10.07","FunCat.description":"metabolism of cyclic and unusual nucleotides;rRNA modification;protein binding;nucleolus","PubMed.ID":12446766,"subunits.Protein.name.":"H/ACA ribonucleoprotein complex subunit 4 ;H/ACA ribonucleoprotein complex subunit 1 ;H/ACA ribonucleoprotein complex subunit 3 ;H/ACA ribonucleoprotein complex subunit 2","subunits.Gene.name.":"Dkc1;Gar1;Nop10;Nhp2","subunits.Gene.name.syn.":"Nap57;Nola1;Nola3;Nola2","Disease.comment":"None","Subunits.comment":"Since Nhp2 and Nop10 from rat were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.","Complex.comment":"NAP57, GAR1, NHP2, and NOP10, and a snoRNA were apparently sufficient for site-specific pseudouridylation of synthetic rRNA substrates. Except for physiological concentration of salt, no exogenous factors were required for catalysis. The box H/ACA snoRNPs associated with phosphorylated but not dephosphorylated Nopp140 and were active in rRNA pseudouridylation independently of their Nopp140 association.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":419,"ComplexName":"Farnesyltransferase","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P49354;P49356","subunits.Entrez.IDs.":"2339;2342","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0006497;GO:0005515","GO.description":"protein lipidation;protein binding","FunCat.ID":"14.07.01;16.01","FunCat.description":"modification with fatty acids (e.g. myristylation, palmitylation, farnesylation);protein binding","PubMed.ID":11687658,"subunits.Protein.name.":"Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha ;Protein farnesyltransferase subunit beta","subunits.Gene.name.":"FNTA;FNTB","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":420,"ComplexName":"SAP97-Cav-3-Kv1.5 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS-7 cells, heart muscle","subunits.UniProt.IDs.":"P19024;P51637;Q811D0","subunits.Entrez.IDs.":"25470;12391;13383","Protein.complex.purification.method":"MI:0096-pull down","GO.ID":"GO:0006461;GO:0050789;GO:0005886","GO.description":"protein complex assembly;regulation of biological process;plasma membrane","FunCat.ID":"14.10;18;70.02","FunCat.description":"assembly of protein complexes;REGULATION OF METABOLISM AND PROTEIN FUNCTION;eukaryotic plasma membrane / membrane attached","PubMed.ID":15277200,"subunits.Protein.name.":"Potassium voltage-gated channel subfamily A member 5;Caveolin-3;Disks large homolog 1","subunits.Gene.name.":"Kcna5;Cav3;Dlg1","subunits.Gene.name.syn.":"None;None;Dlgh1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results show that a scaffolding complex containing Cav-3 and SAP97 can recruit Kv1.5 by means of multiple protein-protein interactions.","SWISSPROT.organism":"Rattus norvegicus (Rat);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":421,"ComplexName":"SAP97-Cav-3-Kv1.5 complex","Organism":"Rat","Synonyms":"None","Cell.line":"heart muscle","subunits.UniProt.IDs.":"P19024;P51638;Q62696","subunits.Entrez.IDs.":"25470;29161;25252","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006461;GO:0050789;GO:0005886","GO.description":"protein complex assembly;regulation of biological process;plasma membrane","FunCat.ID":"14.10;18;70.02","FunCat.description":"assembly of protein complexes;REGULATION OF METABOLISM AND PROTEIN FUNCTION;eukaryotic plasma membrane / membrane attached","PubMed.ID":15277200,"subunits.Protein.name.":"Potassium voltage-gated channel subfamily A member 5;Caveolin-3;Disks large homolog 1","subunits.Gene.name.":"Kcna5;Cav3;Dlg1","subunits.Gene.name.syn.":"None;None;Dlgh1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results show that a scaffolding complex containing Cav-3 and SAP97 can recruit Kv1.5 by means of multiple protein-protein interactions.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":422,"ComplexName":"Beta-dystroglycan-caveolin-3 complex","Organism":"Human","Synonyms":"None","Cell.line":"muscle","subunits.UniProt.IDs.":"P56539;Q14118","subunits.Entrez.IDs.":"859;1605","Protein.complex.purification.method":"MI:0096- pull down;MI:0019- coimmunoprecipitation;MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006461;GO:0005886","GO.description":"protein complex assembly;plasma membrane","FunCat.ID":"14.10;70.02","FunCat.description":"assembly of protein complexes;eukaryotic plasma membrane / membrane attached","PubMed.ID":10988290,"subunits.Protein.name.":"Caveolin-3 ;Dystroglycan","subunits.Gene.name.":"CAV3;DAG1","subunits.Gene.name.syn.":";","Disease.comment":"DAG1 is involved in muscular dystrophy and cardiomyopathy (PMID:15117830).","Subunits.comment":"None","Complex.comment":"Caveolin-3 can effectively block the interaction of dystrophin with beta -dystroglycan.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":423,"ComplexName":"EXO1-MLH1-PMS2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P40692;P54278;Q9UQ84","subunits.Entrez.IDs.":"4292;5395;9156","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006308;GO:0006401;GO:0006281;GO:0006974;GO:0005634","GO.description":"DNA catabolic process;RNA catabolic process;DNA repair;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"01.03.16.03;01.03.16.01;10.01.05.01;32.01.09;70.10","FunCat.description":"DNA degradation;RNA degradation;DNA repair;DNA damage response;nucleus","PubMed.ID":14676842,"subunits.Protein.name.":"DNA mismatch repair protein Mlh1 ;Mismatch repair endonuclease PMS2 ;Exonuclease 1","subunits.Gene.name.":"MLH1;PMS2;EXO1","subunits.Gene.name.syn.":"COCA2;PMSL2;EXOI HEX1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"EXO1 plays a role in events at the replication sites as well as a functional role in the DNA mismatch repair and/or recombination processes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":424,"ComplexName":"EXO1-MLH1-PCNA complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12004;P40692;Q9UQ84","subunits.Entrez.IDs.":"5111;4292;9156","Protein.complex.purification.method":"MI:0663- confocal microscopy","GO.ID":"GO:0006308;GO:0006401;GO:0006281;GO:0006974;GO:0005634","GO.description":"DNA catabolic process;RNA catabolic process;DNA repair;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"01.03.16.03;01.03.16.01;10.01.05.01;32.01.09;70.10","FunCat.description":"DNA degradation;RNA degradation;DNA repair;DNA damage response;nucleus","PubMed.ID":14676842,"subunits.Protein.name.":"Proliferating cell nuclear antigen;DNA mismatch repair protein Mlh1 ;Exonuclease 1","subunits.Gene.name.":"PCNA;MLH1;EXO1","subunits.Gene.name.syn.":"None;COCA2;EXOI HEX1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"EXO1 plays a role in events at the replication sites as well as a functional role in the DNA mismatch repair and/or recombination processes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":425,"ComplexName":"MSH4-MSH5-GPS2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15457;O43196;Q13227","subunits.Entrez.IDs.":"4438;4439;2874","Protein.complex.purification.method":"MI:0437- protein tri hybrid; MI:0007- anti tag coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0006281;GO:0007131;GO:0006974","GO.description":"DNA repair;reciprocal meiotic recombination;cellular response to DNA damage stimulus","FunCat.ID":"10.01.05.01;10.01.05.03.01;32.01.09","FunCat.description":"DNA repair;meiotic recombination;DNA damage response","PubMed.ID":16122992,"subunits.Protein.name.":"MutS protein homolog 4 ;MutS protein homolog 5 ;G protein pathway suppressor 2","subunits.Gene.name.":"MSH4;MSH5;GPS2","subunits.Gene.name.syn.":";;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The association with GPS2 is mediated through the interface of hMSH4-hMSH5 complex and the N-terminal region of GPS2.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":426,"ComplexName":"Meprin A","Organism":"Human","Synonyms":"PABA peptide hydrolase","Cell.line":"None","subunits.UniProt.IDs.":"Q16819;Q16820","subunits.Entrez.IDs.":"4224;4225","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0044257;GO:0005515;GO:0005886","GO.description":"cellular protein catabolic process;protein binding;plasma membrane","FunCat.ID":"14.13.01;16.01;70.02","FunCat.description":"cytoplasmic and nuclear protein degradation;protein binding;eukaryotic plasma membrane / membrane attached","PubMed.ID":8262185,"subunits.Protein.name.":"Meprin A subunit alpha ;Meprin A subunit beta","subunits.Gene.name.":"MEP1A;MEP1B","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":427,"ComplexName":"Tripeptidyl peptidase","Organism":"Mouse","Synonyms":"TPPII","Cell.line":"None","subunits.UniProt.IDs.":"Q64514","subunits.Entrez.IDs.":"22019","Protein.complex.purification.method":"MI:0226- ion exchange chromatography; MI:0071- molecular sieving","GO.ID":"GO:0044257;GO:0005737","GO.description":"cellular protein catabolic process;cytoplasm","FunCat.ID":"14.13.01;70.03","FunCat.description":"cytoplasmic and nuclear protein degradation;cytoplasm","PubMed.ID":9974389,"subunits.Protein.name.":"Tripeptidyl-peptidase 2","subunits.Gene.name.":"Tpp2","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TPPII is a homomeric high molecular-weight protease with an estimated mass between 5 and 9 MD. The particle is larger than the 26S proteasome and has a rod-shaped, dynamic supramolecular structure. TPPII exhibits enhanced activity in proteasome inhibitor-adapted cells and degrades polypeptides by exo- as well as predominantly trypsin-like endoproteolytic cleavage.","SWISSPROT.organism":"Mus musculus (Mouse)"}
{"ComplexID":428,"ComplexName":"Molybdopterin synthase","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O96007;O96033","subunits.Entrez.IDs.":"4338;4338","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0051191;GO:0009110;GO:0051188;GO:0005515","GO.description":"prosthetic group biosynthetic process;vitamin biosynthetic process;cofactor biosynthetic process;protein binding","FunCat.ID":"01.07.01;16.01","FunCat.description":"biosynthesis of vitamins, cofactors, and prosthetic groups;protein binding","PubMed.ID":12732628,"subunits.Protein.name.":"Molybdopterin synthase catalytic subunit ;Molybdopterin synthase sulfur carrier subunit","subunits.Gene.name.":"MOCS2;MOCS2","subunits.Gene.name.syn.":"MCBPE MOCO1;MOCO1","Disease.comment":"Human Moco deficiency leads to the pleiotropic loss of all three of these molybdoenzymes and usually progresses to death at an early age.","Subunits.comment":"None","Complex.comment":"Molybdenum cofactor (Moco)1 biosynthesis is an ancient, ubiquitous, and highly conserved pathway leading to the biochemical activation of molybdenum. Moco is essential for the activity of sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase in humans. MOCS2A and MOCS2B are encoded on a single bicistronic mRNA.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":429,"ComplexName":"Phosphatidylinositol 3-kinase complex (PIK3C3, PIK3R4)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q8NEB9;Q99570","subunits.Entrez.IDs.":"5289;30849","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0006468;GO:0006470;GO:0046777;GO:0005515;GO:0005524;GO:0007167;GO:0005886","GO.description":"intracellular protein transport;protein targeting;protein transport;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;protein binding;ATP binding;enzyme linked receptor protein signaling pathway;plasma membrane","FunCat.ID":"14.04;20.01.10;14.07.03;16.01;16.19.03;30.05.01;70.02","FunCat.description":"protein targeting, sorting and translocation;protein transport;modification by phosphorylation, dephosphorylation, autophosphorylation;protein binding;ATP binding;receptor enzyme mediated signalling;eukaryotic plasma membrane / membrane attached","PubMed.ID":7628435,"subunits.Protein.name.":"Phosphatidylinositol 3-kinase catalytic subunit type 3;Phosphoinositide 3-kinase regulatory subunit 4","subunits.Gene.name.":"PIK3C3;PIK3R4","subunits.Gene.name.syn.":"VPS34;VPS15","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The homologous Vps34p-Vps15p complex in yeast mediates protein trafficking.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":430,"ComplexName":"18S U11/U12 snRNP","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43143;O75533;P14678;P62304;P62306;P62308;P62314;P62316;P62318;P67809;Q13435;Q15393;Q15427;Q15696;Q16560;Q6IEG0;Q6P2Q9;Q8N8D1;Q8TBF4;Q96LT9;Q9BV90;Q9BWJ5;Q9UDW3;Q9Y3B4","subunits.Entrez.IDs.":"1665;23451;6628;6635;6636;6637;6632;6633;6634;4904;10992;23450;10262;8233;11066;154007;10594;10081;85437;55599;79622;83443;55954;51639","Protein.complex.purification.method":"MI:0069- mass spectrometry studies of complexes; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0000398;GO:0006397;GO:0005634","GO.description":"mRNA splicing, via spliceosome;mRNA processing;nucleus","FunCat.ID":"11.04.03;70.10","FunCat.description":"mRNA processing (splicing, 5'-, 3'-end processing);nucleus","PubMed.ID":15146077,"subunits.Protein.name.":"Pre-mRNA-splicing factor ATP-dependent RNA helicase DHX15 ;Splicing factor 3B subunit 1 ;Small nuclear ribonucleoprotein-associated proteins B and B' ;Small nuclear ribonucleoprotein E ;Small nuclear ribonucleoprotein F ;Small nuclear ribonucleoprotein G ;Small nuclear ribonucleoprotein Sm D1 ;Small nuclear ribonucleoprotein Sm D2 ;Small nuclear ribonucleoprotein Sm D3 ;Nuclease-sensitive element-binding protein 1 ;Splicing factor 3B subunit 2 ;Splicing factor 3B subunit 3;Splicing factor 3B subunit 4 ;U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2 ;U11/U12 small nuclear ribonucleoprotein 35 kDa protein ;U11/U12 small nuclear ribonucleoprotein 48 kDa protein ;Pre-mRNA-processing-splicing factor 8 ;Programmed cell death protein 7 ;Zinc finger CCHC-type and RNA-binding motif-containing protein 1 ;RNA-binding protein 40 ;U11/U12 small nuclear ribonucleoprotein 25 kDa protein ;Splicing factor 3B subunit 5 ;Zinc finger matrin-type protein 5 ;Splicing factor 3B subunit 6","subunits.Gene.name.":"DHX15;SF3B1;SNRPB;SNRPE;SNRPF;SNRPG;SNRPD1;SNRPD2;SNRPD3;YBX1;SF3B2;SF3B3;SF3B4;ZRSR2;SNRNP35;SNRNP48;PRPF8;PDCD7;ZCRB1;RNPC3;SNRNP25;SF3B5;ZMAT5;SF3B6","subunits.Gene.name.syn.":"DBP1 DDX15;SAP155;COD SNRPB1;;PBSCF;PBSCG;;SNRPD1;;NSEP1 YB1;SAP145;KIAA0017 SAP130;SAP49;U2AF1-RS2 U2AF1L2 U2AF1RS2 URP;HM1 U1SNRNPBP;C6orf151;PRPC8;;;KIAA1839 RBM40 RNP;C16orf33;SF3B10;;SAP14 SF3B14 SF3B14A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"U12-type spliceosomes excise U12-type introns, which comprise less than 1% of all human introns.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":431,"ComplexName":"MSH2-MSH6-PMS2-MLH1 complex","Organism":"Human","Synonyms":"MutS(alpha)-MutL(alpha)-heteroduplex complex","Cell.line":"None","subunits.UniProt.IDs.":"P40692;P43246;P52701;P54278","subunits.Entrez.IDs.":"4292;4436;2956;5395","Protein.complex.purification.method":"MI:0107- surface plasmon resonance","GO.ID":"GO:0006281;GO:0003677;GO:0005524;GO:0006974;GO:0005634","GO.description":"DNA repair;DNA binding;ATP binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;16.03.01;16.19.03;32.01.09;70.10","FunCat.description":"DNA repair;DNA binding;ATP binding;DNA damage response;nucleus","PubMed.ID":11441019,"subunits.Protein.name.":"DNA mismatch repair protein Mlh1 ;DNA mismatch repair protein Msh2 ;DNA mismatch repair protein Msh6 ;Mismatch repair endonuclease PMS2","subunits.Gene.name.":"MLH1;MSH2;MSH6;PMS2","subunits.Gene.name.syn.":"COCA2;;GTBP;PMSL2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"MutS-alpha-MutL-alpha-heteroduplex complex requires DNA mismatch and ATP hydrolysis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":432,"ComplexName":"N-NOS-CHIP-HSP70-1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P0DMV8;P29475;Q9UNE7","subunits.Entrez.IDs.":"3303;4842;10273","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0043161;GO:0006511;GO:0005737","GO.description":"proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;cytoplasm","FunCat.ID":"14.13.01.01;70.03","FunCat.description":"proteasomal degradation (ubiquitin/proteasomal pathway);cytoplasm","PubMed.ID":15466472,"subunits.Protein.name.":"Heat shock 70 kDa protein 1A;Nitric oxide synthase, brain;E3 ubiquitin-protein ligase CHIP","subunits.Gene.name.":"HSPA1A;NOS1;STUB1","subunits.Gene.name.syn.":"HSPA1, HSX70, HSP70-1A;None;CHIP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cells for analysis were treated with lactacystin, a selective inhibitor of the proteasome. The authors found that CHIP acts to ubiquitylate nNOS and that hsp70 and hsp40 can facilitate this conjugation reaction.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":433,"ComplexName":"BASC complex (BRCA1-associated genome surveillance complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60934;P35249;P35250;P35251;P38398;P40692;P43246;P49959;P52701;P54132;Q13315;Q92878","subunits.Entrez.IDs.":"4683;5984;5982;5981;672;4292;4436;4361;2956;641;472;10111","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0226- ion exchange chromatography; MI:0019- coimmunoprecipitation","GO.ID":"GO:0006281;GO:0006974;GO:0005634","GO.description":"DNA repair;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;32.01.09;70.10","FunCat.description":"DNA repair;DNA damage response;nucleus","PubMed.ID":10783165,"subunits.Protein.name.":"Nibrin ;Replication factor C subunit 4;Replication factor C subunit 2;Replication factor C subunit 1;Breast cancer type 1 susceptibility protein;DNA mismatch repair protein Mlh1 ;DNA mismatch repair protein Msh2 ;Double-strand break repair protein MRE11A ;DNA mismatch repair protein Msh6 ;Bloom syndrome protein ;Serine-protein kinase ATM ;DNA repair protein RAD50","subunits.Gene.name.":"NBN;RFC4;RFC2;RFC1;BRCA1;MLH1;MSH2;MRE11A;MSH6;BLM;ATM;RAD50","subunits.Gene.name.syn.":"NBS NBS1 P95;None;None;RFC140;RNF53;COCA2;;HNGS1 MRE11;GTBP;RECQ2 RECQL3;;","Disease.comment":"BRCA1 is involved in breast cancer.","Subunits.comment":"None","Complex.comment":"The BASC complex may serve as a sensor for DNA damage.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":434,"ComplexName":"BASC (Ab 80) complex (BRCA1-associated genome surveillance complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P35249;P35250;P35251;P38398;P40692;P43246;P52701;P54132","subunits.Entrez.IDs.":"5984;5982;5981;672;4292;4436;2956;641","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006281;GO:0006974;GO:0005634","GO.description":"DNA repair;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;32.01.09;70.10","FunCat.description":"DNA repair;DNA damage response;nucleus","PubMed.ID":10783165,"subunits.Protein.name.":"Replication factor C subunit 4;Replication factor C subunit 2;Replication factor C subunit 1;Breast cancer type 1 susceptibility protein;DNA mismatch repair protein Mlh1 ;DNA mismatch repair protein Msh2 ;DNA mismatch repair protein Msh6 ;Bloom syndrome protein","subunits.Gene.name.":"RFC4;RFC2;RFC1;BRCA1;MLH1;MSH2;MSH6;BLM","subunits.Gene.name.syn.":"None;None;RFC140;RNF53;COCA2;;GTBP;RECQ2 RECQL3","Disease.comment":"BRCA1 is involved in breast cancer.","Subunits.comment":"None","Complex.comment":"For isolation of the BASC complex (Ab 80), polyclonal antibodies against GST-BRCA1 1021-1552 were used.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":435,"ComplexName":"BASC (Ab 81) complex (BRCA1-associated genome surveillance complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P35249;P35250;P35251;P38398;P40692;Q13315","subunits.Entrez.IDs.":"5984;5982;5981;672;4292;472","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0226- ion exchange chromatography; MI:0019- coimmunoprecipitation","GO.ID":"GO:0006281;GO:0006974;GO:0005634","GO.description":"DNA repair;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;32.01.09;70.10","FunCat.description":"DNA repair;DNA damage response;nucleus","PubMed.ID":10783165,"subunits.Protein.name.":"Replication factor C subunit 4;Replication factor C subunit 2;Replication factor C subunit 1;Breast cancer type 1 susceptibility protein;DNA mismatch repair protein Mlh1 ;Serine-protein kinase ATM","subunits.Gene.name.":"RFC4;RFC2;RFC1;BRCA1;MLH1;ATM","subunits.Gene.name.syn.":"None;None;RFC140;RNF53;COCA2;","Disease.comment":"BRCA1 is involved in breast cancer.","Subunits.comment":"None","Complex.comment":"For isolation of the BASC complex (Ab 81), polyclonal antibodies against GST-BRCA1 1501-1861 were used.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":436,"ComplexName":"BASC (Ab C-20) complex (BRCA1-associated genome surveillance complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P38398;P52701;Q92878","subunits.Entrez.IDs.":"672;2956;10111","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006281;GO:0006974;GO:0005634","GO.description":"DNA repair;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;32.01.09;70.10","FunCat.description":"DNA repair;DNA damage response;nucleus","PubMed.ID":10783165,"subunits.Protein.name.":"Breast cancer type 1 susceptibility protein;DNA mismatch repair protein Msh6 ;DNA repair protein RAD50","subunits.Gene.name.":"BRCA1;MSH6;RAD50","subunits.Gene.name.syn.":"RNF53;GTBP;","Disease.comment":"BRCA1 is involved in breast cancer.","Subunits.comment":"None","Complex.comment":"For isolation of the BASC complex (Ab C-20), polyclonal antibodies against the carboxy-terminal epitope of BRCA1 were used.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":437,"ComplexName":"AQP2-binding multiprotein force generator complex","Organism":"Rat","Synonyms":"None","Cell.line":"kidney","subunits.UniProt.IDs.":"D3ZRD9;P13832;P16086;P18666;P34080;P48037;P60711;P63259;Q07936;Q62812;Q63610;Q68FP1;Q6I7S1;Q7TQ08;Q9QXQ0","subunits.Entrez.IDs.":"362107;501203;64159;50685;25386;79125;81822;287876;56611;25745;117557;296654;None;298975;63836","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0015267;GO:0050801;GO:0006873;GO:0005886","GO.description":"intracellular protein transport;protein targeting;protein transport;channel activity;ion homeostasis;cellular ion homeostasis;plasma membrane","FunCat.ID":"14.04;20.01.10;20.03.01;34.01;70.02","FunCat.description":"protein targeting, sorting and translocation;protein transport;channel / pore class transport;homeostasis;eukaryotic plasma membrane / membrane attached","PubMed.ID":15823548,"subunits.Protein.name.":"Protein Aif1l;Myosin regulatory light chain RLC-A;Spectrin alpha chain, non-erythrocytic 1;Myosin regulatory light chain 12B;Aquaporin-2;Annexin A6;Actin, cytoplasmic 1;Actin, cytoplasmic 2;Annexin A2;Myosin-9;Tropomyosin alpha-3 chain;Gelsolin;GTPase-activating protein;Scinderin;Alpha-actinin-4","subunits.Gene.name.":"Aif1l;Rlc-a;Sptan1;Myl12b;Aqp2;Anxa6;Actb;Actg1;Anxa2;Myh9;Tpm3;Gsn;Sipa1;Scin;Actn4","subunits.Gene.name.syn.":"RGD1305081_predicted, rCG_45851;None;Spna2 Spta2;Mrlc2 Mrlcb Mylc2b;None;Anx6;None;Actg;Anx2;None;Tpm5;None;SPA-1;Scind;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":438,"ComplexName":"GCN5-TRRAP histone acetyltransferase complex","Organism":"Human","Synonyms":"GCN5-TRRAP-HAT complex","Cell.line":"None","subunits.UniProt.IDs.":"O75486;O75528;O75529;P38398;P43246;P52701;Q12962;Q16594;Q92830;Q9Y4A5","subunits.Entrez.IDs.":"8464;10474;27097;672;4436;2956;6881;6880;2648;8295","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006281;GO:0006265;GO:2001141;GO:0006355;GO:0006974;GO:0051276","GO.description":"DNA repair;DNA topological change;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;cellular response to DNA damage stimulus;chromosome organization","FunCat.ID":"10.01.05.01;10.01.09.05;11.02.03.04;32.01.09;42.10.03","FunCat.description":"DNA repair;DNA conformation modification (e.g. chromatin);transcriptional control;DNA damage response;organization of chromosome structure","PubMed.ID":16260778,"subunits.Protein.name.":"Transcription initiation protein SPT3 homolog;Transcriptional adapter 3;TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L;Breast cancer type 1 susceptibility protein;DNA mismatch repair protein Msh2 ;DNA mismatch repair protein Msh6 ;Transcription initiation factor TFIID subunit 10;Transcription initiation factor TFIID subunit 9;Histone acetyltransferase KAT2A;Transformation/transcription domain-associated protein","subunits.Gene.name.":"SUPT3H;TADA3;TAF5L;BRCA1;MSH2;MSH6;TAF10;TAF9;KAT2A;TRRAP","subunits.Gene.name.syn.":"SPT3;ADA3, TADA3L;PAF65B;RNF53;;GTBP;TAF2A TAF2H TAFII30;TAF2G TAFII31;GCN5, GCN5L2, HGCN5;PAF400","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"hGCN5/TRRAP HAT complex subclass is required for the multiple functions of BRCA1 (PMID:16260778).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":439,"ComplexName":"Phosphatidylinositol 3-kinase complex (PIK3CA, PIK3R1)","Organism":"Bovine","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P23727;P32871","subunits.Entrez.IDs.":"282307;282306","Protein.complex.purification.method":"MI:0226- ion exchange chromatography; MI:0004- affinity chromatography technologies","GO.ID":"GO:0005515;GO:0005524;GO:0007169;GO:0005886","GO.description":"protein binding;ATP binding;transmembrane receptor protein tyrosine kinase signaling pathway;plasma membrane","FunCat.ID":"16.01;16.19.03;30.05.01.12;70.02","FunCat.description":"protein binding;ATP binding;transmembrane receptor protein tyrosine kinase signalling pathways;eukaryotic plasma membrane / membrane attached","PubMed.ID":8383968,"subunits.Protein.name.":"Phosphatidylinositol 3-kinase regulatory subunit alpha ;Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform","subunits.Gene.name.":"PIK3R1;PIK3CA","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Phosphatidylinositol 3-kinases (PI3Ks) are lipid kinases that phosphorylate phosphatidylinositol 4,5-bisphosphate at the 3-position of the inositol ring, and thus generate phosphatidylinositol 3,4,5-trisphosphate (PIP3 ), which, in turn, initiates a vast array of signaling events. PI3Ks are heterodimers, composed of catalytic and regulatory subunits, that are activated by growth factor-receptor tyrosine kinases.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":440,"ComplexName":"Succinate dehydrogenase complex II, mitochondrial","Organism":"Mouse","Synonyms":"Succinate ubiquinone oxidoreductase; Succinate dehydrogenase complex II (EC 1.3.5.1), mitochondrial","Cell.line":"None","subunits.UniProt.IDs.":"Q8K2B3;Q9CQA3;Q9CXV1;Q9CZB0","subunits.Entrez.IDs.":"66945;67680;66925;66052","Protein.complex.purification.method":"MI:0069-mass spectrometry studies of complexes;MI:0019-coimmunoprecipitation","GO.ID":"GO:0019751;GO:0019752;GO:0009313;GO:0016139;GO:0006091;GO:0051536;GO:0006818;GO:0022904;GO:0005743","GO.description":"polyol metabolic process;carboxylic acid metabolic process;oligosaccharide catabolic process;glycoside catabolic process;generation of precursor metabolites and energy;iron-sulfur cluster binding;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01.05.02.07;01;16.21.08;20.01.15;02.11.07;70.16.05","FunCat.description":"sugar, glucoside, polyol and carboxylate catabolism;METABOLISM;Fe/S binding;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":16120479,"subunits.Protein.name.":"Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial;Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial;Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial;Succinate dehydrogenase cytochrome b560 subunit, mitochondrial","subunits.Gene.name.":"Sdha;Sdhb;Sdhd;Sdhc","subunits.Gene.name.syn.":"None;None;None;None","Disease.comment":"Paraganglioma syndrome type 4 is caused by a mutation in the SDHB gene (PMID:17143317).","Subunits.comment":"None","Complex.comment":"The enzyme complex is a heterotetramer divided into three domains: SDHA, the catalytic domain; SDHB, the electron transfer subunit; SDHC/SDHD, the dimeric membrane anchor that contains beta-type heme.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":441,"ComplexName":"TFTC-type histone acetyl transferase complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60244;O75448;P03372;Q15648;Q92830;Q93074;Q9NVC6;Q9UHV7;Q9ULK4;Q9Y2X0;Q9Y4A5","subunits.Entrez.IDs.":"9282;9862;2099;5469;2648;9968;9440;9969;9439;10025;8295","Protein.complex.purification.method":"MI:0091- chromatography technologies;MI:0029- cosedimentation through density gradients;MI:0096- pull down","GO.ID":"GO:0006265;GO:2001141;GO:0006355;GO:0006473;GO:0006476;GO:0023052;GO:0051276;GO:0005634;GO:0005102","GO.description":"DNA topological change;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;signaling;chromosome organization;nucleus;receptor binding","FunCat.ID":"10.01.09.05;11.02.03.04;14.07.04;30.01;42.10.03;70.10;16.01.01","FunCat.description":"DNA conformation modification (e.g. chromatin);transcriptional control;modification by acetylation, deacetylation;cellular signalling;organization of chromosome structure;nucleus;receptor binding","PubMed.ID":11931763,"subunits.Protein.name.":"Mediator of RNA polymerase II transcription subunit 14;Mediator of RNA polymerase II transcription subunit 24;Estrogen receptor;Mediator of RNA polymerase II transcription subunit 1;Histone acetyltransferase KAT2A;Mediator of RNA polymerase II transcription subunit 12;Mediator of RNA polymerase II transcription subunit 17;Mediator of RNA polymerase II transcription subunit 13 ;Mediator of RNA polymerase II transcription subunit 23 ;Mediator of RNA polymerase II transcription subunit 16;Transformation/transcription domain-associated protein","subunits.Gene.name.":"MED14;MED24;ESR1;MED1;KAT2A;MED12;MED17;MED13;MED23;MED16;TRRAP","subunits.Gene.name.syn.":"ARC150 CRSP2 CXorf4 DRIP150 EXLM1 RGR1 TRAP170;ARC100 CRSP4 DRIP100 KIAA0130 THRAP4 TRAP100;ESR, NR3A1;ARC205 CRSP1 CRSP200 DRIP205 DRIP230 PBP PPARBP PPARGBP RB18A TRAP220 TRIP2;GCN5, GCN5L2, HGCN5;ARC240 CAGH45 HOPA KIAA0192 TNRC11 TRAP230;ARC77 CRSP6 DRIP77 DRIP80 TRAP80;ARC250 KIAA0593 THRAP1 TRAP240;ARC130 CRSP3 DRIP130 KIAA1216 SUR2;DRIP92 THRAP5;PAF400","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex is a coactivator of estrogen receptor alpha (ERalpha).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":442,"ComplexName":"Vacuolar ATPase","Organism":"Bovine","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O46563;P11019;P21282;P23956;P31404;P31408;P39942;P61420;P79251;Q28029;Q29466","subunits.Entrez.IDs.":"282657;287017;338089;550622;282147;338082;404152;282148;281641;282405;286768","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006195;GO:0006145;GO:0005515;GO:0008324;GO:0006812;GO:0042626;GO:0016192;GO:0005886","GO.description":"purine nucleotide catabolic process;purine nucleobase catabolic process;protein binding;cation transmembrane transporter activity;cation transport;ATPase activity, coupled to transmembrane movement of substances;vesicle-mediated transport;plasma membrane","FunCat.ID":"01.03.01.01;16.01;20.01.01.01;20.03.22;20.09.07;70.02","FunCat.description":"purine nucleotide /nucleoside/nucleobase catabolism;protein binding;cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);transport ATPases;vesicular transport (Golgi network, etc.);eukaryotic plasma membrane / membrane attached","PubMed.ID":15269204,"subunits.Protein.name.":"V-type proton ATPase subunit H;V-type proton ATPase subunit E 1;V-type proton ATPase subunit C 1;V-type proton ATPase 16 kDa proteolipid subunit;V-type proton ATPase catalytic subunit A;V-type proton ATPase subunit B, brain isoform;V-type proton ATPase subunit D;V-type proton ATPase subunit d 1;V-type proton ATPase subunit G 1;V-type proton ATPase subunit F;V-type proton ATPase 116 kDa subunit a isoform 1","subunits.Gene.name.":"ATP6V1H;ATP6V1E1;ATP6V1C1;ATP6V0C;ATP6V1A;ATP6V1B2;ATP6V1D;ATP6V0D1;ATP6V1G1;ATP6V1F;ATP6V0A1","subunits.Gene.name.syn.":"None;ATP6E;ATP6C VATC;ATP6C ATP6L;ATP6A1 ATP6V1A1;ATP6B2;ATP6M VATD;ATP6D VPATPD;ATP6G ATP6G1;ATP6S14 VATF;ATP6N1 VPP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The complex is found in both the endomembrane system of subcellular organelles and the plasma membrane of certain specialized cells.The function of the V-ATPase is to pump protons across the membrane bilayer, a process powered by hydrolysis of ATP.The V-ATPase is a large, multisubunit complex that can be divided into three domains: a water-soluble V1, which is responsible for binding and hydrolysis of ATP; a membrane embedded V0, which contains the proton translocation pore; and a stalk domain, which functions as a structural and functional connection between the V1 and V0.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":443,"ComplexName":"BP-SMAD complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14867;O15198;O95452;P17980;P19447;P50539;Q13118;Q15582","subunits.Entrez.IDs.":"571;4093;10804;5702;2071;4601;7071;7045","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0045893;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;nucleus","FunCat.ID":"11.02.03.04.01;70.10","FunCat.description":"transcription activation;nucleus","PubMed.ID":16101586,"subunits.Protein.name.":"Transcription regulator protein BACH1 ;Mothers against decapentaplegic homolog 9 ;Gap junction beta-6 protein ;26S protease regulatory subunit 6A ;TFIIH basal transcription factor complex helicase XPB subunit ;Max-interacting protein 1 ;Krueppel-like factor 10 ;Transforming growth factor-beta-induced protein ig-h3","subunits.Gene.name.":"BACH1;SMAD9;GJB6;PSMC3;ERCC3;MXI1;KLF10;TGFBI","subunits.Gene.name.syn.":";MADH6 MADH9;;TBP1;XPB XPBC;BHLHC11;TIEG TIEG1;BIGH3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Homozygous knockout mice for the homeobox protein Msx1 (Hox7) die at birth exhibiting severe abnormalities limited to the craniofacial region, including a complete cleft of the secondary palate. Results suggest that the BP-SMAD complex is required for transcriptional activation of the mouse Msx1 gene.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":444,"ComplexName":"Signal peptidase complex","Organism":"Dog","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P13679;P61008;P67811;P83362;Q28250","subunits.Entrez.IDs.":"404003;404005;404004;None;404016","Protein.complex.purification.method":"MI:0401- biochemical","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0005515;GO:0008565;GO:0005783","GO.description":"intracellular protein transport;protein targeting;protein transport;protein binding;protein transporter activity;endoplasmic reticulum","FunCat.ID":"14.04;20.01.10;16.01;70.07","FunCat.description":"protein targeting, sorting and translocation;protein transport;protein binding;endoplasmic reticulum","PubMed.ID":8632014,"subunits.Protein.name.":"Signal peptidase complex catalytic subunit SEC11C ;Signal peptidase complex subunit 3 ;Signal peptidase complex catalytic subunit SEC11A ;Signal peptidase complex subunit 1 ;Signal peptidase complex subunit 2","subunits.Gene.name.":"SEC11C;SPCS3;SEC11A;SPCS1;SPCS2","subunits.Gene.name.syn.":"SEC11L3 SPC21;SPC22;SEC11L1 SPC18;SPC12;SPC25","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Canis lupus familiaris (Dog) (Canis familiaris);Canis lupus familiaris (Dog) (Canis familiaris);Canis lupus familiaris (Dog) (Canis familiaris);Canis lupus familiaris (Dog) (Canis familiaris);Canis lupus familiaris (Dog) (Canis familiaris)"}
{"ComplexID":445,"ComplexName":"TFTC complex (TATA-binding protein-free TAF-II-containing complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00268;O15265;O75486;O75528;O75529;P49848;Q12962;Q15393;Q15542;Q15545;Q16514;Q16594;Q6P1X5;Q92830;Q9Y4A5;Q9Y6J9","subunits.Entrez.IDs.":"6874;6314;8464;10474;27097;6878;6881;23450;6877;6879;6883;6880;6873;2648;8295;10629","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006265;GO:0006352;GO:0045893;GO:0006473;GO:0006476;GO:0051276;GO:0005634","GO.description":"DNA topological change;DNA-templated transcription, initiation;positive regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.01.01;11.02.03.04.01;14.07.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription initiation;transcription activation;modification by acetylation, deacetylation;organization of chromosome structure;nucleus","PubMed.ID":10373431,"subunits.Protein.name.":"Transcription initiation factor TFIID subunit 4;Ataxin-7;Transcription initiation protein SPT3 homolog;Transcriptional adapter 3;TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L;Transcription initiation factor TFIID subunit 6;Transcription initiation factor TFIID subunit 10;Splicing factor 3B subunit 3;Transcription initiation factor TFIID subunit 5;Transcription initiation factor TFIID subunit 7;Transcription initiation factor TFIID subunit 12;Transcription initiation factor TFIID subunit 9;Transcription initiation factor TFIID subunit 2 ;Histone acetyltransferase KAT2A;Transformation/transcription domain-associated protein;TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L","subunits.Gene.name.":"TAF4;ATXN7;SUPT3H;TADA3;TAF5L;TAF6;TAF10;SF3B3;TAF5;TAF7;TAF12;TAF9;TAF2;KAT2A;TRRAP;TAF6L","subunits.Gene.name.syn.":"TAF2C TAF2C1 TAF4A TAFII130 TAFII135;SCA7;SPT3;ADA3, TADA3L;PAF65B;TAF2E TAFII70;TAF2A TAF2H TAFII30;KIAA0017 SAP130;TAF2D;TAF2F TAFII55;TAF15 TAF2J TAFII20;TAF2G TAFII31;CIF150 TAF2B;GCN5, GCN5L2, HGCN5;PAF400;PAF65A","Disease.comment":"None","Subunits.comment":"Three other subunits of the complex were found in the analysis, which have not been further characterized. In following publications these proteins were identified as ataxin-7, splicing factor 3B subunit 3 and PAF65A.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":446,"ComplexName":"Succinate dehydrogenase complex II, mitochondrial","Organism":"Bovine","Synonyms":"Succinate ubiquinone oxidoreductase; Succinate dehydrogenase complex II (EC 1.3.5.1), mitochondrial","Cell.line":"None","subunits.UniProt.IDs.":"P31039;P35720;Q3T189;Q95123","subunits.Entrez.IDs.":"281480;None;286840;281481","Protein.complex.purification.method":"MI:0069-mass spectrometry studies of complexes;MI:0019-coimmunoprecipitation","GO.ID":"GO:0019751;GO:0019752;GO:0009313;GO:0016139;GO:0006091;GO:0051536;GO:0006818;GO:0022904;GO:0005743","GO.description":"polyol metabolic process;carboxylic acid metabolic process;oligosaccharide catabolic process;glycoside catabolic process;generation of precursor metabolites and energy;iron-sulfur cluster binding;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01.05.02.07;01;16.21.08;20.01.15;02.11.07;70.16.05","FunCat.description":"sugar, glucoside, polyol and carboxylate catabolism;METABOLISM;Fe/S binding;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":16120479,"subunits.Protein.name.":"Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial;Succinate dehydrogenase cytochrome b560 subunit, mitochondrial;Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial;Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial","subunits.Gene.name.":"SDHA;SDHC;SDHB;SDHD","subunits.Gene.name.syn.":"SDH2 SDHFP1;CYB560;None;SDH4","Disease.comment":"Paraganglioma syndrome type 4 is caused by a mutation in the SDHB gene (PMID:17143317).","Subunits.comment":"None","Complex.comment":"The enzyme complex is a heterotetramer divided into three domains: SDHA, the catalytic domain; SDHB, the electron transfer subunit; SDHC/SDHD, the dimeric membrane anchor that contains beta-type heme.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":447,"ComplexName":"Kir4.1-dystrophin complex, retinal Mueller cells","Organism":"Rat","Synonyms":"None","Cell.line":"retinal Mueller cells","subunits.UniProt.IDs.":"P11530;P49655","subunits.Entrez.IDs.":"24907;29718","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0030-cross-linking studies","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;eukaryotic plasma membrane / membrane attached","PubMed.ID":16206160,"subunits.Protein.name.":"Dystrophin;ATP-sensitive inward rectifier potassium channel 10","subunits.Gene.name.":"Dmd;Kcnj10","subunits.Gene.name.syn.":"None;Kab-2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors describe that interactions between the DGC, Kir4.1, and AQP4 may influence the efficiency of the glial (K+)o buffering function.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":448,"ComplexName":"Kir4.1-alpha-syntrophin complex, retinal Mueller cells","Organism":"Rat","Synonyms":"None","Cell.line":"retinal Mueller cells","subunits.UniProt.IDs.":"P49655;Q498T0","subunits.Entrez.IDs.":"29718;362242","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0030-cross-linking studies","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;eukaryotic plasma membrane / membrane attached","PubMed.ID":16206160,"subunits.Protein.name.":"ATP-sensitive inward rectifier potassium channel 10;Snta1 protein","subunits.Gene.name.":"Kcnj10;Snta1","subunits.Gene.name.syn.":"Kab-2;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors describe that interactions between the DGC, Kir4.1, and AQP4 may influence the efficiency of the glial (K+)o buffering function.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":449,"ComplexName":"Kir4.1-beta-dystroglycan complex, retinal Mueller cells","Organism":"Rat","Synonyms":"None","Cell.line":"retinal Mueller cells","subunits.UniProt.IDs.":"P49655;Q91XP6","subunits.Entrez.IDs.":"29718;114489","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0030-cross-linking studies","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;eukaryotic plasma membrane / membrane attached","PubMed.ID":16206160,"subunits.Protein.name.":"ATP-sensitive inward rectifier potassium channel 10;Dystroglycan 1","subunits.Gene.name.":"Kcnj10;Dag1","subunits.Gene.name.syn.":"Kab-2;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors describe that interactions between the DGC, Kir4.1, and AQP4 may influence the efficiency of the glial (K+)o buffering function.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":450,"ComplexName":"Kir4.1-Aqp4 complex, retinal Mueller cells","Organism":"Rat","Synonyms":"None","Cell.line":"retinal Mueller cells","subunits.UniProt.IDs.":"P47863;P49655","subunits.Entrez.IDs.":"25293;29718","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0030-cross-linking studies","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;eukaryotic plasma membrane / membrane attached","PubMed.ID":16206160,"subunits.Protein.name.":"Aquaporin-4;ATP-sensitive inward rectifier potassium channel 10","subunits.Gene.name.":"Aqp4;Kcnj10","subunits.Gene.name.syn.":"None;Kab-2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors describe that interactions between the DGC, Kir4.1, and AQP4 may influence the efficiency of the glial (K+)o buffering function.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":451,"ComplexName":"Kir4.1-dystrobrevin complex, retinal Mueller cells","Organism":"Rat","Synonyms":"None","Cell.line":"retinal Mueller cells","subunits.UniProt.IDs.":"P49655;P84060","subunits.Entrez.IDs.":"29718;362715","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0030-cross-linking studies","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;eukaryotic plasma membrane / membrane attached","PubMed.ID":16206160,"subunits.Protein.name.":"ATP-sensitive inward rectifier potassium channel 10;Dystrobrevin beta","subunits.Gene.name.":"Kcnj10;Dtnb","subunits.Gene.name.syn.":"Kab-2;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors describe that interactions between the DGC, Kir4.1, and AQP4 may influence the efficiency of the glial (K+)o buffering function.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":452,"ComplexName":"Aqp4-alpha-syntrophin complex, retinal Mueller cells","Organism":"Rat","Synonyms":"None","Cell.line":"retinal Mueller cells","subunits.UniProt.IDs.":"P47863;Q498T0","subunits.Entrez.IDs.":"25293;362242","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0030-cross-linking studies","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;eukaryotic plasma membrane / membrane attached","PubMed.ID":16206160,"subunits.Protein.name.":"Aquaporin-4;Snta1 protein","subunits.Gene.name.":"Aqp4;Snta1","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors describe that interactions between the DGC, Kir4.1, and AQP4 may influence the efficiency of the glial (K+)o buffering function.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":453,"ComplexName":"Aqp4-beta-dystroglycan complex, retinal Mueller cells","Organism":"Rat","Synonyms":"None","Cell.line":"retinal Mueller cells","subunits.UniProt.IDs.":"P47863;Q91XP6","subunits.Entrez.IDs.":"25293;114489","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0030-cross-linking studies","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;eukaryotic plasma membrane / membrane attached","PubMed.ID":16206160,"subunits.Protein.name.":"Aquaporin-4;Dystroglycan 1","subunits.Gene.name.":"Aqp4;Dag1","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors describe that interactions between the DGC, Kir4.1, and AQP4 may influence the efficiency of the glial (K+)o buffering function.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":454,"ComplexName":"MKP3-CK2alpha complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q60737;Q9DBB1","subunits.Entrez.IDs.":"12995;67603","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0018- two hybrid","GO.ID":"GO:0030234;GO:0050790;GO:0035556;GO:0030182;GO:0007420","GO.description":"enzyme regulator activity;regulation of catalytic activity;intracellular signal transduction;neuron differentiation;brain development","FunCat.ID":"18.02.01;30.01;43.03.13;47.03.01.01.01","FunCat.description":"enzymatic activity regulation / enzyme regulator;cellular signalling;neuron;brain","PubMed.ID":15284227,"subunits.Protein.name.":"Casein kinase II subunit alpha;Dual specificity protein phosphatase 6","subunits.Gene.name.":"Csnk2a1;Dusp6","subunits.Gene.name.syn.":"Ckiia;Mkp3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex can include ERK2 protein. CK2 can selectively phosphorylate MKP3, suggesting cross-regulation between CK2alpha and MKP3, as well as a modulation of ERK2-MAPK signaling by CK2alpha via MKP3.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":455,"ComplexName":"TFTC complex (TATA-binding protein-free TAF-II-containing complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00268;O15265;O75486;O75528;O75529;P49848;Q12962;Q15393;Q15542;Q15545;Q16514;Q16594;Q6P1X5;Q92830;Q9Y4A5;Q9Y6J9","subunits.Entrez.IDs.":"6874;6314;8464;10474;27097;6878;6881;23450;6877;6879;6883;6880;6873;2648;8295;10629","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006265;GO:0006352;GO:0045893;GO:0006473;GO:0006476;GO:0051276;GO:0005634","GO.description":"DNA topological change;DNA-templated transcription, initiation;positive regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.01.01;11.02.03.04.01;14.07.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription initiation;transcription activation;modification by acetylation, deacetylation;organization of chromosome structure;nucleus","PubMed.ID":12601814,"subunits.Protein.name.":"Transcription initiation factor TFIID subunit 4;Ataxin-7;Transcription initiation protein SPT3 homolog;Transcriptional adapter 3;TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L;Transcription initiation factor TFIID subunit 6;Transcription initiation factor TFIID subunit 10;Splicing factor 3B subunit 3;Transcription initiation factor TFIID subunit 5;Transcription initiation factor TFIID subunit 7;Transcription initiation factor TFIID subunit 12;Transcription initiation factor TFIID subunit 9;Transcription initiation factor TFIID subunit 2 ;Histone acetyltransferase KAT2A;Transformation/transcription domain-associated protein;TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L","subunits.Gene.name.":"TAF4;ATXN7;SUPT3H;TADA3;TAF5L;TAF6;TAF10;SF3B3;TAF5;TAF7;TAF12;TAF9;TAF2;KAT2A;TRRAP;TAF6L","subunits.Gene.name.syn.":"TAF2C TAF2C1 TAF4A TAFII130 TAFII135;SCA7;SPT3;ADA3, TADA3L;PAF65B;TAF2E TAFII70;TAF2A TAF2H TAFII30;KIAA0017 SAP130;TAF2D;TAF2F TAFII55;TAF15 TAF2J TAFII20;TAF2G TAFII31;CIF150 TAF2B;GCN5, GCN5L2, HGCN5;PAF400;PAF65A","Disease.comment":"None","Subunits.comment":"TAF-II-30, TAF-II-55 and ADA3 were not identified as TFTC subunits in this study.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":456,"ComplexName":"TFTC complex (TATA-binding protein-free TAF-II-containing complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00268;O15265;O75486;O75528;O75529;P49848;Q12962;Q15393;Q15542;Q15545;Q16514;Q16594;Q6P1X5;Q92830;Q9Y4A5;Q9Y6J9","subunits.Entrez.IDs.":"6874;6314;8464;10474;27097;6878;6881;23450;6877;6879;6883;6880;6873;2648;8295;10629","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006265;GO:0006352;GO:0045893;GO:0006473;GO:0006476;GO:0051276;GO:0005634","GO.description":"DNA topological change;DNA-templated transcription, initiation;positive regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.01.01;11.02.03.04.01;14.07.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription initiation;transcription activation;modification by acetylation, deacetylation;organization of chromosome structure;nucleus","PubMed.ID":15115762,"subunits.Protein.name.":"Transcription initiation factor TFIID subunit 4;Ataxin-7;Transcription initiation protein SPT3 homolog;Transcriptional adapter 3;TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L;Transcription initiation factor TFIID subunit 6;Transcription initiation factor TFIID subunit 10;Splicing factor 3B subunit 3;Transcription initiation factor TFIID subunit 5;Transcription initiation factor TFIID subunit 7;Transcription initiation factor TFIID subunit 12;Transcription initiation factor TFIID subunit 9;Transcription initiation factor TFIID subunit 2 ;Histone acetyltransferase KAT2A;Transformation/transcription domain-associated protein;TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L","subunits.Gene.name.":"TAF4;ATXN7;SUPT3H;TADA3;TAF5L;TAF6;TAF10;SF3B3;TAF5;TAF7;TAF12;TAF9;TAF2;KAT2A;TRRAP;TAF6L","subunits.Gene.name.syn.":"TAF2C TAF2C1 TAF4A TAFII130 TAFII135;SCA7;SPT3;ADA3, TADA3L;PAF65B;TAF2E TAFII70;TAF2A TAF2H TAFII30;KIAA0017 SAP130;TAF2D;TAF2F TAFII55;TAF15 TAF2J TAFII20;TAF2G TAFII31;CIF150 TAF2B;GCN5, GCN5L2, HGCN5;PAF400;PAF65A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":457,"ComplexName":"Dystrophin-associated glycoprotein complex DGC (Dag1, Dp71f, Sgcd, Snta1), retinal glia cells","Organism":"Rat","Synonyms":"None","Cell.line":"retinal glia cells","subunits.UniProt.IDs.":"P11531;P82347;Q498T0;Q91XP7","subunits.Entrez.IDs.":"13405;24052;362242;114489","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007044;GO:0005886","GO.description":"cell-substrate junction assembly;plasma membrane","FunCat.ID":"42.06.03;70.02","FunCat.description":"cell-substrate adherens junction;eukaryotic plasma membrane / membrane attached","PubMed.ID":10984432,"subunits.Protein.name.":"Dystrophin;Delta-sarcoglycan;Snta1 protein;Dystroglycan 1","subunits.Gene.name.":"Dmd;Sgcd;Snta1;Dag1","subunits.Gene.name.syn.":"None;None;None;None","Disease.comment":"None","Subunits.comment":"Since Sgcd and Dmd (described as Dp71f) from rat were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.","Complex.comment":"The results indicate that the DGC could have both structural and signaling functions in retina.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":458,"ComplexName":"Dystrophin-associated glycoprotein complex DGC (Dag1, Dp71f, Utrn), retinal glia cells","Organism":"Rat","Synonyms":"None","Cell.line":"retinal glia cells","subunits.UniProt.IDs.":"O55147;P11531;Q91XP7","subunits.Entrez.IDs.":"25600;13405;114489","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007044;GO:0005886","GO.description":"cell-substrate junction assembly;plasma membrane","FunCat.ID":"42.06.03;70.02","FunCat.description":"cell-substrate adherens junction;eukaryotic plasma membrane / membrane attached","PubMed.ID":10984432,"subunits.Protein.name.":"Rattus norvegicus utrophin;Dystrophin;Dystroglycan 1","subunits.Gene.name.":"Utrn;Dmd;Dag1","subunits.Gene.name.syn.":"None;None;None","Disease.comment":"None","Subunits.comment":"Since Dmd (described as Dp71f) from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"The results indicate that the DGC could have both structural and signaling functions in retina.","SWISSPROT.organism":"Rattus norvegicus (Rat);Mus musculus (Mouse);Rattus norvegicus (Rat)"}
{"ComplexID":459,"ComplexName":"TFTC complex (TATA-binding protein-free TAF-II-containing complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00268;O15265;O75486;O75528;O75529;P49848;Q12962;Q15393;Q15542;Q15545;Q16514;Q16594;Q6P1X5;Q92830;Q9Y4A5;Q9Y6J9","subunits.Entrez.IDs.":"6874;6314;8464;10474;27097;6878;6881;23450;6877;6879;6883;6880;6873;2648;8295;10629","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0006265;GO:0006352;GO:0045893;GO:0006473;GO:0006476;GO:0006974;GO:0051276;GO:0005634","GO.description":"DNA repair;DNA topological change;DNA-templated transcription, initiation;positive regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;cellular response to DNA damage stimulus;chromosome organization;nucleus","FunCat.ID":"10.01.05.01;10.01.09.05;11.02.03.01.01;11.02.03.04.01;14.07.04;32.01.09;42.10.03;70.10","FunCat.description":"DNA repair;DNA conformation modification (e.g. chromatin);transcription initiation;transcription activation;modification by acetylation, deacetylation;DNA damage response;organization of chromosome structure;nucleus","PubMed.ID":15115762,"subunits.Protein.name.":"Transcription initiation factor TFIID subunit 4;Ataxin-7;Transcription initiation protein SPT3 homolog;Transcriptional adapter 3;TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L;Transcription initiation factor TFIID subunit 6;Transcription initiation factor TFIID subunit 10;Splicing factor 3B subunit 3;Transcription initiation factor TFIID subunit 5;Transcription initiation factor TFIID subunit 7;Transcription initiation factor TFIID subunit 12;Transcription initiation factor TFIID subunit 9;Transcription initiation factor TFIID subunit 2 ;Histone acetyltransferase KAT2A;Transformation/transcription domain-associated protein;TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L","subunits.Gene.name.":"TAF4;ATXN7;SUPT3H;TADA3;TAF5L;TAF6;TAF10;SF3B3;TAF5;TAF7;TAF12;TAF9;TAF2;KAT2A;TRRAP;TAF6L","subunits.Gene.name.syn.":"TAF2C TAF2C1 TAF4A TAFII130 TAFII135;SCA7;SPT3;ADA3, TADA3L;PAF65B;TAF2E TAFII70;TAF2A TAF2H TAFII30;KIAA0017 SAP130;TAF2D;TAF2F TAFII55;TAF15 TAF2J TAFII20;TAF2G TAFII31;CIF150 TAF2B;GCN5, GCN5L2, HGCN5;PAF400;PAF65A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":460,"ComplexName":"CRB1-MPP5-INADL complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P82279;Q8N3R9;Q8NI35","subunits.Entrez.IDs.":"23418;64398;10207","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0051211;GO:0009798;GO:0007043;GO:0030054","GO.description":"anisotropic cell growth;axis specification;cell-cell junction assembly;cell junction","FunCat.ID":"40.01.03;41.05.19;42.06.04;70.06","FunCat.description":"directional cell growth (morphogenesis);asymmetries and axis determination;intercellular junction (gap junction/adherens junction);cell junction","PubMed.ID":11927608,"subunits.Protein.name.":"Protein crumbs homolog 1;MAGUK p55 subfamily member 5;InaD-like protein","subunits.Gene.name.":"CRB1;MPP5;PATJ","subunits.Gene.name.syn.":"None;None;INADL","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex  appears to be evolutionarily conserved and likely plays an important role in protein targeting and cell polarity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":461,"ComplexName":"MPP4-MPP5-CRB1 complex","Organism":"Human","Synonyms":"None","Cell.line":"eye","subunits.UniProt.IDs.":"P82279;Q8N3R9;Q96JB8","subunits.Entrez.IDs.":"23418;64398;58538","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0009583;GO:0009416","GO.description":"detection of light stimulus;response to light stimulus","FunCat.ID":"34.11.01","FunCat.description":"photoperception and response","PubMed.ID":15914641,"subunits.Protein.name.":"Protein crumbs homolog 1;MAGUK p55 subfamily member 5;MAGUK p55 subfamily member 4","subunits.Gene.name.":"CRB1;MPP5;MPP4","subunits.Gene.name.syn.":"None;None;ALS2CR5 DLG6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex is localized in outer limiting membrane.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":462,"ComplexName":"TFTC complex (TATA-binding protein-free TAF-II-containing complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00268;O15265;O75486;O75528;O75529;P49848;Q12962;Q15393;Q15542;Q15545;Q16514;Q16594;Q6P1X5;Q92830;Q9Y4A5;Q9Y6J9","subunits.Entrez.IDs.":"6874;6314;8464;10474;27097;6878;6881;23450;6877;6879;6883;6880;6873;2648;8295;10629","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0006- anti bait coimmunoprecipitation; MI:0071- molecular sieving","GO.ID":"GO:0006265;GO:0006352;GO:0045893;GO:0006473;GO:0006476;GO:0051276;GO:0005634","GO.description":"DNA topological change;DNA-templated transcription, initiation;positive regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.01.01;11.02.03.04.01;14.07.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription initiation;transcription activation;modification by acetylation, deacetylation;organization of chromosome structure;nucleus","PubMed.ID":9603525,"subunits.Protein.name.":"Transcription initiation factor TFIID subunit 4;Ataxin-7;Transcription initiation protein SPT3 homolog;Transcriptional adapter 3;TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L;Transcription initiation factor TFIID subunit 6;Transcription initiation factor TFIID subunit 10;Splicing factor 3B subunit 3;Transcription initiation factor TFIID subunit 5;Transcription initiation factor TFIID subunit 7;Transcription initiation factor TFIID subunit 12;Transcription initiation factor TFIID subunit 9;Transcription initiation factor TFIID subunit 2 ;Histone acetyltransferase KAT2A;Transformation/transcription domain-associated protein;TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L","subunits.Gene.name.":"TAF4;ATXN7;SUPT3H;TADA3;TAF5L;TAF6;TAF10;SF3B3;TAF5;TAF7;TAF12;TAF9;TAF2;KAT2A;TRRAP;TAF6L","subunits.Gene.name.syn.":"TAF2C TAF2C1 TAF4A TAFII130 TAFII135;SCA7;SPT3;ADA3, TADA3L;PAF65B;TAF2E TAFII70;TAF2A TAF2H TAFII30;KIAA0017 SAP130;TAF2D;TAF2F TAFII55;TAF15 TAF2J TAFII20;TAF2G TAFII31;CIF150 TAF2B;GCN5, GCN5L2, HGCN5;PAF400;PAF65A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TFTC complex can replace TFIID in vitro, indicating that multiple preinitiation complexes may play an important role in regulating gene expression.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":463,"ComplexName":"TFIID-beta complex","Organism":"Human","Synonyms":"TFIID(beta) transcription factor complex","Cell.line":"None","subunits.UniProt.IDs.":"O00268;P20226;P21675;P49848;Q12962;Q15542;Q15543;Q15544;Q15545;Q16514;Q16594","subunits.Entrez.IDs.":"6874;6908;6872;6878;6881;6877;6884;6882;6879;6883;6880","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0004- affinity chromatography technologies; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006352;GO:2001141;GO:0006355;GO:0003677;GO:0005634","GO.description":"DNA-templated transcription, initiation;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.01.01;11.02.03.04;16.03.01;70.10","FunCat.description":"transcription initiation;transcriptional control;DNA binding;nucleus","PubMed.ID":9603525,"subunits.Protein.name.":"Transcription initiation factor TFIID subunit 4;TATA-box-binding protein;Transcription initiation factor TFIID subunit 1;Transcription initiation factor TFIID subunit 6;Transcription initiation factor TFIID subunit 10;Transcription initiation factor TFIID subunit 5;Transcription initiation factor TFIID subunit 13;Transcription initiation factor TFIID subunit 11;Transcription initiation factor TFIID subunit 7;Transcription initiation factor TFIID subunit 12;Transcription initiation factor TFIID subunit 9","subunits.Gene.name.":"TAF4;TBP;TAF1;TAF6;TAF10;TAF5;TAF13;TAF11;TAF7;TAF12;TAF9","subunits.Gene.name.syn.":"TAF2C TAF2C1 TAF4A TAFII130 TAFII135;GTF2D1 TF2D TFIID;BA2R CCG1 CCGS TAF2A;TAF2E TAFII70;TAF2A TAF2H TAFII30;TAF2D;TAF2K TAFII18;TAF2I;TAF2F TAFII55;TAF15 TAF2J TAFII20;TAF2G TAFII31","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":464,"ComplexName":"InsP3R1-HAP1A-Htt complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P29994;P51111;P54256","subunits.Entrez.IDs.":"25262;29424;29430","Protein.complex.purification.method":"MI:0096- pull down;MI:0019- coimmunoprecipitation","GO.ID":"GO:0019722","GO.description":"calcium-mediated signaling","FunCat.ID":"30.01.09.03","FunCat.description":"Ca2+ mediated signal transduction","PubMed.ID":12873381,"subunits.Protein.name.":"Inositol 1,4,5-trisphosphate receptor type 1;Huntingtin ;Huntingtin-associated protein 1","subunits.Gene.name.":"Itpr1;Htt;Hap1","subunits.Gene.name.syn.":"Insp3r;Hd Hdh;","Disease.comment":"Htt is involved in Huntingtons disease (PMID:15379999).","Subunits.comment":"None","Complex.comment":"HAP1A facilitates functional effects of Htt and Htt(exp) on InsP3R1 in planar lipid bilayers (PMID:15379999).","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":465,"ComplexName":"InsP3R1-HAP1A-Htt complex","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"O35668;P11881;P42859","subunits.Entrez.IDs.":"15114;16438;15194","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0019722","GO.description":"calcium-mediated signaling","FunCat.ID":"30.01.09.03","FunCat.description":"Ca2+ mediated signal transduction","PubMed.ID":12873381,"subunits.Protein.name.":"Huntingtin-associated protein 1 ;Inositol 1,4,5-trisphosphate receptor type 1 ;Huntingtin","subunits.Gene.name.":"Hap1;Itpr1;Htt","subunits.Gene.name.syn.":";Insp3r Pcd6 Pcp1;Hd Hdh","Disease.comment":"Htt is involved in Huntingtons disease (PMID:15379999).","Subunits.comment":"None","Complex.comment":"HAP1A facilitates functional effects of Htt and Htt(exp) on InsP3R1 in planar lipid bilayers (PMID:15379999).","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":466,"ComplexName":"Gamma-secretase complex (APH1A, PSEN1, PSENEN, NCSTN)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P49768;Q92542;Q96BI3;Q9NZ42","subunits.Entrez.IDs.":"5663;23385;51107;55851","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016485;GO:0023052;GO:0007219;GO:0005886;GO:0005794","GO.description":"protein processing;signaling;Notch signaling pathway;plasma membrane;Golgi apparatus","FunCat.ID":"14.07.11;30.01;30.05.02.14;70.02;70.08","FunCat.description":"protein processing (proteolytic);cellular signalling;Notch-receptor signalling pathway;eukaryotic plasma membrane / membrane attached;Golgi","PubMed.ID":15286082,"subunits.Protein.name.":"Presenilin-1;Nicastrin;Gamma-secretase subunit APH-1A;Gamma-secretase subunit PEN-2","subunits.Gene.name.":"PSEN1;NCSTN;APH1A;PSENEN","subunits.Gene.name.syn.":"AD3 PS1 PSNL1;KIAA0253;PSF;PEN2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Proteolytic cleavage within the hydrophobic transmembrane domains of Notch and APP are intimately associated with a multimeric gamma-secretase complex that contains the presenilin-1 or presenilin-2 and the membrane glycoprotein nicastrin. Three variants of APH1 (APH1A short, APH1A long and APH1B) as well as two presenillin variants (PSEN1 and PSEN2) allow the formation of six different gamma-secretase complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":467,"ComplexName":"Gamma-secretase complex (APH1B, PSEN2, PSENEN, NCSTN)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P49810;Q8WW43;Q92542;Q9NZ42","subunits.Entrez.IDs.":"5664;83464;23385;55851","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016485;GO:0016485;GO:0051090;GO:0023052;GO:0007219;GO:0005886;GO:0005794","GO.description":"protein processing;protein processing;regulation of sequence-specific DNA binding transcription factor activity;signaling;Notch signaling pathway;plasma membrane;Golgi apparatus","FunCat.ID":"14.07.11;18.02.09;30.01;30.05.02.14;70.02;70.08","FunCat.description":"protein processing (proteolytic);regulator of transcription factor;cellular signalling;Notch-receptor signalling pathway;eukaryotic plasma membrane / membrane attached;Golgi","PubMed.ID":15286082,"subunits.Protein.name.":"Presenilin-2 ;Gamma-secretase subunit APH-1B ;Nicastrin;Gamma-secretase subunit PEN-2","subunits.Gene.name.":"PSEN2;APH1B;NCSTN;PSENEN","subunits.Gene.name.syn.":"AD4 PS2 PSNL2 STM2;PSFL;KIAA0253;PEN2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Proteolytic cleavage within the hydrophobic transmembrane domains of Notch and APP are intimately associated with a multimeric gamma-secretase complex that contains the presenilin-1 or presenilin-2 and the membrane glycoprotein nicastrin. Three variants of APH1 (APH1A short, APH1A long and APH1B) as well as two presenilin variants (PSEN1 and PSEN2) allow the formation of six different gamma-secretase complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":468,"ComplexName":"Gamma-secretase complex (APH1A, PSEN2, PSENEN, NCSTN)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P49810;Q92542;Q96BI3;Q9NZ42","subunits.Entrez.IDs.":"5664;23385;51107;55851","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016485;GO:0016485;GO:0051090;GO:0023052;GO:0007219;GO:0005886;GO:0005794","GO.description":"protein processing;protein processing;regulation of sequence-specific DNA binding transcription factor activity;signaling;Notch signaling pathway;plasma membrane;Golgi apparatus","FunCat.ID":"14.07.11;18.02.09;30.01;30.05.02.14;70.02;70.08","FunCat.description":"protein processing (proteolytic);regulator of transcription factor;cellular signalling;Notch-receptor signalling pathway;eukaryotic plasma membrane / membrane attached;Golgi","PubMed.ID":15286082,"subunits.Protein.name.":"Presenilin-2 ;Nicastrin;Gamma-secretase subunit APH-1A;Gamma-secretase subunit PEN-2","subunits.Gene.name.":"PSEN2;NCSTN;APH1A;PSENEN","subunits.Gene.name.syn.":"AD4 PS2 PSNL2 STM2;KIAA0253;PSF;PEN2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Proteolytic cleavage within the hydrophobic transmembrane domains of Notch and APP are intimately associated with a multimeric gamma-secretase complex that contains the presenilin-1 or presenilin-2 and the membrane glycoprotein nicastrin. Three variants of APH1 (APH1A short, APH1A long and APH1B) as well as two presenillin variants (PSEN1 and PSEN2) allow the formation of six different gamma-secretase complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":469,"ComplexName":"TFIID-beta complex","Organism":"Human","Synonyms":"TFIID(beta) transcription factor complex","Cell.line":"None","subunits.UniProt.IDs.":"O00268;P20226;P21675;P49848;Q12962;Q15542;Q15543;Q15544;Q15545;Q16514;Q16594;Q6P1X5","subunits.Entrez.IDs.":"6874;6908;6872;6878;6881;6877;6884;6882;6879;6883;6880;6873","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0006- anti bait coimmunoprecipitation; MI:0040- electron microscopy; MI:0428- imaging techniques","GO.ID":"GO:0006352;GO:2001141;GO:0006355;GO:0005634","GO.description":"DNA-templated transcription, initiation;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;nucleus","FunCat.ID":"11.02.03.01.01;11.02.03.04;70.10","FunCat.description":"transcription initiation;transcriptional control;nucleus","PubMed.ID":10591645,"subunits.Protein.name.":"Transcription initiation factor TFIID subunit 4;TATA-box-binding protein;Transcription initiation factor TFIID subunit 1;Transcription initiation factor TFIID subunit 6;Transcription initiation factor TFIID subunit 10;Transcription initiation factor TFIID subunit 5;Transcription initiation factor TFIID subunit 13;Transcription initiation factor TFIID subunit 11;Transcription initiation factor TFIID subunit 7;Transcription initiation factor TFIID subunit 12;Transcription initiation factor TFIID subunit 9;Transcription initiation factor TFIID subunit 2","subunits.Gene.name.":"TAF4;TBP;TAF1;TAF6;TAF10;TAF5;TAF13;TAF11;TAF7;TAF12;TAF9;TAF2","subunits.Gene.name.syn.":"TAF2C TAF2C1 TAF4A TAFII130 TAFII135;GTF2D1 TF2D TFIID;BA2R CCG1 CCGS TAF2A;TAF2E TAFII70;TAF2A TAF2H TAFII30;TAF2D;TAF2K TAFII18;TAF2I;TAF2F TAFII55;TAF15 TAF2J TAFII20;TAF2G TAFII31;CIF150 TAF2B","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":470,"ComplexName":"TFTC complex (TATA-binding protein-free TAF-II-containing complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00268;O15265;O75486;O75528;O75529;P49848;Q12962;Q15393;Q15542;Q15543;Q15545;Q16514;Q16594;Q6P1X5;Q92830;Q9Y4A5;Q9Y6J9","subunits.Entrez.IDs.":"6874;6314;8464;10474;27097;6878;6881;23450;6877;6884;6879;6883;6880;6873;2648;8295;10629","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0006- anti bait coimmunoprecipitation; MI:0428- imaging techniques; MI:0040- electron microscopy","GO.ID":"GO:0006265;GO:0006352;GO:0045893;GO:0006473;GO:0006476;GO:0051276;GO:0005634","GO.description":"DNA topological change;DNA-templated transcription, initiation;positive regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.01.01;11.02.03.04.01;14.07.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription initiation;transcription activation;modification by acetylation, deacetylation;organization of chromosome structure;nucleus","PubMed.ID":10591645,"subunits.Protein.name.":"Transcription initiation factor TFIID subunit 4;Ataxin-7;Transcription initiation protein SPT3 homolog;Transcriptional adapter 3;TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L;Transcription initiation factor TFIID subunit 6;Transcription initiation factor TFIID subunit 10;Splicing factor 3B subunit 3;Transcription initiation factor TFIID subunit 5;Transcription initiation factor TFIID subunit 13;Transcription initiation factor TFIID subunit 7;Transcription initiation factor TFIID subunit 12;Transcription initiation factor TFIID subunit 9;Transcription initiation factor TFIID subunit 2 ;Histone acetyltransferase KAT2A;Transformation/transcription domain-associated protein;TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L","subunits.Gene.name.":"TAF4;ATXN7;SUPT3H;TADA3;TAF5L;TAF6;TAF10;SF3B3;TAF5;TAF13;TAF7;TAF12;TAF9;TAF2;KAT2A;TRRAP;TAF6L","subunits.Gene.name.syn.":"TAF2C TAF2C1 TAF4A TAFII130 TAFII135;SCA7;SPT3;ADA3, TADA3L;PAF65B;TAF2E TAFII70;TAF2A TAF2H TAFII30;KIAA0017 SAP130;TAF2D;TAF2K TAFII18;TAF2F TAFII55;TAF15 TAF2J TAFII20;TAF2G TAFII31;CIF150 TAF2B;GCN5, GCN5L2, HGCN5;PAF400;PAF65A","Disease.comment":"None","Subunits.comment":"Three other subunits of the complex were found in the analysis, which have not been further characterized. In following publications these proteins were identified as ataxin-7, splicing factor 3B subunit 3 and PAF65A.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":471,"ComplexName":"PCAF complex","Organism":"Human","Synonyms":"PCAF histone acetylase-associated complex","Cell.line":"None","subunits.UniProt.IDs.":"O75478;O75486;O75528;O75529;Q12962;Q16514;Q16594;Q92831;Q9Y4A5;Q9Y6J9","subunits.Entrez.IDs.":"6871;8464;10474;27097;6881;6883;6880;8850;8295;10629","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0004- affinity chromatography technologies","GO.ID":"GO:0006265;GO:0006351;GO:2001141;GO:0006355;GO:0006473;GO:0006476;GO:0051276;GO:0005634","GO.description":"DNA topological change;transcription, DNA-templated;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11;11.02.03.04;14.07.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);TRANSCRIPTION;transcriptional control;modification by acetylation, deacetylation;organization of chromosome structure;nucleus","PubMed.ID":9674425,"subunits.Protein.name.":"Transcriptional adapter 2-alpha;Transcription initiation protein SPT3 homolog;Transcriptional adapter 3;TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L;Transcription initiation factor TFIID subunit 10;Transcription initiation factor TFIID subunit 12;Transcription initiation factor TFIID subunit 9;Histone acetyltransferase KAT2B;Transformation/transcription domain-associated protein;TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L","subunits.Gene.name.":"TADA2A;SUPT3H;TADA3;TAF5L;TAF10;TAF12;TAF9;KAT2B;TRRAP;TAF6L","subunits.Gene.name.syn.":"TADA2L, ADA2A;SPT3;ADA3, TADA3L;PAF65B;TAF2A TAF2H TAFII30;TAF15 TAF2J TAFII20;TAF2G TAFII31;PCAF;PAF400;PAF65A","Disease.comment":"None","Subunits.comment":"PCAF is a complex consisting of more than 20 different proteins. Several proteins have not been characterized in this study.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":472,"ComplexName":"Prolyl 4-hydroxylase (alpha(I)-type)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P07237;P13674","subunits.Entrez.IDs.":"5034;5033","Protein.complex.purification.method":"MI:0027- cosedimentation","GO.ID":"GO:0018126;GO:0006479;GO:0005515;GO:0048037;GO:0005783","GO.description":"protein hydroxylation;protein methylation;protein binding;cofactor binding;endoplasmic reticulum","FunCat.ID":"14.07.09;16.01;16.21;70.07","FunCat.description":"posttranslational modification of amino acids (e.g. hydroxylation, methylation);protein binding;complex cofactor/cosubstrate/vitamine binding;endoplasmic reticulum","PubMed.ID":7753822,"subunits.Protein.name.":"Protein disulfide-isomerase ;Prolyl 4-hydroxylase subunit alpha-1","subunits.Gene.name.":"P4HB;P4HA1","subunits.Gene.name.syn.":"ERBA2L PDI PDIA1 PO4DB;P4HA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Prolyl 4-hydroxylase (EC 1.14.11.2) catalyzes the formation of 4-hydroxyproline in collagens and related proteins.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":473,"ComplexName":"Prolyl 4-hydroxylase (alpha(II)-type)","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P07237;Q60716","subunits.Entrez.IDs.":"5034;18452","Protein.complex.purification.method":"MI:0027- cosedimentation","GO.ID":"GO:0018126;GO:0006479;GO:0005515;GO:0048037;GO:0005783","GO.description":"protein hydroxylation;protein methylation;protein binding;cofactor binding;endoplasmic reticulum","FunCat.ID":"14.07.09;16.01;16.21;70.07","FunCat.description":"posttranslational modification of amino acids (e.g. hydroxylation, methylation);protein binding;complex cofactor/cosubstrate/vitamine binding;endoplasmic reticulum","PubMed.ID":7753822,"subunits.Protein.name.":"Protein disulfide-isomerase ;Prolyl 4-hydroxylase subunit alpha-2","subunits.Gene.name.":"P4HB;P4ha2","subunits.Gene.name.syn.":"ERBA2L PDI PDIA1 PO4DB;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Prolyl 4-hydroxylase (EC 1.14.11.2) catalyzes the formation of 4-hydroxyproline in collagens and related proteins.","SWISSPROT.organism":"Homo sapiens (Human);Mus musculus (Mouse)"}
{"ComplexID":474,"ComplexName":"Prolyl 4-hydroxylase (alpha(III)-type)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P07237;Q7Z4N8","subunits.Entrez.IDs.":"5034;283208","Protein.complex.purification.method":"MI:0027- cosedimentation","GO.ID":"GO:0018126;GO:0006479;GO:0005515;GO:0048037;GO:0005783","GO.description":"protein hydroxylation;protein methylation;protein binding;cofactor binding;endoplasmic reticulum","FunCat.ID":"14.07.09;16.01;16.21;70.07","FunCat.description":"posttranslational modification of amino acids (e.g. hydroxylation, methylation);protein binding;complex cofactor/cosubstrate/vitamine binding;endoplasmic reticulum","PubMed.ID":14500733,"subunits.Protein.name.":"Protein disulfide-isomerase ;Prolyl 4-hydroxylase subunit alpha-3","subunits.Gene.name.":"P4HB;P4HA3","subunits.Gene.name.syn.":"ERBA2L PDI PDIA1 PO4DB;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Prolyl 4-hydroxylase (EC 1.14.11.2) catalyzes the formation of 4-hydroxyproline in collagens and related proteins.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":475,"ComplexName":"STAGA complex","Organism":"Human","Synonyms":"STAGA coactivator complex; SPT3-TAF9-GCN5 acetyltransferase complex","Cell.line":"None","subunits.UniProt.IDs.":"O75486;O75528;O75529;O94864;Q12962;Q15393;Q16514;Q16594;Q92830;Q96BN2;Q9Y4A5;Q9Y6J9","subunits.Entrez.IDs.":"8464;10474;27097;9913;6881;23450;6883;6880;2648;117143;8295;10629","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies;MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045893;GO:0006974;GO:0051276;GO:0005634;GO:0016573","GO.description":"DNA topological change;positive regulation of transcription, DNA-templated;cellular response to DNA damage stimulus;chromosome organization;nucleus;histone acetylation","FunCat.ID":"10.01.09.05;11.02.03.04.01;32.01.09;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription activation;DNA damage response;organization of chromosome structure;nucleus","PubMed.ID":11564863,"subunits.Protein.name.":"Transcription initiation protein SPT3 homolog;Transcriptional adapter 3;TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L;STAGA complex 65 subunit gamma;Transcription initiation factor TFIID subunit 10;Splicing factor 3B subunit 3;Transcription initiation factor TFIID subunit 12;Transcription initiation factor TFIID subunit 9;Histone acetyltransferase KAT2A;Transcriptional adapter 1;Transformation/transcription domain-associated protein;TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L","subunits.Gene.name.":"SUPT3H;TADA3;TAF5L;SUPT7L;TAF10;SF3B3;TAF12;TAF9;KAT2A;TADA1;TRRAP;TAF6L","subunits.Gene.name.syn.":"SPT3;ADA3, TADA3L;PAF65B;KIAA0764, STAF65gamma;TAF2A TAF2H TAFII30;KIAA0017 SAP130;TAF15 TAF2J TAFII20;TAF2G TAFII31;GCN5, GCN5L2, HGCN5;TADA1L, STAF42;PAF400;PAF65A","Disease.comment":"None","Subunits.comment":"Three other subunits of the complex were found in the analysis, which have not been further characterized: STAF60, STAF55, STAF46.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":476,"ComplexName":"STAGA complex","Organism":"Human","Synonyms":"STAGA coactivator complex; SPT3-TAF9-GCN5 acetyltransferase complex","Cell.line":"None","subunits.UniProt.IDs.":"O15265;O75486;O75528;O75529;O94864;Q12962;Q15393;Q16514;Q16594;Q92830;Q96BN2;Q9Y4A5;Q9Y6J9","subunits.Entrez.IDs.":"6314;8464;10474;27097;9913;6881;23450;6883;6880;2648;117143;8295;10629","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045893;GO:0006974;GO:0051276;GO:0005634;GO:0016573","GO.description":"DNA topological change;positive regulation of transcription, DNA-templated;cellular response to DNA damage stimulus;chromosome organization;nucleus;histone acetylation","FunCat.ID":"10.01.09.05;11.02.03.04.01;32.01.09;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription activation;DNA damage response;organization of chromosome structure;nucleus","PubMed.ID":15115762,"subunits.Protein.name.":"Ataxin-7;Transcription initiation protein SPT3 homolog;Transcriptional adapter 3;TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L;STAGA complex 65 subunit gamma;Transcription initiation factor TFIID subunit 10;Splicing factor 3B subunit 3;Transcription initiation factor TFIID subunit 12;Transcription initiation factor TFIID subunit 9;Histone acetyltransferase KAT2A;Transcriptional adapter 1;Transformation/transcription domain-associated protein;TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L","subunits.Gene.name.":"ATXN7;SUPT3H;TADA3;TAF5L;SUPT7L;TAF10;SF3B3;TAF12;TAF9;KAT2A;TADA1;TRRAP;TAF6L","subunits.Gene.name.syn.":"SCA7;SPT3;ADA3, TADA3L;PAF65B;KIAA0764, STAF65gamma;TAF2A TAF2H TAFII30;KIAA0017 SAP130;TAF15 TAF2J TAFII20;TAF2G TAFII31;GCN5, GCN5L2, HGCN5;TADA1L, STAF42;PAF400;PAF65A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex is a coactivator required for transcription of a subset of RNA polymerase II-dependent genes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":477,"ComplexName":"PCAF complex","Organism":"Human","Synonyms":"PCAF histone acetylase-associated complex","Cell.line":"None","subunits.UniProt.IDs.":"O75478;O75486;O75528;O75529;Q12962;Q16514;Q16594;Q92831;Q9Y4A5;Q9Y6J9","subunits.Entrez.IDs.":"6871;8464;10474;27097;6881;6883;6880;8850;8295;10629","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0004- affinity chromatography technologies","GO.ID":"GO:0006265;GO:0006351;GO:2001141;GO:0006355;GO:0006473;GO:0006476;GO:0051276;GO:0005634","GO.description":"DNA topological change;transcription, DNA-templated;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11;11.02.03.04;14.07.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);TRANSCRIPTION;transcriptional control;modification by acetylation, deacetylation;organization of chromosome structure;nucleus","PubMed.ID":9885574,"subunits.Protein.name.":"Transcriptional adapter 2-alpha;Transcription initiation protein SPT3 homolog;Transcriptional adapter 3;TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L;Transcription initiation factor TFIID subunit 10;Transcription initiation factor TFIID subunit 12;Transcription initiation factor TFIID subunit 9;Histone acetyltransferase KAT2B;Transformation/transcription domain-associated protein;TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L","subunits.Gene.name.":"TADA2A;SUPT3H;TADA3;TAF5L;TAF10;TAF12;TAF9;KAT2B;TRRAP;TAF6L","subunits.Gene.name.syn.":"TADA2L, ADA2A;SPT3;ADA3, TADA3L;PAF65B;TAF2A TAF2H TAFII30;TAF15 TAF2J TAFII20;TAF2G TAFII31;PCAF;PAF400;PAF65A","Disease.comment":"None","Subunits.comment":"PCAF is a complex consisting of more than 20 different proteins. Several proteins have not been characterized in this study.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":478,"ComplexName":"STAGA core complex","Organism":"Human","Synonyms":"SPT3-TAF9-GCN5 acetyltransferase complex","Cell.line":"None","subunits.UniProt.IDs.":"O75486;Q16594;Q92830","subunits.Entrez.IDs.":"8464;6880;2648","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045893;GO:0051276;GO:0005634;GO:0016573","GO.description":"DNA topological change;positive regulation of transcription, DNA-templated;chromosome organization;nucleus;histone acetylation","FunCat.ID":"10.01.09.05;11.02.03.04.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription activation;organization of chromosome structure;nucleus","PubMed.ID":9726987,"subunits.Protein.name.":"Transcription initiation protein SPT3 homolog;Transcription initiation factor TFIID subunit 9;Histone acetyltransferase KAT2A","subunits.Gene.name.":"SUPT3H;TAF9;KAT2A","subunits.Gene.name.syn.":"SPT3;TAF2G TAFII31;GCN5, GCN5L2, HGCN5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":479,"ComplexName":"Mupp1-Dlg4-Syngap1-CamkII complex","Organism":"Rat","Synonyms":"None","Cell.line":"hippocampal neurons","subunits.UniProt.IDs.":"O55164;P08413;P11275;P31016;Q9QUH6","subunits.Entrez.IDs.":"29365;24245;25400;29495;192117","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007268","GO.description":"synaptic transmission","FunCat.ID":"34.03.01","FunCat.description":"synaptic transmission","PubMed.ID":15312654,"subunits.Protein.name.":"Multiple PDZ domain protein ;Calcium/calmodulin-dependent protein kinase type II subunit beta ;Calcium/calmodulin-dependent protein kinase type II subunit alpha ;Disks large homolog 4;Ras/Rap GTPase-activating protein SynGAP","subunits.Gene.name.":"Mpdz;Camk2b;Camk2a;Dlg4;Syngap1","subunits.Gene.name.syn.":"Mupp1;;;Dlgh4, Psd95;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The SynGAP-alpha-MUPP1-CAMKII complex is a component of the NMDAR supramolecular structure in hippocampal pyramidal neurons. The integrity of this complex is critical for synaptic NMDAR-dependent AMPA receptor trafficking.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":480,"ComplexName":"TIF-IB complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P29037;P97357;P97358;Q6PDZ2","subunits.Entrez.IDs.":"21374;21339;21340;21341","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0004- affinity chromatography technologies","GO.ID":"GO:0009303;GO:0006352;GO:0005634","GO.description":"rRNA transcription;DNA-templated transcription, initiation;nucleus","FunCat.ID":"11.02.01;11.02.03.01.01;70.10","FunCat.description":"rRNA synthesis;transcription initiation;nucleus","PubMed.ID":8414971,"subunits.Protein.name.":"TATA-box-binding protein;TATA box-binding protein-associated factor RNA polymerase I subunit A ;TATA box-binding protein-associated factor RNA polymerase I subunit B ;TATA box-binding protein-associated factor RNA polymerase I subunit C","subunits.Gene.name.":"Tbp;Taf1a;Taf1b;Taf1c","subunits.Gene.name.syn.":"Tfiid;;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TIF-IB complex interacts with the mouse ribosomal gene promoter and nucleates the formation of an initiation complex containing RNA polymerase I.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":482,"ComplexName":"cRET-Shc-Grb2-Gab2-P85PI3K-Shp2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P26450;P35235;P35546;P98083;Q60631;Q9Z1S8","subunits.Entrez.IDs.":"18708;19247;19713;20416;14784;14389","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0019932;GO:0007169","GO.description":"second-messenger-mediated signaling;transmembrane receptor protein tyrosine kinase signaling pathway","FunCat.ID":"30.01.09;30.05.01.12","FunCat.description":"second messenger mediated signal transduction;transmembrane receptor protein tyrosine kinase signalling pathways","PubMed.ID":10995764,"subunits.Protein.name.":"Phosphatidylinositol 3-kinase regulatory subunit alpha ;Tyrosine-protein phosphatase non-receptor type 11;Proto-oncogene tyrosine-protein kinase receptor Ret ;SHC-transforming protein 1 ;Growth factor receptor-bound protein 2;GRB2-associated-binding protein 2","subunits.Gene.name.":"Pik3r1;Ptpn11;Ret;Shc1;Grb2;Gab2","subunits.Gene.name.syn.":";None;;Shc ShcA;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":484,"ComplexName":"TFIID complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00268;P20226;P21675;P49848;Q12962;Q15542;Q15543;Q15544;Q15545;Q16514;Q16594","subunits.Entrez.IDs.":"6874;6908;6872;6878;6881;6877;6884;6882;6879;6883;6880","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006352;GO:2001141;GO:0006355;GO:0003677;GO:0005634","GO.description":"DNA-templated transcription, initiation;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.01.01;11.02.03.04;16.03.01;70.10","FunCat.description":"transcription initiation;transcriptional control;DNA binding;nucleus","PubMed.ID":7729427,"subunits.Protein.name.":"Transcription initiation factor TFIID subunit 4;TATA-box-binding protein;Transcription initiation factor TFIID subunit 1;Transcription initiation factor TFIID subunit 6;Transcription initiation factor TFIID subunit 10;Transcription initiation factor TFIID subunit 5;Transcription initiation factor TFIID subunit 13;Transcription initiation factor TFIID subunit 11;Transcription initiation factor TFIID subunit 7;Transcription initiation factor TFIID subunit 12;Transcription initiation factor TFIID subunit 9","subunits.Gene.name.":"TAF4;TBP;TAF1;TAF6;TAF10;TAF5;TAF13;TAF11;TAF7;TAF12;TAF9","subunits.Gene.name.syn.":"TAF2C TAF2C1 TAF4A TAFII130 TAFII135;GTF2D1 TF2D TFIID;BA2R CCG1 CCGS TAF2A;TAF2E TAFII70;TAF2A TAF2H TAFII30;TAF2D;TAF2K TAFII18;TAF2I;TAF2F TAFII55;TAF15 TAF2J TAFII20;TAF2G TAFII31","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":485,"ComplexName":"TFIID complex, B-cell specific","Organism":"Human","Synonyms":"None","Cell.line":"Daudi cells","subunits.UniProt.IDs.":"O00268;P20226;P21675;P49848;Q12962;Q15542;Q15543;Q15544;Q15545;Q16514;Q16594;Q92750","subunits.Entrez.IDs.":"6874;6908;6872;6878;6881;6877;6884;6882;6879;6883;6880;6875","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0006352;GO:2001141;GO:0006355;GO:0003677;GO:0005634","GO.description":"DNA-templated transcription, initiation;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.01.01;11.02.03.04;16.03.01;70.10","FunCat.description":"transcription initiation;transcriptional control;DNA binding;nucleus","PubMed.ID":8858156,"subunits.Protein.name.":"Transcription initiation factor TFIID subunit 4;TATA-box-binding protein;Transcription initiation factor TFIID subunit 1;Transcription initiation factor TFIID subunit 6;Transcription initiation factor TFIID subunit 10;Transcription initiation factor TFIID subunit 5;Transcription initiation factor TFIID subunit 13;Transcription initiation factor TFIID subunit 11;Transcription initiation factor TFIID subunit 7;Transcription initiation factor TFIID subunit 12;Transcription initiation factor TFIID subunit 9;Transcription initiation factor TFIID subunit 4B","subunits.Gene.name.":"TAF4;TBP;TAF1;TAF6;TAF10;TAF5;TAF13;TAF11;TAF7;TAF12;TAF9;TAF4B","subunits.Gene.name.syn.":"TAF2C TAF2C1 TAF4A TAFII130 TAFII135;GTF2D1 TF2D TFIID;BA2R CCG1 CCGS TAF2A;TAF2E TAFII70;TAF2A TAF2H TAFII30;TAF2D;TAF2K TAFII18;TAF2I;TAF2F TAFII55;TAF15 TAF2J TAFII20;TAF2G TAFII31;TAF2C2 TAFII105","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TAF-II-105 (TAF4B) is a cell-type specific subunit of TFIID complex. Up to now TAF-II-105 is only found in differentiated B cells.Isolation of TBP and TAF9-TAF13 was not shown in this paper.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":486,"ComplexName":"WIP-WASp-actin-myosin-IIa complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43516;P19105;P35579;P42768;P60660;P62736","subunits.Entrez.IDs.":"7456;10627;4627;7454;4637;59","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0050896;GO:0030036;GO:0005856","GO.description":"response to stimulus;actin cytoskeleton organization;cytoskeleton","FunCat.ID":"36.25;42.04.03;70.04","FunCat.description":"animal specific systemic sensing and response;actin cytoskeleton;cytoskeleton","PubMed.ID":16606694,"subunits.Protein.name.":"WAS/WASL-interacting protein family member 1;Myosin regulatory light chain 12A ;Myosin-9 ;Wiskott-Aldrich syndrome protein;Myosin light polypeptide 6 ;Actin, aortic smooth muscle","subunits.Gene.name.":"WIPF1;MYL12A;MYH9;WAS;MYL6;ACTA2","subunits.Gene.name.syn.":"WASPIP WIP;MLCB MRLC3 RLC;;IMD2;;ACTSA ACTVS","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The multiprotein complex is important for NK cell function. Killer cell immunoglobulin-like receptor inhibitory signaling affects proteins involved in cytoskeletal rearrangements. WIP plays a central role in the formation of the complex and in the regulation of NK cell activity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":487,"ComplexName":"Cytochrome bc1-complex, mitochondrial","Organism":"Bovine","Synonyms":"Cytochrome bc1-complex (EC 1.10.2.2), mitochondrial; Complex III; Cytochrome reductase; Ubiquinol:cytochrome c oxidoreductase","Cell.line":"heart muscle","subunits.UniProt.IDs.":"P00125;P00126;P00129;P00130;P00157;P07552;P13271;P13272;P23004;P31800","subunits.Entrez.IDs.":"512500;613899;616871;616109;3283889;281570;286885;287020;282394;282393","Protein.complex.purification.method":"MI:0069-mass spectrometry studies of complexes;MI:0019-coimmunoprecipitation","GO.ID":"GO:0006099;GO:0006091;GO:0009060;GO:0006818;GO:0022904;GO:0005743","GO.description":"tricarboxylic acid cycle;generation of precursor metabolites and energy;aerobic respiration;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"02.10;01;02.13.03;20.01.15;02.11.07;70.16.05","FunCat.description":"tricarboxylic-acid pathway (citrate cycle, Krebs cycle, TCA cycle);METABOLISM;aerobic respiration;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":16120479,"subunits.Protein.name.":"Cytochrome c1, heme protein, mitochondrial;Cytochrome b-c1 complex subunit 6, mitochondrial;Cytochrome b-c1 complex subunit 7;Cytochrome b-c1 complex subunit 9;Cytochrome b;Cytochrome b-c1 complex subunit 10;Cytochrome b-c1 complex subunit 8;Cytochrome b-c1 complex subunit Rieske, mitochondrial;Cytochrome b-c1 complex subunit 2, mitochondrial;Cytochrome b-c1 complex subunit 1, mitochondrial","subunits.Gene.name.":"CYC1;UQCRH;UQCRB;UQCR10;MT-CYB;UQCR11;UQCRQ;UQCRFS1;UQCRC2;UQCRC1","subunits.Gene.name.syn.":"None;None;None;None;COB CYTB MTCYB;UQCR;None;None;None;None","Disease.comment":"None","Subunits.comment":"Complex III consists of 11 subunits; displayed just 10 subunits; reason:Subunit V (Rieske iron sulfur protein) contains subunit IX (= precursor of subunit V), compare PMID:8386158; subunit XI (P07552) could not be experimentally identified.","Complex.comment":"None","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":488,"ComplexName":"Vezf1-p68RacGap complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q5SXC4;Q8BL80","subunits.Entrez.IDs.":"22344;239027","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0035556;GO:0001568;GO:0001944;GO:0005737;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;intracellular signal transduction;blood vessel development;vasculature development;cytoplasm;nucleus","FunCat.ID":"11.02.03.04;30.01;47.03.03.02;70.03;70.10","FunCat.description":"transcriptional control;cellular signalling;vessels;cytoplasm;nucleus","PubMed.ID":14966113,"subunits.Protein.name.":"Protein Vezf1;Rho GTPase-activating protein 22","subunits.Gene.name.":"Vezf1;Arhgap22","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":489,"ComplexName":"TFIIA complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P52655;P52657","subunits.Entrez.IDs.":"2957;2958","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006352;GO:2001141;GO:0006355;GO:0005634","GO.description":"DNA-templated transcription, initiation;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;nucleus","FunCat.ID":"11.02.03.01.01;11.02.03.04;70.10","FunCat.description":"transcription initiation;transcriptional control;nucleus","PubMed.ID":8224848,"subunits.Protein.name.":"Transcription initiation factor IIA subunit 1 ;Transcription initiation factor IIA subunit 2","subunits.Gene.name.":"GTF2A1;GTF2A2","subunits.Gene.name.syn.":"TF2A1;TF2A2","Disease.comment":"None","Subunits.comment":"GTF2A1 encodes both the alpha and beta subunits.","Complex.comment":"TFIIA is a heterotrimer of an alpha (p35), a beta (p19) and a gamma subunit (p12).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":490,"ComplexName":"TFIIA complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P52655;P52657","subunits.Entrez.IDs.":"2957;2958","Protein.complex.purification.method":"MI:0091- chromatography technologies","GO.ID":"GO:0006352;GO:2001141;GO:0006355;GO:0005634","GO.description":"DNA-templated transcription, initiation;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;nucleus","FunCat.ID":"11.02.03.01.01;11.02.03.04;70.10","FunCat.description":"transcription initiation;transcriptional control;nucleus","PubMed.ID":2247058,"subunits.Protein.name.":"Transcription initiation factor IIA subunit 1 ;Transcription initiation factor IIA subunit 2","subunits.Gene.name.":"GTF2A1;GTF2A2","subunits.Gene.name.syn.":"TF2A1;TF2A2","Disease.comment":"None","Subunits.comment":"GTF2A1 encodes both the alpha and beta subunits.","Complex.comment":"TFIIA is a heterotrimer of an alpha (p35), a beta (p19) and a gamma subunit (p12).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":492,"ComplexName":"DA complex","Organism":"Human","Synonyms":"TFIID-TFIIA complex","Cell.line":"None","subunits.UniProt.IDs.":"O00268;P20226;P21675;P49848;P52655;P52657;Q12962;Q15542;Q15543;Q15544;Q15545;Q16514;Q16594;Q5VWG9;Q6P1X5","subunits.Entrez.IDs.":"6874;6908;6872;6878;2957;2958;6881;6877;6884;6882;6879;6883;6880;83860;6873","Protein.complex.purification.method":"MI:0091- chromatography technologies","GO.ID":"GO:0006352;GO:2001141;GO:0006355;GO:0003677;GO:0005634","GO.description":"DNA-templated transcription, initiation;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.01.01;11.02.03.04;16.03.01;70.10","FunCat.description":"transcription initiation;transcriptional control;DNA binding;nucleus","PubMed.ID":2247058,"subunits.Protein.name.":"Transcription initiation factor TFIID subunit 4;TATA-box-binding protein;Transcription initiation factor TFIID subunit 1;Transcription initiation factor TFIID subunit 6;Transcription initiation factor IIA subunit 1 ;Transcription initiation factor IIA subunit 2 ;Transcription initiation factor TFIID subunit 10;Transcription initiation factor TFIID subunit 5;Transcription initiation factor TFIID subunit 13;Transcription initiation factor TFIID subunit 11;Transcription initiation factor TFIID subunit 7;Transcription initiation factor TFIID subunit 12;Transcription initiation factor TFIID subunit 9;Transcription initiation factor TFIID subunit 3 ;Transcription initiation factor TFIID subunit 2","subunits.Gene.name.":"TAF4;TBP;TAF1;TAF6;GTF2A1;GTF2A2;TAF10;TAF5;TAF13;TAF11;TAF7;TAF12;TAF9;TAF3;TAF2","subunits.Gene.name.syn.":"TAF2C TAF2C1 TAF4A TAFII130 TAFII135;GTF2D1 TF2D TFIID;BA2R CCG1 CCGS TAF2A;TAF2E TAFII70;TF2A1;TF2A2;TAF2A TAF2H TAFII30;TAF2D;TAF2K TAFII18;TAF2I;TAF2F TAFII55;TAF15 TAF2J TAFII20;TAF2G TAFII31;;CIF150 TAF2B","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"DA is a multiprotein complex consisting of TFIID complex and TFIIA complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":493,"ComplexName":"DAB complex","Organism":"Human","Synonyms":"TFIID-TFIIA-TFIIB complex","Cell.line":"None","subunits.UniProt.IDs.":"O00268;P20226;P21675;P49848;P52655;P52657;Q00403;Q12962;Q15542;Q15543;Q15544;Q15545;Q16514;Q16594;Q5VWG9;Q6P1X5","subunits.Entrez.IDs.":"6874;6908;6872;6878;2957;2958;2959;6881;6877;6884;6882;6879;6883;6880;83860;6873","Protein.complex.purification.method":"MI:0091- chromatography technologies","GO.ID":"GO:0006352;GO:2001141;GO:0006355;GO:0003677;GO:0005634","GO.description":"DNA-templated transcription, initiation;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.01.01;11.02.03.04;16.03.01;70.10","FunCat.description":"transcription initiation;transcriptional control;DNA binding;nucleus","PubMed.ID":2247058,"subunits.Protein.name.":"Transcription initiation factor TFIID subunit 4;TATA-box-binding protein;Transcription initiation factor TFIID subunit 1;Transcription initiation factor TFIID subunit 6;Transcription initiation factor IIA subunit 1 ;Transcription initiation factor IIA subunit 2 ;Transcription initiation factor IIB;Transcription initiation factor TFIID subunit 10;Transcription initiation factor TFIID subunit 5;Transcription initiation factor TFIID subunit 13;Transcription initiation factor TFIID subunit 11;Transcription initiation factor TFIID subunit 7;Transcription initiation factor TFIID subunit 12;Transcription initiation factor TFIID subunit 9;Transcription initiation factor TFIID subunit 3 ;Transcription initiation factor TFIID subunit 2","subunits.Gene.name.":"TAF4;TBP;TAF1;TAF6;GTF2A1;GTF2A2;GTF2B;TAF10;TAF5;TAF13;TAF11;TAF7;TAF12;TAF9;TAF3;TAF2","subunits.Gene.name.syn.":"TAF2C TAF2C1 TAF4A TAFII130 TAFII135;GTF2D1 TF2D TFIID;BA2R CCG1 CCGS TAF2A;TAF2E TAFII70;TF2A1;TF2A2;TF2B TFIIB;TAF2A TAF2H TAFII30;TAF2D;TAF2K TAFII18;TAF2I;TAF2F TAFII55;TAF15 TAF2J TAFII20;TAF2G TAFII31;;CIF150 TAF2B","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"DAB is a multiprotein complex consisting of TFIID complex, TFIIA complex and TFIIB.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":494,"ComplexName":"Cytochrome bc1-complex, mitochondrial","Organism":"Bovine","Synonyms":"Cytochrome bc1-complex (EC 1.10.2.2), mitochondrial; complex III; Cytochrome reductase; Ubiquinol:cytochrome c oxidoreductase","Cell.line":"heart muscle","subunits.UniProt.IDs.":"P00125;P00126;P00129;P00130;P00157;P07552;P13271;P13272;P23004;P31800","subunits.Entrez.IDs.":"512500;613899;616871;616109;3283889;281570;286885;287020;282394;282393","Protein.complex.purification.method":"MI:0047-far western blotting","GO.ID":"GO:0006099;GO:0006091;GO:0009060;GO:0006818;GO:0022904;GO:0005743","GO.description":"tricarboxylic acid cycle;generation of precursor metabolites and energy;aerobic respiration;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"02.10;01;02.13.03;20.01.15;02.11.07;70.16.05","FunCat.description":"tricarboxylic-acid pathway (citrate cycle, Krebs cycle, TCA cycle);METABOLISM;aerobic respiration;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":8386158,"subunits.Protein.name.":"Cytochrome c1, heme protein, mitochondrial;Cytochrome b-c1 complex subunit 6, mitochondrial;Cytochrome b-c1 complex subunit 7;Cytochrome b-c1 complex subunit 9;Cytochrome b;Cytochrome b-c1 complex subunit 10;Cytochrome b-c1 complex subunit 8;Cytochrome b-c1 complex subunit Rieske, mitochondrial;Cytochrome b-c1 complex subunit 2, mitochondrial;Cytochrome b-c1 complex subunit 1, mitochondrial","subunits.Gene.name.":"CYC1;UQCRH;UQCRB;UQCR10;MT-CYB;UQCR11;UQCRQ;UQCRFS1;UQCRC2;UQCRC1","subunits.Gene.name.syn.":"None;None;None;None;COB CYTB MTCYB;UQCR;None;None;None;None","Disease.comment":"None","Subunits.comment":"The mitochondrial targeting presequence of the Rieske iron-sulfur protein is processed in a single step after insertion into the cytochrome bc1 complex in mammals and retained as a subunit in the complex.","Complex.comment":"None","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":495,"ComplexName":"Cytochrome bc1-complex, mitochondrial","Organism":"Mouse","Synonyms":"Cytochrome bc1-complex (EC 1.10.2.2), mitochondrial; Complex III; Cytochrome reductase; Ubiquinol:cytochrome c oxidoreductase","Cell.line":"heart muscle","subunits.UniProt.IDs.":"P00158;P99028;Q8R1I1;Q9CPX8;Q9CQ69;Q9CR68;Q9CZ13;Q9D0M3;Q9D855;Q9DB77","subunits.Entrez.IDs.":"17711;66576;66152;66594;22272;66694;22273;66445;67530;67003","Protein.complex.purification.method":"MI:0069-mass spectrometry studies of complexes;MI:0019-coimmunoprecipitation","GO.ID":"GO:0006099;GO:0006091;GO:0009060;GO:0006818;GO:0022904;GO:0005743","GO.description":"tricarboxylic acid cycle;generation of precursor metabolites and energy;aerobic respiration;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"02.10;01;02.13.03;20.01.15;02.11.07;70.16.05","FunCat.description":"tricarboxylic-acid pathway (citrate cycle, Krebs cycle, TCA cycle);METABOLISM;aerobic respiration;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":16120479,"subunits.Protein.name.":"Cytochrome b;Cytochrome b-c1 complex subunit 6, mitochondrial;Cytochrome b-c1 complex subunit 9;Cytochrome b-c1 complex subunit 10;Cytochrome b-c1 complex subunit 8;Cytochrome b-c1 complex subunit Rieske, mitochondrial;Cytochrome b-c1 complex subunit 1, mitochondrial;Cytochrome c1, heme protein, mitochondrial;Cytochrome b-c1 complex subunit 7;Cytochrome b-c1 complex subunit 2, mitochondrial","subunits.Gene.name.":"Mt-Cyb;Uqcrh;Uqcr10;Uqcr11;Uqcrq;Uqcrfs1;Uqcrc1;Cyc1;Uqcrb;Uqcrc2","subunits.Gene.name.syn.":"Cob Cytb mt-Cytb Mtcyb;None;None;Uqcr;None;None;None;None;None;None","Disease.comment":"None","Subunits.comment":"Complex III consists of 11 subunits; displayed just 10 subunits; reason:Subunit V precursor (Rieske iron sulfur protein) contains subunit IX, compare PMID:8386158;subunit XI (Q9CPX8) could not be experimentally identified.","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":496,"ComplexName":"TFIID complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P29037;Q62311;Q80UV9;Q8C092;Q8C176;Q8K0H5;Q8VE65;Q8VI33;Q91WW6;Q99JX1;Q9EQH4;Q9R1C0","subunits.Entrez.IDs.":"21374;21343;270627;226182;319944;24075;66464;108143;228980;68776;63856;24074","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006352;GO:2001141;GO:0006355;GO:0003677;GO:0005634","GO.description":"DNA-templated transcription, initiation;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.01.01;11.02.03.04;16.03.01;70.10","FunCat.description":"transcription initiation;transcriptional control;DNA binding;nucleus","PubMed.ID":10438527,"subunits.Protein.name.":"TATA-box-binding protein;Transcription initiation factor TFIID subunit 6 ;Transcription initiation factor TFIID subunit 1;Transcription initiation factor TFIID subunit 5 ;Transcription initiation factor TFIID subunit 2 ;Transcription initiation factor TFIID subunit 10 ;Transcription initiation factor TFIID subunit 12 ;Transcription initiation factor TFIID subunit 9 ;TATA-binding protein associated factor TAFII135 ;Transcription initiation factor TFIID subunit 11 ;Transcription initiation factor TFIID subunit 8 ;Transcription initiation factor TFIID subunit 7","subunits.Gene.name.":"Tbp;Taf6;Taf1;Taf5;Taf2;Taf10;Taf12;Taf9;Taf4;Taf11;Taf8;Taf7","subunits.Gene.name.syn.":"Tfiid;Taf2e;Ccg1;;;Taf2h Tafii30;;Taf2g;Taf4a;;Tbn;Taf2f","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":497,"ComplexName":"TAF4-TAF12 subcomplex of TFIID complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00268;Q16514","subunits.Entrez.IDs.":"6874;6883","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0114- x-ray crystallography","GO.ID":"GO:0006352;GO:2001141;GO:0006355;GO:0005515;GO:0005634","GO.description":"DNA-templated transcription, initiation;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein binding;nucleus","FunCat.ID":"11.02.03.01.01;11.02.03.04;16.01;70.10","FunCat.description":"transcription initiation;transcriptional control;protein binding;nucleus","PubMed.ID":12237304,"subunits.Protein.name.":"Transcription initiation factor TFIID subunit 4;Transcription initiation factor TFIID subunit 12","subunits.Gene.name.":"TAF4;TAF12","subunits.Gene.name.syn.":"TAF2C TAF2C1 TAF4A TAFII130 TAFII135;TAF15 TAF2J TAFII20","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TAF12 forms a histone-like heterodimer with TAF4, rather than homodimerizing as suggested earlier (PMID:8598932).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":498,"ComplexName":"Ryk-Wny1-Fzd8 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04426;Q01887;Q61091","subunits.Entrez.IDs.":"22408;20187;14370","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016055","GO.description":"Wnt signaling pathway","FunCat.ID":"30.05.02.20","FunCat.description":"Wnt signalling pathway","PubMed.ID":15454084,"subunits.Protein.name.":"Proto-oncogene Wnt-1 ;Tyrosine-protein kinase RYK ;Frizzled-8","subunits.Gene.name.":"Wnt1;Ryk;Fzd8","subunits.Gene.name.syn.":"Int-1 Wnt-1;Mrk;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":499,"ComplexName":"Ryk-Wny1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04426;Q01887","subunits.Entrez.IDs.":"22408;20187","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016055","GO.description":"Wnt signaling pathway","FunCat.ID":"30.05.02.20","FunCat.description":"Wnt signalling pathway","PubMed.ID":15454084,"subunits.Protein.name.":"Proto-oncogene Wnt-1 ;Tyrosine-protein kinase RYK","subunits.Gene.name.":"Wnt1;Ryk","subunits.Gene.name.syn.":"Int-1 Wnt-1;Mrk","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":500,"ComplexName":"Ryk-Wnt3a complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P27467;Q01887","subunits.Entrez.IDs.":"22416;20187","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016055","GO.description":"Wnt signaling pathway","FunCat.ID":"30.05.02.20","FunCat.description":"Wnt signalling pathway","PubMed.ID":15454084,"subunits.Protein.name.":"Protein Wnt-3a;Tyrosine-protein kinase RYK","subunits.Gene.name.":"Wnt3a;Ryk","subunits.Gene.name.syn.":"Wnt-3a;Mrk","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":501,"ComplexName":"Ryk-Dvl1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P51141;Q01887","subunits.Entrez.IDs.":"13542;20187","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016055","GO.description":"Wnt signaling pathway","FunCat.ID":"30.05.02.20","FunCat.description":"Wnt signalling pathway","PubMed.ID":15454084,"subunits.Protein.name.":"Segment polarity protein dishevelled homolog DVL-1;Tyrosine-protein kinase RYK","subunits.Gene.name.":"Dvl1;Ryk","subunits.Gene.name.syn.":"Dvl;Mrk","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":502,"ComplexName":"Kir4.1-dystrophin complex, whole brain lysate","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P11531;Q9JM63","subunits.Entrez.IDs.":"13405;16513","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0030- cross-linking studies","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;eukaryotic plasma membrane / membrane attached","PubMed.ID":15102837,"subunits.Protein.name.":"Dystrophin;ATP-sensitive inward rectifier potassium channel 10","subunits.Gene.name.":"Dmd;Kcnj10","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"The dystrophin isoform has been described as Dp71.","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":503,"ComplexName":"Kir4.1-alpha-1-syntrophin complex, whole brain lysate","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"Q61234;Q9JM63","subunits.Entrez.IDs.":"20648;16513","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0030- cross-linking studies","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;eukaryotic plasma membrane / membrane attached","PubMed.ID":15102837,"subunits.Protein.name.":"Alpha-1-syntrophin;ATP-sensitive inward rectifier potassium channel 10","subunits.Gene.name.":"Snta1;Kcnj10","subunits.Gene.name.syn.":"Snt1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results suggest that Kir4.1 is localized in glial cells by its association with the DGC through a PDZ domain-mediated interaction with alpha-syntrophin and suggest an important role for the DGC in central nervous system physiology.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":504,"ComplexName":"Kir4.1-beta-dystroglycan complex, whole brain lysate","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"Q62165;Q9JM63","subunits.Entrez.IDs.":"13138;16513","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0030- cross-linking studies","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;eukaryotic plasma membrane / membrane attached","PubMed.ID":15102837,"subunits.Protein.name.":"Dystroglycan;ATP-sensitive inward rectifier potassium channel 10","subunits.Gene.name.":"Dag1;Kcnj10","subunits.Gene.name.syn.":"Dag-1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The dystroglycan subunit has been described as beta-dystroglycan.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":505,"ComplexName":"Kir4.1-dystrophin complex, cortical astrocytes","Organism":"Mouse","Synonyms":"None","Cell.line":"cortical astrocytes","subunits.UniProt.IDs.":"P11531;Q9JM63","subunits.Entrez.IDs.":"13405;16513","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0030-cross-linking studies","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;eukaryotic plasma membrane / membrane attached","PubMed.ID":15102837,"subunits.Protein.name.":"Dystrophin;ATP-sensitive inward rectifier potassium channel 10","subunits.Gene.name.":"Dmd;Kcnj10","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"The dystrophin isoform has been described as Dp71.","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":506,"ComplexName":"Kir4.1-alpha-1-syntrophin complex, cortical astrocytes","Organism":"Mouse","Synonyms":"None","Cell.line":"cortical astrocytes","subunits.UniProt.IDs.":"Q61234;Q9JM63","subunits.Entrez.IDs.":"20648;16513","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0030-cross-linking studies","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;eukaryotic plasma membrane / membrane attached","PubMed.ID":15102837,"subunits.Protein.name.":"Alpha-1-syntrophin;ATP-sensitive inward rectifier potassium channel 10","subunits.Gene.name.":"Snta1;Kcnj10","subunits.Gene.name.syn.":"Snt1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results suggest that Kir4.1 is localized in glial cells by its association with the DGC through a PDZ domain-mediated interaction with alpha-syntrophin and suggest an important role for the DGC in central nervous system physiology.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":507,"ComplexName":"Kir4.1-beta-dystroglycan complex, cortical astrocytes","Organism":"Mouse","Synonyms":"None","Cell.line":"cortical astrocytes","subunits.UniProt.IDs.":"Q62165;Q9JM63","subunits.Entrez.IDs.":"13138;16513","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0030-cross-linking studies","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;eukaryotic plasma membrane / membrane attached","PubMed.ID":15102837,"subunits.Protein.name.":"Dystroglycan;ATP-sensitive inward rectifier potassium channel 10","subunits.Gene.name.":"Dag1;Kcnj10","subunits.Gene.name.syn.":"Dag-1;None","Disease.comment":"None","Subunits.comment":"The dystroglycan subunit has been described as beta-dystroglycan.","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":508,"ComplexName":"TFIID complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00268;P20226;P21675;P49848;Q12962;Q15542;Q15544;Q15545;Q16514;Q16594","subunits.Entrez.IDs.":"6874;6908;6872;6878;6881;6877;6882;6879;6883;6880","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006352;GO:2001141;GO:0006355;GO:0003677;GO:0005634","GO.description":"DNA-templated transcription, initiation;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.01.01;11.02.03.04;16.03.01;70.10","FunCat.description":"transcription initiation;transcriptional control;DNA binding;nucleus","PubMed.ID":8663456,"subunits.Protein.name.":"Transcription initiation factor TFIID subunit 4;TATA-box-binding protein;Transcription initiation factor TFIID subunit 1;Transcription initiation factor TFIID subunit 6;Transcription initiation factor TFIID subunit 10;Transcription initiation factor TFIID subunit 5;Transcription initiation factor TFIID subunit 11;Transcription initiation factor TFIID subunit 7;Transcription initiation factor TFIID subunit 12;Transcription initiation factor TFIID subunit 9","subunits.Gene.name.":"TAF4;TBP;TAF1;TAF6;TAF10;TAF5;TAF11;TAF7;TAF12;TAF9","subunits.Gene.name.syn.":"TAF2C TAF2C1 TAF4A TAFII130 TAFII135;GTF2D1 TF2D TFIID;BA2R CCG1 CCGS TAF2A;TAF2E TAFII70;TAF2A TAF2H TAFII30;TAF2D;TAF2I;TAF2F TAFII55;TAF15 TAF2J TAFII20;TAF2G TAFII31","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":509,"ComplexName":"TFIID complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00268;P20226;P21675;P49848;Q12962;Q15542;Q15543;Q15544;Q15545;Q16514;Q16594;Q92804","subunits.Entrez.IDs.":"6874;6908;6872;6878;6881;6877;6884;6882;6879;6883;6880;8148","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006352;GO:2001141;GO:0006355;GO:0003677;GO:0005634","GO.description":"DNA-templated transcription, initiation;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.01.01;11.02.03.04;16.03.01;70.10","FunCat.description":"transcription initiation;transcriptional control;DNA binding;nucleus","PubMed.ID":8890175,"subunits.Protein.name.":"Transcription initiation factor TFIID subunit 4;TATA-box-binding protein;Transcription initiation factor TFIID subunit 1;Transcription initiation factor TFIID subunit 6;Transcription initiation factor TFIID subunit 10;Transcription initiation factor TFIID subunit 5;Transcription initiation factor TFIID subunit 13;Transcription initiation factor TFIID subunit 11;Transcription initiation factor TFIID subunit 7;Transcription initiation factor TFIID subunit 12;Transcription initiation factor TFIID subunit 9;TATA-binding protein-associated factor 2N","subunits.Gene.name.":"TAF4;TBP;TAF1;TAF6;TAF10;TAF5;TAF13;TAF11;TAF7;TAF12;TAF9;TAF15","subunits.Gene.name.syn.":"TAF2C TAF2C1 TAF4A TAFII130 TAFII135;GTF2D1 TF2D TFIID;BA2R CCG1 CCGS TAF2A;TAF2E TAFII70;TAF2A TAF2H TAFII30;TAF2D;TAF2K TAFII18;TAF2I;TAF2F TAFII55;TAF15 TAF2J TAFII20;TAF2G TAFII31;RBP56 TAF2N","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":510,"ComplexName":"TFIID subcomplex, testis-specific","Organism":"Mouse","Synonyms":"None","Cell.line":"male gonad (testis)","subunits.UniProt.IDs.":"P29037;Q9D3R9","subunits.Entrez.IDs.":"21374;74469","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0006352;GO:2001141;GO:0006355;GO:0003677;GO:0007276;GO:0005634","GO.description":"DNA-templated transcription, initiation;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;gamete generation;nucleus","FunCat.ID":"11.02.03.01.01;11.02.03.04;16.03.01;41.05.25;70.10","FunCat.description":"transcription initiation;transcriptional control;DNA binding;gametogenesis;nucleus","PubMed.ID":12665565,"subunits.Protein.name.":"TATA-box-binding protein;Transcription initiation factor TFIID subunit 7-like","subunits.Gene.name.":"Tbp;Taf7l","subunits.Gene.name.syn.":"Tfiid;Taf2q","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":511,"ComplexName":"TFIID subcomplex, testis-specific","Organism":"Mouse","Synonyms":"None","Cell.line":"male gonad (testis)","subunits.UniProt.IDs.":"Q80UV9;Q9D3R9","subunits.Entrez.IDs.":"270627;74469","Protein.complex.purification.method":"MI:0018-two hybrid","GO.ID":"GO:0006352;GO:2001141;GO:0006355;GO:0003677;GO:0007276;GO:0005634","GO.description":"DNA-templated transcription, initiation;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;gamete generation;nucleus","FunCat.ID":"11.02.03.01.01;11.02.03.04;16.03.01;41.05.25;70.10","FunCat.description":"transcription initiation;transcriptional control;DNA binding;gametogenesis;nucleus","PubMed.ID":12665565,"subunits.Protein.name.":"Transcription initiation factor TFIID subunit 1;Transcription initiation factor TFIID subunit 7-like","subunits.Gene.name.":"Taf1;Taf7l","subunits.Gene.name.syn.":"Ccg1;Taf2q","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":512,"ComplexName":"AQP-1 regulatory complex","Organism":"Rat","Synonyms":"None","Cell.line":"pancreas","subunits.UniProt.IDs.":"P08753;P14423;P29975;P35525;Q63664","subunits.Entrez.IDs.":"25643;29692;25240;29232;25472","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006811;GO:0015267;GO:0046903;GO:0032940","GO.description":"ion transport;channel activity;secretion;secretion by cell","FunCat.ID":"20.01.01;20.03.01;20.09.16","FunCat.description":"ion transport;channel / pore class transport;cellular export and secretion","PubMed.ID":14759764,"subunits.Protein.name.":"Guanine nucleotide-binding protein G;Phospholipase A2, membrane associated ;Aquaporin-1 ;Chloride channel protein 2 ;ATP-sensitive inward rectifier potassium channel 8","subunits.Gene.name.":"Gnai3;Pla2g2a;Aqp1;Clcn2;Kcnj8","subunits.Gene.name.syn.":"Gnai-3;;Chip28;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":513,"ComplexName":"TFTC complex (TATA-binding protein-free TAF-II-containing complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00268;O15265;O75486;O75528;O75529;P49848;Q12962;Q15393;Q15542;Q15545;Q16514;Q16594;Q6P1X5;Q92830;Q9HBM6;Q9Y4A5;Q9Y6J9","subunits.Entrez.IDs.":"6874;6314;8464;10474;27097;6878;6881;23450;6877;6879;6883;6880;6873;2648;51616;8295;10629","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0006- anti bait coimmunoprecipitation; MI:0071- molecular sieving","GO.ID":"GO:0006265;GO:0006352;GO:0045893;GO:0006473;GO:0006476;GO:0051276;GO:0005634","GO.description":"DNA topological change;DNA-templated transcription, initiation;positive regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.01.01;11.02.03.04.01;14.07.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription initiation;transcription activation;modification by acetylation, deacetylation;organization of chromosome structure;nucleus","PubMed.ID":15899866,"subunits.Protein.name.":"Transcription initiation factor TFIID subunit 4;Ataxin-7;Transcription initiation protein SPT3 homolog;Transcriptional adapter 3;TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L;Transcription initiation factor TFIID subunit 6;Transcription initiation factor TFIID subunit 10;Splicing factor 3B subunit 3;Transcription initiation factor TFIID subunit 5;Transcription initiation factor TFIID subunit 7;Transcription initiation factor TFIID subunit 12;Transcription initiation factor TFIID subunit 9;Transcription initiation factor TFIID subunit 2 ;Histone acetyltransferase KAT2A;Transcription initiation factor TFIID subunit 9B;Transformation/transcription domain-associated protein;TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L","subunits.Gene.name.":"TAF4;ATXN7;SUPT3H;TADA3;TAF5L;TAF6;TAF10;SF3B3;TAF5;TAF7;TAF12;TAF9;TAF2;KAT2A;TAF9B;TRRAP;TAF6L","subunits.Gene.name.syn.":"TAF2C TAF2C1 TAF4A TAFII130 TAFII135;SCA7;SPT3;ADA3, TADA3L;PAF65B;TAF2E TAFII70;TAF2A TAF2H TAFII30;KIAA0017 SAP130;TAF2D;TAF2F TAFII55;TAF15 TAF2J TAFII20;TAF2G TAFII31;CIF150 TAF2B;GCN5, GCN5L2, HGCN5;TAF9L;PAF400;PAF65A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Gene expression profiling revealed that Taf9 and Taf9b control the expression of different sets of genes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":514,"ComplexName":"TFIID-beta complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00268;P20226;P21675;P49848;Q12962;Q15542;Q15543;Q15544;Q15545;Q16514;Q16594;Q9HBM6","subunits.Entrez.IDs.":"6874;6908;6872;6878;6881;6877;6884;6882;6879;6883;6880;51616","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0004- affinity chromatography technologies; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006352;GO:2001141;GO:0006355;GO:0003677;GO:0005634","GO.description":"DNA-templated transcription, initiation;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.01.01;11.02.03.04;16.03.01;70.10","FunCat.description":"transcription initiation;transcriptional control;DNA binding;nucleus","PubMed.ID":15899866,"subunits.Protein.name.":"Transcription initiation factor TFIID subunit 4;TATA-box-binding protein;Transcription initiation factor TFIID subunit 1;Transcription initiation factor TFIID subunit 6;Transcription initiation factor TFIID subunit 10;Transcription initiation factor TFIID subunit 5;Transcription initiation factor TFIID subunit 13;Transcription initiation factor TFIID subunit 11;Transcription initiation factor TFIID subunit 7;Transcription initiation factor TFIID subunit 12;Transcription initiation factor TFIID subunit 9;Transcription initiation factor TFIID subunit 9B","subunits.Gene.name.":"TAF4;TBP;TAF1;TAF6;TAF10;TAF5;TAF13;TAF11;TAF7;TAF12;TAF9;TAF9B","subunits.Gene.name.syn.":"TAF2C TAF2C1 TAF4A TAFII130 TAFII135;GTF2D1 TF2D TFIID;BA2R CCG1 CCGS TAF2A;TAF2E TAFII70;TAF2A TAF2H TAFII30;TAF2D;TAF2K TAFII18;TAF2I;TAF2F TAFII55;TAF15 TAF2J TAFII20;TAF2G TAFII31;TAF9L","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Gene expression profiling revealed that Taf9 and Taf9b control the expression of different sets of genes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":515,"ComplexName":"Inner medullary AKAP-signaling complex","Organism":"Rat","Synonyms":"None","Cell.line":"IMCD (inner medullary collecting duct) endosomes","subunits.UniProt.IDs.":"P09217;P12368;P63329;Q5U301","subunits.Entrez.IDs.":"25522;29699;24674;None","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0006468;GO:0006470;GO:0046777;GO:0005768","GO.description":"intracellular protein transport;protein targeting;protein transport;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;endosome","FunCat.ID":"14.04;20.01.10;14.07.03;70.22","FunCat.description":"protein targeting, sorting and translocation;protein transport;modification by phosphorylation, dephosphorylation, autophosphorylation;endosome","PubMed.ID":11592953,"subunits.Protein.name.":"Protein kinase C zeta type;cAMP-dependent protein kinase type II-alpha regulatory subunit;Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform;A-kinase anchor protein 2","subunits.Gene.name.":"Prkcz;Prkar2a;Ppp3ca;Akap2","subunits.Gene.name.syn.":"Pkcz;None;Calna;None","Disease.comment":"None","Subunits.comment":"The 75- to 90-kDa putative AKAP protein(s) reported on here awaits further characterization to determine whether it is a novel member of the AKAP family or represents a member of the AKAP-KL (expressed in kidney and lung) family of proteins, as reported. For annotation of the complex AKAP-KL (Akap2) was used.Since the authors did not specify PKA type II regulatory subunit RII, we used Prkar2a.Since the authors did not specify  PP2B catalytic subunit, we used Prkar2a.","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":516,"ComplexName":"Cytochrome bc1-complex, mitochondrial","Organism":"Rat","Synonyms":"Cytochrome bc1-complex (EC 1.10.2.2), mitochondrial; Complex III; Cytochrome reductase; Ubiquinol:cytochrome c oxidoreductase","Cell.line":"heart muscle","subunits.UniProt.IDs.":"A9UMV7;B2RYS2;P00159;P20788;P32551;Q5M9I5;Q68FY0;Q7TQ16;Q8R1I1;Q9D0M3","subunits.Entrez.IDs.":"690848;362897;None;291103;293448;366448;301011;497902;66152;66445","Protein.complex.purification.method":"MI:0047-far western blotting","GO.ID":"GO:0006099;GO:0006091;GO:0009060;GO:0006818;GO:0022904;GO:0005743","GO.description":"tricarboxylic acid cycle;generation of precursor metabolites and energy;aerobic respiration;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"02.10;01;02.13.03;20.01.15;02.11.07;70.16.05","FunCat.description":"tricarboxylic-acid pathway (citrate cycle, Krebs cycle, TCA cycle);METABOLISM;aerobic respiration;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":12794875,"subunits.Protein.name.":"Protein Uqcr11;Cytochrome b-c1 complex subunit 7;Cytochrome b;Cytochrome b-c1 complex subunit Rieske, mitochondrial;Cytochrome b-c1 complex subunit 2, mitochondrial;Cytochrome b-c1 complex subunit 6, mitochondrial;Cytochrome b-c1 complex subunit 1, mitochondrial;Cytochrome b-c1 complex subunit 8;Cytochrome b-c1 complex subunit 9;Cytochrome c1, heme protein, mitochondrial","subunits.Gene.name.":"Uqcr11;Uqcrb;Mt-Cyb;Uqcrfs1;Uqcrc2;Uqcrh;Uqcrc1;Uqcrq;Uqcr10;Cyc1","subunits.Gene.name.syn.":"LOC686442 Uqcr;LOC685596;Cob Cytb mt-Cytb Mtcyb;None;None;None;None;Qpc;None;None","Disease.comment":"None","Subunits.comment":"Since the complete protein information from rat was not available in the UniProt database at the time of annotation, some of the orthologous proteins from mouse (Cyc1, Uqcr10) were used.","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":517,"ComplexName":"Kinase-scaffold-phosphatase complex, PKA-AKAP79-CaN","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P13861;P24588;Q08209","subunits.Entrez.IDs.":"5576;9495;5530","Protein.complex.purification.method":"MI:0055- fluorescent resonance energy transfer","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0006468;GO:0006470;GO:0046777;GO:0006461;GO:0007166;GO:0005886;GO:0005856","GO.description":"intracellular protein transport;protein targeting;protein transport;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;protein complex assembly;cell surface receptor signaling pathway;plasma membrane;cytoskeleton","FunCat.ID":"14.04;20.01.10;14.07.03;14.10;30.05;70.02;70.04","FunCat.description":"protein targeting, sorting and translocation;protein transport;modification by phosphorylation, dephosphorylation, autophosphorylation;assembly of protein complexes;transmembrane signal transduction;eukaryotic plasma membrane / membrane attached;cytoskeleton","PubMed.ID":12507994,"subunits.Protein.name.":"cAMP-dependent protein kinase type II-alpha regulatory subunit;A-kinase anchor protein 5;Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform","subunits.Gene.name.":"PRKAR2A;AKAP5;PPP3CA","subunits.Gene.name.syn.":"PKR2, PRKAR2;AKAP79;CALNA CNA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":518,"ComplexName":"AKAP250-PKA-PDE4D complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"P17612;Q02952;Q08499","subunits.Entrez.IDs.":"5566;9590;5144","Protein.complex.purification.method":"MI:0415-enzymatic studies;MI:0019-coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0008104;GO:0030234;GO:0050790;GO:0019933;GO:0005886","GO.description":"intracellular protein transport;protein targeting;protein transport;protein localization;enzyme regulator activity;regulation of catalytic activity;cAMP-mediated signaling;plasma membrane","FunCat.ID":"14.04;20.01.10;18.01.03;18.02.01;30.01.09.07;70.02","FunCat.description":"protein targeting, sorting and translocation;protein transport;regulation by localization;enzymatic activity regulation / enzyme regulator;cAMP/cGMP mediated signal transduction;eukaryotic plasma membrane / membrane attached","PubMed.ID":16642035,"subunits.Protein.name.":"cAMP-dependent protein kinase catalytic subunit alpha;A-kinase anchor protein 12;cAMP-specific 3',5'-cyclic phosphodiesterase 4D","subunits.Gene.name.":"PRKACA;AKAP12;PDE4D","subunits.Gene.name.syn.":"PKACA;AKAP250;DPDE3","Disease.comment":"None","Subunits.comment":"Since the authors did not specify PKA catalytic subunit, we used PRKACA.","Complex.comment":"PDE4D protein isoforms were specified as PDE4D5 and PDE4D3. The authors identified gravin as the AKAP responsible for the localized regulation of cAMP levels by PKA and PDE4 activity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":519,"ComplexName":"AMY-1-S-AKAP84-RII-beta complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P31323;Q92667;Q99417","subunits.Entrez.IDs.":"5577;8165;26292","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0019933;GO:0007276;GO:0005739","GO.description":"cAMP-mediated signaling;gamete generation;mitochondrion","FunCat.ID":"30.01.09.07;41.05.25;70.16","FunCat.description":"cAMP/cGMP mediated signal transduction;gametogenesis;mitochondrion","PubMed.ID":11483602,"subunits.Protein.name.":"cAMP-dependent protein kinase type II-beta regulatory subunit;A-kinase anchor protein 1, mitochondrial ;C-Myc-binding protein","subunits.Gene.name.":"PRKAR2B;AKAP1;MYCBP","subunits.Gene.name.syn.":"None;AKAP149 PRKA1;AMY1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":520,"ComplexName":"KCNQ1 macromolecular complex","Organism":"Human","Synonyms":"None","Cell.line":"heart muscle","subunits.UniProt.IDs.":"P13861;P17612;P51787;P62136;Q99996","subunits.Entrez.IDs.":"5576;5566;3784;5499;10142","Protein.complex.purification.method":"MI:0096-pull down;MI:0019-coimmunoprecipitation","GO.ID":"GO:0005216;GO:0019933;GO:0050896","GO.description":"ion channel activity;cAMP-mediated signaling;response to stimulus","FunCat.ID":"20.03.01.01;30.01.09.07;36.25","FunCat.description":"ion channels;cAMP/cGMP mediated signal transduction;animal specific systemic sensing and response","PubMed.ID":11799244,"subunits.Protein.name.":"cAMP-dependent protein kinase type II-alpha regulatory subunit;cAMP-dependent protein kinase catalytic subunit alpha;Potassium voltage-gated channel subfamily KQT member 1;Serine/threonine-protein phosphatase PP1-alpha catalytic subunit;A-kinase anchor protein 9","subunits.Gene.name.":"PRKAR2A;PRKACA;KCNQ1;PPP1CA;AKAP9","subunits.Gene.name.syn.":"PKR2, PRKAR2;PKACA;KCNA8, KCNA9, KVLQT1, Kv1.7;PPP1A;AKAP350 AKAP450 KIAA0803","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex is required for beta adrenergic receptor modulation of the KCNQ1-KCNE1 potassium channel.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":521,"ComplexName":"Polycystin-1-E-cadherin-beta-catenin complex","Organism":"Human","Synonyms":"None","Cell.line":"epithelium","subunits.UniProt.IDs.":"P12830;P35222;P98161","subunits.Entrez.IDs.":"999;1499;5310","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0045216;GO:0007043;GO:0030855;GO:0002009;GO:0001822;GO:0005886;GO:0005737","GO.description":"cell-cell junction organization;cell-cell junction assembly;epithelial cell differentiation;morphogenesis of an epithelium;kidney development;plasma membrane;cytoplasm","FunCat.ID":"42.06.04;45.03.09;47.03.07.01;70.02;70.03","FunCat.description":"intercellular junction (gap junction/adherens junction);epithelium;kidney;eukaryotic plasma membrane / membrane attached;cytoplasm","PubMed.ID":14718571,"subunits.Protein.name.":"Cadherin-1;Catenin beta-1;Polycystin-1","subunits.Gene.name.":"CDH1;CTNNB1;PKD1","subunits.Gene.name.syn.":"CDHE UVO;CTNNB;None","Disease.comment":"Polycystin-1-E-cadherin-beta-catenin complex is involved in autosomal dominant polycystic kidney disease (ADPKD). The authors suggest that the expression of mutant polycystin-1 in ADPKD cells, which fails to be cell surface-expressed and assemble into multiprotein complexes with E-cadherin, results in altered cell-cell adhesion and polycystin-1 signaling, thereby triggering dedifferentiation.","Subunits.comment":"None","Complex.comment":"Complex is disrupted in ADPKD cells.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":522,"ComplexName":"Polycystin-1-E-cadherin-beta-catenin-Flotillin-2 complex","Organism":"Human","Synonyms":"None","Cell.line":"kidney epithelium","subunits.UniProt.IDs.":"P12830;P35222;P98161;Q14254","subunits.Entrez.IDs.":"999;1499;5310;2319","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0029-cosedimentation through density gradients","GO.ID":"GO:0008289;GO:0045216;GO:0007043;GO:0030855;GO:0002009;GO:0001822;GO:0005886","GO.description":"lipid binding;cell-cell junction organization;cell-cell junction assembly;epithelial cell differentiation;morphogenesis of an epithelium;kidney development;plasma membrane","FunCat.ID":"16.09;42.06.04;45.03.09;47.03.07.01;70.02","FunCat.description":"lipid binding;intercellular junction (gap junction/adherens junction);epithelium;kidney;eukaryotic plasma membrane / membrane attached","PubMed.ID":16038619,"subunits.Protein.name.":"Cadherin-1;Catenin beta-1;Polycystin-1;Flotillin-2","subunits.Gene.name.":"CDH1;CTNNB1;PKD1;FLOT2","subunits.Gene.name.syn.":"CDHE UVO;CTNNB;None;ESA1 M17S1","Disease.comment":"PKD1 is involved in ADPKD (autosomal dominant polycystic kidney disease).","Subunits.comment":"None","Complex.comment":"The authors conclude that even though the large multiprotein complex formed by polycystin-1, E-cadherin, beta-catenin and flotillin-2 is not associated with typical lipid rafts, it contains cholesterol molecules that mediate interactions between complexed proteins and may represent a specific membrane domain organization.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":523,"ComplexName":"Yotiao-RII-NR1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"striatal and cerebellar neurons","subunits.UniProt.IDs.":"P12368;P12369;P35439;Q9JHE0","subunits.Entrez.IDs.":"29699;24679;24408;246150","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0030545;GO:0019933","GO.description":"receptor regulator activity;cAMP-mediated signaling","FunCat.ID":"18.02.07;30.01.09.07","FunCat.description":"regulator of receptor activity;cAMP/cGMP mediated signal transduction","PubMed.ID":10618500,"subunits.Protein.name.":"cAMP-dependent protein kinase type II-alpha regulatory subunit;cAMP-dependent protein kinase type II-beta regulatory subunit;Glutamate receptor ionotropic, NMDA 1 ;Yotiao protein","subunits.Gene.name.":"Prkar2a;Prkar2b;Grin1;Akap9","subunits.Gene.name.syn.":"None;None;Nmdar1;yotiao","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex probably promote cAMP-dependent modulation of NMDA receptor activity at synapses.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":525,"ComplexName":"TIP60 histone acetylase complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O96019;Q92993;Q9Y230;Q9Y265;Q9Y4A5","subunits.Entrez.IDs.":"86;10524;10856;8607;8295","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0051276;GO:0006281;GO:0006265;GO:0006473;GO:0006476;GO:0003677;GO:0006915;GO:0051276;GO:0005634","GO.description":"chromosome organization;DNA repair;DNA topological change;protein acetylation;protein deacetylation;DNA binding;apoptotic process;chromosome organization;nucleus","FunCat.ID":"42.10.03;10.01.05.01;10.01.09.05;14.07.04;16.03.01;40.10.02;70.10","FunCat.description":"organization of chromosome structure;DNA repair;DNA conformation modification (e.g. chromatin);modification by acetylation, deacetylation;DNA binding;apoptosis (type I programmed cell death);nucleus","PubMed.ID":10966108,"subunits.Protein.name.":"Actin-like protein 6A;Histone acetyltransferase KAT5;RuvB-like 2;RuvB-like 1;Transformation/transcription domain-associated protein","subunits.Gene.name.":"ACTL6A;KAT5;RUVBL2;RUVBL1;TRRAP","subunits.Gene.name.syn.":"BAF53 BAF53A INO80K;HTATIP TIP60;INO80J TIP48 TIP49B;INO80H NMP238 TIP49 TIP49A;PAF400","Disease.comment":"None","Subunits.comment":"Additional unknown members of the TIP60 complex (p160, p150, p100, p70, p57, p40, p31, p29) have been isolated.","Complex.comment":"The TIP60 histone acetylase complex plays a role in DNA repair and apoptosis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":526,"ComplexName":"TRPC3-TRPC4 channel complex, redox-sensitive","Organism":"Pig","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q9QUQ5;Q9QZC1","subunits.Entrez.IDs.":"22066;22065","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0000302;GO:0006979;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;response to reactive oxygen species;response to oxidative stress;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;32.01.01;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;oxidative stress response;eukaryotic plasma membrane / membrane attached","PubMed.ID":16537542,"subunits.Protein.name.":"Short transient receptor potential channel 4 ;Short transient receptor potential channel 3","subunits.Gene.name.":"Trpc4;Trpc3","subunits.Gene.name.syn.":"Trrp4;Trp3 Trrp3","Disease.comment":"None","Subunits.comment":"Since TRPC3 and TRPC4 from pig were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.","Complex.comment":"Complex analysed in porcine aortic endothelial cells (PAECs). The authors propose TRPC3 and TRPC4 as subunits of native endothelial cation channels that are governed by the cellular redox state.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":527,"ComplexName":"TRPC3-TRPC4 channel complex, redox-sensitive","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q13507;Q9UBN4","subunits.Entrez.IDs.":"7222;7223","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0055- fluorescent resonance energy transfer","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0000302;GO:0006979;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;response to reactive oxygen species;response to oxidative stress;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;32.01.01;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;oxidative stress response;eukaryotic plasma membrane / membrane attached","PubMed.ID":16537542,"subunits.Protein.name.":"Short transient receptor potential channel 3 ;Short transient receptor potential channel 4","subunits.Gene.name.":"TRPC3;TRPC4","subunits.Gene.name.syn.":"TRP3;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex analysed in the HEK293 expression system. The authors propose TRPC3 and TRPC4 as subunits of native endothelial cation channels that are governed by the cellular redox state.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":528,"ComplexName":"NuA4/Tip60 HAT complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95619;O96019;Q15014;Q92993;Q96L91;Q9H0E9;Q9H2F5;Q9HAF1;Q9NPF5;Q9NV56;Q9NXR8;Q9UBU8;Q9Y230;Q9Y265;Q9Y4A5","subunits.Entrez.IDs.":"8089;86;9643;10524;57634;10902;80314;64769;55929;55257;54556;10933;10856;8607;8295","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006794;GO:0006796;GO:0051276;GO:0006281;GO:0006265;GO:0006473;GO:0006476;GO:0003677;GO:0051276;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;chromosome organization;DNA repair;DNA topological change;protein acetylation;protein deacetylation;DNA binding;chromosome organization;nucleus","FunCat.ID":"01.04;42.10.03;10.01.05.01;10.01.09.05;14.07.04;16.03.01;70.10","FunCat.description":"phosphate metabolism;organization of chromosome structure;DNA repair;DNA conformation modification (e.g. chromatin);modification by acetylation, deacetylation;DNA binding;nucleus","PubMed.ID":12963728,"subunits.Protein.name.":"YEATS domain-containing protein 4;Actin-like protein 6A;Mortality factor 4-like protein 2 ;Histone acetyltransferase KAT5;E1A-binding protein p400;Bromodomain-containing protein 8;Enhancer of polycomb homolog 1;Chromatin modification-related protein MEAF6;DNA methyltransferase 1-associated protein 1;MRG/MORF4L-binding protein ;Inhibitor of growth protein 3;Mortality factor 4-like protein 1;RuvB-like 2;RuvB-like 1;Transformation/transcription domain-associated protein","subunits.Gene.name.":"YEATS4;ACTL6A;MORF4L2;KAT5;EP400;BRD8;EPC1;MEAF6;DMAP1;MRGBP;ING3;MORF4L1;RUVBL2;RUVBL1;TRRAP","subunits.Gene.name.syn.":"GAS41;BAF53 BAF53A INO80K;KIAA0026 MRGX;HTATIP TIP60;CAGH32 KIAA1498 KIAA1818 TNRC12;SMAP SMAP2;None;C1orf149 CENP-28 EAF6;KIAA1425;C20orf20;None;MRG15;INO80J TIP48 TIP49B;INO80H NMP238 TIP49 TIP49A;PAF400","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The NuA4 histone acetyltransferase (HAT) multisubunit complex is responsible for acetylation of histone H4 and H2A N-terminal tails in yeast. The NuA4/Tip60 HAT complex is highly conserved in eukaryotes playing primary roles in transcription, cellular response to DNA damage, and cell cycle control.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":529,"ComplexName":"NuA4/Tip60 HAT complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95619;O96019;Q15014;Q15906;Q92993;Q96L91;Q9H0E9;Q9H2F5;Q9HAF1;Q9NPF5;Q9NV56;Q9NXR8;Q9UBU8;Q9Y230;Q9Y265;Q9Y4A5","subunits.Entrez.IDs.":"8089;86;9643;6944;10524;57634;10902;80314;64769;55929;55257;54556;10933;10856;8607;8295","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006794;GO:0006796;GO:0051276;GO:0006281;GO:0006265;GO:0006473;GO:0006476;GO:0003677;GO:0051276;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;chromosome organization;DNA repair;DNA topological change;protein acetylation;protein deacetylation;DNA binding;chromosome organization;nucleus","FunCat.ID":"01.04;42.10.03;10.01.05.01;10.01.09.05;14.07.04;16.03.01;70.10","FunCat.description":"phosphate metabolism;organization of chromosome structure;DNA repair;DNA conformation modification (e.g. chromatin);modification by acetylation, deacetylation;DNA binding;nucleus","PubMed.ID":15647280,"subunits.Protein.name.":"YEATS domain-containing protein 4;Actin-like protein 6A;Mortality factor 4-like protein 2 ;Vacuolar protein sorting-associated protein 72 homolog ;Histone acetyltransferase KAT5;E1A-binding protein p400;Bromodomain-containing protein 8;Enhancer of polycomb homolog 1;Chromatin modification-related protein MEAF6;DNA methyltransferase 1-associated protein 1;MRG/MORF4L-binding protein ;Inhibitor of growth protein 3;Mortality factor 4-like protein 1;RuvB-like 2;RuvB-like 1;Transformation/transcription domain-associated protein","subunits.Gene.name.":"YEATS4;ACTL6A;MORF4L2;VPS72;KAT5;EP400;BRD8;EPC1;MEAF6;DMAP1;MRGBP;ING3;MORF4L1;RUVBL2;RUVBL1;TRRAP","subunits.Gene.name.syn.":"GAS41;BAF53 BAF53A INO80K;KIAA0026 MRGX;TCFL1 YL1;HTATIP TIP60;CAGH32 KIAA1498 KIAA1818 TNRC12;SMAP SMAP2;None;C1orf149 CENP-28 EAF6;KIAA1425;C20orf20;None;MRG15;INO80J TIP48 TIP49B;INO80H NMP238 TIP49 TIP49A;PAF400","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The NuA4 histone acetyltransferase (HAT) multisubunit complex is responsible for acetylation of histone H4 and H2A N-terminal tails in yeast. The NuA4/Tip60 HAT complex is highly conserved in eukaryotes playing primary roles in transcription, cellular response to DNA damage, and cell cycle control.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":530,"ComplexName":"Cytochrome c oxidase, mitochondrial","Organism":"Bovine","Synonyms":"Cytochrome c oxidase (EC 1.9.3.1), mitochondrial; Complex IV; COX","Cell.line":"None","subunits.UniProt.IDs.":"P00396;P00415;P00423;P00426;P00428;P00429;P00430;P04038;P07470;P07471;P10175;P13183;P68530","subunits.Entrez.IDs.":"None;None;281090;444878;287012;100270792;327718;782486;338086;282200;615757;327674;3283880","Protein.complex.purification.method":"MI:0024-confirmational text mining","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":11943460,"subunits.Protein.name.":"Cytochrome c oxidase subunit 1;Cytochrome c oxidase subunit 3;Cytochrome c oxidase subunit 4 isoform 1, mitochondrial;Cytochrome c oxidase subunit 5A, mitochondrial;Cytochrome c oxidase subunit 5B, mitochondrial;Cytochrome c oxidase subunit 6B1;Cytochrome c oxidase subunit 7C, mitochondrial;Cytochrome c oxidase subunit 6C;Cytochrome c oxidase subunit 7A1, mitochondrial;Cytochrome c oxidase subunit 6A2, mitochondrial;Cytochrome c oxidase subunit 8B, mitochondrial;Cytochrome c oxidase subunit 7B, mitochondrial;Cytochrome c oxidase subunit 2","subunits.Gene.name.":"MT-CO1;MT-CO3;COX4I1;COX5A;COX5B;COX6B1;COX7C;COX6C;COX7A1;COX6A2;COX8B;COX7B;MT-CO2","subunits.Gene.name.syn.":"COI COXI MTCO1;COIII COXIII MTCO3;COX4;None;None;COX6B;COX7CP1;None;COX7A COX7AH;COX6A;COX8H;None;COII COXII MTCO2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cytochrome oxidase (COX) is the fourth complex ofthe mitochondrial respiratory chain. It transfers electrons fromferrocytochrome c to molecular oxygen.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":531,"ComplexName":"XPA-ERCC1-ERCC4 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P07992;P23025;Q92889","subunits.Entrez.IDs.":"2067;7507;2072","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006281;GO:0006950;GO:0005634","GO.description":"DNA repair;response to stress;nucleus","FunCat.ID":"10.01.05.01;32.01;70.10","FunCat.description":"DNA repair;stress response;nucleus","PubMed.ID":8197175,"subunits.Protein.name.":"DNA excision repair protein ERCC-1;DNA repair protein complementing XP-A cells ;DNA repair endonuclease XPF","subunits.Gene.name.":"ERCC1;XPA;ERCC4","subunits.Gene.name.syn.":";XPAC;ERCC11 XPF","Disease.comment":"ERCC4 is involved in Xeroderma pigmentosum group F.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":532,"ComplexName":"M1 mAChR-TRPC6-multiprotein complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P05696;P08482;P62161;P63329;Q62658;Q99N78","subunits.Entrez.IDs.":"24680;25229;None;24674;25639;89823","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0030234;GO:0050790;GO:0008324;GO:0006812;GO:0015267;GO:0007213","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;enzyme regulator activity;regulation of catalytic activity;cation transmembrane transporter activity;cation transport;channel activity;G-protein coupled acetylcholine receptor signaling pathway","FunCat.ID":"14.07.03;18.02.01;20.01.01.01;20.03.01;30.05.02.24.02","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;enzymatic activity regulation / enzyme regulator;cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);channel / pore class transport;acetyl choline receptor signalling pathway","PubMed.ID":15994335,"subunits.Protein.name.":"Protein kinase C alpha type;Muscarinic acetylcholine receptor M1;Calmodulin;Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform;Peptidyl-prolyl cis-trans isomerase FKBP1A;Protein Trpc6","subunits.Gene.name.":"Prkca;Chrm1;Calm1; Cal;Ppp3ca;Fkbp1a;Trpc6","subunits.Gene.name.syn.":"Pkca;Chrm-1;Calm, Cam, Cam1, Cam2, Camb, Cam3, Camc;Calna;Fkbp1;trp6A","Disease.comment":"None","Subunits.comment":"Since the authors did not specify Protein kinase C , we used isoform Prkca.","Complex.comment":"Complex constitutes only after stimulation of M1 mAChRs with carbachol. The results of the examinations of the time course of these associations suggest that M1 mAChRs and PKC associate with TRPC6 channels at the same time or slightly earlier than FKBP12, calcineurin, and calmodulin and that the later proteins remain in the TRPC6 complex after M1 mAChRs and PKC have disappeared.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":533,"ComplexName":"IMP3-IMP4-MPP10 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00566;Q96G21;Q9NV31","subunits.Entrez.IDs.":"10199;92856;55272","Protein.complex.purification.method":"MI:0096- pull down; MI:0029- cosedimentation through density gradients; MI:0019- coimmunoprecipitation","GO.ID":"GO:0006461;GO:0005515;GO:0003723;GO:0005634","GO.description":"protein complex assembly;protein binding;RNA binding;nucleus","FunCat.ID":"14.10;16.01;16.03.03;70.10","FunCat.description":"assembly of protein complexes;protein binding;RNA binding;nucleus","PubMed.ID":12655004,"subunits.Protein.name.":"U3 small nucleolar ribonucleoprotein protein MPP10 ;U3 small nucleolar ribonucleoprotein protein IMP4 ;U3 small nucleolar ribonucleoprotein protein IMP3","subunits.Gene.name.":"MPHOSPH10;IMP4;IMP3","subunits.Gene.name.syn.":"MPP10;BXDC4;C15orf12 MRPS4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The formation of the hImp3-hMpp10-hImp4 complex correlates with the nucleolar localization of these proteins.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":534,"ComplexName":"M1 mAChR-TRPC6-PKC complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P05696;P08482;Q99N77","subunits.Entrez.IDs.":"24680;25229;89823","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0051098;GO:0005515;GO:0030234;GO:0050790;GO:0008324;GO:0006812;GO:0015267;GO:0007213","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;regulation of binding;protein binding;enzyme regulator activity;regulation of catalytic activity;cation transmembrane transporter activity;cation transport;channel activity;G-protein coupled acetylcholine receptor signaling pathway","FunCat.ID":"14.07.03;18.01.07;16.01;18.02.01;20.01.01.01;20.03.01;30.05.02.24.02","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;regulation by binding / dissociation;protein binding;enzymatic activity regulation / enzyme regulator;cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);channel / pore class transport;acetyl choline receptor signalling pathway","PubMed.ID":15994335,"subunits.Protein.name.":"Protein kinase C alpha type;Muscarinic acetylcholine receptor M1;Transient receptor potential Ca2+ channel 6B","subunits.Gene.name.":"Prkca;Chrm1;trp6B","subunits.Gene.name.syn.":"Pkca;Chrm-1;Trpc6","Disease.comment":"None","Subunits.comment":"The authors didn't describe the specific isoform of protein kinase C.","Complex.comment":"Complex constitutes only after stimulation of M1 mAChRs with carbachol. The results of the examinations of the time course of these associations suggest that M1 mAChRs and PKC associate with TRPC6 channels at the same time or slightly earlier than FKBP12, calcineurin, and calmodulin and that the later proteins remain in the TRPC6 complex after M1 mAChRs and PKC have disappeared. Maximal association of M1 mAChRs and PKC with TRPC6 channels occurs ~2 min after the addition of carbachol.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":535,"ComplexName":"TRAP complex","Organism":"Human","Synonyms":"thyroid hormone receptor-associated protein complex","Cell.line":"None","subunits.UniProt.IDs.":"O60244;O75448;O75586;P10827;P24863;Q13503;Q15648;Q6P2C8;Q93074;Q9BTT4;Q9NPJ6;Q9NVC6;Q9UHV7;Q9Y2W1;Q9Y2X0;Q9Y3C7","subunits.Entrez.IDs.":"9282;9862;10001;7067;892;9412;5469;9442;9968;84246;29079;9440;9969;9967;10025;51003","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:2001141;GO:0006355;GO:0051090;GO:0009755;GO:0023052;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;regulation of sequence-specific DNA binding transcription factor activity;hormone-mediated signaling pathway;signaling;nucleus","FunCat.ID":"11.02.03.04;18.02.09;30.01.09.08;30.01;70.10","FunCat.description":"transcriptional control;regulator of transcription factor;hormone mediated signal transduction;cellular signalling;nucleus","PubMed.ID":10198638,"subunits.Protein.name.":"Mediator of RNA polymerase II transcription subunit 14;Mediator of RNA polymerase II transcription subunit 24;Mediator of RNA polymerase II transcription subunit 6 ;Thyroid hormone receptor alpha;Cyclin-C;Mediator of RNA polymerase II transcription subunit 21;Mediator of RNA polymerase II transcription subunit 1;Mediator of RNA polymerase II transcription subunit 27 ;Mediator of RNA polymerase II transcription subunit 12;Mediator of RNA polymerase II transcription subunit 10 ;Mediator of RNA polymerase II transcription subunit 4 ;Mediator of RNA polymerase II transcription subunit 17;Mediator of RNA polymerase II transcription subunit 13 ;Thyroid hormone receptor-associated protein 3;Mediator of RNA polymerase II transcription subunit 16;Mediator of RNA polymerase II transcription subunit 31","subunits.Gene.name.":"MED14;MED24;MED6;THRA;CCNC;MED21;MED1;MED27;MED12;MED10;MED4;MED17;MED13;THRAP3;MED16;MED31","subunits.Gene.name.syn.":"ARC150 CRSP2 CXorf4 DRIP150 EXLM1 RGR1 TRAP170;ARC100 CRSP4 DRIP100 KIAA0130 THRAP4 TRAP100;ARC33;EAR7 ERBA1 NR1A1 THRA1 THRA2;None;SRB7 SURB7;ARC205 CRSP1 CRSP200 DRIP205 DRIP230 PBP PPARBP PPARGBP RB18A TRAP220 TRIP2;CRSP34 CRSP8;ARC240 CAGH45 HOPA KIAA0192 TNRC11 TRAP230;;ARC36 DRIP36 VDRIP;ARC77 CRSP6 DRIP77 DRIP80 TRAP80;ARC250 KIAA0593 THRAP1 TRAP240;TRAP150;DRIP92 THRAP5;SOH1","Disease.comment":"None","Subunits.comment":"Two, up to now uncharacterized members of the complex have been additionally isolated: TRAP97 and TRAP93.","Complex.comment":"The human thyroid hormone receptor-associated protein (TRAP) complex is a coactivator for nuclear receptors.  Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":536,"ComplexName":"TRPC1-TRPC3-TRPC7 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P48995;Q13507;Q9HCX4","subunits.Entrez.IDs.":"7220;7222;57113","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0015267;GO:0006875;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;channel activity;cellular metal ion homeostasis;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01;34.01.01.01;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);channel / pore class transport;homeostasis of metal ions (Na, K, Ca etc.);eukaryotic plasma membrane / membrane attached","PubMed.ID":15972814,"subunits.Protein.name.":"Short transient receptor potential channel 1 ;Short transient receptor potential channel 3 ;Short transient receptor potential channel 7","subunits.Gene.name.":"TRPC1;TRPC3;TRPC7","subunits.Gene.name.syn.":"TRP1;TRP3;TRP7","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results indicate that endogenous TRPC1, TRPC3, and TRPC7 participate in forming heteromeric store-operated channels, whereas TRPC3 and TRPC7 can also participate in forming heteromeric receptor-operated channels.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":537,"ComplexName":"Mediator complex","Organism":"Mouse","Synonyms":"Mediator of transcriptional regulation","Cell.line":"None","subunits.UniProt.IDs.":"A2ABV5;O35692;Q6PGF3;Q8VCD5;Q921D4;Q9CQ39;Q9CQA5;Q9CZB6;Q9R0X0","subunits.Entrez.IDs.":"26896;57261;216154;234959;69792;108098;67381;66213;56771","Protein.complex.purification.method":"MI:0091- chromatography technologies; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0009299;GO:2001141;GO:0006355;GO:0005515;GO:0051098;GO:0051090;GO:0035556;GO:0005634","GO.description":"mRNA transcription;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein binding;regulation of binding;regulation of sequence-specific DNA binding transcription factor activity;intracellular signal transduction;nucleus","FunCat.ID":"11.02.03;11.02.03.04;16.01;18.01.07;18.02.09;30.01;70.10","FunCat.description":"mRNA synthesis;transcriptional control;protein binding;regulation by binding / dissociation;regulator of transcription factor;cellular signalling;nucleus","PubMed.ID":9671713,"subunits.Protein.name.":"Mediator of RNA polymerase II transcription subunit 14 ;Fsh-like protein ;Mediator of RNA polymerase II transcription subunit 16;Mediator of RNA polymerase II transcription subunit 17 ;Mediator of RNA polymerase II transcription subunit 6;Mediator of RNA polymerase II transcription subunit 21 ;Mediator of RNA polymerase II transcription subunit 4 ;Mediator of RNA polymerase II transcription subunit 7 ;Mediator of RNA polymerase II transcription subunit 20","subunits.Gene.name.":"Med14;Brd4;Med16;Med17;Med6;Med21;Med4;Med7;Med20","subunits.Gene.name.syn.":"Crsp2 Gm641 Trap170;;Thrap5;Crsp6 Trap80;None;Srb7 Surb7;Vdrip;Crsp9;Trfp","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Regulation of transcription by RNA polymerase II (Pol II) is controlled by specific combinations of sequence-specific, DNA binding regulatory transcription factors (TFs) bound to a gene's promoter and enhancer regions. These TFs interact with several multiprotein complexes that remodel the chromatin context of the promoter, integrate signals from multiple TFs to control the frequency of transcription initiation, and regulate the efficiency of transcription elongation. One such complex is the Mediator, an ~2-megadalton complex of 20 to 30 subunits that is believed to function as a molecular bridge by simultaneously interacting with both DNA-bound TFs and Pol II. The mouse mediator complex binds to the RNA polymerase II C-terminal domain (CTD) and stimulates phosphorylation of the CTD by TFIIH. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":538,"ComplexName":"Cytochrome c oxidase, mitochondrial","Organism":"Mouse","Synonyms":"Cytochrome c oxidase (EC 1.9.3.1), mitochondrial; Complex IV; COX","Cell.line":"None","subunits.UniProt.IDs.":"P00405;P00416;P12787;P17665;P19536;P19783;P43024;P48771;P56391;P56393;Q64445;Q9CPQ1;Q9MD68","subunits.Entrez.IDs.":"17709;None;12858;12867;12859;12857;12861;12866;110323;66142;12868;12864;19224","Protein.complex.purification.method":"MI:0047-far western blotting","GO.ID":"GO:0006091;GO:0009060;GO:0005515;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;protein binding;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;16.01;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;protein binding;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":12865426,"subunits.Protein.name.":"Cytochrome c oxidase subunit 2;Cytochrome c oxidase subunit 3;Cytochrome c oxidase subunit 5A, mitochondrial;Cytochrome c oxidase subunit 7C, mitochondrial;Cytochrome c oxidase subunit 5B, mitochondrial;Cytochrome c oxidase subunit 4 isoform 1, mitochondrial;Cytochrome c oxidase subunit 6A1, mitochondrial;Cytochrome c oxidase subunit 7A2, mitochondrial;Cytochrome c oxidase subunit 6B1;Cytochrome c oxidase subunit 7B, mitochondrial;Cytochrome c oxidase subunit 8A, mitochondrial;Cytochrome c oxidase subunit 6C;Cytochrome c oxidase subunit 1","subunits.Gene.name.":"Mtco2;mt-Co3;Cox5a;Cox7c;Cox5b;Cox4i1;Cox6a1;Cox7a2;Cox6b1;Cox7b;Cox8a;Cox6c;mt-Co1","subunits.Gene.name.syn.":"COII mt-Co2;COIII Mtco3;None;Cox7c1;None;Cox4 Cox4a;Cox6al;Cox7a3 Cox7al;Cox6b;None;Cox8 Cox8l;None;Co1 COI COX1 COXI","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cytochrome oxidase (COX) is the fourth complex of the mitochondrial respiratory chain. It transfers electrons from ferrocytochrome c to molecular oxygen.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":540,"ComplexName":"HMG1-TBP-TATA complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P10103;P20226","subunits.Entrez.IDs.":"282691;6908","Protein.complex.purification.method":"MI:0413- electrophoretic mobility shift assay","GO.ID":"GO:0045892;GO:0003677","GO.description":"negative regulation of transcription, DNA-templated;DNA binding","FunCat.ID":"11.02.03.04.03;16.03.01","FunCat.description":"transcription repression;DNA binding","PubMed.ID":11390376,"subunits.Protein.name.":"High mobility group protein B1 ;TATA-box-binding protein","subunits.Gene.name.":"HMGB1;TBP","subunits.Gene.name.syn.":"HMG1;GTF2D1 TF2D TFIID","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"HMG-1 binding increases the affinity of TBP for the TATA box. The HMG1-TBP-TATA complex is proposed to inhibit the assembly of the preinitiation complex.","SWISSPROT.organism":"Bos taurus (Bovine);Homo sapiens (Human)"}
{"ComplexID":541,"ComplexName":"IGF1-IGFBP3-ALS complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P05019;P17936;P35858","subunits.Entrez.IDs.":"3479;3486;3483","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0050896","GO.description":"response to stimulus","FunCat.ID":"36.25","FunCat.description":"animal specific systemic sensing and response","PubMed.ID":9795367,"subunits.Protein.name.":"Insulin-like growth factor I ;Insulin-like growth factor-binding protein 3 ;Insulin-like growth factor-binding protein complex acid labile subunit","subunits.Gene.name.":"IGF1;IGFBP3;IGFALS","subunits.Gene.name.syn.":"IBP1;IBP3;ALS","Disease.comment":"IGF1 is implicated in the pathophysiology of pre-eclampsia.","Subunits.comment":"None","Complex.comment":"Circulating levels of IGF-I, IGFBP-3 and ALS, and their degree of association in the ternary complex in the fetus increased with gestational age.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":542,"ComplexName":"Cytochrome c oxidase, mitochondrial","Organism":"Bovine","Synonyms":"Cytochrome c oxidase (EC 1.9.3.1), mitochondrial; Complex IV, heart; COX","Cell.line":"None","subunits.UniProt.IDs.":"P00396;P00415;P00423;P00426;P00428;P00429;P00430;P04038;P07470;P07471;P10175;P13183;P68530","subunits.Entrez.IDs.":"None;None;281090;444878;287012;100270792;327718;782486;338086;282200;615757;327674;3283880","Protein.complex.purification.method":"MI:0047-far western blotting;MI:0019-coimmunoprecipitation","GO.ID":"GO:0006091;GO:0009060;GO:0005515;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;protein binding;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;16.01;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;protein binding;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":6303162,"subunits.Protein.name.":"Cytochrome c oxidase subunit 1;Cytochrome c oxidase subunit 3;Cytochrome c oxidase subunit 4 isoform 1, mitochondrial;Cytochrome c oxidase subunit 5A, mitochondrial;Cytochrome c oxidase subunit 5B, mitochondrial;Cytochrome c oxidase subunit 6B1;Cytochrome c oxidase subunit 7C, mitochondrial;Cytochrome c oxidase subunit 6C;Cytochrome c oxidase subunit 7A1, mitochondrial;Cytochrome c oxidase subunit 6A2, mitochondrial;Cytochrome c oxidase subunit 8B, mitochondrial;Cytochrome c oxidase subunit 7B, mitochondrial;Cytochrome c oxidase subunit 2","subunits.Gene.name.":"MT-CO1;MT-CO3;COX4I1;COX5A;COX5B;COX6B1;COX7C;COX6C;COX7A1;COX6A2;COX8B;COX7B;MT-CO2","subunits.Gene.name.syn.":"COI COXI MTCO1;COIII COXIII MTCO3;COX4;None;None;COX6B;COX7CP1;None;COX7A COX7AH;COX6A;COX8H;None;COII COXII MTCO2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cytochrome oxidase (COX) is the fourth complex ofthe mitochondrial respiratory chain. It transfers electrons fromferrocytochrome c to molecular oxygen.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":543,"ComplexName":"Cytochrome c oxidase, mitochondrial","Organism":"Bovine","Synonyms":"Cytochrome c oxidase (EC 1.9.3.1), mitochondrial; Complex IV, liver; COX","Cell.line":"None","subunits.UniProt.IDs.":"P00396;P00415;P00423;P00426;P00428;P00429;P00430;P04038;P13182;P13183;P13184;P14622;P68530","subunits.Entrez.IDs.":"None;None;281090;444878;287012;100270792;327718;782486;282199;327674;327688;281091;3283880","Protein.complex.purification.method":"MI:0047-far western blotting;MI:0019-coimmunoprecipitation","GO.ID":"GO:0006091;GO:0009060;GO:0005515;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;protein binding;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;16.01;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;protein binding;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":6303162,"subunits.Protein.name.":"Cytochrome c oxidase subunit 1;Cytochrome c oxidase subunit 3;Cytochrome c oxidase subunit 4 isoform 1, mitochondrial;Cytochrome c oxidase subunit 5A, mitochondrial;Cytochrome c oxidase subunit 5B, mitochondrial;Cytochrome c oxidase subunit 6B1;Cytochrome c oxidase subunit 7C, mitochondrial;Cytochrome c oxidase subunit 6C;Cytochrome c oxidase subunit 6A1, mitochondrial;Cytochrome c oxidase subunit 7B, mitochondrial;Cytochrome c oxidase subunit 7A2, mitochondrial;Cytochrome c oxidase subunit 8A, mitochondrial;Cytochrome c oxidase subunit 2","subunits.Gene.name.":"MT-CO1;MT-CO3;COX4I1;COX5A;COX5B;COX6B1;COX7C;COX6C;COX6A1;COX7B;COX7A2;COX8A;MT-CO2","subunits.Gene.name.syn.":"COI COXI MTCO1;COIII COXIII MTCO3;COX4;None;None;COX6B;COX7CP1;None;None;None;COX7AL;COX8 COX8L;COII COXII MTCO2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cytochrome oxidase (COX) is the fourth complex ofthe mitochondrial respiratory chain. It transfers electrons fromferrocytochrome c to molecular oxygen.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":544,"ComplexName":"TRPC3-TRPC6-Ca2+-signaling complex","Organism":"Dog","Synonyms":"None","Cell.line":"MDCK cells; SMIE cells","subunits.UniProt.IDs.":"O89040;P10687;P29994;Q08849;Q63269;Q99JE6;Q99N78;Q9JID2;Q9JMI9","subunits.Entrez.IDs.":"85240;24654;25262;81802;25679;29322;89823;81662;60395","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0015267;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;channel activity;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);channel / pore class transport;eukaryotic plasma membrane / membrane attached","PubMed.ID":15623527,"subunits.Protein.name.":"1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2;1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1;Inositol 1,4,5-trisphosphate receptor type 1;Syntaxin-3;Inositol 1,4,5-trisphosphate receptor type 3;1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3;Protein Trpc6;Guanine nucleotide-binding protein subunit alpha-11;Short transient receptor potential channel 3","subunits.Gene.name.":"Plcb2;Plcb1;Itpr1;Stx3;Itpr3;Plcb3;Trpc6;Gna11;Trpc3","subunits.Gene.name.syn.":"None;None;Insp3r;Stx3a;None;None;trp6A;None;Trrp3","Disease.comment":"None","Subunits.comment":"Since several proteins  from dog  were not available in the UniProt database at the time of annotation, the orthologous proteins from rat were used.","Complex.comment":"The results demonstrate that most of the same Ca2+-signaling proteins display polarized apical localization in MDCK cells. The data suggest that apically localized TRPC channels can be regulated by Ca2+-signaling mechanisms.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":546,"ComplexName":"Cytochrome c oxidase, mitochondrial","Organism":"Rat","Synonyms":"Cytochrome c oxidase (EC 1.9.3.1), mitochondrial; Complex IV; COX","Cell.line":"None","subunits.UniProt.IDs.":"P00406;P05503;P05505;P10818;P10888;P11240;P11950;P12075;P35171;P80430;P80431;P80432;P80433","subunits.Entrez.IDs.":"26198;26195;26204;25282;29445;252934;286962;94194;29507;None;303393;100188937;171335","Protein.complex.purification.method":"MI:0047-far western blotting;MI:0019-coimmunoprecipitation","GO.ID":"GO:0006091;GO:0009060;GO:0005515;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;protein binding;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;16.01;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;protein binding;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":6303162,"subunits.Protein.name.":"Cytochrome c oxidase subunit 2;Cytochrome c oxidase subunit 1;Cytochrome c oxidase subunit 3;Cytochrome c oxidase subunit 6A1, mitochondrial;Cytochrome c oxidase subunit 4 isoform 1, mitochondrial;Cytochrome c oxidase subunit 5A, mitochondrial;Cytochrome c oxidase subunit 6C-1;Cytochrome c oxidase subunit 5B, mitochondrial;Cytochrome c oxidase subunit 7A2, mitochondrial;Cytochrome c oxidase subunit 6B1;Cytochrome c oxidase subunit 7B, mitochondrial;Cytochrome c oxidase subunit 7C, mitochondrial;Cytochrome c oxidase subunit 8A, mitochondrial","subunits.Gene.name.":"Mtco2;Mtco1;Mtco3;Cox6a1;Cox4i1;Cox5a;Cox6c1;Cox5b;Cox7a2;Cox6b1;Cox7b;Cox7c;Cox8a","subunits.Gene.name.syn.":"Coii mt-Co2;Coi mt-Co1;Coiii mt-Co3;Cox6al;Cox4 Cox4a;None;None;None;Cox7a3 Cox7al;Cox6b;None;Cox7c1;Cox8 Cox8l","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cytochrome oxidase (COX) is the fourth complex ofthe mitochondrial respiratory chain. It transfers electrons fromferrocytochrome c to molecular oxygen.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":547,"ComplexName":"SMCC complex","Organism":"Human","Synonyms":"SRB/MED-containing cofactor complex","Cell.line":"None","subunits.UniProt.IDs.":"O60244;O75448;O75586;P24863;P49336;Q13503;Q15648;Q6P2C8;Q93074;Q9NPJ6;Q9NVC6;Q9UHV7;Q9Y2W1;Q9Y2X0","subunits.Entrez.IDs.":"9282;9862;10001;892;1024;9412;5469;9442;9968;29079;9440;9969;9967;10025","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:2001141;GO:0006355;GO:0005515;GO:0051098;GO:0051090;GO:0023052;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein binding;regulation of binding;regulation of sequence-specific DNA binding transcription factor activity;signaling;nucleus","FunCat.ID":"11.02.03.04;16.01;18.01.07;18.02.09;30.01;70.10","FunCat.description":"transcriptional control;protein binding;regulation by binding / dissociation;regulator of transcription factor;cellular signalling;nucleus","PubMed.ID":10198638,"subunits.Protein.name.":"Mediator of RNA polymerase II transcription subunit 14;Mediator of RNA polymerase II transcription subunit 24;Mediator of RNA polymerase II transcription subunit 6 ;Cyclin-C;Cyclin-dependent kinase 8;Mediator of RNA polymerase II transcription subunit 21;Mediator of RNA polymerase II transcription subunit 1;Mediator of RNA polymerase II transcription subunit 27 ;Mediator of RNA polymerase II transcription subunit 12;Mediator of RNA polymerase II transcription subunit 4 ;Mediator of RNA polymerase II transcription subunit 17;Mediator of RNA polymerase II transcription subunit 13 ;Thyroid hormone receptor-associated protein 3;Mediator of RNA polymerase II transcription subunit 16","subunits.Gene.name.":"MED14;MED24;MED6;CCNC;CDK8;MED21;MED1;MED27;MED12;MED4;MED17;MED13;THRAP3;MED16","subunits.Gene.name.syn.":"ARC150 CRSP2 CXorf4 DRIP150 EXLM1 RGR1 TRAP170;ARC100 CRSP4 DRIP100 KIAA0130 THRAP4 TRAP100;ARC33;None;None;SRB7 SURB7;ARC205 CRSP1 CRSP200 DRIP205 DRIP230 PBP PPARBP PPARGBP RB18A TRAP220 TRIP2;CRSP34 CRSP8;ARC240 CAGH45 HOPA KIAA0192 TNRC11 TRAP230;ARC36 DRIP36 VDRIP;ARC77 CRSP6 DRIP77 DRIP80 TRAP80;ARC250 KIAA0593 THRAP1 TRAP240;TRAP150;DRIP92 THRAP5","Disease.comment":"None","Subunits.comment":"In SMCC two, up to now uncharacterized members of the complex have been additionally isolated: TRAP97 and TRAP93.","Complex.comment":"Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":548,"ComplexName":"DRIP complex","Organism":"Human","Synonyms":"vitamine-D-receptor interacting protein complex","Cell.line":"None","subunits.UniProt.IDs.":"O43513;O60244;O75448;O75586;O95402;P11473;P28702;Q15648;Q93074;Q9NPJ6;Q9NVC6;Q9UHV7;Q9ULK4;Q9Y2X0","subunits.Entrez.IDs.":"9443;9282;9862;10001;9441;7421;6257;5469;9968;29079;9440;9969;9439;10025","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0047- far western blotting","GO.ID":"GO:0045893;GO:0006473;GO:0006476;GO:0051090;GO:0009755;GO:0023052;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;regulation of sequence-specific DNA binding transcription factor activity;hormone-mediated signaling pathway;signaling;nucleus","FunCat.ID":"11.02.03.04.01;14.07.04;18.02.09;30.01.09.08;30.01;70.10","FunCat.description":"transcription activation;modification by acetylation, deacetylation;regulator of transcription factor;hormone mediated signal transduction;cellular signalling;nucleus","PubMed.ID":9637681,"subunits.Protein.name.":"Mediator of RNA polymerase II transcription subunit 7 ;Mediator of RNA polymerase II transcription subunit 14;Mediator of RNA polymerase II transcription subunit 24;Mediator of RNA polymerase II transcription subunit 6 ;Mediator of RNA polymerase II transcription subunit 26 ;Vitamin D3 receptor ;Retinoic acid receptor RXR-beta ;Mediator of RNA polymerase II transcription subunit 1;Mediator of RNA polymerase II transcription subunit 12;Mediator of RNA polymerase II transcription subunit 4 ;Mediator of RNA polymerase II transcription subunit 17;Mediator of RNA polymerase II transcription subunit 13 ;Mediator of RNA polymerase II transcription subunit 23 ;Mediator of RNA polymerase II transcription subunit 16","subunits.Gene.name.":"MED7;MED14;MED24;MED6;MED26;VDR;RXRB;MED1;MED12;MED4;MED17;MED13;MED23;MED16","subunits.Gene.name.syn.":"ARC34 CRSP9;ARC150 CRSP2 CXorf4 DRIP150 EXLM1 RGR1 TRAP170;ARC100 CRSP4 DRIP100 KIAA0130 THRAP4 TRAP100;ARC33;ARC70 CRSP7;NR1I1;NR2B2;ARC205 CRSP1 CRSP200 DRIP205 DRIP230 PBP PPARBP PPARGBP RB18A TRAP220 TRIP2;ARC240 CAGH45 HOPA KIAA0192 TNRC11 TRAP230;ARC36 DRIP36 VDRIP;ARC77 CRSP6 DRIP77 DRIP80 TRAP80;ARC250 KIAA0593 THRAP1 TRAP240;ARC130 CRSP3 DRIP130 KIAA1216 SUR2;DRIP92 THRAP5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Nuclear receptors such as the steroid and thyroid hormone and vitamins A and D receptors, are known to regulate transcription by binding their cognate lipophilic ligands and subsequently undergoing a conformational change that alters their ability to interact with coregulatory proteins. These coregulatory proteins typically consist of complexes like DRIP that either repress (corepressors) or activate (coactivators) transcription. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":549,"ComplexName":"DRIP complex","Organism":"Human","Synonyms":"vitamine-D-receptor interacting protein complex","Cell.line":"None","subunits.UniProt.IDs.":"O43513;O60244;O75448;O75586;O95402;P11473;P28702;Q15648;Q93074;Q9NPJ6;Q9NVC6;Q9UHV7;Q9ULK4;Q9Y2X0","subunits.Entrez.IDs.":"9443;9282;9862;10001;9441;7421;6257;5469;9968;29079;9440;9969;9439;10025","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0045893;GO:0006473;GO:0006476;GO:0005515;GO:0051090;GO:0009755;GO:0023052;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;protein binding;regulation of sequence-specific DNA binding transcription factor activity;hormone-mediated signaling pathway;signaling;nucleus","FunCat.ID":"11.02.03.04.01;14.07.04;16.01;18.02.09;30.01.09.08;30.01;70.10","FunCat.description":"transcription activation;modification by acetylation, deacetylation;protein binding;regulator of transcription factor;hormone mediated signal transduction;cellular signalling;nucleus","PubMed.ID":10235266,"subunits.Protein.name.":"Mediator of RNA polymerase II transcription subunit 7 ;Mediator of RNA polymerase II transcription subunit 14;Mediator of RNA polymerase II transcription subunit 24;Mediator of RNA polymerase II transcription subunit 6 ;Mediator of RNA polymerase II transcription subunit 26 ;Vitamin D3 receptor ;Retinoic acid receptor RXR-beta ;Mediator of RNA polymerase II transcription subunit 1;Mediator of RNA polymerase II transcription subunit 12;Mediator of RNA polymerase II transcription subunit 4 ;Mediator of RNA polymerase II transcription subunit 17;Mediator of RNA polymerase II transcription subunit 13 ;Mediator of RNA polymerase II transcription subunit 23 ;Mediator of RNA polymerase II transcription subunit 16","subunits.Gene.name.":"MED7;MED14;MED24;MED6;MED26;VDR;RXRB;MED1;MED12;MED4;MED17;MED13;MED23;MED16","subunits.Gene.name.syn.":"ARC34 CRSP9;ARC150 CRSP2 CXorf4 DRIP150 EXLM1 RGR1 TRAP170;ARC100 CRSP4 DRIP100 KIAA0130 THRAP4 TRAP100;ARC33;ARC70 CRSP7;NR1I1;NR2B2;ARC205 CRSP1 CRSP200 DRIP205 DRIP230 PBP PPARBP PPARGBP RB18A TRAP220 TRIP2;ARC240 CAGH45 HOPA KIAA0192 TNRC11 TRAP230;ARC36 DRIP36 VDRIP;ARC77 CRSP6 DRIP77 DRIP80 TRAP80;ARC250 KIAA0593 THRAP1 TRAP240;ARC130 CRSP3 DRIP130 KIAA1216 SUR2;DRIP92 THRAP5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Nuclear receptors such as the steroid and thyroid hormone and vitamins A and D receptors, are known to regulate transcription by binding their cognate lipophilic ligands and subsequently undergoing a conformational change that alters their ability to interact with coregulatory proteins. These coregulatory proteins typically consist of complexes like DRIP that either repress (corepressors) or activate (coactivators) transcription. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":550,"ComplexName":"NOS3-CAV1-NOSTRIN complex","Organism":"Human","Synonyms":"None","Cell.line":"whole blood and lymph","subunits.UniProt.IDs.":"P29474;Q03135;Q8IVI9","subunits.Entrez.IDs.":"4846;857;115677","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0663-confocal microscopy","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0005886","GO.description":"intracellular protein transport;protein targeting;protein transport;plasma membrane","FunCat.ID":"14.04;20.01.10;70.02","FunCat.description":"protein targeting, sorting and translocation;protein transport;eukaryotic plasma membrane / membrane attached","PubMed.ID":16807357,"subunits.Protein.name.":"Nitric oxide synthase, endothelial;Caveolin-1;Nostrin","subunits.Gene.name.":"NOS3;CAV1;NOSTRIN","subunits.Gene.name.syn.":"None;CAV;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Translocation of endothelial nitric-oxide synthase involves a ternary complex with caveolin-1 and NOSTRIN.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":551,"ComplexName":"core-histone (H2A/H2B/H3/H4)-TDIF2-TDT complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04053;P62805;P68431;Q16777;Q16778;Q5QJE6","subunits.Entrez.IDs.":"1791;None;None;8338;8349;30836","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005634;GO:0006338;GO:0003677","GO.description":"nucleus;chromatin remodeling;DNA binding","FunCat.ID":"70.10;16.03.01","FunCat.description":"nucleus;DNA binding","PubMed.ID":12786946,"subunits.Protein.name.":"DNA nucleotidylexotransferase;Histone H4;Histone H3.1;Histone H2A type 2-C;Histone H2B type 2-E;Deoxynucleotidyltransferase terminal-interacting protein 2","subunits.Gene.name.":"DNTT;HIST1H4A;;HIST1H3A;;HIST2H2AC;HIST2H2BE;DNTTIP2","subunits.Gene.name.syn.":"TDT;H4/A H4FA; H4/I H4FI; H4/G H4FG; H4/B H4FB; H4/J H4FJ; H4/C H4FC; H4/H H4FH; H4/M H4FM; H4/E H4FE; H;H3FA; H3FL; H3FC; H3FB; H3FD; H3FI; H3FH; H3FK; H3FF; H3FJ;H2AFQ;H2BFQ;ERBP, TDIF2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors propose a dual function for TdIF2 in the N region synthesis. One is the function as an inhibitor of TdT. The other is that of a chromatin remodeling protein.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":552,"ComplexName":"IFNB1-IFNAR1-IFNAR2- complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P01574;P17181;P48551","subunits.Entrez.IDs.":"3456;3454;3455","Protein.complex.purification.method":"MI:0030- cross-linking studies","GO.ID":"GO:0050821;GO:0006457;GO:0005515","GO.description":"protein stabilization;protein folding;protein binding","FunCat.ID":"14.01;16.01","FunCat.description":"protein folding and stabilization;protein binding","PubMed.ID":10493588,"subunits.Protein.name.":"Interferon beta ;Interferon alpha/beta receptor 1 ;Interferon alpha/beta receptor 2","subunits.Gene.name.":"IFNB1;IFNAR1;IFNAR2","subunits.Gene.name.syn.":"IFB IFNB;IFNAR;IFNABR IFNARB","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":553,"ComplexName":"RHOA-IP3R-TRPC1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P48995;P61586;Q14643","subunits.Entrez.IDs.":"7220;387;3708","Protein.complex.purification.method":"MI:0096- pull down; MI:0019- coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0006875;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;cellular metal ion homeostasis;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;34.01.01.01;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;homeostasis of metal ions (Na, K, Ca etc.);eukaryotic plasma membrane / membrane attached","PubMed.ID":12766172,"subunits.Protein.name.":"Short transient receptor potential channel 1 ;Transforming protein RhoA ;Inositol 1,4,5-trisphosphate receptor type 1","subunits.Gene.name.":"TRPC1;RHOA;ITPR1","subunits.Gene.name.syn.":"TRP1;ARH12 ARHA RHO12;INSP3R1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cells were stimulated with thrombin. The authors showed that thrombin stimulation of endothelial cells induced translocation of Rho, and subsequent co-localization of Rho with TRPC1 and IP3R at the plasmalemma.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":554,"ComplexName":"PBAF complex (Polybromo- and BAF containing complex)","Organism":"Human","Synonyms":"SWI/SNF complex B","Cell.line":"None","subunits.UniProt.IDs.":"O96019;P51532;Q12824;Q68CP9;Q86U86;Q8TAQ2;Q92922;Q92925;Q969G3;Q96GM5","subunits.Entrez.IDs.":"86;6597;6598;196528;55193;6601;6599;6603;6605;6602","Protein.complex.purification.method":"MI:0226- ion exchange chromatography","GO.ID":"GO:0006265;GO:0045893;GO:0003677;GO:0009755;GO:0023052;GO:0051276;GO:0005694","GO.description":"DNA topological change;positive regulation of transcription, DNA-templated;DNA binding;hormone-mediated signaling pathway;signaling;chromosome organization;chromosome","FunCat.ID":"10.01.09.05;11.02.03.04.01;16.03.01;30.01.09.08;30.01;42.10.03;70.10.03","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription activation;DNA binding;hormone mediated signal transduction;cellular signalling;organization of chromosome structure;chromosome","PubMed.ID":11780067,"subunits.Protein.name.":"Actin-like protein 6A;Transcription activator BRG1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;AT-rich interactive domain-containing protein 2;Protein polybromo-1;SWI/SNF complex subunit SMARCC2;SWI/SNF complex subunit SMARCC1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","subunits.Gene.name.":"ACTL6A;SMARCA4;SMARCB1;ARID2;PBRM1;SMARCC2;SMARCC1;SMARCD2;SMARCE1;SMARCD1","subunits.Gene.name.syn.":"BAF53 BAF53A INO80K;BAF190A BRG1 SNF2B SNF2L4;BAF47, INI1, SNF5L1;KIAA1557;BAF180 PB1;BAF170;BAF155;BAF60B;BAF57;BAF60A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The chromatin-remodeling complex PBAF facilitates gene activation by assisting transcription machinery to gain access to targets on the chromosome. As additional members of the complex the authors mentioned actin and beta-tubulin.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":555,"ComplexName":"BAF complex","Organism":"Human","Synonyms":"SWI/SNF-A complex","Cell.line":"None","subunits.UniProt.IDs.":"O14497;O96019;P51532;Q12824;Q8TAQ2;Q92922;Q92925;Q969G3;Q96GM5","subunits.Entrez.IDs.":"8289;86;6597;6598;6601;6599;6603;6605;6602","Protein.complex.purification.method":"MI:0226- ion exchange chromatography","GO.ID":"GO:0006265;GO:0045893;GO:0003677;GO:0051276;GO:0005694","GO.description":"DNA topological change;positive regulation of transcription, DNA-templated;DNA binding;chromosome organization;chromosome","FunCat.ID":"10.01.09.05;11.02.03.04.01;16.03.01;42.10.03;70.10.03","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription activation;DNA binding;organization of chromosome structure;chromosome","PubMed.ID":11780067,"subunits.Protein.name.":"AT-rich interactive domain-containing protein 1A;Actin-like protein 6A;Transcription activator BRG1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;SWI/SNF complex subunit SMARCC2;SWI/SNF complex subunit SMARCC1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","subunits.Gene.name.":"ARID1A;ACTL6A;SMARCA4;SMARCB1;SMARCC2;SMARCC1;SMARCD2;SMARCE1;SMARCD1","subunits.Gene.name.syn.":"BAF250 BAF250A C1orf4 OSA1 SMARCF1;BAF53 BAF53A INO80K;BAF190A BRG1 SNF2B SNF2L4;BAF47, INI1, SNF5L1;BAF170;BAF155;BAF60B;BAF57;BAF60A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":556,"ComplexName":"PBAF complex (Polybromo- and BAF containing complex)","Organism":"Human","Synonyms":"SWI/SNF complex B","Cell.line":"None","subunits.UniProt.IDs.":"O96019;P51532;Q12824;Q68CP9;Q86U86;Q8TAQ2;Q92922;Q969G3;Q96GM5","subunits.Entrez.IDs.":"86;6597;6598;196528;55193;6601;6599;6605;6602","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045893;GO:0003677;GO:0009755;GO:0023052;GO:0051276;GO:0005694","GO.description":"DNA topological change;positive regulation of transcription, DNA-templated;DNA binding;hormone-mediated signaling pathway;signaling;chromosome organization;chromosome","FunCat.ID":"10.01.09.05;11.02.03.04.01;16.03.01;30.01.09.08;30.01;42.10.03;70.10.03","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription activation;DNA binding;hormone mediated signal transduction;cellular signalling;organization of chromosome structure;chromosome","PubMed.ID":15985610,"subunits.Protein.name.":"Actin-like protein 6A;Transcription activator BRG1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;AT-rich interactive domain-containing protein 2;Protein polybromo-1;SWI/SNF complex subunit SMARCC2;SWI/SNF complex subunit SMARCC1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","subunits.Gene.name.":"ACTL6A;SMARCA4;SMARCB1;ARID2;PBRM1;SMARCC2;SMARCC1;SMARCE1;SMARCD1","subunits.Gene.name.syn.":"BAF53 BAF53A INO80K;BAF190A BRG1 SNF2B SNF2L4;BAF47, INI1, SNF5L1;KIAA1557;BAF180 PB1;BAF170;BAF155;BAF57;BAF60A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The chromatin-remodeling complex PBAF facilitates gene activation by assisting transcription machinery to gain access to targets on the chromosome.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":557,"ComplexName":"TRP1-G alpha-11-IP3R3-CAV1 signaling complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P29992;P48995;Q03135;Q14573","subunits.Entrez.IDs.":"2767;7220;857;3710","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0006875;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;cellular metal ion homeostasis;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;34.01.01.01;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;homeostasis of metal ions (Na, K, Ca etc.);eukaryotic plasma membrane / membrane attached","PubMed.ID":10766822,"subunits.Protein.name.":"Guanine nucleotide-binding protein subunit alpha-11;Short transient receptor potential channel 1 ;Caveolin-1;Inositol 1,4,5-trisphosphate receptor type 3","subunits.Gene.name.":"GNA11;TRPC1;CAV1;ITPR3","subunits.Gene.name.syn.":"GA11;TRP1;CAV;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results demonstrate that caveolar microdomains provide a scaffold for  assembly of key Ca(2+) signaling proteins into a complex and  coordination of the molecular interactions leading to the activation of SOC (store-operated Ca(2+) influx).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":558,"ComplexName":"Channel complex TRPM6-TRPM7","Organism":"Human","Synonyms":"None","Cell.line":"epithelium","subunits.UniProt.IDs.":"Q96QT4;Q9BX84","subunits.Entrez.IDs.":"54822;140803","Protein.complex.purification.method":"MI:0055- fluorescent resonance energy transfer","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;eukaryotic plasma membrane / membrane attached","PubMed.ID":14976260,"subunits.Protein.name.":"Transient receptor potential cation channel subfamily M member 7 ;Transient receptor potential cation channel subfamily M member 6","subunits.Gene.name.":"TRPM7;TRPM6","subunits.Gene.name.syn.":"CHAK1 LTRPC7;CHAK2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":559,"ComplexName":"Decapping complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P26196;Q6P2E9;Q8IU60;Q96F86;Q9NPI6","subunits.Entrez.IDs.":"1656;23644;167227;80153;55802","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0043488;GO:0005737","GO.description":"regulation of mRNA stability;cytoplasm","FunCat.ID":"11.04.03.11;70.03","FunCat.description":"control of mRNA stability;cytoplasm","PubMed.ID":16364915,"subunits.Protein.name.":"Probable ATP-dependent RNA helicase DDX6;Enhancer of mRNA-decapping protein 4 ;m7GpppN-mRNA hydrolase ;Enhancer of mRNA-decapping protein 3 ;mRNA-decapping enzyme 1A","subunits.Gene.name.":"DDX6;EDC4;DCP2;EDC3;DCP1A","subunits.Gene.name.syn.":"HLR2 RCK;HEDLS;NUDT20;LSM16 YJDC YJEFN2;SMIF","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Decapping is a key step in mRNA turnover. The decapping complex was found to be localized in cytoplasmic processing bodies (PBs), which are thought to be the sites of mRNA decay.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":560,"ComplexName":"Kir6.2-Sur1 complex","Organism":"Mouse","Synonyms":"K(ATP) channel complex","Cell.line":"None","subunits.UniProt.IDs.":"Q09429;Q61743","subunits.Entrez.IDs.":"25559;16514","Protein.complex.purification.method":"MI:0040- electron microscopy; MI:0096- pull down","GO.ID":"GO:0000166;GO:0008324;GO:0006812;GO:0005216;GO:0042626;GO:0005886","GO.description":"nucleotide binding;cation transmembrane transporter activity;cation transport;ion channel activity;ATPase activity, coupled to transmembrane movement of substances;plasma membrane","FunCat.ID":"16.19;20.01.01.01;20.03.01.01;20.03.22;70.02","FunCat.description":"nucleotide/nucleoside/nucleobase binding;cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;transport ATPases;eukaryotic plasma membrane / membrane attached","PubMed.ID":16308567,"subunits.Protein.name.":"ATP-binding cassette sub-family C member 8 ;ATP-sensitive inward rectifier potassium channel 11","subunits.Gene.name.":"Abcc8;Kcnj11","subunits.Gene.name.syn.":"Sur Sur1;Kir6.2","Disease.comment":"None","Subunits.comment":"A fusion protein of rat SUR1 and mouse Kir6.2 was used for analysis.","Complex.comment":"The close juxtaposition of Kir6.2 and SUR1 subunits in both transmembrane and cytosolic domains provides for extensive intersubunit interactions and is consistent with earlier studies demonstrating physical interactions between SUR1 and Kir6.2 within both transmembrane and cytosolic domains.","SWISSPROT.organism":"Rattus norvegicus (Rat);Mus musculus (Mouse)"}
{"ComplexID":561,"ComplexName":"LSm1-7 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15116;P62310;P62312;Q9UK45;Q9Y333;Q9Y4Y9;Q9Y4Z0","subunits.Entrez.IDs.":"27257;27258;11157;51690;57819;23658;25804","Protein.complex.purification.method":"MI:0226- ion exchange chromatography","GO.ID":"GO:0043488;GO:0003723;GO:0005737","GO.description":"regulation of mRNA stability;RNA binding;cytoplasm","FunCat.ID":"11.04.03.11;16.03.03;70.03","FunCat.description":"control of mRNA stability;RNA binding;cytoplasm","PubMed.ID":15711010,"subunits.Protein.name.":"U6 snRNA-associated Sm-like protein LSm1 ;U6 snRNA-associated Sm-like protein LSm3;U6 snRNA-associated Sm-like protein LSm6;U6 snRNA-associated Sm-like protein LSm7;U6 snRNA-associated Sm-like protein LSm2 ;U6 snRNA-associated Sm-like protein LSm5;U6 snRNA-associated Sm-like protein LSm4","subunits.Gene.name.":"LSM1;LSM3;LSM6;LSM7;LSM2;LSM5;LSM4","subunits.Gene.name.syn.":"CASM;;;;C6orf28 G7B;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The cytoplasmic LSm1-7 complex is involved in mRNA decay. The complex has been shown to accumulate in processing bodies (PBs). The LSm2-8 complex which differs in only one subunit from the LSm1-7 complex is involved in RNA splicing. In contrast to the LSM1-7 complex, recombinant LSm2-8 binds to U6 snRNA in vitro.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":562,"ComplexName":"LSm2-8 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95777;P62310;P62312;Q9UK45;Q9Y333;Q9Y4Y9;Q9Y4Z0","subunits.Entrez.IDs.":"51691;27258;11157;51690;57819;23658;25804","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0226- ion exchange chromatography","GO.ID":"GO:0008380;GO:0003723;GO:0005737;GO:0005634","GO.description":"RNA splicing;RNA binding;cytoplasm;nucleus","FunCat.ID":"11.04.03.01;16.03.03;70.03;70.10","FunCat.description":"splicing;RNA binding;cytoplasm;nucleus","PubMed.ID":10523320,"subunits.Protein.name.":"U6 snRNA-associated Sm-like protein LSm8;U6 snRNA-associated Sm-like protein LSm3;U6 snRNA-associated Sm-like protein LSm6;U6 snRNA-associated Sm-like protein LSm7;U6 snRNA-associated Sm-like protein LSm2 ;U6 snRNA-associated Sm-like protein LSm5;U6 snRNA-associated Sm-like protein LSm4","subunits.Gene.name.":"LSM8;LSM3;LSM6;LSM7;LSM2;LSM5;LSM4","subunits.Gene.name.syn.":";;;;C6orf28 G7B;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The LSm2-8 complex which differs in only one subunit from the LSm1-7 complex is involved in RNA splicing. In contrast to the LSM1-7 complex, recombinant LSm2-8 binds to U6 snRNA in vitro.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":563,"ComplexName":"F1F0-ATP synthase, mitochondrial","Organism":"Human","Synonyms":"F1F0-ATP synthase (EC 3.6.3.14), mitochondrial; Complex V; F1F0 ATPase","Cell.line":"heart muscle","subunits.UniProt.IDs.":"O75947;O75964;P00846;P03928;P05496;P06576;P18859;P24539;P25705;P30049;P36542;P48047;P56134;P56381;P56385;Q9UII2","subunits.Entrez.IDs.":"10476;10632;4508;4509;516;506;522;515;498;513;509;539;9551;514;521;93974","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0069-mass spectrometry studies of complexes","GO.ID":"GO:0006794;GO:0006796;GO:0009060;GO:0006091;GO:0005524;GO:0006818;GO:0022904;GO:0005743","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;aerobic respiration;generation of precursor metabolites and energy;ATP binding;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01.04;02.13.03;01;16.19.03;20.01.15;02.11.07;70.16.05","FunCat.description":"phosphate metabolism;aerobic respiration;METABOLISM;ATP binding;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":12110673,"subunits.Protein.name.":"ATP synthase subunit d, mitochondrial;ATP synthase subunit g, mitochondrial;ATP synthase subunit a;ATP synthase protein 8;ATP synthase F;ATP synthase subunit beta, mitochondrial;ATP synthase-coupling factor 6, mitochondrial;ATP synthase F;ATP synthase subunit alpha, mitochondrial;ATP synthase subunit delta, mitochondrial;ATP synthase subunit gamma, mitochondrial;ATP synthase subunit O, mitochondrial;ATP synthase subunit f, mitochondrial;ATP synthase subunit epsilon, mitochondrial;ATP synthase subunit e, mitochondrial;ATPase inhibitor, mitochondrial","subunits.Gene.name.":"ATP5H;ATP5L;MT-ATP6;MT-ATP8;ATP5G1;ATP5B;ATP5J;ATP5F1;ATP5A1;ATP5D;ATP5C1;ATP5O;ATP5J2;ATP5E;ATP5I;ATPIF1","subunits.Gene.name.syn.":"None;None;ATP6 ATPASE6 MTATP6;ATP8 ATPASE8 MTATP8;None;ATPMB ATPSB;ATP5A ATPM;None;ATP5A ATP5AL2 ATPM;None;ATP5C ATP5CL1;ATPO;ATP5JL;None;ATP5K;ATPI","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"F1F0 ATPase is the fifth complex in the respiratory chain.The mammalian complex V consists of 16 different subunits withalpha(3), beta(3), gamma, delta and epsilon comprising the F1 part and a, b, c, d, e, f, g, A6L,OSCP, and coupling factor 6 providing the F0 and stator.Also associated in the complex under some conditions is anintrinsic inhibitor protein IF1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":564,"ComplexName":"BAF complex","Organism":"Human","Synonyms":"SWI/SNF complex A","Cell.line":"None","subunits.UniProt.IDs.":"O14497;O96019;P51531;Q12824;Q8TAQ2;Q92922;Q969G3;Q96GM5","subunits.Entrez.IDs.":"8289;86;6595;6598;6601;6599;6605;6602","Protein.complex.purification.method":"MI:0226-ion exchange chromatography;MI:0004-affinity chromatography technologies","GO.ID":"GO:0006265;GO:0045893;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;positive regulation of transcription, DNA-templated;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.01;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription activation;DNA binding;organization of chromosome structure;nucleus","PubMed.ID":8895581,"subunits.Protein.name.":"AT-rich interactive domain-containing protein 1A;Actin-like protein 6A;Probable global transcription activator SNF2L2;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;SWI/SNF complex subunit SMARCC2;SWI/SNF complex subunit SMARCC1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","subunits.Gene.name.":"ARID1A;ACTL6A;SMARCA2;SMARCB1;SMARCC2;SMARCC1;SMARCE1;SMARCD1","subunits.Gene.name.syn.":"BAF250 BAF250A C1orf4 OSA1 SMARCF1;BAF53 BAF53A INO80K;BAF190B, BRM, SNF2A, SNF2L2;BAF47, INI1, SNF5L1;BAF170;BAF155;BAF57;BAF60A","Disease.comment":"None","Subunits.comment":"Since the authors did not specify SMARCD and SMARCA, we used isoform SMARCD1 and SMARCA2. At the time of annotation, the additional member BAF110 of the protein complex was not found in the UniProt database.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":565,"ComplexName":"PBAF complex (Polybromo- and BAF containing complex)","Organism":"Human","Synonyms":"SWI/SNF complex B","Cell.line":"YT cells","subunits.UniProt.IDs.":"O96019;P51532;Q12824;Q68CP9;Q86U86;Q8TAQ2;Q92922;Q969G3;Q96GM5","subunits.Entrez.IDs.":"86;6597;6598;196528;55193;6601;6599;6605;6602","Protein.complex.purification.method":"MI:0226-ion exchange chromatography;MI:0004-affinity chromatography technologies","GO.ID":"GO:0006265;GO:0045893;GO:0003677;GO:0009755;GO:0051276;GO:0005694","GO.description":"DNA topological change;positive regulation of transcription, DNA-templated;DNA binding;hormone-mediated signaling pathway;chromosome organization;chromosome","FunCat.ID":"10.01.09.05;11.02.03.04.01;16.03.01;30.01.09.08;42.10.03;70.10.03","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription activation;DNA binding;hormone mediated signal transduction;organization of chromosome structure;chromosome","PubMed.ID":8895581,"subunits.Protein.name.":"Actin-like protein 6A;Transcription activator BRG1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;AT-rich interactive domain-containing protein 2;Protein polybromo-1;SWI/SNF complex subunit SMARCC2;SWI/SNF complex subunit SMARCC1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","subunits.Gene.name.":"ACTL6A;SMARCA4;SMARCB1;ARID2;PBRM1;SMARCC2;SMARCC1;SMARCE1;SMARCD1","subunits.Gene.name.syn.":"BAF53 BAF53A INO80K;BAF190A BRG1 SNF2B SNF2L4;BAF47, INI1, SNF5L1;KIAA1557;BAF180 PB1;BAF170;BAF155;BAF57;BAF60A","Disease.comment":"None","Subunits.comment":"Since the authors did not specify SMARCD, we used isoform SMARCD1. At the time of annotation, the additional member BAF110 of the protein complex was not found in the UniProt database.","Complex.comment":"The chromatin-remodeling complex PBAF facilitates gene activation by assisting transcription machinery to gain access to targets on the chromosome.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":566,"ComplexName":"BAF complex","Organism":"Human","Synonyms":"SWI/SNF complex A","Cell.line":"None","subunits.UniProt.IDs.":"O14497;O96019;P51532;P60709;Q12824;Q8TAQ2;Q92922;Q969G3;Q96GM5","subunits.Entrez.IDs.":"8289;86;6597;60;6598;6601;6599;6605;6602","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045893;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;positive regulation of transcription, DNA-templated;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.01;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription activation;DNA binding;organization of chromosome structure;nucleus","PubMed.ID":9845365,"subunits.Protein.name.":"AT-rich interactive domain-containing protein 1A;Actin-like protein 6A;Transcription activator BRG1;Actin, cytoplasmic 1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;SWI/SNF complex subunit SMARCC2;SWI/SNF complex subunit SMARCC1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","subunits.Gene.name.":"ARID1A;ACTL6A;SMARCA4;ACTB;SMARCB1;SMARCC2;SMARCC1;SMARCE1;SMARCD1","subunits.Gene.name.syn.":"BAF250 BAF250A C1orf4 OSA1 SMARCF1;BAF53 BAF53A INO80K;BAF190A BRG1 SNF2B SNF2L4;None;BAF47, INI1, SNF5L1;BAF170;BAF155;BAF57;BAF60A","Disease.comment":"None","Subunits.comment":"Since the authors did not specify SMARCD, we used isoform SMARCD1.","Complex.comment":"Beta-actin and BAF53 directly interact with BRG1 in the BAF complex. The actin subunit is required for optimal ATPase activity of BRG1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":567,"ComplexName":"Clathrin-CAP-1A-Na(v)1.8 channel complex","Organism":"Rat","Synonyms":"None","Cell.line":"dorsal root ganglia (DRG)","subunits.UniProt.IDs.":"P11442;Q62968;Q8CJ99","subunits.Entrez.IDs.":"54241;29571;266809","Protein.complex.purification.method":"MI:0096-pull down","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0006897","GO.description":"intracellular protein transport;protein targeting;protein transport;endocytosis","FunCat.ID":"14.04;20.01.10;20.09.18.09.01","FunCat.description":"protein targeting, sorting and translocation;protein transport;endocytosis","PubMed.ID":15797711,"subunits.Protein.name.":"Clathrin heavy chain 1;Sodium channel protein type 10 subunit alpha;Sodium channel and clathrin linker 1","subunits.Gene.name.":"Cltc;Scn10a;Sclt1","subunits.Gene.name.syn.":"None;Sns;Sap1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The interaction of CAP-1A with Nav1.8 C-terminus recruits clathrin to the protein complex.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":568,"ComplexName":"Nuclear pore complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O08587;O08658;O15504;P11654;P12270;P17955;P35658;P37199;P49791;P49792;P52591;P52948;P55735;P57740;P70581;P70582;Q12769;Q3SWS8;Q5RJY5;Q66HC5;Q68FY1;Q8NFH3;Q8NFH4;Q8WUM0;Q92621;Q96EE3;Q9BW27;Q9NRG9","subunits.Entrez.IDs.":"25497;113929;11097;58958;7175;65274;8021;117021;25281;5903;113975;4928;6396;57122;245922;53372;23279;362281;366016;291874;295692;348995;79023;55746;23165;81929;79902;8086","Protein.complex.purification.method":"MI:0069- mass spectrometry studies of complexes; MI:0028- cosedimentation in solution","GO.ID":"GO:0015031;GO:0008565;GO:0050658;GO:0051033;GO:0006810;GO:0051169;GO:0005635","GO.description":"protein transport;protein transporter activity;RNA transport;RNA transmembrane transporter activity;transport;nuclear transport;nuclear envelope","FunCat.ID":"20.01.10;20.01.21;20;20.09.01;70.10.05","FunCat.description":"protein transport;RNA transport;CELLULAR TRANSPORT, TRANSPORT FACILITIES AND TRANSPORT ROUTES;nuclear transport;nuclear membrane","PubMed.ID":12196509,"subunits.Protein.name.":"Nuclear pore complex protein Nup50 ;Nuclear pore complex protein Nup88 ;Nucleoporin-like protein 2 ;Nuclear pore membrane glycoprotein 210 ;Nucleoprotein TPR ;Nuclear pore glycoprotein p62 ;Nuclear pore complex protein Nup214 ;Nuclear pore complex protein Nup155 ;Nuclear pore complex protein Nup153 ;E3 SUMO-protein ligase RanBP2 ;Nuclear envelope pore membrane protein POM 121 ;Nuclear pore complex protein Nup98-Nup96 [Cleaved into: Nuclear pore complex protein Nup98;Protein SEC13 homolog;Nuclear pore complex protein Nup107;Nucleoporin p58/p45 ;Nuclear pore complex protein Nup54 ;Nuclear pore complex protein Nup160;mRNA export factor ;Nup188 protein ;Nuclear pore complex protein Nup93 ;Nucleoporin NUP53 ;Nucleoporin Nup43 ;Nucleoporin Nup37 ;Nuclear pore complex protein Nup133;Nuclear pore complex protein Nup205 ;Nucleoporin SEH1;Nuclear pore complex protein Nup85 ;Aladin","subunits.Gene.name.":"Nup50;Nup88;NUPL2;Nup210;TPR;Nup62;NUP214;Nup155;Nup153;RANBP2;Pom121;NUP98;SEC13;NUP107;Nup58;Nup54;NUP160;Rae1;Nup188;Nup93;Nup35;NUP43;NUP37;NUP133;NUP205;SEH1L;NUP85;AAAS","subunits.Gene.name.syn.":"Npap60;Nup84;CG1;Gp210 Pom210;;;CAIN CAN KIAA0023;;;NUP358;Nup121;ADAR2;D3S1231E SEC13L1 SEC13R;None;Nupl1;;KIAA0197 NUP120;Mrnp41;;;Nup53;;;None;C7orf14 KIAA0225;SEC13L SEH1;NUP75 PCNT1;ADRACALA","Disease.comment":"None","Subunits.comment":"Since several proteins from rat were not available in the UniProt database at the time of annotation, the orthologous human proteins were used. In rat, the nuclear pore complex contains two different isoforms of NUPL1. Human isoform p45 has not yet been isolated. Isoforms of NUP98 are autoproteolytically cleaved to yield Nup98 and Nup96 or Nup98 only, respectively.","Complex.comment":"All trafficking of macromolecules between the cytoplasm and the nucleus occurs through nuclear pore complexes (NPCs), which are supramolecular assemblies at points of fusion between the inner and outer nuclear membranes. NPCs are composed of an eightfold symmetric spoke-ring complex, cytoplasmic fibers, and a nuclear basket.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Homo sapiens (Human);Rattus norvegicus (Rat);Homo sapiens (Human);Rattus norvegicus (Rat);Homo sapiens (Human);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Homo sapiens (Human);Rattus norvegicus (Rat);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Homo sapiens (Human);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":569,"ComplexName":"PSD95-Nos1-Grin2b complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P29476;P31016;Q00960","subunits.Entrez.IDs.":"24598;29495;24410","Protein.complex.purification.method":"MI:0096- pull down;MI:0018- two hybrid","GO.ID":"GO:0050821;GO:0006457","GO.description":"protein stabilization;protein folding","FunCat.ID":"14.01","FunCat.description":"protein folding and stabilization","PubMed.ID":10488080,"subunits.Protein.name.":"Nitric oxide synthase, brain ;Disks large homolog 4;Glutamate receptor ionotropic, NMDA 2B","subunits.Gene.name.":"Nos1;Dlg4;Grin2b","subunits.Gene.name.syn.":"Bnos;Dlgh4, Psd95;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The mechanism for the assembly of this ternary complex depends on a PDZ-PDZ interaction between PSD-95 and nNOS that is mechanistically distinct from PDZ-peptide interactions in that the tertiary structure of both domains is important.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":570,"ComplexName":"p300-CBP-p270-SWI/SNF complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14497;P51532;Q09472;Q12824;Q8TAQ2;Q92793;Q92922","subunits.Entrez.IDs.":"8289;6597;2033;6598;6601;1387;6599","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045893;GO:0006473;GO:0006476;GO:0003677;GO:0051276;GO:0005694","GO.description":"DNA topological change;positive regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;DNA binding;chromosome organization;chromosome","FunCat.ID":"10.01.09.05;11.02.03.04.01;14.07.04;16.03.01;42.10.03;70.10.03","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription activation;modification by acetylation, deacetylation;DNA binding;organization of chromosome structure;chromosome","PubMed.ID":9584200,"subunits.Protein.name.":"AT-rich interactive domain-containing protein 1A;Transcription activator BRG1;Histone acetyltransferase p300;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;SWI/SNF complex subunit SMARCC2;CREB-binding protein;SWI/SNF complex subunit SMARCC1","subunits.Gene.name.":"ARID1A;SMARCA4;EP300;SMARCB1;SMARCC2;CREBBP;SMARCC1","subunits.Gene.name.syn.":"BAF250 BAF250A C1orf4 OSA1 SMARCF1;BAF190A BRG1 SNF2B SNF2L4;P300;BAF47, INI1, SNF5L1;BAF170;CBP;BAF155","Disease.comment":"None","Subunits.comment":"Several other, not further characterized members of the complex have been isolated: p75,p71,p64,p59 and p50.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":571,"ComplexName":"p300-CBP-p270 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14497;Q09472;Q92793","subunits.Entrez.IDs.":"8289;2033;1387","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0045893;GO:0003677;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04.01;16.03.01;70.10","FunCat.description":"transcription activation;DNA binding;nucleus","PubMed.ID":8995708,"subunits.Protein.name.":"AT-rich interactive domain-containing protein 1A;Histone acetyltransferase p300;CREB-binding protein","subunits.Gene.name.":"ARID1A;EP300;CREBBP","subunits.Gene.name.syn.":"BAF250 BAF250A C1orf4 OSA1 SMARCF1;P300;CBP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":572,"ComplexName":"PYR complex","Organism":"Mouse","Synonyms":"Ikaros containing chromatin remodeling complex","Cell.line":"None","subunits.UniProt.IDs.":"O54941;P60710;P63158;P70288;P97496;Q03267;Q60973;Q61466;Q6PDG5;Q6PDQ2;Q9Z0H3;Q9Z2N8","subunits.Entrez.IDs.":"57376;11461;15289;15182;20588;22778;245688;83797;68094;107932;20587;56456","Protein.complex.purification.method":"MI:0091-chromatography technologies;MI:0004-affinity chromatography technologies","GO.ID":"GO:0006265;GO:2001141;GO:0006355;GO:0006476;GO:0003677;GO:0010074;GO:0051276;GO:0030218;GO:0005634","GO.description":"DNA topological change;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein deacetylation;DNA binding;maintenance of meristem identity;chromosome organization;erythrocyte differentiation;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04;14.07.04;16.03.01;41.05.04;42.10.03;43.03.07;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcriptional control;modification by acetylation, deacetylation;DNA binding;embryogenesis;organization of chromosome structure;blood cell;nucleus","PubMed.ID":11003653,"subunits.Protein.name.":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;Actin, cytoplasmic 1;High mobility group protein B1;Histone deacetylase 2;SWI/SNF complex subunit SMARCC1;DNA-binding protein Ikaros;Histone-binding protein RBBP7;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1;SWI/SNF complex subunit SMARCC2;Chromodomain-helicase-DNA-binding protein 4;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;Actin-like protein 6A","subunits.Gene.name.":"Smarce1;Actb;Hmgb1;Hdac2;Smarcc1;Ikzf1;Rbbp7;Smarcd1;Smarcc2;Chd4;Smarcb1;Actl6a","subunits.Gene.name.syn.":"Baf57;None;Hmg-1 Hmg1;Yy1bp;Baf155 Srg3;Ikaros Lyf1 Zfpn1a1 Znfn1a1;Rbap46;Baf60a D15Kz1;Baf170;None;Baf47 Ini1 Snf5l1;Actl6 Baf53a","Disease.comment":"None","Subunits.comment":"Since the authors did not specify Actin as well as Actin-like protein 6, we used isoform Actb and isoform Actl6a, respectively.","Complex.comment":"Ikaros targets two types of chromatin-remodeling factors-activators (SWI/SNF) and repressors (NuRD)-in a single complex (PYR complex) to the beta-globin locus in adult erythroid cells.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":574,"ComplexName":"F1-ATP synthase -  IF1 (inhibitor protein)  complex, mitochondrial","Organism":"Bovine","Synonyms":"Complex V (F1-ATPase-IF1 subunit); F1-ATP synthase (EC 3.6.3.14) -  IF1 (inhibitor protein)  complex, mitochondrial","Cell.line":"heart muscle","subunits.UniProt.IDs.":"P00829;P01096;P05630;P05631;P05632;P19483","subunits.Entrez.IDs.":"327675;327699;338081;327668;617230;282578","Protein.complex.purification.method":"MI:0114-x-ray crystallography","GO.ID":"GO:0006794;GO:0006796;GO:0009060;GO:0006091;GO:0005515;GO:0005524;GO:0005743","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;aerobic respiration;generation of precursor metabolites and energy;protein binding;ATP binding;mitochondrial inner membrane","FunCat.ID":"01.04;02.13.03;01;16.01;16.19.03;70.16.05","FunCat.description":"phosphate metabolism;aerobic respiration;METABOLISM;protein binding;ATP binding;mitochondrial inner membrane","PubMed.ID":12923572,"subunits.Protein.name.":"ATP synthase subunit beta, mitochondrial;ATPase inhibitor, mitochondrial;ATP synthase subunit delta, mitochondrial;ATP synthase subunit gamma, mitochondrial;ATP synthase subunit epsilon, mitochondrial;ATP synthase subunit alpha, mitochondrial","subunits.Gene.name.":"ATP5B;ATPIF1;ATP5D;ATP5C1;ATP5E;ATP5A1","subunits.Gene.name.syn.":"None;ATPI;None;ATP5C;None;ATP5A2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"F1F0 ATPase is the fifth complex in the respiratory chain.The mammalian complex V consists of 16 different subunits withalpha(3), beta(3), gamma, delta and epsilon comprising the F1 part and a, b, c, d, e, f, g, A6L,OSCP, and coupling factor 6 providing the F0 and stator.Also associated in the complex under some conditions is anintrinsic inhibitor protein IF1.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":575,"ComplexName":"ABIN2-NFKB1-MAP3K8 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P19838;P41279;Q8NFZ5","subunits.Entrez.IDs.":"4790;1326;79155","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0050821;GO:0006457;GO:0005515;GO:0035556","GO.description":"protein stabilization;protein folding;protein binding;intracellular signal transduction","FunCat.ID":"14.01;16.01;30.01","FunCat.description":"protein folding and stabilization;protein binding;cellular signalling","PubMed.ID":15169888,"subunits.Protein.name.":"Nuclear factor NF-kappa-B p105 subunit;Mitogen-activated protein kinase kinase kinase 8 ;TNFAIP3-interacting protein 2","subunits.Gene.name.":"NFKB1;MAP3K8;TNIP2","subunits.Gene.name.syn.":"None;COT ESTF;ABIN2 FLIP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The optimal TPL-2 stability in vivo requires interaction with ABIN-2 as well as p105. Together, these data raise the possibility that ABIN-2 functions in the TLR4 signaling pathway which regulates TPL-2 activation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":576,"ComplexName":"F1F0-ATP synthase, mitochondrial","Organism":"Bovine","Synonyms":"Complex V; F1F0 ATPase; F1F0-ATP synthase (EC 3.6.3.14), mitochondrial","Cell.line":"heart muscle","subunits.UniProt.IDs.":"P00829;P00847;P01096;P02721;P03929;P05630;P05631;P05632;P13619;P13620;P13621;P19483;P32876;Q00361","subunits.Entrez.IDs.":"327675;3283882;327699;282690;3283881;338081;327668;617230;282701;282710;281640;282578;338053;338040","Protein.complex.purification.method":"MI:0114-x-ray crystallography;MI:0226-ion exchange chromatography","GO.ID":"GO:0006794;GO:0006796;GO:0009060;GO:0006091;GO:0005524;GO:0005743","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;aerobic respiration;generation of precursor metabolites and energy;ATP binding;mitochondrial inner membrane","FunCat.ID":"01.04;02.13.03;01;16.19.03;70.16.05","FunCat.description":"phosphate metabolism;aerobic respiration;METABOLISM;ATP binding;mitochondrial inner membrane","PubMed.ID":8240295,"subunits.Protein.name.":"ATP synthase subunit beta, mitochondrial;ATP synthase subunit a;ATPase inhibitor, mitochondrial;ATP synthase-coupling factor 6, mitochondrial;ATP synthase protein 8;ATP synthase subunit delta, mitochondrial;ATP synthase subunit gamma, mitochondrial;ATP synthase subunit epsilon, mitochondrial;ATP synthase F;ATP synthase subunit d, mitochondrial;ATP synthase subunit O, mitochondrial;ATP synthase subunit alpha, mitochondrial;ATP synthase F;ATP synthase subunit e, mitochondrial","subunits.Gene.name.":"ATP5B;MT-ATP6;ATPIF1;ATP5J;MT-ATP8;ATP5D;ATP5C1;ATP5E;ATP5F1;ATP5H;ATP5O;ATP5A1;ATP5G1;ATP5I","subunits.Gene.name.syn.":"None;ATP6 ATPASE6 MTATP6;ATPI;None;ATP8 ATPASE8 MTATP8;None;ATP5C;None;ATP5F;None;None;ATP5A2;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"F1F0 ATPase is the fifth complex in the respiratory chain.The mammalian complex V consists of 16 different subunits withalpha(3), beta(3), gamma, delta and epsilon comprising the F1 part and a, b, c, d, e, f, g, A6L,OSCP, and coupling factor 6 providing the F0 and stator.Also associated in the complex under some conditions is anintrinsic inhibitor protein IF1.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":577,"ComplexName":"FHL2-p53-HIPK2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04637;Q14192;Q9H2X6","subunits.Entrez.IDs.":"7157;2274;28996","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0005515;GO:0050789;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein binding;regulation of biological process;nucleus","FunCat.ID":"11.02.03.04;16.01;18;70.10","FunCat.description":"transcriptional control;protein binding;REGULATION OF METABOLISM AND PROTEIN FUNCTION;nucleus","PubMed.ID":16343438,"subunits.Protein.name.":"Cellular tumor antigen p53;Four and a half LIM domains protein 2 ;Homeodomain-interacting protein kinase 2","subunits.Gene.name.":"TP53;FHL2;HIPK2","subunits.Gene.name.syn.":"P53;DRAL SLIM3;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":578,"ComplexName":"PYR complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O54941;Q61466;Q6PDG5;Q9Z0H3","subunits.Entrez.IDs.":"57376;83797;68094;20587","Protein.complex.purification.method":"MI:0091- chromatography technologies; MI:0004- affinity chromatography technologies; MI:0412- electrophoretic mobility supershift assay","GO.ID":"GO:0006265;GO:2001141;GO:0006355;GO:0006473;GO:0006476;GO:0003677;GO:0010074;GO:0051276;GO:0030218;GO:0005634","GO.description":"DNA topological change;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;DNA binding;maintenance of meristem identity;chromosome organization;erythrocyte differentiation;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04;14.07.04;16.03.01;41.05.04;42.10.03;43.03.07;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcriptional control;modification by acetylation, deacetylation;DNA binding;embryogenesis;organization of chromosome structure;blood cell;nucleus","PubMed.ID":9892636,"subunits.Protein.name.":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1;SWI/SNF complex subunit SMARCC2;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","subunits.Gene.name.":"Smarce1;Smarcd1;Smarcc2;Smarcb1","subunits.Gene.name.syn.":"Baf57;Baf60a D15Kz1;Baf170;Baf47 Ini1 Snf5l1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex is restricted to definitive (adult-type) hematopoietic cells and specifically binds DNA sequences containing long stretches of pyrimidines.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":579,"ComplexName":"Epo-R-PLC-gamma-TRPC2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"blood cell","subunits.UniProt.IDs.":"P14753;Q62077;Q9R244","subunits.Entrez.IDs.":"13857;18803;22064","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0015267;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;channel activity;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);channel / pore class transport;eukaryotic plasma membrane / membrane attached","PubMed.ID":15329338,"subunits.Protein.name.":"Erythropoietin receptor;1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1;Short transient receptor potential channel 2","subunits.Gene.name.":"Epor;Plcg1;Trpc2","subunits.Gene.name.syn.":"None;Plcg-1;Trp2 Trrp2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"PLC is involved in Epo-modulated Ca 2+ influx through TRPC2.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":580,"ComplexName":"Epo-R-IP(3)R type II-TRPC2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P14753;Q9R244;Q9Z329","subunits.Entrez.IDs.":"13857;22064;16439","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0015267;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;channel activity;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);channel / pore class transport;eukaryotic plasma membrane / membrane attached","PubMed.ID":15329338,"subunits.Protein.name.":"Erythropoietin receptor;Short transient receptor potential channel 2;Inositol 1,4,5-trisphosphate receptor type 2","subunits.Gene.name.":"Epor;Trpc2;Itpr2","subunits.Gene.name.syn.":"None;Trp2 Trrp2;Itpr5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Mutant analysis data demonstrates a requirement for IP(3)R binding domains in Epo-modulated Ca 2+ influx through TRPC2.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":581,"ComplexName":"Epo-R-PLC-gamma 1-IP(3)R type II-TRPC2 signaling complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P14753;Q62077;Q9R244;Q9Z329","subunits.Entrez.IDs.":"13857;18803;22064;16439","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0015267;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;channel activity;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);channel / pore class transport;eukaryotic plasma membrane / membrane attached","PubMed.ID":15329338,"subunits.Protein.name.":"Erythropoietin receptor;1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1;Short transient receptor potential channel 2;Inositol 1,4,5-trisphosphate receptor type 2","subunits.Gene.name.":"Epor;Plcg1;Trpc2;Itpr2","subunits.Gene.name.syn.":"None;Plcg-1;Trp2 Trrp2;Itpr5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The experiments support the conclusion that after Epo stimulation, PLC-gamma activation produces IP3, which activates IP3R, and IP3R interaction with TRPC2 contributes to and is required for channel opening.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":582,"ComplexName":"Ikaros complex","Organism":"Mouse","Synonyms":"2 MD complex","Cell.line":"None","subunits.UniProt.IDs.":"O08900;O09106;P70288;P81183;P97496;Q03267;Q3TKT4;Q60972;Q61466;Q6P9Z1;Q6PDQ2;Q99JR8","subunits.Entrez.IDs.":"22780;433759;15182;22779;20588;22778;20586;19646;83797;66993;107932;83796","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0009117;GO:0006265;GO:0045892;GO:0032774;GO:0006473;GO:0006476;GO:0051276;GO:0030217;GO:0005634","GO.description":"nucleotide metabolic process;DNA topological change;negative regulation of transcription, DNA-templated;RNA biosynthetic process;protein acetylation;protein deacetylation;chromosome organization;T cell differentiation;nucleus","FunCat.ID":"01.03;10.01.09.05;11.02.03.04.03;11.02;14.07.04;42.10.03;43.03.07.02.01.02;70.10","FunCat.description":"nucleotide/nucleoside/nucleobase metabolism;DNA conformation modification (e.g. chromatin);transcription repression;RNA synthesis;modification by acetylation, deacetylation;organization of chromosome structure;T-cell;nucleus","PubMed.ID":10204490,"subunits.Protein.name.":"Zinc finger protein Aiolos ;Histone deacetylase 1;Histone deacetylase 2;Zinc finger protein Helios ;SWI/SNF complex subunit SMARCC1;DNA-binding protein Ikaros;Transcription activator BRG1 ;Histone-binding protein RBBP4 ;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3 ;Chromodomain-helicase-DNA-binding protein 4;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","subunits.Gene.name.":"Ikzf3;Hdac1;Hdac2;Ikzf2;Smarcc1;Ikzf1;Smarca4;Rbbp4;Smarcd1;Smarcd3;Chd4;Smarcd2","subunits.Gene.name.syn.":"Zfpn1a3 Znfn1a3;None;Yy1bp;Helios Zfpn1a2 Znfn1a2;Baf155 Srg3;Ikaros Lyf1 Zfpn1a1 Znfn1a1;Baf190a Brg1 Snf2b Snf2l4;Rbap48;Baf60a D15Kz1;Baf60c;None;Baf60b","Disease.comment":"None","Subunits.comment":"At the time of annotation, the additional member of the protein complex, Ikaros isoform 7, was not found in the UniProt database.","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":583,"ComplexName":"Ikaros-NuRD complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O08900;O09106;P70288;P81183;Q03267;Q6PDQ2","subunits.Entrez.IDs.":"22780;433759;15182;22779;22778;107932","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0032774;GO:0006473;GO:0006476;GO:0051276;GO:0030217;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;RNA biosynthetic process;protein acetylation;protein deacetylation;chromosome organization;T cell differentiation;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;11.02;14.07.04;42.10.03;43.03.07.02.01.02;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;RNA synthesis;modification by acetylation, deacetylation;organization of chromosome structure;T-cell;nucleus","PubMed.ID":10204490,"subunits.Protein.name.":"Zinc finger protein Aiolos ;Histone deacetylase 1;Histone deacetylase 2;Zinc finger protein Helios ;DNA-binding protein Ikaros;Chromodomain-helicase-DNA-binding protein 4","subunits.Gene.name.":"Ikzf3;Hdac1;Hdac2;Ikzf2;Ikzf1;Chd4","subunits.Gene.name.syn.":"Zfpn1a3 Znfn1a3;None;Yy1bp;Helios Zfpn1a2 Znfn1a2;Ikaros Lyf1 Zfpn1a1 Znfn1a1;None","Disease.comment":"None","Subunits.comment":"At the time of annotation, the additional member of the protein complex, Ikaros isoform 7, was not found in the UniProt database.","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":584,"ComplexName":"Ppp3cb-RyR2-mAkap complex","Organism":"Rat","Synonyms":"None","Cell.line":"heart muscle","subunits.UniProt.IDs.":"O08661;P20651;Q9WVC7","subunits.Entrez.IDs.":"689560;24675;64553","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0008324;GO:0006812;GO:0005216;GO:0019722;GO:0019933;GO:0007519","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;cation transmembrane transporter activity;cation transport;ion channel activity;calcium-mediated signaling;cAMP-mediated signaling;skeletal muscle tissue development","FunCat.ID":"11.02.03.04;20.01.01.01;20.03.01.01;30.01.09.03;30.01.09.07;41.05.15","FunCat.description":"transcriptional control;cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;Ca2+ mediated signal transduction;cAMP/cGMP mediated signal transduction;myogenesis","PubMed.ID":16306226,"subunits.Protein.name.":"Ryanodine receptor type II;Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform;A-kinase anchor protein 6","subunits.Gene.name.":"RATRYR2;Ppp3cb;Akap6","subunits.Gene.name.syn.":"None;None;mAkap","Disease.comment":"mAKAP complex is involved in adrenergic-induced cardiac hypertrophy.","Subunits.comment":"None","Complex.comment":"RyR and CaN activities are important for the induction of cellular hypertrophy by beta-adrenergic receptor signaling. The results show a novel function of the mAKAP complex involving the integration of cAMP and Ca2+ signals that promote myocyte hypertrophy.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":585,"ComplexName":"Mi2/NuRD-BCL6-MTA3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95983;P41182;Q13547;Q14839;Q9BTC8","subunits.Entrez.IDs.":"53615;604;3065;1108;57504","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0051276;GO:0030183;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;chromosome organization;B cell differentiation;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;42.10.03;43.03.07.02.01.01;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;organization of chromosome structure;B-cell;nucleus","PubMed.ID":15454082,"subunits.Protein.name.":"Methyl-CpG-binding domain protein 3;B-cell lymphoma 6 protein ;Histone deacetylase 1;Chromodomain-helicase-DNA-binding protein 4;Metastasis-associated protein MTA3","subunits.Gene.name.":"MBD3;BCL6;HDAC1;CHD4;MTA3","subunits.Gene.name.syn.":"None;BCL5 LAZ3 ZBTB27 ZNF51;RPD3L1;None;KIAA1266","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":586,"ComplexName":"Ccnb1-Itpr1-Cdc2 signaling complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P29994;P30277;P39951","subunits.Entrez.IDs.":"25262;25203;54237","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000278;GO:0051726;GO:0006468;GO:0006470;GO:0046777;GO:0019722;GO:0006875","GO.description":"mitotic cell cycle;regulation of cell cycle;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;calcium-mediated signaling;cellular metal ion homeostasis","FunCat.ID":"10.03.01.01;10.03.01;14.07.03;30.01.09.03;34.01.01.01","FunCat.description":"mitotic cell cycle;mitotic cell cycle and cell cycle control;modification by phosphorylation, dephosphorylation, autophosphorylation;Ca2+ mediated signal transduction;homeostasis of metal ions (Na, K, Ca etc.)","PubMed.ID":16237118,"subunits.Protein.name.":"Inositol 1,4,5-trisphosphate receptor type 1;G2/mitotic-specific cyclin-B1;Cyclin-dependent kinase 1","subunits.Gene.name.":"Itpr1;Ccnb1;Cdk1","subunits.Gene.name.syn.":"Insp3r;;Cdc2 Cdc2a Cdkn1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The interaction between IP3R1 and CyB/cdc2 can be seen only in PHA-stimulated cells.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":587,"ComplexName":"NuRD.1 complex","Organism":"Human","Synonyms":"nucleosome remodeling and histone deacetylation complex","Cell.line":"None","subunits.UniProt.IDs.":"O95983;Q09028;Q13330;Q14839;Q16576;Q6IT96;Q92769;Q9BTC8","subunits.Entrez.IDs.":"53615;5928;9112;1108;5931;3065;3066;57504","Protein.complex.purification.method":"MI:0091- chromatography technologies; MI:0004- affinity chromatography technologies","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0009755;GO:0023052;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;hormone-mediated signaling pathway;signaling;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;30.01.09.08;30.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;hormone mediated signal transduction;cellular signalling;organization of chromosome structure;nucleus","PubMed.ID":9885572,"subunits.Protein.name.":"Methyl-CpG-binding domain protein 3;Histone-binding protein RBBP4;Metastasis-associated protein MTA1;Chromodomain-helicase-DNA-binding protein 4;Histone-binding protein RBBP7;Histone deacetylase ;Histone deacetylase 2;Metastasis-associated protein MTA3","subunits.Gene.name.":"MBD3;RBBP4;MTA1;CHD4;RBBP7;HDAC1;HDAC2;MTA3","subunits.Gene.name.syn.":"None;RBAP48;None;None;RBAP46;;None;KIAA1266","Disease.comment":"None","Subunits.comment":"Several other subunits of the complex were found in the analysis, which have not been further characterized: N190, N170, N160, N140, N135, N130, N85, N75, N68, N66, N38.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":588,"ComplexName":"Respiratory chain supercomplex (complex I, III, IV), mitochondrial, heart","Organism":"Bovine","Synonyms":"Respirasome","Cell.line":"heart muscle","subunits.UniProt.IDs.":"O97725;P00125;P00126;P00129;P00130;P00157;P00396;P00415;P00423;P00426;P00428;P00429;P00430;P03887;P03892;P03898;P03902;P03910;P03920;P03924;P04038;P04394;P07552;P10175;P13182;P13183;P13184;P13271;P13272;P15690;P17694;P23004;P23709;P23934;P23935;P25708;P25712;P31800;P34942;P34943;P42026;P42028;P42029;P48305;P52505;P68530;Q01321;Q02365;Q02366;Q02367;Q02368;Q02369;Q02370;Q02371;Q02372;Q02373;Q02374;Q02375;Q02376;Q02377;Q02378;Q02379;Q02380;Q02827;Q05752;Q8HXG5;Q8HXG6;Q95KV7","subunits.Entrez.IDs.":"281742;512500;613899;616871;616109;3283889;None;None;281090;444878;287012;100270792;327718;None;None;3283884;3283885;3283886;None;3283888;782486;None;281570;615757;282199;327674;327688;286885;287020;288380;327697;282394;287327;327691;327714;287014;327717;282393;338060;404188;338079;287027;327710;None;327702;3283880;327704;338073;327670;327665;338065;327660;None;338064;282517;327701;327713;327680;282289;None;327690;338057;338061;338046;338063;404161;326346;338084","Protein.complex.purification.method":"MI:0276-blue native page","GO.ID":"GO:0006091;GO:0009060;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":10775262,"subunits.Protein.name.":"NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12;Cytochrome c1, heme protein, mitochondrial;Cytochrome b-c1 complex subunit 6, mitochondrial;Cytochrome b-c1 complex subunit 7;Cytochrome b-c1 complex subunit 9;Cytochrome b;Cytochrome c oxidase subunit 1;Cytochrome c oxidase subunit 3;Cytochrome c oxidase subunit 4 isoform 1, mitochondrial;Cytochrome c oxidase subunit 5A, mitochondrial;Cytochrome c oxidase subunit 5B, mitochondrial;Cytochrome c oxidase subunit 6B1;Cytochrome c oxidase subunit 7C, mitochondrial;NADH-ubiquinone oxidoreductase chain 1;NADH-ubiquinone oxidoreductase chain 2;NADH-ubiquinone oxidoreductase chain 3;NADH-ubiquinone oxidoreductase chain 4L;NADH-ubiquinone oxidoreductase chain 4;NADH-ubiquinone oxidoreductase chain 5;NADH-ubiquinone oxidoreductase chain 6;Cytochrome c oxidase subunit 6C;NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial;Cytochrome b-c1 complex subunit 10;Cytochrome c oxidase subunit 8B, mitochondrial;Cytochrome c oxidase subunit 6A1, mitochondrial;Cytochrome c oxidase subunit 7B, mitochondrial;Cytochrome c oxidase subunit 7A2, mitochondrial;Cytochrome b-c1 complex subunit 8;Cytochrome b-c1 complex subunit Rieske, mitochondrial;NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial;Cytochrome b-c1 complex subunit 2, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5;NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial;NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial;Cytochrome b-c1 complex subunit 1, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4;Acyl carrier protein, mitochondrial;Cytochrome c oxidase subunit 2;Cytochrome c oxidase subunit NDUFA4;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial;NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1;NADH dehydrogenase [ubiquinone] iron-sulfur protein 5;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial;NADH dehydrogenase [ubiquinone] 1 subunit C2;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13","subunits.Gene.name.":"NDUFA12;CYC1;UQCRH;UQCRB;UQCR10;MT-CYB;MT-CO1;MT-CO3;COX4I1;COX5A;COX5B;COX6B1;COX7C;MT-ND1;MT-ND2;MT-ND3;MT-ND4L;MT-ND4;MT-ND5;MT-ND6;COX6C;NDUFV2;UQCR11;COX8B;COX6A1;COX7B;COX7A2;UQCRQ;UQCRFS1;NDUFS1;NDUFS2;UQCRC2;NDUFS3;NDUFS6;NDUFA5;NDUFV1;NDUFV3;UQCRC1;NDUFA10;NDUFA9;NDUFS7;NDUFS8;NDUFA8;NDUFB4;NDUFAB1;MT-CO2;NDUFA4;NDUFB3;NDUFA6;NDUFB6;NDUFB7;NDUFB9;NDUFA2;NDUFA3;NDUFB8;NDUFB10;NDUFB2;NDUFS4;NDUFC1;NDUFA1;NDUFB1;NDUFS5;NDUFB5;NDUFC2;NDUFA7;NDUFB11;NDUFA11;NDUFA13","subunits.Gene.name.syn.":"None;None;None;None;None;COB CYTB MTCYB;COI COXI MTCO1;COIII COXIII MTCO3;COX4;None;None;COX6B;COX7CP1;MTND1 NADH1 ND1;MTND2 NADH2 ND2;MTND3 NADH3 ND3;MTND4L NADH4L ND4L;MTND4 NADH4 ND4;MTND5 NADH5 ND5;MTND6 NADH6 ND6;None;None;UQCR;COX8H;None;None;COX7AL;None;None;None;None;None;None;None;None;UQOR1;None;None;None;None;None;None;None;None;None;COII COXII MTCO2;None;None;None;None;None;UQOR22;None;None;None;None;None;None;None;None;None;None;None;None;CI-B14-5A;None;None;GRIM19","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone.The complete respiratory chain supercomplex consists of:1: complex I = NADH dehydrogenase, mitochondrial2: complex III = bc1-complex, mitochondrial3: complex IV = cytochrome c oxidase, mitochondrialThe stoichiometric association of complexes within the supercomplex varies:complex I was found as monomer,complex III was found as dimer,complex IV was absent or present as monomer, dimer, or trimer;PMID:16782043 predicts the following supercomplex model:complex I: monomercomplex II: dimercomplex IV: tetramerAdditionally the authors present a model for a higher supramolecular association of respirasomes into a respiratory string.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":589,"ComplexName":"Respiratory chain supercomplex (complex I, III, IV), mitochondrial, heart","Organism":"Bovine","Synonyms":"Respirasome","Cell.line":"heart muscle","subunits.UniProt.IDs.":"O97725;P00125;P00126;P00129;P00130;P00157;P00396;P00415;P00423;P00426;P00428;P00429;P00430;P03887;P03892;P03898;P03902;P03910;P03920;P03924;P04038;P04394;P07552;P10175;P13182;P13183;P13184;P13271;P13272;P15690;P17694;P23004;P23709;P23934;P23935;P25708;P25712;P31800;P34942;P34943;P42026;P42028;P42029;P48305;P52505;P68530;Q01321;Q02365;Q02366;Q02367;Q02368;Q02369;Q02370;Q02371;Q02372;Q02373;Q02374;Q02375;Q02376;Q02377;Q02378;Q02379;Q02380;Q02827;Q05752;Q8HXG5;Q8HXG6;Q95KV7","subunits.Entrez.IDs.":"281742;512500;613899;616871;616109;3283889;None;None;281090;444878;287012;100270792;327718;None;None;3283884;3283885;3283886;None;3283888;782486;None;281570;615757;282199;327674;327688;286885;287020;288380;327697;282394;287327;327691;327714;287014;327717;282393;338060;404188;338079;287027;327710;None;327702;3283880;327704;338073;327670;327665;338065;327660;None;338064;282517;327701;327713;327680;282289;None;327690;338057;338061;338046;338063;404161;326346;338084","Protein.complex.purification.method":"MI:0040-electron microscopy","GO.ID":"GO:0006091;GO:0009060;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":16551638,"subunits.Protein.name.":"NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12;Cytochrome c1, heme protein, mitochondrial;Cytochrome b-c1 complex subunit 6, mitochondrial;Cytochrome b-c1 complex subunit 7;Cytochrome b-c1 complex subunit 9;Cytochrome b;Cytochrome c oxidase subunit 1;Cytochrome c oxidase subunit 3;Cytochrome c oxidase subunit 4 isoform 1, mitochondrial;Cytochrome c oxidase subunit 5A, mitochondrial;Cytochrome c oxidase subunit 5B, mitochondrial;Cytochrome c oxidase subunit 6B1;Cytochrome c oxidase subunit 7C, mitochondrial;NADH-ubiquinone oxidoreductase chain 1;NADH-ubiquinone oxidoreductase chain 2;NADH-ubiquinone oxidoreductase chain 3;NADH-ubiquinone oxidoreductase chain 4L;NADH-ubiquinone oxidoreductase chain 4;NADH-ubiquinone oxidoreductase chain 5;NADH-ubiquinone oxidoreductase chain 6;Cytochrome c oxidase subunit 6C;NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial;Cytochrome b-c1 complex subunit 10;Cytochrome c oxidase subunit 8B, mitochondrial;Cytochrome c oxidase subunit 6A1, mitochondrial;Cytochrome c oxidase subunit 7B, mitochondrial;Cytochrome c oxidase subunit 7A2, mitochondrial;Cytochrome b-c1 complex subunit 8;Cytochrome b-c1 complex subunit Rieske, mitochondrial;NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial;Cytochrome b-c1 complex subunit 2, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5;NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial;NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial;Cytochrome b-c1 complex subunit 1, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4;Acyl carrier protein, mitochondrial;Cytochrome c oxidase subunit 2;Cytochrome c oxidase subunit NDUFA4;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial;NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1;NADH dehydrogenase [ubiquinone] iron-sulfur protein 5;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial;NADH dehydrogenase [ubiquinone] 1 subunit C2;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13","subunits.Gene.name.":"NDUFA12;CYC1;UQCRH;UQCRB;UQCR10;MT-CYB;MT-CO1;MT-CO3;COX4I1;COX5A;COX5B;COX6B1;COX7C;MT-ND1;MT-ND2;MT-ND3;MT-ND4L;MT-ND4;MT-ND5;MT-ND6;COX6C;NDUFV2;UQCR11;COX8B;COX6A1;COX7B;COX7A2;UQCRQ;UQCRFS1;NDUFS1;NDUFS2;UQCRC2;NDUFS3;NDUFS6;NDUFA5;NDUFV1;NDUFV3;UQCRC1;NDUFA10;NDUFA9;NDUFS7;NDUFS8;NDUFA8;NDUFB4;NDUFAB1;MT-CO2;NDUFA4;NDUFB3;NDUFA6;NDUFB6;NDUFB7;NDUFB9;NDUFA2;NDUFA3;NDUFB8;NDUFB10;NDUFB2;NDUFS4;NDUFC1;NDUFA1;NDUFB1;NDUFS5;NDUFB5;NDUFC2;NDUFA7;NDUFB11;NDUFA11;NDUFA13","subunits.Gene.name.syn.":"None;None;None;None;None;COB CYTB MTCYB;COI COXI MTCO1;COIII COXIII MTCO3;COX4;None;None;COX6B;COX7CP1;MTND1 NADH1 ND1;MTND2 NADH2 ND2;MTND3 NADH3 ND3;MTND4L NADH4L ND4L;MTND4 NADH4 ND4;MTND5 NADH5 ND5;MTND6 NADH6 ND6;None;None;UQCR;COX8H;None;None;COX7AL;None;None;None;None;None;None;None;None;UQOR1;None;None;None;None;None;None;None;None;None;COII COXII MTCO2;None;None;None;None;None;UQOR22;None;None;None;None;None;None;None;None;None;None;None;None;CI-B14-5A;None;None;GRIM19","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The complete respiratory chain supercomplex consists of:1: complex I = NADH dehydrogenase, mitochondrial2: complex III = bc1-complex, mitochondrial3: complex IV = cytochrome c oxidase, mitochondrialStoichiometric association of complexes within the supercomplex:complex I = monomer,complex III = dimer,complex IV = monomer;PMID:16782043 predicts the following supercomplex model:complex I: monomercomplex II: dimercomplex IV: tetramerAdditionally the authors present a model for a higher supramolecular association of respirasomes into a respiratory string.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":590,"ComplexName":"Kv4.2-KChIP3-Dpp10 channel complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"Q63881;Q6Q629;Q9JM47","subunits.Entrez.IDs.":"65180;363972;65199","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0050789;GO:0008324;GO:0006812;GO:0005216;GO:0001508;GO:0019227;GO:0019228;GO:0005886","GO.description":"intracellular protein transport;protein targeting;protein transport;regulation of biological process;cation transmembrane transporter activity;cation transport;ion channel activity;action potential;neuronal action potential propagation;neuronal action potential;plasma membrane","FunCat.ID":"14.04;20.01.10;18;20.01.01.01;20.03.01.01;34.03.03;70.02","FunCat.description":"protein targeting, sorting and translocation;protein transport;REGULATION OF METABOLISM AND PROTEIN FUNCTION;cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;regulation, generation and propagation of action potential;eukaryotic plasma membrane / membrane attached","PubMed.ID":16123112,"subunits.Protein.name.":"Potassium voltage-gated channel subfamily D member 2;Inactive dipeptidyl peptidase 10 ;Calsenilin","subunits.Gene.name.":"Kcnd2;Dpp10;Kcnip3","subunits.Gene.name.syn.":"None;;Csen Dream Kchip3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Analysis done in heterologously expressing Xenopus oocytes show, that when Kv4.2 is not coexpressed, DPP10 and KChIP3 do not associate with each other.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":591,"ComplexName":"SAP complex (Sin3-associated protein complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75446;Q09028;Q13547;Q16576;Q4LE39;Q92769;Q96ST3;Q9H0E3","subunits.Entrez.IDs.":"8819;5928;3065;5931;51742;3066;25942;79595","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0005515;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;protein binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;16.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;protein binding;organization of chromosome structure;nucleus","PubMed.ID":9885572,"subunits.Protein.name.":"Histone deacetylase complex subunit SAP30;Histone-binding protein RBBP4;Histone deacetylase 1;Histone-binding protein RBBP7;AT-rich interactive domain-containing protein 4B ;Histone deacetylase 2;Paired amphipathic helix protein Sin3a;Histone deacetylase complex subunit SAP130","subunits.Gene.name.":"SAP30;RBBP4;HDAC1;RBBP7;ARID4B;HDAC2;SIN3A;SAP130","subunits.Gene.name.syn.":"None;RBAP48;RPD3L1;RBAP46;BRCAA1 RBBP1L1 RBP1L1 SAP180;None;None;None","Disease.comment":"None","Subunits.comment":"In PMID:12724404, SAP45 has been identified as an additional member of the complex.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":592,"ComplexName":"SAP complex (Sin3-associated protein complex)","Organism":"Human","Synonyms":"mSin3A corepressor complex","Cell.line":"None","subunits.UniProt.IDs.":"O75446;Q09028;Q13547;Q16576;Q4LE39;Q92769;Q96ST3;Q9H0E3;Q9H7L9","subunits.Entrez.IDs.":"8819;5928;3065;5931;51742;3066;25942;79595;64426","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0091- chromatography technologies; MI:0004- affinity chromatography technologies","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0005515;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;protein binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;16.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;protein binding;organization of chromosome structure;nucleus","PubMed.ID":12724404,"subunits.Protein.name.":"Histone deacetylase complex subunit SAP30;Histone-binding protein RBBP4;Histone deacetylase 1;Histone-binding protein RBBP7;AT-rich interactive domain-containing protein 4B ;Histone deacetylase 2;Paired amphipathic helix protein Sin3a;Histone deacetylase complex subunit SAP130;Sin3 histone deacetylase corepressor complex component SDS3","subunits.Gene.name.":"SAP30;RBBP4;HDAC1;RBBP7;ARID4B;HDAC2;SIN3A;SAP130;SUDS3","subunits.Gene.name.syn.":"None;RBAP48;RPD3L1;RBAP46;BRCAA1 RBBP1L1 RBP1L1 SAP180;None;None;None;SAP45 SDS3","Disease.comment":"None","Subunits.comment":"SAP45 has been newly identified as a member of the SAP complex. Two other subunits of the complex were found in the analysis, which have not been further characterized: SAP38, SAP28.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":593,"ComplexName":"Kv4.2-Dpp10 channel complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"Q63881;Q6Q629","subunits.Entrez.IDs.":"65180;363972","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0050789;GO:0008324;GO:0006812;GO:0005216;GO:0001508;GO:0019227;GO:0019228;GO:0005886","GO.description":"intracellular protein transport;protein targeting;protein transport;regulation of biological process;cation transmembrane transporter activity;cation transport;ion channel activity;action potential;neuronal action potential propagation;neuronal action potential;plasma membrane","FunCat.ID":"14.04;20.01.10;18;20.01.01.01;20.03.01.01;34.03.03;70.02","FunCat.description":"protein targeting, sorting and translocation;protein transport;REGULATION OF METABOLISM AND PROTEIN FUNCTION;cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;regulation, generation and propagation of action potential;eukaryotic plasma membrane / membrane attached","PubMed.ID":15671030,"subunits.Protein.name.":"Potassium voltage-gated channel subfamily D member 2;Inactive dipeptidyl peptidase 10","subunits.Gene.name.":"Kcnd2;Dpp10","subunits.Gene.name.syn.":"None;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results distinguish DPPX and DPP10 as a functional DPP subfamily able to effectively traffic and modulate Kv4 channels, a unique property within the larger DPPIV-like class of proteins.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":594,"ComplexName":"Kv4.2-DPPX channel complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P46101;Q63881","subunits.Entrez.IDs.":"29272;65180","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0050789;GO:0008324;GO:0006812;GO:0005216;GO:0001508;GO:0019227;GO:0019228;GO:0005886","GO.description":"intracellular protein transport;protein targeting;protein transport;regulation of biological process;cation transmembrane transporter activity;cation transport;ion channel activity;action potential;neuronal action potential propagation;neuronal action potential;plasma membrane","FunCat.ID":"14.04;20.01.10;18;20.01.01.01;20.03.01.01;34.03.03;70.02","FunCat.description":"protein targeting, sorting and translocation;protein transport;REGULATION OF METABOLISM AND PROTEIN FUNCTION;cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;regulation, generation and propagation of action potential;eukaryotic plasma membrane / membrane attached","PubMed.ID":15671030,"subunits.Protein.name.":"Dipeptidyl aminopeptidase-like protein 6;Potassium voltage-gated channel subfamily D member 2","subunits.Gene.name.":"Dpp6;Kcnd2","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results distinguish DPPX and DPP10 as a functional DPP subfamily able to effectively traffic and modulate Kv4 channels, a unique property within the larger DPPIV-like class of proteins.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":595,"ComplexName":"Kv4.2-DPP10 channel complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q8N608;Q9NZV8","subunits.Entrez.IDs.":"57628;3751","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0050789;GO:0008324;GO:0006812;GO:0005216;GO:0001508;GO:0019227;GO:0019228;GO:0005886","GO.description":"intracellular protein transport;protein targeting;protein transport;regulation of biological process;cation transmembrane transporter activity;cation transport;ion channel activity;action potential;neuronal action potential propagation;neuronal action potential;plasma membrane","FunCat.ID":"14.04;20.01.10;18;20.01.01.01;20.03.01.01;34.03.03;70.02","FunCat.description":"protein targeting, sorting and translocation;protein transport;REGULATION OF METABOLISM AND PROTEIN FUNCTION;cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;regulation, generation and propagation of action potential;eukaryotic plasma membrane / membrane attached","PubMed.ID":15454437,"subunits.Protein.name.":"Inactive dipeptidyl peptidase 10 ;Potassium voltage-gated channel subfamily D member 2","subunits.Gene.name.":"DPP10;KCND2","subunits.Gene.name.syn.":"DPRP3 KIAA1492;KIAA1044","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This study shows that, similar to DPP6, DPP10 may play a critical part in the assembly of the Kv4 macromolecular complex in the brain and modulate its function.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":596,"ComplexName":"SIN3-HDAC-SAP30-ARID4 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75446;Q09028;Q13547;Q16576;Q4LE39;Q92769;Q96ST3","subunits.Entrez.IDs.":"8819;5928;3065;5931;51742;3066;25942","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0004- affinity chromatography technologies","GO.ID":"GO:0006265;GO:0007050;GO:0045892;GO:0006473;GO:0006476;GO:0051276;GO:0005634","GO.description":"DNA topological change;cell cycle arrest;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;10.03.01.02;11.02.03.04.03;14.07.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);cell cycle arrest;transcription repression;modification by acetylation, deacetylation;organization of chromosome structure;nucleus","PubMed.ID":11283269,"subunits.Protein.name.":"Histone deacetylase complex subunit SAP30;Histone-binding protein RBBP4;Histone deacetylase 1;Histone-binding protein RBBP7;AT-rich interactive domain-containing protein 4B ;Histone deacetylase 2;Paired amphipathic helix protein Sin3a","subunits.Gene.name.":"SAP30;RBBP4;HDAC1;RBBP7;ARID4B;HDAC2;SIN3A","subunits.Gene.name.syn.":"None;RBAP48;RPD3L1;RBAP46;BRCAA1 RBBP1L1 RBP1L1 SAP180;None;None","Disease.comment":"None","Subunits.comment":"Two other subunits of the complex were found in the analysis, which have not been further characterized: SAP38, SAP28.","Complex.comment":"RBP1 associates with mSIN3-HDAC complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":597,"ComplexName":"Cx43-Tom20-Hsp90ab complex","Organism":"Rat","Synonyms":"Gja1-Tomm20-Hsp90ab complex","Cell.line":"None","subunits.UniProt.IDs.":"P08050;P34058;Q62760","subunits.Entrez.IDs.":"24392;301252;266601","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006839;GO:0005743;GO:0031072;GO:0051879","GO.description":"mitochondrial transport;mitochondrial inner membrane;heat shock protein binding;Hsp90 protein binding","FunCat.ID":"20.09.04;70.16.05","FunCat.description":"mitochondrial transport;mitochondrial inner membrane","PubMed.ID":16741159,"subunits.Protein.name.":"Gap junction alpha-1 protein;Heat shock protein HSP 90-beta;Mitochondrial import receptor subunit TOM20 homolog","subunits.Gene.name.":"Gja1;Hsp90ab1;Tomm20","subunits.Gene.name.syn.":"Cxn-43, Cx43;Hsp84 Hspcb;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cx43 is transported to the inner mitochondrial membrane through translocation via the TOM complex.A normal mitochondrial Cx43 content is important for the diazoxide-related pathway of preconditioning.Its genetic depletion abolishes the protection of ischemia- and diazoxide-induced preconditioning.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":598,"ComplexName":"Kv4.3-Dpp10 channel complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q62897;Q6Q629","subunits.Entrez.IDs.":"65195;363972","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0050789;GO:0008324;GO:0006812;GO:0005216;GO:0001508;GO:0019227;GO:0019228;GO:0005886","GO.description":"intracellular protein transport;protein targeting;protein transport;regulation of biological process;cation transmembrane transporter activity;cation transport;ion channel activity;action potential;neuronal action potential propagation;neuronal action potential;plasma membrane","FunCat.ID":"14.04;20.01.10;18;20.01.01.01;20.03.01.01;34.03.03;70.02","FunCat.description":"protein targeting, sorting and translocation;protein transport;REGULATION OF METABOLISM AND PROTEIN FUNCTION;cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;regulation, generation and propagation of action potential;eukaryotic plasma membrane / membrane attached","PubMed.ID":15911355,"subunits.Protein.name.":"Potassium voltage-gated channel subfamily D member 3 ;Inactive dipeptidyl peptidase 10","subunits.Gene.name.":"Kcnd3;Dpp10","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"DPP10 preferentially binds to Kv4 channel proteins to increase current density and alter channel gating. DPPY(DPP10) also form homomers by themselves and heteromers with DPPX(DPP6) in the absence of Kv4 channels.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":599,"ComplexName":"Kv4.3-Dpp6 channel complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P46101;Q62897","subunits.Entrez.IDs.":"29272;65195","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0050789;GO:0008324;GO:0006812;GO:0005216;GO:0001508;GO:0019227;GO:0019228;GO:0005886","GO.description":"intracellular protein transport;protein targeting;protein transport;regulation of biological process;cation transmembrane transporter activity;cation transport;ion channel activity;action potential;neuronal action potential propagation;neuronal action potential;plasma membrane","FunCat.ID":"14.04;20.01.10;18;20.01.01.01;20.03.01.01;34.03.03;70.02","FunCat.description":"protein targeting, sorting and translocation;protein transport;REGULATION OF METABOLISM AND PROTEIN FUNCTION;cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;regulation, generation and propagation of action potential;eukaryotic plasma membrane / membrane attached","PubMed.ID":15911355,"subunits.Protein.name.":"Dipeptidyl aminopeptidase-like protein 6;Potassium voltage-gated channel subfamily D member 3","subunits.Gene.name.":"Dpp6;Kcnd3","subunits.Gene.name.syn.":"None;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"DPPX (Dpp6) and DPPY preferentially form complexes with channel proteins in Kv4 family.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":600,"ComplexName":"Kv4.1-Dpp6 channel complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P46101;Q03719","subunits.Entrez.IDs.":"29272;16506","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0050789;GO:0008324;GO:0006812;GO:0005216;GO:0001508;GO:0019227;GO:0019228;GO:0005886","GO.description":"intracellular protein transport;protein targeting;protein transport;regulation of biological process;cation transmembrane transporter activity;cation transport;ion channel activity;action potential;neuronal action potential propagation;neuronal action potential;plasma membrane","FunCat.ID":"14.04;20.01.10;18;20.01.01.01;20.03.01.01;34.03.03;70.02","FunCat.description":"protein targeting, sorting and translocation;protein transport;REGULATION OF METABOLISM AND PROTEIN FUNCTION;cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;regulation, generation and propagation of action potential;eukaryotic plasma membrane / membrane attached","PubMed.ID":15911355,"subunits.Protein.name.":"Dipeptidyl aminopeptidase-like protein 6;Potassium voltage-gated channel subfamily D member 1","subunits.Gene.name.":"Dpp6;Kcnd1","subunits.Gene.name.syn.":"None;","Disease.comment":"None","Subunits.comment":"Since Kcnd1 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"DPPX (Dpp6) and DPPY preferentially form complexes with channel proteins in Kv4 family.","SWISSPROT.organism":"Rattus norvegicus (Rat);Mus musculus (Mouse)"}
{"ComplexID":601,"ComplexName":"Kv4.1-Dpp10 channel complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q03719;Q6Q629","subunits.Entrez.IDs.":"16506;363972","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0050789;GO:0008324;GO:0006812;GO:0005216;GO:0001508;GO:0019227;GO:0019228;GO:0005886","GO.description":"intracellular protein transport;protein targeting;protein transport;regulation of biological process;cation transmembrane transporter activity;cation transport;ion channel activity;action potential;neuronal action potential propagation;neuronal action potential;plasma membrane","FunCat.ID":"14.04;20.01.10;18;20.01.01.01;20.03.01.01;34.03.03;70.02","FunCat.description":"protein targeting, sorting and translocation;protein transport;REGULATION OF METABOLISM AND PROTEIN FUNCTION;cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;regulation, generation and propagation of action potential;eukaryotic plasma membrane / membrane attached","PubMed.ID":15911355,"subunits.Protein.name.":"Potassium voltage-gated channel subfamily D member 1 ;Inactive dipeptidyl peptidase 10","subunits.Gene.name.":"Kcnd1;Dpp10","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"Since Kcnd1 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"DPPY(DPP10) also form homomers by themselves and heteromers with DPPX(DPP6) in the absence of Kv4 channels.","SWISSPROT.organism":"Mus musculus (Mouse);Rattus norvegicus (Rat)"}
{"ComplexID":602,"ComplexName":"Kv4.2-Dpp10 channel complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q63881;Q6Q629","subunits.Entrez.IDs.":"65180;363972","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0050789;GO:0008324;GO:0006812;GO:0005216;GO:0001508;GO:0019227;GO:0019228;GO:0005886","GO.description":"intracellular protein transport;protein targeting;protein transport;regulation of biological process;cation transmembrane transporter activity;cation transport;ion channel activity;action potential;neuronal action potential propagation;neuronal action potential;plasma membrane","FunCat.ID":"14.04;20.01.10;18;20.01.01.01;20.03.01.01;34.03.03;70.02","FunCat.description":"protein targeting, sorting and translocation;protein transport;REGULATION OF METABOLISM AND PROTEIN FUNCTION;cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;regulation, generation and propagation of action potential;eukaryotic plasma membrane / membrane attached","PubMed.ID":15911355,"subunits.Protein.name.":"Potassium voltage-gated channel subfamily D member 2;Inactive dipeptidyl peptidase 10","subunits.Gene.name.":"Kcnd2;Dpp10","subunits.Gene.name.syn.":"None;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"DPPY(DPP10) also form homomers by themselves and heteromers with DPPX(DPP6) in the absence of Kv4 channels.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":603,"ComplexName":"Kv4.2-Dpp6 channel complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P46101;Q63881","subunits.Entrez.IDs.":"29272;65180","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0050789;GO:0008324;GO:0006812;GO:0005216;GO:0001508;GO:0019227;GO:0019228;GO:0005886","GO.description":"intracellular protein transport;protein targeting;protein transport;regulation of biological process;cation transmembrane transporter activity;cation transport;ion channel activity;action potential;neuronal action potential propagation;neuronal action potential;plasma membrane","FunCat.ID":"14.04;20.01.10;18;20.01.01.01;20.03.01.01;34.03.03;70.02","FunCat.description":"protein targeting, sorting and translocation;protein transport;REGULATION OF METABOLISM AND PROTEIN FUNCTION;cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;regulation, generation and propagation of action potential;eukaryotic plasma membrane / membrane attached","PubMed.ID":15911355,"subunits.Protein.name.":"Dipeptidyl aminopeptidase-like protein 6;Potassium voltage-gated channel subfamily D member 2","subunits.Gene.name.":"Dpp6;Kcnd2","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"DPPX (Dpp6) and DPPY preferentially form complexes with channel proteins in Kv4 family.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":604,"ComplexName":"Kv4.2-DPPX-KChIP channel complex","Organism":"Rat","Synonyms":"None","Cell.line":"cerebellar membranes","subunits.UniProt.IDs.":"P46101;Q63881;Q8R426","subunits.Entrez.IDs.":"29272;65180;65023","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0008324;GO:0006812;GO:0005216;GO:0001508;GO:0019227;GO:0019228;GO:0005886","GO.description":"intracellular protein transport;protein targeting;protein transport;cation transmembrane transporter activity;cation transport;ion channel activity;action potential;neuronal action potential propagation;neuronal action potential;plasma membrane","FunCat.ID":"14.04;20.01.10;20.01.01.01;20.03.01.01;34.03.03;70.02","FunCat.description":"protein targeting, sorting and translocation;protein transport;cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;regulation, generation and propagation of action potential;eukaryotic plasma membrane / membrane attached","PubMed.ID":12575952,"subunits.Protein.name.":"Dipeptidyl aminopeptidase-like protein 6;Potassium voltage-gated channel subfamily D member 2;Kv channel-interacting protein 1","subunits.Gene.name.":"Dpp6;Kcnd2;Kcnip1","subunits.Gene.name.syn.":"None;None;Kchip1","Disease.comment":"None","Subunits.comment":"Since the authors did not specify Kv channel-interacting protein, we used subunit Kcnip1 (Kchip1)","Complex.comment":"DPPX facilitates the intracellular trafficking of Kv4 proteins and drastically increases the surface expression of Kv4 channels.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":605,"ComplexName":"TIM (TIM17A, TIM17B, TIM23, TIM44) complex, mitochondrial","Organism":"Human","Synonyms":"TIM (TIMM17A, TIMM17B, TIMM23, TIMM44) complex, mitochondrial","Cell.line":"None","subunits.UniProt.IDs.":"O14925;O43615;O60830;Q99595","subunits.Entrez.IDs.":"100287932;10469;10245;10440","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0071-molecular sieving","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0005743","GO.description":"intracellular protein transport;protein targeting;protein transport;mitochondrial inner membrane","FunCat.ID":"14.04;20.01.10;70.16.05","FunCat.description":"protein targeting, sorting and translocation;protein transport;mitochondrial inner membrane","PubMed.ID":10339406,"subunits.Protein.name.":"Mitochondrial import inner membrane translocase subunit Tim23;Mitochondrial import inner membrane translocase subunit TIM44;Mitochondrial import inner membrane translocase subunit Tim17-B;Mitochondrial import inner membrane translocase subunit Tim17-A","subunits.Gene.name.":"TIMM23;TIMM44;TIMM17B;TIMM17A","subunits.Gene.name.syn.":"TIM23;MIMT44 TIM44;TIM17B;MIMT17, TIM17, TIM17A TIMM17","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Translocation of nuclear-encoded mitochondrial preproteins is mediated by translocases in the outer (TOM) and inner (TIM)  membranes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":606,"ComplexName":"Kv4.2-Kchip1 channel complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain, hippocampal membranes","subunits.UniProt.IDs.":"Q63881;Q8R426","subunits.Entrez.IDs.":"65180;65023","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0001508;GO:0019227;GO:0019228;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;action potential;neuronal action potential propagation;neuronal action potential;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;34.03.03;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;regulation, generation and propagation of action potential;eukaryotic plasma membrane / membrane attached","PubMed.ID":15356203,"subunits.Protein.name.":"Potassium voltage-gated channel subfamily D member 2;Kv channel-interacting protein 1","subunits.Gene.name.":"Kcnd2;Kcnip1","subunits.Gene.name.syn.":"None;Kchip1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Immunohistochemical and immunofluorescence data show that there is preferential codistribution of Kv4.2 with KChIPs 2, 3, and 4 and preferential codistribution of Kv4.3 with KChIP1.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":607,"ComplexName":"Kv4.2-Kchip2 channel complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain, hippocampal membranes","subunits.UniProt.IDs.":"Q63881;Q9JM59","subunits.Entrez.IDs.":"65180;None","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0001508;GO:0019227;GO:0019228;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;action potential;neuronal action potential propagation;neuronal action potential;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;34.03.03;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;regulation, generation and propagation of action potential;eukaryotic plasma membrane / membrane attached","PubMed.ID":15356203,"subunits.Protein.name.":"Potassium voltage-gated channel subfamily D member 2;Kv channel-interacting protein 2","subunits.Gene.name.":"Kcnd2;Kcnip2","subunits.Gene.name.syn.":"None;Kchip2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Immunohistochemical and immunofluorescence data show that there is preferential codistribution of Kv4.2 with KChIPs 2, 3, and 4 and preferential codistribution of Kv4.3 with KChIP1.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":608,"ComplexName":"Kv4.2-Kchip3 channel complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain, hippocampal membranes","subunits.UniProt.IDs.":"Q63881;Q9JM47","subunits.Entrez.IDs.":"65180;65199","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0001508;GO:0019227;GO:0019228;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;action potential;neuronal action potential propagation;neuronal action potential;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;34.03.03;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;regulation, generation and propagation of action potential;eukaryotic plasma membrane / membrane attached","PubMed.ID":15356203,"subunits.Protein.name.":"Potassium voltage-gated channel subfamily D member 2;Calsenilin","subunits.Gene.name.":"Kcnd2;Kcnip3","subunits.Gene.name.syn.":"None;Csen Dream Kchip3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Immunohistochemical and immunofluorescence data show that there is preferential codistribution of Kv4.2 with KChIPs 2, 3, and 4 and preferential codistribution of Kv4.3 with KChIP1.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":609,"ComplexName":"Kv4.2-Kv4.3 channel complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain, hippocampal membranes","subunits.UniProt.IDs.":"Q62897;Q63881","subunits.Entrez.IDs.":"65195;65180","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0001508;GO:0019227;GO:0019228;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;action potential;neuronal action potential propagation;neuronal action potential;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;34.03.03;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;regulation, generation and propagation of action potential;eukaryotic plasma membrane / membrane attached","PubMed.ID":15356203,"subunits.Protein.name.":"Potassium voltage-gated channel subfamily D member 3 ;Potassium voltage-gated channel subfamily D member 2","subunits.Gene.name.":"Kcnd3;Kcnd2","subunits.Gene.name.syn.":";None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":610,"ComplexName":"MSL complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q7Z3B3;Q8N5Y2;Q9H7Z6;Q9HCI7","subunits.Entrez.IDs.":"284058;10943;84148;55167","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006265;GO:0006473;GO:0006476;GO:0005634","GO.description":"DNA topological change;protein acetylation;protein deacetylation;nucleus","FunCat.ID":"10.01.09.05;14.07.04;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);modification by acetylation, deacetylation;nucleus","PubMed.ID":16227571,"subunits.Protein.name.":"KAT8 regulatory NSL complex subunit 1 ;Male-specific lethal 3 homolog ;Histone acetyltransferase KAT8 ;E3 ubiquitin-protein ligase MSL2","subunits.Gene.name.":"KANSL1;MSL3;KAT8;MSL2","subunits.Gene.name.syn.":"CENP-36 KIAA1267 MSL1V1 NSL1;MSL3L1;MOF MYST1;KIAA1585 MSL2L1 RNF184","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors found that reduction in the levels of hMSLs and acetylation of H4 at lysine 16 are correlated with reduced transcription of some genes and with a G2/M cell cycle arrest.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":611,"ComplexName":"Exocyst complex","Organism":"Rat","Synonyms":"Sec6/8 complex","Cell.line":"None","subunits.UniProt.IDs.":"O54921;O54922;O54923;O54924;P97878;Q62824;Q62825;Q8R3S6","subunits.Entrez.IDs.":"171455;64632;50556;245709;60627;116654;252881;69940","Protein.complex.purification.method":"MI:0226- ion exchange chromatography; MI:0071- molecular sieving","GO.ID":"GO:0005515;GO:0015031;GO:0008565;GO:0006887;GO:0005886","GO.description":"protein binding;protein transport;protein transporter activity;exocytosis;plasma membrane","FunCat.ID":"16.01;20.01.10;20.09.16.09.03;70.02","FunCat.description":"protein binding;protein transport;exocytosis;eukaryotic plasma membrane / membrane attached","PubMed.ID":8982167,"subunits.Protein.name.":"Exocyst complex component 2 ;Exocyst complex component 7 ;Exocyst complex component 6 ;Exocyst complex component 8 ;Exocyst complex component 5 ;Exocyst complex component 4 ;Exocyst complex component 3 ;Exocyst complex component 1","subunits.Gene.name.":"Exoc2;Exoc7;Exoc6;Exoc8;Exoc5;Exoc4;Exoc3;Exoc1","subunits.Gene.name.syn.":"Sec5 Sec5l1;Exo70;Sec15 Sec15a Sec15l1;Exo84;Sec10l1;Sec8 Sec8l1;Sec6 Sec6l1;Sec3 Sec3l1","Disease.comment":"None","Subunits.comment":"Since Exoc1 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"The exocyst is a conserved eight-subunit complex involved in the docking of exocytic vesicles. It is thought to be involved in directing vesicles to their precise sites of fusion. The exocyst is regulated by many small GTPases, including members of the Rab, Rho and Ral families.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Mus musculus (Mouse)"}
{"ComplexID":612,"ComplexName":"CTF18-CTF8-DCC1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P0CG13;Q8WVB6;Q9BVC3","subunits.Entrez.IDs.":"54921;63922;79075","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007049;GO:0007059;GO:0005634","GO.description":"cell cycle;chromosome segregation;nucleus","FunCat.ID":"10.03;10.03.04.05;70.10","FunCat.description":"cell cycle;chromosome segregation/division;nucleus","PubMed.ID":12766176,"subunits.Protein.name.":"Chromosome transmission fidelity protein 8 homolog;Chromosome transmission fidelity protein 18 homolog;Sister chromatid cohesion protein DCC1","subunits.Gene.name.":"CHTF8;CHTF18;DSCC1","subunits.Gene.name.syn.":"CTF8;C16orf41 CTF18;DCC1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex is required for sister chromatid cohesion and loads proliferating cell nuclear antigen onto DNA (PMID:12930902).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":613,"ComplexName":"CTF18-CTF8-DCC1-RFC3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P0CG13;P40938;Q8WVB6;Q9BVC3","subunits.Entrez.IDs.":"54921;5983;63922;79075","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005515;GO:0005634","GO.description":"protein binding;nucleus","FunCat.ID":"16.01;70.10","FunCat.description":"protein binding;nucleus","PubMed.ID":12766176,"subunits.Protein.name.":"Chromosome transmission fidelity protein 8 homolog;Replication factor C subunit 3;Chromosome transmission fidelity protein 18 homolog;Sister chromatid cohesion protein DCC1","subunits.Gene.name.":"CHTF8;RFC3;CHTF18;DSCC1","subunits.Gene.name.syn.":"CTF8;None;C16orf41 CTF18;DCC1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":614,"ComplexName":"NRD complex (Nucleosome remodeling and deacetylation complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60341;Q09028;Q12873;Q13330;Q13547;Q14839;Q92769","subunits.Entrez.IDs.":"23028;5928;1107;9112;3065;1108;3066","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006265;GO:2001141;GO:0006355;GO:0006473;GO:0006476;GO:0051276;GO:0005634","GO.description":"DNA topological change;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04;14.07.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcriptional control;modification by acetylation, deacetylation;organization of chromosome structure;nucleus","PubMed.ID":9804427,"subunits.Protein.name.":"Lysine-specific histone demethylase 1A;Histone-binding protein RBBP4;Chromodomain-helicase-DNA-binding protein 3;Metastasis-associated protein MTA1;Histone deacetylase 1;Chromodomain-helicase-DNA-binding protein 4;Histone deacetylase 2","subunits.Gene.name.":"KDM1A;RBBP4;CHD3;MTA1;HDAC1;CHD4;HDAC2","subunits.Gene.name.syn.":"AOF2 KDM1 KIAA0601 LSD1;RBAP48;None;None;RPD3L1;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":615,"ComplexName":"Ubiquitin E3 ligase (SKP1A, SKP2, CUL1)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P63208;Q13309;Q13616","subunits.Entrez.IDs.":"6500;6502;8454","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000082;GO:0016567;GO:0016579;GO:0043161;GO:0006511;GO:0005634","GO.description":"G1/S transition of mitotic cell cycle;protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;nucleus","FunCat.ID":"10.03.01.01.03;14.07.05;14.13.01.01;70.10","FunCat.description":"G1/S transition of mitotic cell cycle;modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway);nucleus","PubMed.ID":9736735,"subunits.Protein.name.":"S-phase kinase-associated protein 1;S-phase kinase-associated protein 2;Cullin-1","subunits.Gene.name.":"SKP1;SKP2;CUL1","subunits.Gene.name.syn.":"EMC19, OCP2, SKP1A, TCEB1L;FBXL1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Human CUL-1 associates with the SKP1/SKP2 complex and regulates p21(CIP1/WAF1) and cyclin D proteins.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":616,"ComplexName":"TIM (Tim17A, Tim23, Tim44, Hsp70) complex, mitochondrial","Organism":"Rat","Synonyms":"TIM (Timm17a, Timm23, Timm44, mHsp70) complex,","Cell.line":"liver mitochondria","subunits.UniProt.IDs.":"O35092;O35093;O35094;P0DMW0","subunits.Entrez.IDs.":"54311;54312;29635;108348108","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0031072;GO:0005739;GO:0006886;GO:0005743;GO:0015031","GO.description":"heat shock protein binding;mitochondrion;intracellular protein transport;mitochondrial inner membrane;protein transport","FunCat.ID":"70.16;14.04;70.16.05;20.01.10","FunCat.description":"mitochondrion;protein targeting, sorting and translocation;mitochondrial inner membrane;protein transport","PubMed.ID":9538267,"subunits.Protein.name.":"Mitochondrial import inner membrane translocase subunit Tim17-A;Mitochondrial import inner membrane translocase subunit Tim23;Mitochondrial import inner membrane translocase subunit TIM44;Heat shock 70 kDa protein 1A","subunits.Gene.name.":"Timm17a;Timm23;Timm44;Hspa1a","subunits.Gene.name.syn.":"Mimt17, Tim17, Tim17a, Timm17;Tim23;Mimt44, Tim44;Hspa1, Hsp70-1","Disease.comment":"None","Subunits.comment":"Since the authors did not specify HSP70, we used isoform Hspa1a.","Complex.comment":"Mitochondria must import almost all of the proteinsnecessary for their function from the cytosol and thisimport is mediated by two distinct import machineries,namely the translocase of the outer membrane (Tom system) and the translocase of the inner membrane (Tim system). Tim17 and Tim23 share sequence similarity and form a subcomplex which is believed to constitute the translocationchannel of the inner mitochondrial membrane. Tim44, aperipheral protein bound to the matrix side of the innermembrane, recruits mHsp70 to the trans site of the importchannel and the Tim44-mHsp70 complex drives, in collaboration with GrpE, translocation of the precursor proteins in an ATP-dependent manner.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":617,"ComplexName":"CASK-LIN7C-APBA1 complex","Organism":"Human","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"O14936;Q02410;Q9NUP9","subunits.Entrez.IDs.":"8573;320;55327","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0006497","GO.description":"intracellular protein transport;protein targeting;protein transport;protein lipidation","FunCat.ID":"14.04;20.01.10;14.07.01","FunCat.description":"protein targeting, sorting and translocation;protein transport;modification with fatty acids (e.g. myristylation, palmitylation, farnesylation)","PubMed.ID":9822620,"subunits.Protein.name.":"Peripheral plasma membrane protein CASK ;Amyloid beta A4 precursor protein-binding family A member 1 ;Protein lin-7 homolog C","subunits.Gene.name.":"CASK;APBA1;LIN7C","subunits.Gene.name.syn.":"LIN2;MINT1 X11;MALS3 VELI3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex may play an important role in the trafficking and processing of APP in neurons.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":618,"ComplexName":"MRN complex (MRE11-RAD50-NBN complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60934;P49959;Q92878","subunits.Entrez.IDs.":"4683;4361;10111","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006308;GO:0006281;GO:0000075;GO:0003677;GO:0006974;GO:0005634","GO.description":"DNA catabolic process;DNA repair;cell cycle checkpoint;DNA binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"01.03.16.03;10.01.05.01;10.03.01.03;16.03.01;32.01.09;70.10","FunCat.description":"DNA degradation;DNA repair;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA binding;DNA damage response;nucleus","PubMed.ID":16163361,"subunits.Protein.name.":"Nibrin ;Double-strand break repair protein MRE11A ;DNA repair protein RAD50","subunits.Gene.name.":"NBN;MRE11A;RAD50","subunits.Gene.name.syn.":"NBS NBS1 P95;HNGS1 MRE11;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The MRN complex functions as an essential guardian of genome integrity by directing the proper processing of DNA ends, including DNA breaks.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":619,"ComplexName":"MRE11A-RAD50-NBN-TRF2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60934;P49959;Q15554;Q92878","subunits.Entrez.IDs.":"4683;4361;7014;10111","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0000075;GO:0003677;GO:0051276;GO:0005694","GO.description":"cell cycle checkpoint;DNA binding;chromosome organization;chromosome","FunCat.ID":"10.03.01.03;16.03.01;42.10.03;70.10.03","FunCat.description":"cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA binding;organization of chromosome structure;chromosome","PubMed.ID":10888888,"subunits.Protein.name.":"Nibrin ;Double-strand break repair protein MRE11A ;Telomeric repeat-binding factor 2 ;DNA repair protein RAD50","subunits.Gene.name.":"NBN;MRE11A;TERF2;RAD50","subunits.Gene.name.syn.":"NBS NBS1 P95;HNGS1 MRE11;TRBF2 TRF2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Several experiments indicate that TRF2 is not involved in DSB repair. RAD50-MRE11-NBS1 complex functions at telomeres, possibly by modulating t-loop formation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":620,"ComplexName":"CoREST-HDAC complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60341;O75362;Q13547;Q92769;Q96BD5;Q9P0W2;Q9UKL0","subunits.Entrez.IDs.":"23028;7764;3065;3066;51317;10362;23186","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;organization of chromosome structure;nucleus","PubMed.ID":11171972,"subunits.Protein.name.":"Lysine-specific histone demethylase 1A;Zinc finger protein 217;Histone deacetylase 1;Histone deacetylase 2;PHD finger protein 21A;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related;REST corepressor 1","subunits.Gene.name.":"KDM1A;ZNF217;HDAC1;HDAC2;PHF21A;HMG20B;RCOR1","subunits.Gene.name.syn.":"AOF2 KDM1 KIAA0601 LSD1;ZABC1;RPD3L1;None;BHC80 KIAA1696;BRAF35 HMGX2 HMGXB2 SMARCE1R;KIAA0071 RCOR","Disease.comment":"None","Subunits.comment":"RbAp46 and RbAp48 were not identified in this complex, although these proteins have been observed in all previously identified complexes and are thought to be part of an HDAC1/2 core.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":621,"ComplexName":"AKAP250-PKA-PDE4D complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"P17612;Q02952;Q08499","subunits.Entrez.IDs.":"5566;9590;5144","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0008104;GO:0030234;GO:0050790;GO:0019933;GO:0005886","GO.description":"intracellular protein transport;protein targeting;protein transport;protein localization;enzyme regulator activity;regulation of catalytic activity;cAMP-mediated signaling;plasma membrane","FunCat.ID":"14.04;20.01.10;18.01.03;18.02.01;30.01.09.07;70.02","FunCat.description":"protein targeting, sorting and translocation;protein transport;regulation by localization;enzymatic activity regulation / enzyme regulator;cAMP/cGMP mediated signal transduction;eukaryotic plasma membrane / membrane attached","PubMed.ID":16642035,"subunits.Protein.name.":"cAMP-dependent protein kinase catalytic subunit alpha;A-kinase anchor protein 12;cAMP-specific 3',5'-cyclic phosphodiesterase 4D","subunits.Gene.name.":"PRKACA;AKAP12;PDE4D","subunits.Gene.name.syn.":"PKACA;AKAP250;DPDE3","Disease.comment":"None","Subunits.comment":"Since the authors did not specify cAMP-dependent protein kinase catalytic subunit , we used isoform PRKACA.","Complex.comment":"This complex localized cAMP-degrading enzyme activity to plasma membrane sites to generate transient cAMP changes in response to adenylyl cyclase activity. The authors don't show PKA in coimmunoprecipitation experiment but describe that PKA is acting through an association with PDE4.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":622,"ComplexName":"Ubiquitin E3 ligase (VHL, TCEB1, TCEB2, CUL2)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P40337;Q13617;Q15369;Q15370","subunits.Entrez.IDs.":"7428;8453;6921;6923","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0051- fluorescence technologies","GO.ID":"GO:0016567;GO:0016579;GO:0030163;GO:0005737;GO:0005634","GO.description":"protein ubiquitination;protein deubiquitination;protein catabolic process;cytoplasm;nucleus","FunCat.ID":"14.07.05;14.13;70.03;70.10","FunCat.description":"modification by ubiquitination, deubiquitination;protein/peptide degradation;cytoplasm;nucleus","PubMed.ID":9122164,"subunits.Protein.name.":"Von Hippel-Lindau disease tumor suppressor;Cullin-2;Transcription elongation factor B polypeptide 1;Transcription elongation factor B polypeptide 2","subunits.Gene.name.":"VHL;CUL2;TCEB1;TCEB2","subunits.Gene.name.syn.":"None;None;elongin c;elongin b","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":623,"ComplexName":"TIM (TIM9, TIM10) complex, mitochondrial","Organism":"Human","Synonyms":"TIM (TIMM9, TIMM10) complex, mitochondrial","Cell.line":"None","subunits.UniProt.IDs.":"P62072;Q9Y5J7","subunits.Entrez.IDs.":"26519;26520","Protein.complex.purification.method":"MI:0040-electron microscopy","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0005743","GO.description":"intracellular protein transport;protein targeting;protein transport;mitochondrial inner membrane","FunCat.ID":"14.04;20.01.10;70.16.05","FunCat.description":"protein targeting, sorting and translocation;protein transport;mitochondrial inner membrane","PubMed.ID":16387659,"subunits.Protein.name.":"Mitochondrial import inner membrane translocase subunit Tim10;Mitochondrial import inner membrane translocase subunit Tim9","subunits.Gene.name.":"TIMM10;TIMM9","subunits.Gene.name.syn.":"TIM10;TIM9 TIM9A TIMM9A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Translocation of nuclear-encoded mitochondrial preproteins is mediated by translocases in the outer (TOM) and inner (TIM) membranes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":624,"ComplexName":"LSD1-CoREST complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60341;Q9UKL0","subunits.Entrez.IDs.":"23028;23186","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0006265;GO:0045892;GO:0018126;GO:0006479;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein hydroxylation;protein methylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.09;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;posttranslational modification of amino acids (e.g. hydroxylation, methylation);organization of chromosome structure;nucleus","PubMed.ID":16885027,"subunits.Protein.name.":"Lysine-specific histone demethylase 1A;REST corepressor 1","subunits.Gene.name.":"KDM1A;RCOR1","subunits.Gene.name.syn.":"AOF2 KDM1 KIAA0601 LSD1;KIAA0071 RCOR","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"CoREST endows LSD1 with the ability to demethylate nucleosomal substrates and protects LSD1 from proteasomal degradation in vivo.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":626,"ComplexName":"LSD1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60341;O75362;P0DMV8;P0DMV9;Q13363;Q13547;Q92766;Q96BD5;Q96EK2;Q9NP66;Q9P0W2;Q9P2K3;Q9UBW7;Q9UKL0","subunits.Entrez.IDs.":"23028;7764;3303;3304;1487;3065;6239;51317;112885;10363;10362;55758;7750;23186","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0018126;GO:0006479;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;protein hydroxylation;protein methylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;14.07.09;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;posttranslational modification of amino acids (e.g. hydroxylation, methylation);organization of chromosome structure;nucleus","PubMed.ID":16140033,"subunits.Protein.name.":"Lysine-specific histone demethylase 1A;Zinc finger protein 217;Heat shock 70 kDa protein 1A;Heat shock 70 kDa protein 1B;C-terminal-binding protein 1;Histone deacetylase 1;Ras-responsive element-binding protein 1;PHD finger protein 21A;PHD finger protein 21B;High mobility group protein 20A;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related;REST corepressor 3;Zinc finger MYM-type protein 2;REST corepressor 1","subunits.Gene.name.":"KDM1A;ZNF217;HSPA1A;HSPA1B;CTBP1;HDAC1;RREB1;PHF21A;PHF21B;HMG20A;HMG20B;RCOR3;ZMYM2;RCOR1","subunits.Gene.name.syn.":"AOF2 KDM1 KIAA0601 LSD1;ZABC1;HSPA1, HSX70, HSP70-1A;None;CTBP;RPD3L1;FINB;BHC80 KIAA1696;KIAA1661;HMGX1 HMGXB1;BRAF35 HMGX2 HMGXB2 SMARCE1R;KIAA1343;FIM RAMP ZNF198;KIAA0071 RCOR","Disease.comment":"None","Subunits.comment":"Another subunit of the complex was found in the analysis, which has not been further characterized: Y182.","Complex.comment":"CoREST positively regulates LSD1 function, while BHC80 inhibits CoREST/LSD1-mediated demethylation in vitro. These findings suggest that LSD1-mediated histone demethylation is regulated dynamically in vivo.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":627,"ComplexName":"MRN-TRRAP complex (MRE11A-RAD50-NBN-TRRAP complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60934;P49959;Q92878;Q9Y4A5","subunits.Entrez.IDs.":"4683;4361;10111;8295","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0006308;GO:0006281;GO:0000075;GO:0003677;GO:0006974;GO:0005634","GO.description":"DNA catabolic process;DNA repair;cell cycle checkpoint;DNA binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"01.03.16.03;10.01.05.01;10.03.01.03;16.03.01;32.01.09;70.10","FunCat.description":"DNA degradation;DNA repair;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA binding;DNA damage response;nucleus","PubMed.ID":16382133,"subunits.Protein.name.":"Nibrin ;Double-strand break repair protein MRE11A ;DNA repair protein RAD50 ;Transformation/transcription domain-associated protein","subunits.Gene.name.":"NBN;MRE11A;RAD50;TRRAP","subunits.Gene.name.syn.":"NBS NBS1 P95;HNGS1 MRE11;;PAF400","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TRRAP-depleted extracts show a reduced nonhomologous DNA end-joining activity in vitro. TRRAP may function as a molecular link between DSB signaling, repair, and chromatin remodeling.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":628,"ComplexName":"SNARE complex (Stx, Stx8, Vti1b, VAMP8)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O70257;P58200;Q9WUF4;Q9Z2Q7","subunits.Entrez.IDs.":"60466;366673;83730;59074","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515;GO:0015031;GO:0008565;GO:0006906;GO:0048489;GO:0016079;GO:0005886;GO:0005768","GO.description":"protein binding;protein transport;protein transporter activity;vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis;plasma membrane;endosome","FunCat.ID":"16.01;20.01.10;20.09.07.27;20.09.16.09.05;70.02;70.22","FunCat.description":"protein binding;protein transport;vesicle fusion;synaptic vesicle exocytosis;eukaryotic plasma membrane / membrane attached;endosome","PubMed.ID":11101518,"subunits.Protein.name.":"Syntaxin-7;Vesicle transport through interaction with t-SNAREs homolog 1B ;Vesicle-associated membrane protein 8 ;Syntaxin-8","subunits.Gene.name.":"Stx7;Vti1b;Vamp8;Stx8","subunits.Gene.name.syn.":";Vti1l1;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway. This SNARE complex functions in the homotypic fusion of late endosomes, which is one step in the delivery of endocytosed material to lysosomes.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":629,"ComplexName":"BLM-TRF2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P54132;P62380","subunits.Entrez.IDs.":"641;9519","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0055- fluorescent resonance energy transfer","GO.ID":"GO:0051276;GO:0007569;GO:0051276","GO.description":"chromosome organization;cell aging;chromosome organization","FunCat.ID":"42.10.03;40.20","FunCat.description":"organization of chromosome structure;cell aging","PubMed.ID":12444098,"subunits.Protein.name.":"Bloom syndrome protein ;TATA box-binding protein-like protein 1","subunits.Gene.name.":"BLM;TBPL1","subunits.Gene.name.syn.":"RECQ2 RECQL3;TLF TLP TLP21 TRF2 TRP","Disease.comment":"BLM is involved in Bloom syndrome (BS).","Subunits.comment":"The results identify BLM as the first protein found to affect telomeric DNA synthesis specifically in human ALT immortalized cell lines.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":630,"ComplexName":"RyR2 macromolecular complex","Organism":"Rat","Synonyms":"None","Cell.line":"heart muscle","subunits.UniProt.IDs.":"O08661;P12368;P27791;P62138;P63331;P97534","subunits.Entrez.IDs.":"689560;29699;25636;24668;24672;58950","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0008324;GO:0006812;GO:0005216;GO:0019933;GO:0050896","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;cation transmembrane transporter activity;cation transport;ion channel activity;cAMP-mediated signaling;response to stimulus","FunCat.ID":"14.07.03;20.01.01.01;20.03.01.01;30.01.09.07;36.25","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;cAMP/cGMP mediated signal transduction;animal specific systemic sensing and response","PubMed.ID":12401811,"subunits.Protein.name.":"Ryanodine receptor type II;cAMP-dependent protein kinase type II-alpha regulatory subunit;cAMP-dependent protein kinase catalytic subunit alpha;Serine/threonine-protein phosphatase PP1-alpha catalytic subunit;Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform;Peptidyl-prolyl cis-trans isomerase FKBP1B","subunits.Gene.name.":"RATRYR2;Prkar2a;Prkaca;Ppp1ca;Ppp2ca;Fkbp1b","subunits.Gene.name.syn.":"None;None;None;Ppp1a;None;None","Disease.comment":"The hyperphosphorylation of RyR2 by protein kinase A is general feature of heart failure.","Subunits.comment":"None","Complex.comment":"This complex contains kinase and two phosphatases that are bound to the channel via targeting proteins.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":631,"ComplexName":"Tacc1-chTOG-AuroraA  complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14965;O75410;Q14008","subunits.Entrez.IDs.":"6790;6867;9793","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0096- pull down;MI:0018- two hybrid","GO.ID":"GO:0051225;GO:0007098;GO:0006417;GO:0000775","GO.description":"spindle assembly;centrosome cycle;regulation of translation;chromosome, centromeric region","FunCat.ID":"10.03.05.01;12.07;70.10.04","FunCat.description":"spindle pole body/centrosome and microtubule cycle;translational control;centromere / kinetochore","PubMed.ID":14603251,"subunits.Protein.name.":"Aurora kinase A;Transforming acidic coiled-coil-containing protein 1 ;Cytoskeleton-associated protein 5","subunits.Gene.name.":"AURKA;TACC1;CKAP5","subunits.Gene.name.syn.":"AIK, AIRK1, ARK1, AURA, AYK1, BTAK, IAK1, STK15, STK6;KIAA1103;KIAA0097","Disease.comment":"This complex may be affected during mammary gland oncogenesis.","Subunits.comment":"None","Complex.comment":"This complex could be involved in the regulation of mRNA translation, cell division in conjunction and microtubule organization.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":632,"ComplexName":"Anti-HDAC2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60341;O94776;P78347;Q09028;Q12873;Q13330;Q13547;Q14202;Q14687;Q14839;Q16576;Q92769;Q96BD5;Q96ST3;Q9P0W2;Q9UBW7;Q9UKL0","subunits.Entrez.IDs.":"23028;9219;2969;5928;1107;9112;3065;9203;23199;1108;5931;3066;51317;25942;10362;7750;23186","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation;MI:0091-chromatography technologies","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;organization of chromosome structure;nucleus","PubMed.ID":12493763,"subunits.Protein.name.":"Lysine-specific histone demethylase 1A;Metastasis-associated protein MTA2;General transcription factor II-I;Histone-binding protein RBBP4;Chromodomain-helicase-DNA-binding protein 3;Metastasis-associated protein MTA1;Histone deacetylase 1;Zinc finger MYM-type protein 3;Genetic suppressor element 1;Chromodomain-helicase-DNA-binding protein 4;Histone-binding protein RBBP7;Histone deacetylase 2;PHD finger protein 21A;Paired amphipathic helix protein Sin3a;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related;Zinc finger MYM-type protein 2;REST corepressor 1","subunits.Gene.name.":"KDM1A;MTA2;GTF2I;RBBP4;CHD3;MTA1;HDAC1;ZMYM3;GSE1;CHD4;RBBP7;HDAC2;PHF21A;SIN3A;HMG20B;ZMYM2;RCOR1","subunits.Gene.name.syn.":"AOF2 KDM1 KIAA0601 LSD1;MTA1L1 PID;BAP135 WBSCR6;RBAP48;None;None;RPD3L1;DXS6673E KIAA0385 ZNF261;KIAA0182;None;RBAP46;None;BHC80 KIAA1696;None;BRAF35 HMGX2 HMGXB2 SMARCE1R;FIM RAMP ZNF198;KIAA0071 RCOR","Disease.comment":"XFIM (ZMYM3) is involved in X-linked mental retardation.","Subunits.comment":"Since the authors did not specify SIN3, we used isoform SIN3A.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":633,"ComplexName":"anti-BHC110 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60341;O75362;P78347;Q13547;Q14202;Q14687;Q92769;Q96BD5;Q9P0W2;Q9UBW7;Q9UKL0","subunits.Entrez.IDs.":"23028;7764;2969;3065;9203;23199;3066;51317;10362;7750;23186","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0091- chromatography technologies","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;organization of chromosome structure;nucleus","PubMed.ID":12493763,"subunits.Protein.name.":"Lysine-specific histone demethylase 1A;Zinc finger protein 217;General transcription factor II-I;Histone deacetylase 1;Zinc finger MYM-type protein 3;Genetic suppressor element 1;Histone deacetylase 2;PHD finger protein 21A;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related;Zinc finger MYM-type protein 2;REST corepressor 1","subunits.Gene.name.":"KDM1A;ZNF217;GTF2I;HDAC1;ZMYM3;GSE1;HDAC2;PHF21A;HMG20B;ZMYM2;RCOR1","subunits.Gene.name.syn.":"AOF2 KDM1 KIAA0601 LSD1;ZABC1;BAP135 WBSCR6;RPD3L1;DXS6673E KIAA0385 ZNF261;KIAA0182;None;BHC80 KIAA1696;BRAF35 HMGX2 HMGXB2 SMARCE1R;FIM RAMP ZNF198;KIAA0071 RCOR","Disease.comment":"XFIM (ZMYM3) is involved in X-linked mental retardation.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":634,"ComplexName":"XFIM complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60341;P78347;Q13547;Q14202;Q92769","subunits.Entrez.IDs.":"23028;2969;3065;9203;3066","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation; MI:0071- molecular sieving","GO.ID":"GO:0006265;GO:0045892;GO:0032774;GO:0006473;GO:0006476;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;RNA biosynthetic process;protein acetylation;protein deacetylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;11.02;14.07.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;RNA synthesis;modification by acetylation, deacetylation;organization of chromosome structure;nucleus","PubMed.ID":12493763,"subunits.Protein.name.":"Lysine-specific histone demethylase 1A;General transcription factor II-I;Histone deacetylase 1;Zinc finger MYM-type protein 3;Histone deacetylase 2","subunits.Gene.name.":"KDM1A;GTF2I;HDAC1;ZMYM3;HDAC2","subunits.Gene.name.syn.":"AOF2 KDM1 KIAA0601 LSD1;BAP135 WBSCR6;RPD3L1;DXS6673E KIAA0385 ZNF261;None","Disease.comment":"XFIM (ZMYM3) is involved in X-linked mental retardation.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":635,"ComplexName":"AGPS-GNPAT complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00116;O15228","subunits.Entrez.IDs.":"8540;8443","Protein.complex.purification.method":"MI:0030- cross-linking studies","GO.ID":"GO:0006720;GO:0006633;GO:0008299;GO:0009062;GO:0016042;GO:0008300;GO:0006629;GO:0006631;GO:0008610;GO:0005777","GO.description":"isoprenoid metabolic process;fatty acid biosynthetic process;isoprenoid biosynthetic process;fatty acid catabolic process;lipid catabolic process;isoprenoid catabolic process;lipid metabolic process;fatty acid metabolic process;lipid biosynthetic process;peroxisome","FunCat.ID":"01.06;01.06.05;01.06.06;70.19","FunCat.description":"lipid, fatty acid and isoprenoid metabolism;fatty acid metabolism;isoprenoid metabolism;peroxisome","PubMed.ID":10215861,"subunits.Protein.name.":"Alkyldihydroxyacetonephosphate synthase, peroxisomal ;Dihydroxyacetone phosphate acyltransferase","subunits.Gene.name.":"AGPS;GNPAT","subunits.Gene.name.syn.":";DAPAT DHAPAT","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":636,"ComplexName":"BHC complex","Organism":"Human","Synonyms":"BRAF-histone deacetylase complex, BRAF-HDAC complex","Cell.line":"None","subunits.UniProt.IDs.":"O60341;Q13547;Q92769;Q96BD5;Q9P0W2;Q9UKL0","subunits.Entrez.IDs.":"23028;3065;3066;51317;10362;23186","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0091- chromatography technologies; MI:0007- anti tag coimmunoprecipitation; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0051276;GO:0030182;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;chromosome organization;neuron differentiation;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;42.10.03;43.03.13;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;organization of chromosome structure;neuron;nucleus","PubMed.ID":12032298,"subunits.Protein.name.":"Lysine-specific histone demethylase 1A;Histone deacetylase 1;Histone deacetylase 2;PHD finger protein 21A;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related;REST corepressor 1","subunits.Gene.name.":"KDM1A;HDAC1;HDAC2;PHF21A;HMG20B;RCOR1","subunits.Gene.name.syn.":"AOF2 KDM1 KIAA0601 LSD1;RPD3L1;None;BHC80 KIAA1696;BRAF35 HMGX2 HMGXB2 SMARCE1R;KIAA0071 RCOR","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The BHC complex mediates repression of neuron-specific genes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":638,"ComplexName":"cGMP kinase signaling complex (IP3RI, IRAG, cGKI-beta)","Organism":"Bovine","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P00516;Q9N1F0;Q9TU34","subunits.Entrez.IDs.":"282004;281918;317697","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0004- affinity chromatography technologies","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0008324;GO:0006812;GO:0019933;GO:0006875;GO:0005886;GO:0005783","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;cation transmembrane transporter activity;cation transport;cAMP-mediated signaling;cellular metal ion homeostasis;plasma membrane;endoplasmic reticulum","FunCat.ID":"14.07.03;20.01.01.01;30.01.09.07;34.01.01.01;70.02;70.07","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);cAMP/cGMP mediated signal transduction;homeostasis of metal ions (Na, K, Ca etc.);eukaryotic plasma membrane / membrane attached;endoplasmic reticulum","PubMed.ID":10724174,"subunits.Protein.name.":"cGMP-dependent protein kinase 1 ;Protein MRVI1 ;Inositol 1,4,5-trisphosphate receptor type 1","subunits.Gene.name.":"PRKG1;MRVI1;ITPR1","subunits.Gene.name.syn.":"PRKG1B PRKGR1A PRKGR1B;IRAG;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results identify IRAG as an essential NO/cGKI-dependent regulator of IP3-induced calcium release.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":639,"ComplexName":"RANBPM-Muskelin-TWA1-HSMpp8 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q96S59;Q99549;Q9NWU2;Q9UL63","subunits.Entrez.IDs.":"10048;54737;54994;4289","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515;GO:0000226;GO:0005737","GO.description":"protein binding;microtubule cytoskeleton organization;cytoplasm","FunCat.ID":"16.01;42.04.05;70.03","FunCat.description":"protein binding;microtubule cytoskeleton;cytoplasm","PubMed.ID":12559565,"subunits.Protein.name.":"Ran-binding protein 9 ;M-phase phosphoprotein 8 ;Glucose-induced degradation protein 8 homolog ;Muskelin","subunits.Gene.name.":"RANBP9;MPHOSPH8;GID8;MKLN1","subunits.Gene.name.syn.":"RANBPM;MPP8;C20orf11;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex might play a role  in RanGTPase cycle.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":640,"ComplexName":"SNARE complex (Snap47, Stx1a, Vamp2)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P32851;P63045;Q6P6S0","subunits.Entrez.IDs.":"116470;24803;303183","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0005515;GO:0006906;GO:0048489;GO:0016079;GO:0005886","GO.description":"protein binding;vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis;plasma membrane","FunCat.ID":"16.01;20.09.07.27;20.09.16.09.05;70.02","FunCat.description":"protein binding;vesicle fusion;synaptic vesicle exocytosis;eukaryotic plasma membrane / membrane attached","PubMed.ID":16621800,"subunits.Protein.name.":"Syntaxin-1A;Vesicle-associated membrane protein 2;Synaptosomal-associated protein 47","subunits.Gene.name.":"Stx1a;Vamp2;Snap47","subunits.Gene.name.syn.":"Sap;Syb2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE complexes are major players in secretory and endocytic vesicular transport. For vesicular fusion, vesicular bound v-SNARE proteins (e.g. synaptobrevin/VAMP) and membrane bound t-SNARE proteins (e.g. syntaxin and SNAP-25) form a ternary complex which performs the fusion of vesicle and membrane.  In vitro, the SNARE complex consisting of Snap47, syntaxin 1a and VAMP-2 was shown to catalyze the fusion of proteoliposomes.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":641,"ComplexName":"RANBPM-SMP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95807;Q96S59","subunits.Entrez.IDs.":"23585;10048","Protein.complex.purification.method":"MI:0018- two hybrid; MI:0019- coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0007276;GO:0005737","GO.description":"gamete generation;cytoplasm","FunCat.ID":"41.05.25;70.03","FunCat.description":"gametogenesis;cytoplasm","PubMed.ID":15014887,"subunits.Protein.name.":"Transmembrane protein 50A ;Ran-binding protein 9","subunits.Gene.name.":"TMEM50A;RANBP9","subunits.Gene.name.syn.":"SMP1;RANBPM","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex may be involved in the process of male germ cell differentiation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":642,"ComplexName":"CtBP complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00257;O60315;O60341;O75362;P37275;P56545;Q13363;Q13547;Q92618;Q92766;Q92769;Q96JN0;Q96KQ7;Q9H9B1;Q9P2K3;Q9UKL0;Q9Y232","subunits.Entrez.IDs.":"8535;9839;23028;7764;6935;1488;1487;3065;9658;6239;3066;84458;10919;79813;55758;23186;9425","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0018126;GO:0006479;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;protein hydroxylation;protein methylation;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;14.07.09;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;posttranslational modification of amino acids (e.g. hydroxylation, methylation);DNA binding;organization of chromosome structure;nucleus","PubMed.ID":12700765,"subunits.Protein.name.":"E3 SUMO-protein ligase CBX4;Zinc finger E-box-binding homeobox 2;Lysine-specific histone demethylase 1A;Zinc finger protein 217;Zinc finger E-box-binding homeobox 1 ;C-terminal-binding protein 2 ;C-terminal-binding protein 1;Histone deacetylase 1;Zinc finger protein 516;Ras-responsive element-binding protein 1;Histone deacetylase 2;Ligand-dependent corepressor ;Histone-lysine N-methyltransferase EHMT2 ;Histone-lysine N-methyltransferase EHMT1 ;REST corepressor 3;REST corepressor 1;Chromodomain Y-like protein","subunits.Gene.name.":"CBX4;ZEB2;KDM1A;ZNF217;ZEB1;CTBP2;CTBP1;HDAC1;ZNF516;RREB1;HDAC2;LCOR;EHMT2;EHMT1;RCOR3;RCOR1;CDYL","subunits.Gene.name.syn.":"None;KIAA0569 SIP1 ZFHX1B ZFX1B;AOF2 KDM1 KIAA0601 LSD1;ZABC1;AREB6 TCF8;;CTBP;RPD3L1;KIAA0222;FINB;None;KIAA1795 MLR2;BAT8 C6orf30 G9A KMT1C NG36;EUHMTASE1 GLP KIAA1876 KMT1D;KIAA1343;KIAA0071 RCOR;CDYL1","Disease.comment":"CtBP is implicated in tumorigenesis.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":643,"ComplexName":"CtBP core complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60341;P37275;P56545;Q13363;Q13547;Q92769;Q96KQ7;Q9H9B1;Q9UKL0","subunits.Entrez.IDs.":"23028;6935;1488;1487;3065;3066;10919;79813;23186","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0071- molecular sieving","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0018126;GO:0006479;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;protein hydroxylation;protein methylation;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;14.07.09;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;posttranslational modification of amino acids (e.g. hydroxylation, methylation);DNA binding;organization of chromosome structure;nucleus","PubMed.ID":12700765,"subunits.Protein.name.":"Lysine-specific histone demethylase 1A;Zinc finger E-box-binding homeobox 1 ;C-terminal-binding protein 2 ;C-terminal-binding protein 1;Histone deacetylase 1;Histone deacetylase 2;Histone-lysine N-methyltransferase EHMT2 ;Histone-lysine N-methyltransferase EHMT1 ;REST corepressor 1","subunits.Gene.name.":"KDM1A;ZEB1;CTBP2;CTBP1;HDAC1;HDAC2;EHMT2;EHMT1;RCOR1","subunits.Gene.name.syn.":"AOF2 KDM1 KIAA0601 LSD1;AREB6 TCF8;;CTBP;RPD3L1;None;BAT8 C6orf30 G9A KMT1C NG36;EUHMTASE1 GLP KIAA1876 KMT1D;KIAA0071 RCOR","Disease.comment":"CtBP is implicated in tumorigenesis.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":644,"ComplexName":"ASPP1-SAM68 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q07666;Q96KQ4","subunits.Entrez.IDs.":"10657;23368","Protein.complex.purification.method":"MI:0018- two hybrid","GO.ID":"GO:0008380;GO:0005634","GO.description":"RNA splicing;nucleus","FunCat.ID":"11.04.03.01;70.10","FunCat.description":"splicing;nucleus","PubMed.ID":16474851,"subunits.Protein.name.":"KH domain-containing, RNA-binding, signal transduction-associated protein 1 ;Apoptosis-stimulating of p53 protein 1","subunits.Gene.name.":"KHDRBS1;PPP1R13B","subunits.Gene.name.syn.":"SAM68;ASPP1 KIAA0771","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors suggest that the interaction of ASPP1 with nuclear SAM68 is spatially restricted to human spermatogenesis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":646,"ComplexName":"HDAC1-associated protein complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60341;O94776;O95983;Q09028;Q12873;Q13547;Q16576;Q9UBB5;Q9UKL0","subunits.Entrez.IDs.":"23028;9219;53615;5928;1107;3065;5931;8932;23186","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0018126;GO:0006479;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;protein hydroxylation;protein methylation;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;14.07.09;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;posttranslational modification of amino acids (e.g. hydroxylation, methylation);DNA binding;organization of chromosome structure;nucleus","PubMed.ID":11102443,"subunits.Protein.name.":"Lysine-specific histone demethylase 1A;Metastasis-associated protein MTA2;Methyl-CpG-binding domain protein 3;Histone-binding protein RBBP4;Chromodomain-helicase-DNA-binding protein 3;Histone deacetylase 1;Histone-binding protein RBBP7;Methyl-CpG-binding domain protein 2;REST corepressor 1","subunits.Gene.name.":"KDM1A;MTA2;MBD3;RBBP4;CHD3;HDAC1;RBBP7;MBD2;RCOR1","subunits.Gene.name.syn.":"AOF2 KDM1 KIAA0601 LSD1;MTA1L1 PID;None;RBAP48;None;RPD3L1;RBAP46;None;KIAA0071 RCOR","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":647,"ComplexName":"HPFH(-198) complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O70422;P13864;P69892;Q3THK3","subunits.Entrez.IDs.":"14885;13433;3048;98053","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:2001141;GO:0006355;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;nucleus","FunCat.ID":"11.02.03.04;70.10","FunCat.description":"transcriptional control;nucleus","PubMed.ID":17114178,"subunits.Protein.name.":"General transcription factor IIH subunit 4 ;DNA ;Hemoglobin subunit gamma-2 ;General transcription factor IIF subunit 1","subunits.Gene.name.":"Gtf2h4;Dnmt1;HBG2;Gtf2f1","subunits.Gene.name.syn.":";Dnmt Met1 Uim;;","Disease.comment":"None","Subunits.comment":"Since Hbg1 from mouse was not available in the UniProt database at the time of annotation, the orthologous protein from human was used.","Complex.comment":"Described complex contains Britisch HPFH mutant carrying a T->C point mutation.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Homo sapiens (Human);Mus musculus (Mouse)"}
{"ComplexID":648,"ComplexName":"HDAC1-associated core complex cI","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60341;Q13547;Q9UKL0","subunits.Entrez.IDs.":"23028;3065;23186","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0007- anti tag coimmunoprecipitation; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0018126;GO:0006479;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;protein hydroxylation;protein methylation;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;14.07.09;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;posttranslational modification of amino acids (e.g. hydroxylation, methylation);DNA binding;organization of chromosome structure;nucleus","PubMed.ID":11102443,"subunits.Protein.name.":"Lysine-specific histone demethylase 1A;Histone deacetylase 1;REST corepressor 1","subunits.Gene.name.":"KDM1A;HDAC1;RCOR1","subunits.Gene.name.syn.":"AOF2 KDM1 KIAA0601 LSD1;RPD3L1;KIAA0071 RCOR","Disease.comment":"None","Subunits.comment":"Another subunit of the complex was found in the analysis, which has not been further characterized: p37.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":649,"ComplexName":"HDAC1-associated core complex cII","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O94776;O95983;Q09028;Q12873;Q13547;Q16576;Q86YP4;Q9UBB5;Q9UKL0","subunits.Entrez.IDs.":"9219;53615;5928;1107;3065;5931;54815;8932;23186","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation;MI:0007-anti tag coimmunoprecipitation;MI:0029-cosedimentation through density gradients","GO.ID":"GO:0006265;GO:0045892;GO:0006476;GO:0018126;GO:0006479;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein deacetylation;protein hydroxylation;protein methylation;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;14.07.09;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;posttranslational modification of amino acids (e.g. hydroxylation, methylation);DNA binding;organization of chromosome structure;nucleus","PubMed.ID":11102443,"subunits.Protein.name.":"Metastasis-associated protein MTA2;Methyl-CpG-binding domain protein 3;Histone-binding protein RBBP4;Chromodomain-helicase-DNA-binding protein 3;Histone deacetylase 1;Histone-binding protein RBBP7;Transcriptional repressor p66-alpha;Methyl-CpG-binding domain protein 2;REST corepressor 1","subunits.Gene.name.":"MTA2;MBD3;RBBP4;CHD3;HDAC1;RBBP7;GATAD2A;MBD2;RCOR1","subunits.Gene.name.syn.":"MTA1L1 PID;None;RBAP48;None;RPD3L1;RBAP46;None;None;KIAA0071 RCOR","Disease.comment":"None","Subunits.comment":"Since the authors did not specify GATAD2, we used isoform GATAD2A.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":650,"ComplexName":"HDAC2-asscociated core complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O94776;O95983;Q09028;Q12873;Q16576;Q86YP4;Q92769","subunits.Entrez.IDs.":"9219;53615;5928;1107;5931;54815;3066","Protein.complex.purification.method":"MI:0029-cosedimentation through density gradients;MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0018126;GO:0006479;GO:0003677;GO:0051276;GO:0005634;GO:0016575","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein hydroxylation;protein methylation;DNA binding;chromosome organization;nucleus;histone deacetylation","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.09;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;posttranslational modification of amino acids (e.g. hydroxylation, methylation);DNA binding;organization of chromosome structure;nucleus","PubMed.ID":11102443,"subunits.Protein.name.":"Metastasis-associated protein MTA2;Methyl-CpG-binding domain protein 3;Histone-binding protein RBBP4;Chromodomain-helicase-DNA-binding protein 3;Histone-binding protein RBBP7;Transcriptional repressor p66-alpha;Histone deacetylase 2","subunits.Gene.name.":"MTA2;MBD3;RBBP4;CHD3;RBBP7;GATAD2A;HDAC2","subunits.Gene.name.syn.":"MTA1L1 PID;None;RBAP48;None;RBAP46;None;None","Disease.comment":"None","Subunits.comment":"Since the authors did not specify GATAD2, we used isoform GATAD2A.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":651,"ComplexName":"SNARE complex (Snap25, Stx1a, Vamp2)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P32851;P60881;P63045","subunits.Entrez.IDs.":"116470;25012;24803","Protein.complex.purification.method":"MI:0091- chromatography technologies","GO.ID":"GO:0005515;GO:0006906;GO:0048489;GO:0016079;GO:0005886","GO.description":"protein binding;vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis;plasma membrane","FunCat.ID":"16.01;20.09.07.27;20.09.16.09.05;70.02","FunCat.description":"protein binding;vesicle fusion;synaptic vesicle exocytosis;eukaryotic plasma membrane / membrane attached","PubMed.ID":9177194,"subunits.Protein.name.":"Syntaxin-1A;Synaptosomal-associated protein 25;Vesicle-associated membrane protein 2","subunits.Gene.name.":"Stx1a;Snap25;Vamp2","subunits.Gene.name.syn.":"Sap;Snap;Syb2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE complexes are major players in secretory and endocytic vesicular transport. For vesicular fusion, vesicular bound v-SNARE proteins (e.g. synaptobrevin/VAMP) and membrane bound t-SNARE proteins (e.g. syntaxin and SNAP-25) form a ternary complex which performs the fusion of vesicle and membrane.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":652,"ComplexName":"AP3-BLOC1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00203;O14617;O95295;P53677;P59780;P78537;Q13367;Q6QNY0;Q6QNY1;Q8TDH9;Q92572;Q96EV8;Q9NUP1;Q9UL45;Q9Y2T2","subunits.Entrez.IDs.":"8546;8943;23557;10947;10239;2647;8120;388552;282991;63915;1176;84062;55330;26258;26985","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":16837549,"subunits.Protein.name.":"AP-3 complex subunit beta-1;AP-3 complex subunit delta-1;SNARE-associated protein Snapin;AP-3 complex subunit mu-2;AP-3 complex subunit sigma-2;Biogenesis of lysosome-related organelles complex 1 subunit 1;AP-3 complex subunit beta-2;Biogenesis of lysosome-related organelles complex 1 subunit 3 ;Biogenesis of lysosome-related organelles complex 1 subunit 2;Biogenesis of lysosome-related organelles complex 1 subunit 5 ;AP-3 complex subunit sigma-1;Dysbindin;Biogenesis of lysosome-related organelles complex 1 subunit 4;Biogenesis of lysosome-related organelles complex 1 subunit 6;AP-3 complex subunit mu-1","subunits.Gene.name.":"AP3B1;AP3D1;SNAPIN;AP3M2;AP3S2;BLOC1S1;AP3B2;BLOC1S3;BLOC1S2;BLOC1S5;AP3S1;DTNBP1;BLOC1S4;BLOC1S6;AP3M1","subunits.Gene.name.syn.":"ADTB3A;None;BLOC1S7 SNAP25BP SNAPAP;None;None;BLOS1 GCN5L1 RT14;None;BLOS3;BLOS2 CEAP;MUTED;CLAPS3;BLOC1S8;CNO;PA, PLDN;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"BLOC-1 interacts physically and functionally with AP-3 to facilitate the trafficking of a known AP-3 cargo.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":653,"ComplexName":"SNARE complex (Ykt6, Stx5, Gosr2, Bet1)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O35165;Q08851;Q5EGY4;Q62896","subunits.Entrez.IDs.":"64154;65134;64351;29631","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515;GO:0006906;GO:0048489;GO:0016079;GO:0005886","GO.description":"protein binding;vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis;plasma membrane","FunCat.ID":"16.01;20.09.07.27;20.09.16.09.05;70.02","FunCat.description":"protein binding;vesicle fusion;synaptic vesicle exocytosis;eukaryotic plasma membrane / membrane attached","PubMed.ID":12589064,"subunits.Protein.name.":"Golgi SNAP receptor complex member 2 ;Syntaxin-5;Synaptobrevin homolog YKT6 ;BET1 homolog","subunits.Gene.name.":"Gosr2;Stx5;Ykt6;Bet1","subunits.Gene.name.syn.":"Gs27;Stx5a;;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE complexes are major players in secretory and endocytic vesicular transport. For vesicular fusion, vesicular bound v-SNARE proteins (e.g. synaptobrevin/VAMP) and membrane bound t-SNARE proteins (e.g. syntaxin and SNAP-25) form a ternary complex which performs the fusion of vesicle and membrane. Ykt6 was found to be selectively expressed in brain neurons.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":654,"ComplexName":"BLOC1-BLOC2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95295;P78537;Q6QNY0;Q6QNY1;Q86YV9;Q8TDH9;Q969F9;Q96EV8;Q9NUP1;Q9UL45;Q9UPZ3","subunits.Entrez.IDs.":"23557;2647;388552;282991;79803;63915;84343;84062;55330;26258;11234","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0005768","GO.description":"intracellular protein transport;protein targeting;protein transport;endosome","FunCat.ID":"14.04;20.01.10;70.22","FunCat.description":"protein targeting, sorting and translocation;protein transport;endosome","PubMed.ID":16837549,"subunits.Protein.name.":"SNARE-associated protein Snapin;Biogenesis of lysosome-related organelles complex 1 subunit 1;Biogenesis of lysosome-related organelles complex 1 subunit 3 ;Biogenesis of lysosome-related organelles complex 1 subunit 2;Hermansky-Pudlak syndrome 6 protein ;Biogenesis of lysosome-related organelles complex 1 subunit 5 ;Hermansky-Pudlak syndrome 3 protein;Dysbindin;Biogenesis of lysosome-related organelles complex 1 subunit 4;Biogenesis of lysosome-related organelles complex 1 subunit 6;Hermansky-Pudlak syndrome 5 protein","subunits.Gene.name.":"SNAPIN;BLOC1S1;BLOC1S3;BLOC1S2;HPS6;BLOC1S5;HPS3;DTNBP1;BLOC1S4;BLOC1S6;HPS5","subunits.Gene.name.syn.":"BLOC1S7 SNAP25BP SNAPAP;BLOS1 GCN5L1 RT14;BLOS3;BLOS2 CEAP;;MUTED;;BLOC1S8;CNO;PA, PLDN;AIBP63 KIAA1017","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"BLOC-1 interacts with BLOC-2 to facilitate Tyrp1 trafficking by a mechanism apparently independent of AP-3 function.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":655,"ComplexName":"HSF1-HSF2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q00613;Q03933","subunits.Entrez.IDs.":"3297;3298","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515","GO.description":"protein binding","FunCat.ID":"16.01","FunCat.description":"protein binding","PubMed.ID":16336210,"subunits.Protein.name.":"Heat shock factor protein 1 ;Heat shock factor protein 2","subunits.Gene.name.":"HSF1;HSF2","subunits.Gene.name.syn.":"HSTF1;HSTF2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":656,"ComplexName":"VPS35-VPS29-VPS26A complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75436;Q96QK1;Q9UBQ0","subunits.Entrez.IDs.":"9559;55737;51699","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031","GO.description":"intracellular protein transport;protein targeting;protein transport","FunCat.ID":"14.04;20.01.10","FunCat.description":"protein targeting, sorting and translocation;protein transport","PubMed.ID":11102511,"subunits.Protein.name.":"Vacuolar protein sorting-associated protein 26A ;Vacuolar protein sorting-associated protein 35 ;Vacuolar protein sorting-associated protein 29","subunits.Gene.name.":"VPS26A;VPS35;VPS29","subunits.Gene.name.syn.":"VPS26;MEM3;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":657,"ComplexName":"Retromer complex (SNX1, SNX2, VPS35, VPS29, VPS26A)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60749;O75436;Q13596;Q96QK1;Q9UBQ0","subunits.Entrez.IDs.":"6643;9559;6642;55737;51699","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0018- two hybrid; MI:0051- fluorescence technologies","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0016192;GO:0036465;GO:0000301","GO.description":"intracellular protein transport;protein targeting;protein transport;vesicle-mediated transport;synaptic vesicle recycling;retrograde transport, vesicle recycling within Golgi","FunCat.ID":"14.04;20.01.10;20.09.07;20.09.07.29;20.09.07.07","FunCat.description":"protein targeting, sorting and translocation;protein transport;vesicular transport (Golgi network, etc.);vesicle recycling;retrograde transport","PubMed.ID":16732284,"subunits.Protein.name.":"Sorting nexin-2 ;Vacuolar protein sorting-associated protein 26A ;Sorting nexin-1;Vacuolar protein sorting-associated protein 35 ;Vacuolar protein sorting-associated protein 29","subunits.Gene.name.":"SNX2;VPS26A;SNX1;VPS35;VPS29","subunits.Gene.name.syn.":";VPS26;;MEM3;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":658,"ComplexName":"SNARE complex (Sec22b, Stx5, Gosr2, Bet1)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O35165;Q08851;Q4KM74;Q62896","subunits.Entrez.IDs.":"64154;65134;310710;29631","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515;GO:0006906;GO:0048489;GO:0016079;GO:0005886","GO.description":"protein binding;vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis;plasma membrane","FunCat.ID":"16.01;20.09.07.27;20.09.16.09.05;70.02","FunCat.description":"protein binding;vesicle fusion;synaptic vesicle exocytosis;eukaryotic plasma membrane / membrane attached","PubMed.ID":11035026,"subunits.Protein.name.":"Golgi SNAP receptor complex member 2 ;Syntaxin-5;Vesicle-trafficking protein SEC22b ;BET1 homolog","subunits.Gene.name.":"Gosr2;Stx5;Sec22b;Bet1","subunits.Gene.name.syn.":"Gs27;Stx5a;Sec22l1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE complexes are major players in secretory and endocytic vesicular transport. For vesicular fusion, vesicular bound v-SNARE proteins (e.g. synaptobrevin/VAMP) and membrane bound t-SNARE proteins (e.g. syntaxin and SNAP-25) form a ternary complex which performs the fusion of vesicle and membrane.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":659,"ComplexName":"MeCP1 complex","Organism":"Human","Synonyms":"Mi2/NuRD-MBD2 complex","Cell.line":"None","subunits.UniProt.IDs.":"O94776;O95983;Q09028;Q13547;Q14839;Q16576;Q8WXI9;Q92769;Q9UBB5","subunits.Entrez.IDs.":"9219;53615;5928;3065;1108;5931;57459;3066;8932","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0032774;GO:0006473;GO:0006476;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;RNA biosynthetic process;protein acetylation;protein deacetylation;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;11.02;14.07.04;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;RNA synthesis;modification by acetylation, deacetylation;DNA binding;organization of chromosome structure;nucleus","PubMed.ID":11297506,"subunits.Protein.name.":"Metastasis-associated protein MTA2;Methyl-CpG-binding domain protein 3;Histone-binding protein RBBP4;Histone deacetylase 1;Chromodomain-helicase-DNA-binding protein 4;Histone-binding protein RBBP7;Transcriptional repressor p66-beta ;Histone deacetylase 2;Methyl-CpG-binding domain protein 2","subunits.Gene.name.":"MTA2;MBD3;RBBP4;HDAC1;CHD4;RBBP7;GATAD2B;HDAC2;MBD2","subunits.Gene.name.syn.":"MTA1L1 PID;None;RBAP48;RPD3L1;None;RBAP46;KIAA1150;None;None","Disease.comment":"CHD4 is involved in dermatomyositis (PMID:9790534).","Subunits.comment":"None","Complex.comment":"MeCP1 protein complex represses transcription through preferential binding, remodeling, and deacetylation of methylated nucleosomes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":661,"ComplexName":"Karyopherin complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P25961;P52296;P83953","subunits.Entrez.IDs.":"56813;24917;288064","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0019- coimmunoprecipitation","GO.ID":"GO:0051169","GO.description":"nuclear transport","FunCat.ID":"20.09.01","FunCat.description":"nuclear transport","PubMed.ID":16574786,"subunits.Protein.name.":"Parathyroid hormone/parathyroid hormone-related peptide receptor ;Importin subunit beta-1 ;Importin subunit alpha-5","subunits.Gene.name.":"Pth1r;Kpnb1;Kpna1","subunits.Gene.name.syn.":"Pthr Pthr1;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":662,"ComplexName":"Hoxa9-PBX2-Meis1 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P09631;P40425;Q60954","subunits.Entrez.IDs.":"15405;5089;17268","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0003677;GO:0030218;GO:0005634","GO.description":"DNA binding;erythrocyte differentiation;nucleus","FunCat.ID":"16.03.01;43.03.07;70.10","FunCat.description":"DNA binding;blood cell;nucleus","PubMed.ID":10082572,"subunits.Protein.name.":"Homeobox protein Hox-A9 ;Pre-B-cell leukemia transcription factor 2 ;Homeobox protein Meis1","subunits.Gene.name.":"Hoxa9;PBX2;Meis1","subunits.Gene.name.syn.":"Hox-1.7 Hoxa-9;G17;","Disease.comment":"Hoxa9, PBX2 and Meis1 are associated with leukemias.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Homo sapiens (Human);Mus musculus (Mouse)"}
{"ComplexID":663,"ComplexName":"SNARE complex (Stx5, Ykt6, Gosr1, Bet1)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O35152;Q08851;Q5EGY4;Q62931","subunits.Entrez.IDs.":"54400;65134;64351;94189","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515;GO:0015031;GO:0008565;GO:0006891;GO:0006906;GO:0048489;GO:0016079;GO:0005794;GO:0005768","GO.description":"protein binding;protein transport;protein transporter activity;intra-Golgi vesicle-mediated transport;vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis;Golgi apparatus;endosome","FunCat.ID":"16.01;20.01.10;20.09.07.05;20.09.07.27;20.09.16.09.05;70.08;70.22","FunCat.description":"protein binding;protein transport;intra Golgi transport;vesicle fusion;synaptic vesicle exocytosis;Golgi;endosome","PubMed.ID":14742712,"subunits.Protein.name.":"BET1-like protein;Syntaxin-5;Synaptobrevin homolog YKT6 ;Golgi SNAP receptor complex member 1","subunits.Gene.name.":"Bet1l;Stx5;Ykt6;Gosr1","subunits.Gene.name.syn.":"Gs15;Stx5a;;Gs28","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":664,"ComplexName":"SNARE complex (Stx5, Gosr2, Sec22b, Bet1)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O35165;Q08851;Q4KM74;Q62896","subunits.Entrez.IDs.":"64154;65134;310710;29631","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515;GO:0015031;GO:0008565;GO:0006891;GO:0006906;GO:0048489;GO:0016079;GO:0005794;GO:0005768","GO.description":"protein binding;protein transport;protein transporter activity;intra-Golgi vesicle-mediated transport;vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis;Golgi apparatus;endosome","FunCat.ID":"16.01;20.01.10;20.09.07.05;20.09.07.27;20.09.16.09.05;70.08;70.22","FunCat.description":"protein binding;protein transport;intra Golgi transport;vesicle fusion;synaptic vesicle exocytosis;Golgi;endosome","PubMed.ID":14742712,"subunits.Protein.name.":"Golgi SNAP receptor complex member 2 ;Syntaxin-5;Vesicle-trafficking protein SEC22b ;BET1 homolog","subunits.Gene.name.":"Gosr2;Stx5;Sec22b;Bet1","subunits.Gene.name.syn.":"Gs27;Stx5a;Sec22l1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":665,"ComplexName":"BKCA alpha-Cav1.2 channel complex","Organism":"Rat","Synonyms":"None","Cell.line":"central nervous system","subunits.UniProt.IDs.":"P22002;Q62976","subunits.Entrez.IDs.":"24239;83731","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies;MI:0019-coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0050896;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;response to stimulus;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;36.25;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;animal specific systemic sensing and response;eukaryotic plasma membrane / membrane attached","PubMed.ID":17068255,"subunits.Protein.name.":"Voltage-dependent L-type calcium channel subunit alpha-1C;Calcium-activated potassium channel subunit alpha-1","subunits.Gene.name.":"Cacna1c;Kcnma1","subunits.Gene.name.syn.":"Cach2 Cacn2 Cacnl1a1 Cchl1a1;Kcnma","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"BKCa-Cav complexes reconstitute a functional Ca(2+) nanodomain where Ca(2+) influx through the Cav channel activates BKCa in the physiological voltage range with submillisecond kinetics.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":666,"ComplexName":"BKCA alpha-Cav2.1 channel complex","Organism":"Rat","Synonyms":"None","Cell.line":"central nervous system","subunits.UniProt.IDs.":"P54282;Q62976","subunits.Entrez.IDs.":"25398;83731","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies;MI:0019-coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0050896;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;response to stimulus;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;36.25;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;animal specific systemic sensing and response;eukaryotic plasma membrane / membrane attached","PubMed.ID":17068255,"subunits.Protein.name.":"Voltage-dependent P/Q-type calcium channel subunit alpha-1A;Calcium-activated potassium channel subunit alpha-1","subunits.Gene.name.":"Cacna1a;Kcnma1","subunits.Gene.name.syn.":"Cach4 Cacn3 Cacnl1a4;Kcnma","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"BKCa-Cav complexes reconstitute a functional Ca(2+) nanodomain where Ca(2+) influx through the Cav channel activates BKCa in the physiological voltage range with submillisecond kinetics.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":667,"ComplexName":"BKCA alpha-Cav2.2 channel complex","Organism":"Rat","Synonyms":"None","Cell.line":"central nervous system","subunits.UniProt.IDs.":"Q02294;Q62976","subunits.Entrez.IDs.":"257648;83731","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies;MI:0019-coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0050896;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;response to stimulus;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;36.25;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;animal specific systemic sensing and response;eukaryotic plasma membrane / membrane attached","PubMed.ID":17068255,"subunits.Protein.name.":"Voltage-dependent N-type calcium channel subunit alpha-1B;Calcium-activated potassium channel subunit alpha-1","subunits.Gene.name.":"Cacna1b;Kcnma1","subunits.Gene.name.syn.":"Cach5 Cacnl1a5;Kcnma","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"BKCa-Cav complexes reconstitute a functional Ca(2+) nanodomain where Ca(2+) influx through the Cav channel activates BKCa in the physiological voltage range with submillisecond kinetics.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":668,"ComplexName":"BKCA-beta2AR-AKAP79 signaling complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P07550;P24588;Q12791","subunits.Entrez.IDs.":"154;9495;3778","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0007186;GO:0050896;GO:0006939","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;G-protein coupled receptor signaling pathway;response to stimulus;smooth muscle contraction","FunCat.ID":"20.01.01.01;20.03.01.01;30.05.02.24;36.25;36.25.09.01","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;G-protein coupled receptor signalling pathway;animal specific systemic sensing and response;smooth muscle contraction","PubMed.ID":15141163,"subunits.Protein.name.":"Beta-2 adrenergic receptor;A-kinase anchor protein 5;Calcium-activated potassium channel subunit alpha-1","subunits.Gene.name.":"ADRB2;AKAP5;KCNMA1","subunits.Gene.name.syn.":"ADRB2R B2AR;AKAP79;KCNMA SLO","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"BKCa is preferentially regulated by beta2AR within the channel macromolecular complex. Only expression of all three components of the complex reconstituted full-beta2 agonist modulation of the channel.  The ability of beta2AR to form a complex with BKCa, and concomitantly bind phosphorylation-modulatory components (AKAP79/150) enables specific and local regulation of BKCa channels and defines a signal transduction pathway governing cellular excitability in diverse tissues.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":669,"ComplexName":"beta2AR-AKAP79/150  complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P10608;P24587","subunits.Entrez.IDs.":"24176;171026","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0007186;GO:0050896","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;G-protein coupled receptor signaling pathway;response to stimulus","FunCat.ID":"20.01.01.01;20.03.01.01;30.05.02.24;36.25","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;G-protein coupled receptor signalling pathway;animal specific systemic sensing and response","PubMed.ID":15141163,"subunits.Protein.name.":"Beta-2 adrenergic receptor ;A-kinase anchor protein 5","subunits.Gene.name.":"Adrb2;Akap5","subunits.Gene.name.syn.":"Adrb2r;Akap150","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Beta2AR constitutively recruits AKAP79, which enables the targeting of AKAP79 to the channel (PMID:10753752).AKAP79 associates with beta2AR via the third intracellular loop and the C-terminus independently (PMID:10753752).","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":670,"ComplexName":"BKCa-AKAP79/150 complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P24587;Q62976","subunits.Entrez.IDs.":"171026;83731","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0007186;GO:0050896","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;G-protein coupled receptor signaling pathway;response to stimulus","FunCat.ID":"20.01.01.01;20.03.01.01;30.05.02.24;36.25","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;G-protein coupled receptor signalling pathway;animal specific systemic sensing and response","PubMed.ID":15141163,"subunits.Protein.name.":"A-kinase anchor protein 5 ;Calcium-activated potassium channel subunit alpha-1","subunits.Gene.name.":"Akap5;Kcnma1","subunits.Gene.name.syn.":"Akap150;Kcnma","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":671,"ComplexName":"BKCa-beta2AR complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P10608;Q62976","subunits.Entrez.IDs.":"24176;83731","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0007186;GO:0050896","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;G-protein coupled receptor signaling pathway;response to stimulus","FunCat.ID":"20.01.01.01;20.03.01.01;30.05.02.24;36.25","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;G-protein coupled receptor signalling pathway;animal specific systemic sensing and response","PubMed.ID":15141163,"subunits.Protein.name.":"Beta-2 adrenergic receptor ;Calcium-activated potassium channel subunit alpha-1","subunits.Gene.name.":"Adrb2;Kcnma1","subunits.Gene.name.syn.":"Adrb2r;Kcnma","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":672,"ComplexName":"BKCA-beta2AR complex","Organism":"Human","Synonyms":"None","Cell.line":"lung","subunits.UniProt.IDs.":"P07550;Q12791","subunits.Entrez.IDs.":"154;3778","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0007186;GO:0050896","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;G-protein coupled receptor signaling pathway;response to stimulus","FunCat.ID":"20.01.01.01;20.03.01.01;30.05.02.24;36.25","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;G-protein coupled receptor signalling pathway;animal specific systemic sensing and response","PubMed.ID":15141163,"subunits.Protein.name.":"Beta-2 adrenergic receptor;Calcium-activated potassium channel subunit alpha-1","subunits.Gene.name.":"ADRB2;KCNMA1","subunits.Gene.name.syn.":"ADRB2R B2AR;KCNMA SLO","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":673,"ComplexName":"SNARE complex (Stx5, p97, Nsfl1c)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O35987;P46462;Q08851","subunits.Entrez.IDs.":"83809;116643;65134","Protein.complex.purification.method":"MI:0040- electron microscopy","GO.ID":"GO:0005515;GO:0015031;GO:0008565;GO:0006888;GO:0006906;GO:0048489;GO:0016079;GO:0005783;GO:0005794","GO.description":"protein binding;protein transport;protein transporter activity;ER to Golgi vesicle-mediated transport;vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis;endoplasmic reticulum;Golgi apparatus","FunCat.ID":"16.01;20.01.10;20.09.07.03;20.09.07.27;20.09.16.09.05;70.07;70.08","FunCat.description":"protein binding;protein transport;ER to Golgi transport;vesicle fusion;synaptic vesicle exocytosis;endoplasmic reticulum;Golgi","PubMed.ID":10930451,"subunits.Protein.name.":"NSFL1 cofactor p47;Transitional endoplasmic reticulum ATPase;Syntaxin-5","subunits.Gene.name.":"Nsfl1c;Vcp;Stx5","subunits.Gene.name.syn.":"None;None;Stx5a","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway. The SNARE complex containing syntaxin5, p97 and p47 is involved in the regulation of the smooth domain of transitional ER and hence one of the earliest membrane differentiated components of the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":674,"ComplexName":"Gamma-secretase complex (Aph1a, Ncstn, Psen1, Psenen, Tmp21)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P49769;P57716;Q8BVF7;Q9CQR7;Q9D1D4","subunits.Entrez.IDs.":"19164;59287;226548;66340;68581","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0050789","GO.description":"regulation of biological process","FunCat.ID":"18","FunCat.description":"REGULATION OF METABOLISM AND PROTEIN FUNCTION","PubMed.ID":16641999,"subunits.Protein.name.":"Presenilin-1 ;Nicastrin;Gamma-secretase subunit APH-1A ;Gamma-secretase subunit PEN-2 ;Transmembrane emp24 domain-containing protein 10","subunits.Gene.name.":"Psen1;Ncstn;Aph1a;Psenen;Tmed10","subunits.Gene.name.syn.":"Ad3h Psnl1;;;Pen2;Tmp21","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":675,"ComplexName":"TMP21-P24 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P97799;Q9D1D4","subunits.Entrez.IDs.":"22360;68581","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016192;GO:0005783;GO:0005794","GO.description":"vesicle-mediated transport;endoplasmic reticulum;Golgi apparatus","FunCat.ID":"20.09.07;70.07;70.08","FunCat.description":"vesicular transport (Golgi network, etc.);endoplasmic reticulum;Golgi","PubMed.ID":16641999,"subunits.Protein.name.":"Neurensin-1 ;Transmembrane emp24 domain-containing protein 10","subunits.Gene.name.":"Nrsn1;Tmed10","subunits.Gene.name.syn.":"Vmp;Tmp21","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":676,"ComplexName":"Metallothionein-3 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"O08553;P11499;P28184;P60710;Q04447;Q61696","subunits.Entrez.IDs.":"12934;15516;17751;11461;12709;193740","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies;MI:0069- mass spectrometry studies of complexes","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":17018872,"subunits.Protein.name.":"Dihydropyrimidinase-related protein 2 ;Heat shock protein HSP 90-beta ;Metallothionein-3 ;Actin, cytoplasmic 1;Creatine kinase B-type ;Heat shock 70 kDa protein 1A","subunits.Gene.name.":"Dpysl2;Hsp90ab1;Mt3;Actb;Ckb;Hspa1a","subunits.Gene.name.syn.":"Crmp2 Ulip2;Hsp84 Hsp84-1 Hspcb;;None;Ckbb;Hsp70-3 Hsp70A1","Disease.comment":"None","Subunits.comment":"Metallothionein-3 consists of 16 proteins but only five were identified.","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":677,"ComplexName":"Mt3-Hsp84-Ck complex","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P11499;P28184;Q04447","subunits.Entrez.IDs.":"15516;17751;12709","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":17018872,"subunits.Protein.name.":"Heat shock protein HSP 90-beta ;Metallothionein-3 ;Creatine kinase B-type","subunits.Gene.name.":"Hsp90ab1;Mt3;Ckb","subunits.Gene.name.syn.":"Hsp84 Hsp84-1 Hspcb;;Ckbb","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":678,"ComplexName":"GINS complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q14691;Q9BRT9;Q9BRX5;Q9Y248","subunits.Entrez.IDs.":"9837;84296;64785;51659","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006267;GO:0003688;GO:0005634","GO.description":"pre-replicative complex assembly involved in nuclear cell cycle DNA replication;DNA replication origin binding;nucleus","FunCat.ID":"10.01.03.03;70.10","FunCat.description":"ori recognition and priming complex formation;nucleus","PubMed.ID":17170760,"subunits.Protein.name.":"DNA replication complex GINS protein PSF1 ;DNA replication complex GINS protein SLD5 ;DNA replication complex GINS protein PSF3 ;DNA replication complex GINS protein PSF2","subunits.Gene.name.":"GINS1;GINS4;GINS3;GINS2","subunits.Gene.name.syn.":"KIAA0186 PSF1;SLD5;PSF3;PSF2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex stimulates DNA polymerase alpha-primase.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":679,"ComplexName":"Tis7-Sin3-Hdac1-Ncor1-Sap30 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O09106;O88574;P19182;Q60974;Q62141","subunits.Entrez.IDs.":"433759;60406;15982;20185;20467","Protein.complex.purification.method":"MI:0018- two hybrid; MI:0019- coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;organization of chromosome structure;nucleus","PubMed.ID":12198164,"subunits.Protein.name.":"Histone deacetylase 1;Histone deacetylase complex subunit SAP30 ;Interferon-related developmental regulator 1 ;Nuclear receptor corepressor 1 ;Paired amphipathic helix protein Sin3b","subunits.Gene.name.":"Hdac1;Sap30;Ifrd1;Ncor1;Sin3b","subunits.Gene.name.syn.":"None;;Tis7;Rxrip13;Kiaa0700","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":680,"ComplexName":"RANBMP-CD39 complex","Organism":"Human","Synonyms":"None","Cell.line":"lymphocyte","subunits.UniProt.IDs.":"P43487;P49961","subunits.Entrez.IDs.":"5902;953","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0030234;GO:0050790;GO:0005886","GO.description":"enzyme regulator activity;regulation of catalytic activity;plasma membrane","FunCat.ID":"18.02.01;70.02","FunCat.description":"enzymatic activity regulation / enzyme regulator;eukaryotic plasma membrane / membrane attached","PubMed.ID":16478441,"subunits.Protein.name.":"Ran-specific GTPase-activating protein;Ectonucleoside triphosphate diphosphohydrolase 1","subunits.Gene.name.":"RANBP1;ENTPD1","subunits.Gene.name.syn.":"None;CD39","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"NTPDase activity of recombinant CD39, but not of N-terminus-deleted-CD39 mutant, is substantially diminished by RanBPM co-expression in COS-7 cells.CD39 associations with RanBPM have the potential to regulate NTPDase catalytic activity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":681,"ComplexName":"(C-CFTR)2-NHERF-ezrin complex","Organism":"Human","Synonyms":"None","Cell.line":"epithelium","subunits.UniProt.IDs.":"O14745;P13569;P15311","subunits.Entrez.IDs.":"9368;1080;7430","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0067-light scattering;MI:0071-molecular sieving;MI:0107-surface plasmon resonance","GO.ID":"GO:0006821;GO:0005216;GO:0005886;GO:0005856","GO.description":"chloride transport;ion channel activity;plasma membrane;cytoskeleton","FunCat.ID":"20.01.01.07.09;20.03.01.01;70.02;70.04","FunCat.description":"chloride transport;ion channels;eukaryotic plasma membrane / membrane attached;cytoskeleton","PubMed.ID":16129695,"subunits.Protein.name.":"Na(+)/H(+) exchange regulatory cofactor NHE-RF1;Cystic fibrosis transmembrane conductance regulator;Ezrin","subunits.Gene.name.":"SLC9A3R1;CFTR;EZR","subunits.Gene.name.syn.":"NHERF, NHERF1;ABCC7;VIL2","Disease.comment":"CFTR is involved in cystic fibrosis (PMID:10811849).","Subunits.comment":"None","Complex.comment":"Ezrin is a regulator that can positively control the cooperative binding of NHERF with the cytoplasmic domains of CFTR, thus modulating the stoichiometry of C-CFTR to NHERF interaction. The regulation of NHERF by ezrin may be employed as a general mechanism to assemble channels and receptors in the membrane cytoskeleton.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":682,"ComplexName":"C-CFTR-NHERF(PDZ1 domain)-ezrin complex","Organism":"Human","Synonyms":"None","Cell.line":"epithelium","subunits.UniProt.IDs.":"O14745;P13569;P15311","subunits.Entrez.IDs.":"9368;1080;7430","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0067- light scattering;MI:0071- molecular sieving;MI:0107- surface plasmon resonance","GO.ID":"GO:0006821;GO:0005216;GO:0005886;GO:0005856","GO.description":"chloride transport;ion channel activity;plasma membrane;cytoskeleton","FunCat.ID":"20.01.01.07.09;20.03.01.01;70.02;70.04","FunCat.description":"chloride transport;ion channels;eukaryotic plasma membrane / membrane attached;cytoskeleton","PubMed.ID":16129695,"subunits.Protein.name.":"Na(+)/H(+) exchange regulatory cofactor NHE-RF1;Cystic fibrosis transmembrane conductance regulator;Ezrin","subunits.Gene.name.":"SLC9A3R1;CFTR;EZR","subunits.Gene.name.syn.":"NHERF, NHERF1;ABCC7;VIL2","Disease.comment":"CFTR is involved in cystic fibrosis (PMID:10811849).","Subunits.comment":"None","Complex.comment":"There are two types of 1:1:1 ternary complexes formed between C-CFTR and NHERF\\u00b7ezFERM. Gel filtration experiments show that the fraction eluted at 11.3 ml is a ternary complex with C-CFTR bound to the first PDZ domain of the binary NHERF\\u00b7ezFERM complex. Ezrin is a regulator that can positively control the cooperative binding of NHERF with the cytoplasmic domains of CFTR, thus modulating the stoichiometry of C-CFTR to NHERF interaction. The regulation of NHERF by ezrin may be employed as a general mechanism to assemble channels and receptors in the membrane cytoskeleton.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":683,"ComplexName":"C-CFTR-NHERF(PDZ2 domain)-ezrin complex","Organism":"Human","Synonyms":"None","Cell.line":"epithelium","subunits.UniProt.IDs.":"O14745;P13569;P15311","subunits.Entrez.IDs.":"9368;1080;7430","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0067- light scattering;MI:0071- molecular sieving;MI:0107- surface plasmon resonance","GO.ID":"GO:0006821;GO:0005216;GO:0005886;GO:0005856","GO.description":"chloride transport;ion channel activity;plasma membrane;cytoskeleton","FunCat.ID":"20.01.01.07.09;20.03.01.01;70.02;70.04","FunCat.description":"chloride transport;ion channels;eukaryotic plasma membrane / membrane attached;cytoskeleton","PubMed.ID":16129695,"subunits.Protein.name.":"Na(+)/H(+) exchange regulatory cofactor NHE-RF1;Cystic fibrosis transmembrane conductance regulator;Ezrin","subunits.Gene.name.":"SLC9A3R1;CFTR;EZR","subunits.Gene.name.syn.":"NHERF, NHERF1;ABCC7;VIL2","Disease.comment":"CFTR is involved in cystic fibrosis (PMID:10811849).","Subunits.comment":"None","Complex.comment":"There are two types of 1:1:1 ternary complexes formed between C-CFTR and NHERF\\u00b7ezFERM. Gel filtration experiments show that the fraction eluted at 11.9 ml is a ternary complex with C-CFTR bound to the second PDZ domain of the binary NHERF\\u00b7ezFERM complex. Ezrin is a regulator that can positively control the cooperative binding of NHERF with the cytoplasmic domains of CFTR, thus modulating the stoichiometry of C-CFTR to NHERF interaction. The regulation of NHERF by ezrin may be employed as a general mechanism to assemble channels and receptors in the membrane cytoskeleton.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":684,"ComplexName":"PAX9-MSX1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P28360;P55771","subunits.Entrez.IDs.":"4487;5083","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0018- two hybrid","GO.ID":"GO:2001141;GO:0006355;GO:0042476","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;odontogenesis","FunCat.ID":"11.02.03.04;41.05.12","FunCat.description":"transcriptional control;odontogenesis","PubMed.ID":15721141,"subunits.Protein.name.":"Homeobox protein MSX-1 ;Paired box protein Pax-9","subunits.Gene.name.":"MSX1;PAX9","subunits.Gene.name.syn.":"HOX7;","Disease.comment":"PAX9 is involved  in tooth agenesis. The results indicate a functional relationship between Pax9 and Msx1 during tooth development.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":685,"ComplexName":"MeCP1 complex","Organism":"Human","Synonyms":"Mi2/NuRD-MBD2 complex","Cell.line":"None","subunits.UniProt.IDs.":"O94776;O95983;Q09028;Q13547;Q14839;Q16576;Q8WXI9;Q92769;Q9UBB5","subunits.Entrez.IDs.":"9219;53615;5928;3065;1108;5931;57459;3066;8932","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0032774;GO:0006473;GO:0006476;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;RNA biosynthetic process;protein acetylation;protein deacetylation;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;11.02;14.07.04;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;RNA synthesis;modification by acetylation, deacetylation;DNA binding;organization of chromosome structure;nucleus","PubMed.ID":11756549,"subunits.Protein.name.":"Metastasis-associated protein MTA2;Methyl-CpG-binding domain protein 3;Histone-binding protein RBBP4;Histone deacetylase 1;Chromodomain-helicase-DNA-binding protein 4;Histone-binding protein RBBP7;Transcriptional repressor p66-beta ;Histone deacetylase 2;Methyl-CpG-binding domain protein 2","subunits.Gene.name.":"MTA2;MBD3;RBBP4;HDAC1;CHD4;RBBP7;GATAD2B;HDAC2;MBD2","subunits.Gene.name.syn.":"MTA1L1 PID;None;RBAP48;RPD3L1;None;RBAP46;KIAA1150;None;None","Disease.comment":"CHD4 is involved in dermatomyositis (PMID:9790534).","Subunits.comment":"None","Complex.comment":"MeCP1 protein complex represses transcription through preferential binding, remodeling, and deacetylation of methylated nucleosomes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":686,"ComplexName":"Apg16L-Apg12-Apg5 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q8C0J2;Q99J83;Q9CQY1","subunits.Entrez.IDs.":"77040;11793;67526","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0069- mass spectrometry studies of complexes; MI:0018- two hybrid; MI:0004- affinity chromatography technologies","GO.ID":"GO:0007039","GO.description":"protein catabolic process in the vacuole","FunCat.ID":"14.13.04.02","FunCat.description":"vacuolar protein degradation","PubMed.ID":12665549,"subunits.Protein.name.":"Autophagy-related protein 16-1 ;Autophagy protein 5 ;Ubiquitin-like protein ATG12","subunits.Gene.name.":"Atg16l1;Atg5;Atg12","subunits.Gene.name.syn.":"Apg16l;Apg5l;Apg12 Apg12l","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In conjunction with Apg12-Apg5, Apg16L associates with the autophagic isolation membrane for the duration of autophagosome formation.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":687,"ComplexName":"CFTR-NHERF-beta(2)AR signaling complex","Organism":"Human","Synonyms":"None","Cell.line":"epithelium","subunits.UniProt.IDs.":"O14745;P07550;P13569","subunits.Entrez.IDs.":"9368;154;1080","Protein.complex.purification.method":"MI:0096- pull down;MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006821;GO:0005216;GO:0023052;GO:0005886","GO.description":"chloride transport;ion channel activity;signaling;plasma membrane","FunCat.ID":"20.01.01.07.09;20.03.01.01;30.01;70.02","FunCat.description":"chloride transport;ion channels;cellular signalling;eukaryotic plasma membrane / membrane attached","PubMed.ID":12502786,"subunits.Protein.name.":"Na(+)/H(+) exchange regulatory cofactor NHE-RF1;Beta-2 adrenergic receptor;Cystic fibrosis transmembrane conductance regulator","subunits.Gene.name.":"SLC9A3R1;ADRB2;CFTR","subunits.Gene.name.syn.":"NHERF, NHERF1;ADRB2R B2AR;ABCC7","Disease.comment":"CFTR is involved in cystic fibrosis (PMID:10811849).","Subunits.comment":"None","Complex.comment":"The results indicate that PDZ-based interactions with ezrin/radixin/moesin-binding phosphoprotein 50 (EBP50) govern both physical and functional regulation of CFTR by beta (2) AR. Assembly of the complex is regulated by PKA-dependent phosphorylation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":688,"ComplexName":"Cd2ap-Fyn complex","Organism":"Mouse","Synonyms":"None","Cell.line":"kidney","subunits.UniProt.IDs.":"P39688;Q9JLQ0","subunits.Entrez.IDs.":"14360;12488","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005515","GO.description":"protein binding","FunCat.ID":"16.01","FunCat.description":"protein binding","PubMed.ID":16628251,"subunits.Protein.name.":"Tyrosine-protein kinase Fyn;CD2-associated protein","subunits.Gene.name.":"Fyn;Cd2ap","subunits.Gene.name.syn.":"None;Mets1","Disease.comment":"Combinations of Cd2ap heterozygosity and heterozygosity Fyn proto-oncogene (Fyn) but not kin of IRRE like 1 (Neph1) resulted in spontaneous proteinuria and in FSGS-like glomerular damage.","Subunits.comment":"None","Complex.comment":"CD2AP associates with Fyn and Synpo but not with Neph1.The association of Fyn with CD2AP is probably mediated by the SH3 domain of Fyn binding to proline sequences in CD2AP.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":690,"ComplexName":"Cd2ap-Synpo complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q8CC35;Q9JLQ0","subunits.Entrez.IDs.":"104027;12488","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0005515;GO:0007010","GO.description":"protein binding;cytoskeleton organization","FunCat.ID":"16.01;42.04","FunCat.description":"protein binding;cytoskeleton/structural proteins","PubMed.ID":16628251,"subunits.Protein.name.":"Synaptopodin;CD2-associated protein","subunits.Gene.name.":"Synpo;Cd2ap","subunits.Gene.name.syn.":"Kiaa1029;Mets1","Disease.comment":"Combinations of Cd2ap heterozygosity and heterozygosity of synaptopodin (Synpo) but not kind of IRRE like 1 (Neph1) resulted in spontaneous proteinuria and in FSGS-like glomerular damage .","Subunits.comment":"None","Complex.comment":"The interaction between CD2AP and Synpo reinforces the idea that CD2AP plays a central role in regulating the actin cytoskeleton. CD2AP associates with Fyn and Synpo but not with Neph1.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":691,"ComplexName":"SIN3-SAP25 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00422;O75446;Q09028;Q13547;Q16576;Q1EHW4;Q4LE39;Q92769;Q96ST3;Q9H0E3;Q9H7L9","subunits.Entrez.IDs.":"10284;8819;5928;3065;5931;751865;51742;3066;25942;79595;64426","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0005515;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;protein binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;16.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;protein binding;organization of chromosome structure;nucleus","PubMed.ID":16449650,"subunits.Protein.name.":"Histone deacetylase complex subunit SAP18;Histone deacetylase complex subunit SAP30;Histone-binding protein RBBP4;Histone deacetylase 1;Histone-binding protein RBBP7;Histone deacetylase complex subunit SAP25 ;AT-rich interactive domain-containing protein 4B ;Histone deacetylase 2;Paired amphipathic helix protein Sin3a;Histone deacetylase complex subunit SAP130;Sin3 histone deacetylase corepressor complex component SDS3","subunits.Gene.name.":"SAP18;SAP30;RBBP4;HDAC1;RBBP7;Sap25;ARID4B;HDAC2;SIN3A;SAP130;SUDS3","subunits.Gene.name.syn.":"None;None;RBAP48;RPD3L1;RBAP46;;BRCAA1 RBBP1L1 RBP1L1 SAP180;None;None;None;SAP45 SDS3","Disease.comment":"None","Subunits.comment":"Since human SAP25 was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Mus musculus (Mouse);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":692,"ComplexName":"LysRS-Hint-Mitf complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O88368;P62959;Q5XIM7","subunits.Entrez.IDs.":"25094;690660;292028","Protein.complex.purification.method":"MI:0091- chromatography technologies","GO.ID":"GO:2001141;GO:0006355;GO:0005515","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein binding","FunCat.ID":"11.02.03.04;16.01","FunCat.description":"transcriptional control;protein binding","PubMed.ID":14975237,"subunits.Protein.name.":"Microphthalmia-associated transcription factor ;Histidine triad nucleotide-binding protein 1 ;Lysine--tRNA ligase","subunits.Gene.name.":"Mitf;Hint1;Kars","subunits.Gene.name.syn.":";Hint Pkci1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"LysRS can play a key role via Ap4A as an important signaling molecule in MITF transcriptional activity.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":693,"ComplexName":"TOM complex (Tom20, Tom22, Tom70), mitochondrial","Organism":"Rat","Synonyms":"TOM (Tomm20, Tomm22, Tomm70) complex, mitochondrial","Cell.line":"None","subunits.UniProt.IDs.":"Q62760;Q75Q39;Q75Q41","subunits.Entrez.IDs.":"266601;304017;300075","Protein.complex.purification.method":"MI:0018-two hybrid;MI:0019-coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0005741;GO:0005739","GO.description":"intracellular protein transport;protein targeting;protein transport;mitochondrial outer membrane;mitochondrion","FunCat.ID":"14.04;20.01.10;70.16.01;70.16","FunCat.description":"protein targeting, sorting and translocation;protein transport;mitochondrial outer membrane;mitochondrion","PubMed.ID":11956321,"subunits.Protein.name.":"Mitochondrial import receptor subunit TOM20 homolog;Mitochondrial import receptor subunit TOM70;Mitochondrial import receptor subunit TOM22 homolog","subunits.Gene.name.":"Tomm20;Tomm70;Tomm22","subunits.Gene.name.syn.":"None;Tomm70a;Tom22","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Translocation of nuclear-encoded mitochondrial preproteins is mediated by translocases in the outer (TOM) and inner (TIM) membranes.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":694,"ComplexName":"Bad-Gk-Wave1-Pkaca-Ppp1cc complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P05132;P52792;Q3U7K1;Q3U9H3;Q8R5H6","subunits.Entrez.IDs.":"18747;103988;19047;12015;83767","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006111;GO:0006110;GO:0006915;GO:0005739","GO.description":"regulation of gluconeogenesis;regulation of glycolytic process;apoptotic process;mitochondrion","FunCat.ID":"02.01.03;40.10.02;70.16","FunCat.description":"regulation of glycolysis and gluconeogenesis;apoptosis (type I programmed cell death);mitochondrion","PubMed.ID":12931191,"subunits.Protein.name.":"cAMP-dependent protein kinase catalytic subunit alpha ;Glucokinase ;Serine/threonine-protein phosphatase ;Bcl-associated death promoter, isoform CRA_a ;Wiskott-Aldrich syndrome protein family member 1","subunits.Gene.name.":"Prkaca;Gck;;Bad;Wasf1","subunits.Gene.name.syn.":"Pkaca;Gk;;;Wave1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":695,"ComplexName":"SIN3-HDAC-SAP30-ARID4 complex","Organism":"Human","Synonyms":"mSin3A corepressor complex","Cell.line":"None","subunits.UniProt.IDs.":"O75446;Q09028;Q13547;Q16576;Q4LE39;Q92769;Q96ST3","subunits.Entrez.IDs.":"8819;5928;3065;5931;51742;3066;25942","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0005515;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;protein binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;16.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;protein binding;organization of chromosome structure;nucleus","PubMed.ID":12724404,"subunits.Protein.name.":"Histone deacetylase complex subunit SAP30;Histone-binding protein RBBP4;Histone deacetylase 1;Histone-binding protein RBBP7;AT-rich interactive domain-containing protein 4B ;Histone deacetylase 2;Paired amphipathic helix protein Sin3a","subunits.Gene.name.":"SAP30;RBBP4;HDAC1;RBBP7;ARID4B;HDAC2;SIN3A","subunits.Gene.name.syn.":"None;RBAP48;RPD3L1;RBAP46;BRCAA1 RBBP1L1 RBP1L1 SAP180;None;None","Disease.comment":"None","Subunits.comment":"Another subunit of the complex was found in the analysis, which has not been further characterized: SAP250.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":696,"ComplexName":"BRMS1-SIN3-HDAC complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75182;O75446;Q09028;Q13547;Q16576;Q92769;Q96ST3;Q9HCU9","subunits.Entrez.IDs.":"23309;8819;5928;3065;5931;3066;25942;25855","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;organization of chromosome structure;nucleus","PubMed.ID":14581478,"subunits.Protein.name.":"Paired amphipathic helix protein Sin3b;Histone deacetylase complex subunit SAP30;Histone-binding protein RBBP4;Histone deacetylase 1;Histone-binding protein RBBP7;Histone deacetylase 2;Paired amphipathic helix protein Sin3a;Breast cancer metastasis-suppressor 1","subunits.Gene.name.":"SIN3B;SAP30;RBBP4;HDAC1;RBBP7;HDAC2;SIN3A;BRMS1","subunits.Gene.name.syn.":"KIAA0700;None;RBAP48;RPD3L1;RBAP46;None;None;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"BRMS1 may participate in transcriptional regulation via interaction with the Sin3-HDAC complex and suggest a novel mechanism by which BRMS1 might suppress cancer metastasis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":697,"ComplexName":"BRMS1-RBP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q4LE39;Q9HCU9","subunits.Entrez.IDs.":"51742;25855","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045892;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;nucleus","FunCat.ID":"11.02.03.04.03;70.10","FunCat.description":"transcription repression;nucleus","PubMed.ID":14581478,"subunits.Protein.name.":"AT-rich interactive domain-containing protein 4B ;Breast cancer metastasis-suppressor 1","subunits.Gene.name.":"ARID4B;BRMS1","subunits.Gene.name.syn.":"BRCAA1 RBBP1L1 RBP1L1 SAP180;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"BRMS1 may participate in transcriptional regulation via interaction with the mSin3.HDAC complex and suggest a novel mechanism by which BRMS1 might suppress cancer metastasis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":698,"ComplexName":"SIN3-HDAC-SAP30-ARID4 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75446;Q09028;Q13547;Q16576;Q4LE39;Q92769;Q96ST3","subunits.Entrez.IDs.":"8819;5928;3065;5931;51742;3066;25942","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;organization of chromosome structure;nucleus","PubMed.ID":9702189,"subunits.Protein.name.":"Histone deacetylase complex subunit SAP30;Histone-binding protein RBBP4;Histone deacetylase 1;Histone-binding protein RBBP7;AT-rich interactive domain-containing protein 4B ;Histone deacetylase 2;Paired amphipathic helix protein Sin3a","subunits.Gene.name.":"SAP30;RBBP4;HDAC1;RBBP7;ARID4B;HDAC2;SIN3A","subunits.Gene.name.syn.":"None;RBAP48;RPD3L1;RBAP46;BRCAA1 RBBP1L1 RBP1L1 SAP180;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SAP30 is involved in the functional recruitment of the mSin3-histone deacetylase complex to a specific subset of N-CoR corepressor complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":700,"ComplexName":"Snap25-caveolin complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain hippocampal homogenate","subunits.UniProt.IDs.":"P41350;P60881","subunits.Entrez.IDs.":"25404;25012","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0416- fluorescence microscopy","GO.ID":"GO:0007268","GO.description":"synaptic transmission","FunCat.ID":"34.03.01","FunCat.description":"synaptic transmission","PubMed.ID":10934248,"subunits.Protein.name.":"Caveolin-1;Synaptosomal-associated protein 25","subunits.Gene.name.":"Cav1;Snap25","subunits.Gene.name.syn.":"Cav;Snap","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"A short-lasting SNAP25-caveolin interaction may be involved in the early phase of synaptic potentiation.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":701,"ComplexName":"HuR-Tia1-Tiar-Hrnpu complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"B5DF91;Q5BJN3;Q5PQR7;Q6IMY8","subunits.Entrez.IDs.":"363854;361655;312510;117280","Protein.complex.purification.method":"MI:0412- electrophoretic mobility supershift assay; MI:0019- coimmunoprecipitation","GO.ID":"GO:0032774;GO:0003723","GO.description":"RNA biosynthetic process;RNA binding","FunCat.ID":"11.02;16.03.03","FunCat.description":"RNA synthesis;RNA binding","PubMed.ID":12855701,"subunits.Protein.name.":"ELAV-like protein 1 ;Protein Tial1 ;Protein Tia1 ;Heterogeneous nuclear ribonucleoprotein U","subunits.Gene.name.":"Elavl1;Tial1;Tia1;Hnrnpu","subunits.Gene.name.syn.":"Hur;Tial1_mapped;;Hnrpu","Disease.comment":"None","Subunits.comment":"Since Elavl1 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"HuR, TIA-1, TIAR, and hnRNP U bind the first 60 nucleotides of the 3'-UTR of murine COX-2.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":702,"ComplexName":"ARD1-NATH complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P36406;Q9BXJ9","subunits.Entrez.IDs.":"373;80155","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0051- fluorescence technologies","GO.ID":"GO:0006417;GO:0005515;GO:0005634","GO.description":"regulation of translation;protein binding;nucleus","FunCat.ID":"12.07;16.01;70.10","FunCat.description":"translational control;protein binding;nucleus","PubMed.ID":15496142,"subunits.Protein.name.":"E3 ubiquitin-protein ligase TRIM23 ;N-alpha-acetyltransferase 15, NatA auxiliary subunit","subunits.Gene.name.":"TRIM23;NAA15","subunits.Gene.name.syn.":"ARD1 ARFD1 RNF46;GA19 NARG1 NATH TBDN100","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":703,"ComplexName":"SNARE complex (Vamp7, Stx5, Bet1, Vti1a)","Organism":"Rat","Synonyms":"PCTV-cis-Golgi SNARE-complex","Cell.line":"None","subunits.UniProt.IDs.":"Q08851;Q62896;Q9JHW5;Q9JI51","subunits.Entrez.IDs.":"65134;29631;85491;65277","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006888;GO:0006906;GO:0048489;GO:0016079","GO.description":"ER to Golgi vesicle-mediated transport;vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.03;20.09.07.27;20.09.16.09.05","FunCat.description":"ER to Golgi transport;vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":16735505,"subunits.Protein.name.":"Syntaxin-5;BET1 homolog;Vesicle-associated membrane protein 7 ;Vesicle transport through interaction with t-SNAREs homolog 1A","subunits.Gene.name.":"Stx5;Bet1;Vamp7;Vti1a","subunits.Gene.name.syn.":"Stx5a;None;Sybl1;Vti1l2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":704,"ComplexName":"SNARE complex (RINT1, ZW10, p31, Stx18)","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43264;P48556;Q68FW4;Q6NUQ1","subunits.Entrez.IDs.":"9183;5714;360953;60561","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0000278;GO:0051726;GO:0006888;GO:0006906;GO:0048489;GO:0016079;GO:0005783","GO.description":"mitotic cell cycle;regulation of cell cycle;ER to Golgi vesicle-mediated transport;vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis;endoplasmic reticulum","FunCat.ID":"10.03.01.01;10.03.01;20.09.07.03;20.09.07.27;20.09.16.09.05;70.07","FunCat.description":"mitotic cell cycle;mitotic cell cycle and cell cycle control;ER to Golgi transport;vesicle fusion;synaptic vesicle exocytosis;endoplasmic reticulum","PubMed.ID":15029241,"subunits.Protein.name.":"Centromere/kinetochore protein zw10 homolog;26S proteasome non-ATPase regulatory subunit 8 ;Syntaxin-18;RAD50-interacting protein 1","subunits.Gene.name.":"ZW10;PSMD8;Stx18;RINT1","subunits.Gene.name.syn.":";;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway. ZW10 is known to participate directly in turning off the spindle checkpoint.  The present results display an unexpected role  in membrane trafficking between ER and Golgi during interphase.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Rattus norvegicus (Rat);Homo sapiens (Human)"}
{"ComplexID":705,"ComplexName":"SNARE complex (RINT1, ZW10, p31)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43264;P48556;Q6NUQ1","subunits.Entrez.IDs.":"9183;5714;60561","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0000278;GO:0051726;GO:0006888;GO:0006906;GO:0048489;GO:0016079;GO:0005783","GO.description":"mitotic cell cycle;regulation of cell cycle;ER to Golgi vesicle-mediated transport;vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis;endoplasmic reticulum","FunCat.ID":"10.03.01.01;10.03.01;20.09.07.03;20.09.07.27;20.09.16.09.05;70.07","FunCat.description":"mitotic cell cycle;mitotic cell cycle and cell cycle control;ER to Golgi transport;vesicle fusion;synaptic vesicle exocytosis;endoplasmic reticulum","PubMed.ID":15029241,"subunits.Protein.name.":"Centromere/kinetochore protein zw10 homolog;26S proteasome non-ATPase regulatory subunit 8 ;RAD50-interacting protein 1","subunits.Gene.name.":"ZW10;PSMD8;RINT1","subunits.Gene.name.syn.":";;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway. ZW10 is known to participate directly in turning off the spindle checkpoint.  The present results display an unexpected role  in membrane trafficking between ER and Golgi during interphase.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":706,"ComplexName":"SNARE complex (HGS, SNAP25, STX13)","Organism":"Human","Synonyms":"HGS-containing complex","Cell.line":"None","subunits.UniProt.IDs.":"O14964;P60880;Q86Y82","subunits.Entrez.IDs.":"9146;6616;23673","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0006906;GO:0048489;GO:0016079;GO:0005768","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis;endosome","FunCat.ID":"20.09.07.27;20.09.16.09.05;70.22","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis;endosome","PubMed.ID":14769786,"subunits.Protein.name.":"Hepatocyte growth factor-regulated tyrosine kinase substrate;Synaptosomal-associated protein 25 ;Syntaxin-12","subunits.Gene.name.":"HGS;SNAP25;STX12","subunits.Gene.name.syn.":"HRS;SNAP;","Disease.comment":"None","Subunits.comment":"STX12 and STX13 are identical (see GeneID:23673): STX12 syntaxin 12 (Homo sapiens) Also known as STX13; STX14; MGC51957.","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":707,"ComplexName":"SNARE complex (VAMP2, SNAP25, STX13)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P60880;P63027;Q86Y82","subunits.Entrez.IDs.":"6616;6844;23673","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":14769786,"subunits.Protein.name.":"Synaptosomal-associated protein 25 ;Vesicle-associated membrane protein 2 ;Syntaxin-12","subunits.Gene.name.":"SNAP25;VAMP2;STX12","subunits.Gene.name.syn.":"SNAP;SYB2;","Disease.comment":"None","Subunits.comment":"STX12 and STX13 are identical (see GeneID:23673): STX12 syntaxin 12 (Homo sapiens) Also known as STX13; STX14; MGC51957.","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":709,"ComplexName":"cGMP kinase signaling complex (IP3RI, IRAG, cGKI-beta)","Organism":"Bovine","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P00516;Q9N1F0;Q9TU34","subunits.Entrez.IDs.":"282004;281918;317697","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0019- coimmunoprecipitation","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0008324;GO:0006812;GO:0019933;GO:0006875;GO:0006939","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;cation transmembrane transporter activity;cation transport;cAMP-mediated signaling;cellular metal ion homeostasis;smooth muscle contraction","FunCat.ID":"14.07.03;20.01.01.01;30.01.09.07;34.01.01.01;36.25.09.01","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);cAMP/cGMP mediated signal transduction;homeostasis of metal ions (Na, K, Ca etc.);smooth muscle contraction","PubMed.ID":10724174,"subunits.Protein.name.":"cGMP-dependent protein kinase 1 ;Protein MRVI1 ;Inositol 1,4,5-trisphosphate receptor type 1","subunits.Gene.name.":"PRKG1;MRVI1;ITPR1","subunits.Gene.name.syn.":"PRKG1B PRKGR1A PRKGR1B;IRAG;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results identify IRAG as an essential NO/cGKI-dependent regulator of IP3-induced calcium release.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":710,"ComplexName":"Brg1-associated complex I","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14497;O14744;O96019;P51532;Q12824;Q8TAQ2;Q92922;Q969G3;Q96GM5","subunits.Entrez.IDs.":"8289;10419;86;6597;6598;6601;6599;6605;6602","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation;MI:0029-cosedimentation through density gradients","GO.ID":"GO:0006265;GO:2001141;GO:0006355;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcriptional control;DNA binding;organization of chromosome structure;nucleus","PubMed.ID":11238380,"subunits.Protein.name.":"AT-rich interactive domain-containing protein 1A;Protein arginine N-methyltransferase 5;Actin-like protein 6A;Transcription activator BRG1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;SWI/SNF complex subunit SMARCC2;SWI/SNF complex subunit SMARCC1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","subunits.Gene.name.":"ARID1A;PRMT5;ACTL6A;SMARCA4;SMARCB1;SMARCC2;SMARCC1;SMARCE1;SMARCD1","subunits.Gene.name.syn.":"BAF250 BAF250A C1orf4 OSA1 SMARCF1;HRMT1L5 IBP72 JBP1 SKB1;BAF53 BAF53A INO80K;BAF190A BRG1 SNF2B SNF2L4;BAF47, INI1, SNF5L1;BAF170;BAF155;BAF57;BAF60A","Disease.comment":"None","Subunits.comment":"In a following paper (PMID:14559996) p66 has been identified as PRMT5. Since the authors did not specify SMARCD, we used isoform SMARCD1.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":711,"ComplexName":"Brm-associated complex","Organism":"Human","Synonyms":"BRM containing SWI/SNF remodeling complex","Cell.line":"None","subunits.UniProt.IDs.":"O14497;O14744;O96019;P51531;Q12824;Q8TAQ2;Q92922;Q969G3;Q96GM5","subunits.Entrez.IDs.":"8289;10419;86;6595;6598;6601;6599;6605;6602","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation;MI:0029-cosedimentation through density gradients","GO.ID":"GO:0006265;GO:2001141;GO:0006355;GO:0018126;GO:0006479;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein hydroxylation;protein methylation;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04;14.07.09;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcriptional control;posttranslational modification of amino acids (e.g. hydroxylation, methylation);DNA binding;organization of chromosome structure;nucleus","PubMed.ID":11238380,"subunits.Protein.name.":"AT-rich interactive domain-containing protein 1A;Protein arginine N-methyltransferase 5;Actin-like protein 6A;Probable global transcription activator SNF2L2;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;SWI/SNF complex subunit SMARCC2;SWI/SNF complex subunit SMARCC1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","subunits.Gene.name.":"ARID1A;PRMT5;ACTL6A;SMARCA2;SMARCB1;SMARCC2;SMARCC1;SMARCE1;SMARCD1","subunits.Gene.name.syn.":"BAF250 BAF250A C1orf4 OSA1 SMARCF1;HRMT1L5 IBP72 JBP1 SKB1;BAF53 BAF53A INO80K;BAF190B, BRM, SNF2A, SNF2L2;BAF47, INI1, SNF5L1;BAF170;BAF155;BAF57;BAF60A","Disease.comment":"None","Subunits.comment":"In a following paper (PMID:14559996) p66 has been identified as PRMT5. Since the authors did not specify SMARCD, we used isoform SMARCD1.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":712,"ComplexName":"cGMP kinase signaling complex (IP3RI, IRAG, cGKI-beta, alpha-actin, calponin H1, PLN, RhoA)","Organism":"Bovine","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P00516;P61014;P61585;P62739;Q2HJ38;Q9N1F0;Q9TU34","subunits.Entrez.IDs.":"282004;18821;338049;515610;534583;281918;317697","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0008324;GO:0006812;GO:0019933;GO:0006875;GO:0006939;GO:0005783","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;cation transmembrane transporter activity;cation transport;cAMP-mediated signaling;cellular metal ion homeostasis;smooth muscle contraction;endoplasmic reticulum","FunCat.ID":"14.07.03;20.01.01.01;30.01.09.07;34.01.01.01;36.25.09.01;70.07","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);cAMP/cGMP mediated signal transduction;homeostasis of metal ions (Na, K, Ca etc.);smooth muscle contraction;endoplasmic reticulum","PubMed.ID":12480535,"subunits.Protein.name.":"cGMP-dependent protein kinase 1 ;Cardiac phospholamban ;Transforming protein RhoA ;Actin, aortic smooth muscle ;Calponin-1 ;Protein MRVI1 ;Inositol 1,4,5-trisphosphate receptor type 1","subunits.Gene.name.":"PRKG1;Pln;RHOA;ACTA2;CNN1;MRVI1;ITPR1","subunits.Gene.name.syn.":"PRKG1B PRKGR1A PRKGR1B;;ARHA RHO12;ACTSA ACTVS;;IRAG;","Disease.comment":"None","Subunits.comment":"Since bovine PLN was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"The results suggest that PLB may have additional functions to regulate the activity of the Calcium-transporting ATPase  SERCA II.","SWISSPROT.organism":"Bos taurus (Bovine);Mus musculus (Mouse);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":713,"ComplexName":"BRG1-SIN3A complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14497;O14744;O96019;P51532;Q09028;Q12824;Q6STE5;Q8TAQ2;Q92769;Q92922;Q92925;Q969G3;Q96GM5;Q96ST3","subunits.Entrez.IDs.":"8289;10419;86;6597;5928;6598;6604;6601;3066;6599;6603;6605;6602;25942","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006265;GO:0045892;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;DNA binding;organization of chromosome structure;nucleus","PubMed.ID":11238380,"subunits.Protein.name.":"AT-rich interactive domain-containing protein 1A;Protein arginine N-methyltransferase 5;Actin-like protein 6A;Transcription activator BRG1;Histone-binding protein RBBP4;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3;SWI/SNF complex subunit SMARCC2;Histone deacetylase 2;SWI/SNF complex subunit SMARCC1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1;Paired amphipathic helix protein Sin3a","subunits.Gene.name.":"ARID1A;PRMT5;ACTL6A;SMARCA4;RBBP4;SMARCB1;SMARCD3;SMARCC2;HDAC2;SMARCC1;SMARCD2;SMARCE1;SMARCD1;SIN3A","subunits.Gene.name.syn.":"BAF250 BAF250A C1orf4 OSA1 SMARCF1;HRMT1L5 IBP72 JBP1 SKB1;BAF53 BAF53A INO80K;BAF190A BRG1 SNF2B SNF2L4;RBAP48;BAF47, INI1, SNF5L1;BAF60C;BAF170;None;BAF155;BAF60B;BAF57;BAF60A;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Components of the Sin3 complex cofractionate with BRG1-associated complex I, but not with BRG1-associated complex II.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":714,"ComplexName":"BRM-SIN3A complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14497;O14744;O96019;P51531;Q09028;Q12824;Q13547;Q6STE5;Q8TAQ2;Q92769;Q92922;Q92925;Q969G3;Q96GM5;Q96ST3","subunits.Entrez.IDs.":"8289;10419;86;6595;5928;6598;3065;6604;6601;3066;6599;6603;6605;6602;25942","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006265;GO:0045892;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;DNA binding;organization of chromosome structure;nucleus","PubMed.ID":11238380,"subunits.Protein.name.":"AT-rich interactive domain-containing protein 1A;Protein arginine N-methyltransferase 5;Actin-like protein 6A;Probable global transcription activator SNF2L2;Histone-binding protein RBBP4;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;Histone deacetylase 1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3;SWI/SNF complex subunit SMARCC2;Histone deacetylase 2;SWI/SNF complex subunit SMARCC1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1;Paired amphipathic helix protein Sin3a","subunits.Gene.name.":"ARID1A;PRMT5;ACTL6A;SMARCA2;RBBP4;SMARCB1;HDAC1;SMARCD3;SMARCC2;HDAC2;SMARCC1;SMARCD2;SMARCE1;SMARCD1;SIN3A","subunits.Gene.name.syn.":"BAF250 BAF250A C1orf4 OSA1 SMARCF1;HRMT1L5 IBP72 JBP1 SKB1;BAF53 BAF53A INO80K;BAF190B, BRM, SNF2A, SNF2L2;RBAP48;BAF47, INI1, SNF5L1;RPD3L1;BAF60C;BAF170;None;BAF155;BAF60B;BAF57;BAF60A;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Components of the Sin3 complex cofractionate with BRM-associated complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":716,"ComplexName":"PU.1-associated protein complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P09405;P17433;P31809;P70696;Q9Z2D6","subunits.Entrez.IDs.":"17975;20375;26365;319177;17257","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04;16.03.01;70.10","FunCat.description":"transcriptional control;DNA binding;nucleus","PubMed.ID":14647463,"subunits.Protein.name.":"Nucleolin;Transcription factor PU.1 ;Carcinoembryonic antigen-related cell adhesion molecule 1 ;Histone H2B type 1-A ;Methyl-CpG-binding protein 2","subunits.Gene.name.":"Ncl;Spi1;Ceacam1;Hist1h2ba;Mecp2","subunits.Gene.name.syn.":"Nuc;Sfpi-1 Sfpi1;Bgp Bgp1;Th2b;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":717,"ComplexName":"PU.1-Sin3A-Hdac-MeCP2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O09106;P17433;Q60520;Q9Z2D6","subunits.Entrez.IDs.":"433759;20375;20466;17257","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0003677;GO:0051276;GO:0030218;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;DNA binding;chromosome organization;erythrocyte differentiation;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;16.03.01;42.10.03;43.03.07;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;DNA binding;organization of chromosome structure;blood cell;nucleus","PubMed.ID":14647463,"subunits.Protein.name.":"Histone deacetylase 1;Transcription factor PU.1 ;Paired amphipathic helix protein Sin3a;Methyl-CpG-binding protein 2","subunits.Gene.name.":"Hdac1;Spi1;Sin3a;Mecp2","subunits.Gene.name.syn.":"None;Sfpi-1 Sfpi1;Kiaa4126;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors suggest that MeCP2 acts as a corepressor of PU.1 probably due to facilitating complex formation with mSin3A and HDACs.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":718,"ComplexName":"TRPV5-S100A10-annexin 2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"epithelium","subunits.UniProt.IDs.":"P07356;P08207;P69744","subunits.Entrez.IDs.":"12306;20194;194352","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies;MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0050789;GO:0008324;GO:0006812;GO:0005216;GO:0005886","GO.description":"intracellular protein transport;protein targeting;protein transport;regulation of biological process;cation transmembrane transporter activity;cation transport;ion channel activity;plasma membrane","FunCat.ID":"14.04;20.01.10;18;20.01.01.01;20.03.01.01;70.02","FunCat.description":"protein targeting, sorting and translocation;protein transport;REGULATION OF METABOLISM AND PROTEIN FUNCTION;cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;eukaryotic plasma membrane / membrane attached","PubMed.ID":12660155,"subunits.Protein.name.":"Annexin A2;Protein S100-A10 ;Transient receptor potential cation channel subfamily V member 5","subunits.Gene.name.":"Anxa2;S100a10;Trpv5","subunits.Gene.name.syn.":"Anx2, Cal1h;Cal1l;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Downregulation of annexin 2  inhibited TRPV5 and TRPV6-mediated currents in transfected HEK293 cells.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":719,"ComplexName":"S100A10-annexin 2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P07356;P08207","subunits.Entrez.IDs.":"12306;20194","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0005509;GO:0050789","GO.description":"intracellular protein transport;protein targeting;protein transport;calcium ion binding;regulation of biological process","FunCat.ID":"14.04;20.01.10;16.17.01;18","FunCat.description":"protein targeting, sorting and translocation;protein transport;calcium binding;REGULATION OF METABOLISM AND PROTEIN FUNCTION","PubMed.ID":12660155,"subunits.Protein.name.":"Annexin A2;Protein S100-A10","subunits.Gene.name.":"Anxa2;S100a10","subunits.Gene.name.syn.":"Anx2, Cal1h;Cal1l","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":720,"ComplexName":"PU.1-SIN3A-HDAC complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P17947;Q13547;Q96ST3","subunits.Entrez.IDs.":"6688;3065;25942","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;DNA binding;organization of chromosome structure;nucleus","PubMed.ID":11593411,"subunits.Protein.name.":"Transcription factor PU.1 ;Histone deacetylase 1;Paired amphipathic helix protein Sin3a","subunits.Gene.name.":"SPI1;HDAC1;SIN3A","subunits.Gene.name.syn.":";RPD3L1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":721,"ComplexName":"PU.1-TBP complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P17947;P20226","subunits.Entrez.IDs.":"6688;6908","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045892;GO:0003677;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04.03;16.03.01;70.10","FunCat.description":"transcription repression;DNA binding;nucleus","PubMed.ID":14647463,"subunits.Protein.name.":"Transcription factor PU.1 ;TATA-box-binding protein","subunits.Gene.name.":"SPI1;TBP","subunits.Gene.name.syn.":";GTF2D1 TF2D TFIID","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":722,"ComplexName":"MRG15-PAM14-RB complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06400;Q9UBU8;Q9Y605","subunits.Entrez.IDs.":"5925;10933;93621","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0045893;GO:0007569;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;cell aging;nucleus","FunCat.ID":"11.02.03.04.01;40.20;70.10","FunCat.description":"transcription activation;cell aging;nucleus","PubMed.ID":11500496,"subunits.Protein.name.":"Retinoblastoma-associated protein ;Mortality factor 4-like protein 1;MORF4 family-associated protein 1","subunits.Gene.name.":"RB1;MORF4L1;MRFAP1","subunits.Gene.name.syn.":";MRG15;PAM14 PGR1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"MRG15 blocks the RB-induced repression of this promotor, leading to transcription activation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":723,"ComplexName":"MAF1 complex","Organism":"Human","Synonyms":"MRG15-associated factors 1","Cell.line":"None","subunits.UniProt.IDs.":"P06400;Q9UBU8;Q9Y605","subunits.Entrez.IDs.":"5925;10933;93621","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0045893;GO:0007569;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;cell aging;nucleus","FunCat.ID":"11.02.03.04.01;40.20;70.10","FunCat.description":"transcription activation;cell aging;nucleus","PubMed.ID":12397079,"subunits.Protein.name.":"Retinoblastoma-associated protein ;Mortality factor 4-like protein 1;MORF4 family-associated protein 1","subunits.Gene.name.":"RB1;MORF4L1;MRFAP1","subunits.Gene.name.syn.":";MRG15;PAM14 PGR1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":724,"ComplexName":"MAF2 complex","Organism":"Human","Synonyms":"MRG15-associated factors 2","Cell.line":"None","subunits.UniProt.IDs.":"Q9H7Z6;Q9UBU8","subunits.Entrez.IDs.":"84148;10933","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0045893;GO:0006473;GO:0006476;GO:0007569;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;cell aging;nucleus","FunCat.ID":"11.02.03.04.01;14.07.04;40.20;70.10","FunCat.description":"transcription activation;modification by acetylation, deacetylation;cell aging;nucleus","PubMed.ID":12397079,"subunits.Protein.name.":"Histone acetyltransferase KAT8 ;Mortality factor 4-like protein 1","subunits.Gene.name.":"KAT8;MORF4L1","subunits.Gene.name.syn.":"MOF MYST1;MRG15","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":725,"ComplexName":"P2X7 receptor signalling complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43707;O95425;P05107;P08238;P0DMV8;P11142;P23467;P42356;P60709;Q13368;Q16787;Q64663","subunits.Entrez.IDs.":"81;6840;3689;3326;3303;3312;5787;5297;60;4356;3909;29665","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006811;GO:0005216;GO:0007166;GO:0007010;GO:0005886","GO.description":"ion transport;ion channel activity;cell surface receptor signaling pathway;cytoskeleton organization;plasma membrane","FunCat.ID":"20.01.01;20.03.01.01;30.05;42.04;70.02","FunCat.description":"ion transport;ion channels;transmembrane signal transduction;cytoskeleton/structural proteins;eukaryotic plasma membrane / membrane attached","PubMed.ID":11707406,"subunits.Protein.name.":"Alpha-actinin-4;Supervillin;Integrin beta-2;Heat shock protein HSP 90-beta;Heat shock 70 kDa protein 1A;Heat shock cognate 71 kDa protein;Receptor-type tyrosine-protein phosphatase beta;Phosphatidylinositol 4-kinase alpha;Actin, cytoplasmic 1;MAGUK p55 subfamily member 3;Laminin subunit alpha-3;P2X purinoceptor 7","subunits.Gene.name.":"ACTN4;SVIL;ITGB2;HSP90AB1;HSPA1A;HSPA8;PTPRB;PI4KA;ACTB;MPP3;LAMA3;P2rx7","subunits.Gene.name.syn.":"None;None;CD18 MFI7;HSP90B HSPC2 HSPCB;HSPA1, HSX70, HSP70-1A;HSC70, HSP73, HSPA10;PTPB;PIK4 PIK4CA;None;DLG3;LAMNA;None","Disease.comment":"None","Subunits.comment":"Since human P2rx7 was not available in the Uniprot database at the time of annotation, the orthologous protein from rat was used. Since the authors did not specify HSP70, we used isoform HSPA1A.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Rattus norvegicus (Rat)"}
{"ComplexID":726,"ComplexName":"DDB2 complex","Organism":"Human","Synonyms":"Ubiquitin E3 ligase","Cell.line":"None","subunits.UniProt.IDs.":"P61201;P62877;Q13098;Q13619;Q16531;Q7L5N1;Q92466;Q92905;Q99627;Q9BT78;Q9UBW8;Q9UNS2","subunits.Entrez.IDs.":"9318;9978;2873;8451;1642;10980;1643;10987;10920;51138;50813;8533","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation;MI:0029-cosedimentation through density gradients","GO.ID":"GO:0006281;GO:0016567;GO:0016579;GO:0003677;GO:0006974;GO:0005634","GO.description":"DNA repair;protein ubiquitination;protein deubiquitination;DNA binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;14.07.05;16.03.01;32.01.09;70.10","FunCat.description":"DNA repair;modification by ubiquitination, deubiquitination;DNA binding;DNA damage response;nucleus","PubMed.ID":12732143,"subunits.Protein.name.":"COP9 signalosome complex subunit 2;E3 ubiquitin-protein ligase RBX1;COP9 signalosome complex subunit 1;Cullin-4A;DNA damage-binding protein 1;COP9 signalosome complex subunit 6;DNA damage-binding protein 2;COP9 signalosome complex subunit 5;COP9 signalosome complex subunit 8;COP9 signalosome complex subunit 4;COP9 signalosome complex subunit 7a;COP9 signalosome complex subunit 3","subunits.Gene.name.":"COPS2;RBX1;GPS1;CUL4A;DDB1;COPS6;DDB2;COPS5;COPS8;COPS4;COPS7A;COPS3","subunits.Gene.name.syn.":"CSN2, TRIP15;RNF75, ROC1;COPS1, CSN1;None;XAP1;CSN6, HVIP;None;CSN5, JAB1;CSN8;CSN4;CSN7A, DERP10;CSN3","Disease.comment":"None","Subunits.comment":"Since the authors did not specify COPS7, we used isoform COPS7A.","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Results suggest that the distinct UV response of the DDB2 and CSA complexes is involved in diverse mechanisms of nucleotide excision repair (NER). The DDB2 complex binds to DNA after UV irradiation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":727,"ComplexName":"CSA complex","Organism":"Human","Synonyms":"Ubiquitin E3 ligase","Cell.line":"None","subunits.UniProt.IDs.":"P61201;P62877;Q13098;Q13216;Q13619;Q16531;Q7L5N1;Q92905;Q99627;Q9BT78;Q9UBW8;Q9UNS2","subunits.Entrez.IDs.":"9318;9978;2873;1161;8451;1642;10980;10987;10920;51138;50813;8533","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation;MI:0029-cosedimentation through density gradients","GO.ID":"GO:0006281;GO:0016567;GO:0016579;GO:0005515;GO:0006974;GO:0005634","GO.description":"DNA repair;protein ubiquitination;protein deubiquitination;protein binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;14.07.05;16.01;32.01.09;70.10","FunCat.description":"DNA repair;modification by ubiquitination, deubiquitination;protein binding;DNA damage response;nucleus","PubMed.ID":12732143,"subunits.Protein.name.":"COP9 signalosome complex subunit 2;E3 ubiquitin-protein ligase RBX1;COP9 signalosome complex subunit 1;DNA excision repair protein ERCC-8;Cullin-4A;DNA damage-binding protein 1;COP9 signalosome complex subunit 6;COP9 signalosome complex subunit 5;COP9 signalosome complex subunit 8;COP9 signalosome complex subunit 4;COP9 signalosome complex subunit 7a;COP9 signalosome complex subunit 3","subunits.Gene.name.":"COPS2;RBX1;GPS1;ERCC8;CUL4A;DDB1;COPS6;COPS5;COPS8;COPS4;COPS7A;COPS3","subunits.Gene.name.syn.":"CSN2, TRIP15;RNF75, ROC1;COPS1, CSN1;CKN1 CSA;None;XAP1;CSN6, HVIP;CSN5, JAB1;CSN8;CSN4;CSN7A, DERP10;CSN3","Disease.comment":"None","Subunits.comment":"Since the authors did not specify COPS7, we used isoform COPS7A.","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Results suggest that the distinct UV response of the DDB2 and CSA complexes is involved in diverse mechanisms of nucleotide excision repair (NER). The CSA complex does not bind to DNA, regardless of UV damage.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":728,"ComplexName":"CSA-POLIIa complex","Organism":"Human","Synonyms":"Ubiquitin E3 ligase","Cell.line":"None","subunits.UniProt.IDs.":"P24928;P61201;P62877;Q13098;Q13216;Q13619;Q16531;Q7L5N1;Q92905;Q99627;Q9BT78;Q9UBW8;Q9UNS2","subunits.Entrez.IDs.":"5430;9318;9978;2873;1161;8451;1642;10980;10987;10920;51138;50813;8533","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation;MI:0029-cosedimentation through density gradients","GO.ID":"GO:0006281;GO:0009299;GO:0016567;GO:0016579;GO:0006974;GO:0005634","GO.description":"DNA repair;mRNA transcription;protein ubiquitination;protein deubiquitination;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;11.02.03;14.07.05;32.01.09;70.10","FunCat.description":"DNA repair;mRNA synthesis;modification by ubiquitination, deubiquitination;DNA damage response;nucleus","PubMed.ID":12732143,"subunits.Protein.name.":"DNA-directed RNA polymerase II subunit RPB1;COP9 signalosome complex subunit 2;E3 ubiquitin-protein ligase RBX1;COP9 signalosome complex subunit 1;DNA excision repair protein ERCC-8;Cullin-4A;DNA damage-binding protein 1;COP9 signalosome complex subunit 6;COP9 signalosome complex subunit 5;COP9 signalosome complex subunit 8;COP9 signalosome complex subunit 4;COP9 signalosome complex subunit 7a;COP9 signalosome complex subunit 3","subunits.Gene.name.":"POLR2A;COPS2;RBX1;GPS1;ERCC8;CUL4A;DDB1;COPS6;COPS5;COPS8;COPS4;COPS7A;COPS3","subunits.Gene.name.syn.":"POLR2;CSN2, TRIP15;RNF75, ROC1;COPS1, CSN1;CKN1 CSA;None;XAP1;CSN6, HVIP;CSN5, JAB1;CSN8;CSN4;CSN7A, DERP10;CSN3","Disease.comment":"None","Subunits.comment":"Since the authors did not specify COPS7, we used isoform COPS7A.","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. This complex has been purified from UV-irradiated cells. Results suggest that the distinct UV response of the DDB2 and CSA complexes is involved in diverse mechanisms of nucleotide excision repair (NER).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":729,"ComplexName":"Ubiquitin E3 ligase (FBXO31, SKP1A, CUL1, RBX1)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62877;P63208;Q13616;Q5XUX0","subunits.Entrez.IDs.":"9978;6500;8454;79791","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0000278;GO:0016567;GO:0016579;GO:0030163;GO:0007569","GO.description":"mitotic cell cycle;protein ubiquitination;protein deubiquitination;protein catabolic process;cell aging","FunCat.ID":"10.03.01.01;14.07.05;14.13;40.20","FunCat.description":"mitotic cell cycle;modification by ubiquitination, deubiquitination;protein/peptide degradation;cell aging","PubMed.ID":16357137,"subunits.Protein.name.":"E3 ubiquitin-protein ligase RBX1;S-phase kinase-associated protein 1;Cullin-1;F-box only protein 31","subunits.Gene.name.":"RBX1;SKP1;CUL1;FBXO31","subunits.Gene.name.syn.":"RNF75, ROC1;EMC19, OCP2, SKP1A, TCEB1L;None;FBX14 FBX31","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. FBXO31 is the chromosome 16q24.3 senescence gene, a candidate breast tumor suppressor, and a component of an SCF complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":730,"ComplexName":"SNARE complex (STX4, SNAP23, VAMP1)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00161;P23763;Q12846","subunits.Entrez.IDs.":"8773;6843;6810","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0047- far western blotting","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":16920918,"subunits.Protein.name.":"Synaptosomal-associated protein 23;Vesicle-associated membrane protein 1 ;Syntaxin-4","subunits.Gene.name.":"SNAP23;VAMP1;STX4","subunits.Gene.name.syn.":"None;SYB1;STX4A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":731,"ComplexName":"SNARE complex (STX4, SNAP23, VAMP2)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00161;P63027;Q12846","subunits.Entrez.IDs.":"8773;6844;6810","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0047- far western blotting","GO.ID":"GO:0006906;GO:0006887","GO.description":"vesicle fusion;exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.03","FunCat.description":"vesicle fusion;exocytosis","PubMed.ID":16920918,"subunits.Protein.name.":"Synaptosomal-associated protein 23;Vesicle-associated membrane protein 2 ;Syntaxin-4","subunits.Gene.name.":"SNAP23;VAMP2;STX4","subunits.Gene.name.syn.":"None;SYB2;STX4A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":732,"ComplexName":"SIN3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00422;O75446;Q09028;Q13547;Q16576;Q92769;Q96ST3","subunits.Entrez.IDs.":"10284;8819;5928;3065;5931;3066;25942","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0091- chromatography technologies","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;DNA binding;organization of chromosome structure;nucleus","PubMed.ID":11784859,"subunits.Protein.name.":"Histone deacetylase complex subunit SAP18;Histone deacetylase complex subunit SAP30;Histone-binding protein RBBP4;Histone deacetylase 1;Histone-binding protein RBBP7;Histone deacetylase 2;Paired amphipathic helix protein Sin3a","subunits.Gene.name.":"SAP18;SAP30;RBBP4;HDAC1;RBBP7;HDAC2;SIN3A","subunits.Gene.name.syn.":"None;None;RBAP48;RPD3L1;RBAP46;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":733,"ComplexName":"SNARE complex (STX4, VAMP1, VAMP7)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P23763;P51809;Q12846","subunits.Entrez.IDs.":"6843;6845;6810","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0047- far western blotting","GO.ID":"GO:0006906;GO:0006887","GO.description":"vesicle fusion;exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.03","FunCat.description":"vesicle fusion;exocytosis","PubMed.ID":16920918,"subunits.Protein.name.":"Vesicle-associated membrane protein 1 ;Vesicle-associated membrane protein 7 ;Syntaxin-4","subunits.Gene.name.":"VAMP1;VAMP7;STX4","subunits.Gene.name.syn.":"SYB1;SYBL1;STX4A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":734,"ComplexName":"SNARE complex (STX4, SNAP23, VAMP2)","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00161;P63045;Q12846","subunits.Entrez.IDs.":"8773;24803;6810","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0047- far western blotting","GO.ID":"GO:0006906;GO:0006887","GO.description":"vesicle fusion;exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.03","FunCat.description":"vesicle fusion;exocytosis","PubMed.ID":16920918,"subunits.Protein.name.":"Synaptosomal-associated protein 23;Vesicle-associated membrane protein 2;Syntaxin-4","subunits.Gene.name.":"SNAP23;Vamp2;STX4","subunits.Gene.name.syn.":"None;Syb2;STX4A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Homo sapiens (Human);Rattus norvegicus (Rat);Homo sapiens (Human)"}
{"ComplexID":735,"ComplexName":"SNARE complex (Vti1b, Stx6, Stx7)","Organism":"Mouse","Synonyms":"Q-SNARE complex","Cell.line":"None","subunits.UniProt.IDs.":"O70439;O88384;Q9JKK1","subunits.Entrez.IDs.":"53331;53612;58244","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006906;GO:0006887;GO:0005794","GO.description":"vesicle fusion;exocytosis;Golgi apparatus","FunCat.ID":"20.09.07.27;20.09.16.09.03;70.08","FunCat.description":"vesicle fusion;exocytosis;Golgi","PubMed.ID":15640147,"subunits.Protein.name.":"Syntaxin-7;Vesicle transport through interaction with t-SNAREs homolog 1B ;Syntaxin-6","subunits.Gene.name.":"Stx7;Vti1b;Stx6","subunits.Gene.name.syn.":"Syn7;Vti1l1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":736,"ComplexName":"SNARE complex (Vti1b, Stx7, Stx8, Vamp8)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O70404;O70439;O88384;O88983","subunits.Entrez.IDs.":"22320;53331;53612;55943","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":15640147,"subunits.Protein.name.":"Vesicle-associated membrane protein 8;Syntaxin-7;Vesicle transport through interaction with t-SNAREs homolog 1B ;Syntaxin-8","subunits.Gene.name.":"Vamp8;Stx7;Vti1b;Stx8","subunits.Gene.name.syn.":"None;Syn7;Vti1l1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":737,"ComplexName":"Ppp2c-PKA-Ryr2-mAkap complex","Organism":"Rat","Synonyms":"None","Cell.line":"heart muscle","subunits.UniProt.IDs.":"B0LPN4;P27791;P63331;Q9WVC7","subunits.Entrez.IDs.":"689560;25636;24672;64553","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0019722;GO:0019933;GO:0005635","GO.description":"calcium-mediated signaling;cAMP-mediated signaling;nuclear envelope","FunCat.ID":"30.01.09.03;30.01.09.07;70.10.05","FunCat.description":"Ca2+ mediated signal transduction;cAMP/cGMP mediated signal transduction;nuclear membrane","PubMed.ID":11590243,"subunits.Protein.name.":"Ryanodine receptor 2;cAMP-dependent protein kinase catalytic subunit alpha;Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform;A-kinase anchor protein 6","subunits.Gene.name.":"Ryr2;Prkaca;Ppp2ca;Akap6","subunits.Gene.name.syn.":"None;None;None;mAkap","Disease.comment":"None","Subunits.comment":"Since the authors did not specify the PP2A catalytic subunit, we used subunit Ppp2ca. Since the authors did not specify the PKA catalytic subunit, we used subunit Prkaca.","Complex.comment":"The authors describe the association of PP2A and RyR with the mAKAP complex, an assembly that is likely to be important to the integration of cAMP and Ca2+ signaling to the myocyte nucleus.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":738,"ComplexName":"SIN3-ING1b complex I","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00422;O75446;Q09028;Q13547;Q16576;Q4LE39;Q92769;Q96ST3;Q9UK53","subunits.Entrez.IDs.":"10284;8819;5928;3065;5931;51742;3066;25942;3621","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0091- chromatography technologies","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;organization of chromosome structure;nucleus","PubMed.ID":11784859,"subunits.Protein.name.":"Histone deacetylase complex subunit SAP18;Histone deacetylase complex subunit SAP30;Histone-binding protein RBBP4;Histone deacetylase 1;Histone-binding protein RBBP7;AT-rich interactive domain-containing protein 4B ;Histone deacetylase 2;Paired amphipathic helix protein Sin3a;Inhibitor of growth protein 1","subunits.Gene.name.":"SAP18;SAP30;RBBP4;HDAC1;RBBP7;ARID4B;HDAC2;SIN3A;ING1","subunits.Gene.name.syn.":"None;None;RBAP48;RPD3L1;RBAP46;BRCAA1 RBBP1L1 RBP1L1 SAP180;None;None;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SAP30 is a specific component of Sin3 complexes since it is absent in other HDAC1/2-containing complexes such as NuRD.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":739,"ComplexName":"SIN3-ING1b complex II","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00422;O14497;O75446;O96019;P51532;Q09028;Q12824;Q13547;Q16576;Q4LE39;Q8TAQ2;Q92769;Q92922;Q96GM5;Q96ST3;Q9UK53","subunits.Entrez.IDs.":"10284;8289;8819;86;6597;5928;6598;3065;5931;51742;6601;3066;6599;6602;25942;3621","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0091- chromatography technologies","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0005515;GO:0051090;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;protein binding;regulation of sequence-specific DNA binding transcription factor activity;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;16.01;18.02.09;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;protein binding;regulator of transcription factor;organization of chromosome structure;nucleus","PubMed.ID":11784859,"subunits.Protein.name.":"Histone deacetylase complex subunit SAP18;AT-rich interactive domain-containing protein 1A;Histone deacetylase complex subunit SAP30;Actin-like protein 6A;Transcription activator BRG1;Histone-binding protein RBBP4;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;Histone deacetylase 1;Histone-binding protein RBBP7;AT-rich interactive domain-containing protein 4B ;SWI/SNF complex subunit SMARCC2;Histone deacetylase 2;SWI/SNF complex subunit SMARCC1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1;Paired amphipathic helix protein Sin3a;Inhibitor of growth protein 1","subunits.Gene.name.":"SAP18;ARID1A;SAP30;ACTL6A;SMARCA4;RBBP4;SMARCB1;HDAC1;RBBP7;ARID4B;SMARCC2;HDAC2;SMARCC1;SMARCD1;SIN3A;ING1","subunits.Gene.name.syn.":"None;BAF250 BAF250A C1orf4 OSA1 SMARCF1;None;BAF53 BAF53A INO80K;BAF190A BRG1 SNF2B SNF2L4;RBAP48;BAF47, INI1, SNF5L1;RPD3L1;RBAP46;BRCAA1 RBBP1L1 RBP1L1 SAP180;BAF170;None;BAF155;BAF60A;None;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SAP30 is a specific component of Sin3 complexes since it is absent in other HDAC1/2-containing complexes such as NuRD.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":740,"ComplexName":"Exon junction complex, EIF4A3-MLN51-MAGOH-Y14 (RNA-protein complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15234;P38919;P61326;Q9Y5S9","subunits.Entrez.IDs.":"22794;9775;4116;9939","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0040- electron microscopy; MI:0071- molecular sieving; MI:0114- x-ray crystallography","GO.ID":"GO:0043488;GO:0006417;GO:0003723;GO:0050658;GO:0051033;GO:0051169;GO:0005737;GO:0005634","GO.description":"regulation of mRNA stability;regulation of translation;RNA binding;RNA transport;RNA transmembrane transporter activity;nuclear transport;cytoplasm;nucleus","FunCat.ID":"11.04.03.11;12.07;16.03.03;20.01.21;20.09.01;70.03;70.10","FunCat.description":"control of mRNA stability;translational control;RNA binding;RNA transport;nuclear transport;cytoplasm;nucleus","PubMed.ID":16797590,"subunits.Protein.name.":"Protein CASC3 ;Eukaryotic initiation factor 4A-III;Protein mago nashi homolog;RNA-binding protein 8A","subunits.Gene.name.":"CASC3;EIF4A3;MAGOH;RBM8A","subunits.Gene.name.syn.":"MLN51;DDX48, KIAA0111;MAGOHA;RBM8, Y14","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This protein complex remains stably bound to the mRNA through different cellular environments. Magoh and Y14 form a tight heterodimer. The authors propose a that eIF4AIII interacts with Y14:Magoh to enforce a compact arrangement of eIF4AIII's two domains and allow MLN51 to interact with both eIF4AIII and the RNA.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":741,"ComplexName":"NCOR-HDAC3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15379;O60907;O75376;Q13227;Q9BZK7","subunits.Entrez.IDs.":"8841;6907;9611;2874;79718","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0032774;GO:0006473;GO:0006476;GO:0007254;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;RNA biosynthetic process;protein acetylation;protein deacetylation;JNK cascade;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;11.02;14.07.04;30.01.05.01.02;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;RNA synthesis;modification by acetylation, deacetylation;JNK cascade;organization of chromosome structure;nucleus","PubMed.ID":11931768,"subunits.Protein.name.":"Histone deacetylase 3;F-box-like/WD repeat-containing protein TBL1X;Nuclear receptor corepressor 1;G protein pathway suppressor 2;F-box-like/WD repeat-containing protein TBL1XR1","subunits.Gene.name.":"HDAC3;TBL1X;NCOR1;GPS2;TBL1XR1","subunits.Gene.name.syn.":"None;TBL1;KIAA1047;None;IRA1 TBLR1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"N-CoR-HDAC3 complex inhibits JNK activation through the associated GPS2 subunit and thus could potentially provide an alternative mechanism for hormone-mediated antagonism of AP-1 function.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":742,"ComplexName":"eIF3 complex (EIF3S6, EIF3S5, EIF3S4, EIF3S3, EIF3S6IP, EIF3S2, EIF3S9, EIF3S12,  EIF3S10, EIF3S8,  EIF3S1, EIF3S7)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00303;O15371;O15372;O75821;O75822;P55884;P60228;Q13347;Q14152;Q99613;Q9UBQ5;Q9Y262","subunits.Entrez.IDs.":"8665;8664;8667;8666;8669;8662;3646;8668;8661;8663;27335;51386","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0004- affinity chromatography technologies","GO.ID":"GO:0006413","GO.description":"translational initiation","FunCat.ID":"12.04.01","FunCat.description":"translation initiation","PubMed.ID":14519125,"subunits.Protein.name.":"Eukaryotic translation initiation factor 3 subunit F ;Eukaryotic translation initiation factor 3 subunit D ;Eukaryotic translation initiation factor 3 subunit H ;Eukaryotic translation initiation factor 3 subunit G ;Eukaryotic translation initiation factor 3 subunit J ;Eukaryotic translation initiation factor 3 subunit B;Eukaryotic translation initiation factor 3 subunit E ;Eukaryotic translation initiation factor 3 subunit I ;Eukaryotic translation initiation factor 3 subunit A ;Eukaryotic translation initiation factor 3 subunit C ;Eukaryotic translation initiation factor 3 subunit K ;Eukaryotic translation initiation factor 3 subunit L","subunits.Gene.name.":"EIF3F;EIF3D;EIF3H;EIF3G;EIF3J;EIF3B;EIF3E;EIF3I;EIF3A;EIF3C;EIF3K;EIF3L","subunits.Gene.name.syn.":"EIF3S5;EIF3S7;EIF3S3;EIF3S4;EIF3S1;EIF3S9;EIF3S6 INT6;EIF3S2 TRIP1;EIF3S10 KIAA0139;EIF3S8;EIF3S12;EIF3EIP EIF3S6IP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":743,"ComplexName":"SIN3-SAP25 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00422;O75446;Q09028;Q13547;Q16576;Q1EHW4;Q4LE39;Q92769;Q96ST3;Q9H0E3;Q9H7L9","subunits.Entrez.IDs.":"10284;8819;5928;3065;5931;751865;51742;3066;25942;79595;64426","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0005515;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;protein binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;16.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;protein binding;organization of chromosome structure;nucleus","PubMed.ID":16449650,"subunits.Protein.name.":"Histone deacetylase complex subunit SAP18;Histone deacetylase complex subunit SAP30;Histone-binding protein RBBP4;Histone deacetylase 1;Histone-binding protein RBBP7;Histone deacetylase complex subunit SAP25 ;AT-rich interactive domain-containing protein 4B ;Histone deacetylase 2;Paired amphipathic helix protein Sin3a;Histone deacetylase complex subunit SAP130;Sin3 histone deacetylase corepressor complex component SDS3","subunits.Gene.name.":"SAP18;SAP30;RBBP4;HDAC1;RBBP7;Sap25;ARID4B;HDAC2;SIN3A;SAP130;SUDS3","subunits.Gene.name.syn.":"None;None;RBAP48;RPD3L1;RBAP46;;BRCAA1 RBBP1L1 RBP1L1 SAP180;None;None;None;SAP45 SDS3","Disease.comment":"None","Subunits.comment":"Since human SAP25 was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"SAP25 binds to the PAH1 domain of SIN3A.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Mus musculus (Mouse);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":744,"ComplexName":"Exon junction complex (EIF4A3-MLN51-MAGOH-Y14)","Organism":"Human","Synonyms":"RNA-protein complex","Cell.line":"None","subunits.UniProt.IDs.":"O15234;P38919;P61326;Q9Y5S9","subunits.Entrez.IDs.":"22794;9775;4116;9939","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0043488;GO:0006417;GO:0003723;GO:0050658;GO:0051033;GO:0051169;GO:0005737;GO:0005634","GO.description":"regulation of mRNA stability;regulation of translation;RNA binding;RNA transport;RNA transmembrane transporter activity;nuclear transport;cytoplasm;nucleus","FunCat.ID":"11.04.03.11;12.07;16.03.03;20.01.21;20.09.01;70.03;70.10","FunCat.description":"control of mRNA stability;translational control;RNA binding;RNA transport;nuclear transport;cytoplasm;nucleus","PubMed.ID":16314458,"subunits.Protein.name.":"Protein CASC3 ;Eukaryotic initiation factor 4A-III;Protein mago nashi homolog;RNA-binding protein 8A","subunits.Gene.name.":"CASC3;EIF4A3;MAGOH;RBM8A","subunits.Gene.name.syn.":"MLN51;DDX48, KIAA0111;MAGOHA;RBM8, Y14","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The experiments demonstrate that eIF4AIII, MLN51, and Magoh:Y14 are able to form a stable tetrameric complex when co-expressed in vivo. Both eIF4AIII and MLN51 are required for the stable association of either with the Magoh:Y14 heterodimer.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":745,"ComplexName":"NCOR-SIN3-RPD3 complex","Organism":"Human","Synonyms":"None","Cell.line":"MCF-7 cells","subunits.UniProt.IDs.":"O75182;Q92769;Q96ST3;Q9Y618","subunits.Entrez.IDs.":"23309;3066;25942;9612","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0032774;GO:0006473;GO:0006476;GO:0009755;GO:0023052;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;RNA biosynthetic process;protein acetylation;protein deacetylation;hormone-mediated signaling pathway;signaling;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;11.02;14.07.04;30.01.09.08;30.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;RNA synthesis;modification by acetylation, deacetylation;hormone mediated signal transduction;cellular signalling;organization of chromosome structure;nucleus","PubMed.ID":9139820,"subunits.Protein.name.":"Paired amphipathic helix protein Sin3b;Histone deacetylase 2;Paired amphipathic helix protein Sin3a;Nuclear receptor corepressor 2","subunits.Gene.name.":"SIN3B;HDAC2;SIN3A;NCOR2","subunits.Gene.name.syn.":"KIAA0700;None;None;CTG26","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors predict that the ligand-induced switch of heterodimeric nuclear receptors from repressor to activator functions involves the exchange of complexes containing histone deacetylases with those that have histone acetylase activity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":746,"ComplexName":"C/EBPalpha-HNF6 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P49715;Q9UBC0","subunits.Entrez.IDs.":"1050;3175","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0019- coimmunoprecipitation","GO.ID":"GO:0045893;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;nucleus","FunCat.ID":"11.02.03.04.01;70.10","FunCat.description":"transcription activation;nucleus","PubMed.ID":16440369,"subunits.Protein.name.":"CCAAT/enhancer-binding protein alpha ;Hepatocyte nuclear factor 6","subunits.Gene.name.":"CEBPA;ONECUT1","subunits.Gene.name.syn.":"CEBP;HNF6 HNF6A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Formation of the C/EBPalpha-HNF6 protein complex required the HNF6 cut domain and the C/EBPalpha activation domain (AD) 1/AD2 sequences. The C/EBPalpha-HNF6 protein complex stimulates recruitment of the CBP coactivator protein for expression of Foxa2.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":747,"ComplexName":"NCOR-SIN3-HDAC1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HL-60 cells","subunits.UniProt.IDs.":"Q13547;Q96ST3;Q9Y618","subunits.Entrez.IDs.":"3065;25942;9612","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006265;GO:0045892;GO:0032774;GO:0006473;GO:0006476;GO:0009755;GO:0023052;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;RNA biosynthetic process;protein acetylation;protein deacetylation;hormone-mediated signaling pathway;signaling;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;11.02;14.07.04;30.01.09.08;30.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;RNA synthesis;modification by acetylation, deacetylation;hormone mediated signal transduction;cellular signalling;organization of chromosome structure;nucleus","PubMed.ID":9150137,"subunits.Protein.name.":"Histone deacetylase 1;Paired amphipathic helix protein Sin3a;Nuclear receptor corepressor 2","subunits.Gene.name.":"HDAC1;SIN3A;NCOR2","subunits.Gene.name.syn.":"RPD3L1;None;CTG26","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"N-CoR directly interact with mSin3A.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":748,"ComplexName":"TRAF6-TAK1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43318;Q9Y4K3","subunits.Entrez.IDs.":"6885;7189","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007178","GO.description":"transmembrane receptor protein serine/threonine kinase signaling pathway","FunCat.ID":"30.05.01.18","FunCat.description":"transmembrane receptor protein serine/threonine kinase signalling pathways","PubMed.ID":16543409,"subunits.Protein.name.":"Mitogen-activated protein kinase kinase kinase 7;TNF receptor-associated factor 6","subunits.Gene.name.":"MAP3K7;TRAF6","subunits.Gene.name.syn.":"TAK1;RNF85","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"During IL-1 signaling cascade a complex consisting of TRAF6, TAK1, TAB1, TAB2, and the two ubiquitin ligases Uev1A and Ubc13 is formed, phosphorylating TRAF6 and subsequently TAK1. TAK1 activation leads to activation of both NF{kappa}B and the MAPKs, followed by gene transcription. SOCS-3 (suppressor of cytokine signaling-3) inhibits IL-1 signal transduction by inhibiting ubiquitination of TRAF6, thus preventing association and activation of TAK1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":749,"ComplexName":"MeCP2-SIN3A-HDAC complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"P51608;Q13547;Q92769;Q96ST3","subunits.Entrez.IDs.":"4204;3065;3066;25942","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006265;GO:0045892;GO:0032774;GO:0006473;GO:0006476;GO:0003677;GO:0009792;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;RNA biosynthetic process;protein acetylation;protein deacetylation;DNA binding;embryo development ending in birth or egg hatching;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;11.02;14.07.04;16.03.01;41.05.04.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;RNA synthesis;modification by acetylation, deacetylation;DNA binding;early embryogenesis;organization of chromosome structure;nucleus","PubMed.ID":9620804,"subunits.Protein.name.":"Methyl-CpG-binding protein 2 ;Histone deacetylase 1;Histone deacetylase 2;Paired amphipathic helix protein Sin3a","subunits.Gene.name.":"MECP2;HDAC1;HDAC2;SIN3A","subunits.Gene.name.syn.":";RPD3L1;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"MeCp binds specifically to methylated DNA, thus linking two global mechanisms of gene regulation, DNA methylation and histone deacetylation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":750,"ComplexName":"MeCP2-Sin3a-Hdac complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"Q00566;Q60520;Q99PA1;Q99PA2","subunits.Entrez.IDs.":"29386;20466;84577;84576","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0032774;GO:0006473;GO:0006476;GO:0003677;GO:0009792;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;RNA biosynthetic process;protein acetylation;protein deacetylation;DNA binding;embryo development ending in birth or egg hatching;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;11.02;14.07.04;16.03.01;41.05.04.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;RNA synthesis;modification by acetylation, deacetylation;DNA binding;early embryogenesis;organization of chromosome structure;nucleus","PubMed.ID":9620804,"subunits.Protein.name.":"Methyl-CpG-binding protein 2 ;Paired amphipathic helix protein Sin3a;Histone deacetylase 2 ;Histone deacetylase 1","subunits.Gene.name.":"Mecp2;Sin3a;Hdac2;Hdac1","subunits.Gene.name.syn.":";Kiaa4126;;HdaC1 Hdac1l","Disease.comment":"None","Subunits.comment":"Since Sin3a from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"MeCp binds specifically to methylated DNA, thus linking two global mechanisms of gene regulation, DNA methylation and histone deacetylation.","SWISSPROT.organism":"Rattus norvegicus (Rat);Mus musculus (Mouse);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":751,"ComplexName":"Trpc1-dystrophin-alpha1-syntrophin complex","Organism":"Mouse","Synonyms":"None","Cell.line":"muscle","subunits.UniProt.IDs.":"P11531;Q61056;Q61234","subunits.Entrez.IDs.":"13405;22063;20648","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0004- affinity chromatography technologies","GO.ID":"GO:0050789;GO:0008324;GO:0006812;GO:0005216;GO:0005886","GO.description":"regulation of biological process;cation transmembrane transporter activity;cation transport;ion channel activity;plasma membrane","FunCat.ID":"18;20.01.01.01;20.03.01.01;70.02","FunCat.description":"REGULATION OF METABOLISM AND PROTEIN FUNCTION;cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;eukaryotic plasma membrane / membrane attached","PubMed.ID":17202249,"subunits.Protein.name.":"Dystrophin;Short transient receptor potential channel 1 ;Alpha-1-syntrophin","subunits.Gene.name.":"Dmd;Trpc1;Snta1","subunits.Gene.name.syn.":"None;Trp1 Trrp1;Snt1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The control of cationic channels by PDZ-containing scaffolding proteins might be a widespread function of dystrophin-associated protein complexes for controlling transmembrane ions fluxes. The authors propose that the dystrophin-based cytoskeleton, by the intermediate of PDZ-containing alpha-1-syntrophin, maintains normal TRPC1-dependent store-operated influx during activation of calcium release in muscle cells.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":752,"ComplexName":"SMRT core complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15379;O60907;Q9Y618","subunits.Entrez.IDs.":"8841;6907;9612","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0226- ion exchange chromatography; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0009755;GO:0023052;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;hormone-mediated signaling pathway;signaling;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;30.01.09.08;30.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;hormone mediated signal transduction;cellular signalling;organization of chromosome structure;nucleus","PubMed.ID":10944117,"subunits.Protein.name.":"Histone deacetylase 3;F-box-like/WD repeat-containing protein TBL1X;Nuclear receptor corepressor 2","subunits.Gene.name.":"HDAC3;TBL1X;NCOR2","subunits.Gene.name.syn.":"None;TBL1;CTG26","Disease.comment":"TBL1 is involved in deafness.","Subunits.comment":"Another subunit of the complex was found in the analysis, which has not been further characterized: SMRT-p37.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":753,"ComplexName":"UTM-SGCE-DAG1-CAV1-NOS3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43556;P29474;P46939;Q03135;Q14118","subunits.Entrez.IDs.":"8910;4846;7402;857;1605","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030234;GO:0050790;GO:0061028","GO.description":"enzyme regulator activity;regulation of catalytic activity;establishment of endothelial barrier","FunCat.ID":"18.02.01","FunCat.description":"enzymatic activity regulation / enzyme regulator","PubMed.ID":17127434,"subunits.Protein.name.":"Epsilon-sarcoglycan ;Nitric oxide synthase, endothelial;Utrophin ;Caveolin-1;Dystroglycan","subunits.Gene.name.":"SGCE;NOS3;UTRN;CAV1;DAG1","subunits.Gene.name.syn.":"ESG;None;DMDL DRP1;CAV;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors propose that this utrophin associated protein complex (UAPC) in human umbilical vein endothelial cells (HUVECs) may play an important role in the regulation of vascular tone.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":754,"ComplexName":"Exon junction complex (EIF4A3-MLN51-UPF3B-MAGOH-Y14)","Organism":"Human","Synonyms":"RNA-protein complex","Cell.line":"None","subunits.UniProt.IDs.":"O15234;P38919;P61326;Q0VAK7;Q9Y5S9","subunits.Entrez.IDs.":"22794;9775;4116;65109;9939","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0043488;GO:0006417;GO:0003723;GO:0050658;GO:0051033;GO:0051169;GO:0005737;GO:0005634","GO.description":"regulation of mRNA stability;regulation of translation;RNA binding;RNA transport;RNA transmembrane transporter activity;nuclear transport;cytoplasm;nucleus","FunCat.ID":"11.04.03.11;12.07;16.03.03;20.01.21;20.09.01;70.03;70.10","FunCat.description":"control of mRNA stability;translational control;RNA binding;RNA transport;nuclear transport;cytoplasm;nucleus","PubMed.ID":16209946,"subunits.Protein.name.":"Protein CASC3 ;Eukaryotic initiation factor 4A-III;Protein mago nashi homolog;UPF3B protein;RNA-binding protein 8A","subunits.Gene.name.":"CASC3;EIF4A3;MAGOH;UPF3B;RBM8A","subunits.Gene.name.syn.":"MLN51;DDX48, KIAA0111;MAGOHA;;RBM8, Y14","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":755,"ComplexName":"Exon junction complex (F4A3-MLN51-UPF3B-MAGOH-Y14-PYM)","Organism":"Human","Synonyms":"RNA-protein complex","Cell.line":"None","subunits.UniProt.IDs.":"O15234;P38919;P61326;Q0VAK7;Q9BRP8;Q9Y5S9","subunits.Entrez.IDs.":"22794;9775;4116;65109;84305;9939","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0043488;GO:0006417;GO:0003723;GO:0050658;GO:0051033;GO:0051169;GO:0005737;GO:0005634","GO.description":"regulation of mRNA stability;regulation of translation;RNA binding;RNA transport;RNA transmembrane transporter activity;nuclear transport;cytoplasm;nucleus","FunCat.ID":"11.04.03.11;12.07;16.03.03;20.01.21;20.09.01;70.03;70.10","FunCat.description":"control of mRNA stability;translational control;RNA binding;RNA transport;nuclear transport;cytoplasm;nucleus","PubMed.ID":16209946,"subunits.Protein.name.":"Protein CASC3 ;Eukaryotic initiation factor 4A-III;Protein mago nashi homolog;UPF3B protein;Partner of Y14 and mago ;RNA-binding protein 8A","subunits.Gene.name.":"CASC3;EIF4A3;MAGOH;UPF3B;PYM1;RBM8A","subunits.Gene.name.syn.":"MLN51;DDX48, KIAA0111;MAGOHA;;PYM WIBG;RBM8, Y14","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":756,"ComplexName":"Prune-Gelsolin complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06396;Q86TP1","subunits.Entrez.IDs.":"2934;58497","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0004- affinity chromatography technologies","GO.ID":"GO:0016477","GO.description":"cell migration","FunCat.ID":"34.05.01","FunCat.description":"cell migration","PubMed.ID":17103319,"subunits.Protein.name.":"Gelsolin ;Protein prune homolog","subunits.Gene.name.":"GSN;PRUNE","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":757,"ComplexName":"Prune-GSK3beta complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P49841;Q86TP1","subunits.Entrez.IDs.":"2932;58497","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0004- affinity chromatography technologies","GO.ID":"GO:0016477","GO.description":"cell migration","FunCat.ID":"34.05.01","FunCat.description":"cell migration","PubMed.ID":17103319,"subunits.Protein.name.":"Glycogen synthase kinase-3 beta;Protein prune homolog","subunits.Gene.name.":"GSK3B;PRUNE","subunits.Gene.name.syn.":"None;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":758,"ComplexName":"Prune/Nm23-H1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P15531;Q86TP1","subunits.Entrez.IDs.":"4830;58497","Protein.complex.purification.method":"MI:0087- predictive text mining","GO.ID":"GO:0006928","GO.description":"movement of cell or subcellular component","FunCat.ID":"34.05","FunCat.description":"cell motility","PubMed.ID":14998490,"subunits.Protein.name.":"Nucleoside diphosphate kinase A;Protein prune homolog","subunits.Gene.name.":"NME1;PRUNE","subunits.Gene.name.syn.":"NDPKA NM23;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":759,"ComplexName":"Fgfr1-Kal1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P23352;Q04589","subunits.Entrez.IDs.":"3730;Error happend while calculation","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008543;GO:0007608;GO:0007420","GO.description":"fibroblast growth factor receptor signaling pathway;sensory perception of smell;brain development","FunCat.ID":"30.05.01.12.03;36.25.01.13;47.03.01.01.01","FunCat.description":"FGF-receptor signalling pathway;olfaction;brain","PubMed.ID":17186267,"subunits.Protein.name.":"Anosmin-1;Fibroblast growth factor receptor 1","subunits.Gene.name.":"ANOS1;Fgfr1","subunits.Gene.name.syn.":"ADMLX KAL KAL1 KALIG1;Flg","Disease.comment":"KAL1 and FGFR1 are involved in Kallmann syndrome.","Subunits.comment":"Since KAL1 from rat was not available in the UniProt database at the time of annotation, the orthologous human protein was used.","Complex.comment":"The authors propose that during the initial steps of olfactory bulb formation, anosmin-1 cooperates with FGFR1 to promote functional FGF-signalling that in turn promotes olfactory bulb development.","SWISSPROT.organism":"Homo sapiens (Human);Rattus norvegicus (Rat)"}
{"ComplexID":760,"ComplexName":"Apoptosis- and splicing-associated protein complex (ASAP-L), SAP18-RNPS1-Acinus-L","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00422;Q15287;Q9UKV3","subunits.Entrez.IDs.":"10284;10921;22985","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0000398;GO:0006397;GO:0006915;GO:0005634","GO.description":"mRNA splicing, via spliceosome;mRNA processing;apoptotic process;nucleus","FunCat.ID":"11.04.03;40.10.02;70.10","FunCat.description":"mRNA processing (splicing, 5'-, 3'-end processing);apoptosis (type I programmed cell death);nucleus","PubMed.ID":12665594,"subunits.Protein.name.":"Histone deacetylase complex subunit SAP18;RNA-binding protein with serine-rich domain 1 ;Apoptotic chromatin condensation inducer in the nucleus","subunits.Gene.name.":"SAP18;RNPS1;ACIN1","subunits.Gene.name.syn.":"None;LDC2;ACINUS KIAA0670","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In vitro splicing assays suggest that the ASAP complexes function to repress splicing in vitro and that the ability of RNPS1 (and possibly Acinus-L) to activate splicing is overcome both when it is a component of ASAP and in the presence of the intact complex. In vitro assays using an apoptotic extract strongly indicate that ASAP complexes disassemble during apoptosis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":761,"ComplexName":"Apoptosis- and splicing-associated protein complex (ASAP-S), SAP18-RNPS1-Acinus-S","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00422;Q15287;Q9UKV3","subunits.Entrez.IDs.":"10284;10921;22985","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0000398;GO:0006397;GO:0006915;GO:0005634","GO.description":"mRNA splicing, via spliceosome;mRNA processing;apoptotic process;nucleus","FunCat.ID":"11.04.03;40.10.02;70.10","FunCat.description":"mRNA processing (splicing, 5'-, 3'-end processing);apoptosis (type I programmed cell death);nucleus","PubMed.ID":12665594,"subunits.Protein.name.":"Histone deacetylase complex subunit SAP18;RNA-binding protein with serine-rich domain 1 ;Apoptotic chromatin condensation inducer in the nucleus","subunits.Gene.name.":"SAP18;RNPS1;ACIN1","subunits.Gene.name.syn.":"None;LDC2;ACINUS KIAA0670","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In vitro splicing assays suggest that the ASAP complexes function to repress splicing in vitro and that the ability of RNPS1 (and possibly Acinus-L) to activate splicing is overcome both when it is a component of ASAP and in the presence of the intact complex. In vitro assays using an apoptotic extract strongly indicate that ASAP complexes disassemble during apoptosis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":762,"ComplexName":"Ahnak1-dysferlin complex","Organism":"Rat","Synonyms":"None","Cell.line":"muscle","subunits.UniProt.IDs.":"Q38PG1;Q9ESD7","subunits.Entrez.IDs.":"191572;26903","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0007009;GO:0007517;GO:0005886","GO.description":"plasma membrane organization;muscle organ development;plasma membrane","FunCat.ID":"42.02;45.03.12;70.02","FunCat.description":"eukaryotic plasma membrane;muscle;eukaryotic plasma membrane / membrane attached","PubMed.ID":17185750,"subunits.Protein.name.":"AHNAK 1 ;Dysferlin","subunits.Gene.name.":";Dysf","subunits.Gene.name.syn.":";Fer1l1","Disease.comment":"Dysf is involved in autosomal recessive limb girdle muscular dystrophy 2B (LGMD2B), Miyoshi myopathy (MM) and distal anterior compartment myopathy (DMAT).","Subunits.comment":"Since Dysf from rat was not available in the UniProt database at the time of annotation, the orthologous protein from human was used.","Complex.comment":"The authors provide evidence for a functional cooperation between dysferlin and AHNAK during muscle regeneration.","SWISSPROT.organism":"Rattus norvegicus (Rat);Mus musculus (Mouse)"}
{"ComplexID":763,"ComplexName":"Y14-Magoh complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P61326;Q9Y5S9","subunits.Entrez.IDs.":"4116;9939","Protein.complex.purification.method":"MI:0055- fluorescent resonance energy transfer; MI:0114- x-ray crystallography; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0000398;GO:0006397;GO:0050658;GO:0051033;GO:0051169;GO:0005737;GO:0005634","GO.description":"mRNA splicing, via spliceosome;mRNA processing;RNA transport;RNA transmembrane transporter activity;nuclear transport;cytoplasm;nucleus","FunCat.ID":"11.04.03;20.01.21;20.09.01;70.03;70.10","FunCat.description":"mRNA processing (splicing, 5'-, 3'-end processing);RNA transport;nuclear transport;cytoplasm;nucleus","PubMed.ID":12781131,"subunits.Protein.name.":"Protein mago nashi homolog;RNA-binding protein 8A","subunits.Gene.name.":"MAGOH;RBM8A","subunits.Gene.name.syn.":"MAGOHA;RBM8, Y14","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Y14 and Magoh form an extremely stable heterodimer. Magoh binds with high affinity to the RNP motif RNA binding domain (RBD) of Y14 and completely masks its RNA binding surface.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":764,"ComplexName":"Dysferlin-affixin complex","Organism":"Human","Synonyms":"None","Cell.line":"striated muscle","subunits.UniProt.IDs.":"O75923;Q9HBI1","subunits.Entrez.IDs.":"8291;29780","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0051-fluorescence technologies","GO.ID":"GO:0007009;GO:0007519;GO:0014706","GO.description":"plasma membrane organization;skeletal muscle tissue development;striated muscle tissue development","FunCat.ID":"42.02;41.05.15;45.03.12.01","FunCat.description":"eukaryotic plasma membrane;myogenesis;striated muscle","PubMed.ID":15835269,"subunits.Protein.name.":"Dysferlin;Beta-parvin","subunits.Gene.name.":"DYSF;PARVB","subunits.Gene.name.syn.":"FER1L1;None","Disease.comment":"DYSF is involved in Miyoshi myopathy (MM) and limb girdle muscular dystrophy type 2B (LGMD2B).","Subunits.comment":"None","Complex.comment":"The results suggest that affixin may participate in membrane repair with dysferlin.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":765,"ComplexName":"SNARE complex (Stx6, Snap29)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q63635;Q9Z2P6","subunits.Entrez.IDs.":"60562;116500","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0047- far western blotting","GO.ID":"GO:0006906;GO:0048489;GO:0016079;GO:0005794","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis;Golgi apparatus","FunCat.ID":"20.09.07.27;20.09.16.09.05;70.08","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis;Golgi","PubMed.ID":9880331,"subunits.Protein.name.":"Syntaxin-6;Synaptosomal-associated protein 29","subunits.Gene.name.":"Stx6;Snap29","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":766,"ComplexName":"Cask-Grip1-Prkce-Rgs4-Gria2 complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P09216;P19491;P49799;P97879;Q62915","subunits.Entrez.IDs.":"29340;29627;29480;84016;29647","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0042133","GO.description":"neurotransmitter metabolic process","FunCat.ID":"01.08.01","FunCat.description":"metabolism of neurotransmitters","PubMed.ID":17084383,"subunits.Protein.name.":"Protein kinase C epsilon type ;Glutamate receptor 2;Regulator of G-protein signaling 4;Glutamate receptor-interacting protein 1;Peripheral plasma membrane protein CASK","subunits.Gene.name.":"Prkce;Gria2;Rgs4;Grip1;Cask","subunits.Gene.name.syn.":"Pkce;Glur2;None;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The associations between CASK, PKCepsilon, and RGS4 were up-regulated in the adult brain compared with postnatal day 11 rat brain. In contrast, the associations of CASK with Mint1, GRIP1, and GluR2/3 were down-regulated in the adult brain. These results suggest that CASK protein complex is developmentally regulated by unknown signals.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":767,"ComplexName":"Cask-Grip1-Gria2-Mint1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"O35430;P19491;P97879;Q62915","subunits.Entrez.IDs.":"83589;29627;84016;29647","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0042133","GO.description":"neurotransmitter metabolic process","FunCat.ID":"01.08.01","FunCat.description":"metabolism of neurotransmitters","PubMed.ID":17084383,"subunits.Protein.name.":"Amyloid beta A4 precursor protein-binding family A member 1;Glutamate receptor 2;Glutamate receptor-interacting protein 1;Peripheral plasma membrane protein CASK","subunits.Gene.name.":"Apba1;Gria2;Grip1;Cask","subunits.Gene.name.syn.":"Mint1 X11;Glur2;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The associations between CASK, PKCepsilon, and RGS4 were up-regulated in the adult brain compared with postnatal day 11 rat brain. In contrast, the associations of CASK with Mint1, GRIP1, and GluR2/3 were down-regulated in the adult brain. These results suggest that CASK protein complex is developmentally regulated by unknown signals.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":768,"ComplexName":"NdpkA-Ampkalpha1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"liver","subunits.UniProt.IDs.":"P54645;Q05982","subunits.Entrez.IDs.":"65248;191575","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005515;GO:0005737","GO.description":"protein binding;cytoplasm","FunCat.ID":"16.01;70.03","FunCat.description":"protein binding;cytoplasm","PubMed.ID":16026327,"subunits.Protein.name.":"5'-AMP-activated protein kinase catalytic subunit alpha-1;Nucleoside diphosphate kinase A","subunits.Gene.name.":"Prkaa1;Nme1","subunits.Gene.name.syn.":"Ampk1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":769,"ComplexName":"Exon junction complex (EIF4A3-MLN51-MAGOH-Y14),  RNA-protein complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15234;P38919;P61326;Q9Y5S9","subunits.Entrez.IDs.":"22794;9775;4116;9939","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0114- x-ray crystallography","GO.ID":"GO:0043488;GO:0006417;GO:0003723;GO:0005524;GO:0050658;GO:0051033;GO:0051169;GO:0005737;GO:0005634","GO.description":"regulation of mRNA stability;regulation of translation;RNA binding;ATP binding;RNA transport;RNA transmembrane transporter activity;nuclear transport;cytoplasm;nucleus","FunCat.ID":"11.04.03.11;12.07;16.03.03;16.19.03;20.01.21;20.09.01;70.03;70.10","FunCat.description":"control of mRNA stability;translational control;RNA binding;ATP binding;RNA transport;nuclear transport;cytoplasm;nucleus","PubMed.ID":16923391,"subunits.Protein.name.":"Protein CASC3 ;Eukaryotic initiation factor 4A-III;Protein mago nashi homolog;RNA-binding protein 8A","subunits.Gene.name.":"CASC3;EIF4A3;MAGOH;RBM8A","subunits.Gene.name.syn.":"MLN51;DDX48, KIAA0111;MAGOHA;RBM8, Y14","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The DEAD-box protein eIF4AIII encloses an ATP molecule and provides the binding sites for six ribonucleotides. Btz wraps around eIF4AIII and stacks against the 5' nucleotide. An intertwined network of interactions anchors Mago-Y14 and Btz at the interface between the two domains of eIF4AIII, effectively stabilizing the ATP bound state.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":770,"ComplexName":"TREX complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q13769;Q13838;Q6I9Y2;Q86V81;Q86W42;Q8NI27;Q96FV9;Q96J01","subunits.Entrez.IDs.":"8563;7919;80145;10189;79228;57187;9984;84321","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0003723;GO:0050658;GO:0051033;GO:0051169;GO:0016363;GO:0016607","GO.description":"RNA binding;RNA transport;RNA transmembrane transporter activity;nuclear transport;nuclear matrix;nuclear speck","FunCat.ID":"16.03.03;20.01.21;20.09.01;70.10.06;70.10.09","FunCat.description":"RNA binding;RNA transport;nuclear transport;nuclear matrix;nuclear speckles","PubMed.ID":15998806,"subunits.Protein.name.":"THO complex subunit 5 homolog;Spliceosome RNA helicase DDX39B ;THO complex subunit 7 homolog;THO complex subunit 4 ;THO complex subunit 6 homolog;THO complex subunit 2;THO complex subunit 1;THO complex subunit 3","subunits.Gene.name.":"THOC5;DDX39B;THOC7;ALYREF;THOC6;THOC2;THOC1;THOC3","subunits.Gene.name.syn.":"C22orf19, KIAA0983;BAT1 UAP56;NIF3L1BP1;ALY BEF THOC4;WDR58;CXorf3;HPR1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The TREX complex is recruited by the CBC complex to the 5-prime end of spliced RNAs and is involved in RNA export from the nucleus into the cytoplasm. The TREX complex contains the THO transcription elongation complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":771,"ComplexName":"NDPKA-AMPKalpha1 complex","Organism":"Human","Synonyms":"None","Cell.line":"liver","subunits.UniProt.IDs.":"P15531;Q13131","subunits.Entrez.IDs.":"4830;5562","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005515;GO:0005737","GO.description":"protein binding;cytoplasm","FunCat.ID":"16.01;70.03","FunCat.description":"protein binding;cytoplasm","PubMed.ID":16026327,"subunits.Protein.name.":"Nucleoside diphosphate kinase A;5'-AMP-activated protein kinase catalytic subunit alpha-1","subunits.Gene.name.":"NME1;PRKAA1","subunits.Gene.name.syn.":"NDPKA NM23;AMPK1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":772,"ComplexName":"eIF4AIII-Btz complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15234;P38919","subunits.Entrez.IDs.":"22794;9775","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0114- x-ray crystallography","GO.ID":"GO:0043488","GO.description":"regulation of mRNA stability","FunCat.ID":"11.04.03.11","FunCat.description":"control of mRNA stability","PubMed.ID":16923391,"subunits.Protein.name.":"Protein CASC3 ;Eukaryotic initiation factor 4A-III","subunits.Gene.name.":"CASC3;EIF4A3","subunits.Gene.name.syn.":"MLN51;DDX48, KIAA0111","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The 3.0 Angstroem resolution structure of the eIF4AIII-Btz subcomplex reveals a dramatic conformational change of the helicase domains as compared to EJC bound eIF4AIII. More generally, the authors propose that similarly to what observed for protein kinases, members of the DEAD-box family of proteins are likely to adopt a similar structure in their 'on' state (when bound to ATP and RNA) despite having different conformations in their 'off' states.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":773,"ComplexName":"Y14-Magoh complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P61326;Q9Y5S9","subunits.Entrez.IDs.":"4116;9939","Protein.complex.purification.method":"MI:0114- x-ray crystallography; MI:0071- molecular sieving","GO.ID":"GO:0000398;GO:0006397;GO:0050658;GO:0051033;GO:0051169;GO:0005737;GO:0005634","GO.description":"mRNA splicing, via spliceosome;mRNA processing;RNA transport;RNA transmembrane transporter activity;nuclear transport;cytoplasm;nucleus","FunCat.ID":"11.04.03;20.01.21;20.09.01;70.03;70.10","FunCat.description":"mRNA processing (splicing, 5'-, 3'-end processing);RNA transport;nuclear transport;cytoplasm;nucleus","PubMed.ID":16923391,"subunits.Protein.name.":"Protein mago nashi homolog;RNA-binding protein 8A","subunits.Gene.name.":"MAGOH;RBM8A","subunits.Gene.name.syn.":"MAGOHA;RBM8, Y14","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Y14 and Magoh form an extremely stable heterodimer. Magoh binds with high affinity to the RNP motif RNA binding domain (RBD) of Y14 and completely masks its RNA binding surface.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":774,"ComplexName":"THO complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q13769;Q6I9Y2;Q86W42;Q8NI27;Q96FV9","subunits.Entrez.IDs.":"8563;80145;79228;57187;9984","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0003723;GO:0016607","GO.description":"RNA binding;nuclear speck","FunCat.ID":"16.03.03;70.10.09","FunCat.description":"RNA binding;nuclear speckles","PubMed.ID":15998806,"subunits.Protein.name.":"THO complex subunit 5 homolog;THO complex subunit 7 homolog;THO complex subunit 6 homolog;THO complex subunit 2;THO complex subunit 1","subunits.Gene.name.":"THOC5;THOC7;THOC6;THOC2;THOC1","subunits.Gene.name.syn.":"C22orf19, KIAA0983;NIF3L1BP1;WDR58;CXorf3;HPR1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The human THO complex associates with spliced mRNA, but not with unspliced pre-mRNA in vitro. Transcription is not required for this recruitment. It was also shown that the human THO complex colocalizes with splicing factors in nuclear speckle domains in vivo. The TREX complex contains the THO transcription elongation complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":775,"ComplexName":"CBC complex (cap binding complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P52298;Q09161","subunits.Entrez.IDs.":"22916;4686","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0003723;GO:0050658;GO:0051033;GO:0051169;GO:0005634","GO.description":"RNA binding;RNA transport;RNA transmembrane transporter activity;nuclear transport;nucleus","FunCat.ID":"16.03.03;20.01.21;20.09.01;70.10","FunCat.description":"RNA binding;RNA transport;nuclear transport;nucleus","PubMed.ID":11545740,"subunits.Protein.name.":"Nuclear cap-binding protein subunit 2;Nuclear cap-binding protein subunit 1","subunits.Gene.name.":"NCBP2;NCBP1","subunits.Gene.name.syn.":"CBP20;CBP80 NCBP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The heterodimeric nuclear cap binding complex (CBC) binds to 5'-capped polymerase II transcripts. It enhances the efficiency of several mRNA maturation steps and is essential for U snRNA nuclear export in multicellular eukaryotes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":776,"ComplexName":"Plp1-Calr-Itgav complex","Organism":"Rat","Synonyms":"None","Cell.line":"glia cell","subunits.UniProt.IDs.":"P18418;P43406;P60203","subunits.Entrez.IDs.":"64202;16410;24943","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007229;GO:0010001","GO.description":"integrin-mediated signaling pathway;glial cell differentiation","FunCat.ID":"30.05.02.26;43.03.11","FunCat.description":"integrin receptor signalling pathway;glia cell","PubMed.ID":12196561,"subunits.Protein.name.":"Calreticulin;Integrin alpha-V;Myelin proteolipid protein","subunits.Gene.name.":"Calr;Itgav;Plp1","subunits.Gene.name.syn.":"None;None;Plp","Disease.comment":"None","Subunits.comment":"Since Itgav from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"The PLP protein may be involved in signaling through integrins in oligodendrocytes.","SWISSPROT.organism":"Rattus norvegicus (Rat);Mus musculus (Mouse);Rattus norvegicus (Rat)"}
{"ComplexID":777,"ComplexName":"Exon junction complex","Organism":"Mammalia","Synonyms":"EJC complex","Cell.line":"COS cells","subunits.UniProt.IDs.":"Q15287;Q86V81;Q8IYB3;Q9BZI7;Q9HAU5;Q9UBU9;Q9Y5S9","subunits.Entrez.IDs.":"10921;10189;10250;65109;26019;10482;9939","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006401;GO:0003723;GO:0050658;GO:0051033;GO:0051169;GO:0005634","GO.description":"RNA catabolic process;RNA binding;RNA transport;RNA transmembrane transporter activity;nuclear transport;nucleus","FunCat.ID":"01.03.16.01;16.03.03;20.01.21;20.09.01;70.10","FunCat.description":"RNA degradation;RNA binding;RNA transport;nuclear transport;nucleus","PubMed.ID":12093754,"subunits.Protein.name.":"RNA-binding protein with serine-rich domain 1 ;THO complex subunit 4 ;Serine/arginine repetitive matrix protein 1 ;Regulator of nonsense transcripts 3B;Regulator of nonsense transcripts 2;Nuclear RNA export factor 1 ;RNA-binding protein 8A","subunits.Gene.name.":"RNPS1;ALYREF;SRRM1;UPF3B;UPF2;NXF1;RBM8A","subunits.Gene.name.syn.":"LDC2;ALY BEF THOC4;SRM160;RENT3B, UPF3X;KIAA1408, RENT2;TAP;RBM8, Y14","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The exon junction complex (EJC) is a protein complex that assembles near exon-exon junctions of mRNAs as a result of splicing. EJC proteins play important roles in postsplicing events including mRNA export, cytoplasmic localization, and nonsense-mediated decay.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":778,"ComplexName":"LARC complex (LCR-associated remodeling complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14497;O94776;O95983;O96019;P07910;P51532;P60709;Q09028;Q12824;Q13547;Q14839;Q8TAQ2;Q8WXI9;Q92769;Q92785;Q92922;Q92925;Q969G3;Q9UBB5","subunits.Entrez.IDs.":"8289;9219;53615;86;3183;6597;60;5928;6598;3065;1108;6601;57459;3066;5977;6599;6603;6605;8932","Protein.complex.purification.method":"MI:0091- chromatography technologies; MI:0004- affinity chromatography technologies","GO.ID":"GO:0006265;GO:2001141;GO:0006355;GO:0006473;GO:0006476;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04;14.07.04;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcriptional control;modification by acetylation, deacetylation;DNA binding;organization of chromosome structure;nucleus","PubMed.ID":16217013,"subunits.Protein.name.":"AT-rich interactive domain-containing protein 1A;Metastasis-associated protein MTA2;Methyl-CpG-binding domain protein 3;Actin-like protein 6A;Heterogeneous nuclear ribonucleoproteins C1/C2 ;Transcription activator BRG1;Actin, cytoplasmic 1;Histone-binding protein RBBP4;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;Histone deacetylase 1;Chromodomain-helicase-DNA-binding protein 4;SWI/SNF complex subunit SMARCC2;Transcriptional repressor p66-beta ;Histone deacetylase 2;Zinc finger protein ubi-d4 ;SWI/SNF complex subunit SMARCC1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;Methyl-CpG-binding domain protein 2","subunits.Gene.name.":"ARID1A;MTA2;MBD3;ACTL6A;HNRNPC;SMARCA4;ACTB;RBBP4;SMARCB1;HDAC1;CHD4;SMARCC2;GATAD2B;HDAC2;DPF2;SMARCC1;SMARCD2;SMARCE1;MBD2","subunits.Gene.name.syn.":"BAF250 BAF250A C1orf4 OSA1 SMARCF1;MTA1L1 PID;None;BAF53 BAF53A INO80K;HNRPC;BAF190A BRG1 SNF2B SNF2L4;None;RBAP48;BAF47, INI1, SNF5L1;RPD3L1;None;BAF170;KIAA1150;None;BAF45D REQ UBID4;BAF155;BAF60B;BAF57;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"LARC binds to the hypersensitive 2 (HS2)-Maf recognition element (MARE) DNA in a sequence-specific manner and remodels nucleosomes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":779,"ComplexName":"K(ATP) macromolecular complex (Kir6.2, Pkm2, Gapdh, Tpi1)","Organism":"Rat","Synonyms":"None","Cell.line":"heart muscle","subunits.UniProt.IDs.":"P04797;P11980;P48500;P70673","subunits.Entrez.IDs.":"24383;25630;24849;83535","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0397-two hybrid array;MI:0416-fluorescence microscopy","GO.ID":"GO:0050789;GO:0008324;GO:0006812;GO:0005216;GO:0005886","GO.description":"regulation of biological process;cation transmembrane transporter activity;cation transport;ion channel activity;plasma membrane","FunCat.ID":"18;20.01.01.01;20.03.01.01;70.02","FunCat.description":"REGULATION OF METABOLISM AND PROTEIN FUNCTION;cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;eukaryotic plasma membrane / membrane attached","PubMed.ID":16170200,"subunits.Protein.name.":"Glyceraldehyde-3-phosphate dehydrogenase;Pyruvate kinase PKM;Triosephosphate isomerase;ATP-sensitive inward rectifier potassium channel 11","subunits.Gene.name.":"Gapdh;Pkm;Tpi1;Kcnj11","subunits.Gene.name.syn.":"Gapd;Pkm2 Pykm;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors provide evidence that the activity of the identified three glycolytic enzymes regulate channel activity, presumably by altering the ATP levels in the microenvironment of the K(ATP) channel protein complex.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":781,"ComplexName":"URI complex (Unconventional prefoldin RPB5 Interactor)","Organism":"Human","Synonyms":"Prefoldin-like complex","Cell.line":"None","subunits.UniProt.IDs.":"O94763;P19388;P63208;Q13309;Q13616;Q9UHV9;Q9ULZ2;Q9Y230;Q9Y265","subunits.Entrez.IDs.":"8725;5434;6500;6502;8454;5202;26228;10856;8607","Protein.complex.purification.method":"MI:0071- molecular sieving;MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0042594;GO:0048015","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;response to starvation;phosphatidylinositol-mediated signaling","FunCat.ID":"11.02.03.04;32.01.11","FunCat.description":"transcriptional control;nutrient starvation response","PubMed.ID":14615539,"subunits.Protein.name.":"Unconventional prefoldin RPB5 interactor 1 ;DNA-directed RNA polymerases I, II, and III subunit RPABC1 ;S-phase kinase-associated protein 1;S-phase kinase-associated protein 2;Cullin-1;Prefoldin subunit 2;Signal-transducing adaptor protein 1 ;RuvB-like 2;RuvB-like 1","subunits.Gene.name.":"URI1;POLR2E;SKP1;SKP2;CUL1;PFDN2;STAP1;RUVBL2;RUVBL1","subunits.Gene.name.syn.":"C19orf2 NNX3 PPP1R19 RMP URI;;EMC19, OCP2, SKP1A, TCEB1L;FBXL1;None;PFD2;BRDG1;INO80J TIP48 TIP49B;INO80H NMP238 TIP49 TIP49A","Disease.comment":"None","Subunits.comment":"Three other subunits of the complex were found in the analysis, which have not been further characterized: p42, p40, p10.At the time of annotation, the additional member PFD4-related protein of the protein complex was not found in the UniProt database.","Complex.comment":"The URI complex participates in the regulation of nutrient-sensitive, TOR-dependent transcription programs.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":782,"ComplexName":"Itch-Fam/Usp9x complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P70398;Q5YB86","subunits.Entrez.IDs.":"22284;311567","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0019- coimmunoprecipitation; MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0016567;GO:0016579;GO:0005515;GO:0050789","GO.description":"protein ubiquitination;protein deubiquitination;protein binding;regulation of biological process","FunCat.ID":"14.07.05;16.01;18","FunCat.description":"modification by ubiquitination, deubiquitination;protein binding;REGULATION OF METABOLISM AND PROTEIN FUNCTION","PubMed.ID":17038327,"subunits.Protein.name.":"Probable ubiquitin carboxyl-terminal hydrolase FAF-X ;Itch E3 ubiquitin ligase","subunits.Gene.name.":"Usp9x;Itch","subunits.Gene.name.syn.":"Fafl Fam;","Disease.comment":"None","Subunits.comment":"Since Usp9x of the rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"Interaction between Itch and FAM reverses Itch auto-ubiquitylation and protects the ligase from proteasomal degradation.","SWISSPROT.organism":"Mus musculus (Mouse);Rattus norvegicus (Rat)"}
{"ComplexID":783,"ComplexName":"ITCH-FAM/USP9x complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q93008;Q96J02","subunits.Entrez.IDs.":"8239;83737","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0019- coimmunoprecipitation; MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0016567;GO:0016579;GO:0005515;GO:0050789","GO.description":"protein ubiquitination;protein deubiquitination;protein binding;regulation of biological process","FunCat.ID":"14.07.05;16.01;18","FunCat.description":"modification by ubiquitination, deubiquitination;protein binding;REGULATION OF METABOLISM AND PROTEIN FUNCTION","PubMed.ID":17038327,"subunits.Protein.name.":"Probable ubiquitin carboxyl-terminal hydrolase FAF-X ;E3 ubiquitin-protein ligase Itchy homolog","subunits.Gene.name.":"USP9X;ITCH","subunits.Gene.name.syn.":"DFFRX FAM USP9;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Interaction between Itch and FAM reverses Itch auto-ubiquitylation and protects the ligase from proteasomal degradation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":784,"ComplexName":"SMG-1-UPF-ERF1-ERF3 complex (SURF)","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"P15170;P62495;Q92900;Q96Q15","subunits.Entrez.IDs.":"2935;2107;5976;23049","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0000184","GO.description":"nuclear-transcribed mRNA catabolic process, nonsense-mediated decay","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":16452507,"subunits.Protein.name.":"Eukaryotic peptide chain release factor GTP-binding subunit ERF3A;Eukaryotic peptide chain release factor subunit 1;Regulator of nonsense transcripts 1;Serine/threonine-protein kinase SMG1","subunits.Gene.name.":"GSPT1;ETF1;UPF1;SMG1","subunits.Gene.name.syn.":"ERF3A;ERF1, RF1, SUP45L1;KIAA0221, RENT1;ATX, KIAA0421, LIP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The SURF complex accumulated greatly when Upf2 or Y14 was depleted or the Upf2-binding region of Upf1 is mutated. SMG-1 forms a complex with Upf1, eRF1, and eRF3in a Upf2- and Y14-independent manner","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":785,"ComplexName":"Exon junction complex","Organism":"Human","Synonyms":"EJC complex","Cell.line":"None","subunits.UniProt.IDs.":"P38919;P61326;Q13838;Q15287;Q86V81;Q8IYB3;Q9BZI7;Q9Y5S9","subunits.Entrez.IDs.":"9775;4116;7919;10921;10189;10250;65109;9939","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006401;GO:0003723;GO:0050658;GO:0051033;GO:0051169;GO:0005634","GO.description":"RNA catabolic process;RNA binding;RNA transport;RNA transmembrane transporter activity;nuclear transport;nucleus","FunCat.ID":"01.03.16.01;16.03.03;20.01.21;20.09.01;70.10","FunCat.description":"RNA degradation;RNA binding;RNA transport;nuclear transport;nucleus","PubMed.ID":1473001,"subunits.Protein.name.":"Eukaryotic initiation factor 4A-III;Protein mago nashi homolog;Spliceosome RNA helicase DDX39B ;RNA-binding protein with serine-rich domain 1 ;THO complex subunit 4 ;Serine/arginine repetitive matrix protein 1 ;Regulator of nonsense transcripts 3B;RNA-binding protein 8A","subunits.Gene.name.":"EIF4A3;MAGOH;DDX39B;RNPS1;ALYREF;SRRM1;UPF3B;RBM8A","subunits.Gene.name.syn.":"DDX48, KIAA0111;MAGOHA;BAT1 UAP56;LDC2;ALY BEF THOC4;SRM160;RENT3B, UPF3X;RBM8, Y14","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The exon junction complex (EJC) is a protein complex that assembles near exon-exon junctions of mRNAs as a result of splicing. EJC proteins play important roles in postsplicing events including mRNA export, cytoplasmic localization, and nonsense-mediated decay.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":786,"ComplexName":"MR-UBC9-SRC1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P08235;Q08209;Q15788","subunits.Entrez.IDs.":"4306;5530;8648","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0051- fluorescence technologies","GO.ID":"GO:2001141;GO:0006355;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;nucleus","FunCat.ID":"11.02.03.04;70.10","FunCat.description":"transcriptional control;nucleus","PubMed.ID":17105732,"subunits.Protein.name.":"Mineralocorticoid receptor ;Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform;Nuclear receptor coactivator 1","subunits.Gene.name.":"NR3C2;PPP3CA;NCOA1","subunits.Gene.name.syn.":"MCR MLR;CALNA CNA;BHLHE74, SRC1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":787,"ComplexName":"NuA4/Tip60-HAT complex B","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O96019;Q92993;Q9H2F5;Q9NPF5;Q9UBU8;Q9Y230;Q9Y265;Q9Y4A5","subunits.Entrez.IDs.":"86;10524;80314;55929;10933;10856;8607;8295","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0051276;GO:0006281;GO:0006265;GO:0006473;GO:0006476;GO:0003677;GO:0006974;GO:0051276;GO:0005634","GO.description":"chromosome organization;DNA repair;DNA topological change;protein acetylation;protein deacetylation;DNA binding;cellular response to DNA damage stimulus;chromosome organization;nucleus","FunCat.ID":"42.10.03;10.01.05.01;10.01.09.05;14.07.04;16.03.01;32.01.09;70.10","FunCat.description":"organization of chromosome structure;DNA repair;DNA conformation modification (e.g. chromatin);modification by acetylation, deacetylation;DNA binding;DNA damage response;nucleus","PubMed.ID":14966270,"subunits.Protein.name.":"Actin-like protein 6A;Histone acetyltransferase KAT5;Enhancer of polycomb homolog 1;DNA methyltransferase 1-associated protein 1;Mortality factor 4-like protein 1;RuvB-like 2;RuvB-like 1;Transformation/transcription domain-associated protein","subunits.Gene.name.":"ACTL6A;KAT5;EPC1;DMAP1;MORF4L1;RUVBL2;RUVBL1;TRRAP","subunits.Gene.name.syn.":"BAF53 BAF53A INO80K;HTATIP TIP60;None;KIAA1425;MRG15;INO80J TIP48 TIP49B;INO80H NMP238 TIP49 TIP49A;PAF400","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The NuA4 histone acetyltransferase (HAT) multisubunit complex is responsible for acetylation of histone H4 and H2A N-terminal tails in yeast. The NuA4/Tip60 HAT complex is highly conserved in eukaryotes playing primary roles in transcription, cellular response to DNA damage, and cell cycle control.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":788,"ComplexName":"Exosome","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q06265;Q13868;Q15024;Q5RKV6;Q96B26;Q9NPD3;Q9NQT4;Q9NQT5;Q9Y2L1;Q9Y3B2","subunits.Entrez.IDs.":"5393;23404;23016;118460;11340;54512;56915;51010;22894;51013","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006401;GO:0003723;GO:0005737;GO:0005634","GO.description":"RNA catabolic process;RNA binding;cytoplasm;nucleus","FunCat.ID":"01.03.16.01;16.03.03;70.03;70.10","FunCat.description":"RNA degradation;RNA binding;cytoplasm;nucleus","PubMed.ID":11719186,"subunits.Protein.name.":"Exosome complex component RRP45 ;Exosome complex component RRP4 ;Exosome complex component RRP42 ;Exosome complex component MTR3 ;Exosome complex component RRP43 ;Exosome complex component RRP41 ;Exosome complex component RRP46 ;Exosome complex component RRP40 ;Exosome complex exonuclease RRP44 ;Exosome complex component CSL4","subunits.Gene.name.":"EXOSC9;EXOSC2;EXOSC7;EXOSC6;EXOSC8;EXOSC4;EXOSC5;EXOSC3;DIS3;EXOSC1","subunits.Gene.name.syn.":"PMSCL1;RRP4;KIAA0116 RRP42;MTR3;OIP2 RRP43;RRP41 SKI6;CML28 RRP46;RRP40;KIAA1008 RRP44;CSL4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Inherently unstable mammalian mRNAs contain AU-rich elements (AREs) within their 3' untranslated regions. The mammalian exosome is required for rapid 3'-to-5' degradation of ARE-containing RNAs but not for poly(A) shortening. ARE recognition requires certain ARE binding proteins that can interact with the exosome and recruit it to unstable RNAs, thereby promoting their rapid degradation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":789,"ComplexName":"Exosome","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q01780;Q06265;Q13868;Q15024;Q5RKV6;Q96B26;Q9NPD3;Q9NQT4;Q9NQT5;Q9Y2L1;Q9Y3B2","subunits.Entrez.IDs.":"5394;5393;23404;23016;118460;11340;54512;56915;51010;22894;51013","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006401;GO:0003723;GO:0005634","GO.description":"RNA catabolic process;RNA binding;nucleus","FunCat.ID":"01.03.16.01;16.03.03;70.10","FunCat.description":"RNA degradation;RNA binding;nucleus","PubMed.ID":11719186,"subunits.Protein.name.":"Exosome component 10 ;Exosome complex component RRP45 ;Exosome complex component RRP4 ;Exosome complex component RRP42 ;Exosome complex component MTR3 ;Exosome complex component RRP43 ;Exosome complex component RRP41 ;Exosome complex component RRP46 ;Exosome complex component RRP40 ;Exosome complex exonuclease RRP44 ;Exosome complex component CSL4","subunits.Gene.name.":"EXOSC10;EXOSC9;EXOSC2;EXOSC7;EXOSC6;EXOSC8;EXOSC4;EXOSC5;EXOSC3;DIS3;EXOSC1","subunits.Gene.name.syn.":"PMSCL PMSCL2 RRP6;PMSCL1;RRP4;KIAA0116 RRP42;MTR3;OIP2 RRP43;RRP41 SKI6;CML28 RRP46;RRP40;KIAA1008 RRP44;CSL4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Inherently unstable mammalian mRNAs contain AU-rich elements (AREs) within their 3' untranslated regions. The mammalian exosome is required for rapid 3'-to-5' degradation of ARE-containing RNAs but not for poly(A) shortening. ARE recognition requires certain ARE binding proteins that can interact with the exosome and recruit it to unstable RNAs, thereby promoting their rapid degradation. The exosome complex containing PMSCL was only found in the nuclear complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":790,"ComplexName":"DDB complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q16531;Q92466","subunits.Entrez.IDs.":"1642;1643","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0028- cosedimentation in solution","GO.ID":"GO:0006281;GO:0003677;GO:0006974","GO.description":"DNA repair;DNA binding;cellular response to DNA damage stimulus","FunCat.ID":"10.01.05.01;16.03.01;32.01.09","FunCat.description":"DNA repair;DNA binding;DNA damage response","PubMed.ID":16223728,"subunits.Protein.name.":"DNA damage-binding protein 1;DNA damage-binding protein 2","subunits.Gene.name.":"DDB1;DDB2","subunits.Gene.name.syn.":"XAP1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":791,"ComplexName":"SNARE complex (Vamp2, Snap25, Stx1a, Cplx1)","Organism":"Rat","Synonyms":"Complexin I complex","Cell.line":"brain","subunits.UniProt.IDs.":"P32851;P60881;P63041;P63045","subunits.Entrez.IDs.":"116470;25012;64832;24803","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030545;GO:0006906;GO:0048489;GO:0016079;GO:0005102","GO.description":"receptor regulator activity;vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis;receptor binding","FunCat.ID":"18.02.07;20.09.07.27;20.09.16.09.05;16.01.01","FunCat.description":"regulator of receptor activity;vesicle fusion;synaptic vesicle exocytosis;receptor binding","PubMed.ID":7553862,"subunits.Protein.name.":"Syntaxin-1A;Synaptosomal-associated protein 25;Complexin-1;Vesicle-associated membrane protein 2","subunits.Gene.name.":"Stx1a;Snap25;Cplx1;Vamp2","subunits.Gene.name.syn.":"Sap;Snap;None;Syb2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":792,"ComplexName":"SNARE complex (Vamp2, Snap25, Cplx2, Stx1a)","Organism":"Rat","Synonyms":"Complexin II complex","Cell.line":"brain","subunits.UniProt.IDs.":"P32851;P60881;P63045;P84087","subunits.Entrez.IDs.":"116470;25012;24803;116657","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030545;GO:0006906;GO:0048489;GO:0016079;GO:0005102","GO.description":"receptor regulator activity;vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis;receptor binding","FunCat.ID":"18.02.07;20.09.07.27;20.09.16.09.05;16.01.01","FunCat.description":"regulator of receptor activity;vesicle fusion;synaptic vesicle exocytosis;receptor binding","PubMed.ID":7553862,"subunits.Protein.name.":"Syntaxin-1A;Synaptosomal-associated protein 25;Vesicle-associated membrane protein 2;Complexin-2","subunits.Gene.name.":"Stx1a;Snap25;Vamp2;Cplx2","subunits.Gene.name.syn.":"Sap;Snap;Syb2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":793,"ComplexName":"SNARE complex (VAMP2, SNAP25, STX1a, CPLX1)","Organism":"Human","Synonyms":"Complexin I complex","Cell.line":"brain","subunits.UniProt.IDs.":"O14810;P60880;P63027;Q16623","subunits.Entrez.IDs.":"10815;6616;6844;6804","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030545;GO:0006906;GO:0048489;GO:0016079;GO:0005102","GO.description":"receptor regulator activity;vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis;receptor binding","FunCat.ID":"18.02.07;20.09.07.27;20.09.16.09.05;16.01.01","FunCat.description":"regulator of receptor activity;vesicle fusion;synaptic vesicle exocytosis;receptor binding","PubMed.ID":7553862,"subunits.Protein.name.":"Complexin-1 ;Synaptosomal-associated protein 25 ;Vesicle-associated membrane protein 2 ;Syntaxin-1A","subunits.Gene.name.":"CPLX1;SNAP25;VAMP2;STX1A","subunits.Gene.name.syn.":";SNAP;SYB2;STX1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":794,"ComplexName":"SNARE complex (VAMP2, SNAP25, STX1a, CPLX2)","Organism":"Human","Synonyms":"Complexin II complex","Cell.line":"brain","subunits.UniProt.IDs.":"P60880;P63027;Q16623;Q6PUV4","subunits.Entrez.IDs.":"6616;6844;6804;10814","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030545;GO:0006906;GO:0048489;GO:0016079;GO:0005102","GO.description":"receptor regulator activity;vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis;receptor binding","FunCat.ID":"18.02.07;20.09.07.27;20.09.16.09.05;16.01.01","FunCat.description":"regulator of receptor activity;vesicle fusion;synaptic vesicle exocytosis;receptor binding","PubMed.ID":7553862,"subunits.Protein.name.":"Synaptosomal-associated protein 25 ;Vesicle-associated membrane protein 2 ;Syntaxin-1A ;Complexin-2","subunits.Gene.name.":"SNAP25;VAMP2;STX1A;CPLX2","subunits.Gene.name.syn.":"SNAP;SYB2;STX1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":795,"ComplexName":"SNARE complex (Vamp2, Snap25, Stx1a, Cplx1)","Organism":"Mouse","Synonyms":"Complexin I complex","Cell.line":"brain","subunits.UniProt.IDs.":"O35526;P60879;P63040;P63044","subunits.Entrez.IDs.":"20907;20614;12889;22318","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030545;GO:0006906;GO:0048489;GO:0016079;GO:0005102","GO.description":"receptor regulator activity;vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis;receptor binding","FunCat.ID":"18.02.07;20.09.07.27;20.09.16.09.05;16.01.01","FunCat.description":"regulator of receptor activity;vesicle fusion;synaptic vesicle exocytosis;receptor binding","PubMed.ID":7553862,"subunits.Protein.name.":"Syntaxin-1A ;Synaptosomal-associated protein 25 ;Complexin-1 ;Vesicle-associated membrane protein 2","subunits.Gene.name.":"Stx1a;Snap25;Cplx1;Vamp2","subunits.Gene.name.syn.":";Snap;;Syb2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":796,"ComplexName":"SNARE complex (Vamp2, Snap25, Stx1a, Cplx2)","Organism":"Mouse","Synonyms":"Complexin II complex","Cell.line":"brain","subunits.UniProt.IDs.":"O35526;P60879;P63044;P84086","subunits.Entrez.IDs.":"20907;20614;22318;12890","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030545;GO:0006906;GO:0048489;GO:0016079;GO:0005102","GO.description":"receptor regulator activity;vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis;receptor binding","FunCat.ID":"18.02.07;20.09.07.27;20.09.16.09.05;16.01.01","FunCat.description":"regulator of receptor activity;vesicle fusion;synaptic vesicle exocytosis;receptor binding","PubMed.ID":7553862,"subunits.Protein.name.":"Syntaxin-1A ;Synaptosomal-associated protein 25 ;Vesicle-associated membrane protein 2 ;Complexin-2","subunits.Gene.name.":"Stx1a;Snap25;Vamp2;Cplx2","subunits.Gene.name.syn.":";Snap;Syb2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":797,"ComplexName":"SNARE complex (STX11, VAMP2, SNAP23)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00161;O75558;P63027","subunits.Entrez.IDs.":"8773;8676;6844","Protein.complex.purification.method":"MI:0018- two hybrid; MI:0019- coimmunoprecipitation","GO.ID":"GO:0015031;GO:0008565;GO:0006906;GO:0048489;GO:0016079;GO:0005768","GO.description":"protein transport;protein transporter activity;vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis;endosome","FunCat.ID":"20.01.10;20.09.07.27;20.09.16.09.05;70.22","FunCat.description":"protein transport;vesicle fusion;synaptic vesicle exocytosis;endosome","PubMed.ID":10036234,"subunits.Protein.name.":"Synaptosomal-associated protein 23;Syntaxin-11;Vesicle-associated membrane protein 2","subunits.Gene.name.":"SNAP23;STX11;VAMP2","subunits.Gene.name.syn.":"None;;SYB2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":798,"ComplexName":"NuA4/Tip60-HAT complex A","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95619;O96019;Q52LR7;Q92993;Q96L91;Q9H0E9;Q9H2F5;Q9HAF1;Q9NPF5;Q9NV56;Q9NXR8;Q9UBU8;Q9Y230;Q9Y265;Q9Y4A5","subunits.Entrez.IDs.":"8089;86;26122;10524;57634;10902;80314;64769;55929;55257;54556;10933;10856;8607;8295","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006794;GO:0006796;GO:0051276;GO:0006281;GO:0006265;GO:0006473;GO:0006476;GO:0003677;GO:0006974;GO:0051276;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;chromosome organization;DNA repair;DNA topological change;protein acetylation;protein deacetylation;DNA binding;cellular response to DNA damage stimulus;chromosome organization;nucleus","FunCat.ID":"01.04;42.10.03;10.01.05.01;10.01.09.05;14.07.04;16.03.01;32.01.09;70.10","FunCat.description":"phosphate metabolism;organization of chromosome structure;DNA repair;DNA conformation modification (e.g. chromatin);modification by acetylation, deacetylation;DNA binding;DNA damage response;nucleus","PubMed.ID":14966270,"subunits.Protein.name.":"YEATS domain-containing protein 4;Actin-like protein 6A;Enhancer of polycomb homolog 2;Histone acetyltransferase KAT5;E1A-binding protein p400;Bromodomain-containing protein 8;Enhancer of polycomb homolog 1;Chromatin modification-related protein MEAF6;DNA methyltransferase 1-associated protein 1;MRG/MORF4L-binding protein ;Inhibitor of growth protein 3;Mortality factor 4-like protein 1;RuvB-like 2;RuvB-like 1;Transformation/transcription domain-associated protein","subunits.Gene.name.":"YEATS4;ACTL6A;EPC2;KAT5;EP400;BRD8;EPC1;MEAF6;DMAP1;MRGBP;ING3;MORF4L1;RUVBL2;RUVBL1;TRRAP","subunits.Gene.name.syn.":"GAS41;BAF53 BAF53A INO80K;None;HTATIP TIP60;CAGH32 KIAA1498 KIAA1818 TNRC12;SMAP SMAP2;None;C1orf149 CENP-28 EAF6;KIAA1425;C20orf20;None;MRG15;INO80J TIP48 TIP49B;INO80H NMP238 TIP49 TIP49A;PAF400","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The NuA4 histone acetyltransferase (HAT) multisubunit complex is responsible for acetylation of histone H4 and H2A N-terminal tails in yeast. The NuA4/Tip60 HAT complex is highly conserved in eukaryotes playing primary roles in transcription, cellular response to DNA damage, and cell cycle control.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":799,"ComplexName":"DMAP1-associated complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O96019;Q15906;Q6ZRS2;Q96L91;Q9H0E9;Q9H2F5;Q9NPF5;Q9Y230;Q9Y265;Q9Y4A5","subunits.Entrez.IDs.":"86;6944;10847;57634;10902;80314;55929;10856;8607;8295","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006794;GO:0006796;GO:0051276;GO:0006281;GO:0006265;GO:0051276;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;chromosome organization;DNA repair;DNA topological change;chromosome organization;nucleus","FunCat.ID":"01.04;42.10.03;10.01.05.01;10.01.09.05;70.10","FunCat.description":"phosphate metabolism;organization of chromosome structure;DNA repair;DNA conformation modification (e.g. chromatin);nucleus","PubMed.ID":14966270,"subunits.Protein.name.":"Actin-like protein 6A;Vacuolar protein sorting-associated protein 72 homolog ;Helicase SRCAP ;E1A-binding protein p400;Bromodomain-containing protein 8;Enhancer of polycomb homolog 1;DNA methyltransferase 1-associated protein 1;RuvB-like 2;RuvB-like 1;Transformation/transcription domain-associated protein","subunits.Gene.name.":"ACTL6A;VPS72;SRCAP;EP400;BRD8;EPC1;DMAP1;RUVBL2;RUVBL1;TRRAP","subunits.Gene.name.syn.":"BAF53 BAF53A INO80K;TCFL1 YL1;KIAA0309;CAGH32 KIAA1498 KIAA1818 TNRC12;SMAP SMAP2;None;KIAA1425;INO80J TIP48 TIP49B;INO80H NMP238 TIP49 TIP49A;PAF400","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":800,"ComplexName":"DNMT1-HDAC2-DMAP1 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"P13864;P70288;Q9JI44","subunits.Entrez.IDs.":"13433;15182;66233","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0006306;GO:0045892;GO:0032774;GO:0005634","GO.description":"DNA methylation;negative regulation of transcription, DNA-templated;RNA biosynthetic process;nucleus","FunCat.ID":"10.01.09.01;11.02.03.04.03;11.02;70.10","FunCat.description":"DNA methylation;transcription repression;RNA synthesis;nucleus","PubMed.ID":10888872,"subunits.Protein.name.":"DNA ;Histone deacetylase 2;DNA methyltransferase 1-associated protein 1","subunits.Gene.name.":"Dnmt1;Hdac2;Dmap1","subunits.Gene.name.syn.":"Dnmt Met1 Uim;Yy1bp;Mmtr","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":801,"ComplexName":"SNARE complex (STX2, SNAP23)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00161;P32856","subunits.Entrez.IDs.":"8773;2054","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":10648404,"subunits.Protein.name.":"Synaptosomal-associated protein 23;Syntaxin-2","subunits.Gene.name.":"SNAP23;STX2","subunits.Gene.name.syn.":"None;EPIM STX2A STX2B STX2C","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":802,"ComplexName":"Cdc42-Par6b-Par3-Prkci complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS-7 cells","subunits.UniProt.IDs.":"P60766;Q62074;Q99NH2;Q9JK83","subunits.Entrez.IDs.":"12540;18759;93742;58220","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0007264;GO:0051211;GO:0009798;GO:0007043;GO:0030054","GO.description":"small GTPase mediated signal transduction;anisotropic cell growth;axis specification;cell-cell junction assembly;cell junction","FunCat.ID":"30.01.05.05.01;40.01.03;41.05.19;42.06.04;70.06","FunCat.description":"small GTPase mediated signal transduction;directional cell growth (morphogenesis);asymmetries and axis determination;intercellular junction (gap junction/adherens junction);cell junction","PubMed.ID":10934474,"subunits.Protein.name.":"Cell division control protein 42 homolog;Protein kinase C iota type;Partitioning defective 3 homolog;Partitioning defective 6 homolog beta","subunits.Gene.name.":"Cdc42;Prkci;Pard3;Pard6b","subunits.Gene.name.syn.":"None;Pkcl, aPKClambda;Par3;Par6b","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results indicate that Cdc42, in the GTP-bound state, links to the Par3-PKC-lambda/iota complex through Par6.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":803,"ComplexName":"BRG1-SIN3A-HDAC containing SWI/SNF remodeling complex I","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14497;O14744;O96019;P51532;Q12824;Q8TAQ2;Q92769;Q92922;Q969G3;Q96GM5;Q96ST3","subunits.Entrez.IDs.":"8289;10419;86;6597;6598;6601;3066;6599;6605;6602;25942","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0004- affinity chromatography technologies; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006265;GO:2001141;GO:0006355;GO:0006473;GO:0006476;GO:0018126;GO:0006479;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;protein hydroxylation;protein methylation;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04;14.07.04;14.07.09;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcriptional control;modification by acetylation, deacetylation;posttranslational modification of amino acids (e.g. hydroxylation, methylation);DNA binding;organization of chromosome structure;nucleus","PubMed.ID":14559996,"subunits.Protein.name.":"AT-rich interactive domain-containing protein 1A;Protein arginine N-methyltransferase 5;Actin-like protein 6A;Transcription activator BRG1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;SWI/SNF complex subunit SMARCC2;Histone deacetylase 2;SWI/SNF complex subunit SMARCC1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1;Paired amphipathic helix protein Sin3a","subunits.Gene.name.":"ARID1A;PRMT5;ACTL6A;SMARCA4;SMARCB1;SMARCC2;HDAC2;SMARCC1;SMARCE1;SMARCD1;SIN3A","subunits.Gene.name.syn.":"BAF250 BAF250A C1orf4 OSA1 SMARCF1;HRMT1L5 IBP72 JBP1 SKB1;BAF53 BAF53A INO80K;BAF190A BRG1 SNF2B SNF2L4;BAF47, INI1, SNF5L1;BAF170;None;BAF155;BAF57;BAF60A;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors provide evidence, that PRMT5, mSin3A/HDAC2, and the Brg1-based hSWI/SNF complex are involved in cad transcriptional repression.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":804,"ComplexName":"CDC42-Par6c-Par3-Prkcz complex","Organism":"Dog","Synonyms":"None","Cell.line":"epithelium","subunits.UniProt.IDs.":"P60952;Q02956;Q99NH2;Q9Z101","subunits.Entrez.IDs.":"403934;18762;93742;56513","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0007264;GO:0051211;GO:0009798;GO:0007043;GO:0030054","GO.description":"small GTPase mediated signal transduction;anisotropic cell growth;axis specification;cell-cell junction assembly;cell junction","FunCat.ID":"30.01.05.05.01;40.01.03;41.05.19;42.06.04;70.06","FunCat.description":"small GTPase mediated signal transduction;directional cell growth (morphogenesis);asymmetries and axis determination;intercellular junction (gap junction/adherens junction);cell junction","PubMed.ID":10934474,"subunits.Protein.name.":"Cell division control protein 42 homolog ;Protein kinase C zeta type ;Partitioning defective 3 homolog;Partitioning defective 6 homolog alpha","subunits.Gene.name.":"CDC42;Prkcz;Pard3;Pard6a","subunits.Gene.name.syn.":";Pkcz;Par3;Par6a","Disease.comment":"None","Subunits.comment":"Since Prkcz, Pard6a and Pard3 from dog were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.","Complex.comment":"Only activated Cdc42 was able to bind to all three endogenous proteins.","SWISSPROT.organism":"Canis lupus familiaris (Dog) (Canis familiaris);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":805,"ComplexName":"SNARE complex (STX4, SNAP23)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00161;Q12846","subunits.Entrez.IDs.":"8773;6810","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":10961877,"subunits.Protein.name.":"Synaptosomal-associated protein 23;Syntaxin-4","subunits.Gene.name.":"SNAP23;STX4","subunits.Gene.name.syn.":"None;STX4A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":806,"ComplexName":"BRM-SIN3A-HDAC complex","Organism":"Human","Synonyms":"BRM-Sin3A-HDAC containing SWI/SNF remodeling complex","Cell.line":"None","subunits.UniProt.IDs.":"O14497;O14744;O96019;P51531;Q12824;Q8TAQ2;Q92769;Q92922;Q92925;Q969G3;Q96GM5;Q96ST3","subunits.Entrez.IDs.":"8289;10419;86;6595;6598;6601;3066;6599;6603;6605;6602;25942","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0004- affinity chromatography technologies; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006265;GO:2001141;GO:0006355;GO:0006473;GO:0006476;GO:0018126;GO:0006479;GO:0051276;GO:0005634","GO.description":"DNA topological change;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;protein hydroxylation;protein methylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04;14.07.04;14.07.09;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcriptional control;modification by acetylation, deacetylation;posttranslational modification of amino acids (e.g. hydroxylation, methylation);organization of chromosome structure;nucleus","PubMed.ID":14559996,"subunits.Protein.name.":"AT-rich interactive domain-containing protein 1A;Protein arginine N-methyltransferase 5;Actin-like protein 6A;Probable global transcription activator SNF2L2;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;SWI/SNF complex subunit SMARCC2;Histone deacetylase 2;SWI/SNF complex subunit SMARCC1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1;Paired amphipathic helix protein Sin3a","subunits.Gene.name.":"ARID1A;PRMT5;ACTL6A;SMARCA2;SMARCB1;SMARCC2;HDAC2;SMARCC1;SMARCD2;SMARCE1;SMARCD1;SIN3A","subunits.Gene.name.syn.":"BAF250 BAF250A C1orf4 OSA1 SMARCF1;HRMT1L5 IBP72 JBP1 SKB1;BAF53 BAF53A INO80K;BAF190B, BRM, SNF2A, SNF2L2;BAF47, INI1, SNF5L1;BAF170;None;BAF155;BAF60B;BAF57;BAF60A;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":807,"ComplexName":"BRG1-associated complex","Organism":"Human","Synonyms":"BRG1 containing SWI/SNF remodeling complex","Cell.line":"None","subunits.UniProt.IDs.":"O14497;O14744;O96019;P51532;Q12824;Q8TAQ2;Q92922;Q969G3;Q96GM5","subunits.Entrez.IDs.":"8289;10419;86;6597;6598;6601;6599;6605;6602","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0004- affinity chromatography technologies","GO.ID":"GO:0006265;GO:2001141;GO:0006355;GO:0018126;GO:0006479;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein hydroxylation;protein methylation;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04;14.07.09;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcriptional control;posttranslational modification of amino acids (e.g. hydroxylation, methylation);DNA binding;organization of chromosome structure;nucleus","PubMed.ID":14559996,"subunits.Protein.name.":"AT-rich interactive domain-containing protein 1A;Protein arginine N-methyltransferase 5;Actin-like protein 6A;Transcription activator BRG1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;SWI/SNF complex subunit SMARCC2;SWI/SNF complex subunit SMARCC1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","subunits.Gene.name.":"ARID1A;PRMT5;ACTL6A;SMARCA4;SMARCB1;SMARCC2;SMARCC1;SMARCE1;SMARCD1","subunits.Gene.name.syn.":"BAF250 BAF250A C1orf4 OSA1 SMARCF1;HRMT1L5 IBP72 JBP1 SKB1;BAF53 BAF53A INO80K;BAF190A BRG1 SNF2B SNF2L4;BAF47, INI1, SNF5L1;BAF170;BAF155;BAF57;BAF60A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":808,"ComplexName":"BRM-associated complex","Organism":"Human","Synonyms":"BRM containing SWI/SNF remodeling complex","Cell.line":"None","subunits.UniProt.IDs.":"O14497;O14744;O96019;P51531;Q12824;Q8TAQ2;Q92922;Q92925;Q969G3;Q96GM5","subunits.Entrez.IDs.":"8289;10419;86;6595;6598;6601;6599;6603;6605;6602","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0004- affinity chromatography technologies","GO.ID":"GO:0006265;GO:2001141;GO:0006355;GO:0018126;GO:0006479;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein hydroxylation;protein methylation;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04;14.07.09;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcriptional control;posttranslational modification of amino acids (e.g. hydroxylation, methylation);DNA binding;organization of chromosome structure;nucleus","PubMed.ID":14559996,"subunits.Protein.name.":"AT-rich interactive domain-containing protein 1A;Protein arginine N-methyltransferase 5;Actin-like protein 6A;Probable global transcription activator SNF2L2;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;SWI/SNF complex subunit SMARCC2;SWI/SNF complex subunit SMARCC1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","subunits.Gene.name.":"ARID1A;PRMT5;ACTL6A;SMARCA2;SMARCB1;SMARCC2;SMARCC1;SMARCD2;SMARCE1;SMARCD1","subunits.Gene.name.syn.":"BAF250 BAF250A C1orf4 OSA1 SMARCF1;HRMT1L5 IBP72 JBP1 SKB1;BAF53 BAF53A INO80K;BAF190B, BRM, SNF2A, SNF2L2;BAF47, INI1, SNF5L1;BAF170;BAF155;BAF60B;BAF57;BAF60A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":809,"ComplexName":"eRF1-eRF3-GTP-Mg(2+) complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P15170;P62495","subunits.Entrez.IDs.":"2935;2107","Protein.complex.purification.method":"MI:0065-isothermal titration calorimetry","GO.ID":"GO:0006415;GO:0000287;GO:0005525;GO:0007264;GO:0005737","GO.description":"translational termination;magnesium ion binding;GTP binding;small GTPase mediated signal transduction;cytoplasm","FunCat.ID":"12.04.03;16.17.07;16.19.05;30.01.05.05.01;70.03","FunCat.description":"translation termination;magnesium binding;GTP binding;small GTPase mediated signal transduction;cytoplasm","PubMed.ID":16914449,"subunits.Protein.name.":"Eukaryotic peptide chain release factor GTP-binding subunit ERF3A;Eukaryotic peptide chain release factor subunit 1","subunits.Gene.name.":"GSPT1;ETF1","subunits.Gene.name.syn.":"ERF3A;ERF1, RF1, SUP45L1","Disease.comment":"None","Subunits.comment":"Since the authors did not specify ERF3 , we used isoform ERF3A.","Complex.comment":"eRF3 binds GDP independently of the presence or absence of eRF1 whereas GTP binds only to the eRF1-eRF3 complex. The authors suggest that the quaternary eRF1-eRF3-GTP-Mg2+ complex binds to the ribosomal pretermination complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":810,"ComplexName":"FCP1-associated protein complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14744;P30876;P35269;P84090;Q15208;Q9BQA1;Q9Y5B0","subunits.Entrez.IDs.":"10419;5431;2962;2079;11329;79084;9150","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006354;GO:0018126;GO:0006479;GO:0005634","GO.description":"DNA-templated transcription, elongation;protein hydroxylation;protein methylation;nucleus","FunCat.ID":"11.02.03.01.04;14.07.09;70.10","FunCat.description":"transcription elongation;posttranslational modification of amino acids (e.g. hydroxylation, methylation);nucleus","PubMed.ID":15670829,"subunits.Protein.name.":"Protein arginine N-methyltransferase 5;DNA-directed RNA polymerase II subunit RPB2 ;General transcription factor IIF subunit 1;Enhancer of rudimentary homolog;Serine/threonine-protein kinase 38 ;Methylosome protein 50 ;RNA polymerase II subunit A C-terminal domain phosphatase","subunits.Gene.name.":"PRMT5;POLR2B;GTF2F1;ERH;STK38;WDR77;CTDP1","subunits.Gene.name.syn.":"HRMT1L5 IBP72 JBP1 SKB1;;RAP74;;NDR1;MEP50 WD45;FCP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"FCP1-associated PRMT5 can methylate histones H4 in vitro.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":811,"ComplexName":"FCP1-associated protein complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14744;P30876;P35269;P84090;Q15208;Q9BQA1;Q9Y5B0","subunits.Entrez.IDs.":"10419;5431;2962;2079;11329;79084;9150","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006354;GO:0018126;GO:0006479;GO:0005634","GO.description":"DNA-templated transcription, elongation;protein hydroxylation;protein methylation;nucleus","FunCat.ID":"11.02.03.01.04;14.07.09;70.10","FunCat.description":"transcription elongation;posttranslational modification of amino acids (e.g. hydroxylation, methylation);nucleus","PubMed.ID":12560496,"subunits.Protein.name.":"Protein arginine N-methyltransferase 5;DNA-directed RNA polymerase II subunit RPB2 ;General transcription factor IIF subunit 1;Enhancer of rudimentary homolog;Serine/threonine-protein kinase 38 ;Methylosome protein 50 ;RNA polymerase II subunit A C-terminal domain phosphatase","subunits.Gene.name.":"PRMT5;POLR2B;GTF2F1;ERH;STK38;WDR77;CTDP1","subunits.Gene.name.syn.":"HRMT1L5 IBP72 JBP1 SKB1;;RAP74;;NDR1;MEP50 WD45;FCP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors suggest a putative role of FCP1 CTD-phosphatase in linking the transcription elongation with the splicing process.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":812,"ComplexName":"Upf complex (UPF1, UPF2, UPF3a)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q92900;Q9H1J1;Q9HAU5","subunits.Entrez.IDs.":"5976;65110;26019","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006401;GO:0003723;GO:0005737;GO:0016363","GO.description":"RNA catabolic process;RNA binding;cytoplasm;nuclear matrix","FunCat.ID":"01.03.16.01;16.03.03;70.03;70.10.06","FunCat.description":"RNA degradation;RNA binding;cytoplasm;nuclear matrix","PubMed.ID":11163187,"subunits.Protein.name.":"Regulator of nonsense transcripts 1;Regulator of nonsense transcripts 3A ;Regulator of nonsense transcripts 2","subunits.Gene.name.":"UPF1;UPF3A;UPF2","subunits.Gene.name.syn.":"KIAA0221, RENT1;RENT3A UPF3;KIAA1408, RENT2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Human Upf proteins target mRNA for nonsense-mediated decay when bound downstream of a termination codon. Nonsense-mediated decay (NMD) rids eukaryotic cells of aberrant mRNAs containing premature termination codons. These are discriminated from true termination codons by downstream cis-elements, such as exon-exon junctions.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":813,"ComplexName":"Upf complex (UPF1, UPF2, UPF3b)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q92900;Q9BZI7;Q9HAU5","subunits.Entrez.IDs.":"5976;65109;26019","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006401;GO:0003723;GO:0005737;GO:0016363","GO.description":"RNA catabolic process;RNA binding;cytoplasm;nuclear matrix","FunCat.ID":"01.03.16.01;16.03.03;70.03;70.10.06","FunCat.description":"RNA degradation;RNA binding;cytoplasm;nuclear matrix","PubMed.ID":11163187,"subunits.Protein.name.":"Regulator of nonsense transcripts 1;Regulator of nonsense transcripts 3B;Regulator of nonsense transcripts 2","subunits.Gene.name.":"UPF1;UPF3B;UPF2","subunits.Gene.name.syn.":"KIAA0221, RENT1;RENT3B, UPF3X;KIAA1408, RENT2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Human Upf proteins target mRNA for nonsense-mediated decay when bound downstream of a termination codon. Nonsense-mediated decay (NMD) rids eukaryotic cells of aberrant mRNAs containing premature termination codons. These are discriminated from true termination codons by downstream cis-elements, such as exon-exon junctions.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":814,"ComplexName":"Postsplicing complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q15287;Q92900;Q9BZI7;Q9H1J1;Q9HAU5;Q9UBU9;Q9Y5S9","subunits.Entrez.IDs.":"10921;5976;65109;65110;26019;10482;9939","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006401;GO:0003723;GO:0016363","GO.description":"RNA catabolic process;RNA binding;nuclear matrix","FunCat.ID":"01.03.16.01;16.03.03;70.10.06","FunCat.description":"RNA degradation;RNA binding;nuclear matrix","PubMed.ID":11546874,"subunits.Protein.name.":"RNA-binding protein with serine-rich domain 1 ;Regulator of nonsense transcripts 1;Regulator of nonsense transcripts 3B;Regulator of nonsense transcripts 3A ;Regulator of nonsense transcripts 2;Nuclear RNA export factor 1 ;RNA-binding protein 8A","subunits.Gene.name.":"RNPS1;UPF1;UPF3B;UPF3A;UPF2;NXF1;RBM8A","subunits.Gene.name.syn.":"LDC2;KIAA0221, RENT1;RENT3B, UPF3X;RENT3A UPF3;KIAA1408, RENT2;TAP;RBM8, Y14","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"A final quality-control step in mRNA maturation is mRNA surveillance. This process detects mRNAs with truncated open reading frames and subjects them to nonsense-mediated mRNA decay (NMD). The protein RNPS1, a component of the postsplicing complex that is deposited 5' to exon-exon junctions, interacts with the evolutionarily conserved human Upf complex, a central component of NMD.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":815,"ComplexName":"MRIP-MBS-RHOA complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14974;P61586;Q6WCQ1","subunits.Entrez.IDs.":"4659;387;23164","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006461;GO:0005515;GO:0030234;GO:0050790","GO.description":"protein complex assembly;protein binding;enzyme regulator activity;regulation of catalytic activity","FunCat.ID":"14.10;16.01;18.02.01","FunCat.description":"assembly of protein complexes;protein binding;enzymatic activity regulation / enzyme regulator","PubMed.ID":14506264,"subunits.Protein.name.":"Protein phosphatase 1 regulatory subunit 12A ;Transforming protein RhoA ;Myosin phosphatase Rho-interacting protein","subunits.Gene.name.":"PPP1R12A;RHOA;MPRIP","subunits.Gene.name.syn.":"MBS MYPT1;ARH12 ARHA RHO12;KIAA0864 MRIP RHOIP3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":816,"ComplexName":"MRIP-RHOA complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P61586;Q6WCQ1","subunits.Entrez.IDs.":"387;23164","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0005515","GO.description":"protein binding","FunCat.ID":"16.01","FunCat.description":"protein binding","PubMed.ID":14506264,"subunits.Protein.name.":"Transforming protein RhoA ;Myosin phosphatase Rho-interacting protein","subunits.Gene.name.":"RHOA;MPRIP","subunits.Gene.name.syn.":"ARH12 ARHA RHO12;KIAA0864 MRIP RHOIP3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":817,"ComplexName":"MRIP-MBS complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14974;Q6WCQ1","subunits.Entrez.IDs.":"4659;23164","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0005515","GO.description":"protein binding","FunCat.ID":"16.01","FunCat.description":"protein binding","PubMed.ID":14506264,"subunits.Protein.name.":"Protein phosphatase 1 regulatory subunit 12A ;Myosin phosphatase Rho-interacting protein","subunits.Gene.name.":"PPP1R12A;MPRIP","subunits.Gene.name.syn.":"MBS MYPT1;KIAA0864 MRIP RHOIP3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":819,"ComplexName":"20S methylosome-SmD complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14744;P54105;P62314;P62318","subunits.Entrez.IDs.":"10419;1207;6632;6634","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0004- affinity chromatography technologies","GO.ID":"GO:0018126;GO:0006479;GO:0006461;GO:0005737","GO.description":"protein hydroxylation;protein methylation;protein complex assembly;cytoplasm","FunCat.ID":"14.07.09;14.10;70.03","FunCat.description":"posttranslational modification of amino acids (e.g. hydroxylation, methylation);assembly of protein complexes;cytoplasm","PubMed.ID":11713266,"subunits.Protein.name.":"Protein arginine N-methyltransferase 5;Methylosome subunit pICln ;Small nuclear ribonucleoprotein Sm D1 ;Small nuclear ribonucleoprotein Sm D3","subunits.Gene.name.":"PRMT5;CLNS1A;SNRPD1;SNRPD3","subunits.Gene.name.syn.":"HRMT1L5 IBP72 JBP1 SKB1;CLCI ICLN;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"PRMT5 and pICln bind only to unmethylated SMD1 and SMD3.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":820,"ComplexName":"SNARE complex (STX6, SNAP23)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00161;O43752","subunits.Entrez.IDs.":"8773;10228","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":11001914,"subunits.Protein.name.":"Synaptosomal-associated protein 23;Syntaxin-6","subunits.Gene.name.":"SNAP23;STX6","subunits.Gene.name.syn.":"None;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":821,"ComplexName":"Par-3-VE-cadherin-alpha-beta-catenin complex","Organism":"Hamster","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P26231;P55284;Q02248;Q99NH2","subunits.Entrez.IDs.":"12385;12562;12387;93742","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0051211;GO:0009798;GO:0007043;GO:0030054","GO.description":"anisotropic cell growth;axis specification;cell-cell junction assembly;cell junction","FunCat.ID":"40.01.03;41.05.19;42.06.04;70.06","FunCat.description":"directional cell growth (morphogenesis);asymmetries and axis determination;intercellular junction (gap junction/adherens junction);cell junction","PubMed.ID":17057644,"subunits.Protein.name.":"Catenin alpha-1 ;Cadherin-5 ;Catenin beta-1;Partitioning defective 3 homolog","subunits.Gene.name.":"Ctnna1;Cdh5;Ctnnb1;Pard3","subunits.Gene.name.syn.":"Catna1;;Catnb;Par3","Disease.comment":"None","Subunits.comment":"Since  Ctnna1, Ctnnb1, Cdh5 and Pard3 from hamster were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.","Complex.comment":"The authors show that both PAR-3 and PAR-6 can directly and independently associate with VE-cadherin, and that both are recruited to cell-cell contacts independently of each other.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":822,"ComplexName":"mRNA decay complex (UPF1, UPF2, UPF3B, DCP2, XRN1, XRN2, EXOSC2, EXOSC4, EXOSC10, PARN)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95453;Q01780;Q13868;Q8IU60;Q8IZH2;Q92900;Q9BZI7;Q9H0D6;Q9HAU5;Q9NPD3","subunits.Entrez.IDs.":"5073;5394;23404;167227;54464;5976;65109;22803;26019;54512","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006401;GO:0003723;GO:0005737;GO:0005634","GO.description":"RNA catabolic process;RNA binding;cytoplasm;nucleus","FunCat.ID":"01.03.16.01;16.03.03;70.03;70.10","FunCat.description":"RNA degradation;RNA binding;cytoplasm;nucleus","PubMed.ID":14527413,"subunits.Protein.name.":"Poly;Exosome component 10 ;Exosome complex component RRP4 ;m7GpppN-mRNA hydrolase ;5'-3' exoribonuclease 1 ;Regulator of nonsense transcripts 1;Regulator of nonsense transcripts 3B;5'-3' exoribonuclease 2 ;Regulator of nonsense transcripts 2;Exosome complex component RRP41","subunits.Gene.name.":"PARN;EXOSC10;EXOSC2;DCP2;XRN1;UPF1;UPF3B;XRN2;UPF2;EXOSC4","subunits.Gene.name.syn.":"DAN;PMSCL PMSCL2 RRP6;RRP4;NUDT20;SEP1;KIAA0221, RENT1;RENT3B, UPF3X;;KIAA1408, RENT2;RRP41 SKI6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"From experiments, it is concluded that nonsense-mediated mRNA decay (NMD) in mammalian cells degrades mRNAs from both 5' and 3' ends by recruiting decapping and 5'-->3' exonuclease activities as well as deadenylating and 3'-->5' exonuclease activities. All these activities are present within the mRNA decay complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":823,"ComplexName":"PAR-3-VE-cadherin complex, endothelial","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P55284;Q99NH2","subunits.Entrez.IDs.":"12562;93742","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0051211;GO:0007043","GO.description":"anisotropic cell growth;cell-cell junction assembly","FunCat.ID":"40.01.03;42.06.04","FunCat.description":"directional cell growth (morphogenesis);intercellular junction (gap junction/adherens junction)","PubMed.ID":17057644,"subunits.Protein.name.":"Cadherin-5 ;Partitioning defective 3 homolog","subunits.Gene.name.":"Cdh5;Pard3","subunits.Gene.name.syn.":";Par3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex isolated from microvascular endothelial monolayers from mouse myocardium (myEnd). Transient transfection experiments confirmed that the recruitment of PAR-3 by VE-cadherin in living cells is mediated through the PDZ-domain-binding motif of VE-cadherin and PDZ domain 3 of PAR-3.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":824,"ComplexName":"Anti-SMN protein complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14893;P14678;P57678;Q16637;Q9UHI6","subunits.Entrez.IDs.":"8487;6628;50628;None;11218","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0008380;GO:0006461;GO:0005737","GO.description":"RNA splicing;protein complex assembly;cytoplasm","FunCat.ID":"11.04.03.01;14.10;70.03","FunCat.description":"splicing;assembly of protein complexes;cytoplasm","PubMed.ID":11713266,"subunits.Protein.name.":"Gem-associated protein 2 ;Small nuclear ribonucleoprotein-associated proteins B and B' ;Gem-associated protein 4 ;Survival motor neuron protein;Probable ATP-dependent RNA helicase DDX20","subunits.Gene.name.":"GEMIN2;SNRPB;GEMIN4;SMN1; SMN2;DDX20","subunits.Gene.name.syn.":"SIP1;COD SNRPB1;;SMN; SMNT; SMNC;DP103 GEMIN3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":825,"ComplexName":"JBP1-pICln complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14744;P14678;P54105","subunits.Entrez.IDs.":"10419;6628;1207","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0018126;GO:0006479;GO:0006461;GO:0005737","GO.description":"protein hydroxylation;protein methylation;protein complex assembly;cytoplasm","FunCat.ID":"14.07.09;14.10;70.03","FunCat.description":"posttranslational modification of amino acids (e.g. hydroxylation, methylation);assembly of protein complexes;cytoplasm","PubMed.ID":11713266,"subunits.Protein.name.":"Protein arginine N-methyltransferase 5;Small nuclear ribonucleoprotein-associated proteins B and B' ;Methylosome subunit pICln","subunits.Gene.name.":"PRMT5;SNRPB;CLNS1A","subunits.Gene.name.syn.":"HRMT1L5 IBP72 JBP1 SKB1;COD SNRPB1;CLCI ICLN","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":826,"ComplexName":"PAR-3-VE-cadherin-beta-catenin complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"P33151;P35222;Q8TEW0","subunits.Entrez.IDs.":"1003;1499;56288","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0051211;GO:0007043;GO:0030054","GO.description":"anisotropic cell growth;cell-cell junction assembly;cell junction","FunCat.ID":"40.01.03;42.06.04;70.06","FunCat.description":"directional cell growth (morphogenesis);intercellular junction (gap junction/adherens junction);cell junction","PubMed.ID":17057644,"subunits.Protein.name.":"Cadherin-5;Catenin beta-1;Partitioning defective 3 homolog","subunits.Gene.name.":"CDH5;CTNNB1;PARD3","subunits.Gene.name.syn.":"None;CTNNB;PAR3, PAR3A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":827,"ComplexName":"NgR-TROY-LINGO1 complex","Organism":"Human","Synonyms":"None","Cell.line":"astrocytes, macrophages/microglia and neurones","subunits.UniProt.IDs.":"Q96FE5;Q9BZR6;Q9NS68","subunits.Entrez.IDs.":"84894;65078;55504","Protein.complex.purification.method":"MI:0051-fluorescence technologies","GO.ID":"GO:0005515","GO.description":"protein binding","FunCat.ID":"16.01","FunCat.description":"protein binding","PubMed.ID":17239012,"subunits.Protein.name.":"Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1 ;Reticulon-4 receptor ;Tumor necrosis factor receptor superfamily member 19","subunits.Gene.name.":"LINGO1;RTN4R;TNFRSF19","subunits.Gene.name.syn.":"LERN1 LRRN6A;NOGOR;TAJ TROY","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":828,"ComplexName":"TRPC1-STIM1-ORAI1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P48995;Q96D31;Q9UQB3","subunits.Entrez.IDs.":"7220;84876;1501","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0050789;GO:0008324;GO:0006812;GO:0005216;GO:0006875;GO:0005886","GO.description":"regulation of biological process;cation transmembrane transporter activity;cation transport;ion channel activity;cellular metal ion homeostasis;plasma membrane","FunCat.ID":"18;20.01.01.01;20.03.01.01;34.01.01.01;70.02","FunCat.description":"REGULATION OF METABOLISM AND PROTEIN FUNCTION;cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;homeostasis of metal ions (Na, K, Ca etc.);eukaryotic plasma membrane / membrane attached","PubMed.ID":17224452,"subunits.Protein.name.":"Short transient receptor potential channel 1 ;Calcium release-activated calcium channel protein 1 ;Catenin delta-2","subunits.Gene.name.":"TRPC1;ORAI1;CTNND2","subunits.Gene.name.syn.":"TRP1;CRACM1 TMEM142A;NPRAP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results show that all three proteins are essential for generation of TRPC1-SOC channels (store-operated calcium channels). The dynamic assembly of a TRPC1-STIM1-Orai1 complex is involved in activation of Ca2+ entry.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":829,"ComplexName":"PAR-6-VE-cadherin complex, endothelial","Organism":"Human","Synonyms":"PARD6A-VE-cadherin complex, endothelial","Cell.line":"None","subunits.UniProt.IDs.":"P33151;Q9NPB6","subunits.Entrez.IDs.":"1003;50855","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0051211;GO:0007043","GO.description":"anisotropic cell growth;cell-cell junction assembly","FunCat.ID":"40.01.03;42.06.04","FunCat.description":"directional cell growth (morphogenesis);intercellular junction (gap junction/adherens junction)","PubMed.ID":17057644,"subunits.Protein.name.":"Cadherin-5;Partitioning defective 6 homolog alpha","subunits.Gene.name.":"CDH5;PARD6A","subunits.Gene.name.syn.":"None;PAR6A, PAR6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":830,"ComplexName":"Trpc1-Stim1-Orai1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P84903;Q5M848;Q9QX01","subunits.Entrez.IDs.":"361618;304496;89821","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0050789;GO:0008324;GO:0006812;GO:0005216;GO:0006875;GO:0005886","GO.description":"regulation of biological process;cation transmembrane transporter activity;cation transport;ion channel activity;cellular metal ion homeostasis;plasma membrane","FunCat.ID":"18;20.01.01.01;20.03.01.01;34.01.01.01;70.02","FunCat.description":"REGULATION OF METABOLISM AND PROTEIN FUNCTION;cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;homeostasis of metal ions (Na, K, Ca etc.);eukaryotic plasma membrane / membrane attached","PubMed.ID":17224452,"subunits.Protein.name.":"Stromal interaction molecule 1;Calcium release-activated calcium channel protein 1 ;Short transient receptor potential channel 1","subunits.Gene.name.":"Stim1;Orai1;Trpc1","subunits.Gene.name.syn.":"Sim;Cracm1 Tmem142a;Trp1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results show that all three proteins are essential for generation of TRPC1-SOC channels (store-operated calcium channels). The dynamic assembly of a TRPC1-STIM1-Orai1 complex is involved in activation of Ca2+ entry.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":831,"ComplexName":"PAR-6-PAR-3-VE-cadherin complex, endothelial","Organism":"Human","Synonyms":"PARD6A-PAR-3-VE-cadherin complex, endothelial","Cell.line":"None","subunits.UniProt.IDs.":"P33151;Q8TEW0;Q9NPB6","subunits.Entrez.IDs.":"1003;56288;50855","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0051211;GO:0007043","GO.description":"anisotropic cell growth;cell-cell junction assembly","FunCat.ID":"40.01.03;42.06.04","FunCat.description":"directional cell growth (morphogenesis);intercellular junction (gap junction/adherens junction)","PubMed.ID":17057644,"subunits.Protein.name.":"Cadherin-5;Partitioning defective 3 homolog;Partitioning defective 6 homolog alpha","subunits.Gene.name.":"CDH5;PARD3;PARD6A","subunits.Gene.name.syn.":"None;PAR3, PAR3A;PAR6A, PAR6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"PAR-3 and PAR-6 are recruited independently to cell-cell contacts and the localization of PAR-6 at cell junctions requires fully matured cell-cell contacts.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":832,"ComplexName":"Anti-Sm protein complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14744;O14893;P14678;P54105;P57678;Q16637;Q9UHI6","subunits.Entrez.IDs.":"10419;8487;6628;1207;50628;None;11218","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0018126;GO:0006479;GO:0005737","GO.description":"protein hydroxylation;protein methylation;cytoplasm","FunCat.ID":"14.07.09;70.03","FunCat.description":"posttranslational modification of amino acids (e.g. hydroxylation, methylation);cytoplasm","PubMed.ID":11713266,"subunits.Protein.name.":"Protein arginine N-methyltransferase 5;Gem-associated protein 2 ;Small nuclear ribonucleoprotein-associated proteins B and B' ;Methylosome subunit pICln ;Gem-associated protein 4 ;Survival motor neuron protein;Probable ATP-dependent RNA helicase DDX20","subunits.Gene.name.":"PRMT5;GEMIN2;SNRPB;CLNS1A;GEMIN4;SMN1; SMN2;DDX20","subunits.Gene.name.syn.":"HRMT1L5 IBP72 JBP1 SKB1;SIP1;COD SNRPB1;CLCI ICLN;;SMN; SMNT; SMNC;DP103 GEMIN3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":833,"ComplexName":"6S methyltransferase complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P54105;P62314;P62318","subunits.Entrez.IDs.":"1207;6632;6634","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006461;GO:0005515;GO:0005737","GO.description":"protein complex assembly;protein binding;cytoplasm","FunCat.ID":"14.10;16.01;70.03","FunCat.description":"assembly of protein complexes;protein binding;cytoplasm","PubMed.ID":11713266,"subunits.Protein.name.":"Methylosome subunit pICln ;Small nuclear ribonucleoprotein Sm D1 ;Small nuclear ribonucleoprotein Sm D3","subunits.Gene.name.":"CLNS1A;SNRPD1;SNRPD3","subunits.Gene.name.syn.":"CLCI ICLN;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":834,"ComplexName":"20S methylosome and RG-containing Sm protein complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14744;P14678;P54105;P62314;P62316;P62318","subunits.Entrez.IDs.":"10419;6628;1207;6632;6633;6634","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0008380;GO:0018126;GO:0006479;GO:0005737","GO.description":"RNA splicing;protein hydroxylation;protein methylation;cytoplasm","FunCat.ID":"11.04.03.01;14.07.09;70.03","FunCat.description":"splicing;posttranslational modification of amino acids (e.g. hydroxylation, methylation);cytoplasm","PubMed.ID":11713266,"subunits.Protein.name.":"Protein arginine N-methyltransferase 5;Small nuclear ribonucleoprotein-associated proteins B and B' ;Methylosome subunit pICln ;Small nuclear ribonucleoprotein Sm D1 ;Small nuclear ribonucleoprotein Sm D2 ;Small nuclear ribonucleoprotein Sm D3","subunits.Gene.name.":"PRMT5;SNRPB;CLNS1A;SNRPD1;SNRPD2;SNRPD3","subunits.Gene.name.syn.":"HRMT1L5 IBP72 JBP1 SKB1;COD SNRPB1;CLCI ICLN;;SNRPD1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":835,"ComplexName":"6S methyltransferase and RG-containing Sm proteins complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P14678;P54105;P62304;P62306;P62308;P62314;P62316;P62318","subunits.Entrez.IDs.":"6628;1207;6635;6636;6637;6632;6633;6634","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0008380;GO:0005737","GO.description":"RNA splicing;cytoplasm","FunCat.ID":"11.04.03.01;70.03","FunCat.description":"splicing;cytoplasm","PubMed.ID":11713266,"subunits.Protein.name.":"Small nuclear ribonucleoprotein-associated proteins B and B' ;Methylosome subunit pICln ;Small nuclear ribonucleoprotein E ;Small nuclear ribonucleoprotein F ;Small nuclear ribonucleoprotein G ;Small nuclear ribonucleoprotein Sm D1 ;Small nuclear ribonucleoprotein Sm D2 ;Small nuclear ribonucleoprotein Sm D3","subunits.Gene.name.":"SNRPB;CLNS1A;SNRPE;SNRPF;SNRPG;SNRPD1;SNRPD2;SNRPD3","subunits.Gene.name.syn.":"COD SNRPB1;CLCI ICLN;;PBSCF;PBSCG;;SNRPD1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"snRNPs, integral components of the pre-mRNA splicing machinery, consist of seven Sm proteins which assemble in the cytoplasm as a ring structure on the snRNAs U1, U2, U4, and U5. The survival motor neuron (SMN) protein, the spinal muscular atrophy disease gene product, is crucial for snRNP core particle assembly in vivo. Results indicate that methylation of Sm proteins by the methylosome directs Sm proteins to the SMN complex for assembly into snRNP core particles and suggest that the methylosome can regulate snRNP assembly.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":836,"ComplexName":"20S methyltransferase core complex","Organism":"Human","Synonyms":"methylosome","Cell.line":"None","subunits.UniProt.IDs.":"O14744;P54105","subunits.Entrez.IDs.":"10419;1207","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0004- affinity chromatography technologies","GO.ID":"GO:0018126;GO:0006479;GO:0006461;GO:0005515;GO:0005737","GO.description":"protein hydroxylation;protein methylation;protein complex assembly;protein binding;cytoplasm","FunCat.ID":"14.07.09;14.10;16.01;70.03","FunCat.description":"posttranslational modification of amino acids (e.g. hydroxylation, methylation);assembly of protein complexes;protein binding;cytoplasm","PubMed.ID":11713266,"subunits.Protein.name.":"Protein arginine N-methyltransferase 5;Methylosome subunit pICln","subunits.Gene.name.":"PRMT5;CLNS1A","subunits.Gene.name.syn.":"HRMT1L5 IBP72 JBP1 SKB1;CLCI ICLN","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The  methylation of Sm proteins by the methylosome directs Sm proteins to the SMN complex for assembly into snRNP core particles and thus the methylosome can regulate snRNP assembly.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":837,"ComplexName":"20S methyltransferase complex","Organism":"Human","Synonyms":"methylosome","Cell.line":"None","subunits.UniProt.IDs.":"O14744;P54105;Q9BQA1","subunits.Entrez.IDs.":"10419;1207;79084","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0018126;GO:0006479;GO:0006461;GO:0005515;GO:0005737","GO.description":"protein hydroxylation;protein methylation;protein complex assembly;protein binding;cytoplasm","FunCat.ID":"14.07.09;14.10;16.01;70.03","FunCat.description":"posttranslational modification of amino acids (e.g. hydroxylation, methylation);assembly of protein complexes;protein binding;cytoplasm","PubMed.ID":11756452,"subunits.Protein.name.":"Protein arginine N-methyltransferase 5;Methylosome subunit pICln ;Methylosome protein 50","subunits.Gene.name.":"PRMT5;CLNS1A;WDR77","subunits.Gene.name.syn.":"HRMT1L5 IBP72 JBP1 SKB1;CLCI ICLN;MEP50 WD45","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":838,"ComplexName":"p27-Cdk2-Fgf2 complex","Organism":"Rabbit","Synonyms":"None","Cell.line":"eye","subunits.UniProt.IDs.":"A8UKE6;P48799;Q0GMK8","subunits.Entrez.IDs.":"None;100009068;None","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006468;GO:0006470;GO:0046777","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation","FunCat.ID":"14.07.03","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation","PubMed.ID":17209046,"subunits.Protein.name.":"Cyclin-dependent kinase 2;Fibroblast growth factor 2;Cyclin-dependent kinase inhibitor 1B","subunits.Gene.name.":"CDK2;FGF2;CDKN1B","subunits.Gene.name.syn.":"None;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Oryctolagus cuniculus (Rabbit);Oryctolagus cuniculus (Rabbit);Oryctolagus cuniculus (Rabbit)"}
{"ComplexID":839,"ComplexName":"LIN9-BMYB complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P10244;Q5TKA1","subunits.Entrez.IDs.":"4605;286826","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000278;GO:0051726","GO.description":"mitotic cell cycle;regulation of cell cycle","FunCat.ID":"10.03.01.01;10.03.01","FunCat.description":"mitotic cell cycle;mitotic cell cycle and cell cycle control","PubMed.ID":17098733,"subunits.Protein.name.":"Myb-related protein B ;Protein lin-9 homolog","subunits.Gene.name.":"MYBL2;LIN9","subunits.Gene.name.syn.":"BMYB;BARA TGS","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":840,"ComplexName":"Disc1-Grb2-Kif5a complex","Organism":"Rat","Synonyms":"None","Cell.line":"hippocampal neurons","subunits.UniProt.IDs.":"P62994;Q6QLM7;Q810H6","subunits.Entrez.IDs.":"81504;314906;307940","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0023052;GO:0050896;GO:0010183","GO.description":"intracellular protein transport;protein targeting;protein transport;signaling;response to stimulus;pollen tube guidance","FunCat.ID":"14.04;20.01.10;30.01;36.25;40.01.03.03","FunCat.description":"protein targeting, sorting and translocation;protein transport;cellular signalling;animal specific systemic sensing and response;guidance of longitudinal cell extension (e.g. pollen tube guidance, axonal pathfinding)","PubMed.ID":17202467,"subunits.Protein.name.":"Growth factor receptor-bound protein 2 ;Kinesin heavy chain isoform 5A;Disrupted in schizophrenia 1 homolog","subunits.Gene.name.":"Grb2;Kif5a;Disc1","subunits.Gene.name.syn.":"Ash;None;","Disease.comment":"DISC1 is involved in Schizophrenia.","Subunits.comment":"None","Complex.comment":"The authors suggest that DISC1 is required for NT-3-induced axon elongation and ERK activation at the distal part of axons by recruiting Grb2 to axonal tips.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":841,"ComplexName":"SNARE complex (Stx1a, Snap25, Vamp)","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P32851;P60881;P63045","subunits.Entrez.IDs.":"116470;25012;24803","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":8824312,"subunits.Protein.name.":"Syntaxin-1A;Synaptosomal-associated protein 25;Vesicle-associated membrane protein 2","subunits.Gene.name.":"Stx1a;Snap25;Vamp2","subunits.Gene.name.syn.":"Sap;Snap;Syb2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":842,"ComplexName":"SNARE complex (Stx3, Snap25, Vamp2, Cplx1)","Organism":"Rat","Synonyms":"None","Cell.line":"eye","subunits.UniProt.IDs.":"P60881;P63041;P63045;Q08849","subunits.Entrez.IDs.":"25012;64832;24803;81802","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":8824312,"subunits.Protein.name.":"Synaptosomal-associated protein 25;Complexin-1;Vesicle-associated membrane protein 2;Syntaxin-3","subunits.Gene.name.":"Snap25;Cplx1;Vamp2;Stx3","subunits.Gene.name.syn.":"Snap;None;Syb2;Stx3a","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":843,"ComplexName":"SNARE complex (STX1A, SNAP25, VAMP2)","Organism":"Bovine","Synonyms":"None","Cell.line":"retina","subunits.UniProt.IDs.":"P32850;P63026;Q17QQ3","subunits.Entrez.IDs.":"788566;282116;540853","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":8824312,"subunits.Protein.name.":"Syntaxin-1A ;Vesicle-associated membrane protein 2 ;Synaptosomal-associated protein 25","subunits.Gene.name.":"STX1A;VAMP2;SNAP25","subunits.Gene.name.syn.":";SYB2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":844,"ComplexName":"SNARE complex (Stx1a, Snap25, Vamp2)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P32851;P60881;P63045","subunits.Entrez.IDs.":"116470;25012;24803","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0047- far western blotting","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":10336434,"subunits.Protein.name.":"Syntaxin-1A;Synaptosomal-associated protein 25;Vesicle-associated membrane protein 2","subunits.Gene.name.":"Stx1a;Snap25;Vamp2","subunits.Gene.name.syn.":"Sap;Snap;Syb2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":845,"ComplexName":"PCI-PSA-SCG2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P05154;P07288;P13521","subunits.Entrez.IDs.":"5104;354;7857","Protein.complex.purification.method":"MI:0401- biochemical","GO.ID":"GO:0050789","GO.description":"regulation of biological process","FunCat.ID":"18","FunCat.description":"REGULATION OF METABOLISM AND PROTEIN FUNCTION","PubMed.ID":17253189,"subunits.Protein.name.":"Plasma serine protease inhibitor ;Prostate-specific antigen ;Secretogranin-2","subunits.Gene.name.":"SERPINA5;KLK3;SCG2","subunits.Gene.name.syn.":"PCI PLANH3 PROCI;APS;CHGC","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The complex formation among PCI, PSA, and Sg is modulated by several factors in seminal plasma.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":846,"ComplexName":"RICH1/AMOT polarity complex, Flag-Rich1 precipitated","Organism":"Human","Synonyms":"None","Cell.line":"epithelium","subunits.UniProt.IDs.":"P47756;P52907;Q4VCS5;Q68EM7;Q8N3R9;Q8NI35;Q96B97;Q9Y5K6","subunits.Entrez.IDs.":"832;829;154796;55114;64398;10207;30011;23607","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation;MI:0069-mass spectrometry studies of complexes","GO.ID":"GO:0008104;GO:0005096;GO:0043547;GO:0007186;GO:0051211;GO:0009798;GO:0007043;GO:0030054","GO.description":"protein localization;GTPase activator activity;positive regulation of GTPase activity;G-protein coupled receptor signaling pathway;anisotropic cell growth;axis specification;cell-cell junction assembly;cell junction","FunCat.ID":"18.01.03;18.02.01.01.01;30.05.02.24;40.01.03;41.05.19;42.06.04;70.06","FunCat.description":"regulation by localization;GTPase activator (GAP);G-protein coupled receptor signalling pathway;directional cell growth (morphogenesis);asymmetries and axis determination;intercellular junction (gap junction/adherens junction);cell junction","PubMed.ID":16678097,"subunits.Protein.name.":"F-actin-capping protein subunit beta;F-actin-capping protein subunit alpha-1;Angiomotin;Rho GTPase-activating protein 17;MAGUK p55 subfamily member 5;InaD-like protein;SH3 domain-containing kinase-binding protein 1;CD2-associated protein","subunits.Gene.name.":"CAPZB;CAPZA1;AMOT;ARHGAP17;MPP5;PATJ;SH3KBP1;CD2AP","subunits.Gene.name.syn.":"CAPB, CAPPB, CAPZ;CAPPA1, CAPZ, CAZ1;KIAA1071;RICH1;None;INADL;CIN85;None","Disease.comment":"None","Subunits.comment":"Since the authors did not specify F-actin-capping protein subunit alpha , we used isoform CAPZA1 .","Complex.comment":"In an additional immunoblot the authors show that Par-3 and aPKC likely associate with Rich1 at lower levels than Pals1 and Patj since they were not identified by MS. The authors propose that Rich1 and Amot maintain TJ integrity by the coordinate regulation of Cdc42 and by linking specific components of the TJ to intracellular protein trafficking.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":847,"ComplexName":"RICH1-PAR3-aPKC polarity complex","Organism":"Human","Synonyms":"None","Cell.line":"epithelium","subunits.UniProt.IDs.":"P41743;Q68EM7;Q8TEW0","subunits.Entrez.IDs.":"5584;55114;56288","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0008104;GO:0005096;GO:0043547;GO:0007186;GO:0051211;GO:0007043;GO:0030054","GO.description":"protein localization;GTPase activator activity;positive regulation of GTPase activity;G-protein coupled receptor signaling pathway;anisotropic cell growth;cell-cell junction assembly;cell junction","FunCat.ID":"18.01.03;18.02.01.01.01;30.05.02.24;40.01.03;42.06.04;70.06","FunCat.description":"regulation by localization;GTPase activator (GAP);G-protein coupled receptor signalling pathway;directional cell growth (morphogenesis);intercellular junction (gap junction/adherens junction);cell junction","PubMed.ID":16678097,"subunits.Protein.name.":"Protein kinase C iota type;Rho GTPase-activating protein 17;Partitioning defective 3 homolog","subunits.Gene.name.":"PRKCI;ARHGAP17;PARD3","subunits.Gene.name.syn.":"DXS1179E;RICH1;PAR3, PAR3A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Immunoblotting revealed aPKC and the 100 kDa isoform of Par-3, but not Par-6, in Rich1 immunoprecipitates. Par-3 and aPKC likely associate with Rich1 at lower levels than Pals1 and Patj since they were not identified by MS (see complex 846).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":848,"ComplexName":"RICH1/AMOT polarity complex, Flag-Amot precipitated","Organism":"Human","Synonyms":"None","Cell.line":"epithelium","subunits.UniProt.IDs.":"O75970;Q4VCS5;Q5T2T1;Q68EM7;Q8IY63;Q8N3R9;Q8NI35;Q9Y2J4","subunits.Entrez.IDs.":"8777;154796;143098;55114;154810;64398;10207;51421","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0008104;GO:0005096;GO:0043547;GO:0007186;GO:0051211;GO:0009798;GO:0007043;GO:0030054","GO.description":"protein localization;GTPase activator activity;positive regulation of GTPase activity;G-protein coupled receptor signaling pathway;anisotropic cell growth;axis specification;cell-cell junction assembly;cell junction","FunCat.ID":"18.01.03;18.02.01.01.01;30.05.02.24;40.01.03;41.05.19;42.06.04;70.06","FunCat.description":"regulation by localization;GTPase activator (GAP);G-protein coupled receptor signalling pathway;directional cell growth (morphogenesis);asymmetries and axis determination;intercellular junction (gap junction/adherens junction);cell junction","PubMed.ID":16678097,"subunits.Protein.name.":"Multiple PDZ domain protein ;Angiomotin;MAGUK p55 subfamily member 7;Rho GTPase-activating protein 17;Angiomotin-like protein 1;MAGUK p55 subfamily member 5;InaD-like protein;Angiomotin-like protein 2","subunits.Gene.name.":"MPDZ;AMOT;MPP7;ARHGAP17;AMOTL1;MPP5;PATJ;AMOTL2","subunits.Gene.name.syn.":"MUPP1;KIAA1071;;RICH1;;None;INADL;KIAA0989","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors suggest that Amot is a component of at least two complexes, only one of which contains Rich1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":851,"ComplexName":"SNARE complex (Stx2, Snap25, Vamp2)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P50279;P60881;P63045","subunits.Entrez.IDs.":"25130;25012;24803","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":10336434,"subunits.Protein.name.":"Syntaxin-2 ;Synaptosomal-associated protein 25;Vesicle-associated membrane protein 2","subunits.Gene.name.":"Stx2;Snap25;Vamp2","subunits.Gene.name.syn.":"Epim;Snap;Syb2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":852,"ComplexName":"SNARE complex (Stx3, Snap25, Vamp2)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P60881;P63045;Q08849","subunits.Entrez.IDs.":"25012;24803;81802","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":10336434,"subunits.Protein.name.":"Synaptosomal-associated protein 25;Vesicle-associated membrane protein 2;Syntaxin-3","subunits.Gene.name.":"Snap25;Vamp2;Stx3","subunits.Gene.name.syn.":"Snap;Syb2;Stx3a","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":853,"ComplexName":"SNARE complex (Stx4, Snap25, Vamp2)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P60881;P63045;Q08850","subunits.Entrez.IDs.":"25012;24803;81803","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":10336434,"subunits.Protein.name.":"Synaptosomal-associated protein 25;Vesicle-associated membrane protein 2;Syntaxin-4","subunits.Gene.name.":"Snap25;Vamp2;Stx4","subunits.Gene.name.syn.":"Snap;Syb2;Stx4a","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":854,"ComplexName":"SNARE complex (Stx1a, Snap25, Vamp8)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P32851;P60881;Q9WUF4","subunits.Entrez.IDs.":"116470;25012;83730","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":10336434,"subunits.Protein.name.":"Syntaxin-1A;Synaptosomal-associated protein 25;Vesicle-associated membrane protein 8","subunits.Gene.name.":"Stx1a;Snap25;Vamp8","subunits.Gene.name.syn.":"Sap;Snap;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":855,"ComplexName":"SNARE complex (Stx2, Snap25, Vamp8)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P50279;P60881;Q9WUF4","subunits.Entrez.IDs.":"25130;25012;83730","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":10336434,"subunits.Protein.name.":"Syntaxin-2 ;Synaptosomal-associated protein 25;Vesicle-associated membrane protein 8","subunits.Gene.name.":"Stx2;Snap25;Vamp8","subunits.Gene.name.syn.":"Epim;Snap;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":856,"ComplexName":"SNARE complex (Stx3, Snap25, Vamp8)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P60881;Q08849;Q9WUF4","subunits.Entrez.IDs.":"25012;81802;83730","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":10336434,"subunits.Protein.name.":"Synaptosomal-associated protein 25;Syntaxin-3;Vesicle-associated membrane protein 8","subunits.Gene.name.":"Snap25;Stx3;Vamp8","subunits.Gene.name.syn.":"Snap;Stx3a;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":857,"ComplexName":"SNARE complex (Stx4, Snap25, Vamp8)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P60881;Q08850;Q9WUF4","subunits.Entrez.IDs.":"25012;81803;83730","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":10336434,"subunits.Protein.name.":"Synaptosomal-associated protein 25;Syntaxin-4;Vesicle-associated membrane protein 8","subunits.Gene.name.":"Snap25;Stx4;Vamp8","subunits.Gene.name.syn.":"Snap;Stx4a;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":858,"ComplexName":"CRB3-PALS1-PATJ cell polarity complex","Organism":"Dog","Synonyms":"None","Cell.line":"epithelium","subunits.UniProt.IDs.":"Q63ZW7;Q8QZT4;Q9JLB2","subunits.Entrez.IDs.":"12695;224912;56217","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0051211;GO:0009798;GO:0007043;GO:0030054","GO.description":"anisotropic cell growth;axis specification;cell-cell junction assembly;cell junction","FunCat.ID":"40.01.03;41.05.19;42.06.04;70.06","FunCat.description":"directional cell growth (morphogenesis);asymmetries and axis determination;intercellular junction (gap junction/adherens junction);cell junction","PubMed.ID":15738264,"subunits.Protein.name.":"InaD-like protein ;Protein crumbs homolog 3;MAGUK p55 subfamily member 5","subunits.Gene.name.":"Patj;Crb3;Mpp5","subunits.Gene.name.syn.":"Cipp Inadl;;Pals1","Disease.comment":"None","Subunits.comment":"Since CRB3, INADL and MPP5 from dog were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.","Complex.comment":"The authors demonstrate that PATJ is required for the correct formation of tight junctions in MDCKII cells.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":859,"ComplexName":"SNARE complex (Stx4, Stx6, Stx7, Vamp3, Vamp7, Vamp8, Vti1b)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O70404;O70439;O88384;P63024;P70280;P70452;Q9JKK1","subunits.Entrez.IDs.":"22320;53331;53612;22319;20955;20909;58244","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":11278762,"subunits.Protein.name.":"Vesicle-associated membrane protein 8;Syntaxin-7;Vesicle transport through interaction with t-SNAREs homolog 1B ;Vesicle-associated membrane protein 3 ;Vesicle-associated membrane protein 7 ;Syntaxin-4;Syntaxin-6","subunits.Gene.name.":"Vamp8;Stx7;Vti1b;Vamp3;Vamp7;Stx4;Stx6","subunits.Gene.name.syn.":"None;Syn7;Vti1l1;Syb3;Sybl1;Stx4a;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":860,"ComplexName":"DNMT1-G9a-PCNA complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12004;P26358;Q96KQ7","subunits.Entrez.IDs.":"5111;1786;10919","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006260;GO:0006306;GO:0018126;GO:0006479;GO:0051276;GO:0005634","GO.description":"DNA replication;DNA methylation;protein hydroxylation;protein methylation;chromosome organization;nucleus","FunCat.ID":"10.01.03;10.01.09.01;14.07.09;42.10.03;70.10","FunCat.description":"DNA synthesis and replication;DNA methylation;posttranslational modification of amino acids (e.g. hydroxylation, methylation);organization of chromosome structure;nucleus","PubMed.ID":17085482,"subunits.Protein.name.":"Proliferating cell nuclear antigen;DNA ;Histone-lysine N-methyltransferase EHMT2","subunits.Gene.name.":"PCNA;DNMT1;EHMT2","subunits.Gene.name.syn.":"None;AIM CXXC9 DNMT;BAT8 C6orf30 G9A KMT1C NG36","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"DNMT1 and G9a are loaded onto the chromatin simultaneously in a ternary complex with loading factor PCNA during chromatin replication. Direct cooperation between DNMT1 and G9a provides a mechanism of coordinated DNA and H3K9 methylation during cell division.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":861,"ComplexName":"Par-3-p75NTR complex","Organism":"Mouse","Synonyms":"None","Cell.line":"Schwann cells","subunits.UniProt.IDs.":"Q99NH2;Q9Z0W1","subunits.Entrez.IDs.":"93742;18053","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation;MI:0096-pull down","GO.ID":"GO:0022008;GO:0048699;GO:0045216;GO:0007043;GO:0030182;GO:0007399;GO:0005911;GO:0042552","GO.description":"neurogenesis;generation of neurons;cell-cell junction organization;cell-cell junction assembly;neuron differentiation;nervous system development;cell-cell junction;myelination","FunCat.ID":"41.05.13;42.06.04;43.03.13;47.03.01;70.06.04","FunCat.description":"neurogenesis;intercellular junction (gap junction/adherens junction);neuron;nervous system;intercellular junction (gap junction/adherens junction)","PubMed.ID":17082460,"subunits.Protein.name.":"Partitioning defective 3 homolog;Tumor necrosis factor receptor superfamily member 16","subunits.Gene.name.":"Pard3;Ngfr","subunits.Gene.name.syn.":"Par3;Tnfrsf16","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors found that Par-3 and p75NTR did not interact in SC/DRG cocultures before the induction of myelination, whereas after induction, Par-3 and p75NTR transiently associated, peaking at 2 days after induction.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":862,"ComplexName":"DNMT1-G9a complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P26358;Q96KQ7","subunits.Entrez.IDs.":"1786;10919","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0006260;GO:0006306;GO:0000084;GO:0018126;GO:0006479;GO:0051276;GO:0005634","GO.description":"DNA replication;DNA methylation;mitotic S phase;protein hydroxylation;protein methylation;chromosome organization;nucleus","FunCat.ID":"10.01.03;10.01.09.01;10.03.01.01.05;14.07.09;42.10.03;70.10","FunCat.description":"DNA synthesis and replication;DNA methylation;S phase of mitotic cell cycle;posttranslational modification of amino acids (e.g. hydroxylation, methylation);organization of chromosome structure;nucleus","PubMed.ID":17085482,"subunits.Protein.name.":"DNA ;Histone-lysine N-methyltransferase EHMT2","subunits.Gene.name.":"DNMT1;EHMT2","subunits.Gene.name.syn.":"AIM CXXC9 DNMT;BAT8 C6orf30 G9A KMT1C NG36","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Direct cooperation between DNMT1 and G9a provides a mechanism of coordinated DNA and H3K9 methylation during cell division. The complex of DNMT1 and G9a led to enhanced DNA and histone methylation of in vitro assembled chromatin substrates.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":863,"ComplexName":"Srf-Myocd-Msx1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q8R5I7;Q9JM73;Q9QUG0","subunits.Entrez.IDs.":"246297;20807;81710","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":17030628,"subunits.Protein.name.":"Myocardin;Serum response factor;Msx-1 protein","subunits.Gene.name.":"Myocd;Srf;Msx1","subunits.Gene.name.syn.":"Mycd;None;Msx-1","Disease.comment":"None","Subunits.comment":"Since Srf from rat was not available in the Uniprot database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"Msx1 or Msx2 formed a ternary complex with SRF and myocardin and inhibited the binding of SRF or SRF/myocardin to the CArG-box motif, resulting in inhibition of their transcription.","SWISSPROT.organism":"Rattus norvegicus (Rat);Mus musculus (Mouse);Rattus norvegicus (Rat)"}
{"ComplexID":864,"ComplexName":"Srf-Myocd-Msx2 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P52953;Q8R5I7;Q9JM73","subunits.Entrez.IDs.":"25483;246297;20807","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":17030628,"subunits.Protein.name.":"Homeobox protein MSX-2 ;Myocardin;Serum response factor","subunits.Gene.name.":"Msx2;Myocd;Srf","subunits.Gene.name.syn.":"Msx-2;Mycd;None","Disease.comment":"None","Subunits.comment":"Since Srf from rat was not available in the Uniprot database at the time of annotation, the orthologous mouse protein was used.","Complex.comment":"Msx1 or Msx2 formed a ternary complex with SRF and myocardin and inhibited the binding of SRF or SRF/myocardin to the CArG-box motif, resulting in inhibition of their transcription.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Mus musculus (Mouse)"}
{"ComplexID":867,"ComplexName":"TRAP-SMCC mediator complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"A0JLT2;Q15528;Q15648;Q71SY5;Q96G25;Q9BUE0;Q9NPJ6;Q9NVC6;Q9NX70;Q9P086","subunits.Entrez.IDs.":"219541;6837;5469;81857;112950;54797;29079;9440;55588;400569","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0045893;GO:0005515;GO:0051098;GO:0051090;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;protein binding;regulation of binding;regulation of sequence-specific DNA binding transcription factor activity;nucleus","FunCat.ID":"11.02.03.04.01;16.01;18.01.07;18.02.09;70.10","FunCat.description":"transcription activation;protein binding;regulation by binding / dissociation;regulator of transcription factor;nucleus","PubMed.ID":14638676,"subunits.Protein.name.":"Mediator of RNA polymerase II transcription subunit 19 ;Mediator of RNA polymerase II transcription subunit 22 ;Mediator of RNA polymerase II transcription subunit 1;Mediator of RNA polymerase II transcription subunit 25 ;Mediator of RNA polymerase II transcription subunit 8 ;Mediator of RNA polymerase II transcription subunit 18 ;Mediator of RNA polymerase II transcription subunit 4 ;Mediator of RNA polymerase II transcription subunit 17;Mediator of RNA polymerase II transcription subunit 29 ;Mediator of RNA polymerase II transcription subunit 11","subunits.Gene.name.":"MED19;MED22;MED1;MED25;MED8;MED18;MED4;MED17;MED29;MED11","subunits.Gene.name.syn.":"LCMR1;SURF5;ARC205 CRSP1 CRSP200 DRIP205 DRIP230 PBP PPARBP PPARGBP RB18A TRAP220 TRIP2;ACID1 ARC92 PTOV2;;;ARC36 DRIP36 VDRIP;ARC77 CRSP6 DRIP77 DRIP80 TRAP80;IXL;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":868,"ComplexName":"aPKC-PAR-6-PAR-3 cell polarity complex","Organism":"Dog","Synonyms":"None","Cell.line":"epithelium","subunits.UniProt.IDs.":"Q62074;Q99NH2;Q9JK83","subunits.Entrez.IDs.":"18759;93742;58220","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0051211;GO:0009798;GO:0007043;GO:0030054","GO.description":"anisotropic cell growth;axis specification;cell-cell junction assembly;cell junction","FunCat.ID":"40.01.03;41.05.19;42.06.04;70.06","FunCat.description":"directional cell growth (morphogenesis);asymmetries and axis determination;intercellular junction (gap junction/adherens junction);cell junction","PubMed.ID":16638806,"subunits.Protein.name.":"Protein kinase C iota type;Partitioning defective 3 homolog;Partitioning defective 6 homolog beta","subunits.Gene.name.":"Prkci;Pard3;Pard6b","subunits.Gene.name.syn.":"Pkcl, aPKClambda;Par3;Par6b","Disease.comment":"None","Subunits.comment":"Since  PRKCI, PARD3 and PARD6b from dog were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.","Complex.comment":"This study suggests that the suppression of apical PAR-3-aPKC-PAR-6 complex activity by mLgl is mediated through the suppression of the interaction of the aPKC-PAR-6 complex with PAR-3 or Cdc42.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":871,"ComplexName":"BRAF53-BRCA2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60341;P51587;Q13547;Q92769;Q96BD5;Q9P0W2;Q9UKL0","subunits.Entrez.IDs.":"23028;675;3065;3066;51317;10362;23186","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0006265;GO:0000278;GO:0045892;GO:0006473;GO:0006476;GO:0003677;GO:0051276;GO:0030182;GO:0005634","GO.description":"DNA repair;DNA topological change;mitotic cell cycle;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;DNA binding;chromosome organization;neuron differentiation;nucleus","FunCat.ID":"10.01.05.01;10.01.09.05;10.03.01.01;11.02.03.04.03;14.07.04;16.03.01;42.10.03;43.03.13;70.10","FunCat.description":"DNA repair;DNA conformation modification (e.g. chromatin);mitotic cell cycle;transcription repression;modification by acetylation, deacetylation;DNA binding;organization of chromosome structure;neuron;nucleus","PubMed.ID":11207365,"subunits.Protein.name.":"Lysine-specific histone demethylase 1A;Breast cancer type 2 susceptibility protein ;Histone deacetylase 1;Histone deacetylase 2;PHD finger protein 21A;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related;REST corepressor 1","subunits.Gene.name.":"KDM1A;BRCA2;HDAC1;HDAC2;PHF21A;HMG20B;RCOR1","subunits.Gene.name.syn.":"AOF2 KDM1 KIAA0601 LSD1;FACD FANCD1;RPD3L1;None;BHC80 KIAA1696;BRAF35 HMGX2 HMGXB2 SMARCE1R;KIAA0071 RCOR","Disease.comment":"BRCA2 confers susceptibility to in breast cancer.","Subunits.comment":"None","Complex.comment":"Antibody microinjection experiments suggest a role for BRCA2/BRAF35 complex in modulation of cell cycle progression.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":872,"ComplexName":"SNARE complex (Stx1a, Snap29)","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P32851;Q9Z2P6","subunits.Entrez.IDs.":"116470;116500","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":11707603,"subunits.Protein.name.":"Syntaxin-1A;Synaptosomal-associated protein 29","subunits.Gene.name.":"Stx1a;Snap29","subunits.Gene.name.syn.":"Sap;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":873,"ComplexName":"SNARE complex (STX1A, SNAP29)","Organism":"Human","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"O95721;Q16623","subunits.Entrez.IDs.":"9342;6804","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":11707603,"subunits.Protein.name.":"Synaptosomal-associated protein 29 ;Syntaxin-1A","subunits.Gene.name.":"SNAP29;STX1A","subunits.Gene.name.syn.":";STX1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":874,"ComplexName":"SNARE complex (VAMP3, VAMP4, VAMP8, STX6)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43752;O75379;Q15836;Q9BV40","subunits.Entrez.IDs.":"10228;8674;9341;8673","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":11839770,"subunits.Protein.name.":"Syntaxin-6;Vesicle-associated membrane protein 4 ;Vesicle-associated membrane protein 3;Vesicle-associated membrane protein 8","subunits.Gene.name.":"STX6;VAMP4;VAMP3;VAMP8","subunits.Gene.name.syn.":";;SYB3;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":875,"ComplexName":"SNARE complex (VAMP3, VAMP4, STX16)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14662;O75379;Q15836","subunits.Entrez.IDs.":"8675;8674;9341","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":11839770,"subunits.Protein.name.":"Syntaxin-16 ;Vesicle-associated membrane protein 4 ;Vesicle-associated membrane protein 3","subunits.Gene.name.":"STX16;VAMP4;VAMP3","subunits.Gene.name.syn.":";;SYB3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":876,"ComplexName":"SNARE complex (VAMP3, STX6, VTI1A)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43752;Q15836;Q96AJ9","subunits.Entrez.IDs.":"10228;9341;143187","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":11839770,"subunits.Protein.name.":"Syntaxin-6;Vesicle-associated membrane protein 3;Vesicle transport through interaction with t-SNAREs homolog 1A","subunits.Gene.name.":"STX6;VAMP3;VTI1A","subunits.Gene.name.syn.":";SYB3;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":877,"ComplexName":"SNARE complex (VAMP4, STX6, STX16, VTI1a, VTI1b)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14662;O43752;O75379;Q96AJ9;Q9UEU0","subunits.Entrez.IDs.":"8675;10228;8674;143187;10490","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":11839770,"subunits.Protein.name.":"Syntaxin-16 ;Syntaxin-6;Vesicle-associated membrane protein 4 ;Vesicle transport through interaction with t-SNAREs homolog 1A ;Vesicle transport through interaction with t-SNAREs homolog 1B","subunits.Gene.name.":"STX16;STX6;VAMP4;VTI1A;VTI1B","subunits.Gene.name.syn.":";;;;VTI1 VTI1L VTI1L1 VTI2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":878,"ComplexName":"PKA (RII-alpha and RII-beta)-AKAP5-ADRB1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK-293 cells","subunits.UniProt.IDs.":"P08588;P13861;P24588;P31323","subunits.Entrez.IDs.":"153;5576;9495;5577","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0055-fluorescent resonance energy transfer","GO.ID":"GO:0007186;GO:0001881;GO:0010737","GO.description":"G-protein coupled receptor signaling pathway;receptor recycling;protein kinase A signaling","FunCat.ID":"30.05.02.24","FunCat.description":"G-protein coupled receptor signalling pathway","PubMed.ID":16940053,"subunits.Protein.name.":"Beta-1 adrenergic receptor;cAMP-dependent protein kinase type II-alpha regulatory subunit;A-kinase anchor protein 5;cAMP-dependent protein kinase type II-beta regulatory subunit","subunits.Gene.name.":"ADRB1;PRKAR2A;AKAP5;PRKAR2B","subunits.Gene.name.syn.":"ADRB1R, B1AR;PKR2, PRKAR2;AKAP79;None","Disease.comment":"ADRB1 is involved in hypertension and heart failure.","Subunits.comment":"None","Complex.comment":"AKAP79 provides PKA to phosphorylate the beta(1)-AR and thereby dictate the recycling and resensitization itineraries of the beta(1)-AR.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":880,"ComplexName":"SNARE complex (Vamp4, Stx6, Stx16, Vti1b)","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"B5DF99;O70480;P58200;Q63635","subunits.Entrez.IDs.":"362283;53330;366673;60562","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006900;GO:0016050;GO:0036465;GO:0000301;GO:0048489;GO:0016079","GO.description":"membrane budding;vesicle organization;synaptic vesicle recycling;retrograde transport, vesicle recycling within Golgi;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.25;20.09.07.29;20.09.07.07;20.09.16.09.05","FunCat.description":"vesicle formation;vesicle recycling;retrograde transport;synaptic vesicle exocytosis","PubMed.ID":12067063,"subunits.Protein.name.":"Stx16 protein ;Vesicle-associated membrane protein 4 ;Vesicle transport through interaction with t-SNAREs homolog 1B ;Syntaxin-6","subunits.Gene.name.":"Stx16;Vamp4;Vti1b;Stx6","subunits.Gene.name.syn.":";;Vti1l1;","Disease.comment":"None","Subunits.comment":"Since VAMP-4 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.This complex may have a role in synaptic vesicle biogenesis or recycling.","SWISSPROT.organism":"Rattus norvegicus (Rat);Mus musculus (Mouse);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":881,"ComplexName":"SNARE complex (Vamp4, Stx6, Stx16, Vti1a)","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"B5DF99;O70480;Q63635;Q9JI51","subunits.Entrez.IDs.":"362283;53330;60562;65277","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006900;GO:0016050;GO:0036465;GO:0000301","GO.description":"membrane budding;vesicle organization;synaptic vesicle recycling;retrograde transport, vesicle recycling within Golgi","FunCat.ID":"20.09.07.25;20.09.07.29;20.09.07.07","FunCat.description":"vesicle formation;vesicle recycling;retrograde transport","PubMed.ID":12067063,"subunits.Protein.name.":"Stx16 protein ;Vesicle-associated membrane protein 4 ;Syntaxin-6;Vesicle transport through interaction with t-SNAREs homolog 1A","subunits.Gene.name.":"Stx16;Vamp4;Stx6;Vti1a","subunits.Gene.name.syn.":";;;Vti1l2","Disease.comment":"None","Subunits.comment":"Since VAMP-4 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.This complex may have a role in synaptic vesicle biogenesis or recycling.","SWISSPROT.organism":"Rattus norvegicus (Rat);Mus musculus (Mouse);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":882,"ComplexName":"PAR-6-aPKC-PAR-3 complex","Organism":"Dog","Synonyms":"None","Cell.line":"epithelium","subunits.UniProt.IDs.":"Q62074;Q99NH2;Q9Z101","subunits.Entrez.IDs.":"18759;93742;56513","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007043;GO:0030054;GO:0030859","GO.description":"cell-cell junction assembly;cell junction;polarized epithelial cell differentiation","FunCat.ID":"42.06.04;70.06","FunCat.description":"intercellular junction (gap junction/adherens junction);cell junction","PubMed.ID":11532031,"subunits.Protein.name.":"Protein kinase C iota type;Partitioning defective 3 homolog;Partitioning defective 6 homolog alpha","subunits.Gene.name.":"Prkci;Pard3;Pard6a","subunits.Gene.name.syn.":"Pkcl, aPKClambda;Par3;Par6a","Disease.comment":"None","Subunits.comment":"Since PARD6, PARD3 and PRKCI from dog were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.","Complex.comment":"The ternary complex formation and junctional co-localization of PAR-6 with aPKC and ASIP/PAR-3 are observed during the early stage of epithelial cell polarization. PAR-6 forms a stable protein complex through the disappearance and reformation of cell-cell contact induced by calcium switch.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":883,"ComplexName":"PAR-6-aPKC-PAR-3-Cdc42-Rac1 complex","Organism":"Dog","Synonyms":"None","Cell.line":"epithelium","subunits.UniProt.IDs.":"P60766;P63001;Q62074;Q99NH2;Q9Z101","subunits.Entrez.IDs.":"12540;19353;18759;93742;56513","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007264;GO:0007043;GO:0030054","GO.description":"small GTPase mediated signal transduction;cell-cell junction assembly;cell junction","FunCat.ID":"30.01.05.05.01;42.06.04;70.06","FunCat.description":"small GTPase mediated signal transduction;intercellular junction (gap junction/adherens junction);cell junction","PubMed.ID":11532031,"subunits.Protein.name.":"Cell division control protein 42 homolog;Ras-related C3 botulinum toxin substrate 1;Protein kinase C iota type;Partitioning defective 3 homolog;Partitioning defective 6 homolog alpha","subunits.Gene.name.":"Cdc42;Rac1;Prkci;Pard3;Pard6a","subunits.Gene.name.syn.":"None;None;Pkcl, aPKClambda;Par3;Par6a","Disease.comment":"None","Subunits.comment":"Since the proteins from dog were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.","Complex.comment":"This is the first in vivo evidence for a molecular interaction between the PAR-6-aPKC-PAR-3 ternary complex and Cdc42-Rac1.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":884,"ComplexName":"GluR1-cadherin-catenin complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain, low-density primary cultures of hippocampal neurons","subunits.UniProt.IDs.":"P19490;Q9WU82;Q9Z1Y3","subunits.Entrez.IDs.":"50592;84353;83501","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007399;GO:0048167","GO.description":"nervous system development;regulation of synaptic plasticity","FunCat.ID":"47.03.01","FunCat.description":"nervous system","PubMed.ID":16515543,"subunits.Protein.name.":"Glutamate receptor 1;Catenin beta-1;Cadherin-2","subunits.Gene.name.":"Gria1;Ctnnb1;Cdh2","subunits.Gene.name.syn.":"Glur1;Catnb;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":885,"ComplexName":"Glur4-cadherin-catenin complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain, low-density primary cultures of hippocampal neurons","subunits.UniProt.IDs.":"P19493;Q9WU82;Q9Z1Y3","subunits.Entrez.IDs.":"29629;84353;83501","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007399;GO:0048167","GO.description":"nervous system development;regulation of synaptic plasticity","FunCat.ID":"47.03.01","FunCat.description":"nervous system","PubMed.ID":16515543,"subunits.Protein.name.":"Glutamate receptor 4;Catenin beta-1;Cadherin-2","subunits.Gene.name.":"Gria4;Ctnnb1;Cdh2","subunits.Gene.name.syn.":"Glur4;Catnb;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":886,"ComplexName":"MTA1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95983;Q09028;Q13330;Q16576;Q6IT96;Q92769","subunits.Entrez.IDs.":"53615;5928;9112;5931;3065;3066","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0091- chromatography technologies","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0009755;GO:0023052;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;hormone-mediated signaling pathway;signaling;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;30.01.09.08;30.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;hormone mediated signal transduction;cellular signalling;organization of chromosome structure;nucleus","PubMed.ID":12920132,"subunits.Protein.name.":"Methyl-CpG-binding domain protein 3;Histone-binding protein RBBP4;Metastasis-associated protein MTA1;Histone-binding protein RBBP7;Histone deacetylase ;Histone deacetylase 2","subunits.Gene.name.":"MBD3;RBBP4;MTA1;RBBP7;HDAC1;HDAC2","subunits.Gene.name.syn.":"None;RBAP48;None;RBAP46;;None","Disease.comment":"MTA1 is involved in metastasis or cancer formation.","Subunits.comment":"Several other subunits of the complex were found in the analysis, which have not been further characterized: p68, p66 and three so-called MTA1-associated proteins.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":887,"ComplexName":"Glur2-Glur4-Plp-Itgav complex","Organism":"Rat","Synonyms":"None","Cell.line":"nervous system","subunits.UniProt.IDs.":"P19491;P19493;P43406;P60203;Q63845","subunits.Entrez.IDs.":"29627;29629;16410;24943;None","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007218","GO.description":"neuropeptide signaling pathway","FunCat.ID":"30.05.02.24.06","FunCat.description":"neuropeptide signalling pathway","PubMed.ID":16510724,"subunits.Protein.name.":"Glutamate receptor 2;Glutamate receptor 4;Integrin alpha-V;Myelin proteolipid protein;Integrin alpha v subunit","subunits.Gene.name.":"Gria2;Gria4;Itgav;Plp1;integrin a","subunits.Gene.name.syn.":"Glur2;Glur4;None;Plp;None","Disease.comment":"None","Subunits.comment":"Since ItgaV from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"The coimmunoprecipitation studies showed an increased association of GluR2 and GluR4 subunits of AMPA receptor with the {alpha}v integrin/PLP complex after agonist stimulation of AMPA receptor (PMID:16510724).","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Mus musculus (Mouse);Rattus norvegicus (Rat);Rattus sp."}
{"ComplexID":888,"ComplexName":"MTA2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O94776;O95983;Q09028;Q13547;Q14839;Q16576;Q92769;Q96ST3","subunits.Entrez.IDs.":"9219;53615;5928;3065;1108;5931;3066;25942","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies;MI:0091-chromatography technologies","GO.ID":"GO:0006265;GO:0045892;GO:0032774;GO:0051276;GO:0005634;GO:0016575","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;RNA biosynthetic process;chromosome organization;nucleus;histone deacetylation","FunCat.ID":"10.01.09.05;11.02.03.04.03;11.02;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;RNA synthesis;organization of chromosome structure;nucleus","PubMed.ID":12920132,"subunits.Protein.name.":"Metastasis-associated protein MTA2;Methyl-CpG-binding domain protein 3;Histone-binding protein RBBP4;Histone deacetylase 1;Chromodomain-helicase-DNA-binding protein 4;Histone-binding protein RBBP7;Histone deacetylase 2;Paired amphipathic helix protein Sin3a","subunits.Gene.name.":"MTA2;MBD3;RBBP4;HDAC1;CHD4;RBBP7;HDAC2;SIN3A","subunits.Gene.name.syn.":"MTA1L1 PID;None;RBAP48;RPD3L1;None;RBAP46;None;None","Disease.comment":"None","Subunits.comment":"Since the authors did not specify SIN3, we used SIN3A.","Complex.comment":"Since MTA2 is not involved in metastasis or cancer formation, the authors suggest a housekeeping role of the MTA2 complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":889,"ComplexName":"MTA1-HDAC core complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q09028;Q13330;Q16576;Q6IT96;Q92769","subunits.Entrez.IDs.":"5928;9112;5931;3065;3066","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0091- chromatography technologies","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0009755;GO:0023052;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;hormone-mediated signaling pathway;signaling;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;30.01.09.08;30.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;hormone mediated signal transduction;cellular signalling;organization of chromosome structure;nucleus","PubMed.ID":12920132,"subunits.Protein.name.":"Histone-binding protein RBBP4;Metastasis-associated protein MTA1;Histone-binding protein RBBP7;Histone deacetylase ;Histone deacetylase 2","subunits.Gene.name.":"RBBP4;MTA1;RBBP7;HDAC1;HDAC2","subunits.Gene.name.syn.":"RBAP48;None;RBAP46;;None","Disease.comment":"MTA1 is involved in metastasis or cancer formation.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":890,"ComplexName":"PAR-3-PKCz-Tiam2 complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P09217;Q6ZPF3;Q9Z340","subunits.Entrez.IDs.":"25522;24001;81918","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0051211;GO:0022008;GO:0048699;GO:0009798;GO:0030182","GO.description":"anisotropic cell growth;neurogenesis;generation of neurons;axis specification;neuron differentiation","FunCat.ID":"40.01.03;41.05.13;41.05.19;43.03.13","FunCat.description":"directional cell growth (morphogenesis);neurogenesis;asymmetries and axis determination;neuron","PubMed.ID":15723051,"subunits.Protein.name.":"Protein kinase C zeta type;T-lymphoma invasion and metastasis-inducing protein 2 ;Partitioning defective 3 homolog","subunits.Gene.name.":"Prkcz;Tiam2;Pard3","subunits.Gene.name.syn.":"Pkcz;Kiaa2016 Stef;Par3","Disease.comment":"None","Subunits.comment":"Since Tiam2 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Mus musculus (Mouse);Rattus norvegicus (Rat)"}
{"ComplexID":891,"ComplexName":"PAR-3-PKC-zeta-Tiam1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P09217;Q60610;Q9Z340","subunits.Entrez.IDs.":"25522;21844;81918","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0051211;GO:0022008;GO:0048699;GO:0009798;GO:0030182","GO.description":"anisotropic cell growth;neurogenesis;generation of neurons;axis specification;neuron differentiation","FunCat.ID":"40.01.03;41.05.13;41.05.19;43.03.13","FunCat.description":"directional cell growth (morphogenesis);neurogenesis;asymmetries and axis determination;neuron","PubMed.ID":15723051,"subunits.Protein.name.":"Protein kinase C zeta type;T-lymphoma invasion and metastasis-inducing protein 1 ;Partitioning defective 3 homolog","subunits.Gene.name.":"Prkcz;Tiam1;Pard3","subunits.Gene.name.syn.":"Pkcz;Tiam-1;Par3","Disease.comment":"None","Subunits.comment":"Since Tiam1 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Mus musculus (Mouse);Rattus norvegicus (Rat)"}
{"ComplexID":892,"ComplexName":"PAR-3-aPKC-Tiam2 complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"Q62074;Q6ZPF3;Q9Z340","subunits.Entrez.IDs.":"18759;24001;81918","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0051211;GO:0022008;GO:0048699;GO:0009798;GO:0030182","GO.description":"anisotropic cell growth;neurogenesis;generation of neurons;axis specification;neuron differentiation","FunCat.ID":"40.01.03;41.05.13;41.05.19;43.03.13","FunCat.description":"directional cell growth (morphogenesis);neurogenesis;asymmetries and axis determination;neuron","PubMed.ID":15723051,"subunits.Protein.name.":"Protein kinase C iota type;T-lymphoma invasion and metastasis-inducing protein 2 ;Partitioning defective 3 homolog","subunits.Gene.name.":"Prkci;Tiam2;Pard3","subunits.Gene.name.syn.":"Pkcl, aPKClambda;Kiaa2016 Stef;Par3","Disease.comment":"None","Subunits.comment":"Since aPKC and Tiam2 from rat were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Rattus norvegicus (Rat)"}
{"ComplexID":893,"ComplexName":"PAR-3-aPKC-Tiam1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"Q60610;Q62074;Q9Z340","subunits.Entrez.IDs.":"21844;18759;81918","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0051211;GO:0022008;GO:0048699;GO:0009798;GO:0030182","GO.description":"anisotropic cell growth;neurogenesis;generation of neurons;axis specification;neuron differentiation","FunCat.ID":"40.01.03;41.05.13;41.05.19;43.03.13","FunCat.description":"directional cell growth (morphogenesis);neurogenesis;asymmetries and axis determination;neuron","PubMed.ID":15723051,"subunits.Protein.name.":"T-lymphoma invasion and metastasis-inducing protein 1 ;Protein kinase C iota type;Partitioning defective 3 homolog","subunits.Gene.name.":"Tiam1;Prkci;Pard3","subunits.Gene.name.syn.":"Tiam-1;Pkcl, aPKClambda;Par3","Disease.comment":"None","Subunits.comment":"Since aPKC and Tiam1 from rat were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Rattus norvegicus (Rat)"}
{"ComplexID":894,"ComplexName":"Tiam2-PAR-3-aPKC-PAR-6-Cdc42-GTP complex","Organism":"Rat","Synonyms":"None","Cell.line":"COS-7 cells","subunits.UniProt.IDs.":"P97701;Q6B4M5;Q6ZPF3;Q8CFN2;Q9Z340","subunits.Entrez.IDs.":"84006;307799;24001;64465;81918","Protein.complex.purification.method":"MI:0096-pull down","GO.ID":"GO:0007264;GO:0051211;GO:0022008;GO:0048699;GO:0009798;GO:0030182","GO.description":"small GTPase mediated signal transduction;anisotropic cell growth;neurogenesis;generation of neurons;axis specification;neuron differentiation","FunCat.ID":"30.01.05.05.01;40.01.03;41.05.13;41.05.19;43.03.13","FunCat.description":"small GTPase mediated signal transduction;directional cell growth (morphogenesis);neurogenesis;asymmetries and axis determination;neuron","PubMed.ID":15723051,"subunits.Protein.name.":"Protein kinase C lambda ;Partitioning defective 6 homolog alpha ;T-lymphoma invasion and metastasis-inducing protein 2 ;Cell division control protein 42 homolog;Partitioning defective 3 homolog","subunits.Gene.name.":";Pard6a;Tiam2;Cdc42;Pard3","subunits.Gene.name.syn.":";Par-6a Par6a;Kiaa2016 Stef;;Par3","Disease.comment":"None","Subunits.comment":"Since Tiam2 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"STEF-DeltaN (Tiam2) interacted with GST-Cdc42-GTPgammaS only in the presence of exogenous PAR-6-aPKC-PAR-3. However, the association of STEF-DeltaN with Cdc42 was not detected in the absence of PAR-3, indicating that STEF forms a complex with activated Cdc42 through the interaction with PAR-3. For pull down analyses immobilized beads were incubated with COS7 cell lysate expressing the indicated proteins.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Mus musculus (Mouse);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":895,"ComplexName":"hMediator complex (MED23, CDK8, CCNC, MED7)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43513;P24863;P49336;Q9ULK4","subunits.Entrez.IDs.":"9443;892;1024;9439","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0226- ion exchange chromatography; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0045893;GO:0051098;GO:0005515;GO:0051090;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;regulation of binding;protein binding;regulation of sequence-specific DNA binding transcription factor activity;nucleus","FunCat.ID":"11.02.03.04.01;18.01.07;16.01;18.02.09;70.10","FunCat.description":"transcription activation;regulation by binding / dissociation;protein binding;regulator of transcription factor;nucleus","PubMed.ID":10353252,"subunits.Protein.name.":"Mediator of RNA polymerase II transcription subunit 7 ;Cyclin-C;Cyclin-dependent kinase 8;Mediator of RNA polymerase II transcription subunit 23","subunits.Gene.name.":"MED7;CCNC;CDK8;MED23","subunits.Gene.name.syn.":"ARC34 CRSP9;None;None;ARC130 CRSP3 DRIP130 KIAA1216 SUR2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The high-molecular-mass mammalian Mediator complexes have many subunits in common. However, their reported subunit compositions are not identical (PMID:10838567).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":896,"ComplexName":"hMediator complex (MED23, CDK8, CCNC)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P24863;P49336;Q9ULK4","subunits.Entrez.IDs.":"892;1024;9439","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0071- molecular sieving","GO.ID":"GO:0045893;GO:0051098;GO:0005515;GO:0051090;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;regulation of binding;protein binding;regulation of sequence-specific DNA binding transcription factor activity;nucleus","FunCat.ID":"11.02.03.04.01;18.01.07;16.01;18.02.09;70.10","FunCat.description":"transcription activation;regulation by binding / dissociation;protein binding;regulator of transcription factor;nucleus","PubMed.ID":11416138,"subunits.Protein.name.":"Cyclin-C;Cyclin-dependent kinase 8;Mediator of RNA polymerase II transcription subunit 23","subunits.Gene.name.":"CCNC;CDK8;MED23","subunits.Gene.name.syn.":"None;None;ARC130 CRSP3 DRIP130 KIAA1216 SUR2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The high-molecular-mass mammalian Mediator complexes have many subunits in common. However, their reported subunit compositions are not identical (PMID:10838567).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":897,"ComplexName":"CDK8-CyclinC-Mediator complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P24863;P49336","subunits.Entrez.IDs.":"892;1024","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0071- molecular sieving","GO.ID":"GO:0045892;GO:0006468;GO:0006470;GO:0046777;GO:0006464;GO:0050789;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;cellular protein modification process;regulation of biological process;nucleus","FunCat.ID":"11.02.03.04.03;14.07.03;14.07;18;70.10","FunCat.description":"transcription repression;modification by phosphorylation, dephosphorylation, autophosphorylation;protein modification;REGULATION OF METABOLISM AND PROTEIN FUNCTION;nucleus","PubMed.ID":11416138,"subunits.Protein.name.":"Cyclin-C;Cyclin-dependent kinase 8","subunits.Gene.name.":"CCNC;CDK8","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"It has been shown hat CDK8 phosphorylates the cyclin H subunit of TFIIH and inhibits its function in transcription (PMID:10993082). This explains, why the CDK8-CyclinC-Mediator complex inhibits basal and activated transcription.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":898,"ComplexName":"Mediator complex 1","Organism":"Human","Synonyms":"High-molecular-mass Mediator complex 1; 2MDa Mediator complex 1","Cell.line":"None","subunits.UniProt.IDs.":"O60244;O75586;P24863;P49336;Q9ULK4","subunits.Entrez.IDs.":"9282;10001;892;1024;9439","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0071- molecular sieving","GO.ID":"GO:0045893;GO:0051098;GO:0005515;GO:0051090;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;regulation of binding;protein binding;regulation of sequence-specific DNA binding transcription factor activity;nucleus","FunCat.ID":"11.02.03.04.01;18.01.07;16.01;18.02.09;70.10","FunCat.description":"transcription activation;regulation by binding / dissociation;protein binding;regulator of transcription factor;nucleus","PubMed.ID":11416138,"subunits.Protein.name.":"Mediator of RNA polymerase II transcription subunit 14;Mediator of RNA polymerase II transcription subunit 6 ;Cyclin-C;Cyclin-dependent kinase 8;Mediator of RNA polymerase II transcription subunit 23","subunits.Gene.name.":"MED14;MED6;CCNC;CDK8;MED23","subunits.Gene.name.syn.":"ARC150 CRSP2 CXorf4 DRIP150 EXLM1 RGR1 TRAP170;ARC33;None;None;ARC130 CRSP3 DRIP130 KIAA1216 SUR2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Regulation of transcription by RNA polymerase II (Pol II) is controlled by specific combinations of sequence-specific, DNA binding regulatory transcription factors (TFs) bound to a gene's promoter and enhancer regions. These TFs interact with several multiprotein complexes that remodel the chromatin context of the promoter, integrate signals from multiple TFs to control the frequency of transcription initiation, and regulate the efficiency of transcription elongation. One such complex is the Mediator, an ~2-megadalton complex of 20 to 30 subunits that is believed to function as a molecular bridge by simultaneously interacting with both DNA-bound TFs and Pol II. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":899,"ComplexName":"Par-3-KIF3A-PKC-zeta complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P09217;Q9WV62;Q9Z340","subunits.Entrez.IDs.":"25522;84392;81918","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0030705;GO:0051211;GO:0022008;GO:0048699;GO:0009798;GO:0030182","GO.description":"cytoskeleton-dependent intracellular transport;anisotropic cell growth;neurogenesis;generation of neurons;axis specification;neuron differentiation","FunCat.ID":"20.09.14;40.01.03;41.05.13;41.05.19;43.03.13","FunCat.description":"cytoskeleton-dependent transport;directional cell growth (morphogenesis);neurogenesis;asymmetries and axis determination;neuron","PubMed.ID":15048131,"subunits.Protein.name.":"Protein kinase C zeta type;Kinesin-like protein KIF3A;Partitioning defective 3 homolog","subunits.Gene.name.":"Prkcz;Kif3a;Pard3","subunits.Gene.name.syn.":"Pkcz;None;Par3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Coimmunoprecipitation done with anti-PAR-3 or with anti-KIF3A yielded the same results.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":900,"ComplexName":"Mediator complex 2","Organism":"Human","Synonyms":"High-molecular-mass Mediator complex 2; 2MDa Mediator complex 2","Cell.line":"None","subunits.UniProt.IDs.":"O60244;O75586;Q9ULK4","subunits.Entrez.IDs.":"9282;10001;9439","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0071- molecular sieving","GO.ID":"GO:0045893;GO:0051098;GO:0005515;GO:0051090;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;regulation of binding;protein binding;regulation of sequence-specific DNA binding transcription factor activity;nucleus","FunCat.ID":"11.02.03.04.01;18.01.07;16.01;18.02.09;70.10","FunCat.description":"transcription activation;regulation by binding / dissociation;protein binding;regulator of transcription factor;nucleus","PubMed.ID":11416138,"subunits.Protein.name.":"Mediator of RNA polymerase II transcription subunit 14;Mediator of RNA polymerase II transcription subunit 6 ;Mediator of RNA polymerase II transcription subunit 23","subunits.Gene.name.":"MED14;MED6;MED23","subunits.Gene.name.syn.":"ARC150 CRSP2 CXorf4 DRIP150 EXLM1 RGR1 TRAP170;ARC33;ARC130 CRSP3 DRIP130 KIAA1216 SUR2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Regulation of transcription by RNA polymerase II (Pol II) is controlled by specific combinations of sequence-specific, DNA binding regulatory transcription factors (TFs) bound to a gene's promoter and enhancer regions. These TFs interact with several multiprotein complexes that remodel the chromatin context of the promoter, integrate signals from multiple TFs to control the frequency of transcription initiation, and regulate the efficiency of transcription elongation. One such complex is the Mediator, an ~2-megadalton complex of 20 to 30 subunits that is believed to function as a molecular bridge by simultaneously interacting with both DNA-bound TFs and Pol II. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":901,"ComplexName":"Par-3-KIF3A-aPKC complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"Q62074;Q9WV62;Q9Z340","subunits.Entrez.IDs.":"18759;84392;81918","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0030705;GO:0051211;GO:0022008;GO:0048699;GO:0009798;GO:0030182","GO.description":"cytoskeleton-dependent intracellular transport;anisotropic cell growth;neurogenesis;generation of neurons;axis specification;neuron differentiation","FunCat.ID":"20.09.14;40.01.03;41.05.13;41.05.19;43.03.13","FunCat.description":"cytoskeleton-dependent transport;directional cell growth (morphogenesis);neurogenesis;asymmetries and axis determination;neuron","PubMed.ID":15048131,"subunits.Protein.name.":"Protein kinase C iota type;Kinesin-like protein KIF3A;Partitioning defective 3 homolog","subunits.Gene.name.":"Prkci;Kif3a;Pard3","subunits.Gene.name.syn.":"Pkcl, aPKClambda;None;Par3","Disease.comment":"None","Subunits.comment":"Since aPKC from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":902,"ComplexName":"SNARE complex (Stx5, Gosr1, GS15)","Organism":"Rat","Synonyms":"None","Cell.line":"liver","subunits.UniProt.IDs.":"O35152;Q08851;Q62931","subunits.Entrez.IDs.":"54400;65134;94189","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006906;GO:0048489;GO:0016079;GO:0005794","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis;Golgi apparatus","FunCat.ID":"20.09.07.27;20.09.16.09.05;70.08","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis;Golgi","PubMed.ID":12070132,"subunits.Protein.name.":"BET1-like protein;Syntaxin-5;Golgi SNAP receptor complex member 1","subunits.Gene.name.":"Bet1l;Stx5;Gosr1","subunits.Gene.name.syn.":"Gs15;Stx5a;Gs28","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":903,"ComplexName":"RET-Rai complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P07949;Q92529","subunits.Entrez.IDs.":"5979;53358","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007166","GO.description":"cell surface receptor signaling pathway","FunCat.ID":"30.05","FunCat.description":"transmembrane signal transduction","PubMed.ID":15940252,"subunits.Protein.name.":"Proto-oncogene tyrosine-protein kinase receptor Ret ;SHC-transforming protein 3","subunits.Gene.name.":"RET;SHC3","subunits.Gene.name.syn.":"CDHF12 CDHR16 PTC RET51;NSHC SHCC","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"RAI protein forms complexes with two variants of RET oncoprotein: MEN2A and PTC.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":904,"ComplexName":"SHC3-GAB1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q13480;Q92529","subunits.Entrez.IDs.":"2549;53358","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007166","GO.description":"cell surface receptor signaling pathway","FunCat.ID":"30.05","FunCat.description":"transmembrane signal transduction","PubMed.ID":15940252,"subunits.Protein.name.":"GRB2-associated-binding protein 1 ;SHC-transforming protein 3","subunits.Gene.name.":"GAB1;SHC3","subunits.Gene.name.syn.":";NSHC SHCC","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"RAI protein forms complexes with two variants of RET oncoprotein: MEN2A and PTC.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":905,"ComplexName":"KIF3A/B-PAR-3-aPKC-PAR-6 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"O15066;P41743;Q8TEW0;Q9NPB6;Q9Y496","subunits.Entrez.IDs.":"9371;5584;56288;50855;11127","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0022008;GO:0048699;GO:0030182;GO:0030010","GO.description":"neurogenesis;generation of neurons;neuron differentiation;establishment of cell polarity","FunCat.ID":"41.05.13;43.03.13","FunCat.description":"neurogenesis;neuron","PubMed.ID":15048131,"subunits.Protein.name.":"Kinesin-like protein KIF3B;Protein kinase C iota type;Partitioning defective 3 homolog;Partitioning defective 6 homolog alpha;Kinesin-like protein KIF3A","subunits.Gene.name.":"KIF3B;PRKCI;PARD3;PARD6A;KIF3A","subunits.Gene.name.syn.":"KIAA0359;DXS1179E;PAR3, PAR3A;PAR6A, PAR6;KIF3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results indicate that PAR-3 interacts with KIF3 in vivo and that aPKC associates with KIF3 through its interaction with PAR-3.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":906,"ComplexName":"ADAR1-CDK2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P24941;P55265","subunits.Entrez.IDs.":"1017;103","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000278;GO:0051726;GO:0006468;GO:0006470;GO:0046777","GO.description":"mitotic cell cycle;regulation of cell cycle;protein phosphorylation;protein dephosphorylation;protein autophosphorylation","FunCat.ID":"10.03.01.01;10.03.01;14.07.03","FunCat.description":"mitotic cell cycle;mitotic cell cycle and cell cycle control;modification by phosphorylation, dephosphorylation, autophosphorylation","PubMed.ID":17224799,"subunits.Protein.name.":"Cyclin-dependent kinase 2;Double-stranded RNA-specific adenosine deaminase","subunits.Gene.name.":"CDK2;ADAR","subunits.Gene.name.syn.":"CDKN2;ADAR1 DSRAD G1P1 IFI4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":907,"ComplexName":"SNARE complex (Stx5, Gosr1, Bet1, Gef2)","Organism":"Rat","Synonyms":"None","Cell.line":"liver","subunits.UniProt.IDs.":"P60522;Q08851;Q62896;Q62931","subunits.Entrez.IDs.":"64670;65134;29631;94189","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006906;GO:0048489;GO:0016079;GO:0005794","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis;Golgi apparatus","FunCat.ID":"20.09.07.27;20.09.16.09.05;70.08","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis;Golgi","PubMed.ID":12070132,"subunits.Protein.name.":"Gamma-aminobutyric acid receptor-associated protein-like 2;Syntaxin-5;BET1 homolog;Golgi SNAP receptor complex member 1","subunits.Gene.name.":"Gabarapl2;Stx5;Bet1;Gosr1","subunits.Gene.name.syn.":"Gef2;Stx5a;None;Gs28","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.Following the MGI nomenclature GEF-2 and GATE-16 are identical.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":908,"ComplexName":"PAR-6-aPKC-PAR-3 complex","Organism":"Dog","Synonyms":"None","Cell.line":"epithelium","subunits.UniProt.IDs.":"Q62074;Q99NH2;Q9Z101","subunits.Entrez.IDs.":"18759;93742;56513","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007043;GO:0030054;GO:0090162","GO.description":"cell-cell junction assembly;cell junction;establishment of epithelial cell polarity","FunCat.ID":"42.06.04;70.06","FunCat.description":"intercellular junction (gap junction/adherens junction);cell junction","PubMed.ID":11257119,"subunits.Protein.name.":"Protein kinase C iota type;Partitioning defective 3 homolog;Partitioning defective 6 homolog alpha","subunits.Gene.name.":"Prkci;Pard3;Pard6a","subunits.Gene.name.syn.":"Pkcl, aPKClambda;Par3;Par6a","Disease.comment":"None","Subunits.comment":"Since  PARD6, PARD3 and PRKCI from dog were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.","Complex.comment":"PAR-6 immunoprecipitates specifically contain endogenous aPKC-lambda, full-length PAR-3, and its splicing variant.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":909,"ComplexName":"ARC92-Mediator complex","Organism":"Human","Synonyms":"A-Med complex","Cell.line":"None","subunits.UniProt.IDs.":"O43513;O60244;O75586;O95402;P49336;Q15648;Q71SY5;Q93074;Q96RN5;Q9NVC6;Q9UHV7;Q9ULK4;Q9Y2X0","subunits.Entrez.IDs.":"9443;9282;10001;9441;1024;5469;81857;9968;51586;9440;9969;9439;10025","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0045893;GO:0005515;GO:0051098;GO:0051090;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;protein binding;regulation of binding;regulation of sequence-specific DNA binding transcription factor activity;nucleus","FunCat.ID":"11.02.03.04.01;16.01;18.01.07;18.02.09;70.10","FunCat.description":"transcription activation;protein binding;regulation by binding / dissociation;regulator of transcription factor;nucleus","PubMed.ID":14657022,"subunits.Protein.name.":"Mediator of RNA polymerase II transcription subunit 7 ;Mediator of RNA polymerase II transcription subunit 14;Mediator of RNA polymerase II transcription subunit 6 ;Mediator of RNA polymerase II transcription subunit 26 ;Cyclin-dependent kinase 8;Mediator of RNA polymerase II transcription subunit 1;Mediator of RNA polymerase II transcription subunit 25 ;Mediator of RNA polymerase II transcription subunit 12;Mediator of RNA polymerase II transcription subunit 15;Mediator of RNA polymerase II transcription subunit 17;Mediator of RNA polymerase II transcription subunit 13 ;Mediator of RNA polymerase II transcription subunit 23 ;Mediator of RNA polymerase II transcription subunit 16","subunits.Gene.name.":"MED7;MED14;MED6;MED26;CDK8;MED1;MED25;MED12;MED15;MED17;MED13;MED23;MED16","subunits.Gene.name.syn.":"ARC34 CRSP9;ARC150 CRSP2 CXorf4 DRIP150 EXLM1 RGR1 TRAP170;ARC33;ARC70 CRSP7;None;ARC205 CRSP1 CRSP200 DRIP205 DRIP230 PBP PPARBP PPARGBP RB18A TRAP220 TRIP2;ACID1 ARC92 PTOV2;ARC240 CAGH45 HOPA KIAA0192 TNRC11 TRAP230;ARC105 CTG7A PCQAP TIG1 TNRC7;ARC77 CRSP6 DRIP77 DRIP80 TRAP80;ARC250 KIAA0593 THRAP1 TRAP240;ARC130 CRSP3 DRIP130 KIAA1216 SUR2;DRIP92 THRAP5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Experiemts show that the transcription coactivator ARC is required for SREBP (sterol regulatory element binding protein) control of cholesterol and lipid homeostasis. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":910,"ComplexName":"CRSP-Mediator 2 complex","Organism":"Human","Synonyms":"CRSP-Med 2 complex","Cell.line":"None","subunits.UniProt.IDs.":"O43513;O60244;O75448;O75586;Q96RN5;Q9BUE0;Q9NPJ6;Q9NVC6;Q9ULK4;Q9Y2X0","subunits.Entrez.IDs.":"9443;9282;9862;10001;51586;54797;29079;9440;9439;10025","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0040- electron microscopy; MI:0004- affinity chromatography technologies","GO.ID":"GO:0045893;GO:0051098;GO:0005515;GO:0051090;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;regulation of binding;protein binding;regulation of sequence-specific DNA binding transcription factor activity;nucleus","FunCat.ID":"11.02.03.04.01;18.01.07;16.01;18.02.09;70.10","FunCat.description":"transcription activation;regulation by binding / dissociation;protein binding;regulator of transcription factor;nucleus","PubMed.ID":15175162,"subunits.Protein.name.":"Mediator of RNA polymerase II transcription subunit 7 ;Mediator of RNA polymerase II transcription subunit 14;Mediator of RNA polymerase II transcription subunit 24;Mediator of RNA polymerase II transcription subunit 6 ;Mediator of RNA polymerase II transcription subunit 15;Mediator of RNA polymerase II transcription subunit 18 ;Mediator of RNA polymerase II transcription subunit 4 ;Mediator of RNA polymerase II transcription subunit 17;Mediator of RNA polymerase II transcription subunit 23 ;Mediator of RNA polymerase II transcription subunit 16","subunits.Gene.name.":"MED7;MED14;MED24;MED6;MED15;MED18;MED4;MED17;MED23;MED16","subunits.Gene.name.syn.":"ARC34 CRSP9;ARC150 CRSP2 CXorf4 DRIP150 EXLM1 RGR1 TRAP170;ARC100 CRSP4 DRIP100 KIAA0130 THRAP4 TRAP100;ARC33;ARC105 CTG7A PCQAP TIG1 TNRC7;;ARC36 DRIP36 VDRIP;ARC77 CRSP6 DRIP77 DRIP80 TRAP80;ARC130 CRSP3 DRIP130 KIAA1216 SUR2;DRIP92 THRAP5","Disease.comment":"None","Subunits.comment":"Two other subunits of the complex were found in the analysis, which have not been further characterized: p97 and p26.","Complex.comment":"The CRSP-Med 2 complex is a promotor-selective coactivator. It cannot activate transcription from a VDR-responsive promoter, which needs coactivator recruitment by Med220. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":911,"ComplexName":"Par3-Apc-Kif3a complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P70478;Q9WV62;Q9Z340","subunits.Entrez.IDs.":"24205;84392;81918","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0030705;GO:0051211;GO:0022008;GO:0048699;GO:0009798;GO:0030182","GO.description":"cytoskeleton-dependent intracellular transport;anisotropic cell growth;neurogenesis;generation of neurons;axis specification;neuron differentiation","FunCat.ID":"20.09.14;40.01.03;41.05.13;41.05.19;43.03.13","FunCat.description":"cytoskeleton-dependent transport;directional cell growth (morphogenesis);neurogenesis;asymmetries and axis determination;neuron","PubMed.ID":15556865,"subunits.Protein.name.":"Adenomatous polyposis coli protein;Kinesin-like protein KIF3A;Partitioning defective 3 homolog","subunits.Gene.name.":"Apc;Kif3a;Pard3","subunits.Gene.name.syn.":"None;None;Par3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results suggest that mPar3 is polarized in developing neurons through APC- and kinesin-mediated transport to the plus ends of rapidly growing microtubules at the nascent axon tip, a process that involves a spatially regulated GSK-3beta activity.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":912,"ComplexName":"Kal1-Fgfr1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"eye","subunits.UniProt.IDs.":"P23352;Q04589","subunits.Entrez.IDs.":"3730;Error happend while calculation","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0008543;GO:0001654","GO.description":"fibroblast growth factor receptor signaling pathway;eye development","FunCat.ID":"30.05.01.12.03;47.03.02.02","FunCat.description":"FGF-receptor signalling pathway;eye","PubMed.ID":17186267,"subunits.Protein.name.":"Anosmin-1;Fibroblast growth factor receptor 1","subunits.Gene.name.":"ANOS1;Fgfr1","subunits.Gene.name.syn.":"ADMLX KAL KAL1 KALIG1;Flg","Disease.comment":"None","Subunits.comment":"Since Kal1 protein from rat was not available in the UniProt database at the time of annotation, the orthologous human protein was used.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Rattus norvegicus (Rat)"}
{"ComplexID":913,"ComplexName":"SNARE complex (Stx1a, Snap25, Cplx2, Vamp2)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P32851;P60881;P63045;P84087","subunits.Entrez.IDs.":"116470;25012;24803;116657","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":11751907,"subunits.Protein.name.":"Syntaxin-1A;Synaptosomal-associated protein 25;Vesicle-associated membrane protein 2;Complexin-2","subunits.Gene.name.":"Stx1a;Snap25;Vamp2;Cplx2","subunits.Gene.name.syn.":"Sap;Snap;Syb2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":914,"ComplexName":"PALS1-PATJ-CRB3-PAR3-PAR6-aPKC-14-3-3 zeta complex","Organism":"Dog","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P63101;Q62074;Q63ZW7;Q8QZT4;Q99NH2;Q9JLB2;Q9Z101","subunits.Entrez.IDs.":"22631;18759;12695;224912;93742;56217;56513","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0051211;GO:0009798;GO:0007043;GO:0030054","GO.description":"anisotropic cell growth;axis specification;cell-cell junction assembly;cell junction","FunCat.ID":"40.01.03;41.05.19;42.06.04;70.06","FunCat.description":"directional cell growth (morphogenesis);asymmetries and axis determination;intercellular junction (gap junction/adherens junction);cell junction","PubMed.ID":14653998,"subunits.Protein.name.":"14-3-3 protein zeta/delta;Protein kinase C iota type;InaD-like protein ;Protein crumbs homolog 3;Partitioning defective 3 homolog;MAGUK p55 subfamily member 5;Partitioning defective 6 homolog alpha","subunits.Gene.name.":"Ywhaz;Prkci;Patj;Crb3;Pard3;Mpp5;Pard6a","subunits.Gene.name.syn.":"None;Pkcl, aPKClambda;Cipp Inadl;;Par3;Pals1;Par6a","Disease.comment":"None","Subunits.comment":"Since  several proteins from dog were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.","Complex.comment":"The authors previously demonstrated that the PALS1/PATJ/CRB3 and Par3/Par6/aPKC complexes interact via PALS1-Par6 binding. Component Par6 was not shown in the pull down experiment. Immobilized CRB3 carboxy-terminal peptides were used for precipitation. The authors suggest that Par3 phosphorylation and subsequent 14-3-3 binding is a crucial mechanism that regulates the function of the Par3/Par6/aPKC complex.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":915,"ComplexName":"SNARE complex (SNAP23, STX1A)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00161;Q16623","subunits.Entrez.IDs.":"8773;6804","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0050789;GO:0006821;GO:0006906;GO:0048489;GO:0016079","GO.description":"regulation of biological process;chloride transport;vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"18;20.01.01.07.09;20.09.07.27;20.09.16.09.05","FunCat.description":"REGULATION OF METABOLISM AND PROTEIN FUNCTION;chloride transport;vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":12209004,"subunits.Protein.name.":"Synaptosomal-associated protein 23;Syntaxin-1A","subunits.Gene.name.":"SNAP23;STX1A","subunits.Gene.name.syn.":"None;STX1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway. SNAP-23 physically associates with CFTR by binding to its amino-terminal tail, a region that modulates channel gating.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":916,"ComplexName":"PALS1-Par3-aPKC-14-3-3 zeta complex","Organism":"Dog","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P63101;Q62074;Q99NH2;Q9JLB2","subunits.Entrez.IDs.":"22631;18759;93742;56217","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0051211;GO:0009798;GO:0007043;GO:0030054","GO.description":"anisotropic cell growth;axis specification;cell-cell junction assembly;cell junction","FunCat.ID":"40.01.03;41.05.19;42.06.04;70.06","FunCat.description":"directional cell growth (morphogenesis);asymmetries and axis determination;intercellular junction (gap junction/adherens junction);cell junction","PubMed.ID":14653998,"subunits.Protein.name.":"14-3-3 protein zeta/delta;Protein kinase C iota type;Partitioning defective 3 homolog;MAGUK p55 subfamily member 5","subunits.Gene.name.":"Ywhaz;Prkci;Pard3;Mpp5","subunits.Gene.name.syn.":"None;Pkcl, aPKClambda;Par3;Pals1","Disease.comment":"None","Subunits.comment":"Since several proteins from dog were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.","Complex.comment":"Immobilized GST-14-3-3 zeta was used for precipitation. The authors found that of the polarity proteins examined, Par3 was highly enriched after GST-14-3-3 zeta pulldown, suggesting that 14-3-3 zeta may directly associate with Par3.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":917,"ComplexName":"CERF complex (CECR2-containing remodeling factor complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P28370;Q9BXF3","subunits.Entrez.IDs.":"6594;27443","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0022008;GO:0048699;GO:0051276;GO:0005634","GO.description":"DNA topological change;neurogenesis;generation of neurons;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;41.05.13;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);neurogenesis;organization of chromosome structure;nucleus","PubMed.ID":15640247,"subunits.Protein.name.":"Probable global transcription activator SNF2L1 ;Cat eye syndrome critical region protein 2","subunits.Gene.name.":"SMARCA1;CECR2","subunits.Gene.name.syn.":"SNF2L SNF2L1;KIAA1740","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"CERF displays an ATP hydrolyzing activity that is stimulated by nucleosomes. CERF plays a critical role in neurolation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":918,"ComplexName":"PAR3-PAR6-PALS1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q8N3R9;Q8TEW0;Q9NPB6","subunits.Entrez.IDs.":"64398;56288;50855","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0051211;GO:0009798;GO:0007043;GO:0030054","GO.description":"anisotropic cell growth;axis specification;cell-cell junction assembly;cell junction","FunCat.ID":"40.01.03;41.05.19;42.06.04;70.06","FunCat.description":"directional cell growth (morphogenesis);asymmetries and axis determination;intercellular junction (gap junction/adherens junction);cell junction","PubMed.ID":12545177,"subunits.Protein.name.":"MAGUK p55 subfamily member 5;Partitioning defective 3 homolog;Partitioning defective 6 homolog alpha","subunits.Gene.name.":"MPP5;PARD3;PARD6A","subunits.Gene.name.syn.":"None;PAR3, PAR3A;PAR6A, PAR6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"HEK 293 cells transiently expressed with Mys-PALS1 and HA-Par6 or HA-Par3 showed that Par6, but not Par3, coimmunoprecipitated with PALS1. However, when all three proteins were expressed together, the authors detected a complex of PALS1 with both Par6 and Par3.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":919,"ComplexName":"hNURF complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P28370;Q09028;Q12830;Q16576","subunits.Entrez.IDs.":"6594;5928;2186;5931","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:2001141;GO:0006355;GO:0022008;GO:0048699;GO:0051276;GO:0030182;GO:0005634","GO.description":"DNA topological change;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;neurogenesis;generation of neurons;chromosome organization;neuron differentiation;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04;41.05.13;42.10.03;43.03.13;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcriptional control;neurogenesis;organization of chromosome structure;neuron;nucleus","PubMed.ID":15640247,"subunits.Protein.name.":"Probable global transcription activator SNF2L1 ;Histone-binding protein RBBP4;Nucleosome-remodeling factor subunit BPTF ;Histone-binding protein RBBP7","subunits.Gene.name.":"SMARCA1;RBBP4;BPTF;RBBP7","subunits.Gene.name.syn.":"SNF2L SNF2L1;RBAP48;FAC1 FALZ;RBAP46","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"hNURF possesses ATP-dependent chromatin remodeling activity and regulates engrailed-1 (en-1) and engrailed-2 (en-2) expression.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":920,"ComplexName":"PAR3-PATJ-PALS1 complex","Organism":"Dog","Synonyms":"None","Cell.line":"MDCK cells","subunits.UniProt.IDs.":"Q63ZW7;Q99NH2;Q9JLB2","subunits.Entrez.IDs.":"12695;93742;56217","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0051211;GO:0009798;GO:0007043;GO:0005886;GO:0030054","GO.description":"anisotropic cell growth;axis specification;cell-cell junction assembly;plasma membrane;cell junction","FunCat.ID":"40.01.03;41.05.19;42.06.04;70.02;70.06","FunCat.description":"directional cell growth (morphogenesis);asymmetries and axis determination;intercellular junction (gap junction/adherens junction);eukaryotic plasma membrane / membrane attached;cell junction","PubMed.ID":12545177,"subunits.Protein.name.":"InaD-like protein ;Partitioning defective 3 homolog;MAGUK p55 subfamily member 5","subunits.Gene.name.":"Patj;Pard3;Mpp5","subunits.Gene.name.syn.":"Cipp Inadl;Par3;Pals1","Disease.comment":"None","Subunits.comment":"Since  several proteins from dog were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.","Complex.comment":"The authors found that endogenous Par3 and PATJ were both coimmunoprecipitated with Myc-PALS1. Collectively, these data indicate that the Crb-PALS1-PATJ and Par3-Par6-aPKC complexes can associate with one another through a PALS1-Par6 interaction.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":921,"ComplexName":"Remodeling and spacing factor (RSF) complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60264;Q96T23","subunits.Entrez.IDs.":"8467;51773","Protein.complex.purification.method":"MI:0091- chromatography technologies","GO.ID":"GO:0009117;GO:0006265;GO:0006352;GO:0051276;GO:0005634","GO.description":"nucleotide metabolic process;DNA topological change;DNA-templated transcription, initiation;chromosome organization;nucleus","FunCat.ID":"01.03;10.01.09.05;11.02.03.01.01;42.10.03;70.10","FunCat.description":"nucleotide/nucleoside/nucleobase metabolism;DNA conformation modification (e.g. chromatin);transcription initiation;organization of chromosome structure;nucleus","PubMed.ID":9836642,"subunits.Protein.name.":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5;Remodeling and spacing factor 1","subunits.Gene.name.":"SMARCA5;RSF1","subunits.Gene.name.syn.":"SNF2H WCRF135;HBXAP XAP8","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"RSF facilitates transcription initiation by remodeling nucleosomes in the promoter region to allow the formation of preinitiation complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":922,"ComplexName":"SNARE complex (Stx1a, Snap25, Cplx2, Vamp2)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P32851;P60881;P63045;P84087","subunits.Entrez.IDs.":"116470;25012;24803;116657","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":10777504,"subunits.Protein.name.":"Syntaxin-1A;Synaptosomal-associated protein 25;Vesicle-associated membrane protein 2;Complexin-2","subunits.Gene.name.":"Stx1a;Snap25;Vamp2;Cplx2","subunits.Gene.name.syn.":"Sap;Snap;Syb2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":923,"ComplexName":"SNF2L-RSF1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P28370;Q96T23","subunits.Entrez.IDs.":"6594;51773","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0051276;GO:0005634","GO.description":"DNA topological change;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);organization of chromosome structure;nucleus","PubMed.ID":15640247,"subunits.Protein.name.":"Probable global transcription activator SNF2L1 ;Remodeling and spacing factor 1","subunits.Gene.name.":"SMARCA1;RSF1","subunits.Gene.name.syn.":"SNF2L SNF2L1;HBXAP XAP8","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":924,"ComplexName":"Toposome","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P07910;P11388;Q08211;Q08945;Q6P2Q9;Q96SB4;Q9NR30","subunits.Entrez.IDs.":"3183;7153;1660;6749;10594;6732;9188","Protein.complex.purification.method":"MI:0226- ion exchange chromatography; MI:0019- coimmunoprecipitation","GO.ID":"GO:0051276;GO:0000278;GO:0051726;GO:0003677;GO:0005634","GO.description":"chromosome organization;mitotic cell cycle;regulation of cell cycle;DNA binding;nucleus","FunCat.ID":"42.10.03;10.03.01.01;10.03.01;16.03.01;70.10","FunCat.description":"organization of chromosome structure;mitotic cell cycle;mitotic cell cycle and cell cycle control;DNA binding;nucleus","PubMed.ID":15034300,"subunits.Protein.name.":"Heterogeneous nuclear ribonucleoproteins C1/C2 ;DNA topoisomerase 2-alpha;ATP-dependent RNA helicase A ;FACT complex subunit SSRP1;Pre-mRNA-processing-splicing factor 8 ;SRSF protein kinase 1 ;Nucleolar RNA helicase 2","subunits.Gene.name.":"HNRNPC;TOP2A;DHX9;SSRP1;PRPF8;SRPK1;DDX21","subunits.Gene.name.syn.":"HNRPC;TOP2;DDX9 LKP NDH2;FACT80;PRPC8;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"During chromosome segregation, the toposome complex separates entangled circular chromatin DNA about fourfold more efficiently than topoisomerase IIalpha alone.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":925,"ComplexName":"WCRF complex","Organism":"Human","Synonyms":"WCRF/hACF complex","Cell.line":"None","subunits.UniProt.IDs.":"O60264;Q9NRL2","subunits.Entrez.IDs.":"8467;11177","Protein.complex.purification.method":"MI:0091- chromatography technologies","GO.ID":"GO:0006265;GO:2001141;GO:0006355;GO:0051276;GO:0005634","GO.description":"DNA topological change;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcriptional control;organization of chromosome structure;nucleus","PubMed.ID":10655480,"subunits.Protein.name.":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5;Bromodomain adjacent to zinc finger domain protein 1A","subunits.Gene.name.":"SMARCA5;BAZ1A","subunits.Gene.name.syn.":"SNF2H WCRF135;ACF1 WCRF180","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"ATPase activity of WCRF complex is stimulated by nucleososmal DNA.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":926,"ComplexName":"SCRIB-LGL2 complex","Organism":"Human","Synonyms":"None","Cell.line":"MDCK cells, HEK 293 cells","subunits.UniProt.IDs.":"Q14160;Q6P1M3","subunits.Entrez.IDs.":"23513;3993","Protein.complex.purification.method":"MI:0276- blue native page; MI:0019- coimmunoprecipitation; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0051211;GO:0009798;GO:0005886;GO:0005737","GO.description":"anisotropic cell growth;axis specification;plasma membrane;cytoplasm","FunCat.ID":"40.01.03;41.05.19;70.02;70.03","FunCat.description":"directional cell growth (morphogenesis);asymmetries and axis determination;eukaryotic plasma membrane / membrane attached;cytoplasm","PubMed.ID":16791850,"subunits.Protein.name.":"Protein scribble homolog;Lethal","subunits.Gene.name.":"SCRIB;LLGL2","subunits.Gene.name.syn.":"CRIB1, KIAA0147, LAP4, SCRB1, VARTUL;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Analyses done to localize the association of the proteins showed that exogenously expressed Scrib and Lgl2 can interact in either location (at the membrane and in the cytosol).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":927,"ComplexName":"CENP-A nucleosome associated complex","Organism":"Human","Synonyms":"CENP-A NAC complex","Cell.line":"None","subunits.UniProt.IDs.":"Q03188;Q71F23;Q96BT3;Q96H22;Q9H3R5;Q9NSP4","subunits.Entrez.IDs.":"1060;79682;80152;55839;64946;79019","Protein.complex.purification.method":"MI:0676- tandem affinity purification","GO.ID":"GO:0006349;GO:0051382;GO:0007059;GO:0051225;GO:0007098;GO:0005694","GO.description":"regulation of gene expression by genetic imprinting;kinetochore assembly;chromosome segregation;spindle assembly;centrosome cycle;chromosome","FunCat.ID":"10.01.09.07;10.03.04.01;10.03.04.05;10.03.05.01;70.10.03","FunCat.description":"DNA imprinting and other epigenetic effects;centromere/kinetochore complex maturation;chromosome segregation/division;spindle pole body/centrosome and microtubule cycle;chromosome","PubMed.ID":16622419,"subunits.Protein.name.":"Centromere protein C ;Centromere protein U ;Centromere protein T;Centromere protein N ;Centromere protein H ;Centromere protein M","subunits.Gene.name.":"CENPC;CENPU;CENPT;CENPN;CENPH;CENPM","subunits.Gene.name.syn.":"CENPC1 ICEN7;ICEN24 KLIP1 MLF1IP PBIP1;C16orf56, ICEN22;C16orf60 ICEN32;ICEN35;C22orf18 ICEN39 PANE1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Assembly of CENP-A NAC complex at centromeres is dependent on CENP-M, CENP-N and CENP-T.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":928,"ComplexName":"SCRIB-VANGL2 complex","Organism":"Human","Synonyms":"None","Cell.line":"epithelium","subunits.UniProt.IDs.":"Q14160;Q9ULK5","subunits.Entrez.IDs.":"23513;57216","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation;MI:0096- pull down","GO.ID":"GO:0009798;GO:0005886","GO.description":"axis specification;plasma membrane","FunCat.ID":"41.05.19;70.02","FunCat.description":"asymmetries and axis determination;eukaryotic plasma membrane / membrane attached","PubMed.ID":16791850,"subunits.Protein.name.":"Protein scribble homolog;Vang-like protein 2","subunits.Gene.name.":"SCRIB;VANGL2","subunits.Gene.name.syn.":"CRIB1, KIAA0147, LAP4, SCRB1, VARTUL;KIAA1215 STB1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"When human EGFP-hVangl2  fusion proteins expressed in transfected MDCK cells were quantitatively immunoprecipitated with anti-GFP, a small (2%) but reproducible amount of total endo Scrib was found in the full-length hVangl2 immunoprecipitate. Further analyses done in HEK293A cell extracts.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":929,"ComplexName":"CEN complex","Organism":"Human","Synonyms":"centromer chromatin complex","Cell.line":"None","subunits.UniProt.IDs.":"O60264;P07199;P11021;P11142;P22087;P35226;P49450;Q02241;Q03188;Q06587;Q08945;Q13185;Q13619;Q15007;Q16531;Q53SF7;Q5T200;Q69YN4;Q6T4P5;Q71F23;Q8N0S6;Q8N1F7;Q8NEM2;Q92620;Q92674;Q96JP5;Q96T23;Q99496;Q9BS16;Q9BU64;Q9BXP5;Q9BZH6;Q9H0H5;Q9H3R5;Q9HC52;Q9NSP4;Q9Y5B9","subunits.Entrez.IDs.":"8467;1059;3309;3312;2091;648;1058;9493;1060;6015;6749;11335;8451;9589;1642;22837;23091;25962;79948;79682;91687;9688;79801;9785;2491;80829;51773;6045;64105;79172;51593;55717;29127;64946;57332;79019;11198","Protein.complex.purification.method":"MI:0402- chromatin immunoprecipitation assays;MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0000278;GO:0051382;GO:0051225;GO:0007098;GO:0005694","GO.description":"mitotic cell cycle;kinetochore assembly;spindle assembly;centrosome cycle;chromosome","FunCat.ID":"10.03.01.01;10.03.04.01;10.03.05.01;70.10.03","FunCat.description":"mitotic cell cycle;centromere/kinetochore complex maturation;spindle pole body/centrosome and microtubule cycle;chromosome","PubMed.ID":15009096,"subunits.Protein.name.":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5;Major centromere autoantigen B ;78 kDa glucose-regulated protein;Heat shock cognate 71 kDa protein;rRNA 2'-O-methyltransferase fibrillarin;Polycomb complex protein BMI-1;Histone H3-like centromeric protein A ;Kinesin-like protein KIF23 ;Centromere protein C ;E3 ubiquitin-protein ligase RING1;FACT complex subunit SSRP1;Chromobox protein homolog 3 ;Cullin-4A;Pre-mRNA-splicing regulator WTAP ;DNA damage-binding protein 1;Cordon-bleu protein-like 1;Zinc finger CCCH domain-containing protein 13;Protein virilizer homolog;Phospholipid phosphatase-related protein type 3 ;Centromere protein U ;Centromere protein L ;Nuclear pore complex protein Nup93 ;SHC SH2 domain-binding protein 1;Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16 ;Centromere protein I ;E3 ubiquitin-protein ligase ZFP91 ;Remodeling and spacing factor 1 ;E3 ubiquitin-protein ligase RING2;Centromere protein K ;Centromere protein O ;Serrate RNA effector molecule homolog ;WD repeat-containing protein 11 ;Rac GTPase-activating protein 1 ;Centromere protein H ;Chromobox protein homolog 8;Centromere protein M ;FACT complex subunit SPT16","subunits.Gene.name.":"SMARCA5;CENPB;HSPA5;HSPA8;FBL;BMI1;CENPA;KIF23;CENPC;RING1;SSRP1;CBX3;CUL4A;WTAP;DDB1;COBLL1;ZC3H13;KIAA1429;PLPPR3;CENPU;CENPL;NUP93;SHCBP1;DHX38;CENPI;ZFP91;RSF1;RNF2;CENPK;CENPO;SRRT;WDR11;RACGAP1;CENPH;CBX8;CENPM;SUPT16H","subunits.Gene.name.syn.":"SNF2H WCRF135;;GRP78;HSC70, HSP73, HSPA10;FIB1 FLRN;PCGF4 RNF51;;KNSL5 MKLP1;CENPC1 ICEN7;RNF1;FACT80;;None;KIAA0105;XAP1;KIAA0977;KIAA0853;;LPPR3 PHP2 PRG2;ICEN24 KLIP1 MLF1IP PBIP1;C1orf155 ICEN33;KIAA0095;;DDX38 KIAA0224 PRP16;FSHPRH1 ICEN19 LRPR1;ZNF757;HBXAP XAP8;BAP1 DING HIPI3 RING1B;ICEN37;ICEN36 MCM21R;ARS2 ASR2;BRWD2 KIAA1351 WDR15;KIAA1478 MGCRACGAP;ICEN35;PC3 RC1;C22orf18 ICEN39 PANE1;FACT140 FACTP140","Disease.comment":"None","Subunits.comment":"Two other subunits of the complex were found in the analysis, which have not been further characterized: unknown protein (40kD) and a protein similar to Riken cDNA 2610510J17.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":930,"ComplexName":"Scrib-beta-PIX-GIT1 complex","Organism":"Human","Synonyms":"None","Cell.line":"nontransformed mammary epithelial MCF10-2A cells","subunits.UniProt.IDs.":"Q14155;Q14160;Q9Y2X7","subunits.Entrez.IDs.":"8874;23513;28964","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation;MI:0069-mass spectrometry studies of complexes;MI:0096-pull down","GO.ID":"GO:0006887;GO:0022008;GO:0048699;GO:0005886;GO:0030054","GO.description":"exocytosis;neurogenesis;generation of neurons;plasma membrane;cell junction","FunCat.ID":"20.09.16.09.03;41.05.13;70.02;70.06","FunCat.description":"exocytosis;neurogenesis;eukaryotic plasma membrane / membrane attached;cell junction","PubMed.ID":15182672,"subunits.Protein.name.":"Rho guanine nucleotide exchange factor 7;Protein scribble homolog;ARF GTPase-activating protein GIT1","subunits.Gene.name.":"ARHGEF7;SCRIB;GIT1","subunits.Gene.name.syn.":"COOL1, KIAA0142, P85SPR, PAK3BP, PIXB;CRIB1, KIAA0147, LAP4, SCRB1, VARTUL;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Yeast two-hybrid analysis showed that beta-PIX directly interacts with hScrib and hScrib PDZ domains. GIT1 had no affinity for Scrib but, as expected, directly bound to beta-PIX. The data highlight the important role of hScrib in the retention of beta-PIX at the plasma membrane upon membrane depolarization.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":931,"ComplexName":"Scrib-beta-PIX-GIT1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"Q68FF6;Q80U72;Q9ES28","subunits.Entrez.IDs.":"216963;105782;54126","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation;MI:0096-pull down","GO.ID":"GO:0006887;GO:0022008;GO:0048699;GO:0005886","GO.description":"exocytosis;neurogenesis;generation of neurons;plasma membrane","FunCat.ID":"20.09.16.09.03;41.05.13;70.02","FunCat.description":"exocytosis;neurogenesis;eukaryotic plasma membrane / membrane attached","PubMed.ID":15182672,"subunits.Protein.name.":"ARF GTPase-activating protein GIT1 ;Protein scribble homolog ;Rho guanine nucleotide exchange factor 7","subunits.Gene.name.":"Git1;Scrib;Arhgef7","subunits.Gene.name.syn.":";Kiaa0147 Lap4 Scrib1;Kiaa0142 Pak3bp","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":932,"ComplexName":"Ppar(alpha)-Pric320 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P37230;Q8BYH8","subunits.Entrez.IDs.":"25747;109151","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0045893;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;nucleus","FunCat.ID":"11.02.03.04.01;70.10","FunCat.description":"transcription activation;nucleus","PubMed.ID":16554032,"subunits.Protein.name.":"Peroxisome proliferator-activated receptor alpha ;Chromodomain-helicase-DNA-binding protein 9","subunits.Gene.name.":"Ppara;Chd9","subunits.Gene.name.syn.":"Nr1c1 Ppar;Kiaa0308 Pric320","Disease.comment":"None","Subunits.comment":"Since Pric320 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Mus musculus (Mouse)"}
{"ComplexID":933,"ComplexName":"SCRIB-APC complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P25054;Q14160","subunits.Entrez.IDs.":"324;23513","Protein.complex.purification.method":"MI:0096- pull down;MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0051211;GO:0009798;GO:0007043;GO:0030182;GO:0030855;GO:0002009;GO:0007416","GO.description":"anisotropic cell growth;axis specification;cell-cell junction assembly;neuron differentiation;epithelial cell differentiation;morphogenesis of an epithelium;synapse assembly","FunCat.ID":"40.01.03;41.05.19;42.06.04;43.03.13;45.03.09;41.05.13.01","FunCat.description":"directional cell growth (morphogenesis);asymmetries and axis determination;intercellular junction (gap junction/adherens junction);neuron;epithelium;synaptogenesis","PubMed.ID":16611247,"subunits.Protein.name.":"Adenomatous polyposis coli protein;Protein scribble homolog","subunits.Gene.name.":"APC;SCRIB","subunits.Gene.name.syn.":"DP2.5;CRIB1, KIAA0147, LAP4, SCRB1, VARTUL","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The in vitro translated APC bound to the PDZ domains 1 and 4 of hScrib. Mutational analysis provided the evidence that APC interacts with hScrib through its C terminal class 1 PDZ domain-binding sequence Threonine-X-Valine, which is shared by the C terminal sequences of the high-risk HPV E6 proteins.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":934,"ComplexName":"FACT-NEK9 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q08945;Q8TD19;Q9Y5B9","subunits.Entrez.IDs.":"6749;91754;11198","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0006265;GO:0000082;GO:0006354;GO:0006468;GO:0006470;GO:0046777;GO:0051276;GO:0005634","GO.description":"DNA topological change;G1/S transition of mitotic cell cycle;DNA-templated transcription, elongation;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;10.03.01.01.03;11.02.03.01.04;14.07.03;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);G1/S transition of mitotic cell cycle;transcription elongation;modification by phosphorylation, dephosphorylation, autophosphorylation;organization of chromosome structure;nucleus","PubMed.ID":14660563,"subunits.Protein.name.":"FACT complex subunit SSRP1;Serine/threonine-protein kinase Nek9;FACT complex subunit SPT16","subunits.Gene.name.":"SSRP1;NEK9;SUPT16H","subunits.Gene.name.syn.":"FACT80;KIAA1995 NERCC;FACT140 FACTP140","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Nek9 forms a stable, approximately 600-kDa complex with FACT in the interphase nuclei.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":935,"ComplexName":"Scrib-APC-beta-catenin complex","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"Q02248;Q61315;Q80U72","subunits.Entrez.IDs.":"12387;11789;105782","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0051211;GO:0009798;GO:0007043;GO:0030182;GO:0030855;GO:0002009;GO:0007416","GO.description":"anisotropic cell growth;axis specification;cell-cell junction assembly;neuron differentiation;epithelial cell differentiation;morphogenesis of an epithelium;synapse assembly","FunCat.ID":"40.01.03;41.05.19;42.06.04;43.03.13;45.03.09;41.05.13.01","FunCat.description":"directional cell growth (morphogenesis);asymmetries and axis determination;intercellular junction (gap junction/adherens junction);neuron;epithelium;synaptogenesis","PubMed.ID":16611247,"subunits.Protein.name.":"Catenin beta-1;Adenomatous polyposis coli protein ;Protein scribble homolog","subunits.Gene.name.":"Ctnnb1;Apc;Scrib","subunits.Gene.name.syn.":"Catnb;;Kiaa0147 Lap4 Scrib1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":936,"ComplexName":"FACT complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q08945;Q9Y5B9","subunits.Entrez.IDs.":"6749;11198","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006265;GO:0006354;GO:0051276;GO:0005634","GO.description":"DNA topological change;DNA-templated transcription, elongation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.01.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription elongation;organization of chromosome structure;nucleus","PubMed.ID":10421373,"subunits.Protein.name.":"FACT complex subunit SSRP1;FACT complex subunit SPT16","subunits.Gene.name.":"SSRP1;SUPT16H","subunits.Gene.name.syn.":"FACT80;FACT140 FACTP140","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"FACT (for facilitates chromatin transcription) is a chromatin-specific elongation factor required for transcription of chromatin templates in vitro.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":938,"ComplexName":"FACT complex, UV-activated","Organism":"Human","Synonyms":"p53 Ser-392 kinase complex","Cell.line":"None","subunits.UniProt.IDs.":"P19784;P67870;P68400;Q08945;Q9Y5B9","subunits.Entrez.IDs.":"1459;1460;1457;6749;11198","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0006794;GO:0006796;GO:0006468;GO:0006470;GO:0046777;GO:0005515;GO:0051098;GO:0050789;GO:0006974;GO:0009314;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;protein binding;regulation of binding;regulation of biological process;cellular response to DNA damage stimulus;response to radiation;nucleus","FunCat.ID":"01.04;14.07.03;16.01;18.01.07;18;32.01.09;32.01.13;70.10","FunCat.description":"phosphate metabolism;modification by phosphorylation, dephosphorylation, autophosphorylation;protein binding;regulation by binding / dissociation;REGULATION OF METABOLISM AND PROTEIN FUNCTION;DNA damage response;electromagnetic waves stress response (e.g. UV, X-ray);nucleus","PubMed.ID":11239457,"subunits.Protein.name.":"Casein kinase II subunit alpha' ;Casein kinase II subunit beta ;Casein kinase II subunit alpha ;FACT complex subunit SSRP1;FACT complex subunit SPT16","subunits.Gene.name.":"CSNK2A2;CSNK2B;CSNK2A1;SSRP1;SUPT16H","subunits.Gene.name.syn.":"CK2A2;CK2N G5A;CK2A1;FACT80;FACT140 FACTP140","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In vitro studies show that FACT alters the specificity of CK2 in the complex such that it selectively phosphorylates p53. Phosphorylation by the kinase complex enhances p53 activity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":939,"ComplexName":"Dysferlin-Dhpr complex","Organism":"Rat","Synonyms":"None","Cell.line":"striated muscle","subunits.UniProt.IDs.":"Q02485;Q9ESD7","subunits.Entrez.IDs.":"682930;26903","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005515","GO.description":"protein binding","FunCat.ID":"16.01","FunCat.description":"protein binding","PubMed.ID":16550931,"subunits.Protein.name.":"Voltage-dependent L-type calcium channel subunit alpha-1S;Dysferlin","subunits.Gene.name.":"Cacna1s;Dysf","subunits.Gene.name.syn.":"Cach1 Cacn1 Cacnl1a3 Cchl1a3;Fer1l1","Disease.comment":"Dysf is involved in Miyoshi myopathy and limb-girdle muscular dystrophy 2B.","Subunits.comment":"Since Dysf from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Mus musculus (Mouse)"}
{"ComplexID":940,"ComplexName":"AnnexinVI-Fyn-Pyk2-RasGAP complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P48037;P50904;P70600;Q62844","subunits.Entrez.IDs.":"79125;25676;50646;25150","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515;GO:0035556","GO.description":"protein binding;intracellular signal transduction","FunCat.ID":"16.01;30.01","FunCat.description":"protein binding;cellular signalling","PubMed.ID":10708762,"subunits.Protein.name.":"Annexin A6;Ras GTPase-activating protein 1 ;Protein-tyrosine kinase 2-beta ;Tyrosine-protein kinase Fyn","subunits.Gene.name.":"Anxa6;Rasa1;Ptk2b;Fyn","subunits.Gene.name.syn.":"Anx6;Rasa;Fak2 Pyk2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":941,"ComplexName":"Arf1-Ap1g1-Ap1b1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"B2RYN6;P52303;P84079","subunits.Entrez.IDs.":"171494;29663;64310","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515;GO:0016192","GO.description":"protein binding;vesicle-mediated transport","FunCat.ID":"16.01;20.09.07","FunCat.description":"protein binding;vesicular transport (Golgi network, etc.)","PubMed.ID":10807927,"subunits.Protein.name.":"Adaptor-related protein complex 1, gamma 1 subunit, isoform CRA_b ;AP-1 complex subunit beta-1 ;ADP-ribosylation factor 1","subunits.Gene.name.":"Ap1g1;Ap1b1;Arf1","subunits.Gene.name.syn.":";Adtb1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":942,"ComplexName":"Cd44-Ots8 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P26051;Q64294","subunits.Entrez.IDs.":"25406;54320","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0030- cross-linking studies","GO.ID":"GO:0016477;GO:0016049;GO:0001935","GO.description":"cell migration;cell growth;endothelial cell proliferation","FunCat.ID":"34.05.01;40.01","FunCat.description":"cell migration;cell growth / morphogenesis","PubMed.ID":10903424,"subunits.Protein.name.":"CD44 antigen;Podoplanin","subunits.Gene.name.":"Cd44;Pdpn","subunits.Gene.name.syn.":"None;Gp38 Ots8","Disease.comment":"CD44 is involved in adhesion interactions and tumor metastasis.","Subunits.comment":"None","Complex.comment":"TS-8 may alter the mode of endothelial cell growth and/or migration induced by CD44 in tumor angiogenesis.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":943,"ComplexName":"Class C Vps complex (VPS11, VPS18, STX7)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15400;Q9H270;Q9P253","subunits.Entrez.IDs.":"8417;55823;57617","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0071- molecular sieving","GO.ID":"GO:0016192;GO:0005768;GO:0005773;GO:0005764","GO.description":"vesicle-mediated transport;endosome;vacuole;lysosome","FunCat.ID":"20.09.07;70.22;70.25","FunCat.description":"vesicular transport (Golgi network, etc.);endosome;vacuole or lysosome","PubMed.ID":11382755,"subunits.Protein.name.":"Syntaxin-7;Vacuolar protein sorting-associated protein 11 homolog;Vacuolar protein sorting-associated protein 18 homolog","subunits.Gene.name.":"STX7;VPS11;VPS18","subunits.Gene.name.syn.":";RNF108;KIAA1475","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Mammalian Class C Vps proteins are predominantly associated with late endosomes/lysosomes and mediate vesicle trafficking steps in the endosome/lysosome pathway.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":944,"ComplexName":"Class C Vps complex (VPS11, VPS18, VPS16)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q9H269;Q9H270;Q9P253","subunits.Entrez.IDs.":"64601;55823;57617","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016192;GO:0005768;GO:0005773;GO:0005764","GO.description":"vesicle-mediated transport;endosome;vacuole;lysosome","FunCat.ID":"20.09.07;70.22;70.25","FunCat.description":"vesicular transport (Golgi network, etc.);endosome;vacuole or lysosome","PubMed.ID":11382755,"subunits.Protein.name.":"Vacuolar protein sorting-associated protein 16 homolog;Vacuolar protein sorting-associated protein 11 homolog;Vacuolar protein sorting-associated protein 18 homolog","subunits.Gene.name.":"VPS16;VPS11;VPS18","subunits.Gene.name.syn.":"None;RNF108;KIAA1475","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Mammalian Class C Vps proteins are predominantly associated with late endosomes/lysosomes, mediate vesicle trafficking steps in the endosome/lysosome pathway and are suggested to play a role in SNARE complex assembly.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":945,"ComplexName":"Class C Vps complex (hVPS11, hVPS18, rVPS33a )","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q63615;Q9H270;Q9P253","subunits.Entrez.IDs.":"65081;55823;57617","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0071- molecular sieving","GO.ID":"GO:0016192;GO:0005768;GO:0005773;GO:0005764","GO.description":"vesicle-mediated transport;endosome;vacuole;lysosome","FunCat.ID":"20.09.07;70.22;70.25","FunCat.description":"vesicular transport (Golgi network, etc.);endosome;vacuole or lysosome","PubMed.ID":11382755,"subunits.Protein.name.":"Vacuolar protein sorting-associated protein 33A ;Vacuolar protein sorting-associated protein 11 homolog;Vacuolar protein sorting-associated protein 18 homolog","subunits.Gene.name.":"Vps33a;VPS11;VPS18","subunits.Gene.name.syn.":";RNF108;KIAA1475","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Mammalian Class C Vps proteins are predominantly associated with late endosomes/lysosomes, mediate vesicle trafficking steps in the endosome/lysosome pathway and are suggested to play a role in SNARE complex assembly.","SWISSPROT.organism":"Rattus norvegicus (Rat);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":946,"ComplexName":"Class C Vps complex (hVPS11, hVPS18, hVPS16, rVPS33a )","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q63615;Q9H269;Q9H270;Q9P253","subunits.Entrez.IDs.":"65081;64601;55823;57617","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016192;GO:0005768;GO:0005773;GO:0005764","GO.description":"vesicle-mediated transport;endosome;vacuole;lysosome","FunCat.ID":"20.09.07;70.22;70.25","FunCat.description":"vesicular transport (Golgi network, etc.);endosome;vacuole or lysosome","PubMed.ID":11382755,"subunits.Protein.name.":"Vacuolar protein sorting-associated protein 33A ;Vacuolar protein sorting-associated protein 16 homolog;Vacuolar protein sorting-associated protein 11 homolog;Vacuolar protein sorting-associated protein 18 homolog","subunits.Gene.name.":"Vps33a;VPS16;VPS11;VPS18","subunits.Gene.name.syn.":";None;RNF108;KIAA1475","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Mammalian Class C Vps proteins are predominantly associated with late endosomes/lysosomes, mediate vesicle trafficking steps in the endosome/lysosome pathway and are suggested to play a role in SNARE complex assembly.","SWISSPROT.organism":"Rattus norvegicus (Rat);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":947,"ComplexName":"CDC7-DBF7 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00311;Q9UBU7","subunits.Entrez.IDs.":"8317;10926","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006260;GO:0051052","GO.description":"DNA replication;regulation of DNA metabolic process","FunCat.ID":"10.01.03;10.01.11","FunCat.description":"DNA synthesis and replication;regulation of DNA processing","PubMed.ID":10523313,"subunits.Protein.name.":"Cell division cycle 7-related protein kinase ;Protein DBF4 homolog A","subunits.Gene.name.":"CDC7;DBF4","subunits.Gene.name.syn.":"CDC7L1;ASK DBF4A ZDBF1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":948,"ComplexName":"Kif17-Lin10 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"Q922R1;Q99PW8","subunits.Entrez.IDs.":"234678;16559","Protein.complex.purification.method":"MI:0018-two hybrid;MI:0107-surface plasmon resonance","GO.ID":"GO:0030705;GO:0050896;GO:0022008;GO:0048699;GO:0030182;GO:0048167","GO.description":"cytoskeleton-dependent intracellular transport;response to stimulus;neurogenesis;generation of neurons;neuron differentiation;regulation of synaptic plasticity","FunCat.ID":"20.09.14;36.25;41.05.13;43.03.13","FunCat.description":"cytoskeleton-dependent transport;animal specific systemic sensing and response;neurogenesis;neuron","PubMed.ID":10846156,"subunits.Protein.name.":"UPF0183 protein C16orf70 homolog;Kinesin-like protein KIF17","subunits.Gene.name.":";Kif17","subunits.Gene.name.syn.":";None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors suggest that KIF17, a neuron-specific molecular motor with microtubule plus-end-directed motility interacts directly with a mLin-10 PDZ domain, resulting in the transport of NR2B in dendrites. They propose this motor-cargo complex as the sorting machinery for NR2B.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":949,"ComplexName":"SNARE complex (Stx1a, Snap25, Vamp2)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P32851;P60881;P63045","subunits.Entrez.IDs.":"116470;25012;24803","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":15316007,"subunits.Protein.name.":"Syntaxin-1A;Synaptosomal-associated protein 25;Vesicle-associated membrane protein 2","subunits.Gene.name.":"Stx1a;Snap25;Vamp2","subunits.Gene.name.syn.":"Sap;Snap;Syb2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":950,"ComplexName":"SNARE complex (Stx1a, Snap25, Stxbp5)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P32851;P60881;Q9WU70","subunits.Entrez.IDs.":"116470;25012;81022","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":15316007,"subunits.Protein.name.":"Syntaxin-1A;Synaptosomal-associated protein 25;Syntaxin-binding protein 5","subunits.Gene.name.":"Stx1a;Snap25;Stxbp5","subunits.Gene.name.syn.":"Sap;Snap;Llgl3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":951,"ComplexName":"Fmrp-Lgl complex","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P35922;Q80Y17","subunits.Entrez.IDs.":"14265;16897","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007416","GO.description":"synapse assembly","FunCat.ID":"41.05.13.01","FunCat.description":"synaptogenesis","PubMed.ID":15621528,"subunits.Protein.name.":"Synaptic functional regulator FMR1 ;Lethal","subunits.Gene.name.":"Fmr1;Llgl1","subunits.Gene.name.syn.":"Fmr-1;Llglh","Disease.comment":"FMR1 gene is involved in Fragile X syndrome.","Subunits.comment":"None","Complex.comment":"The Fmrp/Lgl/mRNA complex is developmentally regulated in mice.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":952,"ComplexName":"Kif13a-AP1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"O35643;P22892;P35585;Q8CA55","subunits.Entrez.IDs.":"11764;11765;11767;16553","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0096-pull down;MI:0018-two hybrid;MI:0027-cosedimentation","GO.ID":"GO:0015031;GO:0008565;GO:0016192","GO.description":"protein transport;protein transporter activity;vesicle-mediated transport","FunCat.ID":"20.01.10;20.09.07","FunCat.description":"protein transport;vesicular transport (Golgi network, etc.)","PubMed.ID":11106728,"subunits.Protein.name.":"AP-1 complex subunit beta-1;AP-1 complex subunit gamma-1;AP-1 complex subunit mu-1;Putative uncharacterized protein","subunits.Gene.name.":"Ap1b1;Ap1g1;Ap1m1;Kif13a","subunits.Gene.name.syn.":"Adtb1;Adtg Clapg1;Cltnm;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"KIF13A transports the mannose-6-phosphate receptor to the plasma membrane through direct interaction with AP-1 complex.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":953,"ComplexName":"p97-Ufd1-Npl4-IP3 receptor complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P11881;P60670;P70362;Q01853","subunits.Entrez.IDs.":"16438;217365;22230;269523","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0043161;GO:0006511;GO:0005515;GO:0005783;GO:0048015","GO.description":"proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;protein binding;endoplasmic reticulum;phosphatidylinositol-mediated signaling","FunCat.ID":"14.13.01.01;16.01;70.07","FunCat.description":"proteasomal degradation (ubiquitin/proteasomal pathway);protein binding;endoplasmic reticulum","PubMed.ID":16103111,"subunits.Protein.name.":"Inositol 1,4,5-trisphosphate receptor type 1 ;Nuclear protein localization protein 4 homolog ;Ubiquitin fusion degradation protein 1 homolog ;Transitional endoplasmic reticulum ATPase","subunits.Gene.name.":"Itpr1;Nploc4;Ufd1l;Vcp","subunits.Gene.name.syn.":"Insp3r Pcd6 Pcp1;Kiaa1499 Npl4;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The p97-Ufd1-Npl4 complex couples ubiquitinated IP3 receptors to proteasomal degradation and plays a key role in IP3 receptor processing. These data also establish that the p97-Ufd1-Npl4 complex mediates endoplasmic reticulum-associated degradation in mammalian cells.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":954,"ComplexName":"p97-Ufd1-Npl4-IP3 receptor complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P29994;P46462;Q9ES53;Q9ES54","subunits.Entrez.IDs.":"25262;116643;84478;140639","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0043161;GO:0006511;GO:0005515;GO:0005783;GO:0048015","GO.description":"proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;protein binding;endoplasmic reticulum;phosphatidylinositol-mediated signaling","FunCat.ID":"14.13.01.01;16.01;70.07","FunCat.description":"proteasomal degradation (ubiquitin/proteasomal pathway);protein binding;endoplasmic reticulum","PubMed.ID":16103111,"subunits.Protein.name.":"Inositol 1,4,5-trisphosphate receptor type 1;Transitional endoplasmic reticulum ATPase;Ubiquitin fusion degradation protein 1 homolog;Nuclear protein localization protein 4 homolog","subunits.Gene.name.":"Itpr1;Vcp;Ufd1l;Nploc4","subunits.Gene.name.syn.":"Insp3r;None;None;Npl4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The p97-Ufd1-Npl4 complex couples ubiquitinated IP3 receptors to proteasomal degradation and plays a key role in IP3 receptor processing. These data also establish that the p97-Ufd1-Npl4 complex mediates endoplasmic reticulum-associated degradation in mammalian cells.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":955,"ComplexName":"LLGL2-PAR-6B-PRKCI complex","Organism":"Human","Synonyms":"None","Cell.line":"epithelium","subunits.UniProt.IDs.":"P41743;Q6P1M3;Q9BYG5","subunits.Entrez.IDs.":"5584;3993;84612","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0051211;GO:0009798;GO:0007043;GO:0030054","GO.description":"anisotropic cell growth;axis specification;cell-cell junction assembly;cell junction","FunCat.ID":"40.01.03;41.05.19;42.06.04;70.06","FunCat.description":"directional cell growth (morphogenesis);asymmetries and axis determination;intercellular junction (gap junction/adherens junction);cell junction","PubMed.ID":12725730,"subunits.Protein.name.":"Protein kinase C iota type;Lethal;Partitioning defective 6 homolog beta","subunits.Gene.name.":"PRKCI;LLGL2;PARD6B","subunits.Gene.name.syn.":"DXS1179E;;PAR6B","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Mammalian Lgl-2 competes with PAR-3 for its incorporation to the PAR-6B/aPKC lambda complex in cDNA-transfected 293T cells  and support the presence of two independent protein complexes containing PAR-6B/aPKC lambda. Further results indicate that mLgl-2 interacts with the PDZ domain of PAR-6B and with the kinase domain of aPKC lambda and forms a protein complex independently of the one containing PAR-3. It was suggested that phosphorylation of mLgl-1/2 by aPKC lambda occurs during the cell-cell contact-induced cell polarization and that this is accompanied by dissociation of the interaction between mLgl-2 and the PAR-6B/aPKC lambda complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":956,"ComplexName":"PAR-3-PAR-6B-PRKCI complex","Organism":"Human","Synonyms":"None","Cell.line":"epithelium","subunits.UniProt.IDs.":"P41743;Q8TEW0;Q9BYG5","subunits.Entrez.IDs.":"5584;56288;84612","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0051211;GO:0009798;GO:0007043;GO:0030054","GO.description":"anisotropic cell growth;axis specification;cell-cell junction assembly;cell junction","FunCat.ID":"40.01.03;41.05.19;42.06.04;70.06","FunCat.description":"directional cell growth (morphogenesis);asymmetries and axis determination;intercellular junction (gap junction/adherens junction);cell junction","PubMed.ID":12725730,"subunits.Protein.name.":"Protein kinase C iota type;Partitioning defective 3 homolog;Partitioning defective 6 homolog beta","subunits.Gene.name.":"PRKCI;PARD3;PARD6B","subunits.Gene.name.syn.":"DXS1179E;PAR3, PAR3A;PAR6B","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Mammalian Lgl-2 competes with PAR-3 for its incorporation to the PAR-6B/aPKC lambda complex in cDNA-transfected 293T cells  and support the presence of two independent protein complexes containing PAR-6B/aPKC lambda.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":957,"ComplexName":"p97-Ufd1-Npl4 complex","Organism":"Rat","Synonyms":"None","Cell.line":"liver","subunits.UniProt.IDs.":"P46462;Q9ES53;Q9ES54","subunits.Entrez.IDs.":"116643;84478;140639","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0006794;GO:0006796;GO:0043161;GO:0006511;GO:0030968;GO:0005737","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;endoplasmic reticulum unfolded protein response;cytoplasm","FunCat.ID":"01.04;14.13.01.01;32.01.07;70.03","FunCat.description":"phosphate metabolism;proteasomal degradation (ubiquitin/proteasomal pathway);unfolded protein response (e.g. ER quality control);cytoplasm","PubMed.ID":10811609,"subunits.Protein.name.":"Transitional endoplasmic reticulum ATPase;Ubiquitin fusion degradation protein 1 homolog;Nuclear protein localization protein 4 homolog","subunits.Gene.name.":"Vcp;Ufd1l;Nploc4","subunits.Gene.name.syn.":"None;None;Npl4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ufd1/Npl4 and p47 compete for p97 binding and form alternative complexes in cytosol.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":958,"ComplexName":"Ufd1-Npl4 complex","Organism":"Rat","Synonyms":"None","Cell.line":"liver","subunits.UniProt.IDs.":"Q9ES53;Q9ES54","subunits.Entrez.IDs.":"84478;140639","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0043161;GO:0006511;GO:0005737","GO.description":"proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;cytoplasm","FunCat.ID":"14.13.01.01;70.03","FunCat.description":"proteasomal degradation (ubiquitin/proteasomal pathway);cytoplasm","PubMed.ID":10811609,"subunits.Protein.name.":"Ubiquitin fusion degradation protein 1 homolog;Nuclear protein localization protein 4 homolog","subunits.Gene.name.":"Ufd1l;Nploc4","subunits.Gene.name.syn.":"None;Npl4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This protein complex acts as adapters, directing a basic TER ATPase activity into different cellular pathways.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":959,"ComplexName":"LLGL1-PAR-6B-PRKCI complex","Organism":"Human","Synonyms":"None","Cell.line":"epithelium","subunits.UniProt.IDs.":"P41743;Q15334;Q9BYG5","subunits.Entrez.IDs.":"5584;3996;84612","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0051211;GO:0009798;GO:0007043;GO:0030054","GO.description":"anisotropic cell growth;axis specification;cell-cell junction assembly;cell junction","FunCat.ID":"40.01.03;41.05.19;42.06.04;70.06","FunCat.description":"directional cell growth (morphogenesis);asymmetries and axis determination;intercellular junction (gap junction/adherens junction);cell junction","PubMed.ID":12725730,"subunits.Protein.name.":"Protein kinase C iota type;Lethal;Partitioning defective 6 homolog beta","subunits.Gene.name.":"PRKCI;LLGL1;PARD6B","subunits.Gene.name.syn.":"DXS1179E;DLG4 HUGL HUGL1;PAR6B","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Experiments done in lysates of MDCK, MTD-1A, or Caco 2 cells. The results indicate that PAR-6/aPKC selectively interacts with either mLgl or PAR-3 under the control of aPKC activity to regulate epithelial cell polarity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":960,"ComplexName":"p97-p47 oligomer complex","Organism":"Rat","Synonyms":"None","Cell.line":"liver","subunits.UniProt.IDs.":"O35987;P46462","subunits.Entrez.IDs.":"83809;116643","Protein.complex.purification.method":"MI:0071-molecular sieving","GO.ID":"GO:0006794;GO:0006796;GO:0006906;GO:0007030;GO:0005737;GO:0005794","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;vesicle fusion;Golgi organization;cytoplasm;Golgi apparatus","FunCat.ID":"01.04;20.09.07.27;42.08;70.03;70.08","FunCat.description":"phosphate metabolism;vesicle fusion;Golgi;cytoplasm;Golgi","PubMed.ID":9214505,"subunits.Protein.name.":"NSFL1 cofactor p47;Transitional endoplasmic reticulum ATPase","subunits.Gene.name.":"Nsfl1c;Vcp","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"p47 is a cofactor for p97-mediated membrane fusion(one trimer of p47 per hexamer of p97).","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":961,"ComplexName":"Tamalin-mGluR1a-cytohesin complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P23385;P63035;Q8R4T5","subunits.Entrez.IDs.":"24414;116692;192254","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0007215","GO.description":"intracellular protein transport;protein targeting;protein transport;glutamate receptor signaling pathway","FunCat.ID":"14.04;20.01.10;30.05.02.24.05","FunCat.description":"protein targeting, sorting and translocation;protein transport;glutamate signalling pathway","PubMed.ID":11850456,"subunits.Protein.name.":"Metabotropic glutamate receptor 1 ;Cytohesin-2 ;General receptor for phosphoinositides 1-associated scaffold protein","subunits.Gene.name.":"Grm1;Cyth2;Grasp","subunits.Gene.name.syn.":"Gprc1a Mglur1;Pscd2 Sec7b;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors  suggest that the PDZ domain-containing proteins like tamalin may play a key role in connecting glutamate receptors to small GTP-binding proteins that regulate intracellular protein transport and synaptic organization.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":962,"ComplexName":"Tamalin-mGluR1a complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P23385;Q8R4T5","subunits.Entrez.IDs.":"24414;192254","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0018- two hybrid","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0007215","GO.description":"intracellular protein transport;protein targeting;protein transport;glutamate receptor signaling pathway","FunCat.ID":"14.04;20.01.10;30.05.02.24.05","FunCat.description":"protein targeting, sorting and translocation;protein transport;glutamate signalling pathway","PubMed.ID":11850456,"subunits.Protein.name.":"Metabotropic glutamate receptor 1 ;General receptor for phosphoinositides 1-associated scaffold protein","subunits.Gene.name.":"Grm1;Grasp","subunits.Gene.name.syn.":"Gprc1a Mglur1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors show that tamalin causes an increase in not only cell-surface expression of mGluR1a in transfected cells but also in neuritic distribution of endogenous mGluR5 in cultured hippocampal neurons.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":963,"ComplexName":"Tamalin-mGluR5 complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P22756;Q8R4T5","subunits.Entrez.IDs.":"29559;192254","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0018- two hybrid","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0007215","GO.description":"intracellular protein transport;protein targeting;protein transport;glutamate receptor signaling pathway","FunCat.ID":"14.04;20.01.10;30.05.02.24.05","FunCat.description":"protein targeting, sorting and translocation;protein transport;glutamate signalling pathway","PubMed.ID":11850456,"subunits.Protein.name.":"Glutamate receptor ionotropic, kainate 1 ;General receptor for phosphoinositides 1-associated scaffold protein","subunits.Gene.name.":"Grik1;Grasp","subunits.Gene.name.syn.":"Glur5;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors show that tamalin causes an increase in not only cell-surface expression of mGluR1a in transfected cells but also in neuritic distribution of endogenous mGluR5 in cultured hippocampal neurons.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":964,"ComplexName":"BRCA1-RAD50-MRE11-NBS1 complex","Organism":"Human","Synonyms":"BRCA1-RAD50-MRE11-p95 complex","Cell.line":"None","subunits.UniProt.IDs.":"O60934;P38398;P49959;Q92878","subunits.Entrez.IDs.":"4683;672;4361;10111","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0006974;GO:0005634","GO.description":"DNA repair;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;32.01.09;70.10","FunCat.description":"DNA repair;DNA damage response;nucleus","PubMed.ID":10426999,"subunits.Protein.name.":"Nibrin ;Breast cancer type 1 susceptibility protein;Double-strand break repair protein MRE11A ;DNA repair protein RAD50","subunits.Gene.name.":"NBN;BRCA1;MRE11A;RAD50","subunits.Gene.name.syn.":"NBS NBS1 P95;RNF53;HNGS1 MRE11;","Disease.comment":"BRCA1 is involved in breast cancer.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":965,"ComplexName":"mPar6c-Mlgl-aPKC complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q62074;Q80Y17;Q9Z101","subunits.Entrez.IDs.":"18759;16897;56513","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0051211;GO:0009798;GO:0030855;GO:0002009","GO.description":"anisotropic cell growth;axis specification;epithelial cell differentiation;morphogenesis of an epithelium","FunCat.ID":"40.01.03;41.05.19;45.03.09","FunCat.description":"directional cell growth (morphogenesis);asymmetries and axis determination;epithelium","PubMed.ID":12629547,"subunits.Protein.name.":"Protein kinase C iota type;Lethal;Partitioning defective 6 homolog alpha","subunits.Gene.name.":"Prkci;Llgl1;Pard6a","subunits.Gene.name.syn.":"Pkcl, aPKClambda;Llglh;Par6a","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The data suggest that the phosphorylation of Mlgl by aPKC is important for appropriate cell polarization in the wounding assay. The authors propose that an interaction between Mlgl, mPar-6C and aPKC, and the consequent phosphorylation of Mlgl, may regulate Mlgl in a polarized fashion such that it can exert localized effects on protein trafficking and secretion.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":966,"ComplexName":"Rab27A-Melanophilin-MyosinVa complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q91V27;Q99104;Q9ERI2","subunits.Entrez.IDs.":"171531;17918;11891","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0015031;GO:0008565","GO.description":"protein transport;protein transporter activity","FunCat.ID":"20.01.10","FunCat.description":"protein transport","PubMed.ID":11856727,"subunits.Protein.name.":"Melanophilin ;Unconventional myosin-Va ;Ras-related protein Rab-27A","subunits.Gene.name.":"Mlph;Myo5a;Rab27a","subunits.Gene.name.syn.":"Ln Slac2a;Dilute;","Disease.comment":"Mutation in the Myo5a gene causes pigment granule transport defects in human Griscelli syndrome.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":967,"ComplexName":"Pallidin-Mu complex","Organism":"Mouse","Synonyms":"BLOC-1 complex","Cell.line":"skin","subunits.UniProt.IDs.":"Q8R015;Q9R0C0","subunits.Entrez.IDs.":"17828;18457","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007040;GO:0007033","GO.description":"lysosome organization;vacuole organization","FunCat.ID":"42.25","FunCat.description":"vacuole or lysosome","PubMed.ID":12019270,"subunits.Protein.name.":"Biogenesis of lysosome-related organelles complex 1 subunit 5;Biogenesis of lysosome-related organelles complex 1 subunit 6","subunits.Gene.name.":"Bloc1s5;Bloc1s6","subunits.Gene.name.syn.":"Mu Muted;P2 Pa Pldn","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors propose that BLOC-1 mediates the biogenesis of lysosome-related organelles by a mechanism that may involve self-assembly and interaction with the actin cytoskeleton.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":968,"ComplexName":"Crb1-Mupp1-Pals1-Mpp4 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"eye","subunits.UniProt.IDs.":"Q6P7F1;Q8VBX6;Q8VHS2;Q9JLB2","subunits.Entrez.IDs.":"227157;17475;170788;56217","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0007601;GO:0051211;GO:0007043;GO:0001654;GO:0030054","GO.description":"visual perception;anisotropic cell growth;cell-cell junction assembly;eye development;cell junction","FunCat.ID":"34.11.01.03;40.01.03;42.06.04;47.03.02.02;70.06","FunCat.description":"visual transduction;directional cell growth (morphogenesis);intercellular junction (gap junction/adherens junction);eye;cell junction","PubMed.ID":15316081,"subunits.Protein.name.":"MAGUK p55 subfamily member 4;Multiple PDZ domain protein;Protein crumbs homolog 1;MAGUK p55 subfamily member 5","subunits.Gene.name.":"Mpp4;Mpdz;Crb1;Mpp5","subunits.Gene.name.syn.":"Dlg6;Mupp1;None;Pals1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In Crb1-/- retinas before the onset of retinal degeneration, the complex between Mupp1, Pals1 and Mpp4 formed in the absence of Crb1, indicating that Crb1 is not essential for this interaction.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":969,"ComplexName":"CRB3-PALS1-PATJ cell polarity complex","Organism":"Dog","Synonyms":"None","Cell.line":"epithelium","subunits.UniProt.IDs.":"Q63ZW7;Q8QZT4;Q9JLB2","subunits.Entrez.IDs.":"12695;224912;56217","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0051211;GO:0009798;GO:0007043;GO:0030054","GO.description":"anisotropic cell growth;axis specification;cell-cell junction assembly;cell junction","FunCat.ID":"40.01.03;41.05.19;42.06.04;70.06","FunCat.description":"directional cell growth (morphogenesis);asymmetries and axis determination;intercellular junction (gap junction/adherens junction);cell junction","PubMed.ID":12527193,"subunits.Protein.name.":"InaD-like protein ;Protein crumbs homolog 3;MAGUK p55 subfamily member 5","subunits.Gene.name.":"Patj;Crb3;Mpp5","subunits.Gene.name.syn.":"Cipp Inadl;;Pals1","Disease.comment":"None","Subunits.comment":"Since CRB3, INADL and MPP5 from dog were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.","Complex.comment":"CRB3, PATJ and PALS1 form a ternary complex in MDCK epithelial cells.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":970,"ComplexName":"Rab11Fip2-Ap2a complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P17426;Q3U366","subunits.Entrez.IDs.":"11771;74998","Protein.complex.purification.method":"MI:0096-pull down","GO.ID":"GO:0006898","GO.description":"receptor-mediated endocytosis","FunCat.ID":"20.09.18.09.01.01","FunCat.description":"receptor-mediated endocytosis","PubMed.ID":12364336,"subunits.Protein.name.":"AP-2 complex subunit alpha-1;Putative uncharacterized protein","subunits.Gene.name.":"Ap2a1;Rab11fip2","subunits.Gene.name.syn.":"Adtaa Clapa1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Rab11-FIP2 influences endocytosis through its ability to interact with the adaptor complex AP-2.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":971,"ComplexName":"Rab11-Fip2-Reps1 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS","subunits.UniProt.IDs.":"O54916;Q3U366","subunits.Entrez.IDs.":"19707;74998","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0006898","GO.description":"intracellular protein transport;protein targeting;protein transport;receptor-mediated endocytosis","FunCat.ID":"14.04;20.01.10;20.09.18.09.01.01","FunCat.description":"protein targeting, sorting and translocation;protein transport;receptor-mediated endocytosis","PubMed.ID":12364336,"subunits.Protein.name.":"RalBP1-associated Eps domain-containing protein 1 ;Putative uncharacterized protein","subunits.Gene.name.":"Reps1;Rab11fip2","subunits.Gene.name.syn.":";None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":972,"ComplexName":"MRN complex (MRE11-RAD50-NBS1 complex)","Organism":"Human","Synonyms":"RAD50-MRE11-p95 complex; MRE11 complex","Cell.line":"None","subunits.UniProt.IDs.":"O60934;P49959;Q92878","subunits.Entrez.IDs.":"4683;4361;10111","Protein.complex.purification.method":"MI:0226- ion exchange chromatography; MI:0006- anti bait coimmunoprecipitation; MI:0071- molecular sieving","GO.ID":"GO:0006308;GO:0006281;GO:0000075;GO:0006974;GO:0005634","GO.description":"DNA catabolic process;DNA repair;cell cycle checkpoint;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"01.03.16.03;10.01.05.01;10.03.01.03;32.01.09;70.10","FunCat.description":"DNA degradation;DNA repair;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA damage response;nucleus","PubMed.ID":9590181,"subunits.Protein.name.":"Nibrin ;Double-strand break repair protein MRE11A ;DNA repair protein RAD50","subunits.Gene.name.":"NBN;MRE11A;RAD50","subunits.Gene.name.syn.":"NBS NBS1 P95;HNGS1 MRE11;","Disease.comment":"Rad50-MRE11-p95 protein complex is involved in Nijmegen breakage syndrome.","Subunits.comment":"None","Complex.comment":"The implication of hMre11/hRad50/p95 protein complex in NBS reveals a direct molecular link between DSB repair and cell cycle checkpoint functions.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":973,"ComplexName":"Sec61alpha-CollagenIV-Hsp47 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P02463;P19324;P61620","subunits.Entrez.IDs.":"12826;12406;53421","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0006461;GO:0005783","GO.description":"intracellular protein transport;protein targeting;protein transport;protein complex assembly;endoplasmic reticulum","FunCat.ID":"14.04;20.01.10;14.10;70.07","FunCat.description":"protein targeting, sorting and translocation;protein transport;assembly of protein complexes;endoplasmic reticulum","PubMed.ID":12532224,"subunits.Protein.name.":"Collagen alpha-1;Serpin H1 ;Protein transport protein Sec61 subunit alpha isoform 1","subunits.Gene.name.":"Col4a1;Serpinh1;Sec61a1","subunits.Gene.name.syn.":";Cbp1 Hsp47;Sec61a","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Sec61a may form complexes with Hsp47 and other ER proteins during the constitutive synthesis of collagen IV by F9 cells after retinoic acid treatment.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":974,"ComplexName":"EED-EZH2 complex","Organism":"Human","Synonyms":"ESC-E(Z) complex; H3-specific methyltransferase complex","Cell.line":"None","subunits.UniProt.IDs.":"O75530;Q09028;Q15022;Q15910;Q6ZN18","subunits.Entrez.IDs.":"8726;5928;23512;2146;121536","Protein.complex.purification.method":"MI:0091- chromatography technologies; MI:0071- molecular sieving; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006265;GO:0032774;GO:0018126;GO:0006479;GO:0051276;GO:0005634","GO.description":"DNA topological change;RNA biosynthetic process;protein hydroxylation;protein methylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02;14.07.09;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);RNA synthesis;posttranslational modification of amino acids (e.g. hydroxylation, methylation);organization of chromosome structure;nucleus","PubMed.ID":12351676,"subunits.Protein.name.":"Polycomb protein EED;Histone-binding protein RBBP4;Polycomb protein SUZ12;Histone-lysine N-methyltransferase EZH2;Zinc finger protein AEBP2","subunits.Gene.name.":"EED;RBBP4;SUZ12;EZH2;AEBP2","subunits.Gene.name.syn.":"None;RBAP48;CHET9 JJAZ1 KIAA0160;KMT6;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results support a model in which ESC-E(Z)-mediated H3-K27 methylation serves as a signal for the recruitment of the PRC1 complex by facilitating PC binding.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":975,"ComplexName":"Ocrl-Cdc42 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P60766;Q6NVF0","subunits.Entrez.IDs.":"12540;320634","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0005794","GO.description":"intracellular protein transport;protein targeting;protein transport;Golgi apparatus","FunCat.ID":"14.04;20.01.10;70.08","FunCat.description":"protein targeting, sorting and translocation;protein transport;Golgi","PubMed.ID":12915445,"subunits.Protein.name.":"Cell division control protein 42 homolog;Inositol polyphosphate 5-phosphatase OCRL-1","subunits.Gene.name.":"Cdc42;Ocrl","subunits.Gene.name.syn.":"None;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cdc42 associates significantly with OCRL1 RhoGAP in GST pulldown and membrane translocation assays, no interaction between endogenous OCRL1 and Cdc42 could be detected in coimmunoprecipitation experiments (PMID:12915445).","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":976,"ComplexName":"SNARE complex (Stx1a, Snap25, Vamp2)","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P32851;P60881;P63045","subunits.Entrez.IDs.":"116470;25012;24803","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":15975093,"subunits.Protein.name.":"Syntaxin-1A;Synaptosomal-associated protein 25;Vesicle-associated membrane protein 2","subunits.Gene.name.":"Stx1a;Snap25;Vamp2","subunits.Gene.name.syn.":"Sap;Snap;Syb2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":977,"ComplexName":"SNARE complex (Stx2, Snap25, Vamp2)","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P50279;P60881;P63045","subunits.Entrez.IDs.":"25130;25012;24803","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":15975093,"subunits.Protein.name.":"Syntaxin-2 ;Synaptosomal-associated protein 25;Vesicle-associated membrane protein 2","subunits.Gene.name.":"Stx2;Snap25;Vamp2","subunits.Gene.name.syn.":"Epim;Snap;Syb2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":978,"ComplexName":"SNARE complex (Stx3, Snap25, Vamp2)","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P60881;P63045;Q08849","subunits.Entrez.IDs.":"25012;24803;81802","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":15975093,"subunits.Protein.name.":"Synaptosomal-associated protein 25;Vesicle-associated membrane protein 2;Syntaxin-3","subunits.Gene.name.":"Snap25;Vamp2;Stx3","subunits.Gene.name.syn.":"Snap;Syb2;Stx3a","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":979,"ComplexName":"SNARE complex (Stx4, Snap25, Vamp2)","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P60881;P63045;Q08850","subunits.Entrez.IDs.":"25012;24803;81803","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":15975093,"subunits.Protein.name.":"Synaptosomal-associated protein 25;Vesicle-associated membrane protein 2;Syntaxin-4","subunits.Gene.name.":"Snap25;Vamp2;Stx4","subunits.Gene.name.syn.":"Snap;Syb2;Stx4a","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":980,"ComplexName":"SNARE complex (Stx4, Snap25, Vamp2, Syt1)","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P21707;P60881;P63045;Q08850","subunits.Entrez.IDs.":"25716;25012;24803;81803","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":15975093,"subunits.Protein.name.":"Synaptotagmin-1 ;Synaptosomal-associated protein 25;Vesicle-associated membrane protein 2;Syntaxin-4","subunits.Gene.name.":"Syt1;Snap25;Vamp2;Stx4","subunits.Gene.name.syn.":";Snap;Syb2;Stx4a","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":981,"ComplexName":"SNARE complex (Stx3, Snap25, Vamp2, Syt1)","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P21707;P60881;P63045;Q08849","subunits.Entrez.IDs.":"25716;25012;24803;81802","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":15975093,"subunits.Protein.name.":"Synaptotagmin-1 ;Synaptosomal-associated protein 25;Vesicle-associated membrane protein 2;Syntaxin-3","subunits.Gene.name.":"Syt1;Snap25;Vamp2;Stx3","subunits.Gene.name.syn.":";Snap;Syb2;Stx3a","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":982,"ComplexName":"SNARE complex (Stx2, Snap25, Vamp2, Syt1)","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P21707;P50279;P60881;P63045","subunits.Entrez.IDs.":"25716;25130;25012;24803","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":15975093,"subunits.Protein.name.":"Synaptotagmin-1 ;Syntaxin-2 ;Synaptosomal-associated protein 25;Vesicle-associated membrane protein 2","subunits.Gene.name.":"Syt1;Stx2;Snap25;Vamp2","subunits.Gene.name.syn.":";Epim;Snap;Syb2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":983,"ComplexName":"SNARE complex (Stx1a, Snap25, Vamp2, Syt1)","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P21707;P32851;P60881;P63045","subunits.Entrez.IDs.":"25716;116470;25012;24803","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":15975093,"subunits.Protein.name.":"Synaptotagmin-1 ;Syntaxin-1A;Synaptosomal-associated protein 25;Vesicle-associated membrane protein 2","subunits.Gene.name.":"Syt1;Stx1a;Snap25;Vamp2","subunits.Gene.name.syn.":";Sap;Snap;Syb2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":984,"ComplexName":"SNARE complex (Stx1a, Snap25, Vamp2, Cplx1)","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P32851;P60881;P63041;P63045","subunits.Entrez.IDs.":"116470;25012;64832;24803","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":15975093,"subunits.Protein.name.":"Syntaxin-1A;Synaptosomal-associated protein 25;Complexin-1;Vesicle-associated membrane protein 2","subunits.Gene.name.":"Stx1a;Snap25;Cplx1;Vamp2","subunits.Gene.name.syn.":"Sap;Snap;None;Syb2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":985,"ComplexName":"SNARE complex (Stx1a, Snap25, Vamp2, Cplx2)","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P32851;P60881;P63045;P84087","subunits.Entrez.IDs.":"116470;25012;24803;116657","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":15975093,"subunits.Protein.name.":"Syntaxin-1A;Synaptosomal-associated protein 25;Vesicle-associated membrane protein 2;Complexin-2","subunits.Gene.name.":"Stx1a;Snap25;Vamp2;Cplx2","subunits.Gene.name.syn.":"Sap;Snap;Syb2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":986,"ComplexName":"SNARE complex (Stx2, Snap25, Vamp2, Cplx1)","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P50279;P60881;P63041;P63045","subunits.Entrez.IDs.":"25130;25012;64832;24803","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":15975093,"subunits.Protein.name.":"Syntaxin-2 ;Synaptosomal-associated protein 25;Complexin-1;Vesicle-associated membrane protein 2","subunits.Gene.name.":"Stx2;Snap25;Cplx1;Vamp2","subunits.Gene.name.syn.":"Epim;Snap;None;Syb2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":987,"ComplexName":"SNARE complex (Stx2, Snap25, Vamp2, Cplx2)","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P50279;P60881;P63045;P84087","subunits.Entrez.IDs.":"25130;25012;24803;116657","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":15975093,"subunits.Protein.name.":"Syntaxin-2 ;Synaptosomal-associated protein 25;Vesicle-associated membrane protein 2;Complexin-2","subunits.Gene.name.":"Stx2;Snap25;Vamp2;Cplx2","subunits.Gene.name.syn.":"Epim;Snap;Syb2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":988,"ComplexName":"SNARE complex (Stx3, Snap25, Vamp2, Cplx2)","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P60881;P63045;P84087;Q08849","subunits.Entrez.IDs.":"25012;24803;116657;81802","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":15975093,"subunits.Protein.name.":"Synaptosomal-associated protein 25;Vesicle-associated membrane protein 2;Complexin-2 ;Syntaxin-3","subunits.Gene.name.":"Snap25;Vamp2;Cplx2;Stx3","subunits.Gene.name.syn.":"Snap;Syb2;;Stx3a","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":989,"ComplexName":"SNARE complex (Stx3, Snap25, Vamp2, Cplx1)","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P60881;P63041;P63045;Q08849","subunits.Entrez.IDs.":"25012;64832;24803;81802","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":15975093,"subunits.Protein.name.":"Synaptosomal-associated protein 25;Complexin-1;Vesicle-associated membrane protein 2;Syntaxin-3","subunits.Gene.name.":"Snap25;Cplx1;Vamp2;Stx3","subunits.Gene.name.syn.":"Snap;None;Syb2;Stx3a","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":990,"ComplexName":"Agap11-AP3 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q8BSZ2;Q8BXK8;Q8R2R9;Q9JKC8;Q9Z1T1","subunits.Entrez.IDs.":"11778;347722;64933;55946;11774","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016192;GO:0005768","GO.description":"vesicle-mediated transport;endosome","FunCat.ID":"20.09.07;70.22","FunCat.description":"vesicular transport (Golgi network, etc.);endosome","PubMed.ID":12967569,"subunits.Protein.name.":"AP-3 complex subunit sigma-2 ;Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 1 ;AP-3 complex subunit mu-2 ;AP-3 complex subunit mu-1 ;AP-3 complex subunit beta-1","subunits.Gene.name.":"Ap3s2;Agap1;Ap3m2;Ap3m1;Ap3b1","subunits.Gene.name.syn.":";Centg2 Kiaa1099;;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":991,"ComplexName":"Tubulin polyglutamylase complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q66JT5;Q91V51;Q91YK0;Q99MS8;Q9CQM0","subunits.Entrez.IDs.":"66648;319953;102747;110012;66257","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0048608","GO.description":"reproductive structure development","FunCat.ID":"45.03.15","FunCat.description":"reproductive tissue","PubMed.ID":15890843,"subunits.Protein.name.":"Tubulin polyglutamylase complex subunit 2 ;Probable tubulin polyglutamylase TTLL1 ;Leucine-rich repeat-containing protein 49 ;Tubulin polyglutamylase complex subunit 1 ;Nicolin-1","subunits.Gene.name.":"Tpgs2;Ttll1;Lrrc49;Tpgs1;Nicn1","subunits.Gene.name.syn.":";;;Gm16517 Gtrgeo22;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":992,"ComplexName":"Kif5a-Dtnb-Dtna complex","Organism":"Rat","Synonyms":"None","Cell.line":"nervous tissue","subunits.UniProt.IDs.":"P84060;Q6QLM7;Q9D2N4","subunits.Entrez.IDs.":"362715;314906;13527","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0006928","GO.description":"intracellular protein transport;protein targeting;protein transport;movement of cell or subcellular component","FunCat.ID":"14.04;20.01.10;34.05","FunCat.description":"protein targeting, sorting and translocation;protein transport;cell motility","PubMed.ID":14600269,"subunits.Protein.name.":"Dystrobrevin beta;Kinesin heavy chain isoform 5A;Dystrobrevin alpha","subunits.Gene.name.":"Dtnb;Kif5a;Dtna","subunits.Gene.name.syn.":"None;None;Dtn","Disease.comment":"None","Subunits.comment":"Since Dtna from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"The authors suggest that the interaction between dystrobrevins and Kif5a/b might be important for the transport of components of the DPC to the neuronal membrane.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Mus musculus (Mouse)"}
{"ComplexID":993,"ComplexName":"Kif5b-Dtnb complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"O70585;Q61768","subunits.Entrez.IDs.":"13528;16573","Protein.complex.purification.method":"MI:0096-pull down","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0006928","GO.description":"intracellular protein transport;protein targeting;protein transport;movement of cell or subcellular component","FunCat.ID":"14.04;20.01.10;34.05","FunCat.description":"protein targeting, sorting and translocation;protein transport;cell motility","PubMed.ID":14600269,"subunits.Protein.name.":"Dystrobrevin beta;Kinesin-1 heavy chain","subunits.Gene.name.":"Dtnb;Kif5b","subunits.Gene.name.syn.":"None;Khcs, Kns1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors suggest that the interaction between dystrobrevins and Kif5a/b might be important for the transport of components of the DPC to the neuronal membrane.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":994,"ComplexName":"GAA1-GPI8-PIGT-PIG-PIGS complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43292;Q92643;Q969N2;Q96S52;Q9H490","subunits.Entrez.IDs.":"8733;10026;51604;94005;128869","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006644;GO:0008654;GO:0009395;GO:0005886","GO.description":"phospholipid metabolic process;phospholipid biosynthetic process;phospholipid catabolic process;plasma membrane","FunCat.ID":"01.06.02.01;70.02","FunCat.description":"phospholipid metabolism;eukaryotic plasma membrane / membrane attached","PubMed.ID":14660601,"subunits.Protein.name.":"Glycosylphosphatidylinositol anchor attachment 1 protein ;GPI-anchor transamidase ;GPI transamidase component PIG-T ;GPI transamidase component PIG-S ;Phosphatidylinositol glycan anchor biosynthesis class U protein","subunits.Gene.name.":"GPAA1;PIGK;PIGT;PIGS;PIGU","subunits.Gene.name.syn.":"GAA1;GPI8;;;CDC91L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":995,"ComplexName":"Polycomb repressive complex 3 (PRC3)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75530;Q09028;Q15022;Q15910;Q16576","subunits.Entrez.IDs.":"8726;5928;23512;2146;5931","Protein.complex.purification.method":"MI:0091- chromatography technologies","GO.ID":"GO:0006265;GO:0032774;GO:0018126;GO:0006479;GO:0051276;GO:0005634","GO.description":"DNA topological change;RNA biosynthetic process;protein hydroxylation;protein methylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02;14.07.09;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);RNA synthesis;posttranslational modification of amino acids (e.g. hydroxylation, methylation);organization of chromosome structure;nucleus","PubMed.ID":15099518,"subunits.Protein.name.":"Polycomb protein EED;Histone-binding protein RBBP4;Polycomb protein SUZ12;Histone-lysine N-methyltransferase EZH2;Histone-binding protein RBBP7","subunits.Gene.name.":"EED;RBBP4;SUZ12;EZH2;RBBP7","subunits.Gene.name.syn.":"None;RBAP48;CHET9 JJAZ1 KIAA0160;KMT6;RBAP46","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"PRC3 associates with the two shortest isoforms of EED. PRC3 methylates nucleosomal H3-lysine 27, PRC2 methylates nucleosomal H1-lysine 26.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":996,"ComplexName":"Polycomb repressive complex 2","Organism":"Human","Synonyms":"PRC2 complex","Cell.line":"None","subunits.UniProt.IDs.":"O75530;Q09028;Q15022;Q15910;Q16576","subunits.Entrez.IDs.":"8726;5928;23512;2146;5931","Protein.complex.purification.method":"MI:0091-chromatography technologies","GO.ID":"GO:0006265;GO:0032774;GO:0018126;GO:0006479;GO:0051276;GO:0005634","GO.description":"DNA topological change;RNA biosynthetic process;protein hydroxylation;protein methylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02;14.07.09;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);RNA synthesis;posttranslational modification of amino acids (e.g. hydroxylation, methylation);organization of chromosome structure;nucleus","PubMed.ID":15099518,"subunits.Protein.name.":"Polycomb protein EED;Histone-binding protein RBBP4;Polycomb protein SUZ12;Histone-lysine N-methyltransferase EZH2;Histone-binding protein RBBP7","subunits.Gene.name.":"EED;RBBP4;SUZ12;EZH2;RBBP7","subunits.Gene.name.syn.":"None;RBAP48;CHET9 JJAZ1 KIAA0160;KMT6;RBAP46","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"PRC2 associates with all three EED isoforms, with the largest form of EED in highest abundance. PRC3 preferentially methylates nucleosomal H3-lysine 27, PRC2 preferentially methylates nucleosomal H1-lysine 26.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":997,"ComplexName":"KIN17-PCNA-RPA70 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60870;P12004;P27694","subunits.Entrez.IDs.":"22944;5111;6117","Protein.complex.purification.method":"MI:0040- electron microscopy; MI:0091- chromatography technologies","GO.ID":"GO:0006260;GO:0000075;GO:0003677;GO:0016363","GO.description":"DNA replication;cell cycle checkpoint;DNA binding;nuclear matrix","FunCat.ID":"10.01.03;10.03.01.03;16.03.01;70.10.06","FunCat.description":"DNA synthesis and replication;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA binding;nuclear matrix","PubMed.ID":15831485,"subunits.Protein.name.":"DNA/RNA-binding protein KIN17 ;Proliferating cell nuclear antigen;Replication protein A 70 kDa DNA-binding subunit","subunits.Gene.name.":"KIN;PCNA;RPA1","subunits.Gene.name.syn.":"BTCD KIN17;None;REPA1 RPA70","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex associates with DNA polymerase alpha.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":998,"ComplexName":"SNARE complex (Snap25, Stx1a, Vamp2)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P32851;P60881;P63045","subunits.Entrez.IDs.":"116470;25012;24803","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":15528447,"subunits.Protein.name.":"Syntaxin-1A;Synaptosomal-associated protein 25;Vesicle-associated membrane protein 2","subunits.Gene.name.":"Stx1a;Snap25;Vamp2","subunits.Gene.name.syn.":"Sap;Snap;Syb2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway. Syntaxin, synaptosome-associated protein of 25kD (SNAP25), and vesicle-associated membrane protein/synaptobrevin are collectively called SNAP receptor (SNARE) proteins. They catalyze neuronal exocytosis by forming a core complex.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":999,"ComplexName":"p23 protein complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P22626;Q15185;Q86W51","subunits.Entrez.IDs.":"3181;10728;10016","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0005515;GO:0043067","GO.description":"protein binding;regulation of programmed cell death","FunCat.ID":"16.01;40.10.02.04","FunCat.description":"protein binding;regulation of apoptosis","PubMed.ID":14675759,"subunits.Protein.name.":"Heterogeneous nuclear ribonucleoproteins A2/B1 ;Prostaglandin E synthase 3;PDCD6 protein","subunits.Gene.name.":"HNRNPA2B1;PTGES3;PDCD6","subunits.Gene.name.syn.":"HNRPA2B1;P23 TEBP;","Disease.comment":"The expression of p23 is increased  after rat focal cerebral ischemia. DHNRPA2B1 is clinical marker of early lung cancer detection (PMID:10632338).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1000,"ComplexName":"TorsinA-TorsinB complex","Organism":"Human","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"O14656;O14657","subunits.Entrez.IDs.":"1861;27348","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008015","GO.description":"blood circulation","FunCat.ID":"34.11.13.07","FunCat.description":"circulation (e.g. blood pressure)","PubMed.ID":15147511,"subunits.Protein.name.":"Torsin-1A ;Torsin-1B","subunits.Gene.name.":"TOR1A;TOR1B","subunits.Gene.name.syn.":"DQ2 DYT1 TA TORA;DQ1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1001,"ComplexName":"DNA synthesome complex","Organism":"Mouse","Synonyms":"MRC complex (Multiprotein DNA Replication Complex); 17S DNA polymerase multiprotein complex; multiprotein form of DNA polymerase","Cell.line":"None","subunits.UniProt.IDs.":"O35654;P17918;P20664;P33609;P33610;P33611;P37913;P52431;Q01320;Q04750;Q9CWP8;Q9EQ28","subunits.Entrez.IDs.":"18972;18538;19075;18968;19076;18969;16881;18971;21973;21969;69745;67967","Protein.complex.purification.method":"MI:0226-ion exchange chromatography","GO.ID":"GO:0006260;GO:0005634","GO.description":"DNA replication;nucleus","FunCat.ID":"10.01.03;70.10","FunCat.description":"DNA synthesis and replication;nucleus","PubMed.ID":8126085,"subunits.Protein.name.":"DNA polymerase delta subunit 2;Proliferating cell nuclear antigen;DNA primase small subunit;DNA polymerase alpha catalytic subunit;DNA primase large subunit;DNA polymerase alpha subunit B;DNA ligase 1;DNA polymerase delta catalytic subunit;DNA topoisomerase 2-alpha;DNA topoisomerase 1;DNA polymerase delta subunit 4;DNA polymerase delta subunit 3","subunits.Gene.name.":"Pold2;Pcna;Prim1;Pola1;Prim2;Pola2;Lig1;Pold1;Top2a;Top1;Pold4;Pold3","subunits.Gene.name.syn.":"None;None;None;Pola;None;None;Lig-1;None;Top-2 Top2;Top-1;None;None","Disease.comment":"None","Subunits.comment":"Since the authors did not specify Top2, we used Top2a.","Complex.comment":"This complex associates also with a not further characterized DNA helicase.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1002,"ComplexName":"Cask-Dlg1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O70589;Q811D0","subunits.Entrez.IDs.":"12361;13383","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0050896","GO.description":"response to stimulus","FunCat.ID":"36.25","FunCat.description":"animal specific systemic sensing and response","PubMed.ID":15266631,"subunits.Protein.name.":"Peripheral plasma membrane protein CASK;Disks large homolog 1","subunits.Gene.name.":"Cask;Dlg1","subunits.Gene.name.syn.":"mLin-2;Dlgh1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"CASK and Dlg may act as a scaffold for organizing receptors and channels at the postsynaptic membrane of the neuromuscular junction (PMID:15266631).","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1003,"ComplexName":"RC complex (Replication competent complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P09884;P20248;P24941;P35249;P35250;P35251;P40937;P40938;Q14181","subunits.Entrez.IDs.":"5422;890;1017;5984;5982;5981;5985;5983;23649","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006260;GO:0000075;GO:0003677;GO:0005694","GO.description":"DNA replication;cell cycle checkpoint;DNA binding;chromosome","FunCat.ID":"10.01.03;10.03.01.03;16.03.01;70.10.03","FunCat.description":"DNA synthesis and replication;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA binding;chromosome","PubMed.ID":12006500,"subunits.Protein.name.":"DNA polymerase alpha catalytic subunit;Cyclin-A2 ;Cyclin-dependent kinase 2;Replication factor C subunit 4;Replication factor C subunit 2;Replication factor C subunit 1;Replication factor C subunit 5;Replication factor C subunit 3;DNA polymerase alpha subunit B","subunits.Gene.name.":"POLA1;CCNA2;CDK2;RFC4;RFC2;RFC1;RFC5;RFC3;POLA2","subunits.Gene.name.syn.":"POLA;CCN1 CCNA;CDKN2;None;None;RFC140;None;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"RC complex might be regulated by specific cyclin/Cdk complexes (PMID:12006500).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1004,"ComplexName":"RC complex during S-phase of cell cycle","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P09874;P09884;P11387;P15927;P18858;P20248;P24941;P27694;P28340;P35244;P35250;P35251;Q07864","subunits.Entrez.IDs.":"142;5422;7150;6118;3978;890;1017;6117;5424;6119;5982;5981;5426","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0029- cosedimentation through density gradients; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006260;GO:0000075;GO:0003677;GO:0005694","GO.description":"DNA replication;cell cycle checkpoint;DNA binding;chromosome","FunCat.ID":"10.01.03;10.03.01.03;16.03.01;70.10.03","FunCat.description":"DNA synthesis and replication;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA binding;chromosome","PubMed.ID":12006500,"subunits.Protein.name.":"Poly [ADP-ribose] polymerase 1;DNA polymerase alpha catalytic subunit;DNA topoisomerase 1;Replication protein A 32 kDa subunit ;DNA ligase 1;Cyclin-A2 ;Cyclin-dependent kinase 2;Replication protein A 70 kDa DNA-binding subunit;DNA polymerase delta catalytic subunit;Replication protein A 14 kDa subunit ;Replication factor C subunit 2;Replication factor C subunit 1;DNA polymerase epsilon catalytic subunit A","subunits.Gene.name.":"PARP1;POLA1;TOP1;RPA2;LIG1;CCNA2;CDK2;RPA1;POLD1;RPA3;RFC2;RFC1;POLE","subunits.Gene.name.syn.":"ADPRT PPOL;POLA;None;REPA2 RPA32 RPA34;None;CCN1 CCNA;CDKN2;REPA1 RPA70;POLD;REPA3 RPA14;None;RFC140;POLE1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"CDK2 associates with the RC complex only during the S-phase of the cell cycle, but disappeares in the G2-phase.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1005,"ComplexName":"RC complex during G2/M-phase of cell cycle","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06493;P09874;P09884;P11387;P14635;P15927;P20248;P27694;P28340;P35244;P35250;P35251;Q07864","subunits.Entrez.IDs.":"983;142;5422;7150;891;6118;890;6117;5424;6119;5982;5981;5426","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0029- cosedimentation through density gradients; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006260;GO:0000075;GO:0003677;GO:0005694","GO.description":"DNA replication;cell cycle checkpoint;DNA binding;chromosome","FunCat.ID":"10.01.03;10.03.01.03;16.03.01;70.10.03","FunCat.description":"DNA synthesis and replication;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA binding;chromosome","PubMed.ID":12006500,"subunits.Protein.name.":"Cyclin-dependent kinase 1 ;Poly [ADP-ribose] polymerase 1;DNA polymerase alpha catalytic subunit;DNA topoisomerase 1;G2/mitotic-specific cyclin-B1;Replication protein A 32 kDa subunit ;Cyclin-A2 ;Replication protein A 70 kDa DNA-binding subunit;DNA polymerase delta catalytic subunit;Replication protein A 14 kDa subunit ;Replication factor C subunit 2;Replication factor C subunit 1;DNA polymerase epsilon catalytic subunit A","subunits.Gene.name.":"CDK1;PARP1;POLA1;TOP1;CCNB1;RPA2;CCNA2;RPA1;POLD1;RPA3;RFC2;RFC1;POLE","subunits.Gene.name.syn.":"CDC2 CDC28A CDKN1 P34CDC2;ADPRT PPOL;POLA;None;CCNB;REPA2 RPA32 RPA34;CCN1 CCNA;REPA1 RPA70;POLD;REPA3 RPA14;None;RFC140;POLE1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"CDK1 and cyclin B1 associate with RC complex only during G2/M-phase of cell cycle. DNA ligase I is not found in the RC complex during G2/M-phase.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1006,"ComplexName":"Caveolin complex","Organism":"Rat","Synonyms":"None","Cell.line":"lung","subunits.UniProt.IDs.":"P20070;P41350;P60711;P63259;Q2IBC5;Q9Z2S9","subunits.Entrez.IDs.":"25035;25404;81822;287876;363425;83764","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0029-cosedimentation through density gradients","GO.ID":"GO:0050982;GO:0009612;GO:0008015;GO:0005886","GO.description":"detection of mechanical stimulus;response to mechanical stimulus;blood circulation;plasma membrane","FunCat.ID":"34.11.05;34.11.13.07;70.02","FunCat.description":"mechanical stimulus perception and response;circulation (e.g. blood pressure);eukaryotic plasma membrane / membrane attached","PubMed.ID":15293782,"subunits.Protein.name.":"NADH-cytochrome b5 reductase 3;Caveolin-1;Actin, cytoplasmic 1;Actin, cytoplasmic 2;Caveolin-2;Flotillin-2","subunits.Gene.name.":"Cyb5r3;Cav1;Actb;Actg1;Cav2;Flot2","subunits.Gene.name.syn.":"Dia1;Cav;None;Actg;None;Reg1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":1007,"ComplexName":"CAK core complex (Cdk-activating kinase core complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P50613;P51946","subunits.Entrez.IDs.":"1022;902","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006794;GO:0006796;GO:0007049;GO:0009299;GO:0006464;GO:0019209;GO:0051090;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;cell cycle;mRNA transcription;cellular protein modification process;kinase activator activity;regulation of sequence-specific DNA binding transcription factor activity;nucleus","FunCat.ID":"01.04;10.03;11.02.03;14.07;18.02.01.01.05;18.02.09;70.10","FunCat.description":"phosphate metabolism;cell cycle;mRNA synthesis;protein modification;kinase activator;regulator of transcription factor;nucleus","PubMed.ID":7533895,"subunits.Protein.name.":"Cyclin-dependent kinase 7 ;Cyclin-H","subunits.Gene.name.":"CDK7;CCNH","subunits.Gene.name.syn.":"CAK CAK1 CDKN7 MO15 STK1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"CAK complex phosphorylates the carboxy-terminal domain of the largest subunit of RNA polymerase II.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1008,"ComplexName":"CAK complex (Cdk-activating kinase complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P50613;P51946;P51948","subunits.Entrez.IDs.":"1022;902;4331","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007049;GO:0009299;GO:0006464;GO:0019209;GO:0051090;GO:0005634","GO.description":"cell cycle;mRNA transcription;cellular protein modification process;kinase activator activity;regulation of sequence-specific DNA binding transcription factor activity;nucleus","FunCat.ID":"10.03;11.02.03;14.07;18.02.01.01.05;18.02.09;70.10","FunCat.description":"cell cycle;mRNA synthesis;protein modification;kinase activator;regulator of transcription factor;nucleus","PubMed.ID":8521818,"subunits.Protein.name.":"Cyclin-dependent kinase 7 ;Cyclin-H ;CDK-activating kinase assembly factor MAT1","subunits.Gene.name.":"CDK7;CCNH;MNAT1","subunits.Gene.name.syn.":"CAK CAK1 CDKN7 MO15 STK1;;CAP35 MAT1 RNF66","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"MAT1 is required for stabilization and assembly of the active CAK complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1009,"ComplexName":"TFIIH transcription factor complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P18074;P19447;P32780;P50613;P51946;P51948;Q13888;Q13889;Q6ZYL4;Q92759","subunits.Entrez.IDs.":"2068;2071;2965;1022;902;4331;2966;2967;404672;2968","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006794;GO:0006796;GO:0006281;GO:0007049;GO:0006351;GO:2001141;GO:0006355;GO:0006464;GO:0030234;GO:0050790;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;DNA repair;cell cycle;transcription, DNA-templated;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;cellular protein modification process;enzyme regulator activity;regulation of catalytic activity;nucleus","FunCat.ID":"01.04;10.01.05.01;10.03;11;11.02.03.04;14.07;18.02.01;70.10","FunCat.description":"phosphate metabolism;DNA repair;cell cycle;TRANSCRIPTION;transcriptional control;protein modification;enzymatic activity regulation / enzyme regulator;nucleus","PubMed.ID":15220921,"subunits.Protein.name.":"TFIIH basal transcription factor complex helicase XPD subunit ;TFIIH basal transcription factor complex helicase XPB subunit ;General transcription factor IIH subunit 1;Cyclin-dependent kinase 7 ;Cyclin-H ;CDK-activating kinase assembly factor MAT1 ;General transcription factor IIH subunit 2 ;General transcription factor IIH subunit 3 ;General transcription factor IIH subunit 5 ;General transcription factor IIH subunit 4","subunits.Gene.name.":"ERCC2;ERCC3;GTF2H1;CDK7;CCNH;MNAT1;GTF2H2;GTF2H3;GTF2H5;GTF2H4","subunits.Gene.name.syn.":"XPD XPDC;XPB XPBC;BTF2;CAK CAK1 CDKN7 MO15 STK1;;CAP35 MAT1 RNF66;BTF2P44;;C6orf175 TTDA;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Transcription factor IIH (TFIIH) is a multisubunit complex required for transcription and for DNA nucleotide excision repair. The GTF2H5 gene product has a role in regulating the level of TFIIH.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1010,"ComplexName":"CAK complex (Cdk-activating kinase complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P50613;P51946;P51948","subunits.Entrez.IDs.":"1022;902;4331","Protein.complex.purification.method":"MI:0091- chromatography technologies; MI:0071- molecular sieving","GO.ID":"GO:0006794;GO:0006796;GO:0007049;GO:0009299;GO:0006464;GO:0019209;GO:0051090;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;cell cycle;mRNA transcription;cellular protein modification process;kinase activator activity;regulation of sequence-specific DNA binding transcription factor activity;nucleus","FunCat.ID":"01.04;10.03;11.02.03;14.07;18.02.01.01.05;18.02.09;70.10","FunCat.description":"phosphate metabolism;cell cycle;mRNA synthesis;protein modification;kinase activator;regulator of transcription factor;nucleus","PubMed.ID":8692842,"subunits.Protein.name.":"Cyclin-dependent kinase 7 ;Cyclin-H ;CDK-activating kinase assembly factor MAT1","subunits.Gene.name.":"CDK7;CCNH;MNAT1","subunits.Gene.name.syn.":"CAK CAK1 CDKN7 MO15 STK1;;CAP35 MAT1 RNF66","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"MAT1 is required for stabilization and assembly of the active CAK complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1011,"ComplexName":"SNARE complex (Stx1a,1b,7,13, Rtn1, Vamp2)","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"G3V7P1;O70257;P32851;P61265;P63045;Q64548","subunits.Entrez.IDs.":"65033;60466;116470;24923;24803;116644","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0047- far western blotting","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":15086514,"subunits.Protein.name.":"Syntaxin-12 ;Syntaxin-7;Syntaxin-1A;Syntaxin-1B ;Vesicle-associated membrane protein 2;Reticulon-1","subunits.Gene.name.":"Stx12;Stx7;Stx1a;Stx1b;Vamp2;Rtn1","subunits.Gene.name.syn.":"Stx13;;Sap;Stx1b2;Syb2;Nsp","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.RTN1-C does apparently not bind to formed SNARE complexes, it might interfere with their formation.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":1012,"ComplexName":"SNARE complex (Snap25, Stx1a, Vamp2)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P32851;P60881;P63045","subunits.Entrez.IDs.":"116470;25012;24803","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":9759724,"subunits.Protein.name.":"Syntaxin-1A;Synaptosomal-associated protein 25;Vesicle-associated membrane protein 2","subunits.Gene.name.":"Stx1a;Snap25;Vamp2","subunits.Gene.name.syn.":"Sap;Snap;Syb2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":1013,"ComplexName":"SNARE complex (Snap25, Stx1a, Vamp2)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P32851;P60881;P63045","subunits.Entrez.IDs.":"116470;25012;24803","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":11533035,"subunits.Protein.name.":"Syntaxin-1A;Synaptosomal-associated protein 25;Vesicle-associated membrane protein 2","subunits.Gene.name.":"Stx1a;Snap25;Vamp2","subunits.Gene.name.syn.":"Sap;Snap;Syb2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":1014,"ComplexName":"Pcdhga1-Pcdha4 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"O88689;Q91XZ0","subunits.Entrez.IDs.":"None;93709","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0008104;GO:0007155","GO.description":"intracellular protein transport;protein targeting;protein transport;protein localization;cell adhesion","FunCat.ID":"14.04;20.01.10;18.01.03;34.07","FunCat.description":"protein targeting, sorting and translocation;protein transport;regulation by localization;cell adhesion","PubMed.ID":15347688,"subunits.Protein.name.":"Protocadherin alpha-4 ;MCG133388, isoform CRA_t","subunits.Gene.name.":"Pcdha4;Pcdhga1","subunits.Gene.name.syn.":"Cnr1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The interactions between CNR/Pcdhalpha and Pcdhgamma regulate their surface expression and contribute to the combinatorial diversity of cell recognition proteins in the brain.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1015,"ComplexName":"Pcdhga1-Pcdhgb2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"O88689;Q91XX7","subunits.Entrez.IDs.":"None;93700","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0008104;GO:0007155","GO.description":"intracellular protein transport;protein targeting;protein transport;protein localization;cell adhesion","FunCat.ID":"14.04;20.01.10;18.01.03;34.07","FunCat.description":"protein targeting, sorting and translocation;protein transport;regulation by localization;cell adhesion","PubMed.ID":15347688,"subunits.Protein.name.":"Protocadherin alpha-4 ;Protein Pcdhgb2","subunits.Gene.name.":"Pcdha4;Pcdhgb2","subunits.Gene.name.syn.":"Cnr1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The interactions between CNR/Pcdhalpha and Pcdhgamma regulate their surface expression and contribute to the combinatorial diversity of cell recognition proteins in the brain.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1016,"ComplexName":"Pcdhga1-Pcdhga3 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"O88689;Q91XY5","subunits.Entrez.IDs.":"None;93711","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0008104;GO:0007155","GO.description":"intracellular protein transport;protein targeting;protein transport;protein localization;cell adhesion","FunCat.ID":"14.04;20.01.10;18.01.03;34.07","FunCat.description":"protein targeting, sorting and translocation;protein transport;regulation by localization;cell adhesion","PubMed.ID":15347688,"subunits.Protein.name.":"Protocadherin alpha-4 ;Protein Pcdhga3","subunits.Gene.name.":"Pcdha4;Pcdhga3","subunits.Gene.name.syn.":"Cnr1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The interactions between CNR/Pcdhalpha and Pcdhgamma regulate their surface expression and contribute to the combinatorial diversity of cell recognition proteins in the brain.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1017,"ComplexName":"Pcdhga1-Pcdhgb4 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"O88689;Q91XX6","subunits.Entrez.IDs.":"None;93701","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0008104;GO:0007155","GO.description":"intracellular protein transport;protein targeting;protein transport;protein localization;cell adhesion","FunCat.ID":"14.04;20.01.10;18.01.03;34.07","FunCat.description":"protein targeting, sorting and translocation;protein transport;regulation by localization;cell adhesion","PubMed.ID":15347688,"subunits.Protein.name.":"Protocadherin alpha-4 ;Protein Pcdhgb4","subunits.Gene.name.":"Pcdha4;Pcdhgb4","subunits.Gene.name.syn.":"Cnr1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The interactions between CNR/Pcdhalpha and Pcdhgamma regulate their surface expression and contribute to the combinatorial diversity of cell recognition proteins in the brain.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1018,"ComplexName":"Pcdha7-Pcdhgb4 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"Q91XX6;Q91Y13","subunits.Entrez.IDs.":"93701;12939","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0008104;GO:0007155","GO.description":"intracellular protein transport;protein targeting;protein transport;protein localization;cell adhesion","FunCat.ID":"14.04;20.01.10;18.01.03;34.07","FunCat.description":"protein targeting, sorting and translocation;protein transport;regulation by localization;cell adhesion","PubMed.ID":15347688,"subunits.Protein.name.":"Protein Pcdhgb4 ;Protocadherin alpha-7","subunits.Gene.name.":"Pcdhgb4;Pcdha7","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The interactions between CNR/Pcdhalpha and Pcdhgamma regulate their surface expression and contribute to the combinatorial diversity of cell recognition proteins in the brain.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1019,"ComplexName":"Pcdha7-Pcdhga3 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"Q91XY5;Q91Y13","subunits.Entrez.IDs.":"93711;12939","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0008104;GO:0007155","GO.description":"intracellular protein transport;protein targeting;protein transport;protein localization;cell adhesion","FunCat.ID":"14.04;20.01.10;18.01.03;34.07","FunCat.description":"protein targeting, sorting and translocation;protein transport;regulation by localization;cell adhesion","PubMed.ID":15347688,"subunits.Protein.name.":"Protein Pcdhga3 ;Protocadherin alpha-7","subunits.Gene.name.":"Pcdhga3;Pcdha7","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The interactions between CNR/Pcdhalpha and Pcdhgamma regulate their surface expression and contribute to the combinatorial diversity of cell recognition proteins in the brain.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1020,"ComplexName":"Pcdha7-Pcdhgb2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"Q91XX7;Q91Y13","subunits.Entrez.IDs.":"93700;12939","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0008104;GO:0007155","GO.description":"intracellular protein transport;protein targeting;protein transport;protein localization;cell adhesion","FunCat.ID":"14.04;20.01.10;18.01.03;34.07","FunCat.description":"protein targeting, sorting and translocation;protein transport;regulation by localization;cell adhesion","PubMed.ID":15347688,"subunits.Protein.name.":"Protein Pcdhgb2 ;Protocadherin alpha-7","subunits.Gene.name.":"Pcdhgb2;Pcdha7","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The interactions between CNR/Pcdhalpha and Pcdhgamma regulate their surface expression and contribute to the combinatorial diversity of cell recognition proteins in the brain.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1021,"ComplexName":"Pcdha7-Pcdhga1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"Q91XZ0;Q91Y13","subunits.Entrez.IDs.":"93709;12939","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0008104;GO:0007155","GO.description":"intracellular protein transport;protein targeting;protein transport;protein localization;cell adhesion","FunCat.ID":"14.04;20.01.10;18.01.03;34.07","FunCat.description":"protein targeting, sorting and translocation;protein transport;regulation by localization;cell adhesion","PubMed.ID":15347688,"subunits.Protein.name.":"MCG133388, isoform CRA_t ;Protocadherin alpha-7","subunits.Gene.name.":"Pcdhga1;Pcdha7","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The interactions between CNR/Pcdhalpha and Pcdhgamma regulate their surface expression and contribute to the combinatorial diversity of cell recognition proteins in the brain.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1022,"ComplexName":"Fgr-Pyk2-p190RhoGap complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P14234;Q91YM2;Q9QVP9","subunits.Entrez.IDs.":"14191;232906;19229","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016477","GO.description":"cell migration","FunCat.ID":"34.05.01","FunCat.description":"cell migration","PubMed.ID":15561106,"subunits.Protein.name.":"Tyrosine-protein kinase Fgr ;Rho GTPase-activating protein 35 ;Protein-tyrosine kinase 2-beta","subunits.Gene.name.":"Fgr;Arhgap35;Ptk2b","subunits.Gene.name.syn.":";Grlf1 Kiaa1722 P190A p190ARHOGAP;Fak2, Pyk2, Raftk","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1023,"ComplexName":"Tiam1-Par-3-aPKC-zeta complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q02956;Q60610;Q99NH2","subunits.Entrez.IDs.":"18762;21844;93742","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007264;GO:0051211;GO:0009798;GO:0007043;GO:0030054","GO.description":"small GTPase mediated signal transduction;anisotropic cell growth;axis specification;cell-cell junction assembly;cell junction","FunCat.ID":"30.01.05.05.01;40.01.03;41.05.19;42.06.04;70.06","FunCat.description":"small GTPase mediated signal transduction;directional cell growth (morphogenesis);asymmetries and axis determination;intercellular junction (gap junction/adherens junction);cell junction","PubMed.ID":16186252,"subunits.Protein.name.":"Protein kinase C zeta type ;T-lymphoma invasion and metastasis-inducing protein 1 ;Partitioning defective 3 homolog","subunits.Gene.name.":"Prkcz;Tiam1;Pard3","subunits.Gene.name.syn.":"Pkcz;Tiam-1;Par3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Tiam1 interacts with Par3 and aPKCzeta, which are two components of the conserved Par3-Par6-aPKC polarity complex, and triggers biogenesis of the TJ through the activation of Rac and aPKCzeta, which is independent of Cdc42.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1024,"ComplexName":"Tiam1-IRSp53 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q60610;Q6GMN2","subunits.Entrez.IDs.":"21844;117542","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0007264;GO:0030036;GO:0015629","GO.description":"intracellular protein transport;protein targeting;protein transport;small GTPase mediated signal transduction;actin cytoskeleton organization;actin cytoskeleton","FunCat.ID":"14.04;20.01.10;30.01.05.05.01;42.04.03;70.04.03","FunCat.description":"protein targeting, sorting and translocation;protein transport;small GTPase mediated signal transduction;actin cytoskeleton;actin cytoskeleton","PubMed.ID":15899863,"subunits.Protein.name.":"T-lymphoma invasion and metastasis-inducing protein 1 ;Brain-specific angiogenesis inhibitor 1-associated protein 2","subunits.Gene.name.":"Tiam1;Baiap2","subunits.Gene.name.syn.":"Tiam-1;","Disease.comment":"None","Subunits.comment":"Since Tiam1 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"Further experiments done in 293T cells and in NIH-3T3 cells. Stimulation of Tiam1 interaction with IRSp53, either through forced Tiam1 overexpression or Ras activation by growth factor, enhances IRSp53 interaction with WAVE2 and Rac and leads to its redistribution, recruiting IRSp53 effects toward a Rac phenotype (ruffles).","SWISSPROT.organism":"Mus musculus (Mouse);Rattus norvegicus (Rat)"}
{"ComplexID":1025,"ComplexName":"Calreticulin-Tnfr1-Tradd complex","Organism":"Rabbit","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P15253;P25118;Q3U0V2","subunits.Entrez.IDs.":"100009050;21937;71609","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0043067","GO.description":"regulation of programmed cell death","FunCat.ID":"40.10.02.04","FunCat.description":"regulation of apoptosis","PubMed.ID":15284227,"subunits.Protein.name.":"Calreticulin ;Tumor necrosis factor receptor superfamily member 1A ;Tumor necrosis factor receptor type 1-associated DEATH domain protein","subunits.Gene.name.":"CALR;Tnfrsf1a;Tradd","subunits.Gene.name.syn.":";Tnfr-1 Tnfr1;","Disease.comment":"None","Subunits.comment":"Since Tradd, Tnrf1 from rabbit were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.","Complex.comment":"None","SWISSPROT.organism":"Oryctolagus cuniculus (Rabbit);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1026,"ComplexName":"Tiam1-spinophilin complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O35274;Q60610","subunits.Entrez.IDs.":"84686;21844","Protein.complex.purification.method":"MI:0018- two hybrid; MI:0019- coimmunoprecipitation","GO.ID":"GO:0006461;GO:0019209;GO:0007264;GO:0005886","GO.description":"protein complex assembly;kinase activator activity;small GTPase mediated signal transduction;plasma membrane","FunCat.ID":"14.10;18.02.01.01.05;30.01.05.05.01;70.02","FunCat.description":"assembly of protein complexes;kinase activator;small GTPase mediated signal transduction;eukaryotic plasma membrane / membrane attached","PubMed.ID":12531897,"subunits.Protein.name.":"Neurabin-2 ;T-lymphoma invasion and metastasis-inducing protein 1","subunits.Gene.name.":"Ppp1r9b;Tiam1","subunits.Gene.name.syn.":";Tiam-1","Disease.comment":"None","Subunits.comment":"Since Tiam1 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"Spinophilin binding promotes the plasma membrane localization of Tiam1 and enhances the ability of Tiam1 to activate p70 S6 kinase.","SWISSPROT.organism":"Rattus norvegicus (Rat);Mus musculus (Mouse)"}
{"ComplexID":1027,"ComplexName":"SNARE complex (Stx4, Vamp7, Snap23, Syt7)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O70377;Q08850;Q62747;Q9JHW5","subunits.Entrez.IDs.":"64630;81803;59267;85491","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0047- far western blotting","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":14993220,"subunits.Protein.name.":"Synaptosomal-associated protein 23 ;Syntaxin-4;Synaptotagmin-7 ;Vesicle-associated membrane protein 7","subunits.Gene.name.":"Snap23;Stx4;Syt7;Vamp7","subunits.Gene.name.syn.":";Stx4a;;Sybl1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":1028,"ComplexName":"HNF4A-SUB1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P41235;P53999","subunits.Entrez.IDs.":"3172;10923","Protein.complex.purification.method":"MI:0024- confirmational text mining","GO.ID":"GO:0045893","GO.description":"positive regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.01","FunCat.description":"transcription activation","PubMed.ID":17317687,"subunits.Protein.name.":"Hepatocyte nuclear factor 4-alpha ;Activated RNA polymerase II transcriptional coactivator p15","subunits.Gene.name.":"HNF4A;SUB1","subunits.Gene.name.syn.":"HNF4 NR2A1 TCF14;PC4 RPO2TC1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The hepatocellular inflammatory-redox (IR) state enhances PC4-HNF4 binding to upregulate transcription of target hepatocyte genes, such as iNOS.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1029,"ComplexName":"TFIIH transcription factor complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P18074;P19447;P32780;P50613;P51946;P51948;Q13888;Q13889;Q6ZYL4;Q92759","subunits.Entrez.IDs.":"2068;2071;2965;1022;902;4331;2966;2967;404672;2968","Protein.complex.purification.method":"MI:0091-chromatography technologies;MI:0071-molecular sieving","GO.ID":"GO:0006796;GO:0006281;GO:0007049;GO:0006351;GO:0006355;GO:0005634","GO.description":"phosphate-containing compound metabolic process;DNA repair;cell cycle;transcription, DNA-templated;regulation of transcription, DNA-templated;nucleus","FunCat.ID":"01.04;10.01.05.01;10.03;11;11.02.03.04;70.10","FunCat.description":"phosphate metabolism;DNA repair;cell cycle;TRANSCRIPTION;transcriptional control;nucleus","PubMed.ID":8692842,"subunits.Protein.name.":"TFIIH basal transcription factor complex helicase XPD subunit ;TFIIH basal transcription factor complex helicase XPB subunit ;General transcription factor IIH subunit 1;Cyclin-dependent kinase 7 ;Cyclin-H ;CDK-activating kinase assembly factor MAT1 ;General transcription factor IIH subunit 2 ;General transcription factor IIH subunit 3 ;General transcription factor IIH subunit 5 ;General transcription factor IIH subunit 4","subunits.Gene.name.":"ERCC2;ERCC3;GTF2H1;CDK7;CCNH;MNAT1;GTF2H2;GTF2H3;GTF2H5;GTF2H4","subunits.Gene.name.syn.":"XPD XPDC;XPB XPBC;BTF2;CAK CAK1 CDKN7 MO15 STK1;;CAP35 MAT1 RNF66;BTF2P44;;C6orf175 TTDA;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Transcription factor IIH (TFIIH) is a multisubunit complex required for transcription and for DNA nucleotide excision repair.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1030,"ComplexName":"CAK-ERCC2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P18074;P50613;P51946;P51948","subunits.Entrez.IDs.":"2068;1022;902;4331","Protein.complex.purification.method":"MI:0091- chromatography technologies; MI:0071- molecular sieving; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006794;GO:0006796;GO:0007049;GO:0009299;GO:0006464;GO:0019209;GO:0051090;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;cell cycle;mRNA transcription;cellular protein modification process;kinase activator activity;regulation of sequence-specific DNA binding transcription factor activity;nucleus","FunCat.ID":"01.04;10.03;11.02.03;14.07;18.02.01.01.05;18.02.09;70.10","FunCat.description":"phosphate metabolism;cell cycle;mRNA synthesis;protein modification;kinase activator;regulator of transcription factor;nucleus","PubMed.ID":8692842,"subunits.Protein.name.":"TFIIH basal transcription factor complex helicase XPD subunit ;Cyclin-dependent kinase 7 ;Cyclin-H ;CDK-activating kinase assembly factor MAT1","subunits.Gene.name.":"ERCC2;CDK7;CCNH;MNAT1","subunits.Gene.name.syn.":"XPD XPDC;CAK CAK1 CDKN7 MO15 STK1;;CAP35 MAT1 RNF66","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"CAK-ERCC2 can efficiently associate with core-TFIIH to reconstitute holo-TFIIH transcription activity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1031,"ComplexName":"ORC complex (origin recognition complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43913;O43929;Q13415;Q13416;Q9UBD5;Q9Y5N6","subunits.Entrez.IDs.":"5001;5000;4998;4999;23595;23594","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006267;GO:0003688;GO:0005524;GO:0005694","GO.description":"pre-replicative complex assembly involved in nuclear cell cycle DNA replication;DNA replication origin binding;ATP binding;chromosome","FunCat.ID":"10.01.03.03;16.19.03;70.10.03","FunCat.description":"ori recognition and priming complex formation;ATP binding;chromosome","PubMed.ID":11323433,"subunits.Protein.name.":"Origin recognition complex subunit 5;Origin recognition complex subunit 4;Origin recognition complex subunit 1 ;Origin recognition complex subunit 2;Origin recognition complex subunit 3 ;Origin recognition complex subunit 6","subunits.Gene.name.":"ORC5;ORC4;ORC1;ORC2;ORC3;ORC6","subunits.Gene.name.syn.":"ORC5L;ORC4L;ORC1L PARC1;ORC2L;LATHEO ORC3L;ORC6L","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"HsOrc2, HsOrc3, and HsOrc4 form a core upon which the ordered assembly of HsOrc5 and HsOrc1 takes place. HsOrc6 appears to be the most weakly bound subunit in the complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1032,"ComplexName":"ORC 2-4 complex (origin recognition 2-4 complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43929;Q13416;Q9UBD5","subunits.Entrez.IDs.":"5000;4999;23595","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006267;GO:0003688;GO:0005524;GO:0005694","GO.description":"pre-replicative complex assembly involved in nuclear cell cycle DNA replication;DNA replication origin binding;ATP binding;chromosome","FunCat.ID":"10.01.03.03;16.19.03;70.10.03","FunCat.description":"ori recognition and priming complex formation;ATP binding;chromosome","PubMed.ID":11323433,"subunits.Protein.name.":"Origin recognition complex subunit 4;Origin recognition complex subunit 2;Origin recognition complex subunit 3","subunits.Gene.name.":"ORC4;ORC2;ORC3","subunits.Gene.name.syn.":"ORC4L;ORC2L;LATHEO ORC3L","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"HsOrc2, HsOrc3, and HsOrc4 form a core upon which the ordered assembly of HsOrc5 and HsOrc1 takes place.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1033,"ComplexName":"ORC complex (origin recognition complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43913;O43929;Q13415;Q13416;Q9UBD5;Q9Y5N6","subunits.Entrez.IDs.":"5001;5000;4998;4999;23595;23594","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006267;GO:0003688;GO:0005524;GO:0005694","GO.description":"pre-replicative complex assembly involved in nuclear cell cycle DNA replication;DNA replication origin binding;ATP binding;chromosome","FunCat.ID":"10.01.03.03;16.19.03;70.10.03","FunCat.description":"ori recognition and priming complex formation;ATP binding;chromosome","PubMed.ID":10945994,"subunits.Protein.name.":"Origin recognition complex subunit 5;Origin recognition complex subunit 4;Origin recognition complex subunit 1 ;Origin recognition complex subunit 2;Origin recognition complex subunit 3 ;Origin recognition complex subunit 6","subunits.Gene.name.":"ORC5;ORC4;ORC1;ORC2;ORC3;ORC6","subunits.Gene.name.syn.":"ORC5L;ORC4L;ORC1L PARC1;ORC2L;LATHEO ORC3L;ORC6L","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Only a small fraction of human ORC1 and ORC6 is associated with a subcomplex of ORC2, 3, 4, and 5.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1034,"ComplexName":"ORC 2-5 complex (origin recognition 2-5 complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43913;O43929;Q13416;Q9UBD5","subunits.Entrez.IDs.":"5001;5000;4999;23595","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006267;GO:0003688;GO:0005524;GO:0005694","GO.description":"pre-replicative complex assembly involved in nuclear cell cycle DNA replication;DNA replication origin binding;ATP binding;chromosome","FunCat.ID":"10.01.03.03;16.19.03;70.10.03","FunCat.description":"ori recognition and priming complex formation;ATP binding;chromosome","PubMed.ID":10945994,"subunits.Protein.name.":"Origin recognition complex subunit 5;Origin recognition complex subunit 4;Origin recognition complex subunit 2;Origin recognition complex subunit 3","subunits.Gene.name.":"ORC5;ORC4;ORC2;ORC3","subunits.Gene.name.syn.":"ORC5L;ORC4L;ORC2L;LATHEO ORC3L","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Only a small fraction of human ORC1 and ORC6 is likely to be associated with a subcomplex of ORC2, 3, 4, and 5.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1035,"ComplexName":"OAP-1-OSP/claudin-11-ITGB1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"brain and oligodendrocyte homogenates","subunits.UniProt.IDs.":"P09055;Q60771;Q9QY33","subunits.Entrez.IDs.":"16412;18417;56434","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation;MI:0663-confocal microscopy","GO.ID":"GO:0016477;GO:0030182;GO:0007399;GO:0007417;GO:0005886;GO:0008347;GO:0042552","GO.description":"cell migration;neuron differentiation;nervous system development;central nervous system development;plasma membrane;glial cell migration;myelination","FunCat.ID":"34.05.01;43.03.13;47.03.01;47.03.01.01;70.02","FunCat.description":"cell migration;neuron;nervous system;central nervous system;eukaryotic plasma membrane / membrane attached","PubMed.ID":11309411,"subunits.Protein.name.":"Integrin beta-1 ;Claudin-11 ;Tetraspanin-3","subunits.Gene.name.":"Itgb1;Cldn11;Tspan3","subunits.Gene.name.syn.":";Osp Otm;Tm4sf8","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Surface biotinylation and immunoelectron microscopy demonstrated the presence of OSP/claudin-11 and OAP-1 (Tspan3) on the oligodendrocyte membrane surface, but it is still not clear whether OSP/claudin-11 complexes with OAP-1 and \\u00df1 integrin at TJs.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1036,"ComplexName":"TFIIH transcription factor complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P18074;P19447;P32780;P50613;P51946;P51948;Q13888;Q13889;Q92759","subunits.Entrez.IDs.":"2068;2071;2965;1022;902;4331;2966;2967;2968","Protein.complex.purification.method":"MI:0091-chromatography technologies","GO.ID":"GO:0006281;GO:0007049;GO:0006351;GO:0006355;GO:0005634","GO.description":"DNA repair;cell cycle;transcription, DNA-templated;regulation of transcription, DNA-templated;nucleus","FunCat.ID":"10.01.05.01;10.03;11;11.02.03.04;70.10","FunCat.description":"DNA repair;cell cycle;TRANSCRIPTION;transcriptional control;nucleus","PubMed.ID":9118947,"subunits.Protein.name.":"TFIIH basal transcription factor complex helicase XPD subunit ;TFIIH basal transcription factor complex helicase XPB subunit ;General transcription factor IIH subunit 1;Cyclin-dependent kinase 7 ;Cyclin-H ;CDK-activating kinase assembly factor MAT1 ;General transcription factor IIH subunit 2 ;General transcription factor IIH subunit 3 ;General transcription factor IIH subunit 4","subunits.Gene.name.":"ERCC2;ERCC3;GTF2H1;CDK7;CCNH;MNAT1;GTF2H2;GTF2H3;GTF2H4","subunits.Gene.name.syn.":"XPD XPDC;XPB XPBC;BTF2;CAK CAK1 CDKN7 MO15 STK1;;CAP35 MAT1 RNF66;BTF2P44;;","Disease.comment":"TFIIH is implicated in DNA repair/transcription deficiency disorders such as the rare autosomal recessive disease xeroderma pigmentosum, Cockayne syndrome, a neuro-developmental disease,  and the brittle hair disease trichothiodystrophy (PMID:9118947).","Subunits.comment":"None","Complex.comment":"Transcription factor IIH (TFIIH) is a multisubunit complex required for transcription and for DNA nucleotide excision repair.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1037,"ComplexName":"TFIIH transcription factor core complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P19447;P32780;Q13888;Q13889;Q92759","subunits.Entrez.IDs.":"2071;2965;2966;2967;2968","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006794;GO:0006796;GO:0006281;GO:0007049;GO:0006351;GO:2001141;GO:0006355;GO:0006464;GO:0030234;GO:0050790;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;DNA repair;cell cycle;transcription, DNA-templated;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;cellular protein modification process;enzyme regulator activity;regulation of catalytic activity;nucleus","FunCat.ID":"01.04;10.01.05.01;10.03;11;11.02.03.04;14.07;18.02.01;70.10","FunCat.description":"phosphate metabolism;DNA repair;cell cycle;TRANSCRIPTION;transcriptional control;protein modification;enzymatic activity regulation / enzyme regulator;nucleus","PubMed.ID":9118947,"subunits.Protein.name.":"TFIIH basal transcription factor complex helicase XPB subunit ;General transcription factor IIH subunit 1;General transcription factor IIH subunit 2 ;General transcription factor IIH subunit 3 ;General transcription factor IIH subunit 4","subunits.Gene.name.":"ERCC3;GTF2H1;GTF2H2;GTF2H3;GTF2H4","subunits.Gene.name.syn.":"XPB XPBC;BTF2;BTF2P44;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1038,"ComplexName":"ORC 1-5 complex (origin recognition 1-5 complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43913;O43929;Q13415;Q13416;Q9UBD5","subunits.Entrez.IDs.":"5001;5000;4998;4999;23595","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0071- molecular sieving","GO.ID":"GO:0006267;GO:0003688;GO:0005524;GO:0005694","GO.description":"pre-replicative complex assembly involved in nuclear cell cycle DNA replication;DNA replication origin binding;ATP binding;chromosome","FunCat.ID":"10.01.03.03;16.19.03;70.10.03","FunCat.description":"ori recognition and priming complex formation;ATP binding;chromosome","PubMed.ID":15618391,"subunits.Protein.name.":"Origin recognition complex subunit 5;Origin recognition complex subunit 4;Origin recognition complex subunit 1 ;Origin recognition complex subunit 2;Origin recognition complex subunit 3","subunits.Gene.name.":"ORC5;ORC4;ORC1;ORC2;ORC3","subunits.Gene.name.syn.":"ORC5L;ORC4L;ORC1L PARC1;ORC2L;LATHEO ORC3L","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"ATP-binding motifs of Orc1, Orc4, Orc5 are all essential for the replication activity of the ORC complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1039,"ComplexName":"PCNA-PAF complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12004;Q15004","subunits.Entrez.IDs.":"5111;9768","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006281;GO:0007049;GO:0006915;GO:0005634;GO:0005739","GO.description":"DNA repair;cell cycle;apoptotic process;nucleus;mitochondrion","FunCat.ID":"10.01.05.01;10.03;40.10.02;70.10;70.16","FunCat.description":"DNA repair;cell cycle;apoptosis (type I programmed cell death);nucleus;mitochondrion","PubMed.ID":16288740,"subunits.Protein.name.":"Proliferating cell nuclear antigen;PCNA-associated factor","subunits.Gene.name.":"PCNA;KIAA0101","subunits.Gene.name.syn.":"None;NS5ATP9 PAF","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1040,"ComplexName":"p33ING1b-PCNA complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q15004;Q9UK53","subunits.Entrez.IDs.":"9768;3621","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006281;GO:0007049;GO:0006915;GO:0005634;GO:0005739","GO.description":"DNA repair;cell cycle;apoptotic process;nucleus;mitochondrion","FunCat.ID":"10.01.05.01;10.03;40.10.02;70.10;70.16","FunCat.description":"DNA repair;cell cycle;apoptosis (type I programmed cell death);nucleus;mitochondrion","PubMed.ID":16288740,"subunits.Protein.name.":"PCNA-associated factor ;Inhibitor of growth protein 1","subunits.Gene.name.":"KIAA0101;ING1","subunits.Gene.name.syn.":"NS5ATP9 PAF;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"p15(PAF) forms part of a larger protein complex potentially involved in the regulation of DNA repair, apoptosis and cell cycle progression.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1041,"ComplexName":"Alpha-dystrobrevin-ZO-1-actin complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"MDCK cells, HT29 cells, epithelium","subunits.UniProt.IDs.":"P60709;Q07157;Q9Y4J8","subunits.Entrez.IDs.":"60;7082;1837","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0007043;GO:0030054","GO.description":"cell-cell junction assembly;cell junction","FunCat.ID":"42.06.04;70.06","FunCat.description":"intercellular junction (gap junction/adherens junction);cell junction","PubMed.ID":15834686,"subunits.Protein.name.":"Actin, cytoplasmic 1;Tight junction protein ZO-1;Dystrobrevin alpha","subunits.Gene.name.":"ACTB;TJP1;DTNA","subunits.Gene.name.syn.":"None;ZO1;DRP3","Disease.comment":"None","Subunits.comment":"Since the authors did not actin, we used isoform ACTB.","Complex.comment":"The TJ- protein ZO-1 and actin were demonstrated in immunoprecipitates of alpha-DB from MDCK I and HT 29 cell lines. These findings suggest that alpha-DB is specifically associated with the reorganizing TJ.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1042,"ComplexName":"SRA-SRC-1 ribonucleoprotein complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q15788;Q9HD15","subunits.Entrez.IDs.":"8648;10011","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0071- molecular sieving","GO.ID":"GO:0045893;GO:0023052;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;signaling;nucleus","FunCat.ID":"11.02.03.04.01;30.01;70.10","FunCat.description":"transcription activation;cellular signalling;nucleus","PubMed.ID":10199399,"subunits.Protein.name.":"Nuclear receptor coactivator 1;Steroid receptor RNA activator 1","subunits.Gene.name.":"NCOA1;SRA1","subunits.Gene.name.syn.":"BHLHE74, SRC1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors conclude that SRA exists in a ribonucleoprotein complex containing SRC-1 and that this complex is recruited by a steroid receptor.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1043,"ComplexName":"Car-Lnx2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P97792;Q91XL2","subunits.Entrez.IDs.":"13052;140887","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0018- two hybrid; MI:0004- affinity chromatography technologies","GO.ID":"GO:0005515;GO:0016337","GO.description":"protein binding;single organismal cell-cell adhesion","FunCat.ID":"16.01;34.07.01","FunCat.description":"protein binding;cell-cell adhesion","PubMed.ID":15979067,"subunits.Protein.name.":"Coxsackievirus and adenovirus receptor homolog ;Ligand of Numb protein X 2","subunits.Gene.name.":"Cxadr;Lnx2","subunits.Gene.name.syn.":"Car;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1044,"ComplexName":"Car-Jam3 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P97792;Q9D8B7","subunits.Entrez.IDs.":"13052;83964","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515;GO:0007281","GO.description":"protein binding;germ cell development","FunCat.ID":"16.01;43.03.02","FunCat.description":"protein binding;germ cell","PubMed.ID":16410001,"subunits.Protein.name.":"Coxsackievirus and adenovirus receptor homolog ;Junctional adhesion molecule C","subunits.Gene.name.":"Cxadr;Jam3","subunits.Gene.name.syn.":"Car;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1045,"ComplexName":"Snurportin-CRM1-RanGTP complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14980;O95149;P62826","subunits.Entrez.IDs.":"7514;10073;5901","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0015031;GO:0008565;GO:0050658;GO:0051033;GO:0051169;GO:0005737;GO:0005634","GO.description":"protein transport;protein transporter activity;RNA transport;RNA transmembrane transporter activity;nuclear transport;cytoplasm;nucleus","FunCat.ID":"20.01.10;20.01.21;20.09.01;70.03;70.10","FunCat.description":"protein transport;RNA transport;nuclear transport;cytoplasm;nucleus","PubMed.ID":10209022,"subunits.Protein.name.":"Exportin-1 ;Snurportin-1 ;GTP-binding nuclear protein Ran","subunits.Gene.name.":"XPO1;SNUPN;RAN","subunits.Gene.name.syn.":"CRM1;RNUT1 SPN1;ARA24","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The complex is exported from the nucleus to the cytoplasm where  RanGTP is removed from CRM1 through the action of RanBP1 and RanGAP.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1046,"ComplexName":"Lnx1-Jam4 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O70263;Q7TSN7","subunits.Entrez.IDs.":"16924;72058","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515;GO:0006897","GO.description":"protein binding;endocytosis","FunCat.ID":"16.01;20.09.18.09.01","FunCat.description":"protein binding;endocytosis","PubMed.ID":16832352,"subunits.Protein.name.":"E3 ubiquitin-protein ligase LNX ;Immunoglobulin superfamily member 5","subunits.Gene.name.":"Lnx1;Igsf5","subunits.Gene.name.syn.":"Lnx;Jam4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ligand-of-Numb protein X1 facilitates endocytosis of JAM4 and is involved in  transforming growth factor beta-induced redistribution of JAM4 in mammary  epithelial cells.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1047,"ComplexName":"Lnx1-Jam4-Numb complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS-7 cells","subunits.UniProt.IDs.":"O70263;Q7TSN7;Q9QZS3","subunits.Entrez.IDs.":"16924;72058;18222","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0005515;GO:0006897","GO.description":"protein binding;endocytosis","FunCat.ID":"16.01;20.09.18.09.01","FunCat.description":"protein binding;endocytosis","PubMed.ID":16832352,"subunits.Protein.name.":"E3 ubiquitin-protein ligase LNX ;Immunoglobulin superfamily member 5 ;Protein numb homolog","subunits.Gene.name.":"Lnx1;Igsf5;Numb","subunits.Gene.name.syn.":"Lnx;Jam4;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Numb is necessary for the LNX1-mediated endocytosis of JAM4.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1048,"ComplexName":"Hnf4-Pc4 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P11031;P49698","subunits.Entrez.IDs.":"20024;15378","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0004- affinity chromatography technologies","GO.ID":"GO:0045892","GO.description":"negative regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.03","FunCat.description":"transcription repression","PubMed.ID":16003322,"subunits.Protein.name.":"Activated RNA polymerase II transcriptional coactivator p15 ;Hepatocyte nuclear factor 4-alpha","subunits.Gene.name.":"Sub1;Hnf4a","subunits.Gene.name.syn.":"Pc4 Rpo2tc1;Hnf-4 Hnf4 Nr2a1 Tcf14","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Redox-mediated upregulation of hepatocyte iNOS transcription requires an HNF-4alpha-PC4 transcriptional complex.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1049,"ComplexName":"SNARE complex (Snap25, Stx1a, Vamp2)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P32851;P60881;P63045","subunits.Entrez.IDs.":"116470;25012;24803","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":9671503,"subunits.Protein.name.":"Syntaxin-1A;Synaptosomal-associated protein 25;Vesicle-associated membrane protein 2","subunits.Gene.name.":"Stx1a;Snap25;Vamp2","subunits.Gene.name.syn.":"Sap;Snap;Syb2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway. A minimal core of the synaptic SNARE complex sufficient for reversible assembly, one of the key steps in mediating exocytosis of synaptic vesicles.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":1050,"ComplexName":"Vdr-Med4 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P48281;Q9CQA5","subunits.Entrez.IDs.":"22337;67381","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0005515","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein binding","FunCat.ID":"11.02.03.04;16.01","FunCat.description":"transcriptional control;protein binding","PubMed.ID":16003322,"subunits.Protein.name.":"Vitamin D3 receptor ;Mediator of RNA polymerase II transcription subunit 4","subunits.Gene.name.":"Vdr;Med4","subunits.Gene.name.syn.":"Nr1i1;Vdrip","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1051,"ComplexName":"Ubiquitin E3 ligase (SKP1A, SKP2, CUL1, RBX1)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62877;P63208;Q13309;Q13616","subunits.Entrez.IDs.":"9978;6500;6502;8454","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511;GO:0005737","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;cytoplasm","FunCat.ID":"14.07.05;14.13.01.01;70.03","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway);cytoplasm","PubMed.ID":10230406,"subunits.Protein.name.":"E3 ubiquitin-protein ligase RBX1;S-phase kinase-associated protein 1;S-phase kinase-associated protein 2;Cullin-1","subunits.Gene.name.":"RBX1;SKP1;SKP2;CUL1","subunits.Gene.name.syn.":"RNF75, ROC1;EMC19, OCP2, SKP1A, TCEB1L;FBXL1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze the ubiquitination of I kappa B alpha.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1052,"ComplexName":"Ubiquitin E3 ligase (FBXW11, SKP1A, CUL1, RBX1)","Organism":"Human","Synonyms":"SCF(HOS)-ROC1  complex","Cell.line":"None","subunits.UniProt.IDs.":"P62877;P63208;Q13616;Q9UKB1","subunits.Entrez.IDs.":"9978;6500;8454;23291","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process","FunCat.ID":"14.07.05;14.13.01.01","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway)","PubMed.ID":10230406,"subunits.Protein.name.":"E3 ubiquitin-protein ligase RBX1;S-phase kinase-associated protein 1;Cullin-1;F-box/WD repeat-containing protein 11","subunits.Gene.name.":"RBX1;SKP1;CUL1;FBXW11","subunits.Gene.name.syn.":"RNF75, ROC1;EMC19, OCP2, SKP1A, TCEB1L;None;BTRCP2 FBW1B FBXW1B KIAA0696","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. This complex catalyzes the phosphorylation-dependent ubiquitination of NF-kappa-B inhibitor alpha.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1054,"ComplexName":"ESR1-RELA-BCL3-NCOA3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P03372;P20749;Q04206;Q9Y6Q9","subunits.Entrez.IDs.":"2099;602;5970;8202","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0023052","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;signaling","FunCat.ID":"11.02.03.04;30.01","FunCat.description":"transcriptional control;cellular signalling","PubMed.ID":16331275,"subunits.Protein.name.":"Estrogen receptor;B-cell lymphoma 3 protein ;Transcription factor p65;Nuclear receptor coactivator 3","subunits.Gene.name.":"ESR1;BCL3;RELA;NCOA3","subunits.Gene.name.syn.":"ESR, NR3A1;BCL4 D19S37;NFKB3;AIB1, BHLHE42, RAC3, TRAM1, ACTR","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1055,"ComplexName":"ZNF198-PML complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P29590;Q9UBW7","subunits.Entrez.IDs.":"5371;7750","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;nucleus","FunCat.ID":"11.02.03.04;70.10","FunCat.description":"transcriptional control;nucleus","PubMed.ID":17027752,"subunits.Protein.name.":"Protein PML ;Zinc finger MYM-type protein 2","subunits.Gene.name.":"PML;ZMYM2","subunits.Gene.name.syn.":"MYL PP8675 RNF71 TRIM19;FIM RAMP ZNF198","Disease.comment":"ZMYM2 is involved in myeloproliferative disorder.","Subunits.comment":"None","Complex.comment":"The authors show by coimmunoprecipitation that PML and sumoylated ZNF198 are in a protein complex in the cell.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1056,"ComplexName":"ZNF198-SUMO1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P63165;Q9UBW7","subunits.Entrez.IDs.":"7341;7750","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0018- two hybrid","GO.ID":"GO:2001141;GO:0006355;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;nucleus","FunCat.ID":"11.02.03.04;70.10","FunCat.description":"transcriptional control;nucleus","PubMed.ID":17027752,"subunits.Protein.name.":"Small ubiquitin-related modifier 1 ;Zinc finger MYM-type protein 2","subunits.Gene.name.":"SUMO1;ZMYM2","subunits.Gene.name.syn.":"SMT3C SMT3H3 UBL1;FIM RAMP ZNF198","Disease.comment":"ZMYM2 is involved in myeloproliferative disorder.","Subunits.comment":"None","Complex.comment":"The results show that ZNF198 is covalently modified by SUMO-1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1057,"ComplexName":"DIPA-MCRS1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q15834;Q96EZ8","subunits.Entrez.IDs.":"11007;10445","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0045892;GO:0005694","GO.description":"negative regulation of transcription, DNA-templated;chromosome","FunCat.ID":"11.02.03.04.03;70.10.03","FunCat.description":"transcription repression;chromosome","PubMed.ID":17014843,"subunits.Protein.name.":"Coiled-coil domain-containing protein 85B ;Microspherule protein 1","subunits.Gene.name.":"CCDC85B;MCRS1","subunits.Gene.name.syn.":"DIPA;INO80Q MSP58","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1058,"ComplexName":"SNX complex (SNX1, SNX6)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q13596;Q9UNH7","subunits.Entrez.IDs.":"6642;58533","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000301;GO:0005768","GO.description":"retrograde transport, vesicle recycling within Golgi;endosome","FunCat.ID":"20.09.07.07;70.22","FunCat.description":"retrograde transport;endosome","PubMed.ID":17148574,"subunits.Protein.name.":"Sorting nexin-1;Sorting nexin-6","subunits.Gene.name.":"SNX1;SNX6","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNX1 and SNX6 exist in a stable, endosomally associated complex that is required for retromer-mediated retrieval of the cation-independent mannose-6-phosphate receptor.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1059,"ComplexName":"Retromer complex (SNX1, SNX2, VPS35, VPS29, VPS26A)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60749;O75436;Q13596;Q96QK1;Q9UBQ0","subunits.Entrez.IDs.":"6643;9559;6642;55737;51699","Protein.complex.purification.method":"MI:0018- two hybrid; MI:0047- far western blotting","GO.ID":"GO:0000301","GO.description":"retrograde transport, vesicle recycling within Golgi","FunCat.ID":"20.09.07.07","FunCat.description":"retrograde transport","PubMed.ID":11102511,"subunits.Protein.name.":"Sorting nexin-2 ;Vacuolar protein sorting-associated protein 26A ;Sorting nexin-1;Vacuolar protein sorting-associated protein 35 ;Vacuolar protein sorting-associated protein 29","subunits.Gene.name.":"SNX2;VPS26A;SNX1;VPS35;VPS29","subunits.Gene.name.syn.":";VPS26;;MEM3;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1060,"ComplexName":"Retromer complex (SNX1, SNX2, VPS35, VPS29, VPS26B)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60749;Q13596;Q4G0F5;Q96QK1;Q9UBQ0","subunits.Entrez.IDs.":"6643;6642;112936;55737;51699","Protein.complex.purification.method":"MI:0018- two hybrid; MI:0047- far western blotting","GO.ID":"GO:0000301","GO.description":"retrograde transport, vesicle recycling within Golgi","FunCat.ID":"20.09.07.07","FunCat.description":"retrograde transport","PubMed.ID":11102511,"subunits.Protein.name.":"Sorting nexin-2 ;Sorting nexin-1;Vacuolar protein sorting-associated protein 26B ;Vacuolar protein sorting-associated protein 35 ;Vacuolar protein sorting-associated protein 29","subunits.Gene.name.":"SNX2;SNX1;VPS26B;VPS35;VPS29","subunits.Gene.name.syn.":";;;MEM3;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1062,"ComplexName":"BAR-BCL2-CASP8 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P10415;Q14790;Q9NZS9","subunits.Entrez.IDs.":"596;841;51283","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006915","GO.description":"apoptotic process","FunCat.ID":"40.10.02","FunCat.description":"apoptosis (type I programmed cell death)","PubMed.ID":10716992,"subunits.Protein.name.":"Apoptosis regulator Bcl-2;Caspase-8;Bifunctional apoptosis regulator","subunits.Gene.name.":"BCL2;CASP8;BFAR","subunits.Gene.name.syn.":"None;MCH5;BAR RNF47","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"BAR can bridge procaspase-8 and Bcl-2 into a protein complex. The BAR protein is anchored in intracellular membranes where Bcl-2 resides. BAR therefore may represent a scaffold protein capable of bridging two major apoptosis pathways (intrinsic and extrinsic).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1063,"ComplexName":"GRASP-GRP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43739;Q7Z6J2","subunits.Entrez.IDs.":"9265;160622","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007264;GO:0005886","GO.description":"small GTPase mediated signal transduction;plasma membrane","FunCat.ID":"30.01.05.05.01;70.02","FunCat.description":"small GTPase mediated signal transduction;eukaryotic plasma membrane / membrane attached","PubMed.ID":10828067,"subunits.Protein.name.":"Cytohesin-3 ;General receptor for phosphoinositides 1-associated scaffold protein","subunits.Gene.name.":"CYTH3;GRASP","subunits.Gene.name.syn.":"ARNO3 GRP1 PSCD3;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors propose that GRASP may aid in the localization of GRP1 to discrete signaling networks and facilitate stimulation of ARF-mediated events at the plasma membrane.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1064,"ComplexName":"IFP35-NMI complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P80217;Q13287","subunits.Entrez.IDs.":"3430;9111","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0018- two hybrid","GO.ID":"GO:0043161;GO:0006511;GO:0051098;GO:0005515","GO.description":"proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;regulation of binding;protein binding","FunCat.ID":"14.13.01.01;18.01.07;16.01","FunCat.description":"proteasomal degradation (ubiquitin/proteasomal pathway);regulation by binding / dissociation;protein binding","PubMed.ID":10950963,"subunits.Protein.name.":"Interferon-induced 35 kDa protein ;N-myc-interactor","subunits.Gene.name.":"IFI35;NMI","subunits.Gene.name.syn.":"IFP35;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors show that IFP 35 is degraded in a proteasome-mediated process, and that a novel function of Nmi is to prevent IFP 35 degradation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1066,"ComplexName":"mPar6c-Mlgl-aPKCz complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q02956;Q80Y17;Q9Z101","subunits.Entrez.IDs.":"18762;16897;56513","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0051211;GO:0009798;GO:0030855;GO:0002009","GO.description":"anisotropic cell growth;axis specification;epithelial cell differentiation;morphogenesis of an epithelium","FunCat.ID":"40.01.03;41.05.19;45.03.09","FunCat.description":"directional cell growth (morphogenesis);asymmetries and axis determination;epithelium","PubMed.ID":12629547,"subunits.Protein.name.":"Protein kinase C zeta type ;Lethal;Partitioning defective 6 homolog alpha","subunits.Gene.name.":"Prkcz;Llgl1;Pard6a","subunits.Gene.name.syn.":"Pkcz;Llglh;Par6a","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The data suggest that the phosphorylation of Mlgl by aPKC is important for appropriate cell polarization in the wounding assay. The authors propose that an interaction between Mlgl, mPar-6C and aPKC, and the consequent phosphorylation of Mlgl, may regulate Mlgl in a polarized fashion such that it can exert localized effects on protein trafficking and secretion.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1067,"ComplexName":"CD8A-LCK complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P01732;P06239","subunits.Entrez.IDs.":"925;3932","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007169;GO:0006955;GO:0005886","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway;immune response;plasma membrane","FunCat.ID":"30.05.01.12;36.25.16;70.02","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways;immune response;eukaryotic plasma membrane / membrane attached","PubMed.ID":11034334,"subunits.Protein.name.":"T-cell surface glycoprotein CD8 alpha chain ;Tyrosine-protein kinase Lck","subunits.Gene.name.":"CD8A;LCK","subunits.Gene.name.syn.":"MAL;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors found that newly synthesized p56lck binds rapidly to CD8-alpha throughout the exocytic pathway and about 50% of complexed p56lck reaches the cell surface.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1068,"ComplexName":"12S U11 snRNP","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P14678;P62304;P62306;P62308;P62314;P62316;P62318;P67809;Q16560;Q16629;Q6IEG0;Q8N8D1;Q96GM8;Q9BV90;Q9H875","subunits.Entrez.IDs.":"6628;6635;6636;6637;6632;6633;6634;4904;11066;6432;154007;10081;114034;79622;79706","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0000398;GO:0006397;GO:0005634","GO.description":"mRNA splicing, via spliceosome;mRNA processing;nucleus","FunCat.ID":"11.04.03;70.10","FunCat.description":"mRNA processing (splicing, 5'-, 3'-end processing);nucleus","PubMed.ID":15146077,"subunits.Protein.name.":"Small nuclear ribonucleoprotein-associated proteins B and B' ;Small nuclear ribonucleoprotein E ;Small nuclear ribonucleoprotein F ;Small nuclear ribonucleoprotein G ;Small nuclear ribonucleoprotein Sm D1 ;Small nuclear ribonucleoprotein Sm D2 ;Small nuclear ribonucleoprotein Sm D3 ;Nuclease-sensitive element-binding protein 1 ;U11/U12 small nuclear ribonucleoprotein 35 kDa protein ;Serine/arginine-rich splicing factor 7 ;U11/U12 small nuclear ribonucleoprotein 48 kDa protein ;Programmed cell death protein 7 ;Target of EGR1 protein 1;U11/U12 small nuclear ribonucleoprotein 25 kDa protein ;PRKR-interacting protein 1","subunits.Gene.name.":"SNRPB;SNRPE;SNRPF;SNRPG;SNRPD1;SNRPD2;SNRPD3;YBX1;SNRNP35;SRSF7;SNRNP48;PDCD7;TOE1;SNRNP25;PRKRIP1","subunits.Gene.name.syn.":"COD SNRPB1;;PBSCF;PBSCG;;SNRPD1;;NSEP1 YB1;HM1 U1SNRNPBP;SFRS7;C6orf151;;;C16orf33;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"U12-type spliceosomes excise U12-type introns, which comprise less than 1% of all human introns.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1069,"ComplexName":"FIF-FGR2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P09038;Q9BZZ5","subunits.Entrez.IDs.":"2247;8539","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0018- two hybrid","GO.ID":"GO:0005515","GO.description":"protein binding","FunCat.ID":"16.01","FunCat.description":"protein binding","PubMed.ID":11075807,"subunits.Protein.name.":"Fibroblast growth factor 2 ;Apoptosis inhibitor 5","subunits.Gene.name.":"FGF2;API5","subunits.Gene.name.syn.":"FGFB;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1070,"ComplexName":"SNX complex (SNX1a, SNX2, SNX4)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60749;O95219;Q13596","subunits.Entrez.IDs.":"6643;8723;6642","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0015031;GO:0008565","GO.description":"protein transport;protein transporter activity","FunCat.ID":"20.01.10","FunCat.description":"protein transport","PubMed.ID":9819414,"subunits.Protein.name.":"Sorting nexin-2 ;Sorting nexin-4;Sorting nexin-1","subunits.Gene.name.":"SNX2;SNX4;SNX1","subunits.Gene.name.syn.":";;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1071,"ComplexName":"PKD2-FPC complex","Organism":"Human","Synonyms":"None","Cell.line":"epithelium, kidney, heart muscle","subunits.UniProt.IDs.":"P08F94;Q13563","subunits.Entrez.IDs.":"5314;5311","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0096-pull down","GO.ID":"GO:0050789;GO:0008324;GO:0006812;GO:0005216;GO:0006875","GO.description":"regulation of biological process;cation transmembrane transporter activity;cation transport;ion channel activity;cellular metal ion homeostasis","FunCat.ID":"18;20.01.01.01;20.03.01.01;34.01.01.01","FunCat.description":"REGULATION OF METABOLISM AND PROTEIN FUNCTION;cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;homeostasis of metal ions (Na, K, Ca etc.)","PubMed.ID":17008358,"subunits.Protein.name.":"Fibrocystin;Polycystin-2","subunits.Gene.name.":"PKHD1;PKD2","subunits.Gene.name.syn.":"FCYT,TIGM1;TRPP2","Disease.comment":"PKD2-FPC complex is involved in polycystic kidney disease (PKD).","Subunits.comment":"None","Complex.comment":"The study shows that fibrocystin is another partner of PC2, which functionally up-regulates its channel function through KIF3B. Interestingly, although KIF3B directly binds PC2, it has no significant effect on PC2 channel function, indicating that it primarily serves as a linker protein.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1072,"ComplexName":"SNX complex (SNX2), oligomeric","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60749","subunits.Entrez.IDs.":"6643","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0015031;GO:0008565","GO.description":"protein transport;protein transporter activity","FunCat.ID":"20.01.10","FunCat.description":"protein transport","PubMed.ID":9819414,"subunits.Protein.name.":"Sorting nexin-2","subunits.Gene.name.":"SNX2","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"SNX2 is able to oligomerize with itself. The exact number of components is not mentioned in paper.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":1073,"ComplexName":"Pkd2-Fpc complex","Organism":"Mouse","Synonyms":"None","Cell.line":"epithelium","subunits.UniProt.IDs.":"O35245;Q8CIS7","subunits.Entrez.IDs.":"18764;241035","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0096- pull down","GO.ID":"GO:0050789;GO:0008324;GO:0006812;GO:0005216;GO:0006875","GO.description":"regulation of biological process;cation transmembrane transporter activity;cation transport;ion channel activity;cellular metal ion homeostasis","FunCat.ID":"18;20.01.01.01;20.03.01.01;34.01.01.01","FunCat.description":"REGULATION OF METABOLISM AND PROTEIN FUNCTION;cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;homeostasis of metal ions (Na, K, Ca etc.)","PubMed.ID":17008358,"subunits.Protein.name.":"Polycystin-2;Polyductin","subunits.Gene.name.":"Pkd2;Pkhd1","subunits.Gene.name.syn.":"TRPP2;None","Disease.comment":"PKD2-FPC complex is involved in polycystic kidney disease (PKD).","Subunits.comment":"None","Complex.comment":"The study shows that fibrocystin is another partner of PC2, which functionally up-regulates its channel function through KIF3B. Interestingly, although KIF3B directly binds PC2, it has no significant effect on PC2 channel function, indicating that it primarily serves as a linker protein.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1074,"ComplexName":"Pkd2-Fpc-Kif3b complex","Organism":"Mouse","Synonyms":"None","Cell.line":"kidney epithelium","subunits.UniProt.IDs.":"O35245;Q61771;Q8CIS7","subunits.Entrez.IDs.":"18764;16569;241035","Protein.complex.purification.method":"MI:0047-far western blotting;MI:0096-pull down;MI:0019-coimmunoprecipitation","GO.ID":"GO:0050789;GO:0008324;GO:0006812;GO:0005216;GO:0006875","GO.description":"regulation of biological process;cation transmembrane transporter activity;cation transport;ion channel activity;cellular metal ion homeostasis","FunCat.ID":"18;20.01.01.01;20.03.01.01;34.01.01.01","FunCat.description":"REGULATION OF METABOLISM AND PROTEIN FUNCTION;cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;homeostasis of metal ions (Na, K, Ca etc.)","PubMed.ID":17008358,"subunits.Protein.name.":"Polycystin-2;Kinesin-like protein KIF3B;Polyductin","subunits.Gene.name.":"Pkd2;Kif3b;Pkhd1","subunits.Gene.name.syn.":"TRPP2;None;None","Disease.comment":"Pkd2-Fpc-Kif3b complex is involved in polycystic kidney disease (PKD).","Subunits.comment":"None","Complex.comment":"Using a combination of in vitro and in vivo approaches, including yeast two-hybrid, GST pull-down and Far WB, the authors have demonstrated that the kinesin-2 motor subunit KIF3B acts as a linker protein, which enables the formation of a triplex, presumably in the form of PC2-KIF3B-FPC. Thus, KIF3B represents the first molecular linker between ADPKD and ARPKD proteins, suggesting that the protein complex PC2-KIF3B-FPC is part of a common molecular pathway implicated in renal cystic diseases. Using the lipid bilayer electrophysiology assay, it was demonstrated that FPC is capable of increasing PC2 channel function in the presence, but not in the absence of KIF3B.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1076,"ComplexName":"Pkhd1-Pkd2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"kidney","subunits.UniProt.IDs.":"O35245;Q8CIS7","subunits.Entrez.IDs.":"18764;241035","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0006875;GO:0050982;GO:0009612;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;cellular metal ion homeostasis;detection of mechanical stimulus;response to mechanical stimulus;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;34.01.01.01;34.11.05;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;homeostasis of metal ions (Na, K, Ca etc.);mechanical stimulus perception and response;eukaryotic plasma membrane / membrane attached","PubMed.ID":17283055,"subunits.Protein.name.":"Polycystin-2;Polyductin","subunits.Gene.name.":"Pkd2;Pkhd1","subunits.Gene.name.syn.":"TRPP2;None","Disease.comment":"Pkhd1-Pkd2 complex  is involved in autosomal recessive polycystic kidney disease (PKD).","Subunits.comment":"None","Complex.comment":"Coimmunoprecipitation of FPC and PC2 done in MDCK cells and mouse kidney tissues. Expression of FPC at the basolateral membrane both in the kidney tubules and in cultured cells suggests a role for FPC in cell-cell and cell-matrix interactions, where it may function as an adhesive molecule in concert with other junction molecules, such as the cadherin family members.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1077,"ComplexName":"Pkd2-Fpc-Kif3a complex","Organism":"Dog","Synonyms":"None","Cell.line":"MDCK cells","subunits.UniProt.IDs.":"O35245;P28741;Q8CIS7","subunits.Entrez.IDs.":"18764;16568;241035","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0006875;GO:0050982;GO:0009612;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;cellular metal ion homeostasis;detection of mechanical stimulus;response to mechanical stimulus;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;34.01.01.01;34.11.05;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;homeostasis of metal ions (Na, K, Ca etc.);mechanical stimulus perception and response;eukaryotic plasma membrane / membrane attached","PubMed.ID":17283055,"subunits.Protein.name.":"Polycystin-2;Kinesin-like protein KIF3A;Polyductin","subunits.Gene.name.":"Pkd2;Kif3a;Pkhd1","subunits.Gene.name.syn.":"TRPP2;Kif3;None","Disease.comment":"Pkd2-Fpc complex is involved in autosomal recessive polycystic kidney disease (PKD).","Subunits.comment":"Since Pkd2, Kif3a and Pkhd1 from dog were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.","Complex.comment":"The results show that Kif3a but not Kif3b was coimmunoprecipitated by both FPC and PC2 antibodies. This indicates that Kif3a is likely to be one of the molecular candidates mediating the interaction between FPC and PC2.  Disruption of either FPC or the PC1/PC2 complex at the primary cilium results in defects in mechanosensation of fluid flow.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1078,"ComplexName":"MSH2-MSH6 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P43246;P52701","subunits.Entrez.IDs.":"4436;2956","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006281;GO:0003677;GO:0000166;GO:0005634","GO.description":"DNA repair;DNA binding;nucleotide binding;nucleus","FunCat.ID":"10.01.05.01;16.03.01;16.19;70.10","FunCat.description":"DNA repair;DNA binding;nucleotide/nucleoside/nucleobase binding;nucleus","PubMed.ID":9428522,"subunits.Protein.name.":"DNA mismatch repair protein Msh2 ;DNA mismatch repair protein Msh6","subunits.Gene.name.":"MSH2;MSH6","subunits.Gene.name.syn.":";GTBP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The MSH2-MSH6 complex binds to mismatched nucleotides only in the ADP-bound form.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1079,"ComplexName":"P-TEFb.1 complex","Organism":"Human","Synonyms":"transcription elongation factor b.1 complex","Cell.line":"None","subunits.UniProt.IDs.":"O60563;P50750","subunits.Entrez.IDs.":"904;1025","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006794;GO:0006796;GO:0006354;GO:0045893;GO:0006464;GO:0043085;GO:0008047;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;DNA-templated transcription, elongation;positive regulation of transcription, DNA-templated;cellular protein modification process;positive regulation of catalytic activity;enzyme activator activity;nucleus","FunCat.ID":"01.04;11.02.03.01.04;11.02.03.04.01;14.07;18.02.01.01;70.10","FunCat.description":"phosphate metabolism;transcription elongation;transcription activation;protein modification;enzyme activator;nucleus","PubMed.ID":9499409,"subunits.Protein.name.":"Cyclin-T1;Cyclin-dependent kinase 9","subunits.Gene.name.":"CCNT1;CDK9","subunits.Gene.name.syn.":"None;CDC2L4, TAK","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cyclin T activates CDK9 in the P-TEFb complex. P-TEFb works as a protein kinase that phosphorylates the C-terminal domain of the RNAPII largest subunit.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1080,"ComplexName":"P-TEFb.2 complex","Organism":"Human","Synonyms":"transcription elongation factor b.2 complex","Cell.line":"None","subunits.UniProt.IDs.":"O60583;P50750","subunits.Entrez.IDs.":"905;1025","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006794;GO:0006796;GO:0006354;GO:0045893;GO:0006464;GO:0043085;GO:0008047;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;DNA-templated transcription, elongation;positive regulation of transcription, DNA-templated;cellular protein modification process;positive regulation of catalytic activity;enzyme activator activity;nucleus","FunCat.ID":"01.04;11.02.03.01.04;11.02.03.04.01;14.07;18.02.01.01;70.10","FunCat.description":"phosphate metabolism;transcription elongation;transcription activation;protein modification;enzyme activator;nucleus","PubMed.ID":9499409,"subunits.Protein.name.":"Cyclin-T2;Cyclin-dependent kinase 9","subunits.Gene.name.":"CCNT2;CDK9","subunits.Gene.name.syn.":"None;CDC2L4, TAK","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cyclin T activates CDK9 in the P-TEFb complex. P-TEFb works as a protein kinase that phosphorylates the C-terminal domain of the RNAPII largest subunit.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1081,"ComplexName":"MRN complex (MRE11-RAD50-NBN complex)","Organism":"Human","Synonyms":"None","Cell.line":"U-1 cells","subunits.UniProt.IDs.":"O60934;P49959;Q92878","subunits.Entrez.IDs.":"4683;4361;10111","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006308;GO:0006281;GO:0000075;GO:0003677;GO:0006974;GO:0005634","GO.description":"DNA catabolic process;DNA repair;cell cycle checkpoint;DNA binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"01.03.16.03;10.01.05.01;10.03.01.03;16.03.01;32.01.09;70.10","FunCat.description":"DNA degradation;DNA repair;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA binding;DNA damage response;nucleus","PubMed.ID":15039997,"subunits.Protein.name.":"Nibrin ;Double-strand break repair protein MRE11A ;DNA repair protein RAD50","subunits.Gene.name.":"NBN;MRE11A;RAD50","subunits.Gene.name.syn.":"NBS NBS1 P95;HNGS1 MRE11;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"After irradiation, the MRN complex rapidly migrates to sites of double strand breaks, forming foci which remain until DSB repair is complete. Mre11 and Rad50 play direct roles in DSB repair, while Nbs1 appears to be involved in damage signaling. Heat shock, alone or in combination with ionizing radiation, induces a reversible translocation of each of these proteins from the nucleus to the cytoplasm.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1082,"ComplexName":"P-TEFb.1 complex","Organism":"Human","Synonyms":"transcription elongation factor b.1 complex","Cell.line":"None","subunits.UniProt.IDs.":"O60563;P50750","subunits.Entrez.IDs.":"904;1025","Protein.complex.purification.method":"MI:0018- two hybrid; MI:0071- molecular sieving","GO.ID":"GO:0006794;GO:0006796;GO:0006354;GO:0045893;GO:0006464;GO:0043085;GO:0008047;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;DNA-templated transcription, elongation;positive regulation of transcription, DNA-templated;cellular protein modification process;positive regulation of catalytic activity;enzyme activator activity;nucleus","FunCat.ID":"01.04;11.02.03.01.04;11.02.03.04.01;14.07;18.02.01.01;70.10","FunCat.description":"phosphate metabolism;transcription elongation;transcription activation;protein modification;enzyme activator;nucleus","PubMed.ID":10574912,"subunits.Protein.name.":"Cyclin-T1;Cyclin-dependent kinase 9","subunits.Gene.name.":"CCNT1;CDK9","subunits.Gene.name.syn.":"None;CDC2L4, TAK","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cyclin T activates CDK9 in the P-TEFb complex. P-TEFb works as a protein kinase that phosphorylates the C-terminal domain of the RNAPII largest subunit.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1083,"ComplexName":"P-TEFb.4 complex","Organism":"Human","Synonyms":"transcription elongation factor b.4 complex","Cell.line":"None","subunits.UniProt.IDs.":"O75909;P50750","subunits.Entrez.IDs.":"8812;1025","Protein.complex.purification.method":"MI:0018- two hybrid; MI:0071- molecular sieving","GO.ID":"GO:0006794;GO:0006796;GO:0006354;GO:0045893;GO:0006464;GO:0043085;GO:0008047;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;DNA-templated transcription, elongation;positive regulation of transcription, DNA-templated;cellular protein modification process;positive regulation of catalytic activity;enzyme activator activity;nucleus","FunCat.ID":"01.04;11.02.03.01.04;11.02.03.04.01;14.07;18.02.01.01;70.10","FunCat.description":"phosphate metabolism;transcription elongation;transcription activation;protein modification;enzyme activator;nucleus","PubMed.ID":10574912,"subunits.Protein.name.":"Cyclin-K;Cyclin-dependent kinase 9","subunits.Gene.name.":"CCNK;CDK9","subunits.Gene.name.syn.":"CPR4;CDC2L4, TAK","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cyclin K functions as regulatory subunit of CDK9.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1084,"ComplexName":"Tiam2-PAR-3-aPKC-PAR-6-Rac1-GTP complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P97701;Q6B4M5;Q6RUV5;Q6ZPF3;Q9Z340","subunits.Entrez.IDs.":"84006;307799;363875;24001;81918","Protein.complex.purification.method":"MI:0096-pull down","GO.ID":"GO:0007264;GO:0051211;GO:0022008;GO:0048699;GO:0009798;GO:0030182","GO.description":"small GTPase mediated signal transduction;anisotropic cell growth;neurogenesis;generation of neurons;axis specification;neuron differentiation","FunCat.ID":"30.01.05.05.01;40.01.03;41.05.13;41.05.19;43.03.13","FunCat.description":"small GTPase mediated signal transduction;directional cell growth (morphogenesis);neurogenesis;asymmetries and axis determination;neuron","PubMed.ID":15723051,"subunits.Protein.name.":"Protein kinase C lambda ;Partitioning defective 6 homolog alpha ;Ras-related C3 botulinum toxin substrate 1 ;T-lymphoma invasion and metastasis-inducing protein 2 ;Partitioning defective 3 homolog","subunits.Gene.name.":";Pard6a;Rac1;Tiam2;Pard3","subunits.Gene.name.syn.":";Par-6a Par6a;;Kiaa2016 Stef;Par3","Disease.comment":"None","Subunits.comment":"Since Tiam2 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Mus musculus (Mouse);Rattus norvegicus (Rat)"}
{"ComplexID":1085,"ComplexName":"DNA repair complex NEIL2-PNK-Pol(beta)-LigIII(alpha)-XRCC1","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00764;P06746;P18887;P49916;Q969S2","subunits.Entrez.IDs.":"8566;5423;7515;3980;252969","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0003677;GO:0005634","GO.description":"DNA repair;DNA binding;nucleus","FunCat.ID":"10.01.05.01;16.03.01;70.10","FunCat.description":"DNA repair;DNA binding;nucleus","PubMed.ID":16982218,"subunits.Protein.name.":"Pyridoxal kinase ;DNA polymerase beta;DNA repair protein XRCC1 ;DNA ligase 3 ;Endonuclease 8-like 2","subunits.Gene.name.":"PDXK;POLB;XRCC1;LIG3;NEIL2","subunits.Gene.name.syn.":"C21orf124 C21orf97 PKH PNK;None;;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1086,"ComplexName":"DNA repair complex NEIL1-PNK-Pol(beta)-LigIII(alpha)-XRCC1","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00764;P06746;P18887;P49916;Q96FI4","subunits.Entrez.IDs.":"8566;5423;7515;3980;79661","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0003677;GO:0005634","GO.description":"DNA repair;DNA binding;nucleus","FunCat.ID":"10.01.05.01;16.03.01;70.10","FunCat.description":"DNA repair;DNA binding;nucleus","PubMed.ID":15260972,"subunits.Protein.name.":"Pyridoxal kinase ;DNA polymerase beta;DNA repair protein XRCC1 ;DNA ligase 3 ;Endonuclease 8-like 1","subunits.Gene.name.":"PDXK;POLB;XRCC1;LIG3;NEIL1","subunits.Gene.name.syn.":"C21orf124 C21orf97 PKH PNK;None;;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1087,"ComplexName":"BIRC5-AURKB-INCENP-EVI5 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15392;O60447;Q96GD4;Q9NQS7","subunits.Entrez.IDs.":"332;7813;9212;3619","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0000910;GO:0000917","GO.description":"cytokinesis;barrier septum assembly","FunCat.ID":"10.03.03","FunCat.description":"cytokinesis (cell division) /septum formation and hydrolysis","PubMed.ID":16764853,"subunits.Protein.name.":"Baculoviral IAP repeat-containing protein 5;Ecotropic viral integration site 5 protein homolog ;Aurora kinase B;Inner centromere protein","subunits.Gene.name.":"BIRC5;EVI5;AURKB;INCENP","subunits.Gene.name.syn.":"API4, IAP4;NB4S;AIK2, AIM1, AIRK2, ARK2 STK1, STK12, STK5;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1088,"ComplexName":"PRNP-ApolopoproteinE3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04156;Q13791","subunits.Entrez.IDs.":"5621;348","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0005515","GO.description":"protein binding","FunCat.ID":"16.01","FunCat.description":"protein binding","PubMed.ID":16764853,"subunits.Protein.name.":"Major prion protein ;Apolipoprotein E3","subunits.Gene.name.":"PRNP;","subunits.Gene.name.syn.":"ALTPRP PRIP PRP;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1089,"ComplexName":"VAM1-VELI1 complex","Organism":"Human","Synonyms":"None","Cell.line":"epithelium, nervous tissue","subunits.UniProt.IDs.":"O14910;Q9NZW5","subunits.Entrez.IDs.":"8825;51678","Protein.complex.purification.method":"MI:0096-pull down","GO.ID":"GO:0005515;GO:0051098","GO.description":"protein binding;regulation of binding","FunCat.ID":"16.01;18.01.07","FunCat.description":"protein binding;regulation by binding / dissociation","PubMed.ID":11311936,"subunits.Protein.name.":"Protein lin-7 homolog A;MAGUK p55 subfamily member 6","subunits.Gene.name.":"LIN7A;MPP6","subunits.Gene.name.syn.":"MALS1 VELI1;VAM1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"VAM-1 may function by promoting the assembly of a Veli-1 containing protein complex in neuronal as well as epithelial cells (PMID:11311936).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1090,"ComplexName":"APLG1-Rababtin5 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43747;Q15276","subunits.Entrez.IDs.":"164;9135","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0018-two hybrid;MI:0096-pull down","GO.ID":"GO:0016192","GO.description":"vesicle-mediated transport","FunCat.ID":"20.09.07","FunCat.description":"vesicular transport (Golgi network, etc.)","PubMed.ID":11872161,"subunits.Protein.name.":"AP-1 complex subunit gamma-1;Rab GTPase-binding effector protein 1","subunits.Gene.name.":"AP1G1;RABEP1","subunits.Gene.name.syn.":"ADTG CLAPG1;RAB5EP RABPT5 RABPT5A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The gamma1-adaptin-Rabaptin-5 complex may play a role in membrane trafficking between the TGN and endosomes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1091,"ComplexName":"SNX complex (SNX1a, SNX2, SNX4, LEPR)","Organism":"Human","Synonyms":"Leptin receptor complex","Cell.line":"None","subunits.UniProt.IDs.":"O60749;O95219;P48357;Q13596","subunits.Entrez.IDs.":"6643;8723;3953;6642","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0015031;GO:0008565;GO:0006898;GO:0007167","GO.description":"protein transport;protein transporter activity;receptor-mediated endocytosis;enzyme linked receptor protein signaling pathway","FunCat.ID":"20.01.10;20.09.18.09.01.01;30.05.01","FunCat.description":"protein transport;receptor-mediated endocytosis;receptor enzyme mediated signalling","PubMed.ID":9819414,"subunits.Protein.name.":"Sorting nexin-2 ;Sorting nexin-4;Leptin receptor ;Sorting nexin-1","subunits.Gene.name.":"SNX2;SNX4;LEPR;SNX1","subunits.Gene.name.syn.":";;DB OBR;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1092,"ComplexName":"PCNA-KU antigen complex","Organism":"Human","Synonyms":"PCNA-Ku70-Ku80 complex","Cell.line":"None","subunits.UniProt.IDs.":"P12004;P12956;P13010","subunits.Entrez.IDs.":"5111;2547;7520","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0003677;GO:0005524;GO:0006974","GO.description":"DNA repair;DNA binding;ATP binding;cellular response to DNA damage stimulus","FunCat.ID":"10.01.05.01;16.03.01;16.19.03;32.01.09","FunCat.description":"DNA repair;DNA binding;ATP binding;DNA damage response","PubMed.ID":11239001,"subunits.Protein.name.":"Proliferating cell nuclear antigen;X-ray repair cross-complementing protein 6 ;X-ray repair cross-complementing protein 5","subunits.Gene.name.":"PCNA;XRCC6;XRCC5","subunits.Gene.name.syn.":"None;G22P1;G22P2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Interaction of PCNA with Ku70 and Ku80 heterodimer increases after DNA damage.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1093,"ComplexName":"SNX complex (SNX1a, SNX2, SNX4, INSR)","Organism":"Human","Synonyms":"Insulin receptor complex","Cell.line":"None","subunits.UniProt.IDs.":"O60749;O95219;P06213;Q13596","subunits.Entrez.IDs.":"6643;8723;3643;6642","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0015031;GO:0008565;GO:0006898;GO:0008286","GO.description":"protein transport;protein transporter activity;receptor-mediated endocytosis;insulin receptor signaling pathway","FunCat.ID":"20.01.10;20.09.18.09.01.01;30.05.01.12.05","FunCat.description":"protein transport;receptor-mediated endocytosis;insulin receptor signalling pathway","PubMed.ID":9819414,"subunits.Protein.name.":"Sorting nexin-2 ;Sorting nexin-4;Insulin receptor ;Sorting nexin-1","subunits.Gene.name.":"SNX2;SNX4;INSR;SNX1","subunits.Gene.name.syn.":";;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1094,"ComplexName":"Frataxin complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"O75964;P10809;P31040;P38646;Q16595;Q9HD34;Q9Y4W6","subunits.Entrez.IDs.":"10632;3329;6389;3313;2395;57128;10939","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515;GO:0005739","GO.description":"protein binding;mitochondrion","FunCat.ID":"16.01;70.16","FunCat.description":"protein binding;mitochondrion","PubMed.ID":17331979,"subunits.Protein.name.":"ATP synthase subunit g, mitochondrial;60 kDa heat shock protein, mitochondrial ;Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial ;Stress-70 protein, mitochondrial ;Frataxin, mitochondrial ;LYR motif-containing protein 4;AFG3-like protein 2","subunits.Gene.name.":"ATP5L;HSPD1;SDHA;HSPA9;FXN;LYRM4;AFG3L2","subunits.Gene.name.syn.":"None;HSP60;SDH2 SDHF;GRP75 HSPA9B mt-HSP70;FRDA X25;C6orf149 ISD11;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1095,"ComplexName":"SNX complex (SNX1a, SNX2, SNX4, EGFR)","Organism":"Human","Synonyms":"EGF receptor complex","Cell.line":"None","subunits.UniProt.IDs.":"O60749;O95219;P00533;Q13596","subunits.Entrez.IDs.":"6643;8723;1956;6642","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0015031;GO:0008565;GO:0006898;GO:0007173","GO.description":"protein transport;protein transporter activity;receptor-mediated endocytosis;epidermal growth factor receptor signaling pathway","FunCat.ID":"20.01.10;20.09.18.09.01.01;30.05.01.12.01","FunCat.description":"protein transport;receptor-mediated endocytosis;EGF-receptor signalling pathway","PubMed.ID":9819414,"subunits.Protein.name.":"Sorting nexin-2 ;Sorting nexin-4;Epidermal growth factor receptor;Sorting nexin-1","subunits.Gene.name.":"SNX2;SNX4;EGFR;SNX1","subunits.Gene.name.syn.":";;ERBB, ERBB1, HER1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1096,"ComplexName":"SNX complex (SNX1,1a,2,4, PDGF receptor)","Organism":"Human","Synonyms":"PDGF receptor complex","Cell.line":"None","subunits.UniProt.IDs.":"O60749;O95219;P16234;Q13596","subunits.Entrez.IDs.":"6643;8723;5156;6642","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0015031;GO:0008565;GO:0006898;GO:0007167","GO.description":"protein transport;protein transporter activity;receptor-mediated endocytosis;enzyme linked receptor protein signaling pathway","FunCat.ID":"20.01.10;20.09.18.09.01.01;30.05.01","FunCat.description":"protein transport;receptor-mediated endocytosis;receptor enzyme mediated signalling","PubMed.ID":9819414,"subunits.Protein.name.":"Sorting nexin-2 ;Sorting nexin-4;Platelet-derived growth factor receptor alpha ;Sorting nexin-1","subunits.Gene.name.":"SNX2;SNX4;PDGFRA;SNX1","subunits.Gene.name.syn.":";;PDGFR2 RHEPDGFRA;","Disease.comment":"None","Subunits.comment":"At the time of annotation, the additional member SNX1a of the protein complex was not found in the UniProt database.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1097,"ComplexName":"eIF3 complex (EIF3S6, EIF3S5, EIF3S4, EIF3S3, EIF3S6IP, EIF3S2, EIF3S9, EIF3S12,  EIF3S10, EIF3S8,  EIF3S1, EIF3S7, PCID1)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00303;O15371;O15372;O75821;O75822;P55884;P60228;Q13347;Q14152;Q7L2H7;Q99613;Q9UBQ5;Q9Y262","subunits.Entrez.IDs.":"8665;8664;8667;8666;8669;8662;3646;8668;8661;10480;8663;27335;51386","Protein.complex.purification.method":"MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0006413","GO.description":"translational initiation","FunCat.ID":"12.04.01","FunCat.description":"translation initiation","PubMed.ID":17322308,"subunits.Protein.name.":"Eukaryotic translation initiation factor 3 subunit F ;Eukaryotic translation initiation factor 3 subunit D ;Eukaryotic translation initiation factor 3 subunit H ;Eukaryotic translation initiation factor 3 subunit G ;Eukaryotic translation initiation factor 3 subunit J ;Eukaryotic translation initiation factor 3 subunit B;Eukaryotic translation initiation factor 3 subunit E ;Eukaryotic translation initiation factor 3 subunit I ;Eukaryotic translation initiation factor 3 subunit A ;Eukaryotic translation initiation factor 3 subunit M ;Eukaryotic translation initiation factor 3 subunit C ;Eukaryotic translation initiation factor 3 subunit K ;Eukaryotic translation initiation factor 3 subunit L","subunits.Gene.name.":"EIF3F;EIF3D;EIF3H;EIF3G;EIF3J;EIF3B;EIF3E;EIF3I;EIF3A;EIF3M;EIF3C;EIF3K;EIF3L","subunits.Gene.name.syn.":"EIF3S5;EIF3S7;EIF3S3;EIF3S4;EIF3S1;EIF3S9;EIF3S6 INT6;EIF3S2 TRIP1;EIF3S10 KIAA0139;HFLB5 PCID1;EIF3S8;EIF3S12;EIF3EIP EIF3S6IP","Disease.comment":"None","Subunits.comment":"Each of 13 subunits of this complex present in stoichiometric amounts (PMID:17322308).","Complex.comment":"Four eIF3 subunits (h, i, k, and m) were found to dissociate preferentially and are therefore likely to be on the periphery of the complex (PMID:17322308).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1098,"ComplexName":"DNA synthesome complex (13 subunits)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P09884;P11387;P11388;P12004;P27694;P28340;P35251;P49005;P49642;P49643;Q14181;Q15054;Q9HCU8","subunits.Entrez.IDs.":"5422;7150;7153;5111;6117;5424;5981;5425;5557;5558;23649;10714;57804","Protein.complex.purification.method":"MI:0226-ion exchange chromatography;MI:0029-cosedimentation through density gradients","GO.ID":"GO:0006260;GO:0005634","GO.description":"DNA replication;nucleus","FunCat.ID":"10.01.03;70.10","FunCat.description":"DNA synthesis and replication;nucleus","PubMed.ID":9279361,"subunits.Protein.name.":"DNA polymerase alpha catalytic subunit;DNA topoisomerase 1;DNA topoisomerase 2-alpha;Proliferating cell nuclear antigen;Replication protein A 70 kDa DNA-binding subunit;DNA polymerase delta catalytic subunit;Replication factor C subunit 1;DNA polymerase delta subunit 2;DNA primase small subunit;DNA primase large subunit;DNA polymerase alpha subunit B;DNA polymerase delta subunit 3;DNA polymerase delta subunit 4","subunits.Gene.name.":"POLA1;TOP1;TOP2A;PCNA;RPA1;POLD1;RFC1;POLD2;PRIM1;PRIM2;POLA2;POLD3;POLD4","subunits.Gene.name.syn.":"POLA;None;TOP2;None;REPA1 RPA70;POLD;RFC140;None;None;PRIM2A;None;KIAA0039;POLDS","Disease.comment":"None","Subunits.comment":"Since the authors did not specify TOP2, we used TOP2A.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1099,"ComplexName":"DNA synthesome complex (17 subunits)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P09884;P11387;P11388;P12004;P27694;P28340;P35251;P49005;P49642;P49643;P56282;Q07864;Q14181;Q15054;Q9HCU8;Q9NR33;Q9NRF9","subunits.Entrez.IDs.":"5422;7150;7153;5111;6117;5424;5981;5425;5557;5558;5427;5426;23649;10714;57804;56655;54107","Protein.complex.purification.method":"MI:0226-ion exchange chromatography;MI:0029-cosedimentation through density gradients","GO.ID":"GO:0006260;GO:0005634","GO.description":"DNA replication;nucleus","FunCat.ID":"10.01.03;70.10","FunCat.description":"DNA synthesis and replication;nucleus","PubMed.ID":9114436,"subunits.Protein.name.":"DNA polymerase alpha catalytic subunit;DNA topoisomerase 1;DNA topoisomerase 2-alpha;Proliferating cell nuclear antigen;Replication protein A 70 kDa DNA-binding subunit;DNA polymerase delta catalytic subunit;Replication factor C subunit 1;DNA polymerase delta subunit 2;DNA primase small subunit;DNA primase large subunit;DNA polymerase epsilon subunit 2;DNA polymerase epsilon catalytic subunit A;DNA polymerase alpha subunit B;DNA polymerase delta subunit 3;DNA polymerase delta subunit 4;DNA polymerase epsilon subunit 4;DNA polymerase epsilon subunit 3","subunits.Gene.name.":"POLA1;TOP1;TOP2A;PCNA;RPA1;POLD1;RFC1;POLD2;PRIM1;PRIM2;POLE2;POLE;POLA2;POLD3;POLD4;POLE4;POLE3","subunits.Gene.name.syn.":"POLA;None;TOP2;None;REPA1 RPA70;POLD;RFC140;None;None;PRIM2A;DPE2;POLE1;None;KIAA0039;POLDS;None;CHRAC17","Disease.comment":"None","Subunits.comment":"Since the authors did not specify TOP2, we used TOP2A.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1100,"ComplexName":"DNA polymerase alpha-primase complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P09884;P49642;P49643;Q14181","subunits.Entrez.IDs.":"5422;5557;5558;23649","Protein.complex.purification.method":"MI:0226- ion exchange chromatography","GO.ID":"GO:0006267;GO:0003688;GO:0005634","GO.description":"pre-replicative complex assembly involved in nuclear cell cycle DNA replication;DNA replication origin binding;nucleus","FunCat.ID":"10.01.03.03;70.10","FunCat.description":"ori recognition and priming complex formation;nucleus","PubMed.ID":12220650,"subunits.Protein.name.":"DNA polymerase alpha catalytic subunit;DNA primase small subunit;DNA primase large subunit;DNA polymerase alpha subunit B","subunits.Gene.name.":"POLA1;PRIM1;PRIM2;POLA2","subunits.Gene.name.syn.":"POLA;None;PRIM2A;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"DNA polymerase alpha-primase can initiate DNA synthesis de novo.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1101,"ComplexName":"TFIIIC containing complex TFIIIC2","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q12789;Q8WUA4;Q9UKN8;Q9Y5Q8;Q9Y5Q9","subunits.Entrez.IDs.":"2975;2976;9329;9328;9330","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04;16.03.01;70.10","FunCat.description":"transcriptional control;DNA binding;nucleus","PubMed.ID":10373544,"subunits.Protein.name.":"General transcription factor 3C polypeptide 1 ;General transcription factor 3C polypeptide 2 ;General transcription factor 3C polypeptide 4 ;General transcription factor 3C polypeptide 5 ;General transcription factor 3C polypeptide 3","subunits.Gene.name.":"GTF3C1;GTF3C2;GTF3C4;GTF3C5;GTF3C3","subunits.Gene.name.syn.":";KIAA0011;;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1103,"ComplexName":"Wave1-Bcl-xl-Pancortin-2 complex, focal ischemic stroke induced","Organism":"Mouse","Synonyms":"None","Cell.line":"cerebral cortical neurons","subunits.UniProt.IDs.":"O88998;Q61337;Q8R5H6","subunits.Entrez.IDs.":"56177;12015;83767","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008637;GO:0005739;GO:0001836;GO:0051402","GO.description":"apoptotic mitochondrial changes;mitochondrion;release of cytochrome c from mitochondria;neuron apoptotic process","FunCat.ID":"40.10.02.02.01;70.16","FunCat.description":"apoptotic mitochondrial changes;mitochondrion","PubMed.ID":17301160,"subunits.Protein.name.":"Noelin ;Bcl2-associated agonist of cell death ;Wiskott-Aldrich syndrome protein family member 1","subunits.Gene.name.":"Olfm1;Bad;Wasf1","subunits.Gene.name.syn.":"Noe1 Noel Noel1;Bbc6;Wave1","Disease.comment":"Wave1-Bcl-xl-Pancortin-2 complex is involved in ischemic stroke.","Subunits.comment":"None","Complex.comment":"Under normal conditions, pancortin-2 is enriched in the adult cerebral cortex but does not interact with WAVE1 and Bcl-xL. The results show that focal ischemic stroke caused the enhancement of the interactions between WAVE1, pancortin-2, and Bcl-xL, which was not attributable to a change in the amounts of these proteins in the cells. The binding of Bcl-xL to WAVE1 is dependent on pancortin-2, and pancortin-2 serves a proapoptotic role in focal ischemic stroke by a mechanism related to its binding to WAVE1 and Bcl-xL. The pancortin-2-WAVE1-Bcl-xL protein complex is associated with mitochondria, and Bax translocation to mitochondria and cytochrome c release is suppressed after brain ischemia in pancortin-/- mice.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1104,"ComplexName":"SNX complex (SNX1a, SNX2, SNX4, TFRC)","Organism":"Human","Synonyms":"Transferrin receptor complex","Cell.line":"None","subunits.UniProt.IDs.":"O60749;O95219;P02786;Q13596","subunits.Entrez.IDs.":"6643;8723;7037;6642","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0015031;GO:0008565;GO:0036465;GO:0000301;GO:0006898","GO.description":"protein transport;protein transporter activity;synaptic vesicle recycling;retrograde transport, vesicle recycling within Golgi;receptor-mediated endocytosis","FunCat.ID":"20.01.10;20.09.07.29;20.09.07.07;20.09.18.09.01.01","FunCat.description":"protein transport;vesicle recycling;retrograde transport;receptor-mediated endocytosis","PubMed.ID":9819414,"subunits.Protein.name.":"Sorting nexin-2 ;Sorting nexin-4;Transferrin receptor protein 1 ;Sorting nexin-1","subunits.Gene.name.":"SNX2;SNX4;TFRC;SNX1","subunits.Gene.name.syn.":";;;","Disease.comment":"None","Subunits.comment":"At the time of annotation, the additional member SNX1a of the protein complex was not found in the UniProt database.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1105,"ComplexName":"TFIIIC containing complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa S3 cells","subunits.UniProt.IDs.":"Q12789;Q8WUA4;Q9UKN8;Q9Y5Q8;Q9Y5Q9","subunits.Entrez.IDs.":"2975;2976;9329;9328;9330","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04;16.03.01;70.10","FunCat.description":"transcriptional control;DNA binding;nucleus","PubMed.ID":9660958,"subunits.Protein.name.":"General transcription factor 3C polypeptide 1 ;General transcription factor 3C polypeptide 2 ;General transcription factor 3C polypeptide 4 ;General transcription factor 3C polypeptide 5 ;General transcription factor 3C polypeptide 3","subunits.Gene.name.":"GTF3C1;GTF3C2;GTF3C4;GTF3C5;GTF3C3","subunits.Gene.name.syn.":";KIAA0011;;;","Disease.comment":"None","Subunits.comment":"At the time of annotation, the additional members of subcomplex TFIIIC1, 70 kDa, 50 kDa, 45kDa and 40 kDa protein were unidentified.","Complex.comment":"The authors differentiate two forms of the isolated complexes, the sucrose gradient centrifugation isolated complex and the immunopurified complex of Hela S3 cell line (C alpha 12), which is called holo TFIIIC. Only the holo TFIIIC shows the further additional components topo I and PC4.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1106,"ComplexName":"TFIIIC containing-TOP1-SUB1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa S3 cells","subunits.UniProt.IDs.":"P11387;P53999;Q12789;Q8WUA4;Q9UKN8;Q9Y5Q8;Q9Y5Q9","subunits.Entrez.IDs.":"7150;10923;2975;2976;9329;9328;9330","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04;16.03.01;70.10","FunCat.description":"transcriptional control;DNA binding;nucleus","PubMed.ID":9660958,"subunits.Protein.name.":"DNA topoisomerase 1;Activated RNA polymerase II transcriptional coactivator p15 ;General transcription factor 3C polypeptide 1 ;General transcription factor 3C polypeptide 2 ;General transcription factor 3C polypeptide 4 ;General transcription factor 3C polypeptide 5 ;General transcription factor 3C polypeptide 3","subunits.Gene.name.":"TOP1;SUB1;GTF3C1;GTF3C2;GTF3C4;GTF3C5;GTF3C3","subunits.Gene.name.syn.":"None;PC4 RPO2TC1;;KIAA0011;;;","Disease.comment":"None","Subunits.comment":"At the time of annotation, the additional members of subcomplex TFIIIC1, 70 kDa, 50 kDa, 45kDa -and 40 kDa protein were unidentified.","Complex.comment":"The authors differentiate two forms of the isolated complexes, the sucrose gradient centrifugation isolated complex and the immunopurified complex of Hela S3 cell line (C alpha 12), which is called holo TFIIIC. Only the holo TFIIIC shows the further additional components topo I and PC4.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1107,"ComplexName":"DNA synthesome core complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P09884;P12004;P28340;P35251;P49005;P49642;P49643;Q14181;Q15054;Q9HCU8","subunits.Entrez.IDs.":"5422;5111;5424;5981;5425;5557;5558;23649;10714;57804","Protein.complex.purification.method":"MI:0226- ion exchange chromatography; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006260;GO:0005634","GO.description":"DNA replication;nucleus","FunCat.ID":"10.01.03;70.10","FunCat.description":"DNA synthesis and replication;nucleus","PubMed.ID":9563011,"subunits.Protein.name.":"DNA polymerase alpha catalytic subunit;Proliferating cell nuclear antigen;DNA polymerase delta catalytic subunit;Replication factor C subunit 1;DNA polymerase delta subunit 2;DNA primase small subunit;DNA primase large subunit;DNA polymerase alpha subunit B;DNA polymerase delta subunit 3;DNA polymerase delta subunit 4","subunits.Gene.name.":"POLA1;PCNA;POLD1;RFC1;POLD2;PRIM1;PRIM2;POLA2;POLD3;POLD4","subunits.Gene.name.syn.":"POLA;None;POLD;RFC140;None;None;PRIM2A;None;KIAA0039;POLDS","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1108,"ComplexName":"DNA synthesome complex (15 subunits)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P09884;P12004;P18858;P28340;P35251;P49005;P49642;P49643;P56282;Q07864;Q14181;Q15054;Q9HCU8;Q9NR33;Q9NRF9","subunits.Entrez.IDs.":"5422;5111;3978;5424;5981;5425;5557;5558;5427;5426;23649;10714;57804;56655;54107","Protein.complex.purification.method":"MI:0226- ion exchange chromatography; MI:0029- cosedimentation through density gradients; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006260;GO:0005634","GO.description":"DNA replication;nucleus","FunCat.ID":"10.01.03;70.10","FunCat.description":"DNA synthesis and replication;nucleus","PubMed.ID":9563011,"subunits.Protein.name.":"DNA polymerase alpha catalytic subunit;Proliferating cell nuclear antigen;DNA ligase 1;DNA polymerase delta catalytic subunit;Replication factor C subunit 1;DNA polymerase delta subunit 2;DNA primase small subunit;DNA primase large subunit;DNA polymerase epsilon subunit 2;DNA polymerase epsilon catalytic subunit A;DNA polymerase alpha subunit B;DNA polymerase delta subunit 3;DNA polymerase delta subunit 4;DNA polymerase epsilon subunit 4;DNA polymerase epsilon subunit 3","subunits.Gene.name.":"POLA1;PCNA;LIG1;POLD1;RFC1;POLD2;PRIM1;PRIM2;POLE2;POLE;POLA2;POLD3;POLD4;POLE4;POLE3","subunits.Gene.name.syn.":"POLA;None;None;POLD;RFC140;None;None;PRIM2A;DPE2;POLE1;None;KIAA0039;POLDS;None;CHRAC17","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1109,"ComplexName":"DNA polymerase alpha","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P33609;P33611","subunits.Entrez.IDs.":"18968;18969","Protein.complex.purification.method":"MI:0091- chromatography technologies; MI:0004- affinity chromatography technologies","GO.ID":"GO:0006260;GO:0005634","GO.description":"DNA replication;nucleus","FunCat.ID":"10.01.03;70.10","FunCat.description":"DNA synthesis and replication;nucleus","PubMed.ID":2226860,"subunits.Protein.name.":"DNA polymerase alpha catalytic subunit;DNA polymerase alpha subunit B","subunits.Gene.name.":"Pola1;Pola2","subunits.Gene.name.syn.":"Pola;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Analysis of the DNA products with poly(dA)-oligo(dT)10 as template-primer revealed that both primase-free DNA polymerase-alpha and the DNA polymerase-alpha-primase complex predominantly synthesized short DNA with less than 30 nucleotides (PMID:2226860).","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1110,"ComplexName":"DNA polymerase alpha-primase complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P20664;P33609;P33610;P33611","subunits.Entrez.IDs.":"19075;18968;19076;18969","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006260;GO:0005634","GO.description":"DNA replication;nucleus","FunCat.ID":"10.01.03;70.10","FunCat.description":"DNA synthesis and replication;nucleus","PubMed.ID":2383257,"subunits.Protein.name.":"DNA primase small subunit;DNA polymerase alpha catalytic subunit;DNA primase large subunit;DNA polymerase alpha subunit B","subunits.Gene.name.":"Prim1;Pola1;Prim2;Pola2","subunits.Gene.name.syn.":"None;Pola;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1111,"ComplexName":"DNA synthesome complex (17 subunits)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P09884;P11387;P11388;P12004;P27694;P28340;P35251;P49005;P49642;P49643;P56282;Q07864;Q14181;Q15054;Q9HCU8;Q9NR33;Q9NRF9","subunits.Entrez.IDs.":"5422;7150;7153;5111;6117;5424;5981;5425;5557;5558;5427;5426;23649;10714;57804;56655;54107","Protein.complex.purification.method":"MI:0226-ion exchange chromatography;MI:0029-cosedimentation through density gradients;MI:0276-blue native page","GO.ID":"GO:0006260;GO:0005634","GO.description":"DNA replication;nucleus","FunCat.ID":"10.01.03;70.10","FunCat.description":"DNA synthesis and replication;nucleus","PubMed.ID":11968016,"subunits.Protein.name.":"DNA polymerase alpha catalytic subunit;DNA topoisomerase 1;DNA topoisomerase 2-alpha;Proliferating cell nuclear antigen;Replication protein A 70 kDa DNA-binding subunit;DNA polymerase delta catalytic subunit;Replication factor C subunit 1;DNA polymerase delta subunit 2;DNA primase small subunit;DNA primase large subunit;DNA polymerase epsilon subunit 2;DNA polymerase epsilon catalytic subunit A;DNA polymerase alpha subunit B;DNA polymerase delta subunit 3;DNA polymerase delta subunit 4;DNA polymerase epsilon subunit 4;DNA polymerase epsilon subunit 3","subunits.Gene.name.":"POLA1;TOP1;TOP2A;PCNA;RPA1;POLD1;RFC1;POLD2;PRIM1;PRIM2;POLE2;POLE;POLA2;POLD3;POLD4;POLE4;POLE3","subunits.Gene.name.syn.":"POLA;None;TOP2;None;REPA1 RPA70;POLD;RFC140;None;None;PRIM2A;DPE2;POLE1;None;KIAA0039;POLDS;None;CHRAC17","Disease.comment":"None","Subunits.comment":"Since the authors did not specify TOP2, we used TOP2A.","Complex.comment":"This complex associates also with a not further characterized DNA helicase.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1112,"ComplexName":"Psd3-Actn1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"hippocampal neurons","subunits.UniProt.IDs.":"Q2PFD7;Q7TPR4","subunits.Entrez.IDs.":"234353;109711","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0018-two hybrid;MI:0096-pull down","GO.ID":"GO:0050789","GO.description":"regulation of biological process","FunCat.ID":"18","FunCat.description":"REGULATION OF METABOLISM AND PROTEIN FUNCTION","PubMed.ID":17298598,"subunits.Protein.name.":"PH and SEC7 domain-containing protein 3 ;Alpha-actinin-1","subunits.Gene.name.":"Psd3;Actn1","subunits.Gene.name.syn.":"Efa6d Kiaa0942;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"EFA6A may form a protein complex with alpha-actinin and activate ARF6 in close proximity of the actin cytoskeleton and membrane proteins in the dendritic spines (PMID:17298598).","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1113,"ComplexName":"5S-DNA-TFIIIA-TFIIIC2 subcomplex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q12789;Q8WUA4;Q92664;Q9UKN8;Q9Y5Q8;Q9Y5Q9","subunits.Entrez.IDs.":"2975;2976;2971;9329;9328;9330","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0004- affinity chromatography technologies","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04;16.03.01;70.10","FunCat.description":"transcriptional control;DNA binding;nucleus","PubMed.ID":12711686,"subunits.Protein.name.":"General transcription factor 3C polypeptide 1 ;General transcription factor 3C polypeptide 2 ;Transcription factor IIIA ;General transcription factor 3C polypeptide 4 ;General transcription factor 3C polypeptide 5 ;General transcription factor 3C polypeptide 3","subunits.Gene.name.":"GTF3C1;GTF3C2;GTF3A;GTF3C4;GTF3C5;GTF3C3","subunits.Gene.name.syn.":";KIAA0011;;;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex could be complemented with TFIIIB beta, TFIIIC1 and RNA polymerase III (pol III) for transcriptional activity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1114,"ComplexName":"5S-DNA-TFIIIA-TFIIIC2-TFIIIB subcomplex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"A6H8Y1;P20226;Q12789;Q8WUA4;Q92664;Q92994;Q9UKN8;Q9Y5Q8;Q9Y5Q9","subunits.Entrez.IDs.":"55814;6908;2975;2976;2971;2972;9329;9328;9330","Protein.complex.purification.method":"MI:0071-molecular sieving;MI:0004-affinity chromatography technologies","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04;16.03.01;70.10","FunCat.description":"transcriptional control;DNA binding;nucleus","PubMed.ID":12711686,"subunits.Protein.name.":"Transcription factor TFIIIB component B'' homolog ;TATA-box-binding protein;General transcription factor 3C polypeptide 1 ;General transcription factor 3C polypeptide 2 ;Transcription factor IIIA ;Transcription factor IIIB 90 kDa subunit ;General transcription factor 3C polypeptide 4 ;General transcription factor 3C polypeptide 5 ;General transcription factor 3C polypeptide 3","subunits.Gene.name.":"BDP1;TBP;GTF3C1;GTF3C2;GTF3A;BRF1;GTF3C4;GTF3C5;GTF3C3","subunits.Gene.name.syn.":"KIAA1241 KIAA1689 TFNR;GTF2D1 TF2D TFIID;;KIAA0011;;BRF GTF3B TAF3B2 TAF3C;;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex has to be complemented with TFIIIC1 and RNA polymerase III (pol III) for full transcriptional activity. Adding pol III to an isolated quaternary 5S-DNA-TFIIIA-TFIIIC2-TFIIIB-beta complex does not suffice for transcription, but the further addition of TFIIIC1 is absolutely required.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1115,"ComplexName":"Cdk5/p35 complex (Cdk5-Cdk5r1 complex)","Organism":"Mouse","Synonyms":"None","Cell.line":"astrocytes","subunits.UniProt.IDs.":"P49615;P61809","subunits.Entrez.IDs.":"12568;12569","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0005515;GO:0007399;GO:0097449","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;protein binding;nervous system development;astrocyte projection","FunCat.ID":"14.07.03;16.01;47.03.01","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;protein binding;nervous system","PubMed.ID":17295212,"subunits.Protein.name.":"Cyclin-dependent-like kinase 5 ;Cyclin-dependent kinase 5 activator 1","subunits.Gene.name.":"Cdk5;Cdk5r1","subunits.Gene.name.syn.":"Cdkn5 Crk6;Cdk5r Nck5a","Disease.comment":"The Cdk5-Cdk5r1 complex (also often called Cdk5/p35 complex) is suggested to be involved in Alzheimers disease (OMIM: 104300). Compare also the CIDER database.","Subunits.comment":"None","Complex.comment":"Astrocytic Cdk5 is involved in process elongation of scratched astrocytes.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1116,"ComplexName":"CRM1-Survivin-AuroraB mitotic complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14980;O15392;Q96GD4","subunits.Entrez.IDs.":"7514;332;9212","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0000278;GO:0051169;GO:0000775","GO.description":"mitotic cell cycle;nuclear transport;chromosome, centromeric region","FunCat.ID":"10.03.01.01;20.09.01;70.10.04","FunCat.description":"mitotic cell cycle;nuclear transport;centromere / kinetochore","PubMed.ID":17099693,"subunits.Protein.name.":"Exportin-1 ;Baculoviral IAP repeat-containing protein 5;Aurora kinase B","subunits.Gene.name.":"XPO1;BIRC5;AURKB","subunits.Gene.name.syn.":"CRM1;API4, IAP4;AIK2, AIM1, AIRK2, ARK2 STK1, STK12, STK5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Crm1 could be recovered in a complex with endogenous Survivin-Aurora-B from mitotic cells, whereas complex formation was abolished on pretreatment with LMB (leptomycin B).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1117,"ComplexName":"CRM1-Survivin mitotic complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14980;O15392","subunits.Entrez.IDs.":"7514;332","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0000278;GO:0051169;GO:0000775","GO.description":"mitotic cell cycle;nuclear transport;chromosome, centromeric region","FunCat.ID":"10.03.01.01;20.09.01;70.10.04","FunCat.description":"mitotic cell cycle;nuclear transport;centromere / kinetochore","PubMed.ID":17099693,"subunits.Protein.name.":"Exportin-1 ;Baculoviral IAP repeat-containing protein 5","subunits.Gene.name.":"XPO1;BIRC5","subunits.Gene.name.syn.":"CRM1;API4, IAP4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The Survivin-Crm1 interaction is essential for chromosomal passenger complex localization and function.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1118,"ComplexName":"Chromosomal passenger complex CPC (INCENP, CDCA8, BIRC5, AURKB)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15392;Q53HL2;Q96GD4;Q9NQS7","subunits.Entrez.IDs.":"332;55143;9212;3619","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0000278;GO:0007059;GO:0000775","GO.description":"mitotic cell cycle;chromosome segregation;chromosome, centromeric region","FunCat.ID":"10.03.01.01;10.03.04.05;70.10.04","FunCat.description":"mitotic cell cycle;chromosome segregation/division;centromere / kinetochore","PubMed.ID":17099693,"subunits.Protein.name.":"Baculoviral IAP repeat-containing protein 5;Borealin ;Aurora kinase B;Inner centromere protein","subunits.Gene.name.":"BIRC5;CDCA8;AURKB;INCENP","subunits.Gene.name.syn.":"API4, IAP4;PESCRG3;AIK2, AIM1, AIRK2, ARK2 STK1, STK12, STK5;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Borealin forms a complex with Survivin, which can bind to Aurora-B kinase and is incorporated into the CP-holocomplex by interacting with INCENP (PMID:16571674). The NES in Survivin mediates the recruitment of Crm1-Ran-GTP, which seems to be involved in guiding the CPC to the centromeres in early prophase by an unknown mechanism.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1119,"ComplexName":"Chromosomal passenger complex CPC (INCENP, CDCA8, BIRC5, AURKB)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15392;Q53HL2;Q96GD4;Q9NQS7","subunits.Entrez.IDs.":"332;55143;9212;3619","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0000278;GO:0007059;GO:0003677;GO:0000775","GO.description":"mitotic cell cycle;chromosome segregation;DNA binding;chromosome, centromeric region","FunCat.ID":"10.03.01.01;10.03.04.05;16.03.01;70.10.04","FunCat.description":"mitotic cell cycle;chromosome segregation/division;DNA binding;centromere / kinetochore","PubMed.ID":16571674,"subunits.Protein.name.":"Baculoviral IAP repeat-containing protein 5;Borealin ;Aurora kinase B;Inner centromere protein","subunits.Gene.name.":"BIRC5;CDCA8;AURKB;INCENP","subunits.Gene.name.syn.":"API4, IAP4;PESCRG3;AIK2, AIM1, AIRK2, ARK2 STK1, STK12, STK5;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Yeast two hybrid analysis pointed out that Aurora B associates with the C terminus of INCENP via the IN-box, Survivin and Borealin interact with the N-terminal 58 amino acids of INCENP and bind to each other.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1120,"ComplexName":"Chromosomal passenger complex CPC (INCENP, CDCA8, BIRC5)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15392;Q53HL2;Q9NQS7","subunits.Entrez.IDs.":"332;55143;3619","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0000278;GO:0007059;GO:0003677;GO:0000775","GO.description":"mitotic cell cycle;chromosome segregation;DNA binding;chromosome, centromeric region","FunCat.ID":"10.03.01.01;10.03.04.05;16.03.01;70.10.04","FunCat.description":"mitotic cell cycle;chromosome segregation/division;DNA binding;centromere / kinetochore","PubMed.ID":16571674,"subunits.Protein.name.":"Baculoviral IAP repeat-containing protein 5;Borealin ;Inner centromere protein","subunits.Gene.name.":"BIRC5;CDCA8;INCENP","subunits.Gene.name.syn.":"API4, IAP4;PESCRG3;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Yeast two hybrid analysis pointed out that Survivin and Borealin interact with the N-terminal 58 amino acids of INCENP and bind to each other. The authors showed that a ternary complex between Borealin, Survivin, and the first 58 amino acids of INCENP (INCENP1-58) exists in vivo. This subcomplex was found to be essential and sufficient for targeting to the centromere. Notably, AuroraB kinase, the enzymatic core of the CPC, was not required for centromere localization of the subcomplex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1121,"ComplexName":"WNK1-OSR1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95747;Q9H4A3","subunits.Entrez.IDs.":"9943;65125","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515;GO:0050789;GO:0006970;GO:0007588;GO:0030104;GO:0043575;GO:0005034","GO.description":"protein binding;regulation of biological process;response to osmotic stress;excretion;water homeostasis;detection of osmotic stimulus;osmosensor activity","FunCat.ID":"16.01;18;34.11.03.13;34.01.05","FunCat.description":"protein binding;REGULATION OF METABOLISM AND PROTEIN FUNCTION;osmosensing  and response;water homeostasis","PubMed.ID":17190791,"subunits.Protein.name.":"Serine/threonine-protein kinase OSR1 ;Serine/threonine-protein kinase WNK1","subunits.Gene.name.":"OXSR1;WNK1","subunits.Gene.name.syn.":"KIAA1101 OSR1;HSN2 KDP KIAA0344 PRKWNK1","Disease.comment":"WNK1 is mutated in Gordon's hypertension syndrome.","Subunits.comment":"None","Complex.comment":"WNK1 and OSR1 regulate NKCC activity (sodium, potassium, two chloride cotransporter) (PMID:16832045).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1122,"ComplexName":"Smcb-Smcd-PW29 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q61550;Q9CU62;Q9CW03","subunits.Entrez.IDs.":"19357;24061;13006","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0000278;GO:0007059;GO:0005694","GO.description":"mitotic cell cycle;chromosome segregation;chromosome","FunCat.ID":"10.03.01.01;10.03.04.05;70.10.03","FunCat.description":"mitotic cell cycle;chromosome segregation/division;chromosome","PubMed.ID":10375619,"subunits.Protein.name.":"Double-strand-break repair protein rad21 homolog ;Structural maintenance of chromosomes protein 1A ;Structural maintenance of chromosomes protein 3","subunits.Gene.name.":"Rad21;Smc1a;Smc3","subunits.Gene.name.syn.":"Hr21;Sb1.8 Smc1 Smc1l1 Smcb;Bam Bmh Cspg6 Mmip1 Smc3l1 Smcd","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors show that overexpression of a PW29-GFP fusion protein in mouse fibroblasts leads to inhibition of proliferation, implicating this protein and its complex with SMC proteins in the control of mitotic cycle progression.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1123,"ComplexName":"WNK1-SPAk complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q9H4A3;Q9UEW8","subunits.Entrez.IDs.":"65125;27347","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515;GO:0050789;GO:0006970;GO:0007588;GO:0030104;GO:0043575;GO:0005034","GO.description":"protein binding;regulation of biological process;response to osmotic stress;excretion;water homeostasis;detection of osmotic stimulus;osmosensor activity","FunCat.ID":"16.01;18;34.11.03.13;34.01.05","FunCat.description":"protein binding;REGULATION OF METABOLISM AND PROTEIN FUNCTION;osmosensing  and response;water homeostasis","PubMed.ID":17190791,"subunits.Protein.name.":"Serine/threonine-protein kinase WNK1;STE20/SPS1-related proline-alanine-rich protein kinase","subunits.Gene.name.":"WNK1;STK39","subunits.Gene.name.syn.":"HSN2 KDP KIAA0344 PRKWNK1;SPAK","Disease.comment":"WNK1 is mutated in Gordon's hypertension syndrome.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1124,"ComplexName":"SNARE complex (Snap25, Stx1a, Vamp2, Cplx1, Cplx3)","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P32851;P60881;P63041;P63045;Q8R1B5","subunits.Entrez.IDs.":"116470;25012;64832;24803;235415","Protein.complex.purification.method":"MI:0027- cosedimentation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":15911881,"subunits.Protein.name.":"Syntaxin-1A;Synaptosomal-associated protein 25;Complexin-1;Vesicle-associated membrane protein 2;Complexin-3","subunits.Gene.name.":"Stx1a;Snap25;Cplx1;Vamp2;Cplx3","subunits.Gene.name.syn.":"Sap;Snap;None;Syb2;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Mus musculus (Mouse)"}
{"ComplexID":1125,"ComplexName":"SNARE complex (Snap25, Stx1a, Vamp2, Cplx3, Cplx4)","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P32851;P60881;P63045;Q80WM3;Q8R1B5","subunits.Entrez.IDs.":"116470;25012;24803;225644;235415","Protein.complex.purification.method":"MI:0027-cosedimentation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":15911881,"subunits.Protein.name.":"Syntaxin-1A;Synaptosomal-associated protein 25;Vesicle-associated membrane protein 2;Complexin-4;Complexin-3","subunits.Gene.name.":"Stx1a;Snap25;Vamp2;Cplx4;Cplx3","subunits.Gene.name.syn.":"Sap;Snap;Syb2;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1126,"ComplexName":"SNARE complex (Snap25, Stx1a,3, Vamp2, Cplx1, Cplx3, Cplx4)","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P32851;P60881;P63041;P63045;Q08849;Q80WM3;Q8R1B5","subunits.Entrez.IDs.":"116470;25012;64832;24803;81802;225644;235415","Protein.complex.purification.method":"MI:0027- cosedimentation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":15911881,"subunits.Protein.name.":"Syntaxin-1A;Synaptosomal-associated protein 25;Complexin-1;Vesicle-associated membrane protein 2;Syntaxin-3;Complexin-4;Complexin-3","subunits.Gene.name.":"Stx1a;Snap25;Cplx1;Vamp2;Stx3;Cplx4;Cplx3","subunits.Gene.name.syn.":"Sap;Snap;None;Syb2;Stx3a;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway. The interaction between the SNARE complex and CPX4 indicates a lower binding affinity.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1127,"ComplexName":"Shps1-Fyb-Skap55r complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS-7 cells","subunits.UniProt.IDs.":"O35601;P97797;Q3UND0","subunits.Entrez.IDs.":"23880;19261;54353","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0023052;GO:0007155;GO:0006909","GO.description":"signaling;cell adhesion;phagocytosis","FunCat.ID":"30.01;34.07;36.25.16.01.03","FunCat.description":"cellular signalling;cell adhesion;phagocyte response (e.g. macrophages, dendritic cells, granulocytes)","PubMed.ID":10469599,"subunits.Protein.name.":"FYN-binding protein ;Tyrosine-protein phosphatase non-receptor type substrate 1 ;Src kinase-associated phosphoprotein 2","subunits.Gene.name.":"Fyb;Sirpa;Skap2","subunits.Gene.name.syn.":";Bit Myd1 Ptpns1 Shps1 Sirp;Prap Ra70 Saps Scap2 Skap55r","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Analysis done in randomly growing normal cells and bone marrow derived macrophages (BMM) from mice homozygotic for the motheaten (me) mutation and in transfected COS-7 cell line. Formation of the complex was independent of SHP-1 and tyrosine phosphorylation of SHPS-1.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1128,"ComplexName":"Shps1-Pyk2 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS-7 cells","subunits.UniProt.IDs.":"P97797;Q9QVP9","subunits.Entrez.IDs.":"19261;19229","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0023052;GO:0007155;GO:0006909","GO.description":"signaling;cell adhesion;phagocytosis","FunCat.ID":"30.01;34.07;36.25.16.01.03","FunCat.description":"cellular signalling;cell adhesion;phagocyte response (e.g. macrophages, dendritic cells, granulocytes)","PubMed.ID":10469599,"subunits.Protein.name.":"Tyrosine-protein phosphatase non-receptor type substrate 1 ;Protein-tyrosine kinase 2-beta","subunits.Gene.name.":"Sirpa;Ptk2b","subunits.Gene.name.syn.":"Bit Myd1 Ptpns1 Shps1 Sirp;Fak2, Pyk2, Raftk","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Analysis done in randomly growing normal cells and bone marrow derived macrophages (BMM) from mice homozygotic for the motheaten (me) mutation and in transfected COS-7 cell line. Formation of the complex was independent of SHP-1 and tyrosine phosphorylation of SHPS-1.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1129,"ComplexName":"Complexin complex (Stx3, Cplx1, Cplx3)","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P63041;Q08849;Q8R1B5","subunits.Entrez.IDs.":"64832;81802;235415","Protein.complex.purification.method":"MI:0027- cosedimentation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":15911881,"subunits.Protein.name.":"Complexin-1;Syntaxin-3;Complexin-3","subunits.Gene.name.":"Cplx1;Stx3;Cplx3","subunits.Gene.name.syn.":"None;Stx3a;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"All known CPXs interact with SNARE complexes. They may therefore play a role in neurotransmitter release.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Mus musculus (Mouse)"}
{"ComplexID":1130,"ComplexName":"Hip1R-cortactin complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75146;Q14247","subunits.Entrez.IDs.":"9026;2017","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0005198;GO:0030048;GO:0005737","GO.description":"structural molecule activity;actin filament-based movement;cytoplasm","FunCat.ID":"16.07;20.09.14.02;70.03","FunCat.description":"structural protein binding;actin dependent transport;cytoplasm","PubMed.ID":17318189,"subunits.Protein.name.":"Huntingtin-interacting protein 1-related protein ;Src substrate cortactin","subunits.Gene.name.":"HIP1R;CTTN","subunits.Gene.name.syn.":"HIP12 KIAA0655;EMS1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The Hip1R-cortactin complex negatively regulates actin assembly associated with endocytosis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1131,"ComplexName":"RFC2-RIalpha complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P30153;P35250","subunits.Entrez.IDs.":"5518;5982","Protein.complex.purification.method":"MI:0018- two hybrid; MI:0019- coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0005515","GO.description":"protein binding","FunCat.ID":"16.01","FunCat.description":"protein binding","PubMed.ID":15655353,"subunits.Protein.name.":"Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform;Replication factor C subunit 2","subunits.Gene.name.":"PPP2R1A;RFC2","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1132,"ComplexName":"RFC2-RIalpha complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P30153;P35249","subunits.Entrez.IDs.":"5518;5984","Protein.complex.purification.method":"MI:0018- two hybrid; MI:0019- coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0005515","GO.description":"protein binding","FunCat.ID":"16.01","FunCat.description":"protein binding","PubMed.ID":15655353,"subunits.Protein.name.":"Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform;Replication factor C subunit 4","subunits.Gene.name.":"PPP2R1A;RFC4","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1133,"ComplexName":"ATR-HDAC2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q13535;Q92769","subunits.Entrez.IDs.":"545;3066","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0019- coimmunoprecipitation","GO.ID":"GO:0006265;GO:0006473;GO:0006476;GO:0051276","GO.description":"DNA topological change;protein acetylation;protein deacetylation;chromosome organization","FunCat.ID":"10.01.09.05;14.07.04;42.10.03","FunCat.description":"DNA conformation modification (e.g. chromatin);modification by acetylation, deacetylation;organization of chromosome structure","PubMed.ID":10545197,"subunits.Protein.name.":"Serine/threonine-protein kinase ATR ;Histone deacetylase 2","subunits.Gene.name.":"ATR;HDAC2","subunits.Gene.name.syn.":"FRP1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The ATR-HDAC2 complex is a robust biochemical entity that withstands ammonium sulfate precipitation and anion exchange chromatography.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1134,"ComplexName":"ATR-HDAC2-CHD4 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q13535;Q14839;Q92769","subunits.Entrez.IDs.":"545;1108;3066","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0006265;GO:0000075;GO:0006473;GO:0006476;GO:0006974;GO:0051276;GO:0005634","GO.description":"DNA topological change;cell cycle checkpoint;protein acetylation;protein deacetylation;cellular response to DNA damage stimulus;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;10.03.01.03;14.07.04;32.01.09;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);modification by acetylation, deacetylation;DNA damage response;organization of chromosome structure;nucleus","PubMed.ID":10545197,"subunits.Protein.name.":"Serine/threonine-protein kinase ATR ;Chromodomain-helicase-DNA-binding protein 4;Histone deacetylase 2","subunits.Gene.name.":"ATR;CHD4;HDAC2","subunits.Gene.name.syn.":"FRP1;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Other members of the NRD complex HDAC1, MTA-1, and MTA-2 are also detectable in ATR immunoprecipitates.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1135,"ComplexName":"Mss4-Itga3 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q62470;Q91X96","subunits.Entrez.IDs.":"16400;98710","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0018- two hybrid","GO.ID":"GO:0005515;GO:0050789;GO:0005886","GO.description":"protein binding;regulation of biological process;plasma membrane","FunCat.ID":"16.01;18;70.02","FunCat.description":"protein binding;REGULATION OF METABOLISM AND PROTEIN FUNCTION;eukaryotic plasma membrane / membrane attached","PubMed.ID":17172637,"subunits.Protein.name.":"Integrin alpha-3 ;Guanine nucleotide exchange factor MSS4","subunits.Gene.name.":"Itga3;Rabif","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Mss4 binds to the cytosolic membrane proximal conserved region of {alpha}-integrin chains and this interaction is essential for MT1-MMP-mediated activation of MMP-2 and -9 as well as for ECM organization (PMID:17172637).","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1136,"ComplexName":"Mss4-Itga7 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q61738;Q91X96","subunits.Entrez.IDs.":"16404;98710","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0018- two hybrid","GO.ID":"GO:0005515;GO:0050789;GO:0005886","GO.description":"protein binding;regulation of biological process;plasma membrane","FunCat.ID":"16.01;18;70.02","FunCat.description":"protein binding;REGULATION OF METABOLISM AND PROTEIN FUNCTION;eukaryotic plasma membrane / membrane attached","PubMed.ID":17172637,"subunits.Protein.name.":"Integrin alpha-7 [Cleaved into: Integrin alpha-7 heavy chain; Integrin alpha-7 light chain];Guanine nucleotide exchange factor MSS4","subunits.Gene.name.":"Itga7;Rabif","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Mss4 binds to the cytosolic membrane proximal conserved region of {alpha}-integrin chains and this interaction is essential for MT1-MMP-mediated activation of MMP-2 and -9 as well as for ECM organization (PMID:17172637).","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1137,"ComplexName":"SNARE complex (VAMP2, SNAP25, STX1a, CPLX1, CPLX3)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14810;P60880;P63027;Q16623;Q8WVH0","subunits.Entrez.IDs.":"10815;6616;6844;6804;594855","Protein.complex.purification.method":"MI:0027- cosedimentation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":15911881,"subunits.Protein.name.":"Complexin-1 ;Synaptosomal-associated protein 25 ;Vesicle-associated membrane protein 2 ;Syntaxin-1A ;Complexin-3","subunits.Gene.name.":"CPLX1;SNAP25;VAMP2;STX1A;CPLX3","subunits.Gene.name.syn.":";SNAP;SYB2;STX1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1138,"ComplexName":"SNARE complex (VAMP2, SNAP25, STX1a, CPLX3, CPLX4)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P60880;P63027;Q16623;Q7Z7G2;Q8WVH0","subunits.Entrez.IDs.":"6616;6844;6804;339302;594855","Protein.complex.purification.method":"MI:0027- cosedimentation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":15911881,"subunits.Protein.name.":"Synaptosomal-associated protein 25 ;Vesicle-associated membrane protein 2 ;Syntaxin-1A ;Complexin-4 ;Complexin-3","subunits.Gene.name.":"SNAP25;VAMP2;STX1A;CPLX4;CPLX3","subunits.Gene.name.syn.":"SNAP;SYB2;STX1;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway. The interaction between the SNARE complex and CPX4 indicates a lower binding affinity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1139,"ComplexName":"SNARE complex (VAMP2, SNAP25, STX1a, STX3, CPLX1, CPLX3, CPLX4)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14810;P60880;P63027;Q13277;Q16623;Q7Z7G2;Q8WVH0","subunits.Entrez.IDs.":"10815;6616;6844;6809;6804;339302;594855","Protein.complex.purification.method":"MI:0027- cosedimentation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":15911881,"subunits.Protein.name.":"Complexin-1 ;Synaptosomal-associated protein 25 ;Vesicle-associated membrane protein 2 ;Syntaxin-3;Syntaxin-1A ;Complexin-4 ;Complexin-3","subunits.Gene.name.":"CPLX1;SNAP25;VAMP2;STX3;STX1A;CPLX4;CPLX3","subunits.Gene.name.syn.":";SNAP;SYB2;STX3A;STX1;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway. The interaction between the SNARE complex and CPX4 indicates a lower binding affinity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1140,"ComplexName":"Complexin complex (STX3, CPLX1, CPLX3)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14810;Q13277;Q8WVH0","subunits.Entrez.IDs.":"10815;6809;594855","Protein.complex.purification.method":"MI:0027- cosedimentation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":15911881,"subunits.Protein.name.":"Complexin-1 ;Syntaxin-3;Complexin-3","subunits.Gene.name.":"CPLX1;STX3;CPLX3","subunits.Gene.name.syn.":";STX3A;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1141,"ComplexName":"CF IIAm complex (Cleavage factor IIAm complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43809;O60231;O94913;P19447;P23246;P26368;P26599;P49959;Q01081;Q07157;Q14444;Q16630;Q8N684;Q92759;Q92989;Q9UKF6","subunits.Entrez.IDs.":"11051;8449;51585;2071;6421;11338;5725;4361;7307;7082;4076;11052;79869;2968;10978;51692","Protein.complex.purification.method":"MI:0226- ion exchange chromatography","GO.ID":"GO:0031123;GO:0031124;GO:0005634","GO.description":"RNA 3'-end processing;mRNA 3'-end processing;nucleus","FunCat.ID":"11.04.03.05;70.10","FunCat.description":"3'-end processing;nucleus","PubMed.ID":11060040,"subunits.Protein.name.":"Cleavage and polyadenylation specificity factor subunit 5 ;Putative pre-mRNA-splicing factor ATP-dependent RNA helicase DHX16 ;Pre-mRNA cleavage complex 2 protein Pcf11 ;TFIIH basal transcription factor complex helicase XPB subunit ;Splicing factor, proline- and glutamine-rich ;Splicing factor U2AF 65 kDa subunit ;Polypyrimidine tract-binding protein 1 ;Double-strand break repair protein MRE11A ;Splicing factor U2AF 35 kDa subunit ;Tight junction protein ZO-1;Caprin-1 ;Cleavage and polyadenylation specificity factor subunit 6 ;Cleavage and polyadenylation specificity factor subunit 7 ;General transcription factor IIH subunit 4 ;Polyribonucleotide 5'-hydroxyl-kinase Clp1 ;Cleavage and polyadenylation specificity factor subunit 3","subunits.Gene.name.":"NUDT21;DHX16;PCF11;ERCC3;SFPQ;U2AF2;PTBP1;MRE11A;U2AF1;TJP1;CAPRIN1;CPSF6;CPSF7;GTF2H4;CLP1;CPSF3","subunits.Gene.name.syn.":"CFIM25 CPSF25 CPSF5;DBP2 DDX16 KIAA0577;KIAA0824;XPB XPBC;PSF;U2AF65;PTB;HNGS1 MRE11;U2AF35 U2AFBP;ZO1;GPIAP1 GPIP137 M11S1 RNG105;CFIM68;;;HEAB;CPSF73","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Eukaryotic mRNA precursors (pre-mRNAs) undergo a number of processing steps before they are exported to the cytoplasm. Six different protein factors are required in vitro for 3' end formation of mammalian pre-mRNAs by endonucleolytic cleavage and polyadenylation. One of these factors is cleavage factor IIm (CF IIm). During purification of CF IIm, the activity separated into an essential fraction (CF IIAm) and an apparently non-essential, but stimulatory component (CF IIBm).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1142,"ComplexName":"SMN complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14893;P14678;P62304;P62306;P62308;P62314;P62316;P62318;Q16637;Q9UHI6","subunits.Entrez.IDs.":"8487;6628;6635;6636;6637;6632;6633;6634;None;11218","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008380;GO:0032774;GO:0006461;GO:0003723;GO:0005737;GO:0005634","GO.description":"RNA splicing;RNA biosynthetic process;protein complex assembly;RNA binding;cytoplasm;nucleus","FunCat.ID":"11.04.03.01;11.02;14.10;16.03.03;70.03;70.10","FunCat.description":"splicing;RNA synthesis;assembly of protein complexes;RNA binding;cytoplasm;nucleus","PubMed.ID":10601333,"subunits.Protein.name.":"Gem-associated protein 2 ;Small nuclear ribonucleoprotein-associated proteins B and B' ;Small nuclear ribonucleoprotein E ;Small nuclear ribonucleoprotein F ;Small nuclear ribonucleoprotein G ;Small nuclear ribonucleoprotein Sm D1 ;Small nuclear ribonucleoprotein Sm D2 ;Small nuclear ribonucleoprotein Sm D3 ;Survival motor neuron protein;Probable ATP-dependent RNA helicase DDX20","subunits.Gene.name.":"GEMIN2;SNRPB;SNRPE;SNRPF;SNRPG;SNRPD1;SNRPD2;SNRPD3;SMN1; SMN2;DDX20","subunits.Gene.name.syn.":"SIP1;COD SNRPB1;;PBSCF;PBSCG;;SNRPD1;;SMN; SMNT; SMNC;DP103 GEMIN3","Disease.comment":"Spinal muscular atrophy (SMA)","Subunits.comment":"Several other subunits of the complex were found in the analysis, which have not been further characterized:  p175, p95, p60, p50 using anti-SMN (2B1) or p175, p115, p95, p50 using anti-Gemin3 (11G9).","Complex.comment":"Assembly of the Sm-class of U-rich small nuclear ribonucleoprotein particles (U snRNPs) is a process facilitated by the macromolecular survival of motor neuron (SMN) complex. Spinal muscular atrophy (SMA) is the most common genetic cause of infant mortality. Deletions or mutations in the survival of motor neurons (SMN1) gene, the SMA-causing gene, are detected in over 95% of SMA patients. The SMN complex is found both in the cytoplasm and in the nucleus, where it is concentrated in gems, nuclear bodies similar in size and number to Cajal (coiled) bodies and often associated with them.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1143,"ComplexName":"SMN complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14893;P14678;P57678;P62304;P62306;P62308;P62314;P62316;P62318;Q16637;Q8TEQ6;Q8WXD5;Q9H840;Q9NWZ8;Q9UHI6;Q9Y3F4","subunits.Entrez.IDs.":"8487;6628;50628;6635;6636;6637;6632;6633;6634;None;25929;79833;79760;54960;11218;11171","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008380;GO:0032774;GO:0006461;GO:0003723;GO:0005737;GO:0005634","GO.description":"RNA splicing;RNA biosynthetic process;protein complex assembly;RNA binding;cytoplasm;nucleus","FunCat.ID":"11.04.03.01;11.02;14.10;16.03.03;70.03;70.10","FunCat.description":"splicing;RNA synthesis;assembly of protein complexes;RNA binding;cytoplasm;nucleus","PubMed.ID":17178713,"subunits.Protein.name.":"Gem-associated protein 2 ;Small nuclear ribonucleoprotein-associated proteins B and B' ;Gem-associated protein 4 ;Small nuclear ribonucleoprotein E ;Small nuclear ribonucleoprotein F ;Small nuclear ribonucleoprotein G ;Small nuclear ribonucleoprotein Sm D1 ;Small nuclear ribonucleoprotein Sm D2 ;Small nuclear ribonucleoprotein Sm D3 ;Survival motor neuron protein;Gem-associated protein 5 ;Gem-associated protein 6 ;Gem-associated protein 7 ;Gem-associated protein 8 ;Probable ATP-dependent RNA helicase DDX20 ;Serine-threonine kinase receptor-associated protein","subunits.Gene.name.":"GEMIN2;SNRPB;GEMIN4;SNRPE;SNRPF;SNRPG;SNRPD1;SNRPD2;SNRPD3;SMN1; SMN2;GEMIN5;GEMIN6;GEMIN7;GEMIN8;DDX20;STRAP","subunits.Gene.name.syn.":"SIP1;COD SNRPB1;;;PBSCF;PBSCG;;SNRPD1;;SMN; SMNT; SMNC;;;;FAM51A1;DP103 GEMIN3;MAWD UNRIP","Disease.comment":"Spinal muscular atrophy (SMA)","Subunits.comment":"None","Complex.comment":"Assembly of the Sm-class of U-rich small nuclear ribonucleoprotein particles (U snRNPs) is a process facilitated by the macromolecular survival of motor neuron (SMN) complex.  Spinal muscular atrophy (SMA) is the most common genetic cause of infant mortality. Deletions or mutations in the survival of motor neurons (SMN1) gene, the SMA-causing gene, are detected in over 95% of SMA patients. The SMN complex is found both in the cytoplasm and in the nucleus, where it is concentrated in gems, nuclear bodies similar in size and number to Cajal (coiled) bodies and often associated with them. Nine factors, including the SMN protein, the product of the spinal muscular atrophy (SMA) disease gene, Gemins 2-8  and unrip have been identified as the major components of the SMN complex. Interaction studies in the present article revealed a framework of the SMN complex with SMN, Gemin7, and Gemin8 as its backbone.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1144,"ComplexName":"Cleavage and polyadenylation factor (CPSF)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95639;Q10570;Q6UN15;Q9P2I0;Q9UKF6","subunits.Entrez.IDs.":"10898;29894;None;53981;51692","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0031123;GO:0031124;GO:0003723;GO:0051098;GO:0005515;GO:0030234;GO:0050790;GO:0005634","GO.description":"RNA 3'-end processing;mRNA 3'-end processing;RNA binding;regulation of binding;protein binding;enzyme regulator activity;regulation of catalytic activity;nucleus","FunCat.ID":"11.04.03.05;16.03.03;18.01.07;16.01;18.02.01;70.10","FunCat.description":"3'-end processing;RNA binding;regulation by binding / dissociation;protein binding;enzymatic activity regulation / enzyme regulator;nucleus","PubMed.ID":14749727,"subunits.Protein.name.":"Cleavage and polyadenylation specificity factor subunit 4 ;Cleavage and polyadenylation specificity factor subunit 1 ;Pre-mRNA 3'-end-processing factor FIP1 ;Cleavage and polyadenylation specificity factor subunit 2 ;Cleavage and polyadenylation specificity factor subunit 3","subunits.Gene.name.":"CPSF4;CPSF1;FIP1L1;CPSF2;CPSF3","subunits.Gene.name.syn.":"CPSF30 NAR NEB1;CPSF160;FIP1 RHE;CPSF100 KIAA1367;CPSF73","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In mammals, polyadenylation of mRNA precursors (pre-mRNAs) by poly(A) polymerase (PAP) depends on cleavage and polyadenylation specificity factor (CPSF). CPSF is a multisubunit complex that binds to the canonical AAUAAA hexamer and to U-rich upstream sequence elements on the pre-mRNA, thereby stimulating the otherwise weakly active and nonspecific polymerase to elongate efficiently RNAs containing a poly(A) signal.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1145,"ComplexName":"Mammalian cleavage factor I (CF Im)","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"O43809;Q16630","subunits.Entrez.IDs.":"11051;11052","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0031123;GO:0031124;GO:0003723;GO:0005634","GO.description":"RNA 3'-end processing;mRNA 3'-end processing;RNA binding;nucleus","FunCat.ID":"11.04.03.05;16.03.03;70.10","FunCat.description":"3'-end processing;RNA binding;nucleus","PubMed.ID":17172643,"subunits.Protein.name.":"Cleavage and polyadenylation specificity factor subunit 5 ;Cleavage and polyadenylation specificity factor subunit 6","subunits.Gene.name.":"NUDT21;CPSF6","subunits.Gene.name.syn.":"CFIM25 CPSF25 CPSF5;CFIM68","Disease.comment":"None","Subunits.comment":"Since NUDT21 and CPSF6 from green monkey were not available in the UniProt database at the time of annotation, the orthologous human proteins were used.","Complex.comment":"Eukaryotic mRNA precursors (pre-mRNAs) undergo a number of processing steps before they are exported to the cytoplasm. The binding of CF Im to the pre-mRNA is thought to be one of the earliest steps in the assembly of the cleavage and polyadenylation machinery and facilitates the recruitment of other processing factors.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1146,"ComplexName":"Cleavage stimulation factor","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P33240;Q05048;Q12996","subunits.Entrez.IDs.":"1478;1477;1479","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0031123;GO:0031124;GO:0003723;GO:0005634","GO.description":"RNA 3'-end processing;mRNA 3'-end processing;RNA binding;nucleus","FunCat.ID":"11.04.03.05;16.03.03;70.10","FunCat.description":"3'-end processing;RNA binding;nucleus","PubMed.ID":10669729,"subunits.Protein.name.":"Cleavage stimulation factor subunit 2 ;Cleavage stimulation factor subunit 1 ;Cleavage stimulation factor subunit 3","subunits.Gene.name.":"CSTF2;CSTF1;CSTF3","subunits.Gene.name.syn.":";;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Polyadenylation of mRNA precursors is a two-step reaction requiring multiple protein factors. Cleavage stimulation factor (CstF) is a heterotrimer necessary for the first step, endonucleolytic cleavage, and it plays an important role in determining the efficiency of polyadenylation. The cleavage and polyadenylation specificity factor (CPSF) recognizes the highly conserved hexanucleotide AAUAAA, whereas CstF binds to GU- or U-rich elements downstream of the poly(A) site.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1147,"ComplexName":"Polyadenylation complex (CSTF1, CSTF2, CSTF3, SYMPK CPSF1, CPSF2, CPSF3)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P33240;Q05048;Q10570;Q12996;Q92797;Q9P2I0;Q9UKF6","subunits.Entrez.IDs.":"1478;1477;29894;1479;8189;53981;51692","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0031123;GO:0031124;GO:0003723;GO:0005634","GO.description":"RNA 3'-end processing;mRNA 3'-end processing;RNA binding;nucleus","FunCat.ID":"11.04.03.05;16.03.03;70.10","FunCat.description":"3'-end processing;RNA binding;nucleus","PubMed.ID":10669729,"subunits.Protein.name.":"Cleavage stimulation factor subunit 2 ;Cleavage stimulation factor subunit 1 ;Cleavage and polyadenylation specificity factor subunit 1 ;Cleavage stimulation factor subunit 3 ;Symplekin;Cleavage and polyadenylation specificity factor subunit 2 ;Cleavage and polyadenylation specificity factor subunit 3","subunits.Gene.name.":"CSTF2;CSTF1;CPSF1;CSTF3;SYMPK;CPSF2;CPSF3","subunits.Gene.name.syn.":";;CPSF160;;SPK;CPSF100 KIAA1367;CPSF73","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Polyadenylation of mRNA precursors is a two-step reaction requiring multiple protein factors. The polyadenylation complex (containing Cstf1, Cstf2, Cstf3, Sympk, Cpsf1, Cpsf2 and Cpsf3), which contains the cleavage stimulation factor (CstF) and subunits of the cleavage and polyadenylation specificity factor (CPSF) might consist of more protein components.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1148,"ComplexName":"snRNP-free U1A (SF-A) complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P09012;P17844;P23246;Q15233","subunits.Entrez.IDs.":"6626;1655;6421;4841","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0031123;GO:0031124;GO:0003723;GO:0005634","GO.description":"RNA 3'-end processing;mRNA 3'-end processing;RNA binding;nucleus","FunCat.ID":"11.04.03.05;16.03.03;70.10","FunCat.description":"3'-end processing;RNA binding;nucleus","PubMed.ID":16373496,"subunits.Protein.name.":"U1 small nuclear ribonucleoprotein A ;Probable ATP-dependent RNA helicase DDX5 ;Splicing factor, proline- and glutamine-rich ;Non-POU domain-containing octamer-binding protein","subunits.Gene.name.":"SNRPA;DDX5;SFPQ;NONO","subunits.Gene.name.syn.":";G17P1 HELR HLR1;PSF;NRB54","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The formation of mRNAs in the nuclei of eukaryotic cells involves several co- and post-transcriptional processing events, including 5' end capping, RNA splicing, and 3' end formation. The SF-A complex was found to be involved in cleavage of the mRNA precursor, an essential step of the 3' end formation process.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1149,"ComplexName":"Histone H3.1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14929;P49321;P62805;P68431;Q09028;Q13111;Q13112;Q8TEX9;Q9NVP2;Q9Y294","subunits.Entrez.IDs.":"8520;4678;None;None;5928;10036;8208;79711;55723;25842","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006461;GO:0005634","GO.description":"protein complex assembly;nucleus","FunCat.ID":"14.10;70.10","FunCat.description":"assembly of protein complexes;nucleus","PubMed.ID":14718166,"subunits.Protein.name.":"Histone acetyltransferase type B catalytic subunit ;Nuclear autoantigenic sperm protein ;Histone H4;Histone H3.1;Histone-binding protein RBBP4;Chromatin assembly factor 1 subunit A ;Chromatin assembly factor 1 subunit B ;Importin-4;Histone chaperone ASF1B ;Histone chaperone ASF1A","subunits.Gene.name.":"HAT1;NASP;HIST1H4A;;HIST1H3A;;RBBP4;CHAF1A;CHAF1B;IPO4;ASF1B;ASF1A","subunits.Gene.name.syn.":"KAT1;;H4/A H4FA; H4/I H4FI; H4/G H4FG; H4/B H4FB; H4/J H4FJ; H4/C H4FC; H4/H H4FH; H4/M H4FM; H4/E H4FE; H;H3FA; H3FL; H3FC; H3FB; H3FD; H3FI; H3FH; H3FK; H3FF; H3FJ;RBAP48;CAF CAF1P150;CAF1A CAF1P60 MPHOSPH7 MPP7;IMP4B, RANBP4;;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The H3.1 and H3.3 complexes contain distinct histone chaperones, CAF-1 and HIRA, that were shown to be necessary to mediate DNA-synthesis-dependent and -independent nucleosome assembly, respectively.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1150,"ComplexName":"Histone H3.3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14929;P49321;P54198;P62805;P84243;Q09028;Q8TEX9;Q9NVP2;Q9Y294","subunits.Entrez.IDs.":"8520;4678;7290;None;None;5928;79711;55723;25842","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006461;GO:0005634","GO.description":"protein complex assembly;nucleus","FunCat.ID":"14.10;70.10","FunCat.description":"assembly of protein complexes;nucleus","PubMed.ID":14718166,"subunits.Protein.name.":"Histone acetyltransferase type B catalytic subunit ;Nuclear autoantigenic sperm protein ;Protein HIRA ;Histone H4;Histone H3.3;Histone-binding protein RBBP4;Importin-4;Histone chaperone ASF1B ;Histone chaperone ASF1A","subunits.Gene.name.":"HAT1;NASP;HIRA;HIST1H4A;;H3F3A; H3F;RBBP4;IPO4;ASF1B;ASF1A","subunits.Gene.name.syn.":"KAT1;;DGCR1 HIR TUPLE1;H4/A H4FA; H4/I H4FI; H4/G H4FG; H4/B H4FB; H4/J H4FJ; H4/C H4FC; H4/H H4FH; H4/M H4FM; H4/E H4FE; H;H3.3A H3F3; H3.3B;RBAP48;IMP4B, RANBP4;;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The H3.1 and H3.3 complexes contain distinct histone chaperones, CAF-1 and HIRA, that were shown to be necessary to mediate DNA-synthesis-dependent and -independent nucleosome assembly, respectively.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1151,"ComplexName":"Sycp1-Syce1-Syce2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q505B8;Q62209;Q9D495","subunits.Entrez.IDs.":"71846;20957;74075","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007126;GO:0005634","GO.description":"meiotic nuclear division;nucleus","FunCat.ID":"10.03.02;70.10","FunCat.description":"meiosis;nucleus","PubMed.ID":15944401,"subunits.Protein.name.":"Synaptonemal complex central element protein 2;Synaptonemal complex protein 1 ;Synaptonemal complex central element protein 1","subunits.Gene.name.":"Syce2;Sycp1;Syce1","subunits.Gene.name.syn.":";Scp1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Completion of meiosis in mammals depends on the formation of the synaptonemal complex, a tripartite structure that physically links homologous chromosomes during prophase I. The function of the Sycp1-Syce1-Syce2 complex is not entirely clear, experiments suggest a role in synaptonemal-complex assembly, and perhaps also stability and recombination.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1152,"ComplexName":"FA complex (Fanconi anemia complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15287;O15360;Q00597;Q8IYD8;Q8NB91;Q9HB96;Q9NPI8;Q9NW38","subunits.Entrez.IDs.":"2189;2175;2176;57697;2187;2178;2188;55120","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0006974;GO:0005634","GO.description":"protein ubiquitination;protein deubiquitination;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"14.07.05;32.01.09;70.10","FunCat.description":"modification by ubiquitination, deubiquitination;DNA damage response;nucleus","PubMed.ID":16116422,"subunits.Protein.name.":"Fanconi anemia group G protein ;Fanconi anemia group A protein ;Fanconi anemia group C protein ;Fanconi anemia group M protein ;Fanconi anemia group B protein ;Fanconi anemia group E protein ;Fanconi anemia group F protein ;E3 ubiquitin-protein ligase FANCL","subunits.Gene.name.":"FANCG;FANCA;FANCC;FANCM;FANCB;FANCE;FANCF;FANCL","subunits.Gene.name.syn.":"XRCC9;FAA FACA FANCH;FAC FACC;KIAA1596;;FACE;;PHF9","Disease.comment":"FA complex is involved in Fanconi anemia (FA) disease.","Subunits.comment":"None","Complex.comment":"The Fanconi complex normally promotes a cascade of changes in a biochemical pathway that ultimately leads to the repair of cellular DNA damage. But if any of the proteins within the complex are mutated, the enzyme FancL is disabled and the DNA repair pathway is disrupted.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1153,"ComplexName":"Integrator complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q5TA45;Q68E01;Q6P9B9;Q75QN2;Q8N201;Q96CB8;Q96HW7;Q9H0H0;Q9NV88;Q9NVH2;Q9NVR2;Q9UL03","subunits.Entrez.IDs.":"54973;65123;80789;55656;26173;57117;92105;57508;55756;25896;55174;26512","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0071- molecular sieving","GO.ID":"GO:0006396;GO:0005634","GO.description":"RNA processing;nucleus","FunCat.ID":"11.04;70.10","FunCat.description":"RNA processing;nucleus","PubMed.ID":16239144,"subunits.Protein.name.":"Integrator complex subunit 11 ;Integrator complex subunit 3 ;Integrator complex subunit 5 ;Integrator complex subunit 8 ;Integrator complex subunit 1 ;Integrator complex subunit 12 ;Integrator complex subunit 4 ;Integrator complex subunit 2 ;Integrator complex subunit 9 ;Integrator complex subunit 7 ;Integrator complex subunit 10 ;Integrator complex subunit 6","subunits.Gene.name.":"CPSF3L;INTS3;INTS5;INTS8;INTS1;INTS12;INTS4;INTS2;INTS9;INTS7;INTS10;INTS6","subunits.Gene.name.syn.":"INTS11 RC68;C1orf193 C1orf60;KIAA1698;C8orf52;KIAA1440;PHF22;;KIAA1287;RC74;C1orf73;C8orf35;DBI1 DDX26 DDX26A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The Intergrator complex is involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3' box-dependent processing. The Integrator complex is recruited to the U1 and U2 snRNA genes and mediates the snRNAs 3' cleavage.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1154,"ComplexName":"DSS1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"A6H687;P51587;P60896;Q5TA45;Q6P9B9;Q75QN2;Q96HW7;Q96PV6;Q9H0H0;Q9NV88;Q9NVH2;Q9NVR2;Q9UL03","subunits.Entrez.IDs.":"66406;675;7979;54973;80789;55656;92105;114823;57508;55756;25896;55174;26512","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0071- molecular sieving","GO.ID":"GO:0005634","GO.description":"nucleus","FunCat.ID":"70.1","FunCat.description":"nucleus","PubMed.ID":16239144,"subunits.Protein.name.":"SAC3 domain-containing protein 1 ;Breast cancer type 2 susceptibility protein ;26S proteasome complex subunit DSS1 ;Integrator complex subunit 11 ;Integrator complex subunit 5 ;Integrator complex subunit 8 ;Integrator complex subunit 4 ;Leukocyte receptor cluster member 8;Integrator complex subunit 2 ;Integrator complex subunit 9 ;Integrator complex subunit 7 ;Integrator complex subunit 10 ;Integrator complex subunit 6","subunits.Gene.name.":"Sac3d1;BRCA2;SHFM1;CPSF3L;INTS5;INTS8;INTS4;LENG8;INTS2;INTS9;INTS7;INTS10;INTS6","subunits.Gene.name.syn.":"Shd1;FACD FANCD1;DSS1 SHFDG1;INTS11 RC68;KIAA1698;C8orf52;;KIAA1932;KIAA1287;RC74;C1orf73;C8orf35;DBI1 DDX26 DDX26A","Disease.comment":"None","Subunits.comment":"Since human SAC3D1 was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1155,"ComplexName":"Integrator-RNAPII complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P24928;P30876;Q5TA45;Q68E01;Q6P9B9;Q75QN2;Q8N201;Q96CB8;Q96HW7;Q9H0H0;Q9NV88;Q9NVH2;Q9NVR2;Q9UL03","subunits.Entrez.IDs.":"5430;5431;54973;65123;80789;55656;26173;57117;92105;57508;55756;25896;55174;26512","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0071- molecular sieving","GO.ID":"GO:0006351;GO:0006396;GO:0005634","GO.description":"transcription, DNA-templated;RNA processing;nucleus","FunCat.ID":"11;11.04;70.10","FunCat.description":"TRANSCRIPTION;RNA processing;nucleus","PubMed.ID":16239144,"subunits.Protein.name.":"DNA-directed RNA polymerase II subunit RPB1;DNA-directed RNA polymerase II subunit RPB2 ;Integrator complex subunit 11 ;Integrator complex subunit 3 ;Integrator complex subunit 5 ;Integrator complex subunit 8 ;Integrator complex subunit 1 ;Integrator complex subunit 12 ;Integrator complex subunit 4 ;Integrator complex subunit 2 ;Integrator complex subunit 9 ;Integrator complex subunit 7 ;Integrator complex subunit 10 ;Integrator complex subunit 6","subunits.Gene.name.":"POLR2A;POLR2B;CPSF3L;INTS3;INTS5;INTS8;INTS1;INTS12;INTS4;INTS2;INTS9;INTS7;INTS10;INTS6","subunits.Gene.name.syn.":"POLR2;;INTS11 RC68;C1orf193 C1orf60;KIAA1698;C8orf52;KIAA1440;PHF22;;KIAA1287;RC74;C1orf73;C8orf35;DBI1 DDX26 DDX26A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The integrator complex interacts with the C-terminal domain of the RNA Polymerase II. The integrator-RNAPII complex mediates RNAPII-dependent transcription of at least U1 and U2 snRNA genes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1156,"ComplexName":"PS1-E-cadherin-catenin complex, epithelial","Organism":"Dog","Synonyms":"None","Cell.line":"MDCK cells, epithelium","subunits.UniProt.IDs.":"P09803;P26231;P49769;Q02248","subunits.Entrez.IDs.":"12550;12385;19164;12387","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation;MI:0029- cosedimentation through density gradients","GO.ID":"GO:0016337;GO:0045216;GO:0007043;GO:0005911","GO.description":"single organismal cell-cell adhesion;cell-cell junction organization;cell-cell junction assembly;cell-cell junction","FunCat.ID":"34.07.01;42.06.04;70.06.04","FunCat.description":"cell-cell adhesion;intercellular junction (gap junction/adherens junction);intercellular junction (gap junction/adherens junction)","PubMed.ID":10635315,"subunits.Protein.name.":"Cadherin-1 ;Catenin alpha-1 ;Presenilin-1 ;Catenin beta-1","subunits.Gene.name.":"Cdh1;Ctnna1;Psen1;Ctnnb1","subunits.Gene.name.syn.":";Catna1;Ad3h Psnl1;Catnb","Disease.comment":"None","Subunits.comment":"Since several proteins from dog were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.","Complex.comment":"Disruption of Ca(2+)-dependent cell-cell contacts reduces surface PS1 and the levels of PS1-E-cadherin complexes. PS1 concentrates at intercellular contacts in epithelial tissue; in brain it forms complexes with both E- and N-cadherin and concentrates at synaptic adhesions.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1157,"ComplexName":"PS1-E-cadherin-catenin complex, brain","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P09803;P15116;P49769;Q02248","subunits.Entrez.IDs.":"12550;12558;19164;12387","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0005509;GO:0016337;GO:0045216;GO:0007043;GO:0005911","GO.description":"calcium ion binding;single organismal cell-cell adhesion;cell-cell junction organization;cell-cell junction assembly;cell-cell junction","FunCat.ID":"16.17.01;34.07.01;42.06.04;70.06.04","FunCat.description":"calcium binding;cell-cell adhesion;intercellular junction (gap junction/adherens junction);intercellular junction (gap junction/adherens junction)","PubMed.ID":10635315,"subunits.Protein.name.":"Cadherin-1 ;Cadherin-2;Presenilin-1 ;Catenin beta-1","subunits.Gene.name.":"Cdh1;Cdh2;Psen1;Ctnnb1","subunits.Gene.name.syn.":";None;Ad3h Psnl1;Catnb","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"PS1 concentrates at intercellular contacts in epithelial tissue; in brain it forms complexes with both E- and N-cadherin and concentrates at synaptic adhesions.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1158,"ComplexName":"p33ING1b-p300 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q09472;Q9UK53","subunits.Entrez.IDs.":"2033;3621","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006265;GO:0000278;GO:0051726;GO:0006473;GO:0006476;GO:0051276;GO:0005694","GO.description":"DNA topological change;mitotic cell cycle;regulation of cell cycle;protein acetylation;protein deacetylation;chromosome organization;chromosome","FunCat.ID":"10.01.09.05;10.03.01.01;10.03.01;14.07.04;42.10.03;70.10.03","FunCat.description":"DNA conformation modification (e.g. chromatin);mitotic cell cycle;mitotic cell cycle and cell cycle control;modification by acetylation, deacetylation;organization of chromosome structure;chromosome","PubMed.ID":12015309,"subunits.Protein.name.":"Histone acetyltransferase p300;Inhibitor of growth protein 1","subunits.Gene.name.":"EP300;ING1","subunits.Gene.name.syn.":"P300;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Anti-p300 immunoprecipitates contained p33ING1b, but not p47ING1a.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1159,"ComplexName":"p33ING1b-HDAC1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q13547;Q9UK53","subunits.Entrez.IDs.":"3065;3621","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006265;GO:0000278;GO:0051726;GO:0006473;GO:0006476;GO:0051276;GO:0005694","GO.description":"DNA topological change;mitotic cell cycle;regulation of cell cycle;protein acetylation;protein deacetylation;chromosome organization;chromosome","FunCat.ID":"10.01.09.05;10.03.01.01;10.03.01;14.07.04;42.10.03;70.10.03","FunCat.description":"DNA conformation modification (e.g. chromatin);mitotic cell cycle;mitotic cell cycle and cell cycle control;modification by acetylation, deacetylation;organization of chromosome structure;chromosome","PubMed.ID":12015309,"subunits.Protein.name.":"Histone deacetylase 1;Inhibitor of growth protein 1","subunits.Gene.name.":"HDAC1;ING1","subunits.Gene.name.syn.":"RPD3L1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"HDAC1 interacts as well with p33ING1b as with p47ING1a.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1160,"ComplexName":"ING1-p300-PCNA complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12004;Q09472;Q9UK53","subunits.Entrez.IDs.":"5111;2033;3621","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0006265;GO:0000278;GO:0051726;GO:0006473;GO:0006476;GO:0051276;GO:0005694","GO.description":"DNA repair;DNA topological change;mitotic cell cycle;regulation of cell cycle;protein acetylation;protein deacetylation;chromosome organization;chromosome","FunCat.ID":"10.01.05.01;10.01.09.05;10.03.01.01;10.03.01;14.07.04;42.10.03;70.10.03","FunCat.description":"DNA repair;DNA conformation modification (e.g. chromatin);mitotic cell cycle;mitotic cell cycle and cell cycle control;modification by acetylation, deacetylation;organization of chromosome structure;chromosome","PubMed.ID":12015309,"subunits.Protein.name.":"Proliferating cell nuclear antigen;Histone acetyltransferase p300;Inhibitor of growth protein 1","subunits.Gene.name.":"PCNA;EP300;ING1","subunits.Gene.name.syn.":"None;P300;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"p33ING1b affects the degree of physical association between proliferating cell nuclear antigen (PCNA) and p300.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1161,"ComplexName":"Smrt-Sin3A-Hdac7 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q60520;Q8C2B3;Q9WU42","subunits.Entrez.IDs.":"20466;56233;20602","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;DNA binding;organization of chromosome structure;nucleus","PubMed.ID":10640276,"subunits.Protein.name.":"Paired amphipathic helix protein Sin3a;Histone deacetylase 7 ;Nuclear receptor corepressor 2","subunits.Gene.name.":"Sin3a;Hdac7;Ncor2","subunits.Gene.name.syn.":"Kiaa4126;Hdac7a;Smrt","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1162,"ComplexName":"Ubiquitin E3 ligase (DDB1, DDB2, CUL4A, CUL4B, RBX1)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62877;Q13619;Q13620;Q16531;Q92466","subunits.Entrez.IDs.":"9978;8451;8450;1642;1643","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0226- ion exchange chromatography","GO.ID":"GO:0016567;GO:0016579;GO:0006464;GO:0006974;GO:0009314;GO:0005634","GO.description":"protein ubiquitination;protein deubiquitination;cellular protein modification process;cellular response to DNA damage stimulus;response to radiation;nucleus","FunCat.ID":"14.07.05;14.07;32.01.09;32.01.13;70.10","FunCat.description":"modification by ubiquitination, deubiquitination;protein modification;DNA damage response;electromagnetic waves stress response (e.g. UV, X-ray);nucleus","PubMed.ID":16678110,"subunits.Protein.name.":"E3 ubiquitin-protein ligase RBX1;Cullin-4A;Cullin-4B;DNA damage-binding protein 1;DNA damage-binding protein 2","subunits.Gene.name.":"RBX1;CUL4A;CUL4B;DDB1;DDB2","subunits.Gene.name.syn.":"RNF75, ROC1;None;KIAA0695;XAP1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. The CUL4-DDB-ROC1 complex is a ubiquitin E3 ligase for histones H3 and H4. CUL4-DDB-ROC1-mediated H3 and H4 ubiquitylation was shown to facilitate cellular response to UV damage by affecting nucleosome stability.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1163,"ComplexName":"ING1-PCNA complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12004;Q9UK53","subunits.Entrez.IDs.":"5111;3621","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006974;GO:0009314;GO:0008219;GO:0005694","GO.description":"cellular response to DNA damage stimulus;response to radiation;cell death;chromosome","FunCat.ID":"32.01.09;32.01.13;40.10;70.10.03","FunCat.description":"DNA damage response;electromagnetic waves stress response (e.g. UV, X-ray);cell death;chromosome","PubMed.ID":11682605,"subunits.Protein.name.":"Proliferating cell nuclear antigen;Inhibitor of growth protein 1","subunits.Gene.name.":"PCNA;ING1","subunits.Gene.name.syn.":"None;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"UV rapidly induces p33ING1b, but not p47ING1a isoform, to bind PCNA.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1164,"ComplexName":"ActRIIA-ActRIB-Smad3-Arip1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"Hippocampal primary neurons","subunits.UniProt.IDs.":"P27038;Q61271;Q8BUN5;Q9WVQ1","subunits.Entrez.IDs.":"11480;11479;17127;50791","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0007178;GO:0032924","GO.description":"transmembrane receptor protein serine/threonine kinase signaling pathway;activin receptor signaling pathway","FunCat.ID":"30.05.01.18","FunCat.description":"transmembrane receptor protein serine/threonine kinase signalling pathways","PubMed.ID":10681527,"subunits.Protein.name.":"Activin receptor type-2A ;Activin receptor type-1B ;Mothers against decapentaplegic homolog 3;Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2","subunits.Gene.name.":"Acvr2a;Acvr1b;Smad3;Magi2","subunits.Gene.name.syn.":"Acvr2;Alk4;Madh3;Acvrinp1 Aip1 Arip1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"When COS-7 cells cotransfected with ActRIIA, ActRIB(K234R), 6Myc-ARIP1, and FLAG-Smad3 were incubated in the presence of (125)I-activin A, the (125)I-labeled receptor complex could be precipitated by either of the anti-Myc and anti-FLAG antibodies. Therefore, ARIP1 is capable of forming a complex with ActRIIA, ActRIB, and Smad3 in the presence of ligand.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1165,"ComplexName":"RNF20-RNF40-UbE2E1 complex","Organism":"Human","Synonyms":"RNF20/40 complex","Cell.line":"None","subunits.UniProt.IDs.":"O75150;P51965;Q5VTR2","subunits.Entrez.IDs.":"9810;7324;56254","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:2001141;GO:0006355;GO:0016567;GO:0016579;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein ubiquitination;protein deubiquitination;nucleus","FunCat.ID":"11.02.03.04;14.07.05;70.10","FunCat.description":"transcriptional control;modification by ubiquitination, deubiquitination;nucleus","PubMed.ID":16307923,"subunits.Protein.name.":"E3 ubiquitin-protein ligase BRE1B ;Ubiquitin-conjugating enzyme E2 E1 ;E3 ubiquitin-protein ligase BRE1A","subunits.Gene.name.":"RNF40;UBE2E1;RNF20","subunits.Gene.name.syn.":"BRE1B KIAA0661;UBCH6;BRE1A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In humans, the 600 kDa RNF20/40 complex is the E3 ligase and UbcH6 is the ubiquitin E2-conjugating enzyme for H2B-Lys120 monoubiquitination.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1166,"ComplexName":"p400-associated complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O96019;P60709;Q96L91;Q9Y230;Q9Y265;Q9Y4A5","subunits.Entrez.IDs.":"86;60;57634;10856;8607;8295","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0051276;GO:0006265;GO:0005515;GO:0005634","GO.description":"chromosome organization;DNA topological change;protein binding;nucleus","FunCat.ID":"42.10.03;10.01.09.05;16.01;70.10","FunCat.description":"organization of chromosome structure;DNA conformation modification (e.g. chromatin);protein binding;nucleus","PubMed.ID":11509179,"subunits.Protein.name.":"Actin-like protein 6A;Actin, cytoplasmic 1;E1A-binding protein p400;RuvB-like 2;RuvB-like 1;Transformation/transcription domain-associated protein","subunits.Gene.name.":"ACTL6A;ACTB;EP400;RUVBL2;RUVBL1;TRRAP","subunits.Gene.name.syn.":"BAF53 BAF53A INO80K;None;CAGH32 KIAA1498 KIAA1818 TNRC12;INO80J TIP48 TIP49B;INO80H NMP238 TIP49 TIP49A;PAF400","Disease.comment":"None","Subunits.comment":"Since the authors did not specify ACTL6, we used ACTL6A.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1167,"ComplexName":"Paf complex","Organism":"Human","Synonyms":"hPAF complex","Cell.line":"None","subunits.UniProt.IDs.":"Q6P1J9;Q6PD62;Q8N7H5;Q8WVC0;Q9GZS3","subunits.Entrez.IDs.":"79577;9646;54623;123169;80349","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006351;GO:0005634","GO.description":"transcription, DNA-templated;nucleus","FunCat.ID":"11;70.10","FunCat.description":"TRANSCRIPTION;nucleus","PubMed.ID":16307923,"subunits.Protein.name.":"Parafibromin ;RNA polymerase-associated protein CTR9 homolog ;RNA polymerase II-associated factor 1 homolog ;RNA polymerase-associated protein LEO1 ;WD repeat-containing protein 61","subunits.Gene.name.":"CDC73;CTR9;PAF1;LEO1;WDR61","subunits.Gene.name.syn.":"C1orf28 HRPT2;KIAA0155 SH2BP1;PD2;RDL;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"hPAF participates in histone H2B monoubiquitiation. In addition, hPAF coordinates events during transcription (initiation, promoter clearance, and elongation) and also events in RNA quality control. The hPAF complex interacts with the hSKI complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1168,"ComplexName":"SKI complex","Organism":"Human","Synonyms":"hSKI complex","Cell.line":"None","subunits.UniProt.IDs.":"Q15477;Q6PGP7;Q9GZS3","subunits.Entrez.IDs.":"6499;9652;80349","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0019- coimmunoprecipitation","GO.ID":"GO:0006351;GO:2001141;GO:0006355;GO:0005737;GO:0005634","GO.description":"transcription, DNA-templated;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;cytoplasm;nucleus","FunCat.ID":"11;11.02.03.04;70.03;70.10","FunCat.description":"TRANSCRIPTION;transcriptional control;cytoplasm;nucleus","PubMed.ID":16024656,"subunits.Protein.name.":"Helicase SKI2W ;Tetratricopeptide repeat protein 37 ;WD repeat-containing protein 61","subunits.Gene.name.":"SKIV2L;TTC37;WDR61","subunits.Gene.name.syn.":"DDX13 SKI2W SKIV2 W;KIAA0372;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"hSKI complex is present at transcriptionally active genes with recruitment dependent on hPAF complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1169,"ComplexName":"SNARE complex (STX4, VAMP8, VAMP3, SNAP23)","Organism":"Human","Synonyms":"None","Cell.line":"platelet","subunits.UniProt.IDs.":"O00161;Q12846;Q15836;Q9BV40","subunits.Entrez.IDs.":"8773;6810;9341;8673","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":12130530,"subunits.Protein.name.":"Synaptosomal-associated protein 23;Syntaxin-4;Vesicle-associated membrane protein 3;Vesicle-associated membrane protein 8","subunits.Gene.name.":"SNAP23;STX4;VAMP3;VAMP8","subunits.Gene.name.syn.":"None;STX4A;SYB3;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.VAMP-3 and VAMP-8 form SNARE complexes with platelet syntaxin 4 and are required for platelet granule secretion.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1170,"ComplexName":"cMYC-ATPase-helicase complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O96019;P01106;Q9Y230;Q9Y265;Q9Y4A5","subunits.Entrez.IDs.":"86;4609;10856;8607;8295","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0051276;GO:0006265;GO:2001141;GO:0006355;GO:0006473;GO:0006476;GO:0003677;GO:0051276;GO:0005634","GO.description":"chromosome organization;DNA topological change;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;DNA binding;chromosome organization;nucleus","FunCat.ID":"42.10.03;10.01.09.05;11.02.03.04;14.07.04;16.03.01;70.10","FunCat.description":"organization of chromosome structure;DNA conformation modification (e.g. chromatin);transcriptional control;modification by acetylation, deacetylation;DNA binding;nucleus","PubMed.ID":10882073,"subunits.Protein.name.":"Actin-like protein 6A;Myc proto-oncogene protein ;RuvB-like 2;RuvB-like 1;Transformation/transcription domain-associated protein","subunits.Gene.name.":"ACTL6A;MYC;RUVBL2;RUVBL1;TRRAP","subunits.Gene.name.syn.":"BAF53 BAF53A INO80K;BHLHE39;INO80J TIP48 TIP49B;INO80H NMP238 TIP49 TIP49A;PAF400","Disease.comment":"None","Subunits.comment":"BAF53 and beta-actin have been described in this paper as p45 and p41. Both subunits were identified in the succeeding paper PMID:11839798.","Complex.comment":"TIP49 and TIP48 are complexed with c-Myc in vivo, and binding is dependent on a c-Myc domain essential for oncogenic activity. TIP49 protein is an essential mediator of c-Myc oncogenic transformation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1171,"ComplexName":"c-MYC-ATPase-helicase complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O96019;P01106;Q9Y230;Q9Y265;Q9Y4A5","subunits.Entrez.IDs.":"86;4609;10856;8607;8295","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0051276;GO:0006265;GO:2001141;GO:0006355;GO:0006473;GO:0006476;GO:0003677;GO:0051276;GO:0005634","GO.description":"chromosome organization;DNA topological change;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;DNA binding;chromosome organization;nucleus","FunCat.ID":"42.10.03;10.01.09.05;11.02.03.04;14.07.04;16.03.01;70.10","FunCat.description":"organization of chromosome structure;DNA conformation modification (e.g. chromatin);transcriptional control;modification by acetylation, deacetylation;DNA binding;nucleus","PubMed.ID":11839798,"subunits.Protein.name.":"Actin-like protein 6A;Myc proto-oncogene protein ;RuvB-like 2;RuvB-like 1;Transformation/transcription domain-associated protein","subunits.Gene.name.":"ACTL6A;MYC;RUVBL2;RUVBL1;TRRAP","subunits.Gene.name.syn.":"BAF53 BAF53A INO80K;BHLHE39;INO80J TIP48 TIP49B;INO80H NMP238 TIP49 TIP49A;PAF400","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1172,"ComplexName":"CBC complex (cap binding complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P52298;Q09161","subunits.Entrez.IDs.":"22916;4686","Protein.complex.purification.method":"MI:0413- electrophoretic mobility shift assay","GO.ID":"GO:0003723;GO:0050658;GO:0051033;GO:0051169;GO:0005634","GO.description":"RNA binding;RNA transport;RNA transmembrane transporter activity;nuclear transport;nucleus","FunCat.ID":"16.03.03;20.01.21;20.09.01;70.10","FunCat.description":"RNA binding;RNA transport;nuclear transport;nucleus","PubMed.ID":10786834,"subunits.Protein.name.":"Nuclear cap-binding protein subunit 2;Nuclear cap-binding protein subunit 1","subunits.Gene.name.":"NCBP2;NCBP1","subunits.Gene.name.syn.":"CBP20;CBP80 NCBP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The heterodimeric nuclear cap binding complex (CBC) binds to 5'-capped polymerase II transcripts. It enhances the efficiency of several mRNA maturation steps and is essential for U snRNA nuclear export in multicellular eukaryotes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1173,"ComplexName":"TIP49-TIP48-BAF53 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O96019;Q9Y230;Q9Y265","subunits.Entrez.IDs.":"86;10856;8607","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0051276;GO:0005634","GO.description":"chromosome organization;nucleus","FunCat.ID":"42.10.03;70.10","FunCat.description":"organization of chromosome structure;nucleus","PubMed.ID":11839798,"subunits.Protein.name.":"Actin-like protein 6A;RuvB-like 2;RuvB-like 1","subunits.Gene.name.":"ACTL6A;RUVBL2;RUVBL1","subunits.Gene.name.syn.":"BAF53 BAF53A INO80K;INO80J TIP48 TIP49B;INO80H NMP238 TIP49 TIP49A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1174,"ComplexName":"PHAX-CBC complex (cap binding complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P52298;Q09161;Q9H814","subunits.Entrez.IDs.":"22916;4686;51808","Protein.complex.purification.method":"MI:0413- electrophoretic mobility shift assay","GO.ID":"GO:0003723;GO:0050658;GO:0051033;GO:0051169;GO:0005737;GO:0005634","GO.description":"RNA binding;RNA transport;RNA transmembrane transporter activity;nuclear transport;cytoplasm;nucleus","FunCat.ID":"16.03.03;20.01.21;20.09.01;70.03;70.10","FunCat.description":"RNA binding;RNA transport;nuclear transport;cytoplasm;nucleus","PubMed.ID":10786834,"subunits.Protein.name.":"Nuclear cap-binding protein subunit 2;Nuclear cap-binding protein subunit 1;Phosphorylated adapter RNA export protein","subunits.Gene.name.":"NCBP2;NCBP1;PHAX","subunits.Gene.name.syn.":"CBP20;CBP80 NCBP;RNUXA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In metazoa, assembly of spliceosomal U snRNPs requires nuclear export of U snRNA precursors. Export depends upon the RNA cap structure, nuclear cap-binding complex (CBC), the export receptor CRM1/Xpo1, and RanGTP. PHAX (phosphorylated adaptor for RNA export) is an additional factor required for U snRNA export complex assembly in vitro. In vivo, PHAX is required for U snRNA export but not for CRM1-mediated export in general. PHAX is phosphorylated in the nucleus and then exported with RNA to the cytoplasm, where it is dephosphorylated. PHAX phosphorylation is essential for export complex assembly while its dephosphorylation causes export complex disassembly. The compartmentalized PHAX phosphorylation cycle can contribute to the directionality of export. PHAX binding to CBC is greatly increased by the presence of capped RNA.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1175,"ComplexName":"TRRAP-BAF53-HAT complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O96019;Q9Y4A5","subunits.Entrez.IDs.":"86;8295","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:2001141;GO:0006355;GO:0006473;GO:0006476;GO:0051276;GO:0005634","GO.description":"DNA topological change;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04;14.07.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcriptional control;modification by acetylation, deacetylation;organization of chromosome structure;nucleus","PubMed.ID":11839798,"subunits.Protein.name.":"Actin-like protein 6A;Transformation/transcription domain-associated protein","subunits.Gene.name.":"ACTL6A;TRRAP","subunits.Gene.name.syn.":"BAF53 BAF53A INO80K;PAF400","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TRRAP and BAF53 associate with an up to now not identified histone acetyltransferase activity which does not contain TIP60, TIP49 or TIP48.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1176,"ComplexName":"CRM1-RAN-PHAX-CBC complex (cap binding complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14980;P52298;P62826;Q09161;Q9H814","subunits.Entrez.IDs.":"7514;22916;5901;4686;51808","Protein.complex.purification.method":"MI:0413- electrophoretic mobility shift assay; MI:0430- nucleic acid uv cross-linking assay","GO.ID":"GO:0003723;GO:0050658;GO:0051033;GO:0051169;GO:0005737;GO:0005634","GO.description":"RNA binding;RNA transport;RNA transmembrane transporter activity;nuclear transport;cytoplasm;nucleus","FunCat.ID":"16.03.03;20.01.21;20.09.01;70.03;70.10","FunCat.description":"RNA binding;RNA transport;nuclear transport;cytoplasm;nucleus","PubMed.ID":10786834,"subunits.Protein.name.":"Exportin-1 ;Nuclear cap-binding protein subunit 2;GTP-binding nuclear protein Ran;Nuclear cap-binding protein subunit 1;Phosphorylated adapter RNA export protein","subunits.Gene.name.":"XPO1;NCBP2;RAN;NCBP1;PHAX","subunits.Gene.name.syn.":"CRM1;CBP20;ARA24;CBP80 NCBP;RNUXA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In metazoa, assembly of spliceosomal U snRNPs requires nuclear export of U snRNA precursors. Export depends upon the RNA cap structure, nuclear cap-binding complex (CBC), the export receptor CRM1/Xpo1, and RanGTP. PHAX (phosphorylated adaptor for RNA export) is an additional factor required for U snRNA export complex assembly in vitro. PHAX binding to CBC is greatly increased by the presence of capped RNA. Phosphorylated PHAX can bind to RanGTP/Xpo1 but does so more strongly in the presence of CBC and even more in the presence of both CBC and RNA. Thus, every step in U snRNA export complex formation involves some degree of cooperativity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1177,"ComplexName":"Polycomb repressive complex 4 (PRC4)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75530;Q15910;Q96EB6","subunits.Entrez.IDs.":"8726;2146;23411","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0226- ion exchange chromatography","GO.ID":"GO:0006265;GO:0032774;GO:0018126;GO:0006479;GO:0051276;GO:0005634","GO.description":"DNA topological change;RNA biosynthetic process;protein hydroxylation;protein methylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02;14.07.09;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);RNA synthesis;posttranslational modification of amino acids (e.g. hydroxylation, methylation);organization of chromosome structure;nucleus","PubMed.ID":15684044,"subunits.Protein.name.":"Polycomb protein EED;Histone-lysine N-methyltransferase EZH2;NAD-dependent protein deacetylase sirtuin-1","subunits.Gene.name.":"EED;EZH2;SIRT1","subunits.Gene.name.syn.":"None;KMT6;SIR2L1","Disease.comment":"PRC complexes are overexpressed in breast, colon, and prostate cancers.","Subunits.comment":"None","Complex.comment":"Polycomb repressive complexes are required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. They are methylating histones at lysine residues. PRC4 methylates preferentially the histone H1b isoform, whereas PRC2 methylated preferentially the histone H1d isoform. The PRC3 complex exclusively targets methylation of histone H3-K27, and the activity is repressed in the presence of histone H1. PRC2 also methylates histone H3-K27 but in the presence of histone H1, PRC2 methylates both H3-K27 and H1-K26.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1178,"ComplexName":"BCOR complex","Organism":"Human","Synonyms":"Ubiquitin E3 ligase","Cell.line":"None","subunits.UniProt.IDs.":"P11142;P63208;Q06587;Q6W2J9;Q8N488;Q8NHM5;Q99496;Q9BSM1","subunits.Entrez.IDs.":"3312;6500;6015;54880;23429;84678;6045;84759","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0006464;GO:0051090;GO:0005634","GO.description":"protein ubiquitination;protein deubiquitination;cellular protein modification process;regulation of sequence-specific DNA binding transcription factor activity;nucleus","FunCat.ID":"14.07.05;14.07;18.02.09;70.10","FunCat.description":"modification by ubiquitination, deubiquitination;protein modification;regulator of transcription factor;nucleus","PubMed.ID":16943429,"subunits.Protein.name.":"Heat shock cognate 71 kDa protein;S-phase kinase-associated protein 1;E3 ubiquitin-protein ligase RING1;BCL-6 corepressor ;RING1 and YY1-binding protein ;Lysine-specific demethylase 2B ;E3 ubiquitin-protein ligase RING2;Polycomb group RING finger protein 1","subunits.Gene.name.":"HSPA8;SKP1;RING1;BCOR;RYBP;KDM2B;RNF2;PCGF1","subunits.Gene.name.syn.":"HSC70, HSP73, HSPA10;EMC19, OCP2, SKP1A, TCEB1L;RNF1;KIAA1575;DEDAF YEAF1;CXXC2 FBL10 FBXL10 JHDM1B PCCX2;BAP1 DING HIPI3 RING1B;NSPC1 RNF68","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. The BCOR complex contains E3 ligase activity for histone H2A. Monoubiquitylated H2A is present together with the BCOR complex at BCL6 target genes in B cells. This strongly suggests a role of BCOR as regulator of BCL6, a sequence-specific transcriptional repressor, that probably plays an important role in lymphomagenesis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1179,"ComplexName":"CENP-A NAC-CAD complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q03188;Q13352;Q6IPU0;Q71F23;Q7L2Z9;Q8N0S6;Q8N2Z9;Q96BT3;Q96H22;Q9BS16;Q9BU64;Q9H3R5;Q9NSP4","subunits.Entrez.IDs.":"1060;23421;401541;79682;55166;91687;None;80152;55839;64105;79172;64946;79019","Protein.complex.purification.method":"MI:0676- tandem affinity purification","GO.ID":"GO:0006349;GO:0051382;GO:0007059;GO:0051225;GO:0007098;GO:0000775","GO.description":"regulation of gene expression by genetic imprinting;kinetochore assembly;chromosome segregation;spindle assembly;centrosome cycle;chromosome, centromeric region","FunCat.ID":"10.01.09.07;10.03.04.01;10.03.04.05;10.03.05.01;70.10.04","FunCat.description":"DNA imprinting and other epigenetic effects;centromere/kinetochore complex maturation;chromosome segregation/division;spindle pole body/centrosome and microtubule cycle;centromere / kinetochore","PubMed.ID":16622419,"subunits.Protein.name.":"Centromere protein C ;Centromere protein R ;Centromere protein P ;Centromere protein U ;Centromere protein Q ;Centromere protein L ;Centromere protein S;Centromere protein T;Centromere protein N ;Centromere protein K ;Centromere protein O ;Centromere protein H ;Centromere protein M","subunits.Gene.name.":"CENPC;ITGB3BP;CENPP;CENPU;CENPQ;CENPL;APITD1;CENPT;CENPN;CENPK;CENPO;CENPH;CENPM","subunits.Gene.name.syn.":"CENPC1 ICEN7;CENPR NRIF3;;ICEN24 KLIP1 MLF1IP PBIP1;C6orf139;C1orf155 ICEN33;CENPS, FAAP16, MHF1;C16orf56, ICEN22;C16orf60 ICEN32;ICEN37;ICEN36 MCM21R;ICEN35;C22orf18 ICEN39 PANE1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Assembly of CENP-A NAC complex at centromeres is dependent on CENP-M, CENP-N and CENP-T.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1180,"ComplexName":"Sur2 subcomplex of mediator","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q6PGF3;Q80YQ2;Q99K74","subunits.Entrez.IDs.":"216154;70208;23989","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0045893;GO:0051098;GO:0005515;GO:0051090;GO:0000165;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;regulation of binding;protein binding;regulation of sequence-specific DNA binding transcription factor activity;MAPK cascade;nucleus","FunCat.ID":"11.02.03.04.01;18.01.07;16.01;18.02.09;30.01.05.01.03;70.10","FunCat.description":"transcription activation;regulation by binding / dissociation;protein binding;regulator of transcription factor;MAPKKK cascade;nucleus","PubMed.ID":11934987,"subunits.Protein.name.":"Mediator of RNA polymerase II transcription subunit 16;Mediator of RNA polymerase II transcription subunit 23;Mediator of RNA polymerase II transcription subunit 24","subunits.Gene.name.":"Med16;Med23;Med24","subunits.Gene.name.syn.":"Thrap5;Crsp3 Kiaa1216 Sur2;D11Ertd307e Thrap4 Trap100","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Regulation of transcription by RNA polymerase II (Pol II) is controlled by specific combinations of sequence-specific, DNA binding regulatory transcription factors (TFs) bound to a gene's promoter and enhancer regions. These TFs interact with several multiprotein complexes that remodel the chromatin context of the promoter, integrate signals from multiple TFs to control the frequency of transcription initiation, and regulate the efficiency of transcription elongation. One such complex is the Mediator, an ~2-megadalton complex of 20 to 30 subunits that is believed to function as a molecular bridge by simultaneously interacting with both DNA-bound TFs and Pol II. In the absence of Sur2 murine Med100 and Med95 were reduced. The results suggest that the mammalian Mediator contains a Sur2 subcomplex that includes Sur2, Med100, and Med95. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1181,"ComplexName":"C complex spliceosome","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43290;O43390;O43660;O60306;O60506;O60508;O75533;O75643;O94906;O95391;O95926;P07910;P08579;P09651;P09661;P11940;P14678;P17844;P22626;P31943;P38159;P38919;P42285;P51991;P52272;P52597;P61326;P61978;P62304;P62306;P62308;P62310;P62314;P62316;P62318;Q00839;Q01081;Q07955;Q12874;Q13435;Q13523;Q13573;Q14331;Q14562;Q15029;Q15393;Q15428;Q15459;Q6NZY4;Q6P2Q9;Q6UX04;Q86V81;Q8IYB3;Q8WUQ7;Q92620;Q96BP3;Q96DF8;Q96DI7;Q99459;Q9BRR8;Q9BRX9;Q9BUQ8;Q9BZJ0;Q9H2H8;Q9H307;Q9H5Z1;Q9HCG8;Q9HCS7;Q9NW64;Q9P013;Q9UBB9;Q9UJV9;Q9UKM9;Q9ULR0;Q9UMS4;Q9UNP9;Q9UQ35;Q9Y333;Q9Y3C6;Q9Y5S9","subunits.Entrez.IDs.":"9092;10236;5356;9716;10492;51362;23451;23020;24148;10569;25949;3183;6629;3178;6627;26986;6628;1655;3181;3187;27316;9775;23517;220988;4670;3185;4116;3190;6635;6636;6637;27258;6632;6633;6634;3192;7307;6426;10946;10992;8899;22938;2483;1659;9343;23450;8175;10291;55596;10594;10283;10189;10250;58509;9785;23398;8220;9410;988;55094;84292;9416;51340;53938;5411;60625;57703;56949;55696;51503;None;51428;22913;57461;27339;10450;23524;57819;51645;9939","Protein.complex.purification.method":"MI:0028- cosedimentation in solution; MI:0096- pull down","GO.ID":"GO:0008380;GO:0003723;GO:0005634","GO.description":"RNA splicing;RNA binding;nucleus","FunCat.ID":"11.04.03.01;16.03.03;70.10","FunCat.description":"splicing;RNA binding;nucleus","PubMed.ID":11991638,"subunits.Protein.name.":"U4/U6.U5 tri-snRNP-associated protein 1 ;Heterogeneous nuclear ribonucleoprotein R ;Pleiotropic regulator 1;Intron-binding protein aquarius ;Heterogeneous nuclear ribonucleoprotein Q;Pre-mRNA-processing factor 17 ;Splicing factor 3B subunit 1 ;U5 small nuclear ribonucleoprotein 200 kDa helicase ;Pre-mRNA-processing factor 6 ;Pre-mRNA-splicing factor SLU7 ;Pre-mRNA-splicing factor SYF2 ;Heterogeneous nuclear ribonucleoproteins C1/C2 ;U2 small nuclear ribonucleoprotein B'' ;Heterogeneous nuclear ribonucleoprotein A1 ;U2 small nuclear ribonucleoprotein A' ;Polyadenylate-binding protein 1;Small nuclear ribonucleoprotein-associated proteins B and B' ;Probable ATP-dependent RNA helicase DDX5 ;Heterogeneous nuclear ribonucleoproteins A2/B1 ;Heterogeneous nuclear ribonucleoprotein H ;RNA-binding motif protein, X chromosome ;Eukaryotic initiation factor 4A-III;Superkiller viralicidic activity 2-like 2 ;Heterogeneous nuclear ribonucleoprotein A3 ;Heterogeneous nuclear ribonucleoprotein M ;Heterogeneous nuclear ribonucleoprotein F ;Protein mago nashi homolog;Heterogeneous nuclear ribonucleoprotein K ;Small nuclear ribonucleoprotein E ;Small nuclear ribonucleoprotein F ;Small nuclear ribonucleoprotein G ;U6 snRNA-associated Sm-like protein LSm3;Small nuclear ribonucleoprotein Sm D1 ;Small nuclear ribonucleoprotein Sm D2 ;Small nuclear ribonucleoprotein Sm D3 ;Heterogeneous nuclear ribonucleoprotein U ;Splicing factor U2AF 35 kDa subunit ;Serine/arginine-rich splicing factor 1 ;Splicing factor 3A subunit 3 ;Splicing factor 3B subunit 2 ;Serine/threonine-protein kinase PRP4 homolog ;SNW domain-containing protein 1 ;Protein FRG1 ;ATP-dependent RNA helicase DHX8 ;116 kDa U5 small nuclear ribonucleoprotein component ;Splicing factor 3B subunit 3;Splicing factor 3A subunit 2 ;Splicing factor 3A subunit 1 ;Zinc finger CCHC domain-containing protein 8 ;Pre-mRNA-processing-splicing factor 8 ;Peptidyl-prolyl cis-trans isomerase CWC27 homolog ;THO complex subunit 4 ;Serine/arginine repetitive matrix protein 1 ;Cactin ;Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16 ;Peptidylprolyl isomerase domain and WD repeat-containing protein 1 ;Protein DGCR14 ;U5 small nuclear ribonucleoprotein 40 kDa protein;Cell division cycle 5-like protein ;G patch domain-containing protein 1 ;WD repeat domain-containing protein 83 ;Probable ATP-dependent RNA helicase DDX23 ;Crooked neck-like protein 1 ;Peptidyl-prolyl cis-trans isomerase-like 3 ;Pinin ;Probable ATP-dependent RNA helicase DHX35 ;Pre-mRNA-splicing factor CWC22 homolog ;Pre-mRNA-splicing factor SYF1 ;Pre-mRNA-splicing factor RBM22 ;Spliceosome-associated protein CWC15 homolog;Tuftelin-interacting protein 11 ;Probable ATP-dependent RNA helicase DDX41 ;RNA-binding protein Raly ;Pre-mRNA-splicing factor ISY1 homolog;Pre-mRNA-processing factor 19 ;Peptidyl-prolyl cis-trans isomerase E ;Serine/arginine repetitive matrix protein 2 ;U6 snRNA-associated Sm-like protein LSm2 ;Peptidyl-prolyl cis-trans isomerase-like 1 ;RNA-binding protein 8A","subunits.Gene.name.":"SART1;HNRNPR;PLRG1;AQR;SYNCRIP;CDC40;SF3B1;SNRNP200;PRPF6;SLU7;SYF2;HNRNPC;SNRPB2;HNRNPA1;SNRPA1;PABPC1;SNRPB;DDX5;HNRNPA2B1;HNRNPH1;RBMX;EIF4A3;SKIV2L2;HNRNPA3;HNRNPM;HNRNPF;MAGOH;HNRNPK;SNRPE;SNRPF;SNRPG;LSM3;SNRPD1;SNRPD2;SNRPD3;HNRNPU;U2AF1;SRSF1;SF3A3;SF3B2;PRPF4B;SNW1;FRG1;DHX8;EFTUD2;SF3B3;SF3A2;SF3A1;ZCCHC8;PRPF8;CWC27;ALYREF;SRRM1;CACTIN;DHX38;PPWD1;DGCR14;SNRNP40;CDC5L;GPATCH1;WDR83;DDX23;CRNKL1;PPIL3;PNN;DHX35;CWC22;XAB2;RBM22;CWC15;TFIP11;DDX41;RALY;ISY1;PRPF19;PPIE;SRRM2;LSM2;PPIL1;RBM8A","subunits.Gene.name.syn.":";HNRPR;;KIAA0560;HNRPQ NSAP1;EHB3 PRP17 PRPF17;SAP155;ASCC3L1 HELIC2 KIAA0788;C20orf14;;CBPIN GCIPIP;HNRPC;;HNRPA1;;PAB1 PABP1 PABPC2;COD SNRPB1;G17P1 HELR HLR1;HNRPA2B1;HNRPH HNRPH1;HNRPG RBMXP1;DDX48, KIAA0111;DOB1 KIAA0052 Mtr4;HNRPA3;HNRPM NAGR1;HNRPF;MAGOHA;HNRPK;;PBSCF;PBSCG;;;SNRPD1;;HNRPU SAFA U21.1;U2AF35 U2AFBP;ASF SF2 SF2P33 SFRS1;SAP61;SAP145;KIAA0536 PRP4 PRP4H PRP4K;SKIIP SKIP;;DDX8;KIAA0031 SNRP116;KIAA0017 SAP130;SAP62;SAP114;;PRPC8;SDCCAG10;ALY BEF THOC4;SRM160;C19orf29;DDX38 KIAA0224 PRP16;KIAA0073;DGCR13 DGSH DGSI ES2;PRP8BP SFP38 WDR57;KIAA0432 PCDC5RP;ECGP GPATC1;MORG1;;CRN;;DRS MEMA;C20orf15 DDX35;KIAA1604 NCM;HCNP KIAA1177 SYF1;ZC3H16;C11orf5;STIP;ABS;HNRPCL2 P542;KIAA1160;NMP200 PRP19 SNEV;CYP33;KIAA0324 SRL300 SRM300;C6orf28 G7B;CYPL1;RBM8, Y14","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In eukaryotes, the removal of introns from nascent transcripts is mediated by a highly dynamic, macromolecular machine called the spliceosome.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1182,"ComplexName":"CDC5L core complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43660;O75934;P11142;Q92616;Q99459;Q9UMS4","subunits.Entrez.IDs.":"5356;10286;3312;10985;988;27339","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0008380;GO:0003723;GO:0005634","GO.description":"RNA splicing;RNA binding;nucleus","FunCat.ID":"11.04.03.01;16.03.03;70.10","FunCat.description":"splicing;RNA binding;nucleus","PubMed.ID":11101529,"subunits.Protein.name.":"Pleiotropic regulator 1;Pre-mRNA-splicing factor SPF27 ;Heat shock cognate 71 kDa protein;eIF-2-alpha kinase activator GCN1 ;Cell division cycle 5-like protein ;Pre-mRNA-processing factor 19","subunits.Gene.name.":"PLRG1;BCAS2;HSPA8;GCN1;CDC5L;PRPF19","subunits.Gene.name.syn.":";DAM1;HSC70, HSP73, HSPA10;GCN1L1 KIAA0219;KIAA0432 PCDC5RP;NMP200 PRP19 SNEV","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The CDC5L complex incorporates into the spliceosome in an ATP-dependent step. This complex is required for the second catalytic step of pre-mRNA splicing. Immunodepletion of the CDC5L complex from HeLa nuclear extract inhibits the formation of pre-mRNA splicing products in vitro but does not prevent spliceosome assembly. Experiments indicate that there exists a CDC5L core complex in HeLa nuclear extract containing at least six proteins that interact with each other and with other splicing factors and enzymes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1183,"ComplexName":"CDC5L complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"A8K8P3;O15297;O43660;O75533;O75934;P09012;P09661;P11142;P11388;P15884;P23246;P38159;P62136;P62314;P62316;P62318;P78527;Q01130;Q07955;Q12905;Q13435;Q14204;Q15427;Q7L1Q6;Q8IYB3;Q92616;Q99459;Q9P013;Q9UMS4;Q9UPN6","subunits.Entrez.IDs.":"9814;8493;5356;23451;10286;6626;6627;3312;7153;6925;6421;27316;5499;6632;6633;6634;5591;6427;6426;3608;10992;1778;10262;9689;10250;10985;988;51503;27339;22828","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0008380;GO:0003723;GO:0005634","GO.description":"RNA splicing;RNA binding;nucleus","FunCat.ID":"11.04.03.01;16.03.03;70.10","FunCat.description":"splicing;RNA binding;nucleus","PubMed.ID":11101529,"subunits.Protein.name.":"Protein SFI1 homolog ;Protein phosphatase 1D ;Pleiotropic regulator 1;Splicing factor 3B subunit 1 ;Pre-mRNA-splicing factor SPF27 ;U1 small nuclear ribonucleoprotein A ;U2 small nuclear ribonucleoprotein A' ;Heat shock cognate 71 kDa protein;DNA topoisomerase 2-alpha;Transcription factor 4 ;Splicing factor, proline- and glutamine-rich ;RNA-binding motif protein, X chromosome ;Serine/threonine-protein phosphatase PP1-alpha catalytic subunit;Small nuclear ribonucleoprotein Sm D1 ;Small nuclear ribonucleoprotein Sm D2 ;Small nuclear ribonucleoprotein Sm D3 ;DNA-dependent protein kinase catalytic subunit ;Serine/arginine-rich splicing factor 2 ;Serine/arginine-rich splicing factor 1 ;Interleukin enhancer-binding factor 2 ;Splicing factor 3B subunit 2 ;Cytoplasmic dynein 1 heavy chain 1;Splicing factor 3B subunit 4 ;Basic leucine zipper and W2 domain-containing protein 1 ;Serine/arginine repetitive matrix protein 1 ;eIF-2-alpha kinase activator GCN1 ;Cell division cycle 5-like protein ;Spliceosome-associated protein CWC15 homolog;Pre-mRNA-processing factor 19 ;Protein SCAF8","subunits.Gene.name.":"SFI1;PPM1D;PLRG1;SF3B1;BCAS2;SNRPA;SNRPA1;HSPA8;TOP2A;TCF4;SFPQ;RBMX;PPP1CA;SNRPD1;SNRPD2;SNRPD3;PRKDC;SRSF2;SRSF1;ILF2;SF3B2;DYNC1H1;SF3B4;BZW1;SRRM1;GCN1;CDC5L;CWC15;PRPF19;SCAF8","subunits.Gene.name.syn.":"KIAA0542;WIP1;;SAP155;DAM1;;;HSC70, HSP73, HSPA10;TOP2;BHLHB19 ITF2 SEF2;PSF;HNRPG RBMXP1;PPP1A;;SNRPD1;;HYRC HYRC1;SFRS2;ASF SF2 SF2P33 SFRS1;NF45;SAP145;DHC1, DNCH1, DNCL, DNECL DYHC, KIAA0325;SAP49;BZAP45 KIAA0005;SRM160;GCN1L1 KIAA0219;KIAA0432 PCDC5RP;C11orf5;NMP200 PRP19 SNEV;CCAP7 KIAA1116 RBM16","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The CDC5L complex incorporates into the spliceosome in an ATP-dependent step. This complex is required for the second catalytic step of pre-mRNA splicing. Immunodepletion of the CDC5L complex from HeLa nuclear extract inhibits the formation of pre-mRNA splicing products in vitro but does not prevent spliceosome assembly.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1184,"ComplexName":"Mediator complex","Organism":"Mouse","Synonyms":"Mediator of transcriptional regulation","Cell.line":"None","subunits.UniProt.IDs.":"A2AGH6;Q569Z6;Q5U427;Q62447;Q6PGF3;Q80YQ2;Q921D4;Q925J9;Q99K74","subunits.Entrez.IDs.":"59024;230753;264064;51813;216154;70208;69792;19014;23989","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0071-molecular sieving;MI:0069-mass spectrometry studies of complexes","GO.ID":"GO:0045893;GO:0051098;GO:0051090;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;regulation of binding;regulation of sequence-specific DNA binding transcription factor activity;nucleus","FunCat.ID":"11.02.03.04.01;18.01.07;18.02.09;70.10","FunCat.description":"transcription activation;regulation by binding / dissociation;regulator of transcription factor;nucleus","PubMed.ID":11934987,"subunits.Protein.name.":"Mediator of RNA polymerase II transcription subunit 12;Thyroid hormone receptor-associated protein 3;Cdk8 protein;Cyclin-C;Mediator of RNA polymerase II transcription subunit 16;Mediator of RNA polymerase II transcription subunit 23;Mediator of RNA polymerase II transcription subunit 6;Mediator of RNA polymerase II transcription subunit 1;Mediator of RNA polymerase II transcription subunit 24","subunits.Gene.name.":"Med12;Thrap3;Cdk8;Ccnc;Med16;Med23;Med6;Med1;Med24","subunits.Gene.name.syn.":"Kiaa0192 Mopa Tnrc11 Trap230;Trap150;None;None;Thrap5;Crsp3 Kiaa1216 Sur2;None;Crsp210 Drip205 Pbp Pparbp Trap220 Trip2;D11Ertd307e Thrap4 Trap100","Disease.comment":"None","Subunits.comment":"At the time of annotation, the additional member med200 of the protein complex was not found in the UniProt database.","Complex.comment":"Regulation of transcription by RNA polymerase II (Pol II) is controlled by specific combinations of sequence-specific, DNA binding regulatory transcription factors (TFs) bound to a gene's promoter and enhancer regions. These TFs interact with several multiprotein complexes that remodel the chromatin context of the promoter, integrate signals from multiple TFs to control the frequency of transcription initiation, and regulate the efficiency of transcription elongation. One such complex is the Mediator, an ~2-megadalton complex of 20 to 30 subunits that is believed to function as a molecular bridge by simultaneously interacting with both DNA-bound TFs and Pol II. Several identical subunits appear in protein complexes like DRIP/ARC, CRSP, NAT, PC2, SMCC and Mediator, indicating that unique classes of transcription activators may share common sets or subsets of cofactors.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1185,"ComplexName":"EGFR-containing signaling complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00443;O00750;P00533;P04626","subunits.Entrez.IDs.":"5286;5287;1956;2064","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007173","GO.description":"epidermal growth factor receptor signaling pathway","FunCat.ID":"30.05.01.12.01","FunCat.description":"EGF-receptor signalling pathway","PubMed.ID":10805725,"subunits.Protein.name.":"Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha ;Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit beta ;Epidermal growth factor receptor;Receptor tyrosine-protein kinase erbB-2","subunits.Gene.name.":"PIK3C2A;PIK3C2B;EGFR;ERBB2","subunits.Gene.name.syn.":";;ERBB, ERBB1, HER1;HER2, MLN19, NEU, NGL","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"EGF stimulation recruits both PI3K-C2alpha  and PI3K-C2beta  to the EGFR-containing signaling complex, together with ErbB-2.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1186,"ComplexName":"ESCRT-III complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43633;Q7LBR1;Q96CF2;Q96FZ7;Q9BY43;Q9H444;Q9HD42;Q9NZZ3;Q9UQN3;Q9Y3E7","subunits.Entrez.IDs.":"27243;57132;92421;79643;29082;128866;5119;51510;25978;51652","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0008565;GO:0016192;GO:0005737","GO.description":"intracellular protein transport;protein targeting;protein transport;protein transporter activity;vesicle-mediated transport;cytoplasm","FunCat.ID":"14.04;20.01.10;20.09.07;70.03","FunCat.description":"protein targeting, sorting and translocation;protein transport;vesicular transport (Golgi network, etc.);cytoplasm","PubMed.ID":14519844,"subunits.Protein.name.":"Charged multivesicular body protein 2a ;Charged multivesicular body protein 1b ;Charged multivesicular body protein 4c ;Charged multivesicular body protein 6 ;Charged multivesicular body protein 4a ;Charged multivesicular body protein 4b ;Charged multivesicular body protein 1a ;Charged multivesicular body protein 5 ;Charged multivesicular body protein 2b ;Charged multivesicular body protein 3","subunits.Gene.name.":"CHMP2A;CHMP1B;CHMP4C;CHMP6;CHMP4A;CHMP4B;CHMP1A;CHMP5;CHMP2B;CHMP3","subunits.Gene.name.syn.":"BC2 CHMP2;C18orf2;SHAX3;VPS20;C14orf123 SHAX2;C20orf178 SHAX1;CHMP1 KIAA0047 PCOLN3 PRSM1;C9orf83 SNF7DC2;;CGI149 NEDF VPS24","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The ESCRT-III complex is required for multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-III complex is probably involved in the concentration of MVB cargo. In the ESCRT-III complex, it probably serves as an acceptor for ESCRT-II complex on endosomal membranes. In case of infection, the HIV-1 virus takes advantage of the ESCRT-III complex for budding and exocytic cargos of viral proteins.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1187,"ComplexName":"ESCRT-II complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q86VN1;Q96H20;Q9BRG1","subunits.Entrez.IDs.":"51028;11267;84313","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0008565;GO:0016192;GO:0005737","GO.description":"intracellular protein transport;protein targeting;protein transport;protein transporter activity;vesicle-mediated transport;cytoplasm","FunCat.ID":"14.04;20.01.10;20.09.07;70.03","FunCat.description":"protein targeting, sorting and translocation;protein transport;vesicular transport (Golgi network, etc.);cytoplasm","PubMed.ID":14519844,"subunits.Protein.name.":"Vacuolar protein-sorting-associated protein 36 ;Vacuolar-sorting protein SNF8 ;Vacuolar protein-sorting-associated protein 25","subunits.Gene.name.":"VPS36;SNF8;VPS25","subunits.Gene.name.syn.":"C13orf9 EAP45;EAP30;DERP9 EAP20","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The ESCRT-II complex is required for multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1188,"ComplexName":"SMRT core complex","Organism":"Human","Synonyms":"TBL1-SMRT-HDAC3 complex","Cell.line":"None","subunits.UniProt.IDs.":"O15379;O60907;Q9Y618","subunits.Entrez.IDs.":"8841;6907;9612","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0069- mass spectrometry studies of complexes; MI:0019- coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0009755;GO:0023052;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;hormone-mediated signaling pathway;signaling;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;30.01.09.08;30.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;hormone mediated signal transduction;cellular signalling;organization of chromosome structure;nucleus","PubMed.ID":10809664,"subunits.Protein.name.":"Histone deacetylase 3;F-box-like/WD repeat-containing protein TBL1X;Nuclear receptor corepressor 2","subunits.Gene.name.":"HDAC3;TBL1X;NCOR2","subunits.Gene.name.syn.":"None;TBL1;CTG26","Disease.comment":"TBL1 is involved in deafness.","Subunits.comment":"None","Complex.comment":"HDAC3 did not interact directly with TBL1. However, addition of SMRT to the mixture of HDAC3 and TBL1 allowed formation of a stable TBL1-SMRT-HDAC3 complex in vitro, suggesting that SMRT mediates the association of TBL1 and HDAC3 in a single complex in vivo.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1189,"ComplexName":"DNA double-strand break end-joining complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60934;P12956;P13010;P49917;P49959;Q13426;Q92878","subunits.Entrez.IDs.":"4683;2547;7520;3981;4361;7518;10111","Protein.complex.purification.method":"MI:0091- chromatography technologies; MI:0071- molecular sieving","GO.ID":"GO:0006281;GO:0003677;GO:0006974;GO:0005634","GO.description":"DNA repair;DNA binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;16.03.01;32.01.09;70.10","FunCat.description":"DNA repair;DNA binding;DNA damage response;nucleus","PubMed.ID":11809878,"subunits.Protein.name.":"Nibrin ;X-ray repair cross-complementing protein 6 ;X-ray repair cross-complementing protein 5 ;DNA ligase 4 ;Double-strand break repair protein MRE11A ;DNA repair protein XRCC4 ;DNA repair protein RAD50","subunits.Gene.name.":"NBN;XRCC6;XRCC5;LIG4;MRE11A;XRCC4;RAD50","subunits.Gene.name.syn.":"NBS NBS1 P95;G22P1;G22P2;;HNGS1 MRE11;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1190,"ComplexName":"NCBP-NIP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q09161;Q96P71","subunits.Entrez.IDs.":"4686;63941","Protein.complex.purification.method":"MI:0018- two hybrid","GO.ID":"GO:0003723;GO:0050789;GO:0005634","GO.description":"RNA binding;regulation of biological process;nucleus","FunCat.ID":"16.03.03;18;70.10","FunCat.description":"RNA binding;REGULATION OF METABOLISM AND PROTEIN FUNCTION;nucleus","PubMed.ID":7478990,"subunits.Protein.name.":"Nuclear cap-binding protein subunit 1;N-terminal EF-hand calcium-binding protein 3","subunits.Gene.name.":"NCBP1;NECAB3","subunits.Gene.name.syn.":"CBP80 NCBP;APBA2BP NIP1 SYTIP2 XB51","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1191,"ComplexName":"RNA pol II containing coactivator complex Tat-SF","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00267;O43719;P19338;P24928;P50750","subunits.Entrez.IDs.":"6829;27336;4691;5430;1025","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04;16.03.01;70.10","FunCat.description":"transcriptional control;DNA binding;nucleus","PubMed.ID":10393184,"subunits.Protein.name.":"Transcription elongation factor SPT5 ;HIV Tat-specific factor 1 ;Nucleolin ;DNA-directed RNA polymerase II subunit RPB1;Cyclin-dependent kinase 9","subunits.Gene.name.":"SUPT5H;HTATSF1;NCL;POLR2A;CDK9","subunits.Gene.name.syn.":"SPT5 SPT5H;;;POLR2;CDC2L4, TAK","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"All fractions with Tat stimulatory activity contained these components as well as CDK9.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1192,"ComplexName":"ESCRT-I complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"A5D8V6;Q99816;Q9UK41","subunits.Entrez.IDs.":"55048;7251;51160","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0008565;GO:0016192;GO:0005737;GO:0005783","GO.description":"intracellular protein transport;protein targeting;protein transport;protein transporter activity;vesicle-mediated transport;cytoplasm;endoplasmic reticulum","FunCat.ID":"14.04;20.01.10;20.09.07;70.03;70.07","FunCat.description":"protein targeting, sorting and translocation;protein transport;vesicular transport (Golgi network, etc.);cytoplasm;endoplasmic reticulum","PubMed.ID":15509564,"subunits.Protein.name.":"Vacuolar protein sorting-associated protein 37C ;Tumor susceptibility gene 101 protein ;Vacuolar protein sorting-associated protein 28 homolog","subunits.Gene.name.":"VPS37C;TSG101;VPS28","subunits.Gene.name.syn.":"PML39;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"ESCRT-I is one of three defined protein complexes in the class E vacuolar protein sorting (VPS) pathway required for the sorting of ubiquitinated transmembrane proteins into internal vesicles of multivesicular bodies.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1193,"ComplexName":"Rap1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P09874;P12956;P13010;P49959;Q15554;Q92878;Q9NYB0","subunits.Entrez.IDs.":"142;2547;7520;4361;7014;10111;54386","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0003677;GO:0006974;GO:0051276;GO:0005634","GO.description":"DNA binding;cellular response to DNA damage stimulus;chromosome organization;nucleus","FunCat.ID":"16.03.01;32.01.09;42.10.03;70.10","FunCat.description":"DNA binding;DNA damage response;organization of chromosome structure;nucleus","PubMed.ID":15100233,"subunits.Protein.name.":"Poly [ADP-ribose] polymerase 1;X-ray repair cross-complementing protein 6 ;X-ray repair cross-complementing protein 5 ;Double-strand break repair protein MRE11A ;Telomeric repeat-binding factor 2 ;DNA repair protein RAD50 ;Telomeric repeat-binding factor 2-interacting protein 1","subunits.Gene.name.":"PARP1;XRCC6;XRCC5;MRE11A;TERF2;RAD50;TERF2IP","subunits.Gene.name.syn.":"ADPRT PPOL;G22P1;G22P2;HNGS1 MRE11;TRBF2 TRF2;;DRIP5 RAP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex is responsible for proper maintenance of telomere length and structure. Rad50, Mre11 and Ku86 are recruited to Rap1 independent of TRF2. PARP1, however, most likely interacts with Rap1 through TRF2.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1194,"ComplexName":"E2F-6 complex","Organism":"Human","Synonyms":"E2F6.com-1 complex","Cell.line":"None","subunits.UniProt.IDs.":"O75461;O75712;P61244;Q06587;Q14186;Q8IWI9;Q8IY57;Q969R5;Q96KQ7;Q99496;Q9BYE7;Q9H9B1","subunits.Entrez.IDs.":"1876;2707;4149;6015;7027;23269;10138;83746;10919;6045;84108;79813","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation; MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0045892;GO:0018126;GO:0006479;GO:0003677;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;protein hydroxylation;protein methylation;DNA binding;nucleus","FunCat.ID":"11.02.03.04.03;14.07.09;16.03.01;70.10","FunCat.description":"transcription repression;posttranslational modification of amino acids (e.g. hydroxylation, methylation);DNA binding;nucleus","PubMed.ID":12004135,"subunits.Protein.name.":"Transcription factor E2F6 ;Gap junction beta-3 protein ;Protein max ;E3 ubiquitin-protein ligase RING1;Transcription factor Dp-1;MAX gene-associated protein ;YY1-associated factor 2;Lethal;Histone-lysine N-methyltransferase EHMT2 ;E3 ubiquitin-protein ligase RING2;Polycomb group RING finger protein 6 ;Histone-lysine N-methyltransferase EHMT1","subunits.Gene.name.":"E2F6;GJB3;MAX;RING1;TFDP1;MGA;YAF2;L3MBTL2;EHMT2;RNF2;PCGF6;EHMT1","subunits.Gene.name.syn.":";CX31;BHLHD4;RNF1;DP1;KIAA0518 MAD5;;;BAT8 C6orf30 G9A KMT1C NG36;BAP1 DING HIPI3 RING1B;MBLR RNF134;EUHMTASE1 GLP KIAA1876 KMT1D","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The E2F-6 complex occupies target promoters like E2F binding elements and contains chromatin modifiers such as histone methyltransferases. Data suggest that these chromatin modifiers contribute to silencing of E2F- and Myc-responsive genes in quiescent cells.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1195,"ComplexName":"Exon junction complex (mRNA splicing-dependent)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q6P2Q9;Q8IYB3","subunits.Entrez.IDs.":"10594;10250","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0019- coimmunoprecipitation; MI:0430- nucleic acid uv cross-linking assay","GO.ID":"GO:0008380;GO:0003723;GO:0005634","GO.description":"RNA splicing;RNA binding;nucleus","FunCat.ID":"11.04.03.01;16.03.03;70.10","FunCat.description":"splicing;RNA binding;nucleus","PubMed.ID":10809668,"subunits.Protein.name.":"Pre-mRNA-processing-splicing factor 8 ;Serine/arginine repetitive matrix protein 1","subunits.Gene.name.":"PRPF8;SRRM1","subunits.Gene.name.syn.":"PRPC8;SRM160","Disease.comment":"None","Subunits.comment":"At the time of annotation, the additional members p50 and p20 of the protein complex remained unidentified.","Complex.comment":"The results indicate that splicing alters the complement of proteins associated with exon-exon junctions regardless of the nature of the photoreactive group, the position of this group relative to the exon-exon junction, or the exact sequence of the 5' exon, even though changing the position or the nature of the photoreactive group can affect exactly which proteins are detected by this method.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1196,"ComplexName":"RAD51C-XRCC3 complex","Organism":"Human","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"O43502;O43542","subunits.Entrez.IDs.":"5889;7517","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies;MI:0018- two hybrid","GO.ID":"GO:0006281;GO:0006310;GO:0003677;GO:0005524;GO:0006974;GO:0005634","GO.description":"DNA repair;DNA recombination;DNA binding;ATP binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;10.01.05.03;16.03.01;16.19.03;32.01.09;70.10","FunCat.description":"DNA repair;DNA recombination;DNA binding;ATP binding;DNA damage response;nucleus","PubMed.ID":11331762,"subunits.Protein.name.":"DNA repair protein RAD51 homolog 3 ;DNA repair protein XRCC3","subunits.Gene.name.":"RAD51C;XRCC3","subunits.Gene.name.syn.":"RAD51L2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Rad51C protein alone catalyzes homologous pairing, suggesting that Rad51C is the catalytic subunit of the complex. The DNA-binding activity of Rad51C-Xrcc3 complex drastically decreases in the absence of Xrcc3, indicating that Xrcc3 is important for the DNA binding activity of the complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1197,"ComplexName":"TRF1-TIN2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P54274;Q15554;Q96AP0;Q9BSI4;Q9NUX5;Q9NYB0","subunits.Entrez.IDs.":"7013;7014;65057;26277;25913;54386","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA binding;chromosome organization;nucleus","FunCat.ID":"16.03.01;42.10.03;70.10","FunCat.description":"DNA binding;organization of chromosome structure;nucleus","PubMed.ID":15181449,"subunits.Protein.name.":"Telomeric repeat-binding factor 1 ;Telomeric repeat-binding factor 2 ;Adrenocortical dysplasia protein homolog ;TERF1-interacting nuclear factor 2 ;Protection of telomeres protein 1 ;Telomeric repeat-binding factor 2-interacting protein 1","subunits.Gene.name.":"TERF1;TERF2;ACD;TINF2;POT1;TERF2IP","subunits.Gene.name.syn.":"PIN2 TRBF1 TRF TRF1;TRBF2 TRF2;PIP1 PTOP TINT1 TPP1;TIN2;;DRIP5 RAP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"PTOP binds to the carboxyl terminus of POT1 and recruits it to telomeres.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1198,"ComplexName":"TIN2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q15554;Q96AP0;Q9BSI4;Q9NUX5","subunits.Entrez.IDs.":"7014;65057;26277;25913","Protein.complex.purification.method":"MI:0226- ion exchange chromatography; MI:0071- molecular sieving","GO.ID":"GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA binding;chromosome organization;nucleus","FunCat.ID":"16.03.01;42.10.03;70.10","FunCat.description":"DNA binding;organization of chromosome structure;nucleus","PubMed.ID":15181449,"subunits.Protein.name.":"Telomeric repeat-binding factor 2 ;Adrenocortical dysplasia protein homolog ;TERF1-interacting nuclear factor 2 ;Protection of telomeres protein 1","subunits.Gene.name.":"TERF2;ACD;TINF2;POT1","subunits.Gene.name.syn.":"TRBF2 TRF2;PIP1 PTOP TINT1 TPP1;TIN2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex regulates telomere length. PTOP binds to the carboxyl terminus of POT1 and recruits it to telomeres.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1199,"ComplexName":"Oligosaccharyltransferase complex (Stt3A variant)","Organism":"Human","Synonyms":"OST complex","Cell.line":"None","subunits.UniProt.IDs.":"P04843;P04844;P39656;P46977;P61803;Q9H0U3","subunits.Entrez.IDs.":"6184;6185;1650;3703;1603;84061","Protein.complex.purification.method":"MI:0028- cosedimentation in solution; MI:0226- ion exchange chromatography","GO.ID":"GO:0006487;GO:0005783","GO.description":"protein N-linked glycosylation;endoplasmic reticulum","FunCat.ID":"14.07.02.02;70.07","FunCat.description":"N-directed glycosylation, deglycosylation;endoplasmic reticulum","PubMed.ID":12887896,"subunits.Protein.name.":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 ;Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2 ;Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit ;Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A ;Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 ;Magnesium transporter protein 1","subunits.Gene.name.":"RPN1;RPN2;DDOST;STT3A;DAD1;MAGT1","subunits.Gene.name.syn.":";;KIAA0115 OST48;ITM1 TMC;;IAG2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Oligosaccharyltransferase (OST) is an integral membrane protein that catalyzes N-linked glycosylation of nascent proteins in the lumen of the endoplasmic reticulum. Genomes of most multicellular eukaryotes encode two homologs of Stt3p and mammals express two homologs of Ost3p. Tissue and cell type-specific differences in expression of the Stt3p homologs suggest that the enzymatic properties of oligosaccharyltransferase are regulated in eukaryotes to respond to alterations in glycoprotein flux through the secretory pathway and may contribute to tissue-specific glycan heterogeneity.  Iag2 appears to be weakly associated with the OST complex and dissociates from the other subunits at various stages during enzyme purification.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1200,"ComplexName":"Oligosaccharyltransferase complex (Stt3B variant)","Organism":"Human","Synonyms":"OST complex","Cell.line":"None","subunits.UniProt.IDs.":"P04843;P04844;P39656;P61803;Q13454;Q8TCJ2;Q9H0U3","subunits.Entrez.IDs.":"6184;6185;1650;1603;7991;201595;84061","Protein.complex.purification.method":"MI:0028- cosedimentation in solution; MI:0226- ion exchange chromatography","GO.ID":"GO:0006487;GO:0005783","GO.description":"protein N-linked glycosylation;endoplasmic reticulum","FunCat.ID":"14.07.02.02;70.07","FunCat.description":"N-directed glycosylation, deglycosylation;endoplasmic reticulum","PubMed.ID":12887896,"subunits.Protein.name.":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 ;Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2 ;Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit ;Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 ;Tumor suppressor candidate 3 ;Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B ;Magnesium transporter protein 1","subunits.Gene.name.":"RPN1;RPN2;DDOST;DAD1;TUSC3;STT3B;MAGT1","subunits.Gene.name.syn.":";;KIAA0115 OST48;;N33;SIMP;IAG2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Oligosaccharyltransferase (OST) is an integral membrane protein that catalyzes N-linked glycosylation of nascent proteins in the lumen of the endoplasmic reticulum. Genomes of most multicellular eukaryotes encode two homologs of Stt3p and mammals express two homologs of Ost3p. Tissue and cell type-specific differences in expression of the Stt3p homologs suggest that the enzymatic properties of oligosaccharyltransferase are regulated in eukaryotes to respond to alterations in glycoprotein flux through the secretory pathway and may contribute to tissue-specific glycan heterogeneity.  Tusc3 and Iag2 appear to be weakly associated with the OST complex and dissociate from the other subunits at various stages during enzyme purification.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1201,"ComplexName":"TRF1-TIN2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P54274;Q96AP0;Q9BSI4;Q9NUX5","subunits.Entrez.IDs.":"7013;65057;26277;25913","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA binding;chromosome organization;nucleus","FunCat.ID":"16.03.01;42.10.03;70.10","FunCat.description":"DNA binding;organization of chromosome structure;nucleus","PubMed.ID":15231715,"subunits.Protein.name.":"Telomeric repeat-binding factor 1 ;Adrenocortical dysplasia protein homolog ;TERF1-interacting nuclear factor 2 ;Protection of telomeres protein 1","subunits.Gene.name.":"TERF1;ACD;TINF2;POT1","subunits.Gene.name.syn.":"PIN2 TRBF1 TRF TRF1;PIP1 PTOP TINT1 TPP1;TIN2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex regulates telomere length.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1202,"ComplexName":"TRF1 telomere length regulation complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95271;P54274;Q9BSI4","subunits.Entrez.IDs.":"8658;7013;26277","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0051276;GO:0005634","GO.description":"chromosome organization;nucleus","FunCat.ID":"42.10.03;70.10","FunCat.description":"organization of chromosome structure;nucleus","PubMed.ID":15133513,"subunits.Protein.name.":"Tankyrase-1 ;Telomeric repeat-binding factor 1 ;TERF1-interacting nuclear factor 2","subunits.Gene.name.":"TNKS;TERF1;TINF2","subunits.Gene.name.syn.":"PARP5A PARPL TIN1 TINF1 TNKS1;PIN2 TRBF1 TRF TRF1;TIN2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Inhibition of TRF1 by tankyrase 1 is controlled by TIN2.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1203,"ComplexName":"Oligosaccharyltransferase OSTC-I","Organism":"Dog","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04843;P04844;P46977;P61803;Q05052;Q8N6L1;Q9NRP0","subunits.Entrez.IDs.":"6184;6185;3703;1603;404012;200185;58505","Protein.complex.purification.method":"MI:0069- mass spectrometry studies of complexes; MI:0028- cosedimentation in solution; MI:0276- blue native page","GO.ID":"GO:0006487;GO:0005783","GO.description":"protein N-linked glycosylation;endoplasmic reticulum","FunCat.ID":"14.07.02.02;70.07","FunCat.description":"N-directed glycosylation, deglycosylation;endoplasmic reticulum","PubMed.ID":15835887,"subunits.Protein.name.":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 ;Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2 ;Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A ;Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 ;Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit ;Keratinocyte-associated protein 2 ;Oligosaccharyltransferase complex subunit OSTC","subunits.Gene.name.":"RPN1;RPN2;STT3A;DAD1;DDOST;KRTCAP2;OSTC","subunits.Gene.name.syn.":";;ITM1 TMC;;OST48;KCP2;","Disease.comment":"None","Subunits.comment":"Since several proteins from dog were not available in the UniProt database at the time of annotation, the orthologous human proteins were used.","Complex.comment":"Oligosaccharyltransferase (OST) catalyzes the cotranslational transfer of high-mannose sugars to nascent polypeptides during N-linked glycosylation in the rough endoplasmic reticulum lumen.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Canis lupus familiaris (Dog) (Canis familiaris);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1204,"ComplexName":"Rap1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P54274;Q15554;Q92878;Q96AP0;Q9BSI4;Q9NUX5;Q9NYB0","subunits.Entrez.IDs.":"7013;7014;10111;65057;26277;25913;54386","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA binding;chromosome organization;nucleus","FunCat.ID":"16.03.01;42.10.03;70.10","FunCat.description":"DNA binding;organization of chromosome structure;nucleus","PubMed.ID":15316005,"subunits.Protein.name.":"Telomeric repeat-binding factor 1 ;Telomeric repeat-binding factor 2 ;DNA repair protein RAD50 ;Adrenocortical dysplasia protein homolog ;TERF1-interacting nuclear factor 2 ;Protection of telomeres protein 1 ;Telomeric repeat-binding factor 2-interacting protein 1","subunits.Gene.name.":"TERF1;TERF2;RAD50;ACD;TINF2;POT1;TERF2IP","subunits.Gene.name.syn.":"PIN2 TRBF1 TRF TRF1;TRBF2 TRF2;;PIP1 PTOP TINT1 TPP1;TIN2;;DRIP5 RAP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TIN2 was found to bind TRF1 and TRF2 simultaneously, showing that TIN2 can link these telomeric proteins. This connection appeared to stabilize TRF2 on the telomeres as the treatment of cells with TIN2 small interfering RNA resulted in a decreased presence of TRF2 and hRap1 at chromosome ends. Only 5-10% of the endogenous TRF1 could be recovered in association with the hRap1 complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1205,"ComplexName":"TRF2-Rap1 complex III","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q15554;Q9NYB0","subunits.Entrez.IDs.":"7014;54386","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA binding;chromosome organization;nucleus","FunCat.ID":"16.03.01;42.10.03;70.10","FunCat.description":"DNA binding;organization of chromosome structure;nucleus","PubMed.ID":15316005,"subunits.Protein.name.":"Telomeric repeat-binding factor 2 ;Telomeric repeat-binding factor 2-interacting protein 1","subunits.Gene.name.":"TERF2;TERF2IP","subunits.Gene.name.syn.":"TRBF2 TRF2;DRIP5 RAP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The TRF2 complex is primarily involved in telomere protection and contains the TRF2 interacting partner human (h)Rap1 as well as several factors involved in the DNA damage response.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1206,"ComplexName":"TRF-Rap1 complex I, 2MD","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95271;P54274;Q15554;Q9BSI4;Q9NUX5;Q9NYB0","subunits.Entrez.IDs.":"8658;7013;7014;26277;25913;54386","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA binding;chromosome organization;nucleus","FunCat.ID":"16.03.01;42.10.03;70.10","FunCat.description":"DNA binding;organization of chromosome structure;nucleus","PubMed.ID":15316005,"subunits.Protein.name.":"Tankyrase-1 ;Telomeric repeat-binding factor 1 ;Telomeric repeat-binding factor 2 ;TERF1-interacting nuclear factor 2 ;Protection of telomeres protein 1 ;Telomeric repeat-binding factor 2-interacting protein 1","subunits.Gene.name.":"TNKS;TERF1;TERF2;TINF2;POT1;TERF2IP","subunits.Gene.name.syn.":"PARP5A PARPL TIN1 TINF1 TNKS1;PIN2 TRBF1 TRF TRF1;TRBF2 TRF2;TIN2;;DRIP5 RAP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1207,"ComplexName":"TRF2-Rap1 complex II","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q15554;Q9BSI4;Q9NUX5;Q9NYB0","subunits.Entrez.IDs.":"7014;26277;25913;54386","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA binding;chromosome organization;nucleus","FunCat.ID":"16.03.01;42.10.03;70.10","FunCat.description":"DNA binding;organization of chromosome structure;nucleus","PubMed.ID":15316005,"subunits.Protein.name.":"Telomeric repeat-binding factor 2 ;TERF1-interacting nuclear factor 2 ;Protection of telomeres protein 1 ;Telomeric repeat-binding factor 2-interacting protein 1","subunits.Gene.name.":"TERF2;TINF2;POT1;TERF2IP","subunits.Gene.name.syn.":"TRBF2 TRF2;TIN2;;DRIP5 RAP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1208,"ComplexName":"Oligosaccharyltransferase OSTC-II","Organism":"Dog","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04843;P04844;P38377;P46977;P60058;P60467;P61803;Q05052;Q8N6L1;Q9NRP0","subunits.Entrez.IDs.":"6184;6185;404006;3703;404017;404018;1603;404012;200185;58505","Protein.complex.purification.method":"MI:0069- mass spectrometry studies of complexes; MI:0028- cosedimentation in solution; MI:0276- blue native page","GO.ID":"GO:0006487;GO:0005783","GO.description":"protein N-linked glycosylation;endoplasmic reticulum","FunCat.ID":"14.07.02.02;70.07","FunCat.description":"N-directed glycosylation, deglycosylation;endoplasmic reticulum","PubMed.ID":15835887,"subunits.Protein.name.":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 ;Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2 ;Protein transport protein Sec61 subunit alpha isoform 1 ;Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A ;Protein transport protein Sec61 subunit gamma;Protein transport protein Sec61 subunit beta;Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 ;Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit ;Keratinocyte-associated protein 2 ;Oligosaccharyltransferase complex subunit OSTC","subunits.Gene.name.":"RPN1;RPN2;SEC61A1;STT3A;SEC61G;SEC61B;DAD1;DDOST;KRTCAP2;OSTC","subunits.Gene.name.syn.":";;;ITM1 TMC;;;;OST48;KCP2;","Disease.comment":"None","Subunits.comment":"Since several proteins from dog were not available in the UniProt database at the time of annotation, the orthologous human proteins were used.","Complex.comment":"Oligosaccharyltransferase (OST) catalyzes the cotranslational transfer of high-mannose sugars to nascent polypeptides during N-linked glycosylation in the rough endoplasmic reticulum lumen.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Canis lupus familiaris (Dog) (Canis familiaris);Homo sapiens (Human);Canis lupus familiaris (Dog) (Canis familiaris);Canis lupus familiaris (Dog) (Canis familiaris);Homo sapiens (Human);Canis lupus familiaris (Dog) (Canis familiaris);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1209,"ComplexName":"Oligosaccharyltransferase OSTC-III","Organism":"Dog","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04843;P04844;P16967;P38377;P46977;P60467;P61803;Q05052;Q8N6L1;Q9NRP0;Q9UNL2","subunits.Entrez.IDs.":"6184;6185;403951;404006;3703;404018;1603;404012;200185;58505;6747","Protein.complex.purification.method":"MI:0069- mass spectrometry studies of complexes; MI:0028- cosedimentation in solution; MI:0276- blue native page","GO.ID":"GO:0006487;GO:0005783","GO.description":"protein N-linked glycosylation;endoplasmic reticulum","FunCat.ID":"14.07.02.02;70.07","FunCat.description":"N-directed glycosylation, deglycosylation;endoplasmic reticulum","PubMed.ID":15835887,"subunits.Protein.name.":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 ;Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2 ;Translocon-associated protein subunit alpha ;Protein transport protein Sec61 subunit alpha isoform 1 ;Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A ;Protein transport protein Sec61 subunit beta;Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 ;Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit ;Keratinocyte-associated protein 2 ;Oligosaccharyltransferase complex subunit OSTC ;Translocon-associated protein subunit gamma","subunits.Gene.name.":"RPN1;RPN2;SSR1;SEC61A1;STT3A;SEC61B;DAD1;DDOST;KRTCAP2;OSTC;SSR3","subunits.Gene.name.syn.":";;;;ITM1 TMC;;;OST48;KCP2;;TRAPG","Disease.comment":"None","Subunits.comment":"Since several proteins from dog were not available in the UniProt database at the time of annotation, the orthologous human proteins were used.","Complex.comment":"Oligosaccharyltransferase (OST) catalyzes the cotranslational transfer of high-mannose sugars to nascent polypeptides during N-linked glycosylation in the rough endoplasmic reticulum lumen.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Canis lupus familiaris (Dog) (Canis familiaris);Canis lupus familiaris (Dog) (Canis familiaris);Homo sapiens (Human);Canis lupus familiaris (Dog) (Canis familiaris);Homo sapiens (Human);Canis lupus familiaris (Dog) (Canis familiaris);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1210,"ComplexName":"Sec61-Sec62-Sec63 complex","Organism":"Bovine","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P60468;Q3T104;Q5EA68;Q99442;Q9UGP8","subunits.Entrez.IDs.":"10952;615778;505064;7095;11231","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0015031;GO:0008565;GO:0015267;GO:0006810;GO:0005783","GO.description":"protein transport;protein transporter activity;channel activity;transport;endoplasmic reticulum","FunCat.ID":"20.01.10;20.03.01;20;70.07","FunCat.description":"protein transport;channel / pore class transport;CELLULAR TRANSPORT, TRANSPORT FACILITIES AND TRANSPORT ROUTES;endoplasmic reticulum","PubMed.ID":10799540,"subunits.Protein.name.":"Protein transport protein Sec61 subunit beta;Protein transport protein Sec61 subunit gamma;Protein transport protein Sec61 subunit alpha isoform 1;Translocation protein SEC62;Translocation protein SEC63 homolog","subunits.Gene.name.":"SEC61B;SEC61G;SEC61A1;SEC62;SEC63","subunits.Gene.name.syn.":"None;None;None;TLOC1;SEC63L","Disease.comment":"None","Subunits.comment":"Since bovine SEC61B,TLOC1 and  SEC63 were not available in the UniProt database at the time of annotation, the orthologous human proteins were used.Since the authors did not specify SEC61A, we used isoform SEC61A1.","Complex.comment":"The Sec61-Sec62-Sec63 complex plays a crucial role in the insertion of secretory and membrane polypeptides into the ER. It is required for assembly of membrane and secretory proteins. The complex is thightly associated with membrane-bound ribosomes, either directly or through adapter proteins.","SWISSPROT.organism":"Homo sapiens (Human);Bos taurus (Bovine);Bos taurus (Bovine);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1211,"ComplexName":"Ubiquitin E3 ligase (AHR, ARNT, DDB1, TBL3, CUL4B, RBX1)","Organism":"Human","Synonyms":"CUL4AhR complex","Cell.line":"None","subunits.UniProt.IDs.":"P27540;P35869;P62877;Q12788;Q13620;Q16531","subunits.Entrez.IDs.":"405;196;9978;10607;8450;1642","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511;GO:0023052;GO:0005634","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;signaling;nucleus","FunCat.ID":"14.07.05;14.13.01.01;30.01;70.10","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway);cellular signalling;nucleus","PubMed.ID":17392787,"subunits.Protein.name.":"Aryl hydrocarbon receptor nuclear translocator ;Aryl hydrocarbon receptor ;E3 ubiquitin-protein ligase RBX1;Transducin beta-like protein 3 ;Cullin-4B;DNA damage-binding protein 1","subunits.Gene.name.":"ARNT;AHR;RBX1;TBL3;CUL4B;DDB1","subunits.Gene.name.syn.":"BHLHE2;BHLHE76;RNF75, ROC1;SAZD;KIAA0695;XAP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. In the CUL4B(AhR) ubiquitin E3 ligase complex, ligand-activated dioxin receptor AhR acts as a substrate-specific adaptor component that targets sex steroid receptors for degradation. Thus, experiments uncover a function for AhR as an atypical component of the ubiquitin ligase complex and demonstrate a non-genomic signalling pathway in which fat-soluble ligands regulate target-protein-selective degradation through a ubiquitin ligase complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1212,"ComplexName":"SNARE complex (Stx4, Vamp8, Snap23)","Organism":"Mouse","Synonyms":"None","Cell.line":"liver, pancreas","subunits.UniProt.IDs.":"O09044;O70404;P70452","subunits.Entrez.IDs.":"20619;22320;20909","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0004- affinity chromatography technologies","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":15363411,"subunits.Protein.name.":"Synaptosomal-associated protein 23 ;Vesicle-associated membrane protein 8;Syntaxin-4","subunits.Gene.name.":"Snap23;Vamp8;Stx4","subunits.Gene.name.syn.":"Sndt;None;Stx4a","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.VAMP8/endobrevin  is a major player in regulated exocytosis of the exocrine pancreas (pancreatic acinar cells). It is enriched on the membrane of zymogen granules.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1213,"ComplexName":"SNARE complex (Stx4, Vamp2, Snap23)","Organism":"Mouse","Synonyms":"None","Cell.line":"pancreas","subunits.UniProt.IDs.":"O09044;P63044;P70452","subunits.Entrez.IDs.":"20619;22318;20909","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":15363411,"subunits.Protein.name.":"Synaptosomal-associated protein 23 ;Vesicle-associated membrane protein 2 ;Syntaxin-4","subunits.Gene.name.":"Snap23;Vamp2;Stx4","subunits.Gene.name.syn.":"Sndt;Syb2;Stx4a","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1214,"ComplexName":"Ubiquitin E3 ligase (DET1, DDB1, CUL4A, RBX1, COP1)","Organism":"Human","Synonyms":"DCXhDET1-hCOP1 complex","Cell.line":"None","subunits.UniProt.IDs.":"P62877;Q13619;Q16531;Q7L5Y6;Q8NHY2","subunits.Entrez.IDs.":"9978;8451;1642;55070;64326","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation; MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511;GO:0023052;GO:0005634","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;signaling;nucleus","FunCat.ID":"14.07.05;14.13.01.01;30.01;70.10","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway);cellular signalling;nucleus","PubMed.ID":14739464,"subunits.Protein.name.":"E3 ubiquitin-protein ligase RBX1;Cullin-4A;DNA damage-binding protein 1;DET1 homolog ;E3 ubiquitin-protein ligase RFWD2","subunits.Gene.name.":"RBX1;CUL4A;DDB1;DET1;RFWD2","subunits.Gene.name.syn.":"RNF75, ROC1;None;XAP1;;COP1 RNF200","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Human DET1 (hDET1) promotes ubiquitination and degradation of the proto-oncogenic transcription factor c-Jun by assembling a multisubunit ubiquitin E3 ligase. Ablation of any subunit by RNA interference stabilized c-Jun and increased c-Jun-activated transcription.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1215,"ComplexName":"Ubiquitin E3 ligase (FBXW7, CUL1, SKP1A, RBX1)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62877;P63208;Q13616;Q969H0","subunits.Entrez.IDs.":"9978;6500;8454;55294","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511;GO:0007219;GO:0023052","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;Notch signaling pathway;signaling","FunCat.ID":"14.07.05;14.13.01.01;30.05.02.14;30.01","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway);Notch-receptor signalling pathway;cellular signalling","PubMed.ID":11585921,"subunits.Protein.name.":"E3 ubiquitin-protein ligase RBX1;S-phase kinase-associated protein 1;Cullin-1;F-box/WD repeat-containing protein 7","subunits.Gene.name.":"RBX1;SKP1;CUL1;FBXW7","subunits.Gene.name.syn.":"RNF75, ROC1;EMC19, OCP2, SKP1A, TCEB1L;None;FBW7, FBX30, SEL10","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. FBXW7 is an inhibitor of notch signaling that targets notch for ubiquitin-mediated protein degradation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1216,"ComplexName":"Hspb2-Hspb3 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O35878;Q9QZ58","subunits.Entrez.IDs.":"161476;78951","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515","GO.description":"protein binding","FunCat.ID":"16.01","FunCat.description":"protein binding","PubMed.ID":10625651,"subunits.Protein.name.":"Heat shock protein beta-2 ;Heat shock protein beta-3","subunits.Gene.name.":"Hspb2;Hspb3","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":1217,"ComplexName":"WRN-TRF2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q14191;Q15554","subunits.Entrez.IDs.":"7486;7014","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0051276;GO:0007569","GO.description":"chromosome organization;cell aging","FunCat.ID":"42.10.03;40.20","FunCat.description":"organization of chromosome structure;cell aging","PubMed.ID":12181313,"subunits.Protein.name.":"Werner syndrome ATP-dependent helicase ;Telomeric repeat-binding factor 2","subunits.Gene.name.":"WRN;TERF2","subunits.Gene.name.syn.":"RECQ3 RECQL2;TRBF2 TRF2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TRF2 interaction with WRN results in a stimulation of WRN-helicase activity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1218,"ComplexName":"BLM-TRF2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P54132;Q15554","subunits.Entrez.IDs.":"641;7014","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0051276;GO:0007569","GO.description":"chromosome organization;cell aging","FunCat.ID":"42.10.03;40.20","FunCat.description":"organization of chromosome structure;cell aging","PubMed.ID":12768206,"subunits.Protein.name.":"Bloom syndrome protein ;Telomeric repeat-binding factor 2","subunits.Gene.name.":"BLM;TERF2","subunits.Gene.name.syn.":"RECQ2 RECQL3;TRBF2 TRF2","Disease.comment":"BLM is involved in Bloom syndrome (BS) (PMID:12444098).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1219,"ComplexName":"Tankyrin 1-tankyrin 2-TRF1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95271;P54274;Q9H2K2","subunits.Entrez.IDs.":"8658;7013;80351","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0051276;GO:0005634","GO.description":"chromosome organization;nucleus","FunCat.ID":"42.10.03;70.10","FunCat.description":"organization of chromosome structure;nucleus","PubMed.ID":12080061,"subunits.Protein.name.":"Tankyrase-1 ;Telomeric repeat-binding factor 1 ;Tankyrase-2","subunits.Gene.name.":"TNKS;TERF1;TNKS2","subunits.Gene.name.syn.":"PARP5A PARPL TIN1 TINF1 TNKS1;PIN2 TRBF1 TRF TRF1;PARP5B TANK2 TNKL","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TRF1 binding allows tankyrase to regulate telomere dynamics. Mouse TRF1 lacks the binding motif for tankyrase.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1220,"ComplexName":"TRF2-Ku complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12956;P13010;Q15554","subunits.Entrez.IDs.":"2547;7520;7014","Protein.complex.purification.method":"MI:0018- two hybrid; MI:0019- coimmunoprecipitation","GO.ID":"GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA binding;chromosome organization;nucleus","FunCat.ID":"16.03.01;42.10.03;70.10","FunCat.description":"DNA binding;organization of chromosome structure;nucleus","PubMed.ID":10984620,"subunits.Protein.name.":"X-ray repair cross-complementing protein 6 ;X-ray repair cross-complementing protein 5 ;Telomeric repeat-binding factor 2","subunits.Gene.name.":"XRCC6;XRCC5;TERF2","subunits.Gene.name.syn.":"G22P1;G22P2;TRBF2 TRF2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1221,"ComplexName":"TFIIA-TRF2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P52655;P52657;Q15554","subunits.Entrez.IDs.":"2957;2958;7014","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;nucleus","FunCat.ID":"11.02.03.04;70.10","FunCat.description":"transcriptional control;nucleus","PubMed.ID":10570139,"subunits.Protein.name.":"Transcription initiation factor IIA subunit 1 ;Transcription initiation factor IIA subunit 2 ;Telomeric repeat-binding factor 2","subunits.Gene.name.":"GTF2A1;GTF2A2;TERF2","subunits.Gene.name.syn.":"TF2A1;TF2A2;TRBF2 TRF2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TRF2-TFIIA complex is able to replace TBP or TFIID in basal or activated transcription from various RNA polymerase II promoters.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1222,"ComplexName":"Irs1-Grb2-Ptpn1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P20417;P35570;P62994","subunits.Entrez.IDs.":"24697;25467;81504","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0008286","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;insulin receptor signaling pathway","FunCat.ID":"14.07.03;30.05.01.12.05","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;insulin receptor signalling pathway","PubMed.ID":10660596,"subunits.Protein.name.":"Tyrosine-protein phosphatase non-receptor type 1 ;Insulin receptor substrate 1 ;Growth factor receptor-bound protein 2","subunits.Gene.name.":"Ptpn1;Irs1;Grb2","subunits.Gene.name.syn.":";Irs-1;Ash","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors suggest that PTP1B and GRB2 may influence the steady-state capacity of IRS-1 to function as a phosphotyrosine scaffold and possibly affect the balance of postreceptor insulin signaling.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":1223,"ComplexName":"H2AX complex, isolated from cells without IR exposure","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43390;P05455;P06748;P11021;P11940;P16104;P27797;P62158;P62805;Q08945;Q8N257;Q9Y262;Q9Y5B9","subunits.Entrez.IDs.":"10236;6741;4869;3309;26986;3014;811;None;None;6749;128312;51386;11198","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0006265;GO:0000075;GO:0006354;GO:0051276;GO:0005634","GO.description":"DNA topological change;cell cycle checkpoint;DNA-templated transcription, elongation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;10.03.01.03;11.02.03.01.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);transcription elongation;organization of chromosome structure;nucleus","PubMed.ID":16522924,"subunits.Protein.name.":"Heterogeneous nuclear ribonucleoprotein R ;Lupus La protein ;Nucleophosmin ;78 kDa glucose-regulated protein;Polyadenylate-binding protein 1;Histone H2AX ;Calreticulin ;Calmodulin;Histone H4;FACT complex subunit SSRP1;Histone H2B type 3-B ;Eukaryotic translation initiation factor 3 subunit L ;FACT complex subunit SPT16","subunits.Gene.name.":"HNRNPR;SSB;NPM1;HSPA5;PABPC1;H2AFX;CALR;CALM1; CAL;HIST1H4A;;SSRP1;HIST3H2BB;EIF3L;SUPT16H","subunits.Gene.name.syn.":"HNRPR;;NPM;GRP78;PAB1 PABP1 PABPC2;H2AX;CRTC;CALM, CAM, CAM1, CAM2, CAMB, CALML2, CAM3, CAMC, CAMIII;H4/A H4FA; H4/I H4FI; H4/G H4FG; H4/B H4FB; H4/J H4FJ; H4/C H4FC; H4/H H4FH; H4/M H4FM; H4/E H4FE; H;FACT80;;EIF3EIP EIF3S6IP;FACT140 FACTP140","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1224,"ComplexName":"Ubiquitin E3 ligase (BMI1, SPOP, CUL3)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43791;P35226;Q13618","subunits.Entrez.IDs.":"8405;648;8452","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0009048;GO:0016567;GO:0016579;GO:0005634","GO.description":"dosage compensation by inactivation of X chromosome;protein ubiquitination;protein deubiquitination;nucleus","FunCat.ID":"10.03.04.06;14.07.05;70.10","FunCat.description":"chromosome inactivation;modification by ubiquitination, deubiquitination;nucleus","PubMed.ID":15897469,"subunits.Protein.name.":"Speckle-type POZ protein ;Polycomb complex protein BMI-1;Cullin-3","subunits.Gene.name.":"SPOP;BMI1;CUL3","subunits.Gene.name.syn.":";PCGF4 RNF51;KIAA0617","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. X inactivation involves the stable silencing of one of the two X chromosomes in XX female mammals. Initiation of this process occurs during early development and involves Xist (X-inactive-specific transcript) RNA coating and the recruitment of Polycomb repressive complex (PRC) 2 and PRC1 proteins. This recruitment results in an inactive state that is initially labile but is further locked in by epigenetic marks such as DNA methylation, histone hypoacetylation, and MACROH2A deposition. The ubiquitin E3 ligase consisting of SPOP and CULLIN3 is able to ubiquitinate the Polycomb group protein BMI1 and the variant histone H2AFY.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1225,"ComplexName":"Ubiquitin E3 ligase (H2AFY, SPOP, CUL3)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43791;O75367;Q13618","subunits.Entrez.IDs.":"8405;9555;8452","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0009048;GO:0016567;GO:0016579;GO:0005634","GO.description":"dosage compensation by inactivation of X chromosome;protein ubiquitination;protein deubiquitination;nucleus","FunCat.ID":"10.03.04.06;14.07.05;70.10","FunCat.description":"chromosome inactivation;modification by ubiquitination, deubiquitination;nucleus","PubMed.ID":15897469,"subunits.Protein.name.":"Speckle-type POZ protein ;Core histone macro-H2A.1 ;Cullin-3","subunits.Gene.name.":"SPOP;H2AFY;CUL3","subunits.Gene.name.syn.":";MACROH2A1;KIAA0617","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. X inactivation involves the stable silencing of one of the two X chromosomes in XX female mammals. Initiation of this process occurs during early development and involves Xist (X-inactive-specific transcript) RNA coating and the recruitment of Polycomb repressive complex (PRC) 2 and PRC1 proteins. This recruitment results in an inactive state that is initially labile but is further locked in by epigenetic marks such as DNA methylation, histone hypoacetylation, and MACROH2A deposition. The ubiquitin E3 ligase consisting of SPOP and CULLIN3 is able to ubiquitinate the Polycomb group protein BMI1 and the variant histone H2AFY.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1226,"ComplexName":"H2AX complex I","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06748;P09874;P11021;P16104;P27797;Q7L2E3;Q8N257","subunits.Entrez.IDs.":"4869;142;3309;3014;811;22907;128312","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0006281;GO:0006265;GO:0000075;GO:0006354;GO:0006974;GO:0051276;GO:0005634","GO.description":"DNA repair;DNA topological change;cell cycle checkpoint;DNA-templated transcription, elongation;cellular response to DNA damage stimulus;chromosome organization;nucleus","FunCat.ID":"10.01.05.01;10.01.09.05;10.03.01.03;11.02.03.01.04;32.01.09;42.10.03;70.10","FunCat.description":"DNA repair;DNA conformation modification (e.g. chromatin);cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);transcription elongation;DNA damage response;organization of chromosome structure;nucleus","PubMed.ID":16522924,"subunits.Protein.name.":"Nucleophosmin ;Poly [ADP-ribose] polymerase 1;78 kDa glucose-regulated protein;Histone H2AX ;Calreticulin ;Putative ATP-dependent RNA helicase DHX30 ;Histone H2B type 3-B","subunits.Gene.name.":"NPM1;PARP1;HSPA5;H2AFX;CALR;DHX30;HIST3H2BB","subunits.Gene.name.syn.":"NPM;ADPRT PPOL;GRP78;H2AX;CRTC;DDX30 KIAA0890;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex has been isolated from cells after IR exposure and recovery for 30 minutes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1227,"ComplexName":"H2AX complex II","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06748;P11021;P16104;P16989;P27797;P33778;P62805;Q8N257;Q96EY7;Q99879","subunits.Entrez.IDs.":"4869;3309;3014;8531;811;3018;None;128312;55037;8342","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0006281;GO:0006265;GO:0000075;GO:0006354;GO:0006974;GO:0051276;GO:0005634","GO.description":"DNA repair;DNA topological change;cell cycle checkpoint;DNA-templated transcription, elongation;cellular response to DNA damage stimulus;chromosome organization;nucleus","FunCat.ID":"10.01.05.01;10.01.09.05;10.03.01.03;11.02.03.01.04;32.01.09;42.10.03;70.10","FunCat.description":"DNA repair;DNA conformation modification (e.g. chromatin);cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);transcription elongation;DNA damage response;organization of chromosome structure;nucleus","PubMed.ID":16522924,"subunits.Protein.name.":"Nucleophosmin ;78 kDa glucose-regulated protein;Histone H2AX ;Y-box-binding protein 3 ;Calreticulin ;Histone H2B type 1-B ;Histone H4;Histone H2B type 3-B ;Pentatricopeptide repeat domain-containing protein 3, mitochondrial ;Histone H2B type 1-M","subunits.Gene.name.":"NPM1;HSPA5;H2AFX;YBX3;CALR;HIST1H2BB;HIST1H4A;;HIST3H2BB;PTCD3;HIST1H2BM","subunits.Gene.name.syn.":"NPM;GRP78;H2AX;CSDA DBPA;CRTC;H2BFF;H4/A H4FA; H4/I H4FI; H4/G H4FG; H4/B H4FB; H4/J H4FJ; H4/C H4FC; H4/H H4FH; H4/M H4FM; H4/E H4FE; H;;MRPS39;H2BFE","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex has been isolated from cells after IR exposure and recovery for 2.5h.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1228,"ComplexName":"Epsin-clathrin complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"O08838;O88339;P18484;P84092;Q05140","subunits.Entrez.IDs.":"60668;117277;81637;116563;65178","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006897;GO:0005737","GO.description":"endocytosis;cytoplasm","FunCat.ID":"20.09.18.09.01;70.03","FunCat.description":"endocytosis;cytoplasm","PubMed.ID":10692452,"subunits.Protein.name.":"Amphiphysin;Epsin-1 ;AP-2 complex subunit alpha-2 ;AP-2 complex subunit mu ;Clathrin coat assembly protein AP180","subunits.Gene.name.":"Amph;Epn1;Ap2a2;Ap2m1;Snap91","subunits.Gene.name.syn.":"Amph1;;Adtab;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"AP-2, clathrin, amphiphysin, eps15, and beta -arrestin, epsin form a multivalent protein network that probably influences the endocytic process.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":1229,"ComplexName":"RACK1-containing mRNP complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P63245;Q6AY21;Q9EPH8;Q9JIR1","subunits.Entrez.IDs.":"83427;305240;171350;266780","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006417;GO:0003723;GO:0007268;GO:0005886","GO.description":"regulation of translation;RNA binding;synaptic transmission;plasma membrane","FunCat.ID":"12.07;16.03.03;34.03.01;70.02","FunCat.description":"translational control;RNA binding;synaptic transmission;eukaryotic plasma membrane / membrane attached","PubMed.ID":12388589,"subunits.Protein.name.":"Receptor of activated protein C kinase 1 ;GTPase activating protein ;Polyadenylate-binding protein 1 ;RIMS-binding protein 2","subunits.Gene.name.":"Rack1;G3bp2;Pabpc1;Rimbp2","subunits.Gene.name.syn.":"Gnb2l1;RGD1309571;Pabp1;Rbp2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":1230,"ComplexName":"WINAC complex","Organism":"Human","Synonyms":"WSTF containing complex","Cell.line":"None","subunits.UniProt.IDs.":"O14497;O96019;P11473;P51531;P51532;Q02880;Q12824;Q13111;Q8TAQ2;Q92922;Q969G3;Q96GM5;Q9UIG0;Q9Y5B9","subunits.Entrez.IDs.":"8289;86;7421;6595;6597;7155;6598;10036;6601;6599;6605;6602;9031;11198","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies;MI:0029- cosedimentation through density gradients;MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006260;GO:0006265;GO:0000084;GO:2001141;GO:0006355;GO:0051276;GO:0005634;GO:0005102","GO.description":"DNA replication;DNA topological change;mitotic S phase;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;chromosome organization;nucleus;receptor binding","FunCat.ID":"10.01.03;10.01.09.05;10.03.01.01.05;11.02.03.04;42.10.03;70.10;16.01.01","FunCat.description":"DNA synthesis and replication;DNA conformation modification (e.g. chromatin);S phase of mitotic cell cycle;transcriptional control;organization of chromosome structure;nucleus;receptor binding","PubMed.ID":12837248,"subunits.Protein.name.":"AT-rich interactive domain-containing protein 1A;Actin-like protein 6A;Vitamin D3 receptor ;Probable global transcription activator SNF2L2;Transcription activator BRG1;DNA topoisomerase 2-beta ;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;Chromatin assembly factor 1 subunit A ;SWI/SNF complex subunit SMARCC2;SWI/SNF complex subunit SMARCC1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1;Tyrosine-protein kinase BAZ1B ;FACT complex subunit SPT16","subunits.Gene.name.":"ARID1A;ACTL6A;VDR;SMARCA2;SMARCA4;TOP2B;SMARCB1;CHAF1A;SMARCC2;SMARCC1;SMARCE1;SMARCD1;BAZ1B;SUPT16H","subunits.Gene.name.syn.":"BAF250 BAF250A C1orf4 OSA1 SMARCF1;BAF53 BAF53A INO80K;NR1I1;BAF190B, BRM, SNF2A, SNF2L2;BAF190A BRG1 SNF2B SNF2L4;;BAF47, INI1, SNF5L1;CAF CAF1P150;BAF170;BAF155;BAF57;BAF60A;WBSC10 WBSCR10 WBSCR9 WSTF;FACT140 FACTP140","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"WINAC mediates the recruitment of unliganded VDR to VDR target sites in promoters, while subsequent binding of coregulators requires ligand binding.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1231,"ComplexName":"FIB-associated protein complex","Organism":"Human","Synonyms":"None","Cell.line":"kidney","subunits.UniProt.IDs.":"O14744;P22087;Q07021;Q71U36;Q99873;Q9H4B7","subunits.Entrez.IDs.":"10419;2091;708;7846;3276;81027","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0006364;GO:0000154;GO:0042254;GO:0005634","GO.description":"rRNA processing;rRNA modification;ribosome biogenesis;nucleus","FunCat.ID":"11.04.01;11.06.01;12.01;70.10","FunCat.description":"rRNA processing;rRNA modification;ribosome biogenesis;nucleus","PubMed.ID":14583623,"subunits.Protein.name.":"Protein arginine N-methyltransferase 5;rRNA 2'-O-methyltransferase fibrillarin;Complement component 1 Q subcomponent-binding protein, mitochondrial;Tubulin alpha-1A chain;Protein arginine N-methyltransferase 1;Tubulin beta-1 chain","subunits.Gene.name.":"PRMT5;FBL;C1QBP;TUBA1A;PRMT1;TUBB1","subunits.Gene.name.syn.":"HRMT1L5 IBP72 JBP1 SKB1;FIB1 FLRN;GC1QBP HABP1 SF2P32;TUBA3;HMT2 HRMT1L2 IR1B4;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"FIB-associated protein complexes contain a number of ribosomal proteins and potential trans-acting factors involved in ribosome biogenesis, and the complexes are dependent on RNA integrity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1232,"ComplexName":"REST-CoREST-mSIN3A complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK-293 cells,","subunits.UniProt.IDs.":"Q13127;Q96ST3;Q9UKL0","subunits.Entrez.IDs.":"5978;25942;23186","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0045892;GO:0022008;GO:0048699;GO:0030182;GO:0007399;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;neurogenesis;generation of neurons;neuron differentiation;nervous system development;nucleus","FunCat.ID":"11.02.03.04.03;41.05.13;43.03.13;47.03.01;70.10","FunCat.description":"transcription repression;neurogenesis;neuron;nervous system;nucleus","PubMed.ID":10734093,"subunits.Protein.name.":"RE1-silencing transcription factor ;Paired amphipathic helix protein Sin3a;REST corepressor 1","subunits.Gene.name.":"REST;SIN3A;RCOR1","subunits.Gene.name.syn.":"NRSF XBR;None;KIAA0071 RCOR","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The REST-mSin3A association involves the NH(2)-terminal repressor domain of REST and the paired amphipathic helix 2 domain of mSin3A. REST forms complexes with endogenous mSin3A in mammalian cells, and both mSin3A and CoREST interact with REST in intact mammalian cells.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1233,"ComplexName":"CoREST-HDAC2 complex","Organism":"Human","Synonyms":"None","Cell.line":"non-neuronal COS 1 cells, neuronal PC12 cells","subunits.UniProt.IDs.":"Q92769;Q9UKL0","subunits.Entrez.IDs.":"3066;23186","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;organization of chromosome structure;nucleus","PubMed.ID":11516394,"subunits.Protein.name.":"Histone deacetylase 2;REST corepressor 1","subunits.Gene.name.":"HDAC2;RCOR1","subunits.Gene.name.syn.":"None;KIAA0071 RCOR","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In the presence of REST, the CoREST/HDAC2 complex represses transcription of the Nav1.2 sodium channel gene.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1235,"ComplexName":"SNARE complex (Vamp2, Snap25, Stx1a, Syt1, Cplx1)","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P21707;P32851;P60881;P63041;P63045","subunits.Entrez.IDs.":"25716;116470;25012;64832;24803","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":10051208,"subunits.Protein.name.":"Synaptotagmin-1 ;Syntaxin-1A;Synaptosomal-associated protein 25;Complexin-1;Vesicle-associated membrane protein 2","subunits.Gene.name.":"Syt1;Stx1a;Snap25;Cplx1;Vamp2","subunits.Gene.name.syn.":";Sap;Snap;None;Syb2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":1236,"ComplexName":"SNARE complex (Vamp2, Snap25, Stx1a, Syt1, Cplx2)","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P21707;P32851;P60881;P63045;P84087","subunits.Entrez.IDs.":"25716;116470;25012;24803;116657","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":10051208,"subunits.Protein.name.":"Synaptotagmin-1 ;Syntaxin-1A;Synaptosomal-associated protein 25;Vesicle-associated membrane protein 2;Complexin-2","subunits.Gene.name.":"Syt1;Stx1a;Snap25;Vamp2;Cplx2","subunits.Gene.name.syn.":";Sap;Snap;Syb2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":1237,"ComplexName":"BAF complex","Organism":"Human","Synonyms":"SWI/SNF complex A","Cell.line":"None","subunits.UniProt.IDs.":"O14497;O96019;P51531;P51532;Q12824;Q8TAQ2;Q92922;Q969G3;Q96GM5","subunits.Entrez.IDs.":"8289;86;6595;6597;6598;6601;6599;6605;6602","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045893;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;positive regulation of transcription, DNA-templated;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.01;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription activation;DNA binding;organization of chromosome structure;nucleus","PubMed.ID":11073988,"subunits.Protein.name.":"AT-rich interactive domain-containing protein 1A;Actin-like protein 6A;Probable global transcription activator SNF2L2;Transcription activator BRG1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;SWI/SNF complex subunit SMARCC2;SWI/SNF complex subunit SMARCC1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","subunits.Gene.name.":"ARID1A;ACTL6A;SMARCA2;SMARCA4;SMARCB1;SMARCC2;SMARCC1;SMARCE1;SMARCD1","subunits.Gene.name.syn.":"BAF250 BAF250A C1orf4 OSA1 SMARCF1;BAF53 BAF53A INO80K;BAF190B, BRM, SNF2A, SNF2L2;BAF190A BRG1 SNF2B SNF2L4;BAF47, INI1, SNF5L1;BAF170;BAF155;BAF57;BAF60A","Disease.comment":"None","Subunits.comment":"Another subunit of the complex was found in the analysis, which has not been further characterized: BAF110.","Complex.comment":"BAF250 confers specificity to the human BAF complex and may recruit the complex to its targets through either protein-DNA or protein-protein interactions.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1238,"ComplexName":"PBAF complex (Polybromo- and BAF containing complex)","Organism":"Human","Synonyms":"SWI/SNF-B complex","Cell.line":"T47D cells","subunits.UniProt.IDs.":"O96019;P51532;Q12824;Q68CP9;Q86U86;Q8TAQ2;Q92922;Q969G3;Q96GM5","subunits.Entrez.IDs.":"86;6597;6598;196528;55193;6601;6599;6605;6602","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045893;GO:0003677;GO:0009755;GO:0023052;GO:0051276;GO:0005694","GO.description":"DNA topological change;positive regulation of transcription, DNA-templated;DNA binding;hormone-mediated signaling pathway;signaling;chromosome organization;chromosome","FunCat.ID":"10.01.09.05;11.02.03.04.01;16.03.01;30.01.09.08;30.01;42.10.03;70.10.03","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription activation;DNA binding;hormone mediated signal transduction;cellular signalling;organization of chromosome structure;chromosome","PubMed.ID":11780067,"subunits.Protein.name.":"Actin-like protein 6A;Transcription activator BRG1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;AT-rich interactive domain-containing protein 2;Protein polybromo-1;SWI/SNF complex subunit SMARCC2;SWI/SNF complex subunit SMARCC1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","subunits.Gene.name.":"ACTL6A;SMARCA4;SMARCB1;ARID2;PBRM1;SMARCC2;SMARCC1;SMARCE1;SMARCD1","subunits.Gene.name.syn.":"BAF53 BAF53A INO80K;BAF190A BRG1 SNF2B SNF2L4;BAF47, INI1, SNF5L1;KIAA1557;BAF180 PB1;BAF170;BAF155;BAF57;BAF60A","Disease.comment":"None","Subunits.comment":"Two other subunits of the complex were found in the analysis, which have not been further characterized: BAF110 and BAF240.","Complex.comment":"The chromatin-remodeling complex PBAF facilitates gene activation by assisting transcription machinery to gain access to targets on the chromosome.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1239,"ComplexName":"EBAFb complex","Organism":"Human","Synonyms":"ENL-associated BAF250b-containing SWI/SNF complex","Cell.line":"None","subunits.UniProt.IDs.":"O96019;P51532;Q03111;Q12824;Q8NFD5;Q8TAQ2;Q92922;Q92925;Q969G3;Q96GM5","subunits.Entrez.IDs.":"86;6597;4298;6598;57492;6601;6599;6603;6605;6602","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0071- molecular sieving","GO.ID":"GO:0006265;GO:0045893;GO:0003677;GO:0051276;GO:0005694","GO.description":"DNA topological change;positive regulation of transcription, DNA-templated;DNA binding;chromosome organization;chromosome","FunCat.ID":"10.01.09.05;11.02.03.04.01;16.03.01;42.10.03;70.10.03","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription activation;DNA binding;organization of chromosome structure;chromosome","PubMed.ID":12665591,"subunits.Protein.name.":"Actin-like protein 6A;Transcription activator BRG1;Protein ENL;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;AT-rich interactive domain-containing protein 1B;SWI/SNF complex subunit SMARCC2;SWI/SNF complex subunit SMARCC1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","subunits.Gene.name.":"ACTL6A;SMARCA4;MLLT1;SMARCB1;ARID1B;SMARCC2;SMARCC1;SMARCD2;SMARCE1;SMARCD1","subunits.Gene.name.syn.":"BAF53 BAF53A INO80K;BAF190A BRG1 SNF2B SNF2L4;ENL, LTG19, YEATS1;BAF47, INI1, SNF5L1;BAF250B DAN15 KIAA1235 OSA2;BAF170;BAF155;BAF60B;BAF57;BAF60A","Disease.comment":"None","Subunits.comment":"Three other subunits of the complex were found in the analysis, which have not been further characterized: EBAF140, EBAF100 and EBAF70.","Complex.comment":"ENL associates and cooperates with SWI/SNF complexes to activate transcription of the promoter of HoxA7, a downstream target essential for oncogenic activity of ENL.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1240,"ComplexName":"SC5bp-7 complex","Organism":"Rabbit","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06684;P10643;P22458;P48747;P98136;Q9QXT7","subunits.Entrez.IDs.":"15139;730;100009128;100009197;100009076;12274","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies;MI:0004-affinity chromatography technologies","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":410885,"subunits.Protein.name.":"Complement C5;Complement component C7;Vitronectin;Complement component C9;Complement component C8 alpha chain;Complement component 6","subunits.Gene.name.":"C5;C7;VTN;C9;C8A;C6","subunits.Gene.name.syn.":"Hc;None;None;None;None;None","Disease.comment":"None","Subunits.comment":"Since C5, C6 and C7 from rabbit were not available in the UniProt database at the time of annotation, the orthologous proteins from human and mouse were used.","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Homo sapiens (Human);Oryctolagus cuniculus (Rabbit);Oryctolagus cuniculus (Rabbit);Oryctolagus cuniculus (Rabbit);Mus musculus (Mouse)"}
{"ComplexID":1241,"ComplexName":"Esr1-Pit1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06211;P10037","subunits.Entrez.IDs.":"24890;25517","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":10809776,"subunits.Protein.name.":"Estrogen receptor ;Pituitary-specific positive transcription factor 1","subunits.Gene.name.":"Esr1;Pou1f1","subunits.Gene.name.syn.":"Esr Estr Nr3a1;Ghf-1 Pit-1 Pit1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors report that estrogen may regulate the interaction between Pit-1 and ER-alpha  proteins through diverse pathways depending on the pituitary cell types. The results also indicate that accessory factor(s) are involved in the synergistic interaction between Pit-1 and ER-alpha  proteins and that synthesis of these factors is likely to be estrogen-induced.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":1243,"ComplexName":"Ubiquitin E3 ligase (SPOP, DAXX, CUL3)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43791;Q13618;Q9UER7","subunits.Entrez.IDs.":"8405;8452;1616","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0016567;GO:0016579;GO:0043161;GO:0006511;GO:0043067;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;regulation of programmed cell death;nucleus","FunCat.ID":"11.02.03.04;14.07.05;14.13.01.01;40.10.02.04;70.10","FunCat.description":"transcriptional control;modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway);regulation of apoptosis;nucleus","PubMed.ID":16524876,"subunits.Protein.name.":"Speckle-type POZ protein ;Cullin-3;Death domain-associated protein 6","subunits.Gene.name.":"SPOP;CUL3;DAXX","subunits.Gene.name.syn.":";KIAA0617;BING2 DAP6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. SPOP serves as an adaptor of Daxx for the ubiquitination by Cul3-based ubiquitin ligase and subsequent degradation by the proteasome. Experiments suggest that SPOP/Cul3-ubiquitin ligase plays an essential role in the control of Daxx level and, thus, in the regulation of Daxx-mediated cellular processes, including transcriptional regulation and apoptosis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1244,"ComplexName":"SNARE complex (STX1A, STX1B, SNAP25, RAB3A, SYT1, VAMP2)","Organism":"Bovine","Synonyms":"Docking/fusion complex","Cell.line":"brain","subunits.UniProt.IDs.":"P11023;P32850;P48018;P61267;P63026;Q17QQ3","subunits.Entrez.IDs.":"282029;788566;281511;282377;282116;540853","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0004- affinity chromatography technologies","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":7654227,"subunits.Protein.name.":"Ras-related protein Rab-3A ;Syntaxin-1A ;Synaptotagmin-1 ;Syntaxin-1B ;Vesicle-associated membrane protein 2 ;Synaptosomal-associated protein 25","subunits.Gene.name.":"RAB3A;STX1A;SYT1;STX1B;VAMP2;SNAP25","subunits.Gene.name.syn.":";;;STX1B2;SYB2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.VAMP/synaptobrevin-2 exists exclusively on the synaptic vesicle membrane and serves as a v-SNARE,while syntaxins 1A and 1 B are mostly on the presynaptic plasma membrane and thus t-SNAREs.The SNARE hypothesis proposes that fusion in membrane transport occurs by combination between a SNARE in the transport vesicle (v-SNARE)and a SNARE in the target membrane (t-SNARE).","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":1245,"ComplexName":"Protein phosphatase 4 complex","Organism":"Human","Synonyms":"PPP4;PPP4c","Cell.line":"None","subunits.UniProt.IDs.":"P60510;Q9NY27","subunits.Entrez.IDs.":"5531;151987","Protein.complex.purification.method":"MI:0028- cosedimentation in solution","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0005813","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;centrosome","FunCat.ID":"14.07.03;70.05","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;centrosome","PubMed.ID":10769191,"subunits.Protein.name.":"Serine/threonine-protein phosphatase 4 catalytic subunit ;Serine/threonine-protein phosphatase 4 regulatory subunit 2","subunits.Gene.name.":"PPP4C;PPP4R2","subunits.Gene.name.syn.":"PPP4 PPX;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Protein phosphatase 4 (PPP4) is a protein serine/threonine phosphatase that has been implicated in microtubule organization at centrosomes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1246,"ComplexName":"ERdj3-BiP complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P20029;Q99KV1","subunits.Entrez.IDs.":"14828;67838","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0050821;GO:0006457;GO:0030968;GO:0005783","GO.description":"protein stabilization;protein folding;endoplasmic reticulum unfolded protein response;endoplasmic reticulum","FunCat.ID":"14.01;32.01.07;70.07","FunCat.description":"protein folding and stabilization;unfolded protein response (e.g. ER quality control);endoplasmic reticulum","PubMed.ID":15525676,"subunits.Protein.name.":"78 kDa glucose-regulated protein ;DnaJ homolog subfamily B member 11","subunits.Gene.name.":"Hspa5;Dnajb11","subunits.Gene.name.syn.":"Grp78;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for interactions of the chaperone BiP with unfolded substrates.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1247,"ComplexName":"SNARE complex (STX1a, STX1b, SNAP25, RAB3a, SYT1, VAMP2, CPLX2)","Organism":"Bovine","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P11023;P32850;P48018;P61267;P63026;P84088;Q17QQ3","subunits.Entrez.IDs.":"282029;788566;281511;282377;282116;281711;540853","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0051098;GO:0005515;GO:0006906;GO:0048489;GO:0016079","GO.description":"regulation of binding;protein binding;vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"18.01.07;16.01;20.09.07.27;20.09.16.09.05","FunCat.description":"regulation by binding / dissociation;protein binding;vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":7654227,"subunits.Protein.name.":"Ras-related protein Rab-3A ;Syntaxin-1A ;Synaptotagmin-1 ;Syntaxin-1B ;Vesicle-associated membrane protein 2 ;Complexin-2 ;Synaptosomal-associated protein 25","subunits.Gene.name.":"RAB3A;STX1A;SYT1;STX1B;VAMP2;CPLX2;SNAP25","subunits.Gene.name.syn.":";;;STX1B2;SYB2;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.Synaphin (19a component) constantly copurifies with the docking/fusion complex irrespective of detergent.It seems to regulate the efficiency of the docking/fusion complex.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":1248,"ComplexName":"Apoptosome","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14727;P99999","subunits.Entrez.IDs.":"317;54205","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0006915;GO:0005737","GO.description":"apoptotic process;cytoplasm","FunCat.ID":"40.10.02;70.03","FunCat.description":"apoptosis (type I programmed cell death);cytoplasm","PubMed.ID":16271896,"subunits.Protein.name.":"Apoptotic protease-activating factor 1 ;Cytochrome c","subunits.Gene.name.":"APAF1;CYCS","subunits.Gene.name.syn.":"KIAA0413;CYC","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The apoptosome is a multiprotein complex mediating the mitochondrial pathway of cell death. Oligomeric Apaf-1 mediates the cytochrome c-dependent autocatalytic activation of pro-caspase-9 (Apaf-3), leading to the activation of caspase-3 and apoptosis. In the absence of an apoptotic signal, Apaf-1 exists in a monomeric form.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1250,"ComplexName":"pRB-E2F-1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06400;Q01094","subunits.Entrez.IDs.":"5925;1869","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007050;GO:0006974;GO:0005634","GO.description":"cell cycle arrest;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.03.01.02;32.01.09;70.10","FunCat.description":"cell cycle arrest;DNA damage response;nucleus","PubMed.ID":17380128,"subunits.Protein.name.":"Retinoblastoma-associated protein ;Transcription factor E2F1","subunits.Gene.name.":"RB1;E2F1","subunits.Gene.name.syn.":";RBBP3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The phosphorylation of pRB at Ser612 is induced by ATM-Chk1/2 kinase after DNA damage, leading to enhancement of the formation of a complex between pRB and E2F-1. It is proposed, that in asynchronously growing cells, pRB exists in a predominantly phosphorylated state, which is dissociated from E2F, allowing E2F-dependent transcription. DNA damage induces dephosphorylation of pRB at Cdk phosphorylation sites, leading to the complex pRB-E2F-1 being formed. DNA damage also activates ATM kinase and transduces signals to the checkpoint kinases Chk1 and Chk2. Activated Chk1 and Chk2 phosphorylate Ser612 of pRB and this phosphorylation enhances the formation of a complex between pRB and E2F-1, leading to repression of the transcriptional activity of E2F-1. Consequently, pRB-dependent cell cycle arrest and repression of apoptosis occur.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1251,"ComplexName":"BAF complex","Organism":"Human","Synonyms":"SWI/SNF-A complex","Cell.line":"None","subunits.UniProt.IDs.":"O14497;O96019;P51531;Q12824;Q8TAQ2;Q92922;Q969G3;Q96GM5","subunits.Entrez.IDs.":"8289;86;6595;6598;6601;6599;6605;6602","Protein.complex.purification.method":"MI:0071-molecular sieving","GO.ID":"GO:0006265;GO:0045893;GO:0003677;GO:0051276;GO:0005694","GO.description":"DNA topological change;positive regulation of transcription, DNA-templated;DNA binding;chromosome organization;chromosome","FunCat.ID":"10.01.09.05;11.02.03.04.01;16.03.01;42.10.03;70.10.03","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription activation;DNA binding;organization of chromosome structure;chromosome","PubMed.ID":12665591,"subunits.Protein.name.":"AT-rich interactive domain-containing protein 1A;Actin-like protein 6A;Probable global transcription activator SNF2L2;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;SWI/SNF complex subunit SMARCC2;SWI/SNF complex subunit SMARCC1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","subunits.Gene.name.":"ARID1A;ACTL6A;SMARCA2;SMARCB1;SMARCC2;SMARCC1;SMARCE1;SMARCD1","subunits.Gene.name.syn.":"BAF250 BAF250A C1orf4 OSA1 SMARCF1;BAF53 BAF53A INO80K;BAF190B, BRM, SNF2A, SNF2L2;BAF47, INI1, SNF5L1;BAF170;BAF155;BAF57;BAF60A","Disease.comment":"None","Subunits.comment":"Since the authors did not specify SMARCA, we used SMARCA2.","Complex.comment":"BAF complex belongs to chromatin remodeling complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1252,"ComplexName":"EBAFa complex","Organism":"Human","Synonyms":"ENL-associated BAF250a-containing SWI/SNF complex","Cell.line":"None","subunits.UniProt.IDs.":"O14497;O96019;P51532;Q03111;Q12824;Q8TAQ2;Q92922;Q92925;Q969G3;Q96GM5","subunits.Entrez.IDs.":"8289;86;6597;4298;6598;6601;6599;6603;6605;6602","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0071- molecular sieving","GO.ID":"GO:0006265;GO:0045893;GO:0003677;GO:0051276;GO:0005694","GO.description":"DNA topological change;positive regulation of transcription, DNA-templated;DNA binding;chromosome organization;chromosome","FunCat.ID":"10.01.09.05;11.02.03.04.01;16.03.01;42.10.03;70.10.03","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription activation;DNA binding;organization of chromosome structure;chromosome","PubMed.ID":12665591,"subunits.Protein.name.":"AT-rich interactive domain-containing protein 1A;Actin-like protein 6A;Transcription activator BRG1;Protein ENL;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;SWI/SNF complex subunit SMARCC2;SWI/SNF complex subunit SMARCC1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","subunits.Gene.name.":"ARID1A;ACTL6A;SMARCA4;MLLT1;SMARCB1;SMARCC2;SMARCC1;SMARCD2;SMARCE1;SMARCD1","subunits.Gene.name.syn.":"BAF250 BAF250A C1orf4 OSA1 SMARCF1;BAF53 BAF53A INO80K;BAF190A BRG1 SNF2B SNF2L4;ENL, LTG19, YEATS1;BAF47, INI1, SNF5L1;BAF170;BAF155;BAF60B;BAF57;BAF60A","Disease.comment":"None","Subunits.comment":"Three other subunits of the complex were found in the analysis, which have not been further characterized: EBAF140, EBAF100 and EBAF70.","Complex.comment":"ENL associates and cooperates with SWI/SNF complexes to activate transcription of the promoter of HoxA7, a downstream target essential for oncogenic activity of ENL.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1253,"ComplexName":"Ubiquitin E3 ligase (FBXW7, CUL1, SKP1A, RBX1)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62877;P63208;Q13616;Q969H0","subunits.Entrez.IDs.":"9978;6500;8454;55294","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511;GO:0007219;GO:0023052","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;Notch signaling pathway;signaling","FunCat.ID":"14.07.05;14.13.01.01;30.05.02.14;30.01","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway);Notch-receptor signalling pathway;cellular signalling","PubMed.ID":11565034,"subunits.Protein.name.":"E3 ubiquitin-protein ligase RBX1;S-phase kinase-associated protein 1;Cullin-1;F-box/WD repeat-containing protein 7","subunits.Gene.name.":"RBX1;SKP1;CUL1;FBXW7","subunits.Gene.name.syn.":"RNF75, ROC1;EMC19, OCP2, SKP1A, TCEB1L;None;FBW7, FBX30, SEL10","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. FBXW7 targets cyclin E, one of the activators of the cyclin-dependent kinase Cdk2 for proteolysis and is mutated in a breast cancer cell line.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1254,"ComplexName":"Menin-associated histone methyltransferase complex","Organism":"Human","Synonyms":"menin HMTase complex","Cell.line":"None","subunits.UniProt.IDs.":"O00255;P30876;P61964;Q15291;Q9C005;Q9UBL3;Q9UMN6","subunits.Entrez.IDs.":"4221;5431;11091;5929;84661;9070;None","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006265;GO:0006349;GO:0045893;GO:0018126;GO:0006479;GO:0051276;GO:0030154;GO:0005634","GO.description":"DNA topological change;regulation of gene expression by genetic imprinting;positive regulation of transcription, DNA-templated;protein hydroxylation;protein methylation;chromosome organization;cell differentiation;nucleus","FunCat.ID":"10.01.09.05;10.01.09.07;11.02.03.04.01;14.07.09;42.10.03;40.02;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);DNA imprinting and other epigenetic effects;transcription activation;posttranslational modification of amino acids (e.g. hydroxylation, methylation);organization of chromosome structure;cell differentiation;nucleus","PubMed.ID":14992727,"subunits.Protein.name.":"Menin;DNA-directed RNA polymerase II subunit RPB2 ;WD repeat-containing protein 5;Retinoblastoma-binding protein 5;Protein dpy-30 homolog;Set1/Ash2 histone methyltransferase complex subunit ASH2;Histone-lysine N-methyltransferase 2B","subunits.Gene.name.":"MEN1;POLR2B;WDR5;RBBP5;DPY30;ASH2L;KMT2B","subunits.Gene.name.syn.":"SCG2;;BIG3;RBQ3;None;ASH2L1;HRX2 KIAA0304 MLL2 MLL4 TRX2 WBP7","Disease.comment":"MEN1 gene is mutated in familial multiple endocrine neoplasia type 1.","Subunits.comment":"None","Complex.comment":"The menin-associated complex methylates histone H3 on lysine 4, suggesting menin activates the transcription of differentiation-regulating genes by covalent histone modification, and that this activity is related to tumor suppression by MEN1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1255,"ComplexName":"Ubiquitin E3 ligase (SIAH1, SIP, SKP1A, TBL1X)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60907;P63208;Q8IUQ4;Q9HB71","subunits.Entrez.IDs.":"6907;6500;6477;27101","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0018- two hybrid","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511;GO:0023052","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;signaling","FunCat.ID":"14.07.05;14.13.01.01;30.01","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway);cellular signalling","PubMed.ID":11389839,"subunits.Protein.name.":"F-box-like/WD repeat-containing protein TBL1X;S-phase kinase-associated protein 1;E3 ubiquitin-protein ligase SIAH1 ;Calcyclin-binding protein","subunits.Gene.name.":"TBL1X;SKP1;SIAH1;CACYBP","subunits.Gene.name.syn.":"TBL1;EMC19, OCP2, SKP1A, TCEB1L;HUMSIAH;S100A6BP SIP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Conditional degradation of beta-catenin represents a central event in the Wnt signaling pathways controlling cell fate and proliferation. A network of protein interactions in which Siah, SIP (a novel Siah-interacting protein), Skp1, and Ebi collaborate in a pathway controlling beta-catenin levels, affecting activity of beta-catenin-dependent Tcf/LEF transcription factors.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1256,"ComplexName":"MLL-HCF complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00255;P05546;P51610;P61964;Q03164;Q15291;Q9UBL3","subunits.Entrez.IDs.":"4221;3053;3054;11091;4297;5929;9070","Protein.complex.purification.method":"MI:0226- ion exchange chromatography; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006265;GO:0006349;GO:2001141;GO:0006355;GO:0018126;GO:0006479;GO:0051276;GO:0005634","GO.description":"DNA topological change;regulation of gene expression by genetic imprinting;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein hydroxylation;protein methylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;10.01.09.07;11.02.03.04;14.07.09;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);DNA imprinting and other epigenetic effects;transcriptional control;posttranslational modification of amino acids (e.g. hydroxylation, methylation);organization of chromosome structure;nucleus","PubMed.ID":15199122,"subunits.Protein.name.":"Menin;Heparin cofactor 2 ;Host cell factor 1;WD repeat-containing protein 5;Histone-lysine N-methyltransferase 2A;Retinoblastoma-binding protein 5;Set1/Ash2 histone methyltransferase complex subunit ASH2","subunits.Gene.name.":"MEN1;SERPIND1;HCFC1;WDR5;KMT2A;RBBP5;ASH2L","subunits.Gene.name.syn.":"SCG2;HCF2;HCF1, HFC1;BIG3;ALL1, CXXC7, HRX, HTRX, MLL, MLL1, TRX1;RBQ3;ASH2L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex links the menin tumor suppressor protein to the MLL histone methyltransferase machinery.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1257,"ComplexName":"ALL-1 supercomplex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00422;O60264;O60341;O75446;O94776;O95983;P20226;P21675;P49848;P51531;P61964;P62826;Q03164;Q09028;Q12824;Q12873;Q13547;Q15029;Q15291;Q16514;Q16576;Q16594;Q8TAQ2;Q92769;Q92797;Q92922;Q96ST3;Q9P2I0","subunits.Entrez.IDs.":"10284;8467;23028;8819;9219;53615;6908;6872;6878;6595;11091;5901;4297;5928;6598;1107;3065;9343;5929;6883;5931;6880;6601;3066;8189;6599;25942;53981","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0071- molecular sieving","GO.ID":"GO:0006265;GO:2001141;GO:0006355;GO:0006473;GO:0006476;GO:0018126;GO:0006479;GO:0051276;GO:0005634","GO.description":"DNA topological change;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;protein hydroxylation;protein methylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04;14.07.04;14.07.09;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcriptional control;modification by acetylation, deacetylation;posttranslational modification of amino acids (e.g. hydroxylation, methylation);organization of chromosome structure;nucleus","PubMed.ID":12453419,"subunits.Protein.name.":"Histone deacetylase complex subunit SAP18;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5;Lysine-specific histone demethylase 1A;Histone deacetylase complex subunit SAP30;Metastasis-associated protein MTA2;Methyl-CpG-binding domain protein 3;TATA-box-binding protein;Transcription initiation factor TFIID subunit 1;Transcription initiation factor TFIID subunit 6;Probable global transcription activator SNF2L2;WD repeat-containing protein 5;GTP-binding nuclear protein Ran;Histone-lysine N-methyltransferase 2A;Histone-binding protein RBBP4;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;Chromodomain-helicase-DNA-binding protein 3;Histone deacetylase 1;116 kDa U5 small nuclear ribonucleoprotein component ;Retinoblastoma-binding protein 5;Transcription initiation factor TFIID subunit 12;Histone-binding protein RBBP7;Transcription initiation factor TFIID subunit 9;SWI/SNF complex subunit SMARCC2;Histone deacetylase 2;Symplekin;SWI/SNF complex subunit SMARCC1;Paired amphipathic helix protein Sin3a;Cleavage and polyadenylation specificity factor subunit 2","subunits.Gene.name.":"SAP18;SMARCA5;KDM1A;SAP30;MTA2;MBD3;TBP;TAF1;TAF6;SMARCA2;WDR5;RAN;KMT2A;RBBP4;SMARCB1;CHD3;HDAC1;EFTUD2;RBBP5;TAF12;RBBP7;TAF9;SMARCC2;HDAC2;SYMPK;SMARCC1;SIN3A;CPSF2","subunits.Gene.name.syn.":"None;SNF2H WCRF135;AOF2 KDM1 KIAA0601 LSD1;None;MTA1L1 PID;None;GTF2D1 TF2D TFIID;BA2R CCG1 CCGS TAF2A;TAF2E TAFII70;BAF190B, BRM, SNF2A, SNF2L2;BIG3;ARA24;ALL1, CXXC7, HRX, HTRX, MLL, MLL1, TRX1;RBAP48;BAF47, INI1, SNF5L1;None;RPD3L1;KIAA0031 SNRP116;RBQ3;TAF15 TAF2J TAFII20;RBAP46;TAF2G TAFII31;BAF170;None;SPK;BAF155;None;CPSF100 KIAA1367","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The proteins associated with ALL-1 can be classified into eight groups.  (1) BRM, BAF170, BAF155, and INI1, the core components of the ATP-dependent SWI/SNF nucleosome remodeling complex,  (2) Mi2, MTA1-L1, HDAC1, HDAC2, RbAp46, RbAp48, MBD3, and KIAA0601, all components of the NuRD complex,  (3) Sin3A, SAP30, SAP18, HDAC1, HDAC2, RbAp48, and RbAp46, components of the histone deacetylase Sin3A complex,  (4) hSNF2H, homolog of ISWI, an ATP-dependent nucleosome remodeling and assembly factor,  (5) TAFII250, TAFII80, TAFII31, TAFII20, and TBP, components of the TFIID complex,  (6) RbBP5  and WDRP5, components of the yeast Set1 complex,  which methylates H3-K4.  (7) Proteins involved in RNA processing, CPSF, Symplekin and EFTUD2.  (8) Ran, which functions in nucleocytoplasmic transport and in spindle assembly during mitosis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1258,"ComplexName":"Ubiquitin E3 ligase (GLMN, FBXW8, SKP1A, RBX1)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62877;P63208;Q8N3Y1;Q92990","subunits.Entrez.IDs.":"9978;6500;26259;11146","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511;GO:0001570","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;vasculogenesis","FunCat.ID":"14.07.05;14.13.01.01;47.03.03","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway);vascular organs","PubMed.ID":12904573,"subunits.Protein.name.":"E3 ubiquitin-protein ligase RBX1;S-phase kinase-associated protein 1;F-box/WD repeat-containing protein 8;Glomulin","subunits.Gene.name.":"RBX1;SKP1;FBXW8;GLMN","subunits.Gene.name.syn.":"RNF75, ROC1;EMC19, OCP2, SKP1A, TCEB1L;FBW6 FBW8 FBX29 FBXO29 FBXW6;FAP48 FAP68 VMGLOM","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Experiments suggest that ubiquitin E3 ligase (containing GLMN, FBXW8, SKP1A and RBX1) plays an important role in vascular morphogenesis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1259,"ComplexName":"Chromatin assembly complex (CAF-1 complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q09028;Q13111;Q13112","subunits.Entrez.IDs.":"5928;10036;8208","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006260;GO:0006265;GO:0000084;GO:0051276;GO:0005634","GO.description":"DNA replication;DNA topological change;mitotic S phase;chromosome organization;nucleus","FunCat.ID":"10.01.03;10.01.09.05;10.03.01.01.05;42.10.03;70.10","FunCat.description":"DNA synthesis and replication;DNA conformation modification (e.g. chromatin);S phase of mitotic cell cycle;organization of chromosome structure;nucleus","PubMed.ID":7600578,"subunits.Protein.name.":"Histone-binding protein RBBP4;Chromatin assembly factor 1 subunit A ;Chromatin assembly factor 1 subunit B","subunits.Gene.name.":"RBBP4;CHAF1A;CHAF1B","subunits.Gene.name.syn.":"RBAP48;CAF CAF1P150;CAF1A CAF1P60 MPHOSPH7 MPP7","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Caf-1 complex assembles nucleosomes in a replication-dependent manner.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1260,"ComplexName":"Neddylin ligase (FBXO11, SKP1, CUL1, RBX1)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62877;P63208;Q13616;Q86XK2","subunits.Entrez.IDs.":"9978;6500;8454;80204","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0000338;GO:0016925;GO:0016926;GO:0045116;GO:0019951;GO:0006464;GO:0051090;GO:0005634","GO.description":"protein deneddylation;protein sumoylation;protein desumoylation;protein neddylation;Smt3-protein conjugation;cellular protein modification process;regulation of sequence-specific DNA binding transcription factor activity;nucleus","FunCat.ID":"14.07.07;14.07;18.02.09;70.10","FunCat.description":"modification by ubiquitin-related proteins;protein modification;regulator of transcription factor;nucleus","PubMed.ID":17098746,"subunits.Protein.name.":"E3 ubiquitin-protein ligase RBX1;S-phase kinase-associated protein 1;Cullin-1;F-box only protein 11","subunits.Gene.name.":"RBX1;SKP1;CUL1;FBXO11","subunits.Gene.name.syn.":"RNF75, ROC1;EMC19, OCP2, SKP1A, TCEB1L;None;FBX11 PRMT9 VIT1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"FBXO11 promotes the neddylation of p53 and inhibits its transcriptional activity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1261,"ComplexName":"SRm160/300 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P08621;P09661;P62995;Q8IYB3;Q9UQ35","subunits.Entrez.IDs.":"6625;6627;6434;10250;23524","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008380;GO:0003723;GO:0005634","GO.description":"RNA splicing;RNA binding;nucleus","FunCat.ID":"11.04.03.01;16.03.03;70.10","FunCat.description":"splicing;RNA binding;nucleus","PubMed.ID":10339552,"subunits.Protein.name.":"U1 small nuclear ribonucleoprotein 70 kDa ;U2 small nuclear ribonucleoprotein A' ;Transformer-2 protein homolog beta;Serine/arginine repetitive matrix protein 1 ;Serine/arginine repetitive matrix protein 2","subunits.Gene.name.":"SNRNP70;SNRPA1;TRA2B;SRRM1;SRRM2","subunits.Gene.name.syn.":"RNPU1Z RPU1 SNRP70 U1AP1;;SFRS10;SRM160;KIAA0324 SRL300 SRM300","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Exonic splicing enhancer (ESE) sequences are important for the recognition of splice sites in pre-mRNA. These sequences are bound by specific serine-arginine (SR) repeat proteins that promote the assembly of splicing complexes at adjacent splice sites. In a study, it was shown that SRm160/300 is required for a purine-rich ESE to promote the splicing of a pre-mRNA derived from the Drosophila doublesex gene. Results suggest a model for ESE function in which the SRm160/300 splicing coactivator promotes critical interactions between ESE-bound activators and the snRNP machinery of the spliceosome.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1287,"ComplexName":"HNRPF-HNRPH1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P31943;P52597","subunits.Entrez.IDs.":"3187;3185","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008380;GO:0003723;GO:0005634","GO.description":"RNA splicing;RNA binding;nucleus","FunCat.ID":"11.04.03.01;16.03.03;70.10","FunCat.description":"splicing;RNA binding;nucleus","PubMed.ID":9858532,"subunits.Protein.name.":"Heterogeneous nuclear ribonucleoprotein H ;Heterogeneous nuclear ribonucleoprotein F","subunits.Gene.name.":"HNRNPH1;HNRNPF","subunits.Gene.name.syn.":"HNRPH HNRPH1;HNRPF","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The complex is involved in alternative splicing.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1288,"ComplexName":"DCS complex (PTBP1, PTBP2, HNRPH1, HNRPF)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P26599;P31943;P52597;Q9UKA9","subunits.Entrez.IDs.":"5725;3187;3185;58155","Protein.complex.purification.method":"MI:0226- ion exchange chromatography; MI:0019- coimmunoprecipitation; MI:0004- affinity chromatography technologies","GO.ID":"GO:0043484;GO:0048024;GO:0003723;GO:0005634","GO.description":"regulation of RNA splicing;regulation of mRNA splicing, via spliceosome;RNA binding;nucleus","FunCat.ID":"11.04.03.01.10;16.03.03;70.10","FunCat.description":"regulation of splicing;RNA binding;nucleus","PubMed.ID":11003644,"subunits.Protein.name.":"Polypyrimidine tract-binding protein 1 ;Heterogeneous nuclear ribonucleoprotein H ;Heterogeneous nuclear ribonucleoprotein F ;Polypyrimidine tract-binding protein 2","subunits.Gene.name.":"PTBP1;HNRNPH1;HNRNPF;PTBP2","subunits.Gene.name.syn.":"PTB;HNRPH HNRPH1;HNRPF;NPTB PTB PTBLP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1293,"ComplexName":"IPO13-RBM8A-MAGOH complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O94829;P61326;Q9Y5S9","subunits.Entrez.IDs.":"9670;4116;9939","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0050658;GO:0051033;GO:0051169;GO:0005634","GO.description":"RNA transport;RNA transmembrane transporter activity;nuclear transport;nucleus","FunCat.ID":"20.01.21;20.09.01;70.10","FunCat.description":"RNA transport;nuclear transport;nucleus","PubMed.ID":11447110,"subunits.Protein.name.":"Importin-13 ;Protein mago nashi homolog;RNA-binding protein 8A","subunits.Gene.name.":"IPO13;MAGOH;RBM8A","subunits.Gene.name.syn.":"KIAA0724 RANBP13;MAGOHA;RBM8, Y14","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1296,"ComplexName":"DCP1A-DCP2 Decapping complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q8IU60;Q9NPI6","subunits.Entrez.IDs.":"167227;55802","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006401;GO:0005737","GO.description":"RNA catabolic process;cytoplasm","FunCat.ID":"01.03.16.01;70.03","FunCat.description":"RNA degradation;cytoplasm","PubMed.ID":12417715,"subunits.Protein.name.":"m7GpppN-mRNA hydrolase ;mRNA-decapping enzyme 1A","subunits.Gene.name.":"DCP2;DCP1A","subunits.Gene.name.syn.":"NUDT20;SMIF","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Although the authors suggest the existence of a protein complex containing DCP proteins and UPF proteins they also state that there is currently no direct evidence for the significance of a strong interaction between hUpf1 and hDcp proteins.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1297,"ComplexName":"MKK4-ARRB2-ASK1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P32121;P45985;Q99683","subunits.Entrez.IDs.":"409;6416;4217","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007254;GO:0000165","GO.description":"JNK cascade;MAPK cascade","FunCat.ID":"30.01.05.01.02;30.01.05.01.03","FunCat.description":"JNK cascade;MAPKKK cascade","PubMed.ID":11090355,"subunits.Protein.name.":"Beta-arrestin-2;Dual specificity mitogen-activated protein kinase kinase 4 ;Mitogen-activated protein kinase kinase kinase 5","subunits.Gene.name.":"ARRB2;MAP2K4;MAP3K5","subunits.Gene.name.syn.":"ARB2, ARR2;JNKK1 MEK4 MKK4 PRKMK4 SEK1 SERK1 SKK1;ASK1 MAPKKK5 MEKK5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The data suggest that ASK1 binds directly to beta -arrestin 2, and MKK4 interacts indirectly with beta -arrestin 2 via ASK1 or JNK3, thus forming a complete MAPK module.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1298,"ComplexName":"MKK4-ARRB2-JNK3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P32121;P45985;P53779","subunits.Entrez.IDs.":"409;6416;5602","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007254;GO:0000165","GO.description":"JNK cascade;MAPK cascade","FunCat.ID":"30.01.05.01.02;30.01.05.01.03","FunCat.description":"JNK cascade;MAPKKK cascade","PubMed.ID":11090355,"subunits.Protein.name.":"Beta-arrestin-2;Dual specificity mitogen-activated protein kinase kinase 4 ;Mitogen-activated protein kinase 10","subunits.Gene.name.":"ARRB2;MAP2K4;MAPK10","subunits.Gene.name.syn.":"ARB2, ARR2;JNKK1 MEK4 MKK4 PRKMK4 SEK1 SERK1 SKK1;JNK3 JNK3A PRKM10 SAPK1B","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The data suggest that ASK1 binds directly to beta -arrestin 2, and MKK4 interacts indirectly with beta -arrestin 2 via ASK1 or JNK3, thus forming a complete MAPK module.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1299,"ComplexName":"POSH-MLK3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q16584;Q7Z6J0","subunits.Entrez.IDs.":"4296;57630","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007254","GO.description":"JNK cascade","FunCat.ID":"30.01.05.01.02","FunCat.description":"JNK cascade","PubMed.ID":14504284,"subunits.Protein.name.":"Mitogen-activated protein kinase kinase kinase 11 ;E3 ubiquitin-protein ligase SH3RF1","subunits.Gene.name.":"MAP3K11;SH3RF1","subunits.Gene.name.syn.":"MLK3 PTK1 SPRK;KIAA1494 POSH RNF142 SH3MD2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"A POSH mutant unable to bind to Akt2 exhibits increased binding to MLK3. This increased binding of MLK3 to POSH is accompanied by increased activation of the JNK signaling pathway.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1300,"ComplexName":"CRLR-RAMP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"O60894;Q16602","subunits.Entrez.IDs.":"10267;10203","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007186;GO:0005886","GO.description":"G-protein coupled receptor signaling pathway;plasma membrane","FunCat.ID":"30.05.02.24;70.02","FunCat.description":"G-protein coupled receptor signalling pathway;eukaryotic plasma membrane / membrane attached","PubMed.ID":11387328,"subunits.Protein.name.":"Receptor activity-modifying protein 1 ;Calcitonin gene-related peptide type 1 receptor","subunits.Gene.name.":"RAMP1;CALCRL","subunits.Gene.name.syn.":";CGRPR","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results demonstrate that RAMP2 and RAMP3 and not only RAMP1 can promote the full maturation of CRLR, leading to its terminal glycosylation, and only the fully processed receptors were found to bind AM (adrenomedullin) and CGRP (calcitonin gene-related peptide).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1301,"ComplexName":"CRLR-RAMP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"O60894;Q16602","subunits.Entrez.IDs.":"10267;10203","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0054- fluorescence-activated cell sorting","GO.ID":"GO:0007186;GO:0005886","GO.description":"G-protein coupled receptor signaling pathway;plasma membrane","FunCat.ID":"30.05.02.24;70.02","FunCat.description":"G-protein coupled receptor signalling pathway;eukaryotic plasma membrane / membrane attached","PubMed.ID":11535606,"subunits.Protein.name.":"Receptor activity-modifying protein 1 ;Calcitonin gene-related peptide type 1 receptor","subunits.Gene.name.":"RAMP1;CALCRL","subunits.Gene.name.syn.":";CGRPR","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"When RAMP1 is expressed with CRLR, it is targeted to the cell surface as a heterodimer. CGRP (calcitonin gene-related peptide) binding and receptor activation lead to the phosphorylation of CRLR and the internalization of the receptor as a stable complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1306,"ComplexName":"PIN1-AUF1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q13526;Q14103","subunits.Entrez.IDs.":"5300;3184","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005125;GO:0005737","GO.description":"cytokine activity;cytoplasm","FunCat.ID":"40.02.03.01;70.03","FunCat.description":"cytokines (interleukines, colony stimulating factors, etc.);cytoplasm","PubMed.ID":16273101,"subunits.Protein.name.":"Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1;Heterogeneous nuclear ribonucleoprotein D0","subunits.Gene.name.":"PIN1;HNRNPD","subunits.Gene.name.syn.":"None;AUF1 HNRPD","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Immunoprecipitation of eosinophil cytoplasmic lysates demonstrated an interaction between Pin1 and all four AUF1 isoforms.Pin1 regulated the association of the AU-rich element\\u2013binding proteins AUF1 and hnRNP C with GM-CSF mRNA, accelerating or slowing decay, respectively.The authors propose that moderately serine-phosphorylated p40 and p45 AUF1, in physical association with serine-phosphorylated Pin1 and unphosphorylated p42 and p37 AUF1, form a ribonucleoprotein complex with GM-CSF mRNA in resting eosinophils.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1307,"ComplexName":"Multiprotein complex (mRNA turnover)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60506;O75534;P11940;Q14103;Q9H074","subunits.Entrez.IDs.":"10492;7812;26986;3184;10605","Protein.complex.purification.method":"MI:0029-cosedimentation through density gradients;MI:0047-far western blotting","GO.ID":"GO:0006401;GO:0005737","GO.description":"RNA catabolic process;cytoplasm","FunCat.ID":"01.03.16.01;70.03","FunCat.description":"RNA degradation;cytoplasm","PubMed.ID":11051545,"subunits.Protein.name.":"Heterogeneous nuclear ribonucleoprotein Q;Cold shock domain-containing protein E1;Polyadenylate-binding protein 1;Heterogeneous nuclear ribonucleoprotein D0;Polyadenylate-binding protein-interacting protein 1","subunits.Gene.name.":"SYNCRIP;CSDE1;PABPC1;HNRNPD;PAIP1","subunits.Gene.name.syn.":"HNRPQ NSAP1;D1S155E KIAA0885 NRU UNR;PAB1 PABP1 PABPC2;AUF1 HNRPD;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1308,"ComplexName":"PABPC1-HSPA8-HNRPD-EIF4G1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P11142;P11940;Q04637;Q14103;Q59EJ3","subunits.Entrez.IDs.":"3312;26986;1981;3184;3303","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006401","GO.description":"RNA catabolic process","FunCat.ID":"01.03.16.01","FunCat.description":"RNA degradation","PubMed.ID":10205060,"subunits.Protein.name.":"Heat shock cognate 71 kDa protein;Polyadenylate-binding protein 1;Eukaryotic translation initiation factor 4 gamma 1;Heterogeneous nuclear ribonucleoprotein D0;Heat shock 70kDa protein 1A variant","subunits.Gene.name.":"HSPA8;PABPC1;EIF4G1;HNRNPD;","subunits.Gene.name.syn.":"HSC70, HSP73, HSPA10;PAB1 PABP1 PABPC2;EIF4F EIF4G EIF4GI;AUF1 HNRPD;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cytokine and proto-oncogene messenger RNAs (mRNAs) are rapidly degraded through AU-rich elements in the 39 untranslated region. Rapid decay involves AU-rich binding protein AUF1, which complexes with heat shock proteins hsc70-hsp70, translation initiation factor eIF4G, and poly(A) binding protein.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1310,"ComplexName":"Rab27a-Mlph-Myo5a complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q91V27;Q99104;Q9ERI2","subunits.Entrez.IDs.":"171531;17918;11891","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0018- two hybrid","GO.ID":"GO:0015031;GO:0008565","GO.description":"protein transport;protein transporter activity","FunCat.ID":"20.01.10","FunCat.description":"protein transport","PubMed.ID":11980908,"subunits.Protein.name.":"Melanophilin ;Unconventional myosin-Va ;Ras-related protein Rab-27A","subunits.Gene.name.":"Mlph;Myo5a;Rab27a","subunits.Gene.name.syn.":"Ln Slac2a;Dilute;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The melanophilin interacts with Rab27a and myosin Va on melanosomes in melanocytes. The melanophilin can associate simultaneously with activated Rab27a and myosin Va via distinct regions, and serve as a linker between these proteins (PMID:11980908).","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1317,"ComplexName":"ATF7-TAF12 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P17544;Q16514","subunits.Entrez.IDs.":"11016;6883","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0045893","GO.description":"positive regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.01","FunCat.description":"transcription activation","PubMed.ID":15735663,"subunits.Protein.name.":"Cyclic AMP-dependent transcription factor ATF-7 ;Transcription initiation factor TFIID subunit 12","subunits.Gene.name.":"ATF7;TAF12","subunits.Gene.name.syn.":"ATFA;TAF15 TAF2J TAFII20","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The overexpression of hsTAF12 potentiates ATF7-induced transcriptional activation through direct interaction with ATF7, suggesting that TAF12 is a functional partner of ATF7. Although both TAF12 isoforms (TAF12-1 and -2, formerly TAF(II)20 and TAF(II)15) interact with the ATF7 activation region through their histone-fold domain, only the largest, hsTAF12-1, mediates transcriptional activation through its N-terminal region.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1318,"ComplexName":"Transcription initiation factor complex (TAF1, TAF5, TAF11, TAF12, TBP)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P20226;P21675;Q15542;Q15544;Q16514","subunits.Entrez.IDs.":"6908;6872;6877;6882;6883","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006352","GO.description":"DNA-templated transcription, initiation","FunCat.ID":"11.02.03.01.01","FunCat.description":"transcription initiation","PubMed.ID":9045704,"subunits.Protein.name.":"TATA-box-binding protein;Transcription initiation factor TFIID subunit 1;Transcription initiation factor TFIID subunit 5;Transcription initiation factor TFIID subunit 11;Transcription initiation factor TFIID subunit 12","subunits.Gene.name.":"TBP;TAF1;TAF5;TAF11;TAF12","subunits.Gene.name.syn.":"GTF2D1 TF2D TFIID;BA2R CCG1 CCGS TAF2A;TAF2D;TAF2I;TAF15 TAF2J TAFII20","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Human transcription initiation factor TFIID contains the TATA-binding protein (TBP) and several TBP-associated factors (TAFs). The authors suggest that hTAFII100 may help stabilize interactions of the histonelike TAFs, perhaps within an octamer structure.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1321,"ComplexName":"Transcription initiation factor complex (TAF5, TAF6, TAF9, TAF11, TBP)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P20226;P49848;Q15542;Q15544;Q16594","subunits.Entrez.IDs.":"6908;6878;6877;6882;6880","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006352","GO.description":"DNA-templated transcription, initiation","FunCat.ID":"11.02.03.01.01","FunCat.description":"transcription initiation","PubMed.ID":9045704,"subunits.Protein.name.":"TATA-box-binding protein;Transcription initiation factor TFIID subunit 6;Transcription initiation factor TFIID subunit 5;Transcription initiation factor TFIID subunit 11;Transcription initiation factor TFIID subunit 9","subunits.Gene.name.":"TBP;TAF6;TAF5;TAF11;TAF9","subunits.Gene.name.syn.":"GTF2D1 TF2D TFIID;TAF2E TAFII70;TAF2D;TAF2I;TAF2G TAFII31","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Human transcription initiation factor TFIID contains the TATA-binding protein (TBP) and several TBP-associated factors (TAFs). The authors suggest that hTAFII100 may help stabilize interactions of the histonelike TAFs, perhaps within an octamer structure.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1332,"ComplexName":"Large Drosha complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00571;O14979;O43143;P17844;P31943;P35637;P52272;Q00839;Q01844;Q12905;Q12906;Q13148;Q8WYQ5;Q92499;Q92804;Q92841;Q96SB4;Q9BUJ2;Q9NRR4;Q9UKM9","subunits.Entrez.IDs.":"1654;9987;1665;1655;3187;2521;4670;3192;2130;3608;3609;23435;54487;1653;8148;10521;6732;11100;29102;22913","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation; MI:0071- molecular sieving","GO.ID":"GO:0006396;GO:0003723;GO:0005634","GO.description":"RNA processing;RNA binding;nucleus","FunCat.ID":"11.04;16.03.03;70.10","FunCat.description":"RNA processing;RNA binding;nucleus","PubMed.ID":15531877,"subunits.Protein.name.":"ATP-dependent RNA helicase DDX3X ;Heterogeneous nuclear ribonucleoprotein D-like ;Pre-mRNA-splicing factor ATP-dependent RNA helicase DHX15 ;Probable ATP-dependent RNA helicase DDX5 ;Heterogeneous nuclear ribonucleoprotein H ;RNA-binding protein FUS ;Heterogeneous nuclear ribonucleoprotein M ;Heterogeneous nuclear ribonucleoprotein U ;RNA-binding protein EWS ;Interleukin enhancer-binding factor 2 ;Interleukin enhancer-binding factor 3 ;TAR DNA-binding protein 43 ;Microprocessor complex subunit DGCR8 ;ATP-dependent RNA helicase DDX1 ;TATA-binding protein-associated factor 2N ;Probable ATP-dependent RNA helicase DDX17 ;SRSF protein kinase 1 ;Heterogeneous nuclear ribonucleoprotein U-like protein 1 ;Ribonuclease 3 ;RNA-binding protein Raly","subunits.Gene.name.":"DDX3X;HNRNPDL;DHX15;DDX5;HNRNPH1;FUS;HNRNPM;HNRNPU;EWSR1;ILF2;ILF3;TARDBP;DGCR8;DDX1;TAF15;DDX17;SRPK1;HNRNPUL1;DROSHA;RALY","subunits.Gene.name.syn.":"DBX DDX3;HNRPDL JKTBP;DBP1 DDX15;G17P1 HELR HLR1;HNRPH HNRPH1;TLS;HNRPM NAGR1;HNRPU SAFA U21.1;EWS;NF45;DRBF MPHOSPH4 NF90;TDP43;C22orf12 DGCRK6;;RBP56 TAF2N;;;E1BAP5 HNRPUL1;RN3 RNASE3L RNASEN;HNRPCL2 P542","Disease.comment":"DGCR8 is deleted in DiGeorge syndrome. EWS is involved in Ewing's sarcoma disease.","Subunits.comment":"None","Complex.comment":"The large Drosha complex shows only weak pri-miRNA processing activity. It might be involved in pri-ribosomal RNA processing.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1335,"ComplexName":"SNW1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75643;O95071;P07437;P11021;P17858;P23246;P26641;P43243;P43246;P68104;Q00839;Q13573;Q15029;Q16531;Q6P2Q9;Q99459;Q9BUQ8;Q9UG63","subunits.Entrez.IDs.":"23020;51366;203068;3309;5211;6421;1937;9782;4436;1915;3192;22938;9343;1642;10594;988;9416;10061","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045893;GO:0008380;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;RNA splicing;nucleus","FunCat.ID":"11.02.03.04.01;11.04.03.01;70.10","FunCat.description":"transcription activation;splicing;nucleus","PubMed.ID":12840015,"subunits.Protein.name.":"U5 small nuclear ribonucleoprotein 200 kDa helicase ;E3 ubiquitin-protein ligase UBR5 ;Tubulin beta chain;78 kDa glucose-regulated protein;ATP-dependent 6-phosphofructokinase, liver type ;Splicing factor, proline- and glutamine-rich ;Elongation factor 1-gamma ;Matrin-3;DNA mismatch repair protein Msh2 ;Elongation factor 1-alpha 1 ;Heterogeneous nuclear ribonucleoprotein U ;SNW domain-containing protein 1 ;116 kDa U5 small nuclear ribonucleoprotein component ;DNA damage-binding protein 1;Pre-mRNA-processing-splicing factor 8 ;Cell division cycle 5-like protein ;Probable ATP-dependent RNA helicase DDX23 ;ATP-binding cassette sub-family F member 2","subunits.Gene.name.":"SNRNP200;UBR5;TUBB;HSPA5;PFKL;SFPQ;EEF1G;MATR3;MSH2;EEF1A1;HNRNPU;SNW1;EFTUD2;DDB1;PRPF8;CDC5L;DDX23;ABCF2","subunits.Gene.name.syn.":"ASCC3L1 HELIC2 KIAA0788;EDD EDD1 HYD KIAA0896;TUBB5;GRP78;;PSF;EF1G;KIAA0723;;EEF1A EF1A LENG7;HNRPU SAFA U21.1;SKIIP SKIP;KIAA0031 SNRP116;XAP1;PRPC8;KIAA0432 PCDC5RP;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Identified subunits of the SNW1 complex represent components of the spliceosome as well as other nuclear matrix-associated proteins. Evidence was found that the complex couples vitamin D receptor-mediated transcription and RNA splicing.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1338,"ComplexName":"FOXO3-PCAF complex, oxidative stress stimulated","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43524;Q92831","subunits.Entrez.IDs.":"2309;8850","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0000302;GO:0006979;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;response to reactive oxygen species;response to oxidative stress;nucleus","FunCat.ID":"11.02.03.04;32.01.01;70.10","FunCat.description":"transcriptional control;oxidative stress response;nucleus","PubMed.ID":14976264,"subunits.Protein.name.":"Forkhead box protein O3;Histone acetyltransferase KAT2B","subunits.Gene.name.":"FOXO3;KAT2B","subunits.Gene.name.syn.":"FKHRL1, FOXO3A;PCAF","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1345,"ComplexName":"Septin complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q15019;Q16181;Q92599;Q9NVA2;Q9UHD8","subunits.Entrez.IDs.":"4735;989;23176;55752;10801","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0030037;GO:0007114","GO.description":"actin filament reorganization involved in cell cycle;cell budding","FunCat.ID":"10.03.05.03;43.01.03.05","FunCat.description":"cell cycle dependent actin filament reorganization;budding, cell polarity and filament formation","PubMed.ID":15485874,"subunits.Protein.name.":"Septin-2 ;Septin-7 ;Septin-8;Septin-11;Septin-9","subunits.Gene.name.":"SEPT2;SEPT7;SEPT8;SEPT11;SEPT9","subunits.Gene.name.syn.":"DIFF6 KIAA0158 NEDD5;CDC10;KIAA0202;;KIAA0991 MSF","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Septins are members of a conserved family of cytoskeletal GTPases, filament-forming and cell division cycle regulatory proteins.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1347,"ComplexName":"NPC subcomplex (NUP98, NUP107, NUP133, NUP160)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P52948;P57740;Q12769;Q8WUM0","subunits.Entrez.IDs.":"4928;57122;23279;55746","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0000278;GO:0015031;GO:0008565;GO:0006810;GO:0051169;GO:0000775","GO.description":"mitotic cell cycle;protein transport;protein transporter activity;transport;nuclear transport;chromosome, centromeric region","FunCat.ID":"10.03.01.01;20.01.10;20;20.09.01;70.10.04","FunCat.description":"mitotic cell cycle;protein transport;CELLULAR TRANSPORT, TRANSPORT FACILITIES AND TRANSPORT ROUTES;nuclear transport;centromere / kinetochore","PubMed.ID":11564755,"subunits.Protein.name.":"Nuclear pore complex protein Nup98-Nup96 [Cleaved into: Nuclear pore complex protein Nup98;Nuclear pore complex protein Nup107;Nuclear pore complex protein Nup160;Nuclear pore complex protein Nup133","subunits.Gene.name.":"NUP98;NUP107;NUP160;NUP133","subunits.Gene.name.syn.":"ADAR2;None;KIAA0197 NUP120;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"All trafficking of macromolecules between the cytoplasm and the nucleus occurs through nuclear pore complexes (NPCs), which are supramolecular assemblies at points of fusion between the inner and outer nuclear membranes. NPCs are composed of an eightfold symmetric spoke-ring complex, cytoplasmic fibers, and a nuclear basket. NUP133 and NUP107 are localized on both sides of the NPC to which they are stably associated at interphase and remain associated as part of a NPC subcomplex during mitosis.They are targeted at early stages to the reforming nuclear envelope.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1348,"ComplexName":"GLE1-NUPL2-NUP155 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15504;O75694;Q53GS7","subunits.Entrez.IDs.":"11097;9631;2733","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006886;GO:0006605;GO:0015031","GO.description":"intracellular protein transport;protein targeting;protein transport","FunCat.ID":"14.04;20.01.10","FunCat.description":"protein targeting, sorting and translocation;protein transport","PubMed.ID":16000379,"subunits.Protein.name.":"Nucleoporin-like protein 2 ;Nuclear pore complex protein Nup155 ;Nucleoporin GLE1","subunits.Gene.name.":"NUPL2;NUP155;GLE1","subunits.Gene.name.syn.":"CG1;KIAA0791;GLE1L","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1352,"ComplexName":"ING4 complex (ING4, MYST2, C1orf149, PHF17)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95251;Q6IE81;Q9HAF1;Q9UNL4","subunits.Entrez.IDs.":"11143;79960;64769;51147","Protein.complex.purification.method":"MI:0069- mass spectrometry studies of complexes; MI:0004- affinity chromatography technologies","GO.ID":"GO:0000278;GO:0051726;GO:0001525","GO.description":"mitotic cell cycle;regulation of cell cycle;angiogenesis","FunCat.ID":"10.03.01.01;10.03.01;41.05.16","FunCat.description":"mitotic cell cycle;mitotic cell cycle and cell cycle control;angiogenesis","PubMed.ID":16387653,"subunits.Protein.name.":"Histone acetyltransferase KAT7 ;Protein Jade-1 ;Chromatin modification-related protein MEAF6;Inhibitor of growth protein 4","subunits.Gene.name.":"KAT7;JADE1;MEAF6;ING4","subunits.Gene.name.syn.":"HBO1 HBOa MYST2;KIAA1807 PHF17;C1orf149 CENP-28 EAF6;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"ING4 associates with the HBO1 HAT required for normal progression through S phase and the majority of histone H4 acetylation in vivo. ING subunits are probably crucial for acetylation of chromatin substrates.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1371,"ComplexName":"Gata1-Tal1-Tcf3-Lmo2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P15806;P17679;P22091;P25801","subunits.Entrez.IDs.":"21423;14460;21349;16909","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0018- two hybrid","GO.ID":"GO:2001141;GO:0006355;GO:0030218;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;erythrocyte differentiation;nucleus","FunCat.ID":"11.02.03.04;43.03.07;70.10","FunCat.description":"transcriptional control;blood cell;nucleus","PubMed.ID":7568177,"subunits.Protein.name.":"Transcription factor E2-alpha ;Erythroid transcription factor ;T-cell acute lymphocytic leukemia protein 1 homolog ;Rhombotin-2","subunits.Gene.name.":"Tcf3;Gata1;Tal1;Lmo2","subunits.Gene.name.syn.":"Alf2 Me2 Tcfe2a;Gf-1;Scl Tal-1;Rbtn-2 Rbtn2 Rhom-2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complexes involving RBTN2, TAL1, and GATA1 (or -2), together with E47, the basic helix-loop-helix heterodimerization partner of TAL1, could be demonstrated. Thus, a molecular link exists between three proteins crucial for erythropoiesis, and the data suggest that variations in amounts of complexes involving RBTN2, TAL1, and GATA1 (or -2) could be important for erythroid differentiation.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1372,"ComplexName":"Rb-tal-1-E2A-Lmo2-Ldb1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06400;P15923;P17542;P25791;Q86U70","subunits.Entrez.IDs.":"5925;6929;6886;4005;8861","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0045892;GO:0030218;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;erythrocyte differentiation;nucleus","FunCat.ID":"11.02.03.04.03;43.03.07;70.10","FunCat.description":"transcription repression;blood cell;nucleus","PubMed.ID":10866689,"subunits.Protein.name.":"Retinoblastoma-associated protein ;Transcription factor E2-alpha ;T-cell acute lymphocytic leukemia protein 1 ;Rhombotin-2 ;LIM domain-binding protein 1","subunits.Gene.name.":"RB1;TCF3;TAL1;LMO2;LDB1","subunits.Gene.name.syn.":";BHLHB21 E2A ITF1;BHLHA17 SCL TCL5;RBTN2 RBTNL1 RHOM2 TTG2;CLIM2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Data indicate that this pentameric complex assembled in maturing erythroblasts plays an important regulatory role in c-kit downmodulation; hypothetically, the complex may regulate the expression of other critical erythroid genes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1373,"ComplexName":"Ldb1-Lmo2-Gata-1-Tal1-E47 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P15806;P17679;P22091;P25801;P70662","subunits.Entrez.IDs.":"21423;14460;21349;16909;16825","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0030218;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;erythrocyte differentiation;nucleus","FunCat.ID":"11.02.03.04;16.03.01;43.03.07;70.10","FunCat.description":"transcriptional control;DNA binding;blood cell;nucleus","PubMed.ID":9214632,"subunits.Protein.name.":"Transcription factor E2-alpha ;Erythroid transcription factor ;T-cell acute lymphocytic leukemia protein 1 homolog ;Rhombotin-2 ;LIM domain-binding protein 1","subunits.Gene.name.":"Tcf3;Gata1;Tal1;Lmo2;Ldb1","subunits.Gene.name.syn.":"Alf2 Me2 Tcfe2a;Gf-1;Scl Tal-1;Rbtn-2 Rbtn2 Rhom-2;Nli","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In erythroid cells Lmo2 forms a novel DNA-binding complex, with GATA-1, TAL1 and E2A, and the recently identified LIM-binding protein Ldb1/NLI. This oligomeric complex binds to a unique, bipartite DNA motif comprising an E-box, CAGGTG, followed approximately 9 bp downstream by a GATA site. The protein complex may play a role in haematopoiesis.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1375,"ComplexName":"Pyruvate dehydrogenase complex","Organism":"Bovine","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P08559;P09622;P11180;P11966;P22439","subunits.Entrez.IDs.":"5160;1738;512723;613610;None","Protein.complex.purification.method":"MI:0401- biochemical","GO.ID":"GO:0008152;GO:0045254;GO:0005739","GO.description":"metabolic process;pyruvate dehydrogenase complex;mitochondrion","FunCat.ID":"01;02.08;70.16","FunCat.description":"METABOLISM;pyruvate dehydrogenase complex;mitochondrion","PubMed.ID":14638692,"subunits.Protein.name.":"Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial ;Dihydrolipoyl dehydrogenase, mitochondrial ;Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex ;Pyruvate dehydrogenase E1 component subunit beta, mitochondrial ;Pyruvate dehydrogenase protein X component","subunits.Gene.name.":"PDHA1;DLD;DLAT;PDHB;PDHX","subunits.Gene.name.syn.":"PHE1A;GCSL LAD PHE3;;;PDX1","Disease.comment":"None","Subunits.comment":"Since bovine Pdha1 and Dld were not available in the UniProt database at the time of annotation, the orthologous human proteins were used.","Complex.comment":"The mitochondrial pyruvate dehydrogenase complex (PDC)1 catalyzes the irreversible conversion of pyruvate to acetyl-CoA along with the reduction of NAD+. PDCs from all known sources contain the pyruvate dehydrogenase (E1), the dihydrolipoyl acetyltransferase (E2), and the dihydrolipoyl dehydrogenase (E3) components.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":1377,"ComplexName":"hASC-1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q15650;Q8N3C0;Q8N9N2;Q9H1I8","subunits.Entrez.IDs.":"9325;10973;51008;84164","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0045893;GO:0023052;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;signaling;nucleus","FunCat.ID":"11.02.03.04.01;30.01;70.10","FunCat.description":"transcription activation;cellular signalling;nucleus","PubMed.ID":12077347,"subunits.Protein.name.":"Activating signal cointegrator 1 ;Activating signal cointegrator 1 complex subunit 3 ;Activating signal cointegrator 1 complex subunit 1 ;Activating signal cointegrator 1 complex subunit 2","subunits.Gene.name.":"TRIP4;ASCC3;ASCC1;ASCC2","subunits.Gene.name.syn.":";HELIC1;;ASC1P100","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Endogenous hASC-1 complex appears to play an essential role in AP-1, SRF, and NF-kappaB transactivation and to mediate the transrepression between nuclear receptors and either AP-1 or NF-kappaB in vivo.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1378,"ComplexName":"Translocon-associated protein (TRAP) complex","Organism":"Dog","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P16967;P23438;P51571;Q9UNL2","subunits.Entrez.IDs.":"403951;403950;6748;6747","Protein.complex.purification.method":"MI:0276- blue native page","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0005509;GO:0008565;GO:0006810;GO:0005783","GO.description":"intracellular protein transport;protein targeting;protein transport;calcium ion binding;protein transporter activity;transport;endoplasmic reticulum","FunCat.ID":"14.04;20.01.10;16.17.01;20;70.07","FunCat.description":"protein targeting, sorting and translocation;protein transport;calcium binding;CELLULAR TRANSPORT, TRANSPORT FACILITIES AND TRANSPORT ROUTES;endoplasmic reticulum","PubMed.ID":10471800,"subunits.Protein.name.":"Translocon-associated protein subunit alpha ;Translocon-associated protein subunit beta ;Translocon-associated protein subunit delta ;Translocon-associated protein subunit gamma","subunits.Gene.name.":"SSR1;SSR2;SSR4;SSR3","subunits.Gene.name.syn.":";;TRAPD;TRAPG","Disease.comment":"None","Subunits.comment":"Since SSR3 and SSR4 from dog were not available in the UniProt database at the time of annotation, the orthologous human proteins were used.","Complex.comment":"TRAP complex regulates the retention of ER resident proteins.","SWISSPROT.organism":"Canis lupus familiaris (Dog) (Canis familiaris);Canis lupus familiaris (Dog) (Canis familiaris);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1379,"ComplexName":"GALNS-lysosomal hydrolase 1.27 MDa complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P10619;P16278;P34059;Q99519","subunits.Entrez.IDs.":"5476;2720;2588;4758","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0029- cosedimentation through density gradients; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0005976;GO:0000271;GO:0000272;GO:0005773;GO:0005764","GO.description":"polysaccharide metabolic process;polysaccharide biosynthetic process;polysaccharide catabolic process;vacuole;lysosome","FunCat.ID":"01.05.03;70.25","FunCat.description":"polysaccharide metabolism;vacuole or lysosome","PubMed.ID":8910459,"subunits.Protein.name.":"Lysosomal protective protein ;Beta-galactosidase ;N-acetylgalactosamine-6-sulfatase ;Sialidase-1","subunits.Gene.name.":"CTSA;GLB1;GALNS;NEU1","subunits.Gene.name.syn.":"PPGB;ELNR1;;NANH","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The 1.27-MDa complex of lysosomal hydrolases is essential for keratan sulfate catabolism. Disruption of this complex may be responsible for the KS accumulation in beta-galactosidosis and galactosialidosis patients. Association of GALNS with the three other lysosomal hydrolases protects GALNS in lysosomes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1380,"ComplexName":"Elongator holo complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95163;Q6IA86;Q96EB1;Q9H9T3","subunits.Entrez.IDs.":"8518;55250;26610;55140","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006354;GO:0006473;GO:0006476;GO:0005634","GO.description":"DNA-templated transcription, elongation;protein acetylation;protein deacetylation;nucleus","FunCat.ID":"11.02.03.01.04;14.07.04;70.10","FunCat.description":"transcription elongation;modification by acetylation, deacetylation;nucleus","PubMed.ID":11714725,"subunits.Protein.name.":"Elongator complex protein 1 ;Elongator complex protein 2 ;Elongator complex protein 4 ;Elongator complex protein 3","subunits.Gene.name.":"IKBKAP;ELP2;ELP4;ELP3","subunits.Gene.name.syn.":"ELP1 IKAP;STATIP1;C11orf19 PAXNEB;","Disease.comment":"None","Subunits.comment":"Two other subunits of the complex were found in the analysis, which have not been further characterized: p38, p30.","Complex.comment":"The holo-Elongator complex has histone acetyltransferase activity directed against histone H3 and H4. Holo-Elongator interacts with RNA polymerase II.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1385,"ComplexName":"DICER1-NCOA6-AGO2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q14686;Q9UKV8;Q9UPY3","subunits.Entrez.IDs.":"23054;27161;23405","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0032774;GO:0006396;GO:0005737","GO.description":"RNA biosynthetic process;RNA processing;cytoplasm","FunCat.ID":"11.02;11.04;70.03","FunCat.description":"RNA synthesis;RNA processing;cytoplasm","PubMed.ID":15973356,"subunits.Protein.name.":"Nuclear receptor coactivator 6;Protein argonaute-2 ;Endoribonuclease Dicer","subunits.Gene.name.":"NCOA6;AGO2;DICER1","subunits.Gene.name.syn.":"AIB3, KIAA0181, RAP250, TRBP;EIF2C2;DICER HERNA KIAA0928","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Results support a role of the Dicer-TRBP complex not only in miRNA processing but also as a platform for RISC assembly.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1386,"ComplexName":"TTP-AGO4 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P26651;Q9HCK5","subunits.Entrez.IDs.":"7538;192670","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006401;GO:0032774;GO:0003723;GO:0005737","GO.description":"RNA catabolic process;RNA biosynthetic process;RNA binding;cytoplasm","FunCat.ID":"01.03.16.01;11.02;16.03.03;70.03","FunCat.description":"RNA degradation;RNA synthesis;RNA binding;cytoplasm","PubMed.ID":15766526,"subunits.Protein.name.":"mRNA decay activator protein ZFP36 ;Protein argonaute-4","subunits.Gene.name.":"ZFP36;AGO4","subunits.Gene.name.syn.":"G0S24 NUP475 RNF162A TIS11A TTP;EIF2C4 KIAA1567","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In analogy to the TTP-AGO2 complex the TTP-AGO4 complex is presumably involved in the miRNA-mediated degradation of RNAs containing AU-rich elements (AREs).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1387,"ComplexName":"TTP-AGO2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P26651;Q9UKV8","subunits.Entrez.IDs.":"7538;27161","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006401;GO:0032774;GO:0003723;GO:0005737","GO.description":"RNA catabolic process;RNA biosynthetic process;RNA binding;cytoplasm","FunCat.ID":"01.03.16.01;11.02;16.03.03;70.03","FunCat.description":"RNA degradation;RNA synthesis;RNA binding;cytoplasm","PubMed.ID":15766526,"subunits.Protein.name.":"mRNA decay activator protein ZFP36 ;Protein argonaute-2","subunits.Gene.name.":"ZFP36;AGO2","subunits.Gene.name.syn.":"G0S24 NUP475 RNF162A TIS11A TTP;EIF2C2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The TTP-AGO2 complex is involved in the miRNA-mediated degradation of RNAs containing AU-rich elements (AREs).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1388,"ComplexName":"RB1-TFAP2A complex","Organism":"Dog","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P05549;Q9XSY1","subunits.Entrez.IDs.":"7020;None","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0045893","GO.description":"positive regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.01","FunCat.description":"transcription activation","PubMed.ID":9632747,"subunits.Protein.name.":"Transcription factor AP-2-alpha ;Retinoblastoma protein","subunits.Gene.name.":"TFAP2A;RB1","subunits.Gene.name.syn.":"AP2TF TFAP2;","Disease.comment":"None","Subunits.comment":"Since TFAP2A from dog was not available in the UniProt database at the time of annotation, the orthologous protein from human was used.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Canis lupus familiaris (Dog) (Canis familiaris)"}
{"ComplexID":1390,"ComplexName":"Rb1-Runx2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P13405;Q08775","subunits.Entrez.IDs.":"19645;12393","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0001649","GO.description":"osteoblast differentiation","FunCat.ID":"43.03.17","FunCat.description":"structural cell of tissue (fibroblast, osteoblast, etc.)","PubMed.ID":11545733,"subunits.Protein.name.":"Retinoblastoma-associated protein ;Runt-related transcription factor 2","subunits.Gene.name.":"Rb1;Runx2","subunits.Gene.name.syn.":"Rb-1;Aml3 Cbfa1 Osf2 Pebp2a","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"pRb physically interacts with the osteoblast transcription factor, CBFA1, and associates with osteoblast-specific promoters in vivo in a CBFA1-dependent fashion. Association of pRb with CBFA1 and promoter sequences results in synergistic transactivation of an osteoblast-specific reporter.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1399,"ComplexName":"WDR5-ASH2L-RBBP5-MLL2 complex","Organism":"Human","Synonyms":"3 H4 methyltransferase complex","Cell.line":"None","subunits.UniProt.IDs.":"O14686;P61964;Q15291;Q9UBL3","subunits.Entrez.IDs.":"8085;11091;5929;9070","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0045893;GO:0018126;GO:0006479;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;protein hydroxylation;protein methylation;nucleus","FunCat.ID":"11.02.03.04.01;14.07.09;70.10","FunCat.description":"transcription activation;posttranslational modification of amino acids (e.g. hydroxylation, methylation);nucleus","PubMed.ID":15960974,"subunits.Protein.name.":"Histone-lysine N-methyltransferase 2D;WD repeat-containing protein 5;Retinoblastoma-binding protein 5;Set1/Ash2 histone methyltransferase complex subunit ASH2","subunits.Gene.name.":"KMT2D;WDR5;RBBP5;ASH2L","subunits.Gene.name.syn.":"ALR, MLL2, MLL4;BIG3;RBQ3;ASH2L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The WDR5-ASH2L-RBBP5-MLL2 complex performs methylation of lysine 4 (K4) of histone H3. Knockdown of xWDR5 during Xenopus development leads to somitic, gut, and hematopoetic defects.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1400,"ComplexName":"ASCOM complex","Organism":"Human","Synonyms":"ASC-2 complex","Cell.line":"None","subunits.UniProt.IDs.":"O14686;P07437;P68366;Q14686;Q15291;Q8NEZ4;Q9UBL3","subunits.Entrez.IDs.":"8085;203068;7277;23054;5929;58508;9070","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045893;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;positive regulation of transcription, DNA-templated;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.01;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription activation;DNA binding;organization of chromosome structure;nucleus","PubMed.ID":12482968,"subunits.Protein.name.":"Histone-lysine N-methyltransferase 2D;Tubulin beta chain;Tubulin alpha-4A chain ;Nuclear receptor coactivator 6;Retinoblastoma-binding protein 5;Histone-lysine N-methyltransferase 2C;Set1/Ash2 histone methyltransferase complex subunit ASH2","subunits.Gene.name.":"KMT2D;TUBB;TUBA4A;NCOA6;RBBP5;KMT2C;ASH2L","subunits.Gene.name.syn.":"ALR, MLL2, MLL4;TUBB5;TUBA1;AIB3, KIAA0181, RAP250, TRBP;RBQ3;HALR, KIAA1506, MLL3;ASH2L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"ASCOM exhibit very weak but specific H3-lysine 4 methylation activities in vitro, and transactivation by retinoic acid receptor appears to involve ligand-dependent recruitment of ASCOM and subsequent transient H3-lysine 4 methylation of the promoter region in vivo. Thus, ASCOM may represent a distinct coactivator complex of nuclear receptors. MALDI-TOF mass spectrometry analyses identified also ALR-2, the splicing isoform of ALR-1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1401,"ComplexName":"MOF complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14686;O15047;P21675;P49848;P61964;Q03164;Q15291;Q16594;Q99496;Q9H7Z6","subunits.Entrez.IDs.":"8085;9739;6872;6878;11091;4297;5929;6880;6045;84148","Protein.complex.purification.method":"MI:0226- ion exchange chromatography; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0005634","GO.description":"nucleus","FunCat.ID":"70.1","FunCat.description":"nucleus","PubMed.ID":15960975,"subunits.Protein.name.":"Histone-lysine N-methyltransferase 2D;Histone-lysine N-methyltransferase SETD1A;Transcription initiation factor TFIID subunit 1;Transcription initiation factor TFIID subunit 6;WD repeat-containing protein 5;Histone-lysine N-methyltransferase 2A;Retinoblastoma-binding protein 5;Transcription initiation factor TFIID subunit 9;E3 ubiquitin-protein ligase RING2;Histone acetyltransferase KAT8","subunits.Gene.name.":"KMT2D;SETD1A;TAF1;TAF6;WDR5;KMT2A;RBBP5;TAF9;RNF2;KAT8","subunits.Gene.name.syn.":"ALR, MLL2, MLL4;KIAA0339, KMT2F, SET1, SET1A;BA2R CCG1 CCGS TAF2A;TAF2E TAFII70;BIG3;ALL1, CXXC7, HRX, HTRX, MLL, MLL1, TRX1;RBQ3;TAF2G TAFII31;BAP1 DING HIPI3 RING1B;MOF MYST1","Disease.comment":"None","Subunits.comment":"Immunoprecipitation of the three step purified complex by anti-MOF antibodies. The complex was not functionally characterized.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1408,"ComplexName":"Ets2-Smarca4-Smarcb1-Smarce1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O35845;O54941;P15037;Q9Z0H3","subunits.Entrez.IDs.":"20586;57376;23872;20587","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045892;GO:0003677;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04.03;16.03.01;70.10","FunCat.description":"transcription repression;DNA binding;nucleus","PubMed.ID":12637547,"subunits.Protein.name.":"Brg1 protein ;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;Protein C-ets-2;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","subunits.Gene.name.":"Smarca4;Smarce1;Ets2;Smarcb1","subunits.Gene.name.syn.":"Brg1;Baf57;;Baf47 Ini1 Snf5l1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ets-2 has previously been characterized as an activator of gene expression. In contrast, in this study, ets-2 directly interacted with Brg-1, the ATPase component of the mSWI/SNF complex, and Brg-1 behaved as a transcriptional co-repressor along with ets-2.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1413,"ComplexName":"NCOR1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15379;O75376;P51532;Q12824;Q13263;Q15393;Q15459;Q6ZRS2;Q8TAQ2;Q92922","subunits.Entrez.IDs.":"8841;9611;6597;6598;10155;23450;10291;10847;6601;6599","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0004- affinity chromatography technologies; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006265;GO:0045892;GO:0032774;GO:0006473;GO:0006476;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;RNA biosynthetic process;protein acetylation;protein deacetylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;11.02;14.07.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;RNA synthesis;modification by acetylation, deacetylation;organization of chromosome structure;nucleus","PubMed.ID":11013263,"subunits.Protein.name.":"Histone deacetylase 3;Nuclear receptor corepressor 1;Transcription activator BRG1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;Transcription intermediary factor 1-beta ;Splicing factor 3B subunit 3;Splicing factor 3A subunit 1 ;Helicase SRCAP ;SWI/SNF complex subunit SMARCC2;SWI/SNF complex subunit SMARCC1","subunits.Gene.name.":"HDAC3;NCOR1;SMARCA4;SMARCB1;TRIM28;SF3B3;SF3A1;SRCAP;SMARCC2;SMARCC1","subunits.Gene.name.syn.":"None;KIAA1047;BAF190A BRG1 SNF2B SNF2L4;BAF47, INI1, SNF5L1;KAP1 RNF96 TIF1B;KIAA0017 SAP130;SAP114;KIAA0309;BAF170;BAF155","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Transcriptional silencing by many transcription factors is mediated by the nuclear receptor corepressor (N-CoR). The mechanism by which N-CoR represses basal transcription involves the direct or indirect recruitment of histone deacetylases (HDACs). Two multiprotein N-CoR complexes have been isolated, designated N-CoR-1 and N-CoR-2, which possess histone deacetylase activity that is mediated by distinct HDACs. Results suggest that N-CoR is found in distinct multiprotein complexes, which are involved in multiple pathways of transcriptional repression.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1423,"ComplexName":"L-periaxin-Drp2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O55103;P11531;Q05AA6;Q61636;Q62165","subunits.Entrez.IDs.":"19153;13405;13497;22288;13138","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005886","GO.description":"plasma membrane","FunCat.ID":"70.02","FunCat.description":"eukaryotic plasma membrane / membrane attached","PubMed.ID":11430802,"subunits.Protein.name.":"Periaxin;Dystrophin;Dystrophin-related protein 2;G-utrophin ;Dystroglycan","subunits.Gene.name.":"Prx;Dmd;Drp2;Utrn;Dag1","subunits.Gene.name.syn.":"None;None;None;G-utrophin;Dag-1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Disruption of the DRP2-dystroglycan complex is followed by hypermyelination and destabilization of the Schwann cell-axon unit in Prx(-/-) mice. Hence, the DRP2-dystroglycan complex likely has a distinct function in the terminal stages of PNS myelinogenesis, possibly in the regulation of myelin thickness. The dystroglycan precursor DAG1 includes alpha-dystroglycan and beta-dystroglycan polypeptides.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1439,"ComplexName":"PTGS2 homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P35354","subunits.Entrez.IDs.":"5743","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0006720;GO:0006633;GO:0008299;GO:0009062;GO:0016042;GO:0008300;GO:0006629;GO:0006631;GO:0008610","GO.description":"isoprenoid metabolic process;fatty acid biosynthetic process;isoprenoid biosynthetic process;fatty acid catabolic process;lipid catabolic process;isoprenoid catabolic process;lipid metabolic process;fatty acid metabolic process;lipid biosynthetic process","FunCat.ID":"01.06;01.06.05;01.06.06","FunCat.description":"lipid, fatty acid and isoprenoid metabolism;fatty acid metabolism;isoprenoid metabolism","PubMed.ID":10811226,"subunits.Protein.name.":"Prostaglandin G/H synthase 2","subunits.Gene.name.":"PTGS2","subunits.Gene.name.syn.":"COX2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":1442,"ComplexName":"Transporter (Ncx1) - receptor complex","Organism":"Rat","Synonyms":"Plasma membrane - cytoskeleton - endoplasmic reticulum complex","Cell.line":"None","subunits.UniProt.IDs.":"P11507;P16086;P29994;P97582;Q01728","subunits.Entrez.IDs.":"29693;64159;25262;362036;29715","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0019722","GO.description":"calcium-mediated signaling","FunCat.ID":"30.01.09.03","FunCat.description":"Ca2+ mediated signal transduction","PubMed.ID":14593108,"subunits.Protein.name.":"Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 ;Spectrin alpha chain, non-erythrocytic 1;Inositol 1,4,5-trisphosphate receptor type 1;Ankyrin ;Sodium/calcium exchanger 1","subunits.Gene.name.":"Atp2a2;Sptan1;Itpr1;Ank2;Slc8a1","subunits.Gene.name.syn.":";Spna2 Spta2;Insp3r;;Ncx1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The experimental data support the idea that in neurons and glia PM microdomains containing Ncx1 and Na+  pumps with alpha2 or alpha3 subunits form Ca2+ signaling complexes with underlying ER containing Serca2 (=Atp2a2) and IP(3)R-1 (=Itpr1).","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":1448,"ComplexName":"LIN2-LIN7-SAP97 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"HEK 293 cells, MDCK cells, epithelium","subunits.UniProt.IDs.":"O14910;O14936;Q12959","subunits.Entrez.IDs.":"8825;8573;1739","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0051211;GO:0009798;GO:0030855;GO:0002009","GO.description":"intracellular protein transport;protein targeting;protein transport;anisotropic cell growth;axis specification;epithelial cell differentiation;morphogenesis of an epithelium","FunCat.ID":"14.04;20.01.10;40.01.03;41.05.19;45.03.09","FunCat.description":"protein targeting, sorting and translocation;protein transport;directional cell growth (morphogenesis);asymmetries and axis determination;epithelium","PubMed.ID":11865057,"subunits.Protein.name.":"Protein lin-7 homolog A;Peripheral plasma membrane protein CASK ;Disks large homolog 1","subunits.Gene.name.":"LIN7A;CASK;DLG1","subunits.Gene.name.syn.":"MALS1 VELI1;LIN2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1449,"ComplexName":"Dlg3-Lin7-SAP97 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"MDCK cells, epithelium","subunits.UniProt.IDs.":"P70175;Q811D0;Q8JZS0","subunits.Entrez.IDs.":"53310;13383;108030","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0051211;GO:0009798","GO.description":"intracellular protein transport;protein targeting;protein transport;anisotropic cell growth;axis specification","FunCat.ID":"14.04;20.01.10;40.01.03;41.05.19","FunCat.description":"protein targeting, sorting and translocation;protein transport;directional cell growth (morphogenesis);asymmetries and axis determination","PubMed.ID":12351654,"subunits.Protein.name.":"Disks large homolog 3 ;Disks large homolog 1;Protein lin-7 homolog A","subunits.Gene.name.":"Dlg3;Dlg1;Lin7a","subunits.Gene.name.syn.":"Dlgh3;Dlgh1;Mals1, Veli1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1452,"ComplexName":"MCM2-MCM6-MCM7 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P33993;P49736;Q14566","subunits.Entrez.IDs.":"4176;4171;4175","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006260;GO:0005634","GO.description":"DNA replication;nucleus","FunCat.ID":"10.01.03;70.10","FunCat.description":"DNA synthesis and replication;nucleus","PubMed.ID":15448696,"subunits.Protein.name.":"DNA replication licensing factor MCM7 ;DNA replication licensing factor MCM2 ;DNA replication licensing factor MCM6","subunits.Gene.name.":"MCM7;MCM2;MCM6","subunits.Gene.name.syn.":"CDC47 MCM2;BM28 CCNL1 CDCL1 KIAA0030;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1457,"ComplexName":"AFF1-MLLT1-CBX8 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P51825;Q03111;Q9HC52","subunits.Entrez.IDs.":"4299;4298;57332","Protein.complex.purification.method":"MI:0027- cosedimentation","GO.ID":"GO:2001141;GO:0006355;GO:0016607","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;nuclear speck","FunCat.ID":"11.02.03.04;70.10.09","FunCat.description":"transcriptional control;nuclear speckles","PubMed.ID":15856011,"subunits.Protein.name.":"AF4/FMR2 family member 1;Protein ENL;Chromobox protein homolog 8","subunits.Gene.name.":"AFF1;MLLT1;CBX8","subunits.Gene.name.syn.":"AF4, FEL, MLLT2, PBM1;ENL, LTG19, YEATS1;PC3 RC1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1458,"ComplexName":"SNF2h-HDAC12 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60264;Q92769","subunits.Entrez.IDs.":"8467;3066","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0051052;GO:0006473;GO:0006476;GO:0051276","GO.description":"regulation of DNA metabolic process;protein acetylation;protein deacetylation;chromosome organization","FunCat.ID":"10.01.11;14.07.04;42.10.03","FunCat.description":"regulation of DNA processing;modification by acetylation, deacetylation;organization of chromosome structure","PubMed.ID":15775975,"subunits.Protein.name.":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5;Histone deacetylase 2","subunits.Gene.name.":"SMARCA5;HDAC2","subunits.Gene.name.syn.":"SNF2H WCRF135;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNF2h-HDAC1/2 complex coordinates G1-specific chromatin remodeling and histone deacetylation with the DNA replication initiation process at OriP.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1462,"ComplexName":"hPRC1L complex","Organism":"Human","Synonyms":"human Polycomb repressive complex 1-like","Cell.line":"None","subunits.UniProt.IDs.":"P35226;Q06587;Q8IXK0;Q99496","subunits.Entrez.IDs.":"648;6015;1912;6045","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0226- ion exchange chromatography","GO.ID":"GO:0006304;GO:0009307;GO:0032774;GO:0016567;GO:0016579;GO:0005634","GO.description":"DNA modification;DNA restriction-modification system;RNA biosynthetic process;protein ubiquitination;protein deubiquitination;nucleus","FunCat.ID":"10.01.09;11.02;14.07.05;70.10","FunCat.description":"DNA restriction or modification;RNA synthesis;modification by ubiquitination, deubiquitination;nucleus","PubMed.ID":15386022,"subunits.Protein.name.":"Polycomb complex protein BMI-1;E3 ubiquitin-protein ligase RING1;Polyhomeotic-like protein 2;E3 ubiquitin-protein ligase RING2","subunits.Gene.name.":"BMI1;RING1;PHC2;RNF2","subunits.Gene.name.syn.":"PCGF4 RNF51;RNF1;EDR2 PH2;BAP1 DING HIPI3 RING1B","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The hPRC1L complex silences transcription by ubiquinating histone H2A at Lys 119.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1464,"ComplexName":"Mis12 centromere complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95229;P45973;Q6P1K2;Q96IY1;Q9H081;Q9H410","subunits.Entrez.IDs.":"11130;23468;11243;25936;79003;79980","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007059;GO:0000775","GO.description":"chromosome segregation;chromosome, centromeric region","FunCat.ID":"10.03.04.05;70.10.04","FunCat.description":"chromosome segregation/division;centromere / kinetochore","PubMed.ID":15502821,"subunits.Protein.name.":"ZW10 interactor ;Chromobox protein homolog 5 ;Polyamine-modulated factor 1 ;Kinetochore-associated protein NSL1 homolog;Protein MIS12 homolog;Kinetochore-associated protein DSN1 homolog","subunits.Gene.name.":"ZWINT;CBX5;PMF1;NSL1;MIS12;DSN1","subunits.Gene.name.syn.":";HP1A;;C1orf48;;C20orf172 MIS13","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1469,"ComplexName":"E2f5-Rbl2-Hdac1 complex","Organism":"Mouse","Synonyms":"E2F5-p130-HDAC1 complex","Cell.line":"None","subunits.UniProt.IDs.":"O09106;Q61502;Q64700","subunits.Entrez.IDs.":"433759;13559;19651","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007050;GO:0003677;GO:0030216","GO.description":"cell cycle arrest;DNA binding;keratinocyte differentiation","FunCat.ID":"10.03.01.02;16.03.01;43.03.04","FunCat.description":"cell cycle arrest;DNA binding;epidermal cell (e.g. keratinocytes)","PubMed.ID":11319226,"subunits.Protein.name.":"Histone deacetylase 1;Transcription factor E2F5 ;Retinoblastoma-like protein 2","subunits.Gene.name.":"Hdac1;E2f5;Rbl2","subunits.Gene.name.syn.":"None;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Induction of differentiation in mouse keratinocytes results in formation of E2f5-Rbl2-Hdac1 complex, which can trigger keratinocyte entry into quiescence.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1470,"ComplexName":"pRb2/p130-multimolecular complex (DNMT1, E2F5, SuV39H1, HDAC1, RBL2)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43463;P26358;Q08999;Q13547;Q15329","subunits.Entrez.IDs.":"6839;1786;5934;3065;1875","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0047- far western blotting","GO.ID":"GO:0006351","GO.description":"transcription, DNA-templated","FunCat.ID":"11","FunCat.description":"TRANSCRIPTION","PubMed.ID":12789259,"subunits.Protein.name.":"Histone-lysine N-methyltransferase SUV39H1 ;DNA ;Retinoblastoma-like protein 2;Histone deacetylase 1;Transcription factor E2F5","subunits.Gene.name.":"SUV39H1;DNMT1;RBL2;HDAC1;E2F5","subunits.Gene.name.syn.":"KMT1A SUV39H;AIM CXXC9 DNMT;RB2, P130;RPD3L1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1471,"ComplexName":"pRb2/p130-multimolecular complex (RB2, E2F5, HDAC1, SUV39H1, P300)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43463;Q08999;Q09472;Q13547;Q15329","subunits.Entrez.IDs.":"6839;5934;2033;3065;1875","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0047- far western blotting","GO.ID":"GO:0006351","GO.description":"transcription, DNA-templated","FunCat.ID":"11","FunCat.description":"TRANSCRIPTION","PubMed.ID":12789259,"subunits.Protein.name.":"Histone-lysine N-methyltransferase SUV39H1 ;Retinoblastoma-like protein 2;Histone acetyltransferase p300;Histone deacetylase 1;Transcription factor E2F5","subunits.Gene.name.":"SUV39H1;RBL2;EP300;HDAC1;E2F5","subunits.Gene.name.syn.":"KMT1A SUV39H;RB2, P130;P300;RPD3L1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1473,"ComplexName":"E2F5-RB2-DP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q08999;Q14186;Q15329","subunits.Entrez.IDs.":"5934;7027;1875","Protein.complex.purification.method":"MI:0018- two hybrid; MI:0019- coimmunoprecipitation","GO.ID":"GO:0006351","GO.description":"transcription, DNA-templated","FunCat.ID":"11","FunCat.description":"TRANSCRIPTION","PubMed.ID":7760804,"subunits.Protein.name.":"Retinoblastoma-like protein 2;Transcription factor Dp-1;Transcription factor E2F5","subunits.Gene.name.":"RBL2;TFDP1;E2F5","subunits.Gene.name.syn.":"RB2, P130;DP1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1474,"ComplexName":"SMAD3/4-E2F4/5-p107-DP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P28749;P84022;Q13485;Q14186;Q15329;Q16254","subunits.Entrez.IDs.":"5933;4088;4089;7027;1875;1874","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation; MI:0402- chromatin immunoprecipitation assays","GO.ID":"GO:0045892;GO:0003677;GO:0007179;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;DNA binding;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"11.02.03.04.03;16.03.01;30.05.01.18.01;70.10","FunCat.description":"transcription repression;DNA binding;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":12150994,"subunits.Protein.name.":"Retinoblastoma-like protein 1;Mothers against decapentaplegic homolog 3;Mothers against decapentaplegic homolog 4;Transcription factor Dp-1;Transcription factor E2F5 ;Transcription factor E2F4","subunits.Gene.name.":"RBL1;SMAD3;SMAD4;TFDP1;E2F5;E2F4","subunits.Gene.name.syn.":"PRB1, p107, CP107;MADH3;DPC4 MADH4;DP1;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"E2F4/5 and p107 act as signal cotransducers that enable a SMAD complex to recognize and repress c-Myc transcription.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1475,"ComplexName":"S-phase-specific E2F-p107 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P97377;Q08639;Q61456;Q64701;Q8R0K9","subunits.Entrez.IDs.":"12566;21781;12427;19650;104394","Protein.complex.purification.method":"MI:0047-far western blotting;MI:0019-coimmunoprecipitation","GO.ID":"GO:0000084;GO:0001889","GO.description":"mitotic S phase;liver development","FunCat.ID":"10.03.01.01.05;47.03.11.07","FunCat.description":"S phase of mitotic cell cycle;liver","PubMed.ID":10082561,"subunits.Protein.name.":"Cyclin-dependent kinase 2;Transcription factor Dp-1;Cyclin-A1;Retinoblastoma-like protein 1;Transcription factor E2F4","subunits.Gene.name.":"Cdk2;Tfdp1;Ccna1;Rbl1;E2f4","subunits.Gene.name.syn.":"Cdkn2;None;None;None;None","Disease.comment":"None","Subunits.comment":"Since the authors did not specify cyclin A, we used isoform cyclin-A1 .","Complex.comment":"The formation of E2F-p107 complexes during prenatal liver development in mice is dependent on C/EBPa.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1488,"ComplexName":"DNMT1-RB1-HDAC1-E2F1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06400;P26358;Q01094;Q13547","subunits.Entrez.IDs.":"5925;1786;1869;3065","Protein.complex.purification.method":"MI:0027- cosedimentation","GO.ID":"GO:0045892","GO.description":"negative regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.03","FunCat.description":"transcription repression","PubMed.ID":10888886,"subunits.Protein.name.":"Retinoblastoma-associated protein ;DNA ;Transcription factor E2F1;Histone deacetylase 1","subunits.Gene.name.":"RB1;DNMT1;E2F1;HDAC1","subunits.Gene.name.syn.":";AIM CXXC9 DNMT;RBBP3;RPD3L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1490,"ComplexName":"DAXX-DNMT1-DMAP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P26358;Q9NPF5;Q9UER7","subunits.Entrez.IDs.":"1786;55929;1616","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0045892","GO.description":"negative regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.03","FunCat.description":"transcription repression","PubMed.ID":14978102,"subunits.Protein.name.":"DNA ;DNA methyltransferase 1-associated protein 1;Death domain-associated protein 6","subunits.Gene.name.":"DNMT1;DMAP1;DAXX","subunits.Gene.name.syn.":"AIM CXXC9 DNMT;KIAA1425;BING2 DAP6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1491,"ComplexName":"RGS6-DNMT1-DMAP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P26358;P49758;Q9NPF5","subunits.Entrez.IDs.":"1786;9628;55929","Protein.complex.purification.method":"MI:0018- two hybrid; MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":14734556,"subunits.Protein.name.":"DNA ;Regulator of G-protein signaling 6 ;DNA methyltransferase 1-associated protein 1","subunits.Gene.name.":"DNMT1;RGS6;DMAP1","subunits.Gene.name.syn.":"AIM CXXC9 DNMT;;KIAA1425","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex inhibits DMAP1 transcriptional repressor activity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1492,"ComplexName":"BHC110 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60341;O75362;Q13547;Q14687;Q92618;Q92769;Q96BD5;Q9P0W2;Q9UBW7;Q9UKL0","subunits.Entrez.IDs.":"23028;7764;3065;23199;9658;3066;51317;10362;7750;23186","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006265;GO:0006473;GO:0006476;GO:0018126;GO:0006479;GO:0005634","GO.description":"DNA topological change;protein acetylation;protein deacetylation;protein hydroxylation;protein methylation;nucleus","FunCat.ID":"10.01.09.05;14.07.04;14.07.09;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);modification by acetylation, deacetylation;posttranslational modification of amino acids (e.g. hydroxylation, methylation);nucleus","PubMed.ID":16079794,"subunits.Protein.name.":"Lysine-specific histone demethylase 1A;Zinc finger protein 217;Histone deacetylase 1;Genetic suppressor element 1;Zinc finger protein 516;Histone deacetylase 2;PHD finger protein 21A;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related;Zinc finger MYM-type protein 2;REST corepressor 1","subunits.Gene.name.":"KDM1A;ZNF217;HDAC1;GSE1;ZNF516;HDAC2;PHF21A;HMG20B;ZMYM2;RCOR1","subunits.Gene.name.syn.":"AOF2 KDM1 KIAA0601 LSD1;ZABC1;RPD3L1;KIAA0182;KIAA0222;None;BHC80 KIAA1696;BRAF35 HMGX2 HMGXB2 SMARCE1R;FIM RAMP ZNF198;KIAA0071 RCOR","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The BHC110 complex performs demethylation of histone H3 lysine 4 (H3K4). The related BHC complex (CORUM ID 636) is recruited by a neuronal silencer, REST (RE1-silencing transcription factor), and mediates the repression of REST-responsive genes. Depletion of the CoREST (RCOR1) subunit of the BHC110 complex and the BHC complex results in de-repression of REST-responsive gene expression and increased methylation of H3K4.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1495,"ComplexName":"PID complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O94776;O95983;Q09028;Q13547;Q14839","subunits.Entrez.IDs.":"9219;53615;5928;3065;1108","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006473;GO:0006476;GO:0006464;GO:0051090;GO:0005634","GO.description":"protein acetylation;protein deacetylation;cellular protein modification process;regulation of sequence-specific DNA binding transcription factor activity;nucleus","FunCat.ID":"14.07.04;14.07;18.02.09;70.10","FunCat.description":"modification by acetylation, deacetylation;protein modification;regulator of transcription factor;nucleus","PubMed.ID":11099047,"subunits.Protein.name.":"Metastasis-associated protein MTA2;Methyl-CpG-binding domain protein 3;Histone-binding protein RBBP4;Histone deacetylase 1;Chromodomain-helicase-DNA-binding protein 4","subunits.Gene.name.":"MTA2;MBD3;RBBP4;HDAC1;CHD4","subunits.Gene.name.syn.":"MTA1L1 PID;None;RBAP48;RPD3L1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"PID complex-mediated repression of p53 transactivation functions acts, in part, through deacetylation of p53 at the C terminus. Experiments  show that PID is involved in the regulation of p53-mediated growth arrest and apoptosis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1503,"ComplexName":"Hdac1-Mecp2-Rcor1-Sin3a complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O09106;Q60520;Q8CFE3;Q9Z2D6","subunits.Entrez.IDs.":"433759;20466;217864;17257","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0045892","GO.description":"negative regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.03","FunCat.description":"transcription repression","PubMed.ID":15907476,"subunits.Protein.name.":"Histone deacetylase 1;Paired amphipathic helix protein Sin3a;REST corepressor 1 ;Methyl-CpG-binding protein 2","subunits.Gene.name.":"Hdac1;Sin3a;Rcor1;Mecp2","subunits.Gene.name.syn.":"None;Kiaa4126;D12Wsu95e Kiaa0071;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1505,"ComplexName":"NCOR2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15379;O75376;O75446;Q13547;Q92769;Q96ST3;Q9Y618","subunits.Entrez.IDs.":"8841;9611;8819;3065;3066;25942;9612","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0029- cosedimentation through density gradients; MI:0004- affinity chromatography technologies","GO.ID":"GO:0006265;GO:0045892;GO:0032774;GO:0006473;GO:0006476;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;RNA biosynthetic process;protein acetylation;protein deacetylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;11.02;14.07.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;RNA synthesis;modification by acetylation, deacetylation;organization of chromosome structure;nucleus","PubMed.ID":11013263,"subunits.Protein.name.":"Histone deacetylase 3;Nuclear receptor corepressor 1;Histone deacetylase complex subunit SAP30;Histone deacetylase 1;Histone deacetylase 2;Paired amphipathic helix protein Sin3a;Nuclear receptor corepressor 2","subunits.Gene.name.":"HDAC3;NCOR1;SAP30;HDAC1;HDAC2;SIN3A;NCOR2","subunits.Gene.name.syn.":"None;KIAA1047;None;RPD3L1;None;None;CTG26","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Transcriptional silencing by many transcription factors is mediated by the nuclear receptor corepressor (N-CoR). The mechanism by which N-CoR represses basal transcription involves the direct or indirect recruitment of histone deacetylases (HDACs). Two multiprotein N-CoR complexes have been isolated, designated N-CoR-1 and N-CoR-2, which possess histone deacetylase activity that is mediated by distinct HDACs. Results suggest that N-CoR is found in distinct multiprotein complexes, which are involved in multiple pathways of transcriptional repression. Only weak amounts of HDAC3 could be detected in the N-CoR-2 complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1508,"ComplexName":"BCL6-ZBTB17 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P41182;Q13105","subunits.Entrez.IDs.":"604;None","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0045892","GO.description":"negative regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.03","FunCat.description":"transcription repression","PubMed.ID":16142238,"subunits.Protein.name.":"B-cell lymphoma 6 protein ;Zinc finger and BTB domain-containing protein 17","subunits.Gene.name.":"BCL6;ZBTB17","subunits.Gene.name.syn.":"BCL5 LAZ3 ZBTB27 ZNF51;MIZ1 ZNF151 ZNF60","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"BCL6 interacted with the transcriptional activator Miz-1 and, via Miz-1, bound to the promoter and suppressed transcription of the cell cycle arrest gene CDKN1A.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1514,"ComplexName":"IL4-IL4R complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P05112;P24394","subunits.Entrez.IDs.":"3565;3566","Protein.complex.purification.method":"MI:0030- cross-linking studies","GO.ID":"GO:0005515;GO:0023052","GO.description":"protein binding;signaling","FunCat.ID":"16.01;30.01","FunCat.description":"protein binding;cellular signalling","PubMed.ID":8266078,"subunits.Protein.name.":"Interleukin-4 ;Interleukin-4 receptor subunit alpha","subunits.Gene.name.":"IL4;IL4R","subunits.Gene.name.syn.":";IL4RA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1515,"ComplexName":"IL4-IL4R-IL2RG complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P05112;P24394;P31785","subunits.Entrez.IDs.":"3565;3566;3561","Protein.complex.purification.method":"MI:0030- cross-linking studies","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":8266078,"subunits.Protein.name.":"Interleukin-4 ;Interleukin-4 receptor subunit alpha ;Cytokine receptor common subunit gamma","subunits.Gene.name.":"IL4;IL4R;IL2RG","subunits.Gene.name.syn.":";IL4RA;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1519,"ComplexName":"IL6ST-PRKCD-STAT3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P40189;P40763;Q05655","subunits.Entrez.IDs.":"3572;6774;5580","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0051098;GO:0005515","GO.description":"regulation of binding;protein binding","FunCat.ID":"18.01.07;16.01","FunCat.description":"regulation by binding / dissociation;protein binding","PubMed.ID":12361954,"subunits.Protein.name.":"Interleukin-6 receptor subunit beta ;Signal transducer and activator of transcription 3;Protein kinase C delta type","subunits.Gene.name.":"IL6ST;STAT3;PRKCD","subunits.Gene.name.syn.":";APRF;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"PKCdelta  is recruited to the receptor gp130 via Stat3, which not only stabilizes the Stat3 and gp130 receptor interaction, but may also phosphorylate gp130.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1520,"ComplexName":"STAT3-NLK-MAP3K7 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43318;P40763;Q9UBE8","subunits.Entrez.IDs.":"6885;6774;None","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007165;GO:0005634","GO.description":"signal transduction;nucleus","FunCat.ID":"30;70.10","FunCat.description":"CELLULAR COMMUNICATION/SIGNAL TRANSDUCTION MECHANISM;nucleus","PubMed.ID":15764709,"subunits.Protein.name.":"Mitogen-activated protein kinase kinase kinase 7;Signal transducer and activator of transcription 3;Serine/threonine-protein kinase NLK","subunits.Gene.name.":"MAP3K7;STAT3;NLK","subunits.Gene.name.syn.":"TAK1;APRF;LAK1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The complex is involved in the TAK1-Nemo-like kinase (NLK) pathway.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1521,"ComplexName":"p300-SMAD1-STAT3 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"P40763;Q09472;Q15797","subunits.Entrez.IDs.":"6774;2033;4086","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045893;GO:0007167;GO:0048708","GO.description":"positive regulation of transcription, DNA-templated;enzyme linked receptor protein signaling pathway;astrocyte differentiation","FunCat.ID":"11.02.03.04.01;30.05.01","FunCat.description":"transcription activation;receptor enzyme mediated signalling","PubMed.ID":10205054,"subunits.Protein.name.":"Signal transducer and activator of transcription 3;Histone acetyltransferase p300;Mothers against decapentaplegic homolog 1","subunits.Gene.name.":"STAT3;EP300;SMAD1","subunits.Gene.name.syn.":"APRF;P300;BSP1 MADH1 MADR1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"P300 acts as an adaptor linking SMAD1 and STAT3.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1522,"ComplexName":"STAT3 homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P40763","subunits.Entrez.IDs.":"6774","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0003677","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding","FunCat.ID":"11.02.03.04;16.03.01","FunCat.description":"transcriptional control;DNA binding","PubMed.ID":15653507,"subunits.Protein.name.":"Signal transducer and activator of transcription 3","subunits.Gene.name.":"STAT3","subunits.Gene.name.syn.":"APRF","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Lys685 acetylation was critical for Stat3 to form stable dimers required for cytokine-stimulated DNA binding and transcriptional regulation, to enhance transcription of cell growth-related genes, and to promote cell cycle progression in response to treatment with oncostatin M.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":1523,"ComplexName":"Stat3-Crebbp complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P42227;P45481","subunits.Entrez.IDs.":"20848;12914","Protein.complex.purification.method":"MI:0402- chromatin immunoprecipitation assays","GO.ID":"GO:0007420","GO.description":"brain development","FunCat.ID":"47.03.01.01.01","FunCat.description":"brain","PubMed.ID":15852015,"subunits.Protein.name.":"Signal transducer and activator of transcription 3 ;CREB-binding protein","subunits.Gene.name.":"Stat3;Crebbp","subunits.Gene.name.syn.":"Aprf;Cbp","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1530,"ComplexName":"Girdin homo-oligomer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q3V6T2","subunits.Entrez.IDs.":"55704","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006928;GO:0030036","GO.description":"movement of cell or subcellular component;actin cytoskeleton organization","FunCat.ID":"34.05;42.04.03","FunCat.description":"cell motility;actin cytoskeleton","PubMed.ID":16139227,"subunits.Protein.name.":"Girdin","subunits.Gene.name.":"CCDC88A","subunits.Gene.name.syn.":"APE GRDN KIAA1212","Disease.comment":"None","Subunits.comment":"Oligomer","Complex.comment":"Girdin is essential for the integrity of the actin cytoskeleton and cell migration.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":1537,"ComplexName":"Heterotrimer complex (Rnd1, Rras, Plxnb1)","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P10833;Q8BLR7;Q8CJH3","subunits.Entrez.IDs.":"20130;223881;235611","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005096;GO:0043547;GO:0007166;GO:0007155;GO:0005102","GO.description":"GTPase activator activity;positive regulation of GTPase activity;cell surface receptor signaling pathway;cell adhesion;receptor binding","FunCat.ID":"18.02.01.01.01;30.05;34.07;16.01.01","FunCat.description":"GTPase activator (GAP);transmembrane signal transduction;cell adhesion;receptor binding","PubMed.ID":15297673,"subunits.Protein.name.":"Ras-related protein R-Ras ;Rho-related GTP-binding protein Rho6 ;Plexin-B1","subunits.Gene.name.":"Rras;Rnd1;Plxnb1","subunits.Gene.name.syn.":";Rho6;Kiaa0407","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1539,"ComplexName":"G protein complex (GNG2, GNB2L1, RAF1)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04049;P59768;P63244","subunits.Entrez.IDs.":"5894;54331;10399","Protein.complex.purification.method":"MI:0047- far western blotting; MI:0018- two hybrid","GO.ID":"GO:0007186","GO.description":"G-protein coupled receptor signaling pathway","FunCat.ID":"30.05.02.24","FunCat.description":"G-protein coupled receptor signalling pathway","PubMed.ID":7782277,"subunits.Protein.name.":"RAF proto-oncogene serine/threonine-protein kinase;Guanine nucleotide-binding protein G;Receptor of activated protein C kinase 1","subunits.Gene.name.":"RAF1;GNG2;RACK1","subunits.Gene.name.syn.":"RAF;None;GNB2L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Raf-1 is a serine-threonine protein kinase critically positioned in a cascade linking activated growth factor receptors with the nucleus and ultimatively regulating the mitogenic response.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1543,"ComplexName":"PPP2CA-PPP2R1A complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P30153;P67775","subunits.Entrez.IDs.":"5518;5515","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030234;GO:0050790","GO.description":"enzyme regulator activity;regulation of catalytic activity","FunCat.ID":"18.02.01","FunCat.description":"enzymatic activity regulation / enzyme regulator","PubMed.ID":12370081,"subunits.Protein.name.":"Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform;Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform","subunits.Gene.name.":"PPP2R1A;PPP2CA","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1544,"ComplexName":"PPP2CA-PPP2R1A-PPP2R3A complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P30153;P67775;Q06190","subunits.Entrez.IDs.":"5518;5515;5523","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030234;GO:0050790","GO.description":"enzyme regulator activity;regulation of catalytic activity","FunCat.ID":"18.02.01","FunCat.description":"enzymatic activity regulation / enzyme regulator","PubMed.ID":12506124,"subunits.Protein.name.":"Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform;Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform;Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit alpha","subunits.Gene.name.":"PPP2R1A;PPP2CA;PPP2R3A","subunits.Gene.name.syn.":"None;None;PPP2R3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1549,"ComplexName":"Kpna2-Kpnb1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P52293;P70168","subunits.Entrez.IDs.":"16647;16211","Protein.complex.purification.method":"MI:0114- x-ray crystallography; MI:0027- cosedimentation; MI:0016- circular dichroism","GO.ID":"GO:0015031;GO:0008565;GO:0006810;GO:0005634","GO.description":"protein transport;protein transporter activity;transport;nucleus","FunCat.ID":"20.01.10;20;70.10","FunCat.description":"protein transport;CELLULAR TRANSPORT, TRANSPORT FACILITIES AND TRANSPORT ROUTES;nucleus","PubMed.ID":11448961,"subunits.Protein.name.":"Importin subunit alpha-1 ;Importin subunit beta-1","subunits.Gene.name.":"Kpna2;Kpnb1","subunits.Gene.name.syn.":"Rch1;Impnb","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The importin-alpha/beta complex binds representative monopartite NLS (simian virus 40 large T-antigen) and bipartite NLS (nucleoplasmin) with affinities (K(D) = 3.5 x 10(-8) m and 4.8 x 10(-8) m, respectively).","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1551,"ComplexName":"IPO13-RAN-EIF1AX complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O94829;P47813;P62826","subunits.Entrez.IDs.":"9670;1964;5901","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0015031;GO:0008565;GO:0051169;GO:0005737;GO:0005634","GO.description":"protein transport;protein transporter activity;nuclear transport;cytoplasm;nucleus","FunCat.ID":"20.01.10;20.09.01;70.03;70.10","FunCat.description":"protein transport;nuclear transport;cytoplasm;nucleus","PubMed.ID":11447110,"subunits.Protein.name.":"Importin-13 ;Eukaryotic translation initiation factor 1A, X-chromosomal ;GTP-binding nuclear protein Ran","subunits.Gene.name.":"IPO13;EIF1AX;RAN","subunits.Gene.name.syn.":"KIAA0724 RANBP13;EIF1A EIF4C;ARA24","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Imp13 operates differently from typical exportins in that the binding of eIF1A to Imp13 is only regulated indirectly by RanGTP, and the cytoplasmic release of eIF1A from Imp13 is triggered by the loading of import substrates onto Imp13 (PMID:11447110).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1552,"ComplexName":"TNPO2-RAN-NXF1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14787;P62826;Q9UBU9","subunits.Entrez.IDs.":"30000;5901;10482","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0003723;GO:0050658;GO:0051033;GO:0051169;GO:0005737;GO:0005634","GO.description":"RNA binding;RNA transport;RNA transmembrane transporter activity;nuclear transport;cytoplasm;nucleus","FunCat.ID":"16.03.03;20.01.21;20.09.01;70.03;70.10","FunCat.description":"RNA binding;RNA transport;nuclear transport;cytoplasm;nucleus","PubMed.ID":12384575,"subunits.Protein.name.":"Transportin-2 ;GTP-binding nuclear protein Ran;Nuclear RNA export factor 1","subunits.Gene.name.":"TNPO2;RAN;NXF1","subunits.Gene.name.syn.":";ARA24;TAP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Kap beta2B participates directly in the export of a large proportion of cellular mRNAs, and TAP connects Kap beta2B to the mRNAs to be exported (PMID:12384575).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1554,"ComplexName":"RANBP1-RAN-KPNB1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P43487;P62826;Q14974","subunits.Entrez.IDs.":"5902;5901;3837","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0015031;GO:0008565;GO:0051169","GO.description":"protein transport;protein transporter activity;nuclear transport","FunCat.ID":"20.01.10;20.09.01","FunCat.description":"protein transport;nuclear transport","PubMed.ID":10037787,"subunits.Protein.name.":"Ran-specific GTPase-activating protein;GTP-binding nuclear protein Ran;Importin subunit beta-1","subunits.Gene.name.":"RANBP1;RAN;KPNB1","subunits.Gene.name.syn.":"None;ARA24;NTF97","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex is exported as a complex from the nucleus to the cytoplasm in living cells. The binding of RanBP1 to the Ran-importin beta  complex is required for the dissociation of the complex in the cytoplasm and that the released Ran is recycled to the nucleus, which is essential for the nuclear protein transport (PMID:10037787).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1555,"ComplexName":"Nmi-Rpa2-Rrn3 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"B2RS91;O35309;Q62193","subunits.Entrez.IDs.":"106298;64685;19891","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0009303","GO.description":"rRNA transcription","FunCat.ID":"11.02.01","FunCat.description":"rRNA synthesis","PubMed.ID":15558034,"subunits.Protein.name.":"RNA polymerase I-specific transcription initiation factor RRN3;N-myc-interactor ;Replication protein A 32 kDa subunit","subunits.Gene.name.":"Rrn3;Nmi;Rpa2","subunits.Gene.name.syn.":";;Rpa34","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1556,"ComplexName":"Rpa2-Rrn3 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"B2RS91;Q62193","subunits.Entrez.IDs.":"106298;19891","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0009303","GO.description":"rRNA transcription","FunCat.ID":"11.02.01","FunCat.description":"rRNA synthesis","PubMed.ID":15558034,"subunits.Protein.name.":"RNA polymerase I-specific transcription initiation factor RRN3;Replication protein A 32 kDa subunit","subunits.Gene.name.":"Rrn3;Rpa2","subunits.Gene.name.syn.":";Rpa34","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1557,"ComplexName":"NMI-POLR1B-RRN3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q13287;Q9H9Y6;Q9NYV6","subunits.Entrez.IDs.":"9111;84172;54700","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0009303","GO.description":"rRNA transcription","FunCat.ID":"11.02.01","FunCat.description":"rRNA synthesis","PubMed.ID":15558034,"subunits.Protein.name.":"N-myc-interactor ;DNA-directed RNA polymerase I subunit RPA2 ;RNA polymerase I-specific transcription initiation factor RRN3","subunits.Gene.name.":"NMI;POLR1B;RRN3","subunits.Gene.name.syn.":";;TIFIA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1558,"ComplexName":"POLR1B-RRN3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q9H9Y6;Q9NYV6","subunits.Entrez.IDs.":"84172;54700","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0009303","GO.description":"rRNA transcription","FunCat.ID":"11.02.01","FunCat.description":"rRNA synthesis","PubMed.ID":15558034,"subunits.Protein.name.":"DNA-directed RNA polymerase I subunit RPA2 ;RNA polymerase I-specific transcription initiation factor RRN3","subunits.Gene.name.":"POLR1B;RRN3","subunits.Gene.name.syn.":";TIFIA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1559,"ComplexName":"NMI-RRN3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q13287;Q9NYV6","subunits.Entrez.IDs.":"9111;54700","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0009303","GO.description":"rRNA transcription","FunCat.ID":"11.02.01","FunCat.description":"rRNA synthesis","PubMed.ID":15558034,"subunits.Protein.name.":"N-myc-interactor ;RNA polymerase I-specific transcription initiation factor RRN3","subunits.Gene.name.":"NMI;RRN3","subunits.Gene.name.syn.":";TIFIA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1560,"ComplexName":"Nmi-Rrn3 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"B2RS91;O35309","subunits.Entrez.IDs.":"106298;64685","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0009303","GO.description":"rRNA transcription","FunCat.ID":"11.02.01","FunCat.description":"rRNA synthesis","PubMed.ID":15558034,"subunits.Protein.name.":"RNA polymerase I-specific transcription initiation factor RRN3;N-myc-interactor","subunits.Gene.name.":"Rrn3;Nmi","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1561,"ComplexName":"NMI homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q13287","subunits.Entrez.IDs.":"9111","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006461","GO.description":"protein complex assembly","FunCat.ID":"14.1","FunCat.description":"assembly of protein complexes","PubMed.ID":11916966,"subunits.Protein.name.":"N-myc-interactor","subunits.Gene.name.":"NMI","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Homodimerization of Nmi enhanced its association with BRCA1.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":1571,"ComplexName":"Vigilin-DNA-PK-Ku antigen complex","Organism":"Human","Synonyms":"vigilin-Ku70-Ku86-DNA-PKcs complex","Cell.line":"None","subunits.UniProt.IDs.":"P12956;P13010;P78527;Q00341","subunits.Entrez.IDs.":"2547;7520;5591;3069","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0007059;GO:0006468;GO:0006470;GO:0046777;GO:0003723;GO:0005694","GO.description":"chromosome segregation;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;RNA binding;chromosome","FunCat.ID":"10.03.04.05;14.07.03;16.03.03;70.10.03","FunCat.description":"chromosome segregation/division;modification by phosphorylation, dephosphorylation, autophosphorylation;RNA binding;chromosome","PubMed.ID":15723802,"subunits.Protein.name.":"X-ray repair cross-complementing protein 6 ;X-ray repair cross-complementing protein 5 ;DNA-dependent protein kinase catalytic subunit ;Vigilin","subunits.Gene.name.":"XRCC6;XRCC5;PRKDC;HDLBP","subunits.Gene.name.syn.":"G22P1;G22P2;HYRC HYRC1;HBP VGL","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors describe, that in the presence of RNA, the Vigilin complex recruits the DNA-PKcs enzyme, which appears to phosphorylate a discrete set of targets, some or all of which are known to participate in chromatin silencing.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1589,"ComplexName":"Junb-Sumo1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P09450;P63166","subunits.Entrez.IDs.":"16477;22218","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":10788439,"subunits.Protein.name.":"Transcription factor jun-B ;Small ubiquitin-related modifier 1","subunits.Gene.name.":"Junb;Sumo1","subunits.Gene.name.syn.":"Jun-b;Smt3c Smt3h3 Ubl1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1595,"ComplexName":"Cdk5-c-Abl-Cables complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P00520;P49615;Q9ESJ1","subunits.Entrez.IDs.":"11350;12568;63955","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0007399","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;nervous system development","FunCat.ID":"14.07.03;47.03.01","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;nervous system","PubMed.ID":10896159,"subunits.Protein.name.":"Tyrosine-protein kinase ABL1 ;Cyclin-dependent-like kinase 5 ;CDK5 and ABL1 enzyme substrate 1","subunits.Gene.name.":"Abl1;Cdk5;Cables1","subunits.Gene.name.syn.":"Abl;Cdkn5 Crk6;Cables","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Data suggest that Cables and Cdk5 tyrosine phosphorylation are involved in axon growth regulation.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1602,"ComplexName":"Cdk5-p35-CaMKII(alpha)-(alpha)actinin1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P11275;P61810;Q03114;Q9Z1P2","subunits.Entrez.IDs.":"25400;116671;140908;81634","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0000278;GO:0051726;GO:0035556;GO:0016477;GO:0022008;GO:0048699;GO:0030182;GO:0007420","GO.description":"mitotic cell cycle;regulation of cell cycle;intracellular signal transduction;cell migration;neurogenesis;generation of neurons;neuron differentiation;brain development","FunCat.ID":"10.03.01.01;10.03.01;30.01;34.05.01;41.05.13;43.03.13;47.03.01.01.01","FunCat.description":"mitotic cell cycle;mitotic cell cycle and cell cycle control;cellular signalling;cell migration;neurogenesis;neuron;brain","PubMed.ID":12223541,"subunits.Protein.name.":"Calcium/calmodulin-dependent protein kinase type II subunit alpha ;Cyclin-dependent kinase 5 activator 1 ;Cyclin-dependent-like kinase 5 ;Alpha-actinin-1","subunits.Gene.name.":"Camk2a;Cdk5r1;Cdk5;Actn1","subunits.Gene.name.syn.":";Cdk5r;Cdkn5;None","Disease.comment":"Cdk5 might be a potential drug target for the treatment of neurodegenerative diseases.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":1608,"ComplexName":"Kir3.2 homotetramer complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P48542","subunits.Entrez.IDs.":"16522","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0008324;GO:0006812;GO:0005216","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity","FunCat.ID":"20.01.01.01;20.03.01.01","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels","PubMed.ID":15723059,"subunits.Protein.name.":"G protein-activated inward rectifier potassium channel 2","subunits.Gene.name.":"Kcnj6","subunits.Gene.name.syn.":"Girk2 Kcnj7 W","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse)"}
{"ComplexID":1609,"ComplexName":"G protein complex (Gngt2, Kcnj3, Gnb1)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62874;P63250;Q61017","subunits.Entrez.IDs.":"14688;16519;14710","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0007186;GO:0023052","GO.description":"G-protein coupled receptor signaling pathway;signaling","FunCat.ID":"30.05.02.24;30.01","FunCat.description":"G-protein coupled receptor signalling pathway;cellular signalling","PubMed.ID":12743112,"subunits.Protein.name.":"Guanine nucleotide-binding protein G;G protein-activated inward rectifier potassium channel 1 ;Guanine nucleotide-binding protein G","subunits.Gene.name.":"Gnb1;Kcnj3;Gngt2","subunits.Gene.name.syn.":";Girk1;Gng8 Gngt8","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1610,"ComplexName":"G protein complex (Gngt2, Kcnj6, Gnb1)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P48542;P62874;Q61017","subunits.Entrez.IDs.":"16522;14688;14710","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0007186;GO:0023052","GO.description":"G-protein coupled receptor signaling pathway;signaling","FunCat.ID":"30.05.02.24;30.01","FunCat.description":"G-protein coupled receptor signalling pathway;cellular signalling","PubMed.ID":12743112,"subunits.Protein.name.":"G protein-activated inward rectifier potassium channel 2 ;Guanine nucleotide-binding protein G;Guanine nucleotide-binding protein G","subunits.Gene.name.":"Kcnj6;Gnb1;Gngt2","subunits.Gene.name.syn.":"Girk2 Kcnj7 W;;Gng8 Gngt8","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1612,"ComplexName":"Heterotrimeric G protein complex (GNG2, GNB1, GNAS)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P59768;P62873;P63092","subunits.Entrez.IDs.":"54331;2782;2778","Protein.complex.purification.method":"MI:0051- fluorescence technologies","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":15782186,"subunits.Protein.name.":"Guanine nucleotide-binding protein G;Guanine nucleotide-binding protein G;Guanine nucleotide-binding protein G","subunits.Gene.name.":"GNG2;GNB1;GNAS","subunits.Gene.name.syn.":"None;None;GNAS1 GSP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Guanine nucleotide-binding proteins  (G proteins) are composed of 3  units, alpha, beta and gamma and  are involved in various transmembrane  signaling systems.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1614,"ComplexName":"G protein complex (MCF2, GNB1, GNG2)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P10911;P59768;P62873","subunits.Entrez.IDs.":"4168;54331;2782","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007186","GO.description":"G-protein coupled receptor signaling pathway","FunCat.ID":"30.05.02.24","FunCat.description":"G-protein coupled receptor signalling pathway","PubMed.ID":10518015,"subunits.Protein.name.":"Proto-oncogene DBL ;Guanine nucleotide-binding protein G;Guanine nucleotide-binding protein G","subunits.Gene.name.":"MCF2;GNG2;GNB1","subunits.Gene.name.syn.":"DBL;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1615,"ComplexName":"G protein complex (BTK, GNG1, GNG2)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P59768;P62873;Q06187","subunits.Entrez.IDs.":"54331;2782;695","Protein.complex.purification.method":"MI:0047-far western blotting","GO.ID":"GO:0007186;GO:0030154","GO.description":"G-protein coupled receptor signaling pathway;cell differentiation","FunCat.ID":"30.05.02.24;40.02","FunCat.description":"G-protein coupled receptor signalling pathway;cell differentiation","PubMed.ID":7972043,"subunits.Protein.name.":"Guanine nucleotide-binding protein G;Guanine nucleotide-binding protein G;Tyrosine-protein kinase BTK","subunits.Gene.name.":"GNG2;GNB1;BTK","subunits.Gene.name.syn.":"None;None;AGMX1 ATK BPK","Disease.comment":"Deficient expression or function of Bruton tyrosine kinase (Btk) causes human X chromosome-linked agammaglobulinemia (XLA) or murine X chromosome-linked immunodeficiency (XID).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1617,"ComplexName":"G protein complex (CACNA1A, GNB1, GNG2)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00555;P59768;P62873","subunits.Entrez.IDs.":"773;54331;2782","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0007186","GO.description":"G-protein coupled receptor signaling pathway","FunCat.ID":"30.05.02.24","FunCat.description":"G-protein coupled receptor signalling pathway","PubMed.ID":9238069,"subunits.Protein.name.":"Voltage-dependent P/Q-type calcium channel subunit alpha-1A ;Guanine nucleotide-binding protein G;Guanine nucleotide-binding protein G","subunits.Gene.name.":"CACNA1A;GNG2;GNB1","subunits.Gene.name.syn.":"CACH4 CACN3 CACNL1A4;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The direct interaction of the G proteins (beta, gamma) with the Ca-channel alpha 1 subunit  is responsible for the channel inhibition by  G protein-coupled receptors.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1618,"ComplexName":"G protein complex (PTHR1, GNB1, GNG2)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P59768;P62873;Q03431","subunits.Entrez.IDs.":"54331;2782;5745","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0007186","GO.description":"G-protein coupled receptor signaling pathway","FunCat.ID":"30.05.02.24","FunCat.description":"G-protein coupled receptor signalling pathway","PubMed.ID":16099817,"subunits.Protein.name.":"Guanine nucleotide-binding protein G;Guanine nucleotide-binding protein G;Parathyroid hormone/parathyroid hormone-related peptide receptor","subunits.Gene.name.":"GNG2;GNB1;PTH1R","subunits.Gene.name.syn.":"None;None;PTHR, PTHR1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The G protein-coupled receptor for PTH-related protein (PTH1R) signals via many intracellular pathways.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1619,"ComplexName":"G protein complex (HDAC5, GNB1, GNG2)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P59768;P62873;Q9UQL6","subunits.Entrez.IDs.":"54331;2782;10014","Protein.complex.purification.method":"MI:0018- two hybrid; MI:0019- coimmunoprecipitation","GO.ID":"GO:0045892;GO:0007186","GO.description":"negative regulation of transcription, DNA-templated;G-protein coupled receptor signaling pathway","FunCat.ID":"11.02.03.04.03;30.05.02.24","FunCat.description":"transcription repression;G-protein coupled receptor signalling pathway","PubMed.ID":16221676,"subunits.Protein.name.":"Guanine nucleotide-binding protein G;Guanine nucleotide-binding protein G;Histone deacetylase 5","subunits.Gene.name.":"GNG2;GNB1;HDAC5","subunits.Gene.name.syn.":"None;None;KIAA0600","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The class II HDAC5 binds to GNB1/GNG2 via its C-terminal domain. The transcriptional co-repression activity is then inhibited.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1620,"ComplexName":"G protein complex (HDAC4, GNB1, GNG2)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P56524;P59768;P62873","subunits.Entrez.IDs.":"9759;54331;2782","Protein.complex.purification.method":"MI:0018- two hybrid; MI:0019- coimmunoprecipitation","GO.ID":"GO:0045892;GO:0007186","GO.description":"negative regulation of transcription, DNA-templated;G-protein coupled receptor signaling pathway","FunCat.ID":"11.02.03.04.03;30.05.02.24","FunCat.description":"transcription repression;G-protein coupled receptor signalling pathway","PubMed.ID":16221676,"subunits.Protein.name.":"Histone deacetylase 4 ;Guanine nucleotide-binding protein G;Guanine nucleotide-binding protein G","subunits.Gene.name.":"HDAC4;GNG2;GNB1","subunits.Gene.name.syn.":"KIAA0288;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The class II HDAC4 binds to GNB1/GNG2 via its C-terminal domain. The transcriptional co-repression activity is then inhibited.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1623,"ComplexName":"FA core complex 1 (Fanconi anemia core complex 1)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15287;O15360;Q00597;Q9HB96;Q9NPI8","subunits.Entrez.IDs.":"2189;2175;2176;2178;2188","Protein.complex.purification.method":"MI:0027- cosedimentation","GO.ID":"GO:0016567;GO:0016579;GO:0006974;GO:0005634","GO.description":"protein ubiquitination;protein deubiquitination;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"14.07.05;32.01.09;70.10","FunCat.description":"modification by ubiquitination, deubiquitination;DNA damage response;nucleus","PubMed.ID":12093742,"subunits.Protein.name.":"Fanconi anemia group G protein ;Fanconi anemia group A protein ;Fanconi anemia group C protein ;Fanconi anemia group E protein ;Fanconi anemia group F protein","subunits.Gene.name.":"FANCG;FANCA;FANCC;FANCE;FANCF","subunits.Gene.name.syn.":"XRCC9;FAA FACA FANCH;FAC FACC;FACE;","Disease.comment":"FA complex is involved in Fanconi anemia (FA) disease.","Subunits.comment":"None","Complex.comment":"FANCE functions to target cytoplasmic FANCC to the nucleus.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1624,"ComplexName":"FA core complex (Fanconi anemia core complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15287;O15360;Q00597;Q0VG06;Q8IYD8;Q8NB91;Q9HB96;Q9NPI8;Q9NW38","subunits.Entrez.IDs.":"2189;2175;2176;80233;57697;2187;2178;2188;55120","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0006974;GO:0005634","GO.description":"protein ubiquitination;protein deubiquitination;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"14.07.05;32.01.09;70.10","FunCat.description":"modification by ubiquitination, deubiquitination;DNA damage response;nucleus","PubMed.ID":15502827,"subunits.Protein.name.":"Fanconi anemia group G protein ;Fanconi anemia group A protein ;Fanconi anemia group C protein ;Fanconi anemia core complex-associated protein 100 ;Fanconi anemia group M protein ;Fanconi anemia group B protein ;Fanconi anemia group E protein ;Fanconi anemia group F protein ;E3 ubiquitin-protein ligase FANCL","subunits.Gene.name.":"FANCG;FANCA;FANCC;FAAP100;FANCM;FANCB;FANCE;FANCF;FANCL","subunits.Gene.name.syn.":"XRCC9;FAA FACA FANCH;FAC FACC;C17orf70;KIAA1596;;FACE;;PHF9","Disease.comment":"FA complex is involved in Fanconi anemia (FA) disease.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1625,"ComplexName":"FA core complex (Fanconi anemia core complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15287;O15360;Q00597;Q8IYD8;Q8NB91;Q9HB96;Q9NPI8","subunits.Entrez.IDs.":"2189;2175;2176;57697;2187;2178;2188","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0006974;GO:0005634","GO.description":"protein ubiquitination;protein deubiquitination;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"14.07.05;32.01.09;70.10","FunCat.description":"modification by ubiquitination, deubiquitination;DNA damage response;nucleus","PubMed.ID":16116434,"subunits.Protein.name.":"Fanconi anemia group G protein ;Fanconi anemia group A protein ;Fanconi anemia group C protein ;Fanconi anemia group M protein ;Fanconi anemia group B protein ;Fanconi anemia group E protein ;Fanconi anemia group F protein","subunits.Gene.name.":"FANCG;FANCA;FANCC;FANCM;FANCB;FANCE;FANCF","subunits.Gene.name.syn.":"XRCC9;FAA FACA FANCH;FAC FACC;KIAA1596;;FACE;","Disease.comment":"FA complex is involved in Fanconi anemia (FA) disease.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1633,"ComplexName":"CyclinD1-CDK4-CDK6 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P11802;P24385;Q00534","subunits.Entrez.IDs.":"1019;595;1021","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0000278;GO:0000082;GO:0035556;GO:0007519","GO.description":"mitotic cell cycle;G1/S transition of mitotic cell cycle;intracellular signal transduction;skeletal muscle tissue development","FunCat.ID":"10.03.01.01;10.03.01.01.03;30.01;41.05.15","FunCat.description":"mitotic cell cycle;G1/S transition of mitotic cell cycle;cellular signalling;myogenesis","PubMed.ID":8930396,"subunits.Protein.name.":"Cyclin-dependent kinase 4 ;G1/S-specific cyclin-D1;Cyclin-dependent kinase 6","subunits.Gene.name.":"CDK4;CCND1;CDK6","subunits.Gene.name.syn.":";BCL1 PRAD1;CDKN6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Upon myocyte differentiation subunit composition of the CDK4/6 complex is altered. Interaction with cyclinD1 is reduced but interaction with cyclinD3 and p21 is enhanced thus inhibiting the kinase activity of CDK4/6.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1634,"ComplexName":"CyclinD1-CDK4-p21 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"BHK21 cells","subunits.UniProt.IDs.":"P11802;P24385;P38936","subunits.Entrez.IDs.":"1019;595;1026","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0007050;GO:0035556","GO.description":"cell cycle arrest;intracellular signal transduction","FunCat.ID":"10.03.01.02;30.01","FunCat.description":"cell cycle arrest;cellular signalling","PubMed.ID":9467962,"subunits.Protein.name.":"Cyclin-dependent kinase 4 ;G1/S-specific cyclin-D1;Cyclin-dependent kinase inhibitor 1","subunits.Gene.name.":"CDK4;CCND1;CDKN1A","subunits.Gene.name.syn.":";BCL1 PRAD1;CAP20 CDKN1 CIP1 MDA6 PIC1 SDI1 WAF1","Disease.comment":"None","Subunits.comment":"Since CCND1 and CDK4 from hamster were not available in the Uniprot database at the time of annotation, the orthologous human proteins were used.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1637,"ComplexName":"Ccnd1-Cdk4 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P25322;P30285","subunits.Entrez.IDs.":"12443;12567","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007050","GO.description":"cell cycle arrest","FunCat.ID":"10.03.01.02","FunCat.description":"cell cycle arrest","PubMed.ID":8534916,"subunits.Protein.name.":"G1/S-specific cyclin-D1;Cyclin-dependent kinase 4","subunits.Gene.name.":"Ccnd1;Cdk4","subunits.Gene.name.syn.":"Cyl-1;Crk3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1642,"ComplexName":"p16-cyclin D2-CDK4 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P11802;P30279;P42771","subunits.Entrez.IDs.":"1019;894;1029","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0000278;GO:0051726;GO:0035556","GO.description":"mitotic cell cycle;regulation of cell cycle;intracellular signal transduction","FunCat.ID":"10.03.01.01;10.03.01;30.01","FunCat.description":"mitotic cell cycle;mitotic cell cycle and cell cycle control;cellular signalling","PubMed.ID":7739547,"subunits.Protein.name.":"Cyclin-dependent kinase 4 ;G1/S-specific cyclin-D2;Cyclin-dependent kinase inhibitor 2A","subunits.Gene.name.":"CDK4;CCND2;CDKN2A","subunits.Gene.name.syn.":";;CDKN2 MTS1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"p16 binds to preassembled cyclinD-CDK complex in vitro and inhibits their activity without replacing Cyclin D. However, affinity for p16 to the uncomplexed CDK4 is higher.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1652,"ComplexName":"Ccna2-Cdk2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P51943;P97377","subunits.Entrez.IDs.":"12428;12566","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007050","GO.description":"cell cycle arrest","FunCat.ID":"10.03.01.02","FunCat.description":"cell cycle arrest","PubMed.ID":8534916,"subunits.Protein.name.":"Cyclin-A2 ;Cyclin-dependent kinase 2","subunits.Gene.name.":"Ccna2;Cdk2","subunits.Gene.name.syn.":"Ccna Cyca;Cdkn2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1656,"ComplexName":"p27-cyclinE-CDK2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P24864;P24941;P46527","subunits.Entrez.IDs.":"898;1017;1027","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0000082;GO:0050789;GO:0005634","GO.description":"G1/S transition of mitotic cell cycle;regulation of biological process;nucleus","FunCat.ID":"10.03.01.01.03;18;70.10","FunCat.description":"G1/S transition of mitotic cell cycle;REGULATION OF METABOLISM AND PROTEIN FUNCTION;nucleus","PubMed.ID":17409098,"subunits.Protein.name.":"G1/S-specific cyclin-E1;Cyclin-dependent kinase 2;Cyclin-dependent kinase inhibitor 1B","subunits.Gene.name.":"CCNE1;CDK2;CDKN1B","subunits.Gene.name.syn.":"CCNE;CDKN2;KIP1","Disease.comment":"Overexpression of p27 in certain cancer cells prevents DNA replication and tumor formation in nude mice, whereas the loss of p27 has been reported in many human cancers and predicts a poor prognosis in breast, prostate, colon, gastric, lung, and esophageal cancers.","Subunits.comment":"None","Complex.comment":"p27, an important cell cycle regulator, blocks the G1/S transition in cells by binding and inhibiting Cdk2/cyclin A and Cdk2/cyclin E complexes. Ubiquitination and subsequent degradation play a critical role in regulating the levels of p27 during cell cycle progression.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1661,"ComplexName":"E2F4-p107-cyclinA complex","Organism":"Human","Synonyms":"None","Cell.line":"MCF-7 cells","subunits.UniProt.IDs.":"P20248;P28749;Q16254","subunits.Entrez.IDs.":"890;5933;1874","Protein.complex.purification.method":"MI:0412- electrophoretic mobility supershift assay","GO.ID":"GO:0000082;GO:0005634","GO.description":"G1/S transition of mitotic cell cycle;nucleus","FunCat.ID":"10.03.01.01.03;70.10","FunCat.description":"G1/S transition of mitotic cell cycle;nucleus","PubMed.ID":12096339,"subunits.Protein.name.":"Cyclin-A2 ;Retinoblastoma-like protein 1;Transcription factor E2F4","subunits.Gene.name.":"CCNA2;RBL1;E2F4","subunits.Gene.name.syn.":"CCN1 CCNA;PRB1, p107, CP107;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In proliferating MCF-7 cells the complex contains mostly cyclin A. After overexpression of cyclin E most of the complexes contain cyclin E.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1695,"ComplexName":"SCAMP1-SCAMP2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15126;O15127","subunits.Entrez.IDs.":"9522;10066","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0030- cross-linking studies","GO.ID":"GO:0015031;GO:0008565;GO:0006892","GO.description":"protein transport;protein transporter activity;post-Golgi vesicle-mediated transport","FunCat.ID":"20.01.10;20.09.07.06","FunCat.description":"protein transport;post Golgi transport","PubMed.ID":9224770,"subunits.Protein.name.":"Secretory carrier-associated membrane protein 1 ;Secretory carrier-associated membrane protein 2","subunits.Gene.name.":"SCAMP1;SCAMP2","subunits.Gene.name.syn.":"SCAMP;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1700,"ComplexName":"ABL2-HRAS-RIN1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P01112;P42684;Q13671","subunits.Entrez.IDs.":"3265;27;9610","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0035556","GO.description":"intracellular signal transduction","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":15886098,"subunits.Protein.name.":"GTPase HRas;Abelson tyrosine-protein kinase 2 ;Ras and Rab interactor 1","subunits.Gene.name.":"HRAS;ABL2;RIN1","subunits.Gene.name.syn.":"HRAS1;ABLL ARG;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The formation of this stable complex is consistent with a pathway connecting RAS proteins with the cytoplasmic functions of ABL-family tyrosine kinases through RIN1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1703,"ComplexName":"IGHM-VPREB1-IGLL1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P01871;P12018;P15814","subunits.Entrez.IDs.":"3507;7441;3543","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030183","GO.description":"B cell differentiation","FunCat.ID":"43.03.07.02.01.01","FunCat.description":"B-cell","PubMed.ID":11564802,"subunits.Protein.name.":"Ig mu chain C region;Immunoglobulin iota chain ;Immunoglobulin lambda-like polypeptide 1","subunits.Gene.name.":"IGHM;VPREB1;IGLL1","subunits.Gene.name.syn.":";VPREB;IGL1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1707,"ComplexName":"IL2-IL2RA-IL2RB complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P01589;P14784;P60568","subunits.Entrez.IDs.":"3559;3560;3558","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":2303462,"subunits.Protein.name.":"Interleukin-2 receptor subunit alpha ;Interleukin-2 receptor subunit beta ;Interleukin-2","subunits.Gene.name.":"IL2RA;IL2RB;IL2","subunits.Gene.name.syn.":";;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1714,"ComplexName":"TICAM1-TICAM2-TLR4 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00206;Q86XR7;Q8IUC6","subunits.Entrez.IDs.":"7099;None;148022","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005125","GO.description":"cytokine activity","FunCat.ID":"40.02.03.01","FunCat.description":"cytokines (interleukines, colony stimulating factors, etc.)","PubMed.ID":14519765,"subunits.Protein.name.":"Toll-like receptor 4 ;TIR domain-containing adapter molecule 2 ;TIR domain-containing adapter molecule 1","subunits.Gene.name.":"TLR4;TICAM2;TICAM1","subunits.Gene.name.syn.":";TIRAP3 TIRP TRAM;PRVTIRB TRIF","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TICAM-2 physically bridges TLR4 and TICAM-1 and functionally transmits LPS-TLR4 signaling to TICAM-1, which in turn activates IRF-3.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1723,"ComplexName":"Pax3-Lef1-Tle4 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P24610;P27782;Q62441","subunits.Entrez.IDs.":"18505;16842;21888","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016055","GO.description":"Wnt signaling pathway","FunCat.ID":"30.05.02.20","FunCat.description":"Wnt signalling pathway","PubMed.ID":15729346,"subunits.Protein.name.":"Paired box protein Pax-3;Lymphoid enhancer-binding factor 1 ;Transducin-like enhancer protein 4","subunits.Gene.name.":"Pax3;Lef1;Tle4","subunits.Gene.name.syn.":"Pax-3;Lef-1;Grg4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1724,"ComplexName":"Spen-Hivep1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q03172;Q62504","subunits.Entrez.IDs.":"110521;56381","Protein.complex.purification.method":"MI:0096- pull down; MI:0019- coimmunoprecipitation; MI:0018- two hybrid","GO.ID":"GO:0032774;GO:0001501","GO.description":"RNA biosynthetic process;skeletal system development","FunCat.ID":"11.02;47.03.17","FunCat.description":"RNA synthesis;skeletal system","PubMed.ID":15778499,"subunits.Protein.name.":"Zinc finger protein 40 ;Msx2-interacting protein","subunits.Gene.name.":"Hivep1;Spen","subunits.Gene.name.syn.":"Cryabp1 Znf40;Kiaa0929 Mint Sharp","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"MINT and CRYBP1 form a complex on the Col2a1 enhancer.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1728,"ComplexName":"CTCF-nucleophosmin-PARP-HIS-KPNA-LMNA-TOP complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00505;P02545;P06748;P09874;P0C0S5;P11388;P49711;P52294;Q6FI13","subunits.Entrez.IDs.":"None;4000;4869;142;3015;7153;10664;3836;None","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0029- cosedimentation through density gradients; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;nucleus","FunCat.ID":"11.02.03.04;70.10","FunCat.description":"transcriptional control;nucleus","PubMed.ID":14759373,"subunits.Protein.name.":"Importin subunit alpha-4 ;Prelamin-A/C [Cleaved into: Lamin-A/C ;Nucleophosmin ;Poly [ADP-ribose] polymerase 1;Histone H2A.Z ;DNA topoisomerase 2-alpha;Transcriptional repressor CTCF ;Importin subunit alpha-5;Histone H2A type 2-A","subunits.Gene.name.":"KPNA3;LMNA;NPM1;PARP1;H2AFZ;TOP2A;CTCF;KPNA1;HIST2H2AA3","subunits.Gene.name.syn.":"QIP2;LMN1;NPM;ADPRT PPOL;H2AZ;TOP2;;RCH2;H2AFO HIST2H2AA;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Nucleophosmin is the most prominent binding partner of CTCF.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1729,"ComplexName":"TLE1 corepressor complex (MASH1 promoter-corepressor complex)","Organism":"Human","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P06748;P09874;P19338;P34932;P35580;P60709;Q02880;Q04724;Q15233;Q92878","subunits.Entrez.IDs.":"4869;142;4691;3308;4628;60;7155;7088;4841;10111","Protein.complex.purification.method":"MI:0676- tandem affinity purification;MI:0007- anti tag coimmunoprecipitation;MI:0402- chromatin immunoprecipitation assays","GO.ID":"GO:0045892;GO:0005515;GO:0003677;GO:0051098;GO:0051090;GO:0030182;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;protein binding;DNA binding;regulation of binding;regulation of sequence-specific DNA binding transcription factor activity;neuron differentiation;nucleus","FunCat.ID":"11.02.03.04.03;16.01;16.03.01;18.01.07;18.02.09;43.03.13;70.10","FunCat.description":"transcription repression;protein binding;DNA binding;regulation by binding / dissociation;regulator of transcription factor;neuron;nucleus","PubMed.ID":15607978,"subunits.Protein.name.":"Nucleophosmin ;Poly [ADP-ribose] polymerase 1;Nucleolin ;Heat shock 70 kDa protein 4;Myosin-10 ;Actin, cytoplasmic 1;DNA topoisomerase 2-beta ;Transducin-like enhancer protein 1;Non-POU domain-containing octamer-binding protein;DNA repair protein RAD50","subunits.Gene.name.":"NPM1;PARP1;NCL;HSPA4;MYH10;ACTB;TOP2B;TLE1;NONO;RAD50","subunits.Gene.name.syn.":"NPM;ADPRT PPOL;;APG2;;None;;None;NRB54;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The TLE1 complex is required for HES1-mediated transcription repression. PARP1 is inactive in the TLE1 complex. After Ca(2+) induction, kinase CaMKII-delta activates PARP1 leading to dismissal of the TLE1 corepresspor complex from HES1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1730,"ComplexName":"Nfatc2ip-Prmt1","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O09130;Q60591;Q9JIF0","subunits.Entrez.IDs.":"18020;18019;15469","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":15327772,"subunits.Protein.name.":"NFATC2-interacting protein ;Nuclear factor of activated T-cells, cytoplasmic 2 ;Protein arginine N-methyltransferase 1","subunits.Gene.name.":"Nfatc2ip;Nfatc2;Prmt1","subunits.Gene.name.syn.":"Nip45;Nfat1 Nfatp;Hrmt1l2 Mrmt1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"NFATc2, NIP45, and PRMT1 form a ternary complex as evidenced by the fact that PRMT1 and NFATc2 association is substantially promoted by the presence of full-length NIP45 but much less so by the presence of ?N-NIP45. he amino terminus of NIP45 may serve a dual function in supporting NFAT interaction and recruiting PRMT1 to the NFAT transcription-activating complex.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1731,"ComplexName":"PRMT1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q99873","subunits.Entrez.IDs.":"3276","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0018126;GO:0006479;GO:0005634","GO.description":"protein hydroxylation;protein methylation;nucleus","FunCat.ID":"14.07.09;70.10","FunCat.description":"posttranslational modification of amino acids (e.g. hydroxylation, methylation);nucleus","PubMed.ID":11152681,"subunits.Protein.name.":"Protein arginine N-methyltransferase 1","subunits.Gene.name.":"PRMT1","subunits.Gene.name.syn.":"HMT2 HRMT1L2 IR1B4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"PRMT1 (protein-arginine methyltransferase) formes distinct homo-oligomeric complexes, including a dimer and tetramer.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":1734,"ComplexName":"SF3A1-SF3A2-SF3A3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q12874;Q15428;Q15459","subunits.Entrez.IDs.":"10946;8175;10291","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008380;GO:0005634","GO.description":"RNA splicing;nucleus","FunCat.ID":"11.04.03.01;70.10","FunCat.description":"splicing;nucleus","PubMed.ID":11533230,"subunits.Protein.name.":"Splicing factor 3A subunit 3 ;Splicing factor 3A subunit 2 ;Splicing factor 3A subunit 1","subunits.Gene.name.":"SF3A3;SF3A2;SF3A1","subunits.Gene.name.syn.":"SAP61;SAP62;SAP114","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"All SF3A subunits are essential for the formation of the mature 17S U2 snRNP and the prespliceosome.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1737,"ComplexName":"SF3b complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75533;Q13435;Q15393;Q15427;Q7RTV0;Q86XP3;Q9BWJ5;Q9Y3B4","subunits.Entrez.IDs.":"23451;10992;23450;10262;84844;11325;83443;51639","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008380;GO:0005634","GO.description":"RNA splicing;nucleus","FunCat.ID":"11.04.03.01;70.10","FunCat.description":"splicing;nucleus","PubMed.ID":12234937,"subunits.Protein.name.":"Splicing factor 3B subunit 1 ;Splicing factor 3B subunit 2 ;Splicing factor 3B subunit 3;Splicing factor 3B subunit 4 ;PHD finger-like domain-containing protein 5A ;ATP-dependent RNA helicase DDX42 ;Splicing factor 3B subunit 5 ;Splicing factor 3B subunit 6","subunits.Gene.name.":"SF3B1;SF3B2;SF3B3;SF3B4;PHF5A;DDX42;SF3B5;SF3B6","subunits.Gene.name.syn.":"SAP155;SAP145;KIAA0017 SAP130;SAP49;;;SF3B10;SAP14 SF3B14 SF3B14A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The splicing factor SF3b is a multiprotein complex essential for the accurate excision of introns from pre-messenger RNA (PMID:12738865).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1743,"ComplexName":"(E.F.G) complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62304;P62306;P62308","subunits.Entrez.IDs.":"6635;6636;6637","Protein.complex.purification.method":"MI:0114- x-ray crystallography; MI:0028- cosedimentation in solution","GO.ID":"GO:0008380;GO:0005634","GO.description":"RNA splicing;nucleus","FunCat.ID":"11.04.03.01;70.10","FunCat.description":"splicing;nucleus","PubMed.ID":9020971,"subunits.Protein.name.":"Small nuclear ribonucleoprotein E ;Small nuclear ribonucleoprotein F ;Small nuclear ribonucleoprotein G","subunits.Gene.name.":"SNRPE;SNRPF;SNRPG","subunits.Gene.name.syn.":";PBSCF;PBSCG","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"All four spliceosomal small nuclear ribonucleoproteins (snRNPs) U1, U2, U4/U6 and U5 contain a common structural element called the snRNP core. This core is assembled from the common snRNP proteins and the small nuclear RNA (snRNA). The RNA-free (E.F.G) complex contains the smallest U1 and U5 snRNP core proteins, i.e. E, F and G.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1745,"ComplexName":"SMN complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14893;P09012;P14678;P57678;P62304;P62306;P62308;P62314;P62316;P62318;P63162;Q8TEQ6;Q8WXD5;Q9H840;Q9UHI6","subunits.Entrez.IDs.":"8487;6626;6628;50628;6635;6636;6637;6632;6633;6634;6638;25929;79833;79760;11218","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0008380;GO:0032774;GO:0006461;GO:0003723;GO:0005737;GO:0005634","GO.description":"RNA splicing;RNA biosynthetic process;protein complex assembly;RNA binding;cytoplasm;nucleus","FunCat.ID":"11.04.03.01;11.02;14.10;16.03.03;70.03;70.10","FunCat.description":"splicing;RNA synthesis;assembly of protein complexes;RNA binding;cytoplasm;nucleus","PubMed.ID":11748230,"subunits.Protein.name.":"Gem-associated protein 2 ;U1 small nuclear ribonucleoprotein A ;Small nuclear ribonucleoprotein-associated proteins B and B' ;Gem-associated protein 4 ;Small nuclear ribonucleoprotein E ;Small nuclear ribonucleoprotein F ;Small nuclear ribonucleoprotein G ;Small nuclear ribonucleoprotein Sm D1 ;Small nuclear ribonucleoprotein Sm D2 ;Small nuclear ribonucleoprotein Sm D3 ;Small nuclear ribonucleoprotein-associated protein N ;Gem-associated protein 5 ;Gem-associated protein 6 ;Gem-associated protein 7 ;Probable ATP-dependent RNA helicase DDX20","subunits.Gene.name.":"GEMIN2;SNRPA;SNRPB;GEMIN4;SNRPE;SNRPF;SNRPG;SNRPD1;SNRPD2;SNRPD3;SNRPN;GEMIN5;GEMIN6;GEMIN7;DDX20","subunits.Gene.name.syn.":"SIP1;;COD SNRPB1;;;PBSCF;PBSCG;;SNRPD1;;HCERN3 SMN;;;;DP103 GEMIN3","Disease.comment":"Spinal muscular atrophy (SMA) is the most common genetic cause of infant mortality.  Deletions or mutations in the survival of motor neurons (SMN1) gene, the SMA-causing gene, are detected in over 95% of SMA patients.","Subunits.comment":"None","Complex.comment":"Assembly of the Sm-class of U-rich small nuclear ribonucleoprotein particles  (U snRNPs) is a process facilitated by the macromolecular survival of motor  neuron (SMN) complex.  The SMN complex is found both in the cytoplasm and in the nucleus, where it is concentrated in gems, nuclear bodies similar in size and number to Cajal (coiled) bodies and often associated with them.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1746,"ComplexName":"SMN containing complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14893;P09382;P17931;P57678;P62314;P62316;P62318;Q16637","subunits.Entrez.IDs.":"8487;3956;3958;50628;6632;6633;6634;None","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008380;GO:0032774;GO:0006461;GO:0003723;GO:0005634","GO.description":"RNA splicing;RNA biosynthetic process;protein complex assembly;RNA binding;nucleus","FunCat.ID":"11.04.03.01;11.02;14.10;16.03.03;70.10","FunCat.description":"splicing;RNA synthesis;assembly of protein complexes;RNA binding;nucleus","PubMed.ID":11522829,"subunits.Protein.name.":"Gem-associated protein 2 ;Galectin-1 ;Galectin-3 ;Gem-associated protein 4 ;Small nuclear ribonucleoprotein Sm D1 ;Small nuclear ribonucleoprotein Sm D2 ;Small nuclear ribonucleoprotein Sm D3 ;Survival motor neuron protein","subunits.Gene.name.":"GEMIN2;LGALS1;LGALS3;GEMIN4;SNRPD1;SNRPD2;SNRPD3;SMN1; SMN2","subunits.Gene.name.syn.":"SIP1;;MAC2;;;SNRPD1;;SMN; SMNT; SMNC","Disease.comment":"Spinal muscular atrophy (SMA), (PMID:10601333)","Subunits.comment":"None","Complex.comment":"Evidence suggests a role for SMN containing complex in spliceosome assembly.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1748,"ComplexName":"PRMT5 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14744","subunits.Entrez.IDs.":"10419","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0018126;GO:0006479;GO:0005737","GO.description":"protein hydroxylation;protein methylation;cytoplasm","FunCat.ID":"14.07.09;70.03","FunCat.description":"posttranslational modification of amino acids (e.g. hydroxylation, methylation);cytoplasm","PubMed.ID":11152681,"subunits.Protein.name.":"Protein arginine N-methyltransferase 5","subunits.Gene.name.":"PRMT5","subunits.Gene.name.syn.":"HRMT1L5 IBP72 JBP1 SKB1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"PRMT5 (protein-arginine methyltransferase) formes distinct homo-oligomeric complexes, including a dimer and tetramer. Recombinant PRMT5 protein methylates myelin basic protein, histone, and the amino terminus of fibrillarin.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":1749,"ComplexName":"SMN-PolII-RHA complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14893;P08579;P14678;P20226;P24928;P57678;P63162;Q00403;Q08211;Q9UHI6","subunits.Entrez.IDs.":"8487;6629;6628;6908;5430;50628;6638;2959;1660;11218","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008380;GO:0032774;GO:0006461;GO:0003723;GO:0005737;GO:0005634","GO.description":"RNA splicing;RNA biosynthetic process;protein complex assembly;RNA binding;cytoplasm;nucleus","FunCat.ID":"11.04.03.01;11.02;14.10;16.03.03;70.03;70.10","FunCat.description":"splicing;RNA synthesis;assembly of protein complexes;RNA binding;cytoplasm;nucleus","PubMed.ID":11149922,"subunits.Protein.name.":"Gem-associated protein 2 ;U2 small nuclear ribonucleoprotein B'' ;Small nuclear ribonucleoprotein-associated proteins B and B' ;TATA-box-binding protein;DNA-directed RNA polymerase II subunit RPB1;Gem-associated protein 4 ;Small nuclear ribonucleoprotein-associated protein N ;Transcription initiation factor IIB;ATP-dependent RNA helicase A ;Probable ATP-dependent RNA helicase DDX20","subunits.Gene.name.":"GEMIN2;SNRPB2;SNRPB;TBP;POLR2A;GEMIN4;SNRPN;GTF2B;DHX9;DDX20","subunits.Gene.name.syn.":"SIP1;;COD SNRPB1;GTF2D1 TF2D TFIID;POLR2;;HCERN3 SMN;TF2B TFIIB;DDX9 LKP NDH2;DP103 GEMIN3","Disease.comment":"Spinal muscular atrophy (SMA)","Subunits.comment":"None","Complex.comment":"Physical association between the Survival Motor Neuron (SMN) complex,  RNA polymerase II (pol II), snRNPs and RNA helicase A (RHA) suggest a role  for the SMN complex in the assembly of the pol II transcription/processing machinery.  SMN localizes both in the cytoplasm and in gems, nuclear bodies similar in size and  number to coiled bodies (Cajal bodies) and often associated with them.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1750,"ComplexName":"PPP4C-PPP4R2-Gemin3-Gemin4 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P57678;P60510;Q9NY27;Q9UHI6","subunits.Entrez.IDs.":"50628;5531;151987;11218","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0005634","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;nucleus","FunCat.ID":"14.07.03;70.10","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;nucleus","PubMed.ID":12668731,"subunits.Protein.name.":"Gem-associated protein 4 ;Serine/threonine-protein phosphatase 4 catalytic subunit ;Serine/threonine-protein phosphatase 4 regulatory subunit 2;Probable ATP-dependent RNA helicase DDX20","subunits.Gene.name.":"GEMIN4;PPP4C;PPP4R2;DDX20","subunits.Gene.name.syn.":";PPP4 PPX;;DP103 GEMIN3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"PPP4c is a member of the PPP family of protein phosphatases. PPP4 exists as high molecular mass complex of 450-600 kDa, and two putative regulatory subunits have been identified, R1 and R2. Protein phosphatase 4 interacts also with the Survival of Motor Neurons (SMN) complex and enhances the temporal localisation of snRNPs.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1751,"ComplexName":"SMN complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14893;P09012;P14678;P57678;Q16637;Q8TEQ6;Q8WXD5;Q9H840;Q9UHI6;Q9Y3F4","subunits.Entrez.IDs.":"8487;6626;6628;50628;None;25929;79833;79760;11218;11171","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0008380;GO:0032774;GO:0006461;GO:0003723;GO:0006811;GO:0050658;GO:0051033;GO:0051169;GO:0005737;GO:0005634","GO.description":"RNA splicing;RNA biosynthetic process;protein complex assembly;RNA binding;ion transport;RNA transport;RNA transmembrane transporter activity;nuclear transport;cytoplasm;nucleus","FunCat.ID":"11.04.03.01;11.02;14.10;16.03.03;20.01.01;20.01.21;20.09.01;70.03;70.10","FunCat.description":"splicing;RNA synthesis;assembly of protein complexes;RNA binding;ion transport;RNA transport;nuclear transport;cytoplasm;nucleus","PubMed.ID":15494309,"subunits.Protein.name.":"Gem-associated protein 2 ;U1 small nuclear ribonucleoprotein A ;Small nuclear ribonucleoprotein-associated proteins B and B' ;Gem-associated protein 4 ;Survival motor neuron protein;Gem-associated protein 5 ;Gem-associated protein 6 ;Gem-associated protein 7 ;Probable ATP-dependent RNA helicase DDX20 ;Serine-threonine kinase receptor-associated protein","subunits.Gene.name.":"GEMIN2;SNRPA;SNRPB;GEMIN4;SMN1; SMN2;GEMIN5;GEMIN6;GEMIN7;DDX20;STRAP","subunits.Gene.name.syn.":"SIP1;;COD SNRPB1;;SMN; SMNT; SMNC;;;;DP103 GEMIN3;MAWD UNRIP","Disease.comment":"Spinal muscular atrophy (SMA)","Subunits.comment":"None","Complex.comment":"Survival of motor neurons (SMN) protein import depends on the presence of Sm snRNPs.  Conversely, import of labeled U1 snRNPs was SMN complex dependent.  Thus, import of SMN and U snRNPs are coupled in spinal muscular atrophy (SMA).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1752,"ComplexName":"SMN complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14893;P57678;Q16637;Q8TEQ6;Q8WXD5;Q9H840;Q9UHI6","subunits.Entrez.IDs.":"8487;50628;None;25929;79833;79760;11218","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0008380;GO:0032774;GO:0006461;GO:0003723;GO:0005737;GO:0005634","GO.description":"RNA splicing;RNA biosynthetic process;protein complex assembly;RNA binding;cytoplasm;nucleus","FunCat.ID":"11.04.03.01;11.02;14.10;16.03.03;70.03;70.10","FunCat.description":"splicing;RNA synthesis;assembly of protein complexes;RNA binding;cytoplasm;nucleus","PubMed.ID":12065586,"subunits.Protein.name.":"Gem-associated protein 2 ;Gem-associated protein 4 ;Survival motor neuron protein;Gem-associated protein 5 ;Gem-associated protein 6 ;Gem-associated protein 7 ;Probable ATP-dependent RNA helicase DDX20","subunits.Gene.name.":"GEMIN2;GEMIN4;SMN1; SMN2;GEMIN5;GEMIN6;GEMIN7;DDX20","subunits.Gene.name.syn.":"SIP1;;SMN; SMNT; SMNC;;;;DP103 GEMIN3","Disease.comment":"Spinal muscular atrophy (SMA)","Subunits.comment":"None","Complex.comment":"The survival of motor neurons (SMN) protein is the product of the gene mutated or deleted in the neurodegenerative disease,  spinal muscular atrophy.  SMN is part of a large macromolecular complex that also contains Gemin2, Gemin3, Gemin4, Gemin5, and Gemin6.  The SMN complex functions in the assembly of spliceosomal small nuclear ribonucleoproteins and probably other ribonucleoprotein particles.  The SMN complex is found both in the cytoplasm and in the nucleus where it is concentrated in gems, nuclear bodies similar in size and number to  Cajal bodies (coiled bodies (CBs) and often associated with them.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1760,"ComplexName":"TOP1-PSF-P54 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P11387;P23246;Q15233","subunits.Entrez.IDs.":"7150;6421;4841","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0008380;GO:0005634","GO.description":"RNA splicing;nucleus","FunCat.ID":"11.04.03.01;70.10","FunCat.description":"splicing;nucleus","PubMed.ID":9756848,"subunits.Protein.name.":"DNA topoisomerase 1;Splicing factor, proline- and glutamine-rich ;Non-POU domain-containing octamer-binding protein","subunits.Gene.name.":"TOP1;SFPQ;NONO","subunits.Gene.name.syn.":"None;PSF;NRB54","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1767,"ComplexName":"CPSF6-ITCH-NUDT21-POLR2A-UBAP2L complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43809;P24928;Q14157;Q16630;Q96J02","subunits.Entrez.IDs.":"11051;5430;9898;11052;83737","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006351;GO:0030036;GO:0051276","GO.description":"transcription, DNA-templated;actin cytoskeleton organization;chromosome organization","FunCat.ID":"11;42.04.03;42.10.03","FunCat.description":"TRANSCRIPTION;actin cytoskeleton;organization of chromosome structure","PubMed.ID":16055720,"subunits.Protein.name.":"Cleavage and polyadenylation specificity factor subunit 5 ;DNA-directed RNA polymerase II subunit RPB1;Ubiquitin-associated protein 2-like;Cleavage and polyadenylation specificity factor subunit 6 ;E3 ubiquitin-protein ligase Itchy homolog","subunits.Gene.name.":"NUDT21;POLR2A;UBAP2L;CPSF6;ITCH","subunits.Gene.name.syn.":"CFIM25 CPSF25 CPSF5;POLR2;KIAA0144, NICE4;CFIM68;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1768,"ComplexName":"CPSF6-EWSR1-ITCH-NUDT21-POLR2A-UBAP2L complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43809;P24928;Q01844;Q14157;Q16630;Q96J02","subunits.Entrez.IDs.":"11051;5430;2130;9898;11052;83737","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006351;GO:0030036;GO:0051276","GO.description":"transcription, DNA-templated;actin cytoskeleton organization;chromosome organization","FunCat.ID":"11;42.04.03;42.10.03","FunCat.description":"TRANSCRIPTION;actin cytoskeleton;organization of chromosome structure","PubMed.ID":16055720,"subunits.Protein.name.":"Cleavage and polyadenylation specificity factor subunit 5 ;DNA-directed RNA polymerase II subunit RPB1;RNA-binding protein EWS ;Ubiquitin-associated protein 2-like;Cleavage and polyadenylation specificity factor subunit 6 ;E3 ubiquitin-protein ligase Itchy homolog","subunits.Gene.name.":"NUDT21;POLR2A;EWSR1;UBAP2L;CPSF6;ITCH","subunits.Gene.name.syn.":"CFIM25 CPSF25 CPSF5;POLR2;EWS;KIAA0144, NICE4;CFIM68;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1769,"ComplexName":"CPSF6-ITCH-NUDT21-POLR2A complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43809;P24928;Q16630;Q96J02","subunits.Entrez.IDs.":"11051;5430;11052;83737","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006351;GO:0030036;GO:0051276","GO.description":"transcription, DNA-templated;actin cytoskeleton organization;chromosome organization","FunCat.ID":"11;42.04.03;42.10.03","FunCat.description":"TRANSCRIPTION;actin cytoskeleton;organization of chromosome structure","PubMed.ID":16055720,"subunits.Protein.name.":"Cleavage and polyadenylation specificity factor subunit 5 ;DNA-directed RNA polymerase II subunit RPB1;Cleavage and polyadenylation specificity factor subunit 6 ;E3 ubiquitin-protein ligase Itchy homolog","subunits.Gene.name.":"NUDT21;POLR2A;CPSF6;ITCH","subunits.Gene.name.syn.":"CFIM25 CPSF25 CPSF5;POLR2;CFIM68;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1772,"ComplexName":"MICB-KLRK1-HCST complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P26718;Q29980;Q9UBK5","subunits.Entrez.IDs.":"22914;4277;10870","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006955","GO.description":"immune response","FunCat.ID":"36.25.16","FunCat.description":"immune response","PubMed.ID":11239445,"subunits.Protein.name.":"NKG2-D type II integral membrane protein ;MHC class I polypeptide-related sequence B ;Hematopoietic cell signal transducer","subunits.Gene.name.":"KLRK1;MICB;HCST","subunits.Gene.name.syn.":"D12S2489E NKG2D;PERB11.2;DAP10 KAP10 PIK3AP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The ULBPs and the MICs share the property of binding to the NKG2D/DAP10 receptor and provide a positive signal for NK cell activation and cytotoxicity that can override the negative signal mediated by MHC class I/KIR engagement.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1773,"ComplexName":"ULBP3-KLRK1-HCST complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P26718;Q9BZM4;Q9UBK5","subunits.Entrez.IDs.":"22914;79465;10870","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006955","GO.description":"immune response","FunCat.ID":"36.25.16","FunCat.description":"immune response","PubMed.ID":11239445,"subunits.Protein.name.":"NKG2-D type II integral membrane protein ;NKG2D ligand 3 ;Hematopoietic cell signal transducer","subunits.Gene.name.":"KLRK1;ULBP3;HCST","subunits.Gene.name.syn.":"D12S2489E NKG2D;N2DL3 RAET1N;DAP10 KAP10 PIK3AP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The ULBPs and the MICs share the property of binding to the NKG2D/DAP10 receptor and provide a positive signal for NK cell activation and cytotoxicity that can override the negative signal mediated by MHC class I/KIR engagement.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1774,"ComplexName":"MICA-KLRK1-HCST complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P26718;Q29983;Q9UBK5","subunits.Entrez.IDs.":"22914;100507436;10870","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006955","GO.description":"immune response","FunCat.ID":"36.25.16","FunCat.description":"immune response","PubMed.ID":11239445,"subunits.Protein.name.":"NKG2-D type II integral membrane protein ;MHC class I polypeptide-related sequence A ;Hematopoietic cell signal transducer","subunits.Gene.name.":"KLRK1;MICA;HCST","subunits.Gene.name.syn.":"D12S2489E NKG2D;PERB11.1;DAP10 KAP10 PIK3AP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1775,"ComplexName":"ULBP2-KLRK1-HCST complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P26718;Q9BZM5;Q9UBK5","subunits.Entrez.IDs.":"22914;80328;10870","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006955","GO.description":"immune response","FunCat.ID":"36.25.16","FunCat.description":"immune response","PubMed.ID":11239445,"subunits.Protein.name.":"NKG2-D type II integral membrane protein ;NKG2D ligand 2 ;Hematopoietic cell signal transducer","subunits.Gene.name.":"KLRK1;ULBP2;HCST","subunits.Gene.name.syn.":"D12S2489E NKG2D;N2DL2 RAET1H;DAP10 KAP10 PIK3AP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The ULBPs and the MICs share the property of binding to the NKG2D/DAP10 receptor and provide a positive signal for NK cell activation and cytotoxicity that can override the negative signal mediated by MHC class I/KIR engagement.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1777,"ComplexName":"TGF-beta-receptor-SMAD7-SMURF2 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"O15105;P36897;P37173;Q9HAU4","subunits.Entrez.IDs.":"4092;7046;7048;64750","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0007179;GO:0005737","GO.description":"transforming growth factor beta receptor signaling pathway;cytoplasm","FunCat.ID":"30.05.01.18.01;70.03","FunCat.description":"TGF-beta-receptor signalling pathway;cytoplasm","PubMed.ID":11163210,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 7 ;TGF-beta receptor type-1;TGF-beta receptor type-2;E3 ubiquitin-protein ligase SMURF2","subunits.Gene.name.":"SMAD7;TGFBR1;TGFBR2;SMURF2","subunits.Gene.name.syn.":"MADH7 MADH8;ALK5 SKR4;None;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SMAD7 mediates the interaction of SMURF2 with TGF-beta-receptor complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1778,"ComplexName":"TGF-beta-receptor-Strap complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"Q62312;Q64729;Q9Z1Z2","subunits.Entrez.IDs.":"21813;21812;20901","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0007179;GO:0005737","GO.description":"transforming growth factor beta receptor signaling pathway;cytoplasm","FunCat.ID":"30.05.01.18.01;70.03","FunCat.description":"TGF-beta-receptor signalling pathway;cytoplasm","PubMed.ID":9856985,"subunits.Protein.name.":"TGF-beta receptor type-2 ;TGF-beta receptor type-1 ;Serine-threonine kinase receptor-associated protein","subunits.Gene.name.":"Tgfbr2;Tgfbr1;Strap","subunits.Gene.name.syn.":";;Unrip","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1779,"ComplexName":"TGF-beta-receptor-PAR6 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P36897;P37173;Q9NPB6","subunits.Entrez.IDs.":"7046;7048;50855","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation; MI:0729- luminescence based mammalian interactome mapping","GO.ID":"GO:0007179;GO:0007043;GO:0030054","GO.description":"transforming growth factor beta receptor signaling pathway;cell-cell junction assembly;cell junction","FunCat.ID":"30.05.01.18.01;42.06.04;70.06","FunCat.description":"TGF-beta-receptor signalling pathway;intercellular junction (gap junction/adherens junction);cell junction","PubMed.ID":15761148,"subunits.Protein.name.":"TGF-beta receptor type-1;TGF-beta receptor type-2;Partitioning defective 6 homolog alpha","subunits.Gene.name.":"TGFBR1;TGFBR2;PARD6A","subunits.Gene.name.syn.":"ALK5 SKR4;None;PAR6A, PAR6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"PAR6 interacts directly with TGFBR1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1782,"ComplexName":"TGF-beta receptor","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q62312;Q64729","subunits.Entrez.IDs.":"21813;21812","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0005515;GO:0007179;GO:0005886","GO.description":"protein binding;transforming growth factor beta receptor signaling pathway;plasma membrane","FunCat.ID":"16.01;30.05.01.18.01;70.02","FunCat.description":"protein binding;TGF-beta-receptor signalling pathway;eukaryotic plasma membrane / membrane attached","PubMed.ID":14612425,"subunits.Protein.name.":"TGF-beta receptor type-2 ;TGF-beta receptor type-1","subunits.Gene.name.":"Tgfbr2;Tgfbr1","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Tgfbr1 and Tgfbr2 exist as homodimers on the cell surface and form a heterotetramer upon TGF-beta binding (PMID:7521335).","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1783,"ComplexName":"TGF-beta receptor I-SMAD7-SMURF1 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"O15105;P36897;Q9HCE7","subunits.Entrez.IDs.":"4092;7046;57154","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511;GO:0007179;GO:0005737","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;transforming growth factor beta receptor signaling pathway;cytoplasm","FunCat.ID":"14.07.05;14.13.01.01;30.05.01.18.01;70.03","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway);TGF-beta-receptor signalling pathway;cytoplasm","PubMed.ID":11278251,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 7 ;TGF-beta receptor type-1;E3 ubiquitin-protein ligase SMURF1","subunits.Gene.name.":"SMAD7;TGFBR1;SMURF1","subunits.Gene.name.syn.":"MADH7 MADH8;ALK5 SKR4;KIAA1625","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SMAD7 associates with SMURF1 in the nucleus and is exported to the cytoplasm. Thus SMAD7 recruits SMURF1 to TGF-betaRI, resulting in the degradation of Tgf-betaRI.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1784,"ComplexName":"RNF11-SMURF2-STAMBP complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95630;Q9HAU4;Q9Y3C5","subunits.Entrez.IDs.":"10617;64750;26994","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0043161;GO:0006511","GO.description":"proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process","FunCat.ID":"14.13.01.01","FunCat.description":"proteasomal degradation (ubiquitin/proteasomal pathway)","PubMed.ID":14755250,"subunits.Protein.name.":"STAM-binding protein ;E3 ubiquitin-protein ligase SMURF2 ;RING finger protein 11","subunits.Gene.name.":"STAMBP;SMURF2;RNF11","subunits.Gene.name.syn.":"AMSH;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1787,"ComplexName":"Nogo-potassium channel complex","Organism":"Human","Synonyms":"None","Cell.line":"central nervous system","subunits.UniProt.IDs.":"P16389;P78357;Q09470;Q9NQC3","subunits.Entrez.IDs.":"3737;8506;3736;57142","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0047-far western blotting","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0022008;GO:0048699;GO:0007417","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;neurogenesis;generation of neurons;central nervous system development","FunCat.ID":"20.01.01.01;20.03.01.01;41.05.13;47.03.01.01","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;neurogenesis;central nervous system","PubMed.ID":14592966,"subunits.Protein.name.":"Potassium voltage-gated channel subfamily A member 2;Contactin-associated protein 1;Potassium voltage-gated channel subfamily A member 1;Reticulon-4","subunits.Gene.name.":"KCNA2;CNTNAP1;KCNA1;RTN4","subunits.Gene.name.syn.":"None;CASPR NRXN4;None;KIAA0886 NOGO","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Nogo-A is mainly localized at thegaps between Na+ and K+ channels along axons and itsimmunoreactivity is clearly located at sites where glialloops make contact with the axonal membrane surface inadult CNS. Nogo-A is a paranodal glial component.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1791,"ComplexName":"Nbr1-Sqstm1-Trim55 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O08623;Q501R9;Q5PQN5","subunits.Entrez.IDs.":"113894;303554;365751","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0007517","GO.description":"muscle organ development","FunCat.ID":"45.03.12","FunCat.description":"muscle","PubMed.ID":15802564,"subunits.Protein.name.":"Sequestosome-1 ;Next to BRCA1 gene 1 protein ;Tripartite motif-containing protein 55","subunits.Gene.name.":"Sqstm1;Nbr1;Trim55","subunits.Gene.name.syn.":"Zip;;Murf2 Rnf29","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"br1, p62, and MuRF2 proteins interacted in successive pairs in vitro and could be precipitated in a large complex from muscle tissue extracts, demonstrating their association in vivo.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":1792,"ComplexName":"Lingo1-Rtn4r-Tnfrsf19 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q99PI8;Q9D1T0;Q9JLL3","subunits.Entrez.IDs.":"65079;235402;29820","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007399","GO.description":"nervous system development","FunCat.ID":"47.03.01","FunCat.description":"nervous system","PubMed.ID":15694321,"subunits.Protein.name.":"Reticulon-4 receptor ;Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1 ;Tumor necrosis factor receptor superfamily member 19","subunits.Gene.name.":"Rtn4r;Lingo1;Tnfrsf19","subunits.Gene.name.syn.":"Nogor;Lern1 Lrrn6a;Taj Troy","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TROY (also known as TAJ), a TNF receptor family member selectively expressed in the adult nervous system, can form a functional receptor complex with NgR and LINGO-1 to mediate cellular responses to myelin inhibitors.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1793,"ComplexName":"LINGO-1-Nogo-66-p75 signaling complex","Organism":"Human","Synonyms":"None","Cell.line":"COS-7 cells, CG (ciliary ganglion) neurons","subunits.UniProt.IDs.":"P08138;Q96FE5;Q9BZR6","subunits.Entrez.IDs.":"4804;84894;65078","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0411-enzyme linked immunosorbent assay","GO.ID":"GO:0051098;GO:0005515;GO:0022008;GO:0048699;GO:0031641","GO.description":"regulation of binding;protein binding;neurogenesis;generation of neurons;regulation of myelination","FunCat.ID":"18.01.07;16.01;41.05.13","FunCat.description":"regulation by binding / dissociation;protein binding;neurogenesis","PubMed.ID":14966521,"subunits.Protein.name.":"Tumor necrosis factor receptor superfamily member 16 ;Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1 ;Reticulon-4 receptor","subunits.Gene.name.":"NGFR;LINGO1;RTN4R","subunits.Gene.name.syn.":"TNFRSF16;LERN1 LRRN6A;NOGOR","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Triply transfected cells responded to OMgp by activating RhoA, but no activation occurred when binary pairs of NgR1/p75, LINGO-1/p75 or NgR1/LINGO-1 were tested.The binding of LINGO-1 to NgR1, p75 or to both together during CNS development or in response to injury, may modulate RhoA activation status in neurons, and thus control axon growth and extension.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1794,"ComplexName":"SORT1-NGFR complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P08138;Q99523","subunits.Entrez.IDs.":"4804;6272","Protein.complex.purification.method":"MI:0030- cross-linking studies; MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515;GO:0005737","GO.description":"protein binding;cytoplasm","FunCat.ID":"16.01;70.03","FunCat.description":"protein binding;cytoplasm","PubMed.ID":14985763,"subunits.Protein.name.":"Tumor necrosis factor receptor superfamily member 16 ;Sortilin","subunits.Gene.name.":"NGFR;SORT1","subunits.Gene.name.syn.":"TNFRSF16;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1795,"ComplexName":"SORT1-NGFR-NGFB complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P01138;P08138;Q99523","subunits.Entrez.IDs.":"4803;4804;6272","Protein.complex.purification.method":"MI:0030- cross-linking studies","GO.ID":"GO:0006915","GO.description":"apoptotic process","FunCat.ID":"40.10.02","FunCat.description":"apoptosis (type I programmed cell death)","PubMed.ID":14985763,"subunits.Protein.name.":"Beta-nerve growth factor ;Tumor necrosis factor receptor superfamily member 16 ;Sortilin","subunits.Gene.name.":"NGF;NGFR;SORT1","subunits.Gene.name.syn.":"NGFB;TNFRSF16;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1804,"ComplexName":"Smurf1-Par6 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q9CUN6;Q9Z101","subunits.Entrez.IDs.":"75788;56513","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0007043;GO:0030855;GO:0002009;GO:0005737","GO.description":"protein ubiquitination;protein deubiquitination;cell-cell junction assembly;epithelial cell differentiation;morphogenesis of an epithelium;cytoplasm","FunCat.ID":"14.07.05;42.06.04;45.03.09;70.03","FunCat.description":"modification by ubiquitination, deubiquitination;intercellular junction (gap junction/adherens junction);epithelium;cytoplasm","PubMed.ID":15761148,"subunits.Protein.name.":"E3 ubiquitin-protein ligase SMURF1 ;Partitioning defective 6 homolog alpha","subunits.Gene.name.":"Smurf1;Pard6a","subunits.Gene.name.syn.":";Par6a","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The amount of SMURF1-PAR6 complex increases after treatment of the cells with TGF-beta.  This complex is involved in epithelial-to-mesenchymal transition (EMT) process.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1810,"ComplexName":"ITGA4-PXN-GIT1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P13612;P49023;Q9Y2X7","subunits.Entrez.IDs.":"3676;5829;28964","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0050789;GO:0016477","GO.description":"regulation of biological process;cell migration","FunCat.ID":"18;34.05.01","FunCat.description":"REGULATION OF METABOLISM AND PROTEIN FUNCTION;cell migration","PubMed.ID":15793570,"subunits.Protein.name.":"Integrin alpha-4 ;Paxillin;ARF GTPase-activating protein GIT1","subunits.Gene.name.":"ITGA4;PXN;GIT1","subunits.Gene.name.syn.":"CD49D;;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1812,"ComplexName":"AXIN-MEKK4-CCD1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15169;Q155Q3;Q9Y6R4","subunits.Entrez.IDs.":"8312;85458;4216","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0007254","GO.description":"JNK cascade","FunCat.ID":"30.01.05.01.02","FunCat.description":"JNK cascade","PubMed.ID":15262978,"subunits.Protein.name.":"Axin-1 ;Dixin ;Mitogen-activated protein kinase kinase kinase 4","subunits.Gene.name.":"AXIN1;DIXDC1;MAP3K4","subunits.Gene.name.syn.":"AXIN;CCD1 KIAA1735;KIAA0213 MAPKKK4 MEKK4 MTK1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors analyzed that Ccd1 uses its coiled-coil domain to interact with MEKK4 and the DIX domain to interact with Axin, forming a ternary complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1813,"ComplexName":"MAD1L1 homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q9Y6D9","subunits.Entrez.IDs.":"8379","Protein.complex.purification.method":"MI:0018- two hybrid","GO.ID":"GO:0000075;GO:0005813","GO.description":"cell cycle checkpoint;centrosome","FunCat.ID":"10.03.01.03;70.05","FunCat.description":"cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);centrosome","PubMed.ID":9546394,"subunits.Protein.name.":"Mitotic spindle assembly checkpoint protein MAD1","subunits.Gene.name.":"MAD1L1","subunits.Gene.name.syn.":"MAD1 TXBP181","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":1814,"ComplexName":"MAD1L1-MAD2L1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q13257;Q9Y6D9","subunits.Entrez.IDs.":"4085;8379","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0000075","GO.description":"cell cycle checkpoint","FunCat.ID":"10.03.01.03","FunCat.description":"cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle)","PubMed.ID":15694304,"subunits.Protein.name.":"Mitotic spindle assembly checkpoint protein MAD2A ;Mitotic spindle assembly checkpoint protein MAD1","subunits.Gene.name.":"MAD2L1;MAD1L1","subunits.Gene.name.syn.":"MAD2;MAD1 TXBP181","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The closed Mad2 bound to Mad1 represents a template for the conversion of open Mad2 into closed Mad2 bound to Cdc20.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1816,"ComplexName":"JUN-TCF4-CTNNB1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P05412;P15884;P35222","subunits.Entrez.IDs.":"3725;6925;1499","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0016055;GO:0023052","GO.description":"Wnt signaling pathway;signaling","FunCat.ID":"30.05.02.20;30.01","FunCat.description":"Wnt signalling pathway;cellular signalling","PubMed.ID":16007074,"subunits.Protein.name.":"Transcription factor AP-1 ;Transcription factor 4 ;Catenin beta-1","subunits.Gene.name.":"JUN;TCF4;CTNNB1","subunits.Gene.name.syn.":";BHLHB19 ITF2 SEF2;CTNNB","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1826,"ComplexName":"SMAD3-HEF1-APC10-CDH1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12830;P84022;Q14511;Q9UM13","subunits.Entrez.IDs.":"999;4088;4739;10393","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0043161;GO:0006511;GO:0007179;GO:0005737","GO.description":"proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;transforming growth factor beta receptor signaling pathway;cytoplasm","FunCat.ID":"14.13.01.01;30.05.01.18.01;70.03","FunCat.description":"proteasomal degradation (ubiquitin/proteasomal pathway);TGF-beta-receptor signalling pathway;cytoplasm","PubMed.ID":15144564,"subunits.Protein.name.":"Cadherin-1;Mothers against decapentaplegic homolog 3;Enhancer of filamentation 1 ;Anaphase-promoting complex subunit 10","subunits.Gene.name.":"CDH1;SMAD3;NEDD9;ANAPC10","subunits.Gene.name.syn.":"CDHE UVO;MADH3;CASL CASS2;APC10","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SMAD3 regulates the proteosomal degradation of its interacting proteins via recruiting the cell-cycle linked E3 ligase APC. SMAD3 interaction with APC10 is regulated by TGF-beta type I receptor activation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1827,"ComplexName":"PML-SMAD2/3-SARA complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95405;P29590;P84022;Q15796","subunits.Entrez.IDs.":"9372;5371;4088;4087","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0007179;GO:0005737","GO.description":"transforming growth factor beta receptor signaling pathway;cytoplasm","FunCat.ID":"30.05.01.18.01;70.03","FunCat.description":"TGF-beta-receptor signalling pathway;cytoplasm","PubMed.ID":15356634,"subunits.Protein.name.":"Zinc finger FYVE domain-containing protein 9 ;Protein PML ;Mothers against decapentaplegic homolog 3;Mothers against decapentaplegic homolog 2","subunits.Gene.name.":"ZFYVE9;PML;SMAD3;SMAD2","subunits.Gene.name.syn.":"MADHIP SARA SMADIP;MYL PP8675 RNF71 TRIM19;MADH3;MADH2, MADR2","Disease.comment":"Promyelocytic leukaemia","Subunits.comment":"None","Complex.comment":"PML is essential for the formation of a stable and functional SARA-SMAD2/3complex. PML may function as a bridging factor between SARA and SMAD2/3.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1828,"ComplexName":"TGF-beta receptor I-Axin-SMAD3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15169;P36897;P84022","subunits.Entrez.IDs.":"8312;7046;4088","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0007179;GO:0005737","GO.description":"transforming growth factor beta receptor signaling pathway;cytoplasm","FunCat.ID":"30.05.01.18.01;70.03","FunCat.description":"TGF-beta-receptor signalling pathway;cytoplasm","PubMed.ID":11438668,"subunits.Protein.name.":"Axin-1 ;TGF-beta receptor type-1;Mothers against decapentaplegic homolog 3","subunits.Gene.name.":"AXIN1;TGFBR1;SMAD3","subunits.Gene.name.syn.":"AXIN;ALK5 SKR4;MADH3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Phosphorylation of SMAD3 by TGF-betaRI is faciliated in the presence of Axin. In the absence of ligand stimulation, Axin was colocalized with Smad3 in the cytoplasm in vivo. Upon receptor activation, Smad3 was strongly phosphorylated by TGF-beta type I receptor (TGF-betaRI) in the presence of Axin, and dissociated from TGF-betaRI and Axin.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1829,"ComplexName":"SMAD3-VDR complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P48281;Q8BUN5","subunits.Entrez.IDs.":"22337;17127","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0023052;GO:0007179;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;signaling;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"11.02.03.04;30.01;30.05.01.18.01;70.10","FunCat.description":"transcriptional control;cellular signalling;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":10224044,"subunits.Protein.name.":"Vitamin D3 receptor ;Mothers against decapentaplegic homolog 3","subunits.Gene.name.":"Vdr;Smad3","subunits.Gene.name.syn.":"Nr1i1;Madh3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SMAD3 acts as coactivator of VDR and positively regulates vitamin D signaling pathway. SMAD7 inhibits the formation of the SMAD3-VDR complex.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1830,"ComplexName":"Smad3-Hdac-Runx2 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P84025;Q5RJZ2;Q99P99;Q9Z2J9","subunits.Entrez.IDs.":"25631;84580;363287;367218","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0003677;GO:0007179;GO:0051276;GO:0001649;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;DNA binding;transforming growth factor beta receptor signaling pathway;chromosome organization;osteoblast differentiation;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;16.03.01;30.05.01.18.01;42.10.03;43.03.17;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;DNA binding;TGF-beta-receptor signalling pathway;organization of chromosome structure;structural cell of tissue (fibroblast, osteoblast, etc.);nucleus","PubMed.ID":15990875,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 3 ;Hdac5 protein ;Histone deacetylase 4 ;Runt-related transcription factor 2","subunits.Gene.name.":"Smad3;Hdac5;Hdac4;Runx2","subunits.Gene.name.syn.":"Madh3;;;Cbfa1 Osf2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Activated SMAD3 recruits HDAC5 to Runx2 and stabilizes the HDAC/Runx2 complex.  TGF-beta inhibits osteoblast differentiation through inhibition of the function of Runx2 by Smad3.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":1831,"ComplexName":"PIAS3-SMAD3-P300 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P84022;Q09472;Q9Y6X2","subunits.Entrez.IDs.":"4088;2033;10401","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045893;GO:0006473;GO:0006476;GO:0003677;GO:0007179;GO:0051276;GO:0005634","GO.description":"DNA topological change;positive regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;DNA binding;transforming growth factor beta receptor signaling pathway;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.01;14.07.04;16.03.01;30.05.01.18.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription activation;modification by acetylation, deacetylation;DNA binding;TGF-beta-receptor signalling pathway;organization of chromosome structure;nucleus","PubMed.ID":14691252,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 3;Histone acetyltransferase p300;E3 SUMO-protein ligase PIAS3","subunits.Gene.name.":"SMAD3;EP300;PIAS3","subunits.Gene.name.syn.":"MADH3;P300;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TGF-beta treatment increases the complex formation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1834,"ComplexName":"ITGAE-ITGB7-CDH1 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P12830;P26010;P38570","subunits.Entrez.IDs.":"999;3695;3682","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006461","GO.description":"protein complex assembly","FunCat.ID":"14.1","FunCat.description":"assembly of protein complexes","PubMed.ID":10837471,"subunits.Protein.name.":"Cadherin-1;Integrin beta-7 ;Integrin alpha-E","subunits.Gene.name.":"CDH1;ITGB7;ITGAE","subunits.Gene.name.syn.":"CDHE UVO;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1839,"ComplexName":"SDCBP-CTNNB1-CTNNA1-CDH1 complex","Organism":"Dog","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00560;P12830;P35221;P35222","subunits.Entrez.IDs.":"6386;999;1495;1499","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007043","GO.description":"cell-cell junction assembly","FunCat.ID":"42.06.04","FunCat.description":"intercellular junction (gap junction/adherens junction)","PubMed.ID":11179419,"subunits.Protein.name.":"Syntenin-1 ;Cadherin-1;Catenin alpha-1 ;Catenin beta-1","subunits.Gene.name.":"SDCBP;CDH1;CTNNA1;CTNNB1","subunits.Gene.name.syn.":"MDA9 SYCL;CDHE UVO;;CTNNB","Disease.comment":"None","Subunits.comment":"Since  CDH1, CTNNA1, CTNNB1 and SDCBP from dog were not available in the UniProt database at the time of annotation, the orthologous proteins from human were used.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1843,"ComplexName":"EB1-APC-mDia2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q61166;Q61315;Q9Z207","subunits.Entrez.IDs.":"13589;11789;56419","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0016477;GO:0000226;GO:0015630","GO.description":"cell migration;microtubule cytoskeleton organization;microtubule cytoskeleton","FunCat.ID":"34.05.01;42.04.05;70.04.05","FunCat.description":"cell migration;microtubule cytoskeleton;microtubule cytoskeleton","PubMed.ID":15311282,"subunits.Protein.name.":"Microtubule-associated protein RP/EB family member 1 ;Adenomatous polyposis coli protein ;Protein diaphanous homolog 3","subunits.Gene.name.":"Mapre1;Apc;Diaph3","subunits.Gene.name.syn.":";;Diap3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors showed that EB1 and APC interacted with mDia directly, through domains that were distinct from those that interact with each other.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1844,"ComplexName":"APC-IQGAP1 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"P25054;P46940","subunits.Entrez.IDs.":"324;8826","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0016477;GO:0007010;GO:0005856","GO.description":"cell migration;cytoskeleton organization;cytoskeleton","FunCat.ID":"34.05.01;42.04;70.04","FunCat.description":"cell migration;cytoskeleton/structural proteins;cytoskeleton","PubMed.ID":15572129,"subunits.Protein.name.":"Adenomatous polyposis coli protein;Ras GTPase-activating-like protein IQGAP1","subunits.Gene.name.":"APC;IQGAP1","subunits.Gene.name.syn.":"DP2.5;KIAA0051","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors demonstrate that the amount of IQGAP1 is about 20 times more than that of APC, and that the armadillo repeats of APC are responsible for the interaction with IQGAP1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1845,"ComplexName":"APC-IQGAP1-CLIP-170 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"P25054;P30622;P46940","subunits.Entrez.IDs.":"324;6249;8826","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0016477;GO:0007010;GO:0005856","GO.description":"cell migration;cytoskeleton organization;cytoskeleton","FunCat.ID":"34.05.01;42.04;70.04","FunCat.description":"cell migration;cytoskeleton/structural proteins;cytoskeleton","PubMed.ID":15572129,"subunits.Protein.name.":"Adenomatous polyposis coli protein;CAP-Gly domain-containing linker protein 1 ;Ras GTPase-activating-like protein IQGAP1","subunits.Gene.name.":"APC;CLIP1;IQGAP1","subunits.Gene.name.syn.":"DP2.5;CYLN1 RSN;KIAA0051","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1847,"ComplexName":"Axin-GSK-3-beta-beta-catenin complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"O70239;P18266;Q9WU82","subunits.Entrez.IDs.":"79257;84027;84353","Protein.complex.purification.method":"MI:0096-pull down;MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0016055","GO.description":"Wnt signaling pathway","FunCat.ID":"30.05.02.20","FunCat.description":"Wnt signalling pathway","PubMed.ID":9482734,"subunits.Protein.name.":"Axin-1 ;Glycogen synthase kinase-3 beta ;Catenin beta-1","subunits.Gene.name.":"Axin1;Gsk3b;Ctnnb1","subunits.Gene.name.syn.":"Axin;;Catnb","Disease.comment":"Desmoid-type fibromatosis (PMID:23614534).","Subunits.comment":"None","Complex.comment":"The results show that GSK-3b, rAxin and b-catenin form a ternary complex in intact cells and that GSK-3b and b-catenin interact with separate sites on rAxin.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":1851,"ComplexName":"BUB1-BUB3 complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa S3 cells","subunits.UniProt.IDs.":"O43683;O43684","subunits.Entrez.IDs.":"699;9184","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006468;GO:0006470;GO:0046777","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation","FunCat.ID":"14.07.03","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation","PubMed.ID":15525512,"subunits.Protein.name.":"Mitotic checkpoint serine/threonine-protein kinase BUB1 ;Mitotic checkpoint protein BUB3","subunits.Gene.name.":"BUB1;BUB3","subunits.Gene.name.syn.":"BUB1L;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Bub1-Bub3 phosphorylated Cdc20. Bub1 alone also efficiently phosphorylated Cdc20, indicating that Bub3 is not required for this process.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1856,"ComplexName":"CDCA5-PDS5A-RAD21-SMC1A-PDS5B-SMC3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60216;Q14683;Q29RF7;Q96FF9;Q9NTI5;Q9UQE7","subunits.Entrez.IDs.":"5885;8243;23244;113130;23047;9126","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0000278","GO.description":"mitotic cell cycle","FunCat.ID":"10.03.01.01","FunCat.description":"mitotic cell cycle","PubMed.ID":15837422,"subunits.Protein.name.":"Double-strand-break repair protein rad21 homolog ;Structural maintenance of chromosomes protein 1A ;Sister chromatid cohesion protein PDS5 homolog A ;Sororin ;Sister chromatid cohesion protein PDS5 homolog B ;Structural maintenance of chromosomes protein 3","subunits.Gene.name.":"RAD21;SMC1A;PDS5A;CDCA5;PDS5B;SMC3","subunits.Gene.name.syn.":"HR21 KIAA0078 NXP1;DXS423E KIAA0178 SB1.8 SMC1 SMC1L1;KIAA0648 PDS5;;APRIN AS3 KIAA0979;BAM BMH CSPG6 SMC3L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1863,"ComplexName":"TSG101-VPS37B-VPS28 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q99816;Q9H9H4;Q9UK41","subunits.Entrez.IDs.":"7251;79720;51160","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031","GO.description":"intracellular protein transport;protein targeting;protein transport","FunCat.ID":"14.04;20.01.10","FunCat.description":"protein targeting, sorting and translocation;protein transport","PubMed.ID":15218037,"subunits.Protein.name.":"Tumor susceptibility gene 101 protein ;Vacuolar protein sorting-associated protein 37B ;Vacuolar protein sorting-associated protein 28 homolog","subunits.Gene.name.":"TSG101;VPS37B;VPS28","subunits.Gene.name.syn.":";;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1867,"ComplexName":"ERC2-RIMS1-UNC13B complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"Q62769;Q8K3M6;Q9JIR4","subunits.Entrez.IDs.":"64830;259269;84556","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007268","GO.description":"synaptic transmission","FunCat.ID":"34.03.01","FunCat.description":"synaptic transmission","PubMed.ID":12163476,"subunits.Protein.name.":"Protein unc-13 homolog B ;ERC protein 2 ;Regulating synaptic membrane exocytosis protein 1","subunits.Gene.name.":"Unc13b;Erc2;Rims1","subunits.Gene.name.syn.":"Unc13h2;Cast1 Cmbp;Rim1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":1873,"ComplexName":"SNARE complex (Snap25, Syt1, Unc13b, Vamp2, Stx1b2, Stx1a)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P21707;P32851;P60881;P61265;P63045;Q62769","subunits.Entrez.IDs.":"25716;116470;25012;24923;24803;64830","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0027- cosedimentation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":8999968,"subunits.Protein.name.":"Synaptotagmin-1 ;Syntaxin-1A;Synaptosomal-associated protein 25;Syntaxin-1B ;Vesicle-associated membrane protein 2;Protein unc-13 homolog B","subunits.Gene.name.":"Syt1;Stx1a;Snap25;Stx1b;Vamp2;Unc13b","subunits.Gene.name.syn.":";Sap;Snap;Stx1b2;Syb2;Unc13h2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":1874,"ComplexName":"SNARE complex (SNAP25, VAMP3, VAMP2, NAPB, STX13)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P60880;P63027;Q15836;Q86Y82;Q9H115","subunits.Entrez.IDs.":"6616;6844;9341;23673;63908","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":9817754,"subunits.Protein.name.":"Synaptosomal-associated protein 25 ;Vesicle-associated membrane protein 2 ;Vesicle-associated membrane protein 3;Syntaxin-12;Beta-soluble NSF attachment protein","subunits.Gene.name.":"SNAP25;VAMP2;VAMP3;STX12;NAPB","subunits.Gene.name.syn.":"SNAP;SYB2;SYB3;;SNAPB","Disease.comment":"None","Subunits.comment":"Entrez Gene says that stx12 is synonym to stx13.","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1875,"ComplexName":"STX12-SNAP25-HGS-VAMP2 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"G3V7P1;P60881;P63045;Q9JJ50","subunits.Entrez.IDs.":"65033;25012;24803;56084","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0007032","GO.description":"endosome organization","FunCat.ID":"42.22","FunCat.description":"endosome","PubMed.ID":12847087,"subunits.Protein.name.":"Syntaxin-12 ;Synaptosomal-associated protein 25;Vesicle-associated membrane protein 2;Hepatocyte growth factor-regulated tyrosine kinase substrate","subunits.Gene.name.":"Stx12;Snap25;Vamp2;Hgs","subunits.Gene.name.syn.":"Stx13;Snap;Syb2;Hrs Hrs2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":1876,"ComplexName":"SNARE complex (Stx4, Napa, Vamp3, Nsf, Vamp2)","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P54921;P63025;P63045;Q08850;Q9QUL6","subunits.Entrez.IDs.":"140673;29528;24803;81803;60355","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":8973549,"subunits.Protein.name.":"Alpha-soluble NSF attachment protein;Vesicle-associated membrane protein 3 ;Vesicle-associated membrane protein 2;Syntaxin-4;Vesicle-fusing ATPase","subunits.Gene.name.":"Napa;Vamp3;Vamp2;Stx4;Nsf","subunits.Gene.name.syn.":"Snap Snapa;Syb3;Syb2;Stx4a;Erg1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":1879,"ComplexName":"Nsf-Stx1a-NAPB complex","Organism":"Rat","Synonyms":"None","Cell.line":"liver","subunits.UniProt.IDs.":"P32851;P85969;Q9QUL6","subunits.Entrez.IDs.":"116470;499903;60355","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":1315316,"subunits.Protein.name.":"Syntaxin-1A;Beta-soluble NSF attachment protein;Vesicle-fusing ATPase","subunits.Gene.name.":"Stx1a;Napb;Nsf","subunits.Gene.name.syn.":"Sap;Snapb;Erg1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":1880,"ComplexName":"SNARE complex (Stx1a, Napa, Snap25, Vamp2, Nsf)","Organism":"Rat","Synonyms":"None","Cell.line":"adipose tissue","subunits.UniProt.IDs.":"P32851;P54921;P60881;P63045;Q9QUL6","subunits.Entrez.IDs.":"116470;140673;25012;24803;60355","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":9267032,"subunits.Protein.name.":"Syntaxin-1A;Alpha-soluble NSF attachment protein;Synaptosomal-associated protein 25;Vesicle-associated membrane protein 2;Vesicle-fusing ATPase","subunits.Gene.name.":"Stx1a;Napa;Snap25;Vamp2;Nsf","subunits.Gene.name.syn.":"Sap;Snap Snapa;Snap;Syb2;Erg1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":1883,"ComplexName":"Stx7-Vti1b-Vamp8-Stx8 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O70257;P58200;Q9WUF4;Q9Z2Q7","subunits.Entrez.IDs.":"60466;366673;83730;59074","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0006906","GO.description":"vesicle fusion","FunCat.ID":"20.09.07.27","FunCat.description":"vesicle fusion","PubMed.ID":11786915,"subunits.Protein.name.":"Syntaxin-7;Vesicle transport through interaction with t-SNAREs homolog 1B ;Vesicle-associated membrane protein 8 ;Syntaxin-8","subunits.Gene.name.":"Stx7;Vti1b;Vamp8;Stx8","subunits.Gene.name.syn.":";Vti1l1;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":1890,"ComplexName":"ELK1-SRF-ELK4 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P11831;P19419;P28324","subunits.Entrez.IDs.":"6722;2002;2005","Protein.complex.purification.method":"MI:0413- electrophoretic mobility shift assay","GO.ID":"GO:2001141;GO:0006355","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":7540136,"subunits.Protein.name.":"Serum response factor ;ETS domain-containing protein Elk-1;ETS domain-containing protein Elk-4","subunits.Gene.name.":"SRF;ELK1;ELK4","subunits.Gene.name.syn.":";;SAP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1893,"ComplexName":"mTOR-RICTOR complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"P42345;Q6R327;Q9BVC4","subunits.Entrez.IDs.":"2475;253260;64223","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0035556;GO:0000902;GO:0016049;GO:0030036","GO.description":"intracellular signal transduction;cell morphogenesis;cell growth;actin cytoskeleton organization","FunCat.ID":"30.01;40.01;42.04.03","FunCat.description":"cellular signalling;cell growth / morphogenesis;actin cytoskeleton","PubMed.ID":15268862,"subunits.Protein.name.":"Serine/threonine-protein kinase mTOR ;Rapamycin-insensitive companion of mTOR ;Target of rapamycin complex subunit LST8","subunits.Gene.name.":"MTOR;RICTOR;MLST8","subunits.Gene.name.syn.":"FRAP FRAP1 FRAP2 RAFT1 RAPT1;KIAA1999;GBL LST8","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors found that the rictor-mTOR complex modulates the phosphorylation of Protein Kinase C alpha (PKCalpha) and the actin cytoskeleton. The rictor-mTOR complex is insensitive to rapamycin.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1895,"ComplexName":"RICTOR-mTOR complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P42345;Q8N6M7;Q9BVC4","subunits.Entrez.IDs.":"2475;253260;64223","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006468;GO:0006470;GO:0046777","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation","FunCat.ID":"14.07.03","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation","PubMed.ID":15718470,"subunits.Protein.name.":"Serine/threonine-protein kinase mTOR ;RICTOR protein;Target of rapamycin complex subunit LST8","subunits.Gene.name.":"MTOR;RICTOR;MLST8","subunits.Gene.name.syn.":"FRAP FRAP1 FRAP2 RAFT1 RAPT1;;GBL LST8","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Rictor-mTOR may serve as a drug target in tumors that have lost the expression of PTEN.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1897,"ComplexName":"RAPTOR-mTOR complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P42345;Q8N122;Q9BVC4","subunits.Entrez.IDs.":"2475;57521;64223","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006468;GO:0006470;GO:0046777","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation","FunCat.ID":"14.07.03","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation","PubMed.ID":15718470,"subunits.Protein.name.":"Serine/threonine-protein kinase mTOR ;Regulatory-associated protein of mTOR ;Target of rapamycin complex subunit LST8","subunits.Gene.name.":"MTOR;RPTOR;MLST8","subunits.Gene.name.syn.":"FRAP FRAP1 FRAP2 RAFT1 RAPT1;KIAA1303 RAPTOR;GBL LST8","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1899,"ComplexName":"NTF4 homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P34130","subunits.Entrez.IDs.":"4909","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0030182","GO.description":"neuron differentiation","FunCat.ID":"43.03.13","FunCat.description":"neuron","PubMed.ID":10631974,"subunits.Protein.name.":"Neurotrophin-4","subunits.Gene.name.":"NTF4","subunits.Gene.name.syn.":"NTF5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The structures of the neurotrophin homodimers reveals common features that may be important in the binding between the neurotrophins and their receptors.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":1900,"ComplexName":"PSD-95-TrkB complex","Organism":"Rat","Synonyms":"None","Cell.line":"Hippocampal neurons","subunits.UniProt.IDs.":"P10686;P31016;P35439;Q5M824;Q63604","subunits.Entrez.IDs.":"25738;29495;24408;85385;25054","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0019933;GO:0007169;GO:0001508;GO:0019227;GO:0019228;GO:0030182;GO:0007417;GO:0007416","GO.description":"cAMP-mediated signaling;transmembrane receptor protein tyrosine kinase signaling pathway;action potential;neuronal action potential propagation;neuronal action potential;neuron differentiation;central nervous system development;synapse assembly","FunCat.ID":"30.01.09.07;30.05.01.12;34.03.03;43.03.13;47.03.01.01;41.05.13.01","FunCat.description":"cAMP/cGMP mediated signal transduction;transmembrane receptor protein tyrosine kinase signalling pathways;regulation, generation and propagation of action potential;neuron;central nervous system;synaptogenesis","PubMed.ID":15665879,"subunits.Protein.name.":"1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 ;Disks large homolog 4;Glutamate receptor ionotropic, NMDA 1 ;SHC-transforming protein 1 ;BDNF/NT-3 growth factors receptor","subunits.Gene.name.":"Plcg1;Dlg4;Grin1;Shc1;Ntrk2","subunits.Gene.name.syn.":";Dlgh4, Psd95;Nmdar1;;Trkb","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors show that cAMP modulates TrkB signaling in two ways: cAMP gates BDNF-induced TrkB phosphorylation and cAMP facilitates the distribution of TrkB into the PSD in the spines of hippocampal neurons. They propose that cAMP gating occurs at the TrkB receptor level, rather than at intracellular signaling molecules.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":1901,"ComplexName":"Drd1-Nmdar1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"striatal neurons","subunits.UniProt.IDs.":"P18901;P35439","subunits.Entrez.IDs.":"24316;24408","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation;MI:0096- pull down;MI:0012- bioluminescence resonance energy transfer","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0050896;GO:0005886;GO:0005794","GO.description":"intracellular protein transport;protein targeting;protein transport;response to stimulus;plasma membrane;Golgi apparatus","FunCat.ID":"14.04;20.01.10;36.25;70.02;70.08","FunCat.description":"protein targeting, sorting and translocation;protein transport;animal specific systemic sensing and response;eukaryotic plasma membrane / membrane attached;Golgi","PubMed.ID":12646556,"subunits.Protein.name.":"D;Glutamate receptor ionotropic, NMDA 1","subunits.Gene.name.":"Drd1;Grin1","subunits.Gene.name.syn.":"Drd1a;Nmdar1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors describe that this interaction is constitutive, occurs in the endoplasmic reticulum (ER), influences D1 receptor targeting to the cell membrane, and prevents agonist-induced D1 receptor internalization. The experiments suggest that D1 and NMDA receptors are assembled as oligomeric units in the ER and transported to the  cell surface as a preformed complex.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":1907,"ComplexName":"NMDA receptor complex (NR2B, NR1, PSD-95, SynGAP, CaMK-II)","Organism":"Rat","Synonyms":"None","Cell.line":"mature hippocampal neurons","subunits.UniProt.IDs.":"P11275;P31016;P35439;Q00960;Q9QUH6","subunits.Entrez.IDs.":"25400;29495;24408;24410;192117","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0005216;GO:0007264;GO:0007215;GO:0023052;GO:0050896;GO:0005886","GO.description":"intracellular protein transport;protein targeting;protein transport;ion channel activity;small GTPase mediated signal transduction;glutamate receptor signaling pathway;signaling;response to stimulus;plasma membrane","FunCat.ID":"14.04;20.01.10;20.03.01.01;30.01.05.05.01;30.05.02.24.05;30.01;36.25;70.02","FunCat.description":"protein targeting, sorting and translocation;protein transport;ion channels;small GTPase mediated signal transduction;glutamate signalling pathway;cellular signalling;animal specific systemic sensing and response;eukaryotic plasma membrane / membrane attached","PubMed.ID":15924861,"subunits.Protein.name.":"Calcium/calmodulin-dependent protein kinase type II subunit alpha ;Disks large homolog 4;Glutamate receptor ionotropic, NMDA 1 ;Glutamate receptor ionotropic, NMDA 2B ;Ras/Rap GTPase-activating protein SynGAP","subunits.Gene.name.":"Camk2a;Dlg4;Grin1;Grin2b;Syngap1","subunits.Gene.name.syn.":";Dlgh4, Psd95;Nmdar1;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors analyse the links between NMDAR subtypes, Ras-ERK signaling, and AMPAR trafficking. They find that NR2A and NR2B have antagonistic actions on Ras-ERK activation and AMPAR distribution in mature neurons. NR2A-NMDARs promote, whereas NR2B-NMDARs inhibit, the surface expression of GluR1 - primarily by regulating GluR1 surface insertion. Coimmunoprecipitation done with NR2B antibody after depletion of NR2A.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":1908,"ComplexName":"NMDA receptor complex (NR2A, NR2B, NR1, PSD-95, SynGAP, CaMK-II)","Organism":"Rat","Synonyms":"None","Cell.line":"mature hippocampal neurons","subunits.UniProt.IDs.":"P11275;P31016;P35439;Q00959;Q00960;Q9QUH6","subunits.Entrez.IDs.":"25400;29495;24408;24409;24410;192117","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0005216;GO:0007264;GO:0007215;GO:0023052;GO:0050896;GO:0005886","GO.description":"intracellular protein transport;protein targeting;protein transport;ion channel activity;small GTPase mediated signal transduction;glutamate receptor signaling pathway;signaling;response to stimulus;plasma membrane","FunCat.ID":"14.04;20.01.10;20.03.01.01;30.01.05.05.01;30.05.02.24.05;30.01;36.25;70.02","FunCat.description":"protein targeting, sorting and translocation;protein transport;ion channels;small GTPase mediated signal transduction;glutamate signalling pathway;cellular signalling;animal specific systemic sensing and response;eukaryotic plasma membrane / membrane attached","PubMed.ID":15924861,"subunits.Protein.name.":"Calcium/calmodulin-dependent protein kinase type II subunit alpha ;Disks large homolog 4;Glutamate receptor ionotropic, NMDA 1 ;Glutamate receptor ionotropic, NMDA 2A ;Glutamate receptor ionotropic, NMDA 2B ;Ras/Rap GTPase-activating protein SynGAP","subunits.Gene.name.":"Camk2a;Dlg4;Grin1;Grin2a;Grin2b;Syngap1","subunits.Gene.name.syn.":";Dlgh4, Psd95;Nmdar1;;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors analyse the links between NMDAR subtypes, Ras-ERK signaling, and AMPAR trafficking. They find that NR2A and NR2B have antagonistic actions on Ras-ERK activation and AMPAR distribution in mature neurons. NR2A-NMDARs promote, whereas NR2B-NMDARs inhibit, the surface expression of GluR1 - primarily by regulating GluR1 surface insertion.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":1909,"ComplexName":"APC-DLG4 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P25054;P78352","subunits.Entrez.IDs.":"324;1742","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016477;GO:0000902;GO:0016049","GO.description":"cell migration;cell morphogenesis;cell growth","FunCat.ID":"34.05.01;40.01","FunCat.description":"cell migration;cell growth / morphogenesis","PubMed.ID":9326658,"subunits.Protein.name.":"Adenomatous polyposis coli protein;Disks large homolog 4","subunits.Gene.name.":"APC;DLG4","subunits.Gene.name.syn.":"DP2.5;PSD95","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1913,"ComplexName":"GluR delta-2 complex, postsynaptic (GluR delta-2, Shank1, Shank2, mGluR1 alpha, Homer, PSD-95)","Organism":"Mouse","Synonyms":"None","Cell.line":"synaptosomal plasma membrane fractions","subunits.UniProt.IDs.":"P97772;Q61625;Q62108;Q80Z38;Q9WV48;Q9Z2Y3","subunits.Entrez.IDs.":"14816;14804;13385;210274;78957;26556","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0005216;GO:0007268;GO:0007416","GO.description":"ion channel activity;synaptic transmission;synapse assembly","FunCat.ID":"20.03.01.01;34.03.01;41.05.13.01","FunCat.description":"ion channels;synaptic transmission;synaptogenesis","PubMed.ID":15207857,"subunits.Protein.name.":"Metabotropic glutamate receptor 1 ;Glutamate receptor ionotropic, delta-2 ;Disks large homolog 4 ;SH3 and multiple ankyrin repeat domains protein 2 ;SH3 and multiple ankyrin repeat domains protein 1 ;Homer protein homolog 1","subunits.Gene.name.":"Grm1;Grid2;Dlg4;Shank2;Shank1;Homer1","subunits.Gene.name.syn.":"Gprc1a Mglur1;;Dlgh4 Psd95;Cortbp1 Kiaa1022;;Vesl1","Disease.comment":"None","Subunits.comment":"Since Shank1 from mouse was not available in the UniProt database at the time of annotation, the orthologous protein from rat was used.","Complex.comment":"The immunoprecipitation experiments with SPM (synaptosomal plasma membrane) fractions of cerebella showed that GluR delta-2 formed the postsynaptic protein complex with Homer and mGluR1 alpha in vivo. The authors suppose that it is likely that GluR delta-2-Shank complex interacted with mGluR1 alpha via Homer.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Rattus norvegicus (Rat);Mus musculus (Mouse)"}
{"ComplexID":1914,"ComplexName":"KIF1B-alpha-PSD-95-SAP-97-S-SCAM complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain, hippocampal neurons","subunits.UniProt.IDs.":"O88382;O88658;P31016;Q62696","subunits.Entrez.IDs.":"113970;117548;29495;25252","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0030705;GO:0050896","GO.description":"intracellular protein transport;protein targeting;protein transport;cytoskeleton-dependent intracellular transport;response to stimulus","FunCat.ID":"14.04;20.01.10;20.09.14;36.25","FunCat.description":"protein targeting, sorting and translocation;protein transport;cytoskeleton-dependent transport;animal specific systemic sensing and response","PubMed.ID":12097473,"subunits.Protein.name.":"Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2;Kinesin-like protein KIF1B;Disks large homolog 4;Disks large homolog 1","subunits.Gene.name.":"Magi2;Kif1b;Dlg4;Dlg1","subunits.Gene.name.syn.":"Acvrinp1, Aip1, Sscam;;Dlgh4, Psd95;Dlgh1","Disease.comment":"KIF1B is involved in Charcot-Marie-Tooth disease type 2A (CMT2A).","Subunits.comment":"None","Complex.comment":"The results demonstrated that KIF1B-alpha , unlike the dendrite-specific KIF17, is widely distributed in both dendrites and axons along with SAP97 and S-SCAM, and biochemically associates with SAP97 and S-SCAM. The authors suggest that the PSD-95 family proteins and S-SCAM have a novel function as KIF1B-alpha  receptors, linking KIF1B-alpha  to its specific cargos, and are involved in peripheral neuropathies.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":1923,"ComplexName":"CaMKII-densin180-NR2B-(alpha)actinin-2 complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P11275;P70587;Q00960;Q9JI91","subunits.Entrez.IDs.":"25400;None;24410;11472","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0019722","GO.description":"calcium-mediated signaling","FunCat.ID":"30.01.09.03","FunCat.description":"Ca2+ mediated signal transduction","PubMed.ID":16120608,"subunits.Protein.name.":"Calcium/calmodulin-dependent protein kinase type II subunit alpha ;Leucine-rich repeat-containing protein 7 ;Glutamate receptor ionotropic, NMDA 2B ;Alpha-actinin-2","subunits.Gene.name.":"Camk2a;Lrrc7;Grin2b;Actn2","subunits.Gene.name.syn.":";Lap1;;","Disease.comment":"None","Subunits.comment":"Since Actn2 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Mus musculus (Mouse)"}
{"ComplexID":1926,"ComplexName":"Foxh1-Nkx2-5 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O88621;P42582","subunits.Entrez.IDs.":"14106;18091","Protein.complex.purification.method":"MI:0402- chromatin immunoprecipitation assays","GO.ID":"GO:0048738;GO:0007507","GO.description":"cardiac muscle tissue development;heart development","FunCat.ID":"45.03.12.03","FunCat.description":"heart muscle","PubMed.ID":15363409,"subunits.Protein.name.":"Forkhead box protein H1 ;Homeobox protein Nkx-2.5","subunits.Gene.name.":"Foxh1;Nkx2-5","subunits.Gene.name.syn.":"Fast1 Fast2;Csx, Nkx-2.5, Nkx2e","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Foxh1 and Nkx2-5 functionally interact and are essential for development of the anterior heart field (AHF) and its derivatives, the right ventricle (RV) and outflow tract (OFT), in response to TGFbeta-like signals.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1927,"ComplexName":"PKD2-PACS1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q13563;Q6VY07","subunits.Entrez.IDs.":"5311;55690","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005216","GO.description":"ion channel activity","FunCat.ID":"20.03.01.01","FunCat.description":"ion channels","PubMed.ID":15692563,"subunits.Protein.name.":"Polycystin-2;Phosphofurin acidic cluster sorting protein 1","subunits.Gene.name.":"PKD2;PACS1","subunits.Gene.name.syn.":"TRPP2;KIAA1175","Disease.comment":"Mutations of PKD2, a member of the TRP family of cation channels, cause autosomal dominant polycystic kidney disease.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1932,"ComplexName":"NEK2-NEK11 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P51955;Q8NG66","subunits.Entrez.IDs.":"4751;79858","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007050","GO.description":"cell cycle arrest","FunCat.ID":"10.03.01.02","FunCat.description":"cell cycle arrest","PubMed.ID":15161910,"subunits.Protein.name.":"Serine/threonine-protein kinase Nek2 ;Serine/threonine-protein kinase Nek11","subunits.Gene.name.":"NEK2;NEK11","subunits.Gene.name.syn.":"NEK2A NLK1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1937,"ComplexName":"Olfr992-Rtp1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q8C8C1;Q8VGC6","subunits.Entrez.IDs.":"239766;258865","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030545","GO.description":"receptor regulator activity","FunCat.ID":"18.02.07","FunCat.description":"regulator of receptor activity","PubMed.ID":15550249,"subunits.Protein.name.":"Receptor-transporting protein 1;Olfactory receptor","subunits.Gene.name.":"Rtp1;Olfr992","subunits.Gene.name.syn.":"Gm604;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"These protein are associated with OR proteins and enhance the OR responses to odorants.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1938,"ComplexName":"Olfr992-Reep1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q8BGH4;Q8VGC6","subunits.Entrez.IDs.":"52250;258865","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030545","GO.description":"receptor regulator activity","FunCat.ID":"18.02.07","FunCat.description":"regulator of receptor activity","PubMed.ID":15550249,"subunits.Protein.name.":"Receptor expression-enhancing protein 1;Olfactory receptor","subunits.Gene.name.":"Reep1;Olfr992","subunits.Gene.name.syn.":"D6Ertd253e;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"These protein are associated with OR proteins and enhance the OR responses to odorants.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1941,"ComplexName":"Sirpa-Pik3cg complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P97797;Q9JHG7","subunits.Entrez.IDs.":"19261;30955","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0051098;GO:0005515","GO.description":"regulation of binding;protein binding","FunCat.ID":"18.01.07;16.01","FunCat.description":"regulation by binding / dissociation;protein binding","PubMed.ID":15797027,"subunits.Protein.name.":"Tyrosine-protein phosphatase non-receptor type substrate 1 ;Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform","subunits.Gene.name.":"Sirpa;Pik3cg","subunits.Gene.name.syn.":"Bit Myd1 Ptpns1 Shps1 Sirp;Pi3kg1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Binding of p84 to p110(gamma) substantially increases the ability of G(beta)(gamma) to stimulate phosphatidylinositol (3,4,5)-trisphosphate (PtdIns(3,4,5)P(3)) production both in vitro and in vivo.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":1944,"ComplexName":"IRAK1-IRAK2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43187;P51617","subunits.Entrez.IDs.":"3656;3654","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0045087","GO.description":"innate immune response","FunCat.ID":"36.25.16.01","FunCat.description":"innate immune response (invertebrates and vertebrates)","PubMed.ID":10383454,"subunits.Protein.name.":"Interleukin-1 receptor-associated kinase-like 2 ;Interleukin-1 receptor-associated kinase 1","subunits.Gene.name.":"IRAK2;IRAK1","subunits.Gene.name.syn.":";IRAK","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1945,"ComplexName":"IRAK1-IRAK3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P51617;Q9Y616","subunits.Entrez.IDs.":"3654;11213","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0045087","GO.description":"innate immune response","FunCat.ID":"36.25.16.01","FunCat.description":"innate immune response (invertebrates and vertebrates)","PubMed.ID":10383454,"subunits.Protein.name.":"Interleukin-1 receptor-associated kinase 1 ;Interleukin-1 receptor-associated kinase 3","subunits.Gene.name.":"IRAK1;IRAK3","subunits.Gene.name.syn.":"IRAK;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1949,"ComplexName":"MAML2-RBP-Jkappa-Notch1 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P31266;P46531;Q7TPU6","subunits.Entrez.IDs.":"19664;4851;270118","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0007219;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;Notch signaling pathway;nucleus","FunCat.ID":"11.02.03.04;16.03.01;30.05.02.14;70.10","FunCat.description":"transcriptional control;DNA binding;Notch-receptor signalling pathway;nucleus","PubMed.ID":12370315,"subunits.Protein.name.":"Recombining binding protein suppressor of hairless;Neurogenic locus notch homolog protein 1 ;Maml2 protein","subunits.Gene.name.":"Rbpj;NOTCH1;Maml2","subunits.Gene.name.syn.":"Igkjrb1 Igkrsbp Rbpsuh;TAN1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Homo sapiens (Human);Mus musculus (Mouse)"}
{"ComplexID":1957,"ComplexName":"DAP12 signaling homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43914","subunits.Entrez.IDs.":"7305","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007169","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway","FunCat.ID":"30.05.01.12","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways","PubMed.ID":15845448,"subunits.Protein.name.":"TYRO protein tyrosine kinase-binding protein","subunits.Gene.name.":"TYROBP","subunits.Gene.name.syn.":"DAP12 KARAP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":1970,"ComplexName":"BMP4-TWSG1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12644;Q9GZX9","subunits.Entrez.IDs.":"652;57045","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007178","GO.description":"transmembrane receptor protein serine/threonine kinase signaling pathway","FunCat.ID":"30.05.01.18","FunCat.description":"transmembrane receptor protein serine/threonine kinase signalling pathways","PubMed.ID":15775969,"subunits.Protein.name.":"Bone morphogenetic protein 4 ;Twisted gastrulation protein homolog 1","subunits.Gene.name.":"BMP4;TWSG1","subunits.Gene.name.syn.":"BMP2B DVR4;TSG","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1972,"ComplexName":"BMP4-BGN complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12644;P21810","subunits.Entrez.IDs.":"652;633","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":15775969,"subunits.Protein.name.":"Bone morphogenetic protein 4 ;Biglycan","subunits.Gene.name.":"BMP4;BGN","subunits.Gene.name.syn.":"BMP2B DVR4;SLRR1A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1975,"ComplexName":"GT198 homodimer complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q91ZY6","subunits.Entrez.IDs.":"140938","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0018- two hybrid","GO.ID":"GO:0009755;GO:0005634","GO.description":"hormone-mediated signaling pathway;nucleus","FunCat.ID":"30.01.09.08;70.10","FunCat.description":"hormone mediated signal transduction;nucleus","PubMed.ID":11739747,"subunits.Protein.name.":"Homologous-pairing protein 2 homolog","subunits.Gene.name.":"Psmc3ip","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"GT198 contains a leucine zipper required for its dimerization. As many nuclear receptors act as dimers on hormone response elements, the dimerization of GT198 might be important for the action on the DBD of nuclear receptors.","SWISSPROT.organism":"Rattus norvegicus (Rat)"}
{"ComplexID":1976,"ComplexName":"MTNR1A homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P48039","subunits.Entrez.IDs.":"4543","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":15266022,"subunits.Protein.name.":"Melatonin receptor type 1A","subunits.Gene.name.":"MTNR1A","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":1977,"ComplexName":"MTNR1B homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P49286","subunits.Entrez.IDs.":"4544","Protein.complex.purification.method":"MI:0012- bioluminescence resonance energy transfer;MI:0019- coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":15266022,"subunits.Protein.name.":"Melatonin receptor type 1B","subunits.Gene.name.":"MTNR1B","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":1978,"ComplexName":"MTNR1A-MTNR1B complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P48039;P49286","subunits.Entrez.IDs.":"4543;4544","Protein.complex.purification.method":"MI:0012- bioluminescence resonance energy transfer;MI:0019- coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":15266022,"subunits.Protein.name.":"Melatonin receptor type 1A ;Melatonin receptor type 1B","subunits.Gene.name.":"MTNR1A;MTNR1B","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This heterodimers contain two functional ligand binding sites that maintain their respective selectivity for MT(1) and MT(2) ligands. Occupation of either binding site is sufficient to induce a conformational change within the heterodimer. Taken together, these results show that the probability of GPCR heterodimer formation may be equal to or even higher than that of the corresponding homodimers and that specific properties of heterodimers can be revealed using a BRET-based ligand/receptor interaction assay.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1982,"ComplexName":"CACY homodimer  complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06703","subunits.Entrez.IDs.":"6277","Protein.complex.purification.method":"MI:0027- cosedimentation","GO.ID":"GO:0005509;GO:0008270","GO.description":"calcium ion binding;zinc ion binding","FunCat.ID":"16.17.01","FunCat.description":"calcium binding","PubMed.ID":9578461,"subunits.Protein.name.":"Protein S100-A6","subunits.Gene.name.":"S100A6","subunits.Gene.name.syn.":"CACY","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":1983,"ComplexName":"Retn homohexamer  complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q99P87","subunits.Entrez.IDs.":"57264","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0043609;GO:0043610;GO:0006109;GO:0042445","GO.description":"regulation of carbon utilization;regulation of carbohydrate utilization;regulation of carbohydrate metabolic process;hormone metabolic process","FunCat.ID":"01.05.25;01.08.02","FunCat.description":"regulation of C-compound and carbohydrate metabolism;metabolism of hormones","PubMed.ID":15155948,"subunits.Protein.name.":"Resistin","subunits.Gene.name.":"Retn","subunits.Gene.name.syn.":"Fizz3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse)"}
{"ComplexID":1984,"ComplexName":"PEX14 homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75381","subunits.Entrez.IDs.":"5195","Protein.complex.purification.method":"MI:0030- cross-linking studies; MI:0018- two hybrid","GO.ID":"GO:0006461;GO:0007031;GO:0005777","GO.description":"protein complex assembly;peroxisome organization;peroxisome","FunCat.ID":"14.10;42.19;70.19","FunCat.description":"assembly of protein complexes;peroxisome;peroxisome","PubMed.ID":12096124,"subunits.Protein.name.":"Peroxisomal membrane protein PEX14","subunits.Gene.name.":"PEX14","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":1985,"ComplexName":"AIRE homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43918","subunits.Entrez.IDs.":"326","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0018- two hybrid","GO.ID":"GO:0045893","GO.description":"positive regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.01","FunCat.description":"transcription activation","PubMed.ID":10748110,"subunits.Protein.name.":"Autoimmune regulator","subunits.Gene.name.":"AIRE","subunits.Gene.name.syn.":"APECED","Disease.comment":"Autoimmune polyendocrinopathy candidiasis ectodermal dystrophy is caused by mutations in the autoimmune regulator (AIRE) gene.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":1986,"ComplexName":"Endoglin homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P17813","subunits.Entrez.IDs.":"2022","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":15806144,"subunits.Protein.name.":"Endoglin","subunits.Gene.name.":"ENG","subunits.Gene.name.syn.":"END","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":1987,"ComplexName":"MYOM1 homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"muscle","subunits.UniProt.IDs.":"P52179","subunits.Entrez.IDs.":"8736","Protein.complex.purification.method":"MI:0018- two hybrid;MI:0019- coimmunoprecipitation;MI:0096- pull down","GO.ID":"GO:0007517","GO.description":"muscle organ development","FunCat.ID":"45.03.12","FunCat.description":"muscle","PubMed.ID":15571722,"subunits.Protein.name.":"Myomesin-1","subunits.Gene.name.":"MYOM1","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":1988,"ComplexName":"Bcl2 homodimer complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P10417","subunits.Entrez.IDs.":"12043","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0043067","GO.description":"regulation of programmed cell death","FunCat.ID":"40.10.02.04","FunCat.description":"regulation of apoptosis","PubMed.ID":7609638,"subunits.Protein.name.":"Apoptosis regulator Bcl-2","subunits.Gene.name.":"Bcl2","subunits.Gene.name.syn.":"Bcl-2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse)"}
{"ComplexID":1989,"ComplexName":"BANF1 homodimer protein","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75531","subunits.Entrez.IDs.":"8815","Protein.complex.purification.method":"MI:0077- nuclear magnetic resonance","GO.ID":"GO:0003677;GO:0009607","GO.description":"DNA binding;response to biotic stimulus","FunCat.ID":"16.03.01;34.11.10","FunCat.description":"DNA binding;response to biotic stimulus","PubMed.ID":9783751,"subunits.Protein.name.":"Barrier-to-autointegration factor","subunits.Gene.name.":"BANF1","subunits.Gene.name.syn.":"BAF, BCRG1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":1990,"ComplexName":"PGRMC1-SCAP complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00264;Q12770","subunits.Entrez.IDs.":"10857;22937","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0030- cross-linking studies","GO.ID":"GO:0042632;GO:0005783","GO.description":"cholesterol homeostasis;endoplasmic reticulum","FunCat.ID":"34.01.07;70.07","FunCat.description":"cholesterol homeostasis;endoplasmic reticulum","PubMed.ID":15782218,"subunits.Protein.name.":"Membrane-associated progesterone receptor component 1 ;Sterol regulatory element-binding protein cleavage-activating protein","subunits.Gene.name.":"PGRMC1;SCAP","subunits.Gene.name.syn.":"HPR6.6 PGRMC;KIAA0199","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":1991,"ComplexName":"PRMT2 homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P55345","subunits.Entrez.IDs.":"3275","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0030545","GO.description":"receptor regulator activity","FunCat.ID":"18.02.07","FunCat.description":"regulator of receptor activity","PubMed.ID":12039952,"subunits.Protein.name.":"Protein arginine N-methyltransferase 2","subunits.Gene.name.":"PRMT2","subunits.Gene.name.syn.":"HMT1 HRMT1L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":1992,"ComplexName":"LEPR homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P48357","subunits.Entrez.IDs.":"3953","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005125","GO.description":"cytokine activity","FunCat.ID":"40.02.03.01","FunCat.description":"cytokines (interleukines, colony stimulating factors, etc.)","PubMed.ID":9038364,"subunits.Protein.name.":"Leptin receptor","subunits.Gene.name.":"LEPR","subunits.Gene.name.syn.":"DB OBR","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":1993,"ComplexName":"SLC1A2 homotrimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P43004","subunits.Entrez.IDs.":"6506","Protein.complex.purification.method":"MI:0030- cross-linking studies","GO.ID":"GO:0015171;GO:0006865","GO.description":"amino acid transmembrane transporter activity;amino acid transport","FunCat.ID":"20.01.07","FunCat.description":"amino acid/amino acid derivatives transport","PubMed.ID":15483603,"subunits.Protein.name.":"Excitatory amino acid transporter 2","subunits.Gene.name.":"SLC1A2","subunits.Gene.name.syn.":"EAAT2 GLT1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":1995,"ComplexName":"Sgk3 homodimer complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q9ERE3","subunits.Entrez.IDs.":"None","Protein.complex.purification.method":"MI:0114- x-ray crystallography; MI:0030- cross-linking studies","GO.ID":"GO:0000902;GO:0016049","GO.description":"cell morphogenesis;cell growth","FunCat.ID":"40.01","FunCat.description":"cell growth / morphogenesis","PubMed.ID":15126499,"subunits.Protein.name.":"Serine/threonine-protein kinase Sgk3","subunits.Gene.name.":"Sgk3","subunits.Gene.name.syn.":"Cisk Sgkl","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse)"}
{"ComplexID":1997,"ComplexName":"Adiponectin homotrimer complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q60994","subunits.Entrez.IDs.":"11450","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":15558058,"subunits.Protein.name.":"Adiponectin","subunits.Gene.name.":"Adipoq","subunits.Gene.name.syn.":"Acdc Acrp30 Apm1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse)"}
{"ComplexID":1998,"ComplexName":"Adiponectin homohexamer complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q60994","subunits.Entrez.IDs.":"11450","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":15558058,"subunits.Protein.name.":"Adiponectin","subunits.Gene.name.":"Adipoq","subunits.Gene.name.syn.":"Acdc Acrp30 Apm1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse)"}
{"ComplexID":2000,"ComplexName":"BAX homo-oligomer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q07812","subunits.Entrez.IDs.":"581","Protein.complex.purification.method":"MI:0030- cross-linking studies; MI:0019- coimmunoprecipitation","GO.ID":"GO:0097190","GO.description":"apoptotic signaling pathway","FunCat.ID":"40.10.02.03.01","FunCat.description":"induction of apoptosis by extracellular signals","PubMed.ID":15735709,"subunits.Protein.name.":"Apoptosis regulator BAX","subunits.Gene.name.":"BAX","subunits.Gene.name.syn.":"BCL2L4","Disease.comment":"None","Subunits.comment":"Oligomer","Complex.comment":"Arsenic trioxide  As(2)O(3) treatment triggered Bax conformational change and subsequent translocation from cytosol to mitochondria to form various multimeric homo-oligomers in IM-9 cells.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":2001,"ComplexName":"NOD1 homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q9Y239","subunits.Entrez.IDs.":"10392","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0007249;GO:0006954","GO.description":"I-kappaB kinase/NF-kappaB signaling;inflammatory response","FunCat.ID":"30.01.05.01.04;36.25.16.07","FunCat.description":"NIK-I-kappaB/NF-kappaB cascade;inflammatory response","PubMed.ID":18186648,"subunits.Protein.name.":"Nucleotide-binding oligomerization domain-containing protein 1","subunits.Gene.name.":"NOD1","subunits.Gene.name.syn.":"CARD4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":2003,"ComplexName":"COX1 homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P23219","subunits.Entrez.IDs.":"5742","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0006643;GO:0005737","GO.description":"membrane lipid metabolic process;cytoplasm","FunCat.ID":"01.06.02;70.03","FunCat.description":"membrane lipid metabolism;cytoplasm","PubMed.ID":11318639,"subunits.Protein.name.":"Prostaglandin G/H synthase 1","subunits.Gene.name.":"PTGS1","subunits.Gene.name.syn.":"COX1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":2004,"ComplexName":"C1D homodimer protein","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q13901","subunits.Entrez.IDs.":"10438","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006461","GO.description":"protein complex assembly","FunCat.ID":"14.1","FunCat.description":"assembly of protein complexes","PubMed.ID":11801738,"subunits.Protein.name.":"Nuclear nucleic acid-binding protein C1D","subunits.Gene.name.":"C1D","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Only the dimeric but not the monomeric form of C1D can interact with TRAX protein. The finding that the SDS-resistant homodimers of C1D and TRAX interact only after gamma-irradiation may indicate that a post-translational modification is required for the interaction.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":2005,"ComplexName":"PTPRA homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P18433","subunits.Entrez.IDs.":"5786","Protein.complex.purification.method":"MI:0030- cross-linking studies;MI:0055- fluorescent resonance energy transfer","GO.ID":"GO:0007167","GO.description":"enzyme linked receptor protein signaling pathway","FunCat.ID":"30.05.01","FunCat.description":"receptor enzyme mediated signalling","PubMed.ID":11401727,"subunits.Protein.name.":"Receptor-type tyrosine-protein phosphatase alpha","subunits.Gene.name.":"PTPRA","subunits.Gene.name.syn.":"PTPA PTPRL2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"RPTPalpha dimerized constitutively in living cells, which may be mediated by the transmembrane domain, providing strong support for the model that dimerization is involved in regulation of RPTPs.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":2006,"ComplexName":"Ptpra homodimer complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P18052","subunits.Entrez.IDs.":"19262","Protein.complex.purification.method":"MI:0030- cross-linking studies","GO.ID":"GO:0004857;GO:0005737","GO.description":"enzyme inhibitor activity;cytoplasm","FunCat.ID":"18.02.01.02;70.03","FunCat.description":"enzyme inhibitor;cytoplasm","PubMed.ID":10913175,"subunits.Protein.name.":"Receptor-type tyrosine-protein phosphatase alpha","subunits.Gene.name.":"Ptpra","subunits.Gene.name.syn.":"Lrp Ptpa","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Based on surface cross-linking studies, the authors provide the first evidence that RPTPalpha homodimerizes efficiently on the cell surface via multiple domains, suggesting that dimerization-mediated negative regulation of RPTPalpha biological activity is likely to be physiologically relevant.","SWISSPROT.organism":"Mus musculus (Mouse)"}
{"ComplexID":2007,"ComplexName":"PRNP homo-oligomer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04156","subunits.Entrez.IDs.":"5621","Protein.complex.purification.method":"MI:0276-blue native page","GO.ID":"GO:0030182","GO.description":"neuron differentiation","FunCat.ID":"43.03.13","FunCat.description":"neuron","PubMed.ID":16148934,"subunits.Protein.name.":"Major prion protein","subunits.Gene.name.":"PRNP","subunits.Gene.name.syn.":"ALTPRP PRIP PRP","Disease.comment":"None","Subunits.comment":"Oligomer","Complex.comment":"The non-fibrillar particles, with masses equivalent to 14-28 PrP molecules, are the most efficient initiators of TSE disease.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":2008,"ComplexName":"Prnp homodimer complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04925","subunits.Entrez.IDs.":"19122","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030182","GO.description":"neuron differentiation","FunCat.ID":"43.03.13","FunCat.description":"neuron","PubMed.ID":7609638,"subunits.Protein.name.":"Major prion protein","subunits.Gene.name.":"Prnp","subunits.Gene.name.syn.":"Prn-p Prp","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse)"}
{"ComplexID":2009,"ComplexName":"Birc6 homodimer complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O88738","subunits.Entrez.IDs.":"12211","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":15200957,"subunits.Protein.name.":"Baculoviral IAP repeat-containing protein 6","subunits.Gene.name.":"Birc6","subunits.Gene.name.syn.":"Kiaa1289","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"It seems possible that only homodimerized full-length BRUCE possesses IAP activity and that the conformation of the 70 kDa dimer renders it inactive.","SWISSPROT.organism":"Mus musculus (Mouse)"}
{"ComplexID":2010,"ComplexName":"AXL homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P30530","subunits.Entrez.IDs.":"558","Protein.complex.purification.method":"MI:0018- two hybrid","GO.ID":"GO:0007169;GO:0005886","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway;plasma membrane","FunCat.ID":"30.05.01.12;70.02","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways;eukaryotic plasma membrane / membrane attached","PubMed.ID":12470648,"subunits.Protein.name.":"Tyrosine-protein kinase receptor UFO","subunits.Gene.name.":"AXL","subunits.Gene.name.syn.":"UFO","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":2013,"ComplexName":"STAT5B homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P51692","subunits.Entrez.IDs.":"6777","Protein.complex.purification.method":"MI:0413- electrophoretic mobility shift assay","GO.ID":"GO:0045893","GO.description":"positive regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.01","FunCat.description":"transcription activation","PubMed.ID":10594041,"subunits.Protein.name.":"Signal transducer and activator of transcription 5B","subunits.Gene.name.":"STAT5B","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":2014,"ComplexName":"Whrn homodimer complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q80VW5","subunits.Entrez.IDs.":"73750","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030154;GO:0043583","GO.description":"cell differentiation;ear development","FunCat.ID":"40.02;47.03.02.01","FunCat.description":"cell differentiation;ear","PubMed.ID":15590698,"subunits.Protein.name.":"Whirlin","subunits.Gene.name.":"Whrn","subunits.Gene.name.syn.":"Dfnb31 Kiaa1526","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse)"}
{"ComplexID":2016,"ComplexName":"IL12A homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P29459","subunits.Entrez.IDs.":"3592","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0071- molecular sieving","GO.ID":"GO:0030217","GO.description":"T cell differentiation","FunCat.ID":"43.03.07.02.01.02","FunCat.description":"T-cell","PubMed.ID":7527811,"subunits.Protein.name.":"Interleukin-12 subunit alpha","subunits.Gene.name.":"IL12A","subunits.Gene.name.syn.":"NKSF1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":2018,"ComplexName":"IL12A-IL12B complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P29459;P29460","subunits.Entrez.IDs.":"3592;3593","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":10899108,"subunits.Protein.name.":"Interleukin-12 subunit alpha ;Interleukin-12 subunit beta","subunits.Gene.name.":"IL12A;IL12B","subunits.Gene.name.syn.":"NKSF1;NKSF2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2019,"ComplexName":"IL12A-IL12B-IL12RB1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P29459;P29460;P42701","subunits.Entrez.IDs.":"3592;3593;3594","Protein.complex.purification.method":"MI:0027- cosedimentation; MI:0099-  scintillation proximity assay","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":9498755,"subunits.Protein.name.":"Interleukin-12 subunit alpha ;Interleukin-12 subunit beta ;Interleukin-12 receptor subunit beta-1","subunits.Gene.name.":"IL12A;IL12B;IL12RB1","subunits.Gene.name.syn.":"NKSF1;NKSF2;IL12R IL12RB","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2020,"ComplexName":"IL12B-IL12RB1-IL12RB2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P29460;P42701;Q99665","subunits.Entrez.IDs.":"3593;3594;3595","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030217","GO.description":"T cell differentiation","FunCat.ID":"43.03.07.02.01.02","FunCat.description":"T-cell","PubMed.ID":7527811,"subunits.Protein.name.":"Interleukin-12 subunit beta ;Interleukin-12 receptor subunit beta-1 ;Interleukin-12 receptor subunit beta-2","subunits.Gene.name.":"IL12B;IL12RB1;IL12RB2","subunits.Gene.name.syn.":"NKSF2;IL12R IL12RB;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"IL12B (p40) homodimer  was capable of competing with IL-12 heterodimer in binding to the IL12R on T cells but was unable to cause cellular proliferation. Furthermore, p40 homodimer inhibited IL-12-induced T cell proliferation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2021,"ComplexName":"IL12A-IL12B-IL12RB2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P29459;P29460;Q99665","subunits.Entrez.IDs.":"3592;3593;3595","Protein.complex.purification.method":"MI:0027- cosedimentation; MI:0099- scintillation proximity assay","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":9498755,"subunits.Protein.name.":"Interleukin-12 subunit alpha ;Interleukin-12 subunit beta ;Interleukin-12 receptor subunit beta-2","subunits.Gene.name.":"IL12A;IL12B;IL12RB2","subunits.Gene.name.syn.":"NKSF1;NKSF2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2022,"ComplexName":"Stat5a-Jak2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P42230;Q62120","subunits.Entrez.IDs.":"20850;16452","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030217","GO.description":"T cell differentiation","FunCat.ID":"43.03.07.02.01.02","FunCat.description":"T-cell","PubMed.ID":9834069,"subunits.Protein.name.":"Signal transducer and activator of transcription 5A ;Tyrosine-protein kinase JAK2","subunits.Gene.name.":"Stat5a;Jak2","subunits.Gene.name.syn.":"Mgf Mpf;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The phosphorylation of STAT5 associated with JAK2 was found to be induced in the absence of JAK3 activation.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2023,"ComplexName":"STAT5A homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P42229","subunits.Entrez.IDs.":"6776","Protein.complex.purification.method":"MI:0413- electrophoretic mobility shift assay","GO.ID":"GO:0045893","GO.description":"positive regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.01","FunCat.description":"transcription activation","PubMed.ID":10594041,"subunits.Protein.name.":"Signal transducer and activator of transcription 5A","subunits.Gene.name.":"STAT5A","subunits.Gene.name.syn.":"STAT5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":2024,"ComplexName":"Agtr1a-Jak2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P29754;Q62120","subunits.Entrez.IDs.":"11607;16452","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030234;GO:0050790","GO.description":"enzyme regulator activity;regulation of catalytic activity","FunCat.ID":"18.02.01","FunCat.description":"enzymatic activity regulation / enzyme regulator","PubMed.ID":15146194,"subunits.Protein.name.":"Type-1A angiotensin II receptor ;Tyrosine-protein kinase JAK2","subunits.Gene.name.":"Agtr1a;Jak2","subunits.Gene.name.syn.":"Agtr1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Mechanical stretch induces association of the AT1 receptor with Janus kinase 2, and translocation of G proteins into the cytosol.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2026,"ComplexName":"IL12RB1-IL12RB2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P42701;Q99665","subunits.Entrez.IDs.":"3594;3595","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0023052;GO:0005886","GO.description":"signaling;plasma membrane","FunCat.ID":"30.01;70.02","FunCat.description":"cellular signalling;eukaryotic plasma membrane / membrane attached","PubMed.ID":8943050,"subunits.Protein.name.":"Interleukin-12 receptor subunit beta-1 ;Interleukin-12 receptor subunit beta-2","subunits.Gene.name.":"IL12RB1;IL12RB2","subunits.Gene.name.syn.":"IL12R IL12RB;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2028,"ComplexName":"JAK2-IL12RB2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60674;Q99665","subunits.Entrez.IDs.":"3717;3595","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":9038232,"subunits.Protein.name.":"Tyrosine-protein kinase JAK2 ;Interleukin-12 receptor subunit beta-2","subunits.Gene.name.":"JAK2;IL12RB2","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2029,"ComplexName":"BNIP2-ARHGAP8 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P85298;Q12982","subunits.Entrez.IDs.":"23779;663","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0005096;GO:0043547","GO.description":"GTPase activator activity;positive regulation of GTPase activity","FunCat.ID":"18.02.01.01.01","FunCat.description":"GTPase activator (GAP)","PubMed.ID":12944407,"subunits.Protein.name.":"Rho GTPase-activating protein 8 ;BCL2/adenovirus E1B 19 kDa protein-interacting protein 2","subunits.Gene.name.":"ARHGAP8;BNIP2","subunits.Gene.name.syn.":";NIP2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2034,"ComplexName":"Apaf1 homo-oligomer complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O88879","subunits.Entrez.IDs.":"11783","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0043067","GO.description":"regulation of programmed cell death","FunCat.ID":"40.10.02.04","FunCat.description":"regulation of apoptosis","PubMed.ID":15907471,"subunits.Protein.name.":"Apoptotic protease-activating factor 1","subunits.Gene.name.":"Apaf1","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"Oligomer","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse)"}
{"ComplexID":2051,"ComplexName":"MALT1 oligomer complex","Organism":"Human","Synonyms":"None","Cell.line":"lymphocyte","subunits.UniProt.IDs.":"Q9UDY8","subunits.Entrez.IDs.":"10892","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0043085;GO:0008047","GO.description":"positive regulation of catalytic activity;enzyme activator activity","FunCat.ID":"18.02.01.01","FunCat.description":"enzyme activator","PubMed.ID":15125833,"subunits.Protein.name.":"Mucosa-associated lymphoid tissue lymphoma translocation protein 1","subunits.Gene.name.":"MALT1","subunits.Gene.name.syn.":"MLT","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TRAF6 ubiquitin ligase and TAK1 protein kinase mediate IKK activation by MALT1 and BCL10 in lymphocytes.Only oligomers of MALT1 and BCL10 can activate IKK in vitro.MALT1 oligomers bind to TRAF6, induce TRAF6 oligomerization, and activate the ligase activity of TRAF6 to polyubiquinate NEMO.These results reveal an oligomerization-ubiquination-phosphorylation cascade that culminates in NF-kappaB activation in T lymphocytes.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":2052,"ComplexName":"BCL10 oligomer complex","Organism":"Human","Synonyms":"None","Cell.line":"lymphocyte","subunits.UniProt.IDs.":"O95999","subunits.Entrez.IDs.":"8915","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0043085;GO:0008047","GO.description":"positive regulation of catalytic activity;enzyme activator activity","FunCat.ID":"18.02.01.01","FunCat.description":"enzyme activator","PubMed.ID":15125833,"subunits.Protein.name.":"B-cell lymphoma/leukemia 10","subunits.Gene.name.":"BCL10","subunits.Gene.name.syn.":"CIPER CLAP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TRAF6 ubiquitin ligase and TAK1 protein kinase mediate IKK activation by MALT1 and BCL10 in lymphocytes.Only oligomers of MALT1 and BCL10 can activate IKK in vitro.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":2053,"ComplexName":"BCL10-MALT1 complex","Organism":"Human","Synonyms":"None","Cell.line":"lymphocyte","subunits.UniProt.IDs.":"O95999;Q9UDY8","subunits.Entrez.IDs.":"8915;10892","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0043085;GO:0008047","GO.description":"positive regulation of catalytic activity;enzyme activator activity","FunCat.ID":"18.02.01.01","FunCat.description":"enzyme activator","PubMed.ID":15125833,"subunits.Protein.name.":"B-cell lymphoma/leukemia 10;Mucosa-associated lymphoid tissue lymphoma translocation protein 1","subunits.Gene.name.":"BCL10;MALT1","subunits.Gene.name.syn.":"CIPER CLAP;MLT","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"BCL10 binds to the Ig domains of MALT1 and promotes MALT1 oligomerization.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2054,"ComplexName":"CASP8-FADD-MALT1-BCL10 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95999;Q13158;Q14790;Q9UDY8","subunits.Entrez.IDs.":"8915;8772;841;10892","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0045893","GO.description":"positive regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.01","FunCat.description":"transcription activation","PubMed.ID":15746428,"subunits.Protein.name.":"B-cell lymphoma/leukemia 10;FAS-associated death domain protein;Caspase-8;Mucosa-associated lymphoid tissue lymphoma translocation protein 1","subunits.Gene.name.":"BCL10;FADD;CASP8;MALT1","subunits.Gene.name.syn.":"CIPER CLAP;MORT1;MCH5;MLT","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2055,"ComplexName":"CASP8-CHUK-IKBKB-MALT1-BCL10 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14920;O15111;O95999;Q14790;Q9UDY8","subunits.Entrez.IDs.":"3551;1147;8915;841;10892","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0045893","GO.description":"positive regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.01","FunCat.description":"transcription activation","PubMed.ID":15746428,"subunits.Protein.name.":"Inhibitor of nuclear factor kappa-B kinase subunit beta;Inhibitor of nuclear factor kappa-B kinase subunit alpha;B-cell lymphoma/leukemia 10;Caspase-8;Mucosa-associated lymphoid tissue lymphoma translocation protein 1","subunits.Gene.name.":"IKBKB;CHUK;BCL10;CASP8;MALT1","subunits.Gene.name.syn.":"IKKB;IKKA, TCF16;CIPER CLAP;MCH5;MLT","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2056,"ComplexName":"BCL10-CHUK-BCL10-IKBKB complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14920;O15111;O95999;Q14790","subunits.Entrez.IDs.":"3551;1147;8915;841","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0045893","GO.description":"positive regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.01","FunCat.description":"transcription activation","PubMed.ID":15746428,"subunits.Protein.name.":"Inhibitor of nuclear factor kappa-B kinase subunit beta;Inhibitor of nuclear factor kappa-B kinase subunit alpha;B-cell lymphoma/leukemia 10;Caspase-8","subunits.Gene.name.":"IKBKB;CHUK;BCL10;CASP8","subunits.Gene.name.syn.":"IKKB;IKKA, TCF16;CIPER CLAP;MCH5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2073,"ComplexName":"TNFRSF11A-TRAF6-SRC complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12931;Q9Y4K3;Q9Y6Q6","subunits.Entrez.IDs.":"6714;7189;8792","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":10635328,"subunits.Protein.name.":"Proto-oncogene tyrosine-protein kinase Src;TNF receptor-associated factor 6;Tumor necrosis factor receptor superfamily member 11A","subunits.Gene.name.":"SRC;TRAF6;TNFRSF11A","subunits.Gene.name.syn.":"SRC1;RNF85;RANK","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2074,"ComplexName":"TRAF6 oligomer complex","Organism":"Human","Synonyms":"None","Cell.line":"lymphocyte","subunits.UniProt.IDs.":"Q9Y4K3","subunits.Entrez.IDs.":"7189","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0043085;GO:0008047","GO.description":"positive regulation of catalytic activity;enzyme activator activity","FunCat.ID":"18.02.01.01","FunCat.description":"enzyme activator","PubMed.ID":15125833,"subunits.Protein.name.":"TNF receptor-associated factor 6","subunits.Gene.name.":"TRAF6","subunits.Gene.name.syn.":"RNF85","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"MALT1 oligomers bind to TRAF6, induce TRAF6 oligomerization, and activate the ligase activity of TRAF6 to polyubiquinate NEMO.These results reveal an oligomerization-ubiquination-phosphorylation cascade that culminates in NF-kappaB activation in T lymphocytes.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":2077,"ComplexName":"B-raf-MAP3K11 complex","Organism":"Human","Synonyms":"None","Cell.line":"CCD-18Co cells","subunits.UniProt.IDs.":"Q16584;Q9NY11","subunits.Entrez.IDs.":"4296;6635","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":15258589,"subunits.Protein.name.":"Mitogen-activated protein kinase kinase kinase 11 ;B-Raf protein","subunits.Gene.name.":"MAP3K11;B-raf","subunits.Gene.name.syn.":"MLK3 PTK1 SPRK;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"MLK3 and B-Raf form a complex in vivo.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2084,"ComplexName":"NFKB1-NFKB2-REL-RELA-RELB complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P19838;Q00653;Q01201;Q04206;Q04864","subunits.Entrez.IDs.":"4790;4791;5971;5970;5966","Protein.complex.purification.method":"MI:0413- electrophoretic mobility shift assay","GO.ID":"GO:2001141;GO:0006355","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":15782119,"subunits.Protein.name.":"Nuclear factor NF-kappa-B p105 subunit;Nuclear factor NF-kappa-B p100 subunit ;Transcription factor RelB;Transcription factor p65;Proto-oncogene c-Rel","subunits.Gene.name.":"NFKB1;NFKB2;RELB;RELA;REL","subunits.Gene.name.syn.":"None;LYT10;None;NFKB3;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2086,"ComplexName":"NFKB1-NFKB2-RELA-RELB complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P19838;Q00653;Q01201;Q04206","subunits.Entrez.IDs.":"4790;4791;5971;5970","Protein.complex.purification.method":"MI:0413- electrophoretic mobility shift assay","GO.ID":"GO:2001141;GO:0006355","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":15782119,"subunits.Protein.name.":"Nuclear factor NF-kappa-B p105 subunit;Nuclear factor NF-kappa-B p100 subunit ;Transcription factor RelB;Transcription factor p65","subunits.Gene.name.":"NFKB1;NFKB2;RELB;RELA","subunits.Gene.name.syn.":"None;LYT10;None;NFKB3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2100,"ComplexName":"CHUK-IKBKB-MAP3K14 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14920;O15111;Q99558","subunits.Entrez.IDs.":"3551;1147;9020","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030234;GO:0050790","GO.description":"enzyme regulator activity;regulation of catalytic activity","FunCat.ID":"18.02.01","FunCat.description":"enzymatic activity regulation / enzyme regulator","PubMed.ID":9346485,"subunits.Protein.name.":"Inhibitor of nuclear factor kappa-B kinase subunit beta;Inhibitor of nuclear factor kappa-B kinase subunit alpha;Mitogen-activated protein kinase kinase kinase 14","subunits.Gene.name.":"IKBKB;CHUK;MAP3K14","subunits.Gene.name.syn.":"IKKB;IKKA, TCF16;NIK","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2101,"ComplexName":"IKKA-IKKB complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14920;O15111","subunits.Entrez.IDs.":"3551;1147","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030234;GO:0050790","GO.description":"enzyme regulator activity;regulation of catalytic activity","FunCat.ID":"18.02.01","FunCat.description":"enzymatic activity regulation / enzyme regulator","PubMed.ID":9346485,"subunits.Protein.name.":"Inhibitor of nuclear factor kappa-B kinase subunit beta;Inhibitor of nuclear factor kappa-B kinase subunit alpha","subunits.Gene.name.":"IKBKB;CHUK","subunits.Gene.name.syn.":"IKKB;IKKA, TCF16","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2104,"ComplexName":"IKKB-NIK complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14920;Q99558","subunits.Entrez.IDs.":"3551;9020","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030234;GO:0050790","GO.description":"enzyme regulator activity;regulation of catalytic activity","FunCat.ID":"18.02.01","FunCat.description":"enzymatic activity regulation / enzyme regulator","PubMed.ID":9346485,"subunits.Protein.name.":"Inhibitor of nuclear factor kappa-B kinase subunit beta;Mitogen-activated protein kinase kinase kinase 14","subunits.Gene.name.":"IKBKB;MAP3K14","subunits.Gene.name.syn.":"IKKB;NIK","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2105,"ComplexName":"IkappaB kinase complex (IKBKB, CHUK, IKBKAP, NFKBIA, RELA, MAP3K14)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14920;O15111;O95163;P25963;Q04206;Q99558","subunits.Entrez.IDs.":"3551;1147;8518;4792;5970;9020","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007249;GO:0023052","GO.description":"I-kappaB kinase/NF-kappaB signaling;signaling","FunCat.ID":"30.01.05.01.04;30.01","FunCat.description":"NIK-I-kappaB/NF-kappaB cascade;cellular signalling","PubMed.ID":9751059,"subunits.Protein.name.":"Inhibitor of nuclear factor kappa-B kinase subunit beta;Inhibitor of nuclear factor kappa-B kinase subunit alpha;Elongator complex protein 1 ;NF-kappa-B inhibitor alpha ;Transcription factor p65;Mitogen-activated protein kinase kinase kinase 14","subunits.Gene.name.":"IKBKB;CHUK;IKBKAP;NFKBIA;RELA;MAP3K14","subunits.Gene.name.syn.":"IKKB;IKKA, TCF16;ELP1 IKAP;IKBA MAD3 NFKBI;NFKB3;NIK","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2112,"ComplexName":"CDC37-HSP90AA1-HSP90AB1-MAP3K11 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P07900;P08238;Q16543;Q16584","subunits.Entrez.IDs.":"3320;3326;11140;4296","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0004- affinity chromatography technologies","GO.ID":"GO:0030234;GO:0050790","GO.description":"enzyme regulator activity;regulation of catalytic activity","FunCat.ID":"18.02.01","FunCat.description":"enzymatic activity regulation / enzyme regulator","PubMed.ID":15001580,"subunits.Protein.name.":"Heat shock protein HSP 90-alpha;Heat shock protein HSP 90-beta;Hsp90 co-chaperone Cdc37;Mitogen-activated protein kinase kinase kinase 11","subunits.Gene.name.":"HSP90AA1;HSP90AB1;CDC37;MAP3K11","subunits.Gene.name.syn.":"HSP90A HSPC1 HSPCA;HSP90B HSPC2 HSPCB;CDC37A;MLK3 PTK1 SPRK","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"MLK3 associates with Hsp90/p50(cdc37) through its catalytic domain in an activity-independent manner.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2118,"ComplexName":"CHUK-ERC1-IKBKB-IKBKG","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14920;O15111;Q8IUD2;Q9Y6K9","subunits.Entrez.IDs.":"3551;1147;23085;8517","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":15218148,"subunits.Protein.name.":"Inhibitor of nuclear factor kappa-B kinase subunit beta;Inhibitor of nuclear factor kappa-B kinase subunit alpha;ELKS/Rab6-interacting/CAST family member 1 ;NF-kappa-B essential modulator","subunits.Gene.name.":"IKBKB;CHUK;ERC1;IKBKG","subunits.Gene.name.syn.":"IKKB;IKKA, TCF16;ELKS KIAA1081 RAB6IP2;FIP3, NEMO","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"ELKS may contribute an important oligomerization interface to members of the IKK complex as well as to other upstream or downstream regulators of NF-kappaB transcriptional activity, such as I(kappa)B(alpha).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2120,"ComplexName":"Chuk-Ikbkb-Ikbkg complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O88351;O88522;Q60680","subunits.Entrez.IDs.":"16150;16151;12675","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007517","GO.description":"muscle organ development","FunCat.ID":"45.03.12","FunCat.description":"muscle","PubMed.ID":15479644,"subunits.Protein.name.":"Inhibitor of nuclear factor kappa-B kinase subunit beta ;NF-kappa-B essential modulator;Inhibitor of nuclear factor kappa-B kinase subunit alpha","subunits.Gene.name.":"Ikbkb;Ikbkg;Chuk","subunits.Gene.name.syn.":"Ikkb;Nemo;Ikka","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2121,"ComplexName":"CHUK-IKBKB-IKBKG complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14920;O15111;Q9Y6K9","subunits.Entrez.IDs.":"3551;1147;8517","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0050789","GO.description":"regulation of biological process","FunCat.ID":"18","FunCat.description":"REGULATION OF METABOLISM AND PROTEIN FUNCTION","PubMed.ID":9751060,"subunits.Protein.name.":"Inhibitor of nuclear factor kappa-B kinase subunit beta;Inhibitor of nuclear factor kappa-B kinase subunit alpha;NF-kappa-B essential modulator","subunits.Gene.name.":"IKBKB;CHUK;IKBKG","subunits.Gene.name.syn.":"IKKB;IKKA, TCF16;FIP3, NEMO","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2123,"ComplexName":"IKBKG homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q9Y6K9","subunits.Entrez.IDs.":"8517","Protein.complex.purification.method":"MI:0018- two hybrid; MI:0030- cross-linking studies","GO.ID":"GO:0030234;GO:0050790","GO.description":"enzyme regulator activity;regulation of catalytic activity","FunCat.ID":"18.02.01","FunCat.description":"enzymatic activity regulation / enzyme regulator","PubMed.ID":12435599,"subunits.Protein.name.":"NF-kappa-B essential modulator","subunits.Gene.name.":"IKBKG","subunits.Gene.name.syn.":"FIP3, NEMO","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"KK-gamma forms homodimer and homotrimer both in vitro and in yeast or mammalian cells through a C-terminal domain comprising amino acids 251-419.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":2124,"ComplexName":"IKK-alpha--ER-alpha-AIB1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15111;P03372;Q9Y6Q9","subunits.Entrez.IDs.":"1147;2099;8202","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0402- chromatin immunoprecipitation assays","GO.ID":"GO:2001141;GO:0006355;GO:0006468;GO:0006470;GO:0046777;GO:0003677;GO:0023052","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;DNA binding;signaling","FunCat.ID":"11.02.03.04;14.07.03;16.03.01;30.01","FunCat.description":"transcriptional control;modification by phosphorylation, dephosphorylation, autophosphorylation;DNA binding;cellular signalling","PubMed.ID":15808510,"subunits.Protein.name.":"Inhibitor of nuclear factor kappa-B kinase subunit alpha;Estrogen receptor;Nuclear receptor coactivator 3","subunits.Gene.name.":"CHUK;ESR1;NCOA3","subunits.Gene.name.syn.":"IKKA, TCF16;ESR, NR3A1;AIB1, BHLHE42, RAC3, TRAM1, ACTR","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors showed that in estradiol-stimulated MCF7 cells, the association of both ER-alpha and AIB1/SRC-3 with IKK-alpha bound to the cyclin D1 promoter was markedly increased in an estrogen-dependent manner. Further siRNA experiments showed that IKK-alpha contributes to the estrogen-mediated phosphorylation of both ER-alpha and AIB1/SRC-3.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2129,"ComplexName":"DNAJB2-HSPA8-PSMA3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P11142;P25686;P25788","subunits.Entrez.IDs.":"3312;3300;5684","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0043161;GO:0006511","GO.description":"intracellular protein transport;protein targeting;protein transport;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process","FunCat.ID":"14.04;20.01.10;14.13.01.01","FunCat.description":"protein targeting, sorting and translocation;protein transport;proteasomal degradation (ubiquitin/proteasomal pathway)","PubMed.ID":15936278,"subunits.Protein.name.":"Heat shock cognate 71 kDa protein;DnaJ homolog subfamily B member 2 ;Proteasome subunit alpha type-3","subunits.Gene.name.":"HSPA8;DNAJB2;PSMA3","subunits.Gene.name.syn.":"HSC70, HSP73, HSPA10;HSJ1 HSPF3;HC8 PSC8","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2142,"ComplexName":"Map2k5-Map3k3 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q61084;Q9WVS7","subunits.Entrez.IDs.":"26406;23938","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0035556;GO:0023052","GO.description":"intracellular signal transduction;signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":12912994,"subunits.Protein.name.":"Mitogen-activated protein kinase kinase kinase 3 ;Dual specificity mitogen-activated protein kinase kinase 5","subunits.Gene.name.":"Map3k3;Map2k5","subunits.Gene.name.syn.":"Mekk3;Mek5 Mkk5 Prkmk5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2143,"ComplexName":"MAP2K5-PRKCI-SQSTM1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P41743;Q13163;Q13501","subunits.Entrez.IDs.":"5584;5607;8878","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0035556;GO:0023052","GO.description":"intracellular signal transduction;signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":12813044,"subunits.Protein.name.":"Protein kinase C iota type;Dual specificity mitogen-activated protein kinase kinase 5 ;Sequestosome-1","subunits.Gene.name.":"PRKCI;MAP2K5;SQSTM1","subunits.Gene.name.syn.":"DXS1179E;MEK5 MKK5 PRKMK5;ORCA OSIL","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2145,"ComplexName":"HSF1-YWHAE complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62258;Q00613","subunits.Entrez.IDs.":"7531;3297","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0096- pull down","GO.ID":"GO:0009408","GO.description":"response to heat","FunCat.ID":"32.01.05","FunCat.description":"heat shock response","PubMed.ID":15364926,"subunits.Protein.name.":"14-3-3 protein epsilon ;Heat shock factor protein 1","subunits.Gene.name.":"YWHAE;HSF1","subunits.Gene.name.syn.":";HSTF1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2147,"ComplexName":"Aip-Hsp90-Ahr complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O08915;P11499;P30561","subunits.Entrez.IDs.":"11632;15516;11622","Protein.complex.purification.method":"MI:0018- two hybrid; MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0006886;GO:0006605;GO:0015031;GO:0005737","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;intracellular protein transport;protein targeting;protein transport;cytoplasm","FunCat.ID":"11.02.03.04;14.04;20.01.10;70.03","FunCat.description":"transcriptional control;protein targeting, sorting and translocation;protein transport;cytoplasm","PubMed.ID":9083006,"subunits.Protein.name.":"AH receptor-interacting protein ;Heat shock protein HSP 90-beta ;Aryl hydrocarbon receptor","subunits.Gene.name.":"Aip;Hsp90ab1;Ahr","subunits.Gene.name.syn.":";Hsp84 Hsp84-1 Hspcb;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors suggest that AIP influences ligand receptivity and/or nuclear targeting of AhR.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2149,"ComplexName":"Arnt-Sim2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P53762;Q61079","subunits.Entrez.IDs.":"11863;20465","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":11782478,"subunits.Protein.name.":"Aryl hydrocarbon receptor nuclear translocator;Single-minded homolog 2","subunits.Gene.name.":"Arnt;Sim2","subunits.Gene.name.syn.":"None;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The murine SIM factors, in combination with ARNT, attenuate transcription from the hypoxia-inducible erythropoietin (EPO) enhancer during hypoxia.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2151,"ComplexName":"Arnt-Sim1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P53762;Q61045","subunits.Entrez.IDs.":"11863;20464","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008152","GO.description":"metabolic process","FunCat.ID":"1","FunCat.description":"METABOLISM","PubMed.ID":11782478,"subunits.Protein.name.":"Aryl hydrocarbon receptor nuclear translocator;Single-minded homolog 1","subunits.Gene.name.":"Arnt;Sim1","subunits.Gene.name.syn.":"None;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The murine SIM factors, in combination with ARNT, attenuate transcription from the hypoxia-inducible erythropoietin (EPO) enhancer during hypoxia.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2152,"ComplexName":"ARNT-HLF complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P27540;Q16534","subunits.Entrez.IDs.":"405;3131","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0045893","GO.description":"positive regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.01","FunCat.description":"transcription activation","PubMed.ID":9113979,"subunits.Protein.name.":"Aryl hydrocarbon receptor nuclear translocator ;Hepatic leukemia factor","subunits.Gene.name.":"ARNT;HLF","subunits.Gene.name.syn.":"BHLHE2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2153,"ComplexName":"ITGAM-ITGB2-CD11 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"blood cell","subunits.UniProt.IDs.":"P05107;P08962;P11215","subunits.Entrez.IDs.":"3689;967;3684","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0023052;GO:0007155","GO.description":"signaling;cell adhesion","FunCat.ID":"30.01;34.07","FunCat.description":"cellular signalling;cell adhesion","PubMed.ID":8871662,"subunits.Protein.name.":"Integrin beta-2;CD63 antigen;Integrin alpha-M","subunits.Gene.name.":"ITGB2;CD63;ITGAM","subunits.Gene.name.syn.":"CD18 MFI7;MLA1 TSPAN30;CD11B CR3A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2156,"ComplexName":"YBX1-AKT1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P31749;P67809","subunits.Entrez.IDs.":"207;4904","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0019- coimmunoprecipitation","GO.ID":"GO:0008361;GO:0005634","GO.description":"regulation of cell size;nucleus","FunCat.ID":"40.01.05;70.10","FunCat.description":"growth regulators / regulation of cell size;nucleus","PubMed.ID":15806160,"subunits.Protein.name.":"RAC-alpha serine/threonine-protein kinase;Nuclease-sensitive element-binding protein 1","subunits.Gene.name.":"AKT1;YBX1","subunits.Gene.name.syn.":"PKB, RAC;NSEP1 YB1","Disease.comment":"Akt and YB-1 work together to promote the growth and possibly the development of breast tumors.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2159,"ComplexName":"AR-AKT-APPL complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P10275;P31749;Q9UKG1","subunits.Entrez.IDs.":"367;207;26060","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":12621049,"subunits.Protein.name.":"Androgen receptor;RAC-alpha serine/threonine-protein kinase;DCC-interacting protein 13-alpha","subunits.Gene.name.":"AR;AKT1;APPL1","subunits.Gene.name.syn.":"DHTR, NR3C4;PKB, RAC;APPL DIP13A KIAA1428","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors  suggest that APPL, Akt, and AR may exist in a complex and Akt may serve as an important bridge factor for the association of APPL with AR. They demonstrated that the APPL\\u00b7AR complex was not clearly seen, and that the addition of Akt markedly enhanced APPL\\u00b7AR complex formation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2160,"ComplexName":"AOF2-AR complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60341;P10275","subunits.Entrez.IDs.":"23028;367","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0045893","GO.description":"positive regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.01","FunCat.description":"transcription activation","PubMed.ID":16079795,"subunits.Protein.name.":"Lysine-specific histone demethylase 1A;Androgen receptor","subunits.Gene.name.":"KDM1A;AR","subunits.Gene.name.syn.":"AOF2 KDM1 KIAA0601 LSD1;DHTR, NR3C4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The androgen receptor and LSD1 form chromatin-associated complexes in a ligand-dependent manner. LSD1 co-localizes with the androgen receptor in normal human prostate and prostate tumour.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2162,"ComplexName":"APPBP1-UBA3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q13564;Q8TBC4","subunits.Entrez.IDs.":"8883;9039","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0016567;GO:0016579","GO.description":"protein ubiquitination;protein deubiquitination","FunCat.ID":"14.07.05","FunCat.description":"modification by ubiquitination, deubiquitination","PubMed.ID":12646924,"subunits.Protein.name.":"NEDD8-activating enzyme E1 regulatory subunit ;NEDD8-activating enzyme E1 catalytic subunit","subunits.Gene.name.":"NAE1;UBA3","subunits.Gene.name.syn.":"APPBP1;UBE1C","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The APPBP1-UBA3 complex initiates NEDD8 conjugation by first catalyzing adenylation of the C terminus of NEDD8 and ultimately catalyzing transfer of NEDD8 to the downstream enzyme in the pathway, Ubc12 (PMID:16275315).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2169,"ComplexName":"Ubiquitin E3 ligase (Neurl2, Tceb1, Tceb2, Cul5, Rbx1)","Organism":"Mouse","Synonyms":"Ozz-E3","Cell.line":"None","subunits.UniProt.IDs.":"P62869;P62878;P83940;Q9D0S4;Q9D5V5","subunits.Entrez.IDs.":"67673;56438;67923;415115;75717","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511;GO:0007519;GO:0014706","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;skeletal muscle tissue development;striated muscle tissue development","FunCat.ID":"14.07.05;14.13.01.01;41.05.15;45.03.12.01","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway);myogenesis;striated muscle","PubMed.ID":14960280,"subunits.Protein.name.":"Transcription elongation factor B polypeptide 2 ;E3 ubiquitin-protein ligase RBX1;Transcription elongation factor B polypeptide 1 ;Neuralized-like protein 2;Cullin-5","subunits.Gene.name.":"Tceb2;Rbx1;Tceb1;Neurl2;Cul5","subunits.Gene.name.syn.":";None;;Ozz;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. In the differentiating myofibers, the RING-type ubiquitin E3 ligase (containing Neurl2, Tceb1, Tceb2, Cul5 and Rbx1) regulates the levels of sarcolemma-associated beta-catenin by mediating its degradation via the proteasome. Expression of beta-catenin mutants that reduce the binding of Ozz to endogenous beta-catenin leads to Mb-beta-catenin accumulation and myofibrillogenesis defects similar to those observed in Ozz None myocytes.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2170,"ComplexName":"Ubiquitin E3 ligase (CDC34, CUL1, RBX1)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P49427;P62877;Q13616","subunits.Entrez.IDs.":"997;9978;8454","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process","FunCat.ID":"14.07.05;14.13.01.01","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway)","PubMed.ID":11675391,"subunits.Protein.name.":"Ubiquitin-conjugating enzyme E2 R1 ;E3 ubiquitin-protein ligase RBX1;Cullin-1","subunits.Gene.name.":"CDC34;RBX1;CUL1","subunits.Gene.name.syn.":"UBCH3 UBE2R1;RNF75, ROC1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. The conjugation of Nedd8 to the ROC1-CUL1 complex selectively stimulates Cdc34-catalyzed Lys48-linked multiubiquitin chain assembly.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2171,"ComplexName":"Ubiquitin E3 ligase (CHEK1, CUL4A)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14757;Q13619","subunits.Entrez.IDs.":"1111;8451","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511;GO:0006974;GO:0005634","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"14.07.05;14.13.01.01;32.01.09;70.10","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway);DNA damage response;nucleus","PubMed.ID":16137618,"subunits.Protein.name.":"Serine/threonine-protein kinase Chk1 ;Cullin-4A","subunits.Gene.name.":"CHEK1;CUL4A","subunits.Gene.name.syn.":"CHK1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. The Chk1 kinase is a major effector of S phase checkpoint signaling during the cellular response to genotoxic stress. Replicative stress induces the polyubiquitination and degradation of Chk1 in human cells.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2172,"ComplexName":"Ubiquitin E3 ligase (CDT1, DDB1, CUL4A, RBX1)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62877;Q13619;Q16531;Q9H211","subunits.Entrez.IDs.":"9978;8451;1642;81620","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511;GO:0006974","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;cellular response to DNA damage stimulus","FunCat.ID":"14.07.05;14.13.01.01;32.01.09","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway);DNA damage response","PubMed.ID":15448697,"subunits.Protein.name.":"E3 ubiquitin-protein ligase RBX1;Cullin-4A;DNA damage-binding protein 1;DNA replication factor Cdt1","subunits.Gene.name.":"RBX1;CUL4A;DDB1;CDT1","subunits.Gene.name.syn.":"RNF75, ROC1;None;XAP1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. The CDT1-DDB1-CUL4A complex was observed in an investigation of targeted ubiquitination of CDT1 by the DDB1-CUL4A-ROC1 ligase in response to DNA damage.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2173,"ComplexName":"COP9 signalosome complex","Organism":"Mouse","Synonyms":"CSN","Cell.line":"COS cells; liver","subunits.UniProt.IDs.":"O35864;P56213;P61202;Q8VBV7;Q99LD4","subunits.Entrez.IDs.":"26754;11692;12848;108679;209318","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0276-blue native page","GO.ID":"GO:0001889;GO:0005634","GO.description":"liver development;nucleus","FunCat.ID":"47.03.11.07;70.10","FunCat.description":"liver;nucleus","PubMed.ID":15304329,"subunits.Protein.name.":"COP9 signalosome complex subunit 5;FAD-linked sulfhydryl oxidase ALR;COP9 signalosome complex subunit 2;COP9 signalosome complex subunit 8;COP9 signalosome complex subunit 1","subunits.Gene.name.":"Cops5;Gfer;Cops2;Cops8;Gps1","subunits.Gene.name.syn.":"Csn5, Jab1, Kic2;Alr;Csn2, Trip15;Csn8;Cops1, Csn1","Disease.comment":"None","Subunits.comment":"At the time of annotation, the members of the protein complex (green monkey) were not found in the UniProt database.The orthologous proteins from mouse were used.","Complex.comment":"CSN is a key player in the functional regulation of hepatopoietin (HPO).It also functions at the interface between signal transduction, ubiquitin-dependent proteolysis, and developmental control.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2174,"ComplexName":"COP9 signalosome complex","Organism":"Human","Synonyms":"JAB1-containing signalosome (GPS1, COPS2, COPS3, COPS4, COPS5, COPS6, COPS7); COP9 complex homolog","Cell.line":"None","subunits.UniProt.IDs.":"P61201;Q13098;Q7L5N1;Q92905;Q99627;Q9BT78;Q9UBW8;Q9UNS2","subunits.Entrez.IDs.":"9318;2873;10980;10987;10920;51138;50813;8533","Protein.complex.purification.method":"MI:0047-far western blotting","GO.ID":"GO:2001141;GO:0006355;GO:0007165;GO:0009583;GO:0009416","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;signal transduction;detection of light stimulus;response to light stimulus","FunCat.ID":"11.02.03.04;30;34.11.01","FunCat.description":"transcriptional control;CELLULAR COMMUNICATION/SIGNAL TRANSDUCTION MECHANISM;photoperception and response","PubMed.ID":9535219,"subunits.Protein.name.":"COP9 signalosome complex subunit 2;COP9 signalosome complex subunit 1;COP9 signalosome complex subunit 6;COP9 signalosome complex subunit 5;COP9 signalosome complex subunit 8;COP9 signalosome complex subunit 4;COP9 signalosome complex subunit 7a;COP9 signalosome complex subunit 3","subunits.Gene.name.":"COPS2;GPS1;COPS6;COPS5;COPS8;COPS4;COPS7A;COPS3","subunits.Gene.name.syn.":"CSN2, TRIP15;COPS1, CSN1;CSN6, HVIP;CSN5, JAB1;CSN8;CSN4;CSN7A, DERP10;CSN3","Disease.comment":"None","Subunits.comment":"Since the authors did not specify COP7, we used isoform COPS7A.","Complex.comment":"The purified complex is very similar, if not identical, to the plant COP9 complex involved in light-mediated signal transduction. A regulating transcriptional activity is discussed.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2179,"ComplexName":"CNS-P53 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04637;P61201;Q13098;Q7L5N1;Q92905;Q99627;Q9BT78;Q9UBW8;Q9UNS2","subunits.Entrez.IDs.":"7157;9318;2873;10980;10987;10920;51138;50813;8533","Protein.complex.purification.method":"MI:0096- pull down; MI:0047- far western blotting; MI:0040- electron microscopy","GO.ID":"GO:0006886;GO:0006605;GO:0015031","GO.description":"intracellular protein transport;protein targeting;protein transport","FunCat.ID":"14.04;20.01.10","FunCat.description":"protein targeting, sorting and translocation;protein transport","PubMed.ID":11285227,"subunits.Protein.name.":"Cellular tumor antigen p53;COP9 signalosome complex subunit 2;COP9 signalosome complex subunit 1;COP9 signalosome complex subunit 6;COP9 signalosome complex subunit 5;COP9 signalosome complex subunit 8;COP9 signalosome complex subunit 4;COP9 signalosome complex subunit 7a;COP9 signalosome complex subunit 3","subunits.Gene.name.":"TP53;COPS2;GPS1;COPS6;COPS5;COPS8;COPS4;COPS7A;COPS3","subunits.Gene.name.syn.":"P53;CSN2, TRIP15;COPS1, CSN1;CSN6, HVIP;CSN5, JAB1;CSN8;CSN4;CSN7A, DERP10;CSN3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2183,"ComplexName":"Kaiso-NCOR complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15379;O60907;O75164;O75376;P52732;Q13227;Q86T24;Q92828;Q9BZK7;Q9UPN9","subunits.Entrez.IDs.":"8841;6907;9682;9611;3832;2874;10009;7464;79718;51592","Protein.complex.purification.method":"MI:0047-far western blotting","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;DNA binding;organization of chromosome structure;nucleus","PubMed.ID":14527417,"subunits.Protein.name.":"Histone deacetylase 3;F-box-like/WD repeat-containing protein TBL1X;Lysine-specific demethylase 4A;Nuclear receptor corepressor 1;Kinesin-like protein KIF11;G protein pathway suppressor 2;Transcriptional regulator Kaiso;Coronin-2A;F-box-like/WD repeat-containing protein TBL1XR1;E3 ubiquitin-protein ligase TRIM33","subunits.Gene.name.":"HDAC3;TBL1X;KDM4A;NCOR1;KIF11;GPS2;ZBTB33;CORO2A;TBL1XR1;TRIM33","subunits.Gene.name.syn.":"None;TBL1;JHDM3A JMJD2 JMJD2A KIAA0677;KIAA1047;EG5 KNSL1 TRIP5;None;KAISO ZNF348;IR10 WDR2;IRA1 TBLR1;KIAA1113 RFG7 TIF1G","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Kaiso targets the N-CoR complex to the MTA2 gene promoter in a methylation-dependent manner.The authors postulate that deacetylation of chromatin stabilizes the association of Kaiso-N-CoR with chromatin.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2184,"ComplexName":"Gata1-Gfi1b complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O70237;P17679","subunits.Entrez.IDs.":"14582;14460","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0045892;GO:0030154;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;cell differentiation;nucleus","FunCat.ID":"11.02.03.04.03;40.02;70.10","FunCat.description":"transcription repression;cell differentiation;nucleus","PubMed.ID":15920471,"subunits.Protein.name.":"Zinc finger protein Gfi-1b ;Erythroid transcription factor","subunits.Gene.name.":"Gfi1b;Gata1","subunits.Gene.name.syn.":";Gf-1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Experiments suggest a role for the Gata1-Gfi1b complex in the repression of genes associated with cell proliferation.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2185,"ComplexName":"Gata1-Ldb1-Tal1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P17679;P22091;P70662","subunits.Entrez.IDs.":"14460;21349;16825","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0045893;GO:0030154;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;cell differentiation;nucleus","FunCat.ID":"11.02.03.04.01;40.02;70.10","FunCat.description":"transcription activation;cell differentiation;nucleus","PubMed.ID":15920471,"subunits.Protein.name.":"Erythroid transcription factor ;T-cell acute lymphocytic leukemia protein 1 homolog ;LIM domain-binding protein 1","subunits.Gene.name.":"Gata1;Tal1;Ldb1","subunits.Gene.name.syn.":"Gf-1;Scl Tal-1;Nli","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Strong GATA-1 binding and a clear enrichment for TAL-1 binding were detected at the EKLF enhancer, providing evidence for a role as transcriptional activator for the Gata1-Ldb1-Tal1 complex.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2186,"ComplexName":"Gata1-Snf2h complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P17679;Q91ZW3","subunits.Entrez.IDs.":"14460;93762","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005634","GO.description":"nucleus","FunCat.ID":"70.1","FunCat.description":"nucleus","PubMed.ID":15920471,"subunits.Protein.name.":"Erythroid transcription factor ;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5","subunits.Gene.name.":"Gata1;Smarca5","subunits.Gene.name.syn.":"Gf-1;Snf2h","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The interaction between SNF2h and GATA-1 may help explain the observation that knocking down SNF2h expression in primary hematopoietic progenitor cells blocked erythroid differentiation (PMID:14617767).","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2187,"ComplexName":"Ubiquitin E3 ligase (NFKBIA, FBXW11, BTRC, CUL1, SKP1A)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P25963;P63208;Q13616;Q9UKB1;Q9Y297","subunits.Entrez.IDs.":"4792;6500;8454;23291;8945","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511;GO:0005737","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;cytoplasm","FunCat.ID":"14.07.05;14.13.01.01;70.03","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway);cytoplasm","PubMed.ID":10644755,"subunits.Protein.name.":"NF-kappa-B inhibitor alpha ;S-phase kinase-associated protein 1;Cullin-1;F-box/WD repeat-containing protein 11 ;F-box/WD repeat-containing protein 1A","subunits.Gene.name.":"NFKBIA;SKP1;CUL1;FBXW11;BTRC","subunits.Gene.name.syn.":"IKBA MAD3 NFKBI;EMC19, OCP2, SKP1A, TCEB1L;None;BTRCP2 FBW1B FBXW1B KIAA0696;BTRCP FBW1A FBXW1A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Ubiquitination-dependent destruction of NF-kappa-B inhibitor alpha is mediated by ubiquitin E3 ligases containing heterdimers and homodimers of beta-TrCP1 (BTRC) and beta-TrCP2 (FBXW11).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2188,"ComplexName":"Ubiquitin E3 ligase (CDC34, NEDD8, BTRC, CUL1, SKP1A, RBX1)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62877;P63208;Q13616;Q15843;Q9Y297","subunits.Entrez.IDs.":"9978;6500;8454;4738;8945","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511;GO:0005737","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;cytoplasm","FunCat.ID":"14.07.05;14.13.01.01;70.03","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway);cytoplasm","PubMed.ID":10713156,"subunits.Protein.name.":"E3 ubiquitin-protein ligase RBX1;S-phase kinase-associated protein 1;Cullin-1;NEDD8 ;F-box/WD repeat-containing protein 1A","subunits.Gene.name.":"RBX1;SKP1;CUL1;NEDD8;BTRC","subunits.Gene.name.syn.":"RNF75, ROC1;EMC19, OCP2, SKP1A, TCEB1L;None;;BTRCP FBW1A FBXW1A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Regulation of NF-kappaB occurs through phosphorylation-dependent ubiquitination of IkappaBalpha, which is degraded by the 26S proteasome. Recent studies have shown that ubiquitination of IkappaBalpha is carried out by ubiquitin E3 ligase complexes. Nedd8 modification of the Cul-1 component of ubiquitin E3 ligases is important for ubiquitination of IkappaBalpha.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2189,"ComplexName":"Ubiquitin E3 ligase (SMAD3, BTRC, CUL1, SKP1A, RBX1)","Organism":"Human","Synonyms":"ROC1-SCFFbw1a","Cell.line":"None","subunits.UniProt.IDs.":"P62877;P63208;P84022;Q13616;Q9Y297","subunits.Entrez.IDs.":"9978;6500;4088;8454;8945","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511;GO:0023052;GO:0005737;GO:0005634","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;signaling;cytoplasm;nucleus","FunCat.ID":"14.07.05;14.13.01.01;30.01;70.03;70.10","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway);cellular signalling;cytoplasm;nucleus","PubMed.ID":11359933,"subunits.Protein.name.":"E3 ubiquitin-protein ligase RBX1;S-phase kinase-associated protein 1;Mothers against decapentaplegic homolog 3;Cullin-1;F-box/WD repeat-containing protein 1A","subunits.Gene.name.":"RBX1;SKP1;SMAD3;CUL1;BTRC","subunits.Gene.name.syn.":"RNF75, ROC1;EMC19, OCP2, SKP1A, TCEB1L;MADH3;None;BTRCP FBW1A FBXW1A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Ubiquitin E3 ligase complex ROC1-SCFFbw1a interacts with activated Smad3 through its MH2 domain and induces the ubiquitination and proteasomal degradation of the transcriptional modulator Smad3.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2190,"ComplexName":"Ubiquitin E3 ligase (Fbxo15, Cul1, Skp1a)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q9QZN0;Q9WTX5;Q9WTX6","subunits.Entrez.IDs.":"50764;21402;26965","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579","GO.description":"protein ubiquitination;protein deubiquitination","FunCat.ID":"14.07.05","FunCat.description":"modification by ubiquitination, deubiquitination","PubMed.ID":12665572,"subunits.Protein.name.":"F-box only protein 15;S-phase kinase-associated protein 1;Cullin-1","subunits.Gene.name.":"Fbxo15;Skp1;Cul1","subunits.Gene.name.syn.":"Fbx15;Skp1a;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome.Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. The F-box-containing protein Fbx15 is a novel target of the POU transcription factor Oct3/4 but is dispensable for embryonic stem cell self-renewal and mouse development.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2191,"ComplexName":"Ubiquitin E3 ligase (FBXO18, SKP1A, CUL1, RBX1)","Organism":"Human","Synonyms":"SCFhFBH1 complex","Cell.line":"None","subunits.UniProt.IDs.":"P62877;P63208;Q13616;Q8NFZ0","subunits.Entrez.IDs.":"9978;6500;8454;84893","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process","FunCat.ID":"14.07.05;14.13.01.01","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway)","PubMed.ID":11956208,"subunits.Protein.name.":"E3 ubiquitin-protein ligase RBX1;S-phase kinase-associated protein 1;Cullin-1;F-box DNA helicase 1","subunits.Gene.name.":"RBX1;SKP1;CUL1;FBXO18","subunits.Gene.name.syn.":"RNF75, ROC1;EMC19, OCP2, SKP1A, TCEB1L;None;FBH1 FBX18","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. hFBH1 is the first F-box protein implicated in nucleic acid metabolism.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2192,"ComplexName":"Ubiquitin E3 ligase (NIPA, SKP1A, CUL1, RBX1)","Organism":"Human","Synonyms":"SCF(NIPA)","Cell.line":"None","subunits.UniProt.IDs.":"P62877;P63208;Q13616;Q86WB0","subunits.Entrez.IDs.":"9978;6500;8454;51530","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0000278;GO:0016567;GO:0016579;GO:0043161;GO:0006511;GO:0005634","GO.description":"mitotic cell cycle;protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;nucleus","FunCat.ID":"10.03.01.01;14.07.05;14.13.01.01;70.10","FunCat.description":"mitotic cell cycle;modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway);nucleus","PubMed.ID":16009132,"subunits.Protein.name.":"E3 ubiquitin-protein ligase RBX1;S-phase kinase-associated protein 1;Cullin-1;Nuclear-interacting partner of ALK","subunits.Gene.name.":"RBX1;SKP1;CUL1;ZC3HC1","subunits.Gene.name.syn.":"RNF75, ROC1;EMC19, OCP2, SKP1A, TCEB1L;None;NIPA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Activity of ubiquitin E3 ligase (containing NIPA, SKP1A, CUL1 and RBX1) oscillates throughout the cell cycle, and cell-cycle-regulated phosphorylation of NIPA constitutes the responsible timing circuit. Nuclear cyclin B1 was identified to be a critical substrate of the complex in interphase. According to the oscillating activity of ubiquitin E3 ligase (containing NIPA, SKP1A, CUL1 and RBX1), this targeting process is terminated at G2/M to allow for nuclear cyclin B1 accumulation, which is necessary for mitotic entry.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2193,"ComplexName":"Ubiquitin E3 ligase (Fbxo32, Skp1a, Cul1, Rbx1)","Organism":"Mouse","Synonyms":"None","Cell.line":"striated muscle","subunits.UniProt.IDs.":"P62878;Q9CPU7;Q9WTX5;Q9WTX6","subunits.Entrez.IDs.":"56438;67731;21402;26965","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process","FunCat.ID":"14.07.05;14.13.01.01","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway)","PubMed.ID":11717410,"subunits.Protein.name.":"E3 ubiquitin-protein ligase RBX1;F-box only protein 32;S-phase kinase-associated protein 1;Cullin-1","subunits.Gene.name.":"Rbx1;Fbxo32;Skp1;Cul1","subunits.Gene.name.syn.":"None;None;Skp1a;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Atrogin-1 (Fbxo32) is one of the few examples of an F-box protein or Ub-protein ligase (E3) expressed in a tissue-specific manner (striated muscles) and appears to be a critical component in the enhanced proteolysis leading to muscle atrophy in diverse diseases.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2194,"ComplexName":"Ubiquitin E3 ligase (Fbxo2, Skp1a, Cul1, Rbx1)","Organism":"Mouse","Synonyms":"SCF(Fbx2)","Cell.line":"None","subunits.UniProt.IDs.":"P62878;Q80UW2;Q9WTX5;Q9WTX6","subunits.Entrez.IDs.":"56438;230904;21402;26965","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511;GO:0030968;GO:0005737","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;endoplasmic reticulum unfolded protein response;cytoplasm","FunCat.ID":"14.07.05;14.13.01.01;32.01.07;70.03","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway);unfolded protein response (e.g. ER quality control);cytoplasm","PubMed.ID":12140560,"subunits.Protein.name.":"E3 ubiquitin-protein ligase RBX1;F-box only protein 2;S-phase kinase-associated protein 1;Cullin-1","subunits.Gene.name.":"Rbx1;Fbxo2;Skp1;Cul1","subunits.Gene.name.syn.":"None;Fbs1 Fbx2;Skp1a;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Results indicate that SCF(Fbx2) ubiquitinates N-glycosylated proteins that are translocated from the ER to the cytosol by the quality control mechanism.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2196,"ComplexName":"9-1-1-LIG1 complex","Organism":"Human","Synonyms":"LIG1-9-1-1 complex","Cell.line":"None","subunits.UniProt.IDs.":"O60671;O60921;P18858;Q99638","subunits.Entrez.IDs.":"5810;3364;3978;5883","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0006281;GO:0000075;GO:0006974;GO:0005634","GO.description":"DNA repair;cell cycle checkpoint;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;10.03.01.03;32.01.09;70.10","FunCat.description":"DNA repair;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA damage response;nucleus","PubMed.ID":15871698,"subunits.Protein.name.":"Cell cycle checkpoint protein RAD1;Checkpoint protein HUS1;DNA ligase 1;Cell cycle checkpoint control protein RAD9A","subunits.Gene.name.":"RAD1;HUS1;LIG1;RAD9A","subunits.Gene.name.syn.":"REC1;None;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The 9-1-1 complex can stimulate DNA ligase I.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2197,"ComplexName":"9-1-1-FEN1 complex","Organism":"Human","Synonyms":"FEN1-9-1-1 complex","Cell.line":"None","subunits.UniProt.IDs.":"O60671;O60921;P39748;Q99638","subunits.Entrez.IDs.":"5810;3364;2237;5883","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0006308;GO:0006401;GO:0006281;GO:0000075;GO:0006974;GO:0005634","GO.description":"DNA catabolic process;RNA catabolic process;DNA repair;cell cycle checkpoint;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"01.03.16.03;01.03.16.01;10.01.05.01;10.03.01.03;32.01.09;70.10","FunCat.description":"DNA degradation;RNA degradation;DNA repair;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA damage response;nucleus","PubMed.ID":15556996,"subunits.Protein.name.":"Cell cycle checkpoint protein RAD1;Checkpoint protein HUS1;Flap endonuclease 1;Cell cycle checkpoint control protein RAD9A","subunits.Gene.name.":"RAD1;HUS1;FEN1;RAD9A","subunits.Gene.name.syn.":"REC1;None;RAD2;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The 9-1-1 complex stimulates FEN1 activity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2198,"ComplexName":"9-1-1-POLB complex","Organism":"Human","Synonyms":"RAD9-RAD1-HUS1-POLB complex","Cell.line":"None","subunits.UniProt.IDs.":"O60671;O60921;P06746;Q99638","subunits.Entrez.IDs.":"5810;3364;5423;5883","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0006281;GO:0000075;GO:0006974;GO:0005634","GO.description":"DNA repair;cell cycle checkpoint;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;10.03.01.03;32.01.09;70.10","FunCat.description":"DNA repair;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA damage response;nucleus","PubMed.ID":15314187,"subunits.Protein.name.":"Cell cycle checkpoint protein RAD1;Checkpoint protein HUS1;DNA polymerase beta;Cell cycle checkpoint control protein RAD9A","subunits.Gene.name.":"RAD1;HUS1;POLB;RAD9A","subunits.Gene.name.syn.":"REC1;None;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The 9-1-1 complex directly interacts with and stimulates POLB activity thus recruiting POLB to DNA damage sites.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2199,"ComplexName":"CTF18-RFC subcomplex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P35249;P35250;P40937;P40938;Q8WVB6","subunits.Entrez.IDs.":"5984;5982;5985;5983;63922","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006794;GO:0006796;GO:0006260;GO:0007059;GO:0005515;GO:0003677;GO:0051276;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;DNA replication;chromosome segregation;protein binding;DNA binding;chromosome organization;nucleus","FunCat.ID":"01.04;10.01.03;10.03.04.05;16.01;16.03.01;42.10.03;70.10","FunCat.description":"phosphate metabolism;DNA synthesis and replication;chromosome segregation/division;protein binding;DNA binding;organization of chromosome structure;nucleus","PubMed.ID":12930902,"subunits.Protein.name.":"Replication factor C subunit 4;Replication factor C subunit 2;Replication factor C subunit 5;Replication factor C subunit 3;Chromosome transmission fidelity protein 18 homolog","subunits.Gene.name.":"RFC4;RFC2;RFC5;RFC3;CHTF18","subunits.Gene.name.syn.":"None;None;None;None;C16orf41 CTF18","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"CTF18 interacts with RFC5.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2200,"ComplexName":"RFC2-5 subcomplex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P35249;P35250;P40937;P40938","subunits.Entrez.IDs.":"5984;5982;5985;5983","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006794;GO:0006796;GO:0006260;GO:0003677;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;DNA replication;DNA binding;nucleus","FunCat.ID":"01.04;10.01.03;16.03.01;70.10","FunCat.description":"phosphate metabolism;DNA synthesis and replication;DNA binding;nucleus","PubMed.ID":9488738,"subunits.Protein.name.":"Replication factor C subunit 4;Replication factor C subunit 2;Replication factor C subunit 5;Replication factor C subunit 3","subunits.Gene.name.":"RFC4;RFC2;RFC5;RFC3","subunits.Gene.name.syn.":"None;None;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Reconstitution experiments have revealed that a minimum of three subunits (the 40-, 37-, and 36-kDa subunits) are required for DNA-dependent ATPase activity in vitro.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2201,"ComplexName":"PCNA-RFC2-5 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12004;P35249;P35250;P40937;P40938","subunits.Entrez.IDs.":"5111;5984;5982;5985;5983","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006260;GO:0005634","GO.description":"DNA replication;nucleus","FunCat.ID":"10.01.03;70.10","FunCat.description":"DNA synthesis and replication;nucleus","PubMed.ID":12171929,"subunits.Protein.name.":"Proliferating cell nuclear antigen;Replication factor C subunit 4;Replication factor C subunit 2;Replication factor C subunit 5;Replication factor C subunit 3","subunits.Gene.name.":"PCNA;RFC4;RFC2;RFC5;RFC3","subunits.Gene.name.syn.":"None;None;None;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2202,"ComplexName":"CHL12-RFC2-5 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P35249;P35250;P40937;P40938;Q8WVB6","subunits.Entrez.IDs.":"5984;5982;5985;5983;63922","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006260;GO:0005634","GO.description":"DNA replication;nucleus","FunCat.ID":"10.01.03;70.10","FunCat.description":"DNA synthesis and replication;nucleus","PubMed.ID":12171929,"subunits.Protein.name.":"Replication factor C subunit 4;Replication factor C subunit 2;Replication factor C subunit 5;Replication factor C subunit 3;Chromosome transmission fidelity protein 18 homolog","subunits.Gene.name.":"RFC4;RFC2;RFC5;RFC3;CHTF18","subunits.Gene.name.syn.":"None;None;None;None;C16orf41 CTF18","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2203,"ComplexName":"BRD4-RFC complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60885;P35249;P35250;P35251;P40937;P40938","subunits.Entrez.IDs.":"23476;5984;5982;5981;5985;5983","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0000278;GO:0051726;GO:0000082;GO:0005634","GO.description":"mitotic cell cycle;regulation of cell cycle;G1/S transition of mitotic cell cycle;nucleus","FunCat.ID":"10.03.01.01;10.03.01;10.03.01.01.03;70.10","FunCat.description":"mitotic cell cycle;mitotic cell cycle and cell cycle control;G1/S transition of mitotic cell cycle;nucleus","PubMed.ID":12192049,"subunits.Protein.name.":"Bromodomain-containing protein 4 ;Replication factor C subunit 4;Replication factor C subunit 2;Replication factor C subunit 1;Replication factor C subunit 5;Replication factor C subunit 3","subunits.Gene.name.":"BRD4;RFC4;RFC2;RFC1;RFC5;RFC3","subunits.Gene.name.syn.":"HUNK1;None;None;RFC140;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"BRD4 regulates cell cycle progression from G1 to S phase by interacting with RFC1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2204,"ComplexName":"MCM8-ORC2-CDC6 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q13416;Q99741;Q9UJA3","subunits.Entrez.IDs.":"4999;990;84515","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006260;GO:0000082;GO:0005634","GO.description":"DNA replication;G1/S transition of mitotic cell cycle;nucleus","FunCat.ID":"10.01.03;10.03.01.01.03;70.10","FunCat.description":"DNA synthesis and replication;G1/S transition of mitotic cell cycle;nucleus","PubMed.ID":15684404,"subunits.Protein.name.":"Origin recognition complex subunit 2;Cell division control protein 6 homolog ;DNA helicase MCM8","subunits.Gene.name.":"ORC2;CDC6;MCM8","subunits.Gene.name.syn.":"ORC2L;CDC18L;C20orf154","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Down-regulation of MCM8 impairs the G1-to-S transition.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2205,"ComplexName":"ORC5-ORC1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43913;Q13415","subunits.Entrez.IDs.":"5001;4998","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006267;GO:0003688;GO:0005634","GO.description":"pre-replicative complex assembly involved in nuclear cell cycle DNA replication;DNA replication origin binding;nucleus","FunCat.ID":"10.01.03.03;70.10","FunCat.description":"ori recognition and priming complex formation;nucleus","PubMed.ID":15448696,"subunits.Protein.name.":"Origin recognition complex subunit 5;Origin recognition complex subunit 1","subunits.Gene.name.":"ORC5;ORC1","subunits.Gene.name.syn.":"ORC5L;ORC1L PARC1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2210,"ComplexName":"BRCA1-IRIS-pre-replication complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75496;Q13415;Q5YLB2;Q99741","subunits.Entrez.IDs.":"51053;4998;672;990","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0402- chromatin immunoprecipitation assays","GO.ID":"GO:0006260;GO:0005634","GO.description":"DNA replication;nucleus","FunCat.ID":"10.01.03;70.10","FunCat.description":"DNA synthesis and replication;nucleus","PubMed.ID":15448696,"subunits.Protein.name.":"Geminin;Origin recognition complex subunit 1 ;Breast cancer type 1 susceptibility protein ;Cell division control protein 6 homolog","subunits.Gene.name.":"GMNN;ORC1;BRCA1;CDC6","subunits.Gene.name.syn.":";ORC1L PARC1;;CDC18L","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"BRCA1-IRIS is a BRCA1 gene product encoded by an uninterrupted open reading frame that extends from codon 1 of the known BRCA1 open reading frame to a termination point 34 triplets into intron 11. BRCA1-IRIS localizes to the nucleus and fails to interact with BARD1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2211,"ComplexName":"BARD1-BRCA1-CSTF complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P33240;P38398;Q05048;Q12996;Q99728","subunits.Entrez.IDs.":"1478;672;1477;1479;580","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0031123;GO:0031124;GO:0003723;GO:0005634","GO.description":"RNA 3'-end processing;mRNA 3'-end processing;RNA binding;nucleus","FunCat.ID":"11.04.03.05;16.03.03;70.10","FunCat.description":"3'-end processing;RNA binding;nucleus","PubMed.ID":10477523,"subunits.Protein.name.":"Cleavage stimulation factor subunit 2 ;Breast cancer type 1 susceptibility protein;Cleavage stimulation factor subunit 1 ;Cleavage stimulation factor subunit 3 ;BRCA1-associated RING domain protein 1","subunits.Gene.name.":"CSTF2;BRCA1;CSTF1;CSTF3;BARD1","subunits.Gene.name.syn.":";RNF53;;;","Disease.comment":"BRCA1 is involved in breast cancer.","Subunits.comment":"None","Complex.comment":"Interaction of BARD1 with CstF inhibits RNA polyadenylation and ensures that at DNA damage sites nascent RNAs are not erroneously polyadenylated.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2213,"ComplexName":"BRCA1-BARD1-POLR2A complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P24928;P38398;Q99728","subunits.Entrez.IDs.":"5430;672;580","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0016567;GO:0016579;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein ubiquitination;protein deubiquitination;nucleus","FunCat.ID":"11.02.03.04;14.07.05;70.10","FunCat.description":"transcriptional control;modification by ubiquitination, deubiquitination;nucleus","PubMed.ID":15886201,"subunits.Protein.name.":"DNA-directed RNA polymerase II subunit RPB1;Breast cancer type 1 susceptibility protein;BRCA1-associated RING domain protein 1","subunits.Gene.name.":"POLR2A;BRCA1;BARD1","subunits.Gene.name.syn.":"POLR2;RNF53;","Disease.comment":"BRCA1 is involved in breast cancer.","Subunits.comment":"None","Complex.comment":"BRCA1 and BARD1 heterodimer ubiquitinates a hyperphosphorylated form of POLR2A.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2214,"ComplexName":"LMO4-BRCA1-CTIP-LDB1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P38398;P61968;Q86U70;Q99708","subunits.Entrez.IDs.":"672;8543;8861;5932","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04;16.03.01;70.10","FunCat.description":"transcriptional control;DNA binding;nucleus","PubMed.ID":11751867,"subunits.Protein.name.":"Breast cancer type 1 susceptibility protein;LIM domain transcription factor LMO4 ;LIM domain-binding protein 1 ;DNA endonuclease RBBP8","subunits.Gene.name.":"BRCA1;LMO4;LDB1;RBBP8","subunits.Gene.name.syn.":"RNF53;;CLIM2;CTIP","Disease.comment":"BRCA1 is involved in breast cancer.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2215,"ComplexName":"BRCA1-LMO4-CTIP complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P38398;P61968;Q99708","subunits.Entrez.IDs.":"672;8543;5932","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04;16.03.01;70.10","FunCat.description":"transcriptional control;DNA binding;nucleus","PubMed.ID":11751867,"subunits.Protein.name.":"Breast cancer type 1 susceptibility protein;LIM domain transcription factor LMO4 ;DNA endonuclease RBBP8","subunits.Gene.name.":"BRCA1;LMO4;RBBP8","subunits.Gene.name.syn.":"RNF53;;CTIP","Disease.comment":"BRCA1 is involved in breast cancer.","Subunits.comment":"None","Complex.comment":"LMO4 functions as a repressor of BRCA1 activity in breast tissue.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2217,"ComplexName":"MDC1-MRN-ATM-FANCD2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60934;P49959;Q13315;Q14676;Q92878;Q9BXW9","subunits.Entrez.IDs.":"4683;4361;472;9656;10111;2177","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0000075;GO:0003677;GO:0006974;GO:0005634","GO.description":"DNA repair;cell cycle checkpoint;DNA binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;10.03.01.03;16.03.01;32.01.09;70.10","FunCat.description":"DNA repair;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA binding;DNA damage response;nucleus","PubMed.ID":12607005,"subunits.Protein.name.":"Nibrin ;Double-strand break repair protein MRE11A ;Serine-protein kinase ATM ;Mediator of DNA damage checkpoint protein 1 ;DNA repair protein RAD50 ;Fanconi anemia group D2 protein","subunits.Gene.name.":"NBN;MRE11A;ATM;MDC1;RAD50;FANCD2","subunits.Gene.name.syn.":"NBS NBS1 P95;HNGS1 MRE11;;KIAA0170 NFBD1;;FACD","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Prior exposure of cells to irradiation appears to reduce the interaction of MDC1 with ATM and FANCD2.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2218,"ComplexName":"MDC1-MRE11-RAD50-NBS1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60934;P49959;Q14676;Q92878","subunits.Entrez.IDs.":"4683;4361;9656;10111","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0006281;GO:0000075;GO:0006974;GO:0005634","GO.description":"DNA repair;cell cycle checkpoint;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;10.03.01.03;32.01.09;70.10","FunCat.description":"DNA repair;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA damage response;nucleus","PubMed.ID":12607003,"subunits.Protein.name.":"Nibrin ;Double-strand break repair protein MRE11A ;Mediator of DNA damage checkpoint protein 1 ;DNA repair protein RAD50","subunits.Gene.name.":"NBN;MRE11A;MDC1;RAD50","subunits.Gene.name.syn.":"NBS NBS1 P95;HNGS1 MRE11;KIAA0170 NFBD1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In response to ionizing radiation, MDC1 is hyperphosphorylated and rapidly relocalizes to nuclear foci that also contain the MRE11 complex. MDC1-mediated focus formation by the MRE11 complex at sites of DNA damage is crucial for the efficient activation of the intra-S-phase checkpoint.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2219,"ComplexName":"TERF1 homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P54274","subunits.Entrez.IDs.":"7013","Protein.complex.purification.method":"MI:0413- electrophoretic mobility shift assay","GO.ID":"GO:0000278;GO:0051726;GO:0003677;GO:0051276","GO.description":"mitotic cell cycle;regulation of cell cycle;DNA binding;chromosome organization","FunCat.ID":"10.03.01.01;10.03.01;16.03.01;42.10.03","FunCat.description":"mitotic cell cycle;mitotic cell cycle and cell cycle control;DNA binding;organization of chromosome structure","PubMed.ID":9391075,"subunits.Protein.name.":"Telomeric repeat-binding factor 1","subunits.Gene.name.":"TERF1","subunits.Gene.name.syn.":"PIN2 TRBF1 TRF TRF1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TERF1 is shown to be important in regulating telomere length. It may connect mitotic control to the telomere regulatory machinery.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":2220,"ComplexName":"RAD52-ERCC4-ERCC1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P07992;P43351;Q92889","subunits.Entrez.IDs.":"2067;5893;2072","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006308;GO:0006310;GO:0006281;GO:0005634","GO.description":"DNA catabolic process;DNA recombination;DNA repair;nucleus","FunCat.ID":"01.03.16.03;10.01.05.03;10.01.05.01;70.10","FunCat.description":"DNA degradation;DNA recombination;DNA repair;nucleus","PubMed.ID":14734547,"subunits.Protein.name.":"DNA excision repair protein ERCC-1;DNA repair protein RAD52 homolog;DNA repair endonuclease XPF","subunits.Gene.name.":"ERCC1;RAD52;ERCC4","subunits.Gene.name.syn.":";;ERCC11 XPF","Disease.comment":"ERCC4 is involved in xeroderma pigmentosum group F.","Subunits.comment":"None","Complex.comment":"Rad52-XPF-ERCC1 complex processes recombination intermediates generated during the repair of DNA double strand breaks.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2221,"ComplexName":"RPA-MSH4-BLM complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O88700;Q62193;Q8VEE4;Q99MT2;Q9CQ71","subunits.Entrez.IDs.":"12144;19891;68275;55993;68240","Protein.complex.purification.method":"MI:0416- fluorescence microscopy; MI:0040- electron microscopy","GO.ID":"GO:0000279;GO:0007067;GO:0051276;GO:0005634","GO.description":"M phase;mitotic nuclear division;chromosome organization;nucleus","FunCat.ID":"10.03.01.01.11;42.10.03;70.10","FunCat.description":"M phase;organization of chromosome structure;nucleus","PubMed.ID":11950880,"subunits.Protein.name.":"Bloom syndrome protein homolog ;Replication protein A 32 kDa subunit ;Replication protein A 70 kDa DNA-binding subunit ;MutS protein homolog 4 ;Replication protein A 14 kDa subunit","subunits.Gene.name.":"Blm;Rpa2;Rpa1;Msh4;Rpa3","subunits.Gene.name.syn.":";Rpa34;;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"RPA stimulates helicase activity of BLM.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2222,"ComplexName":"BLM complex II","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P15927;P27694;P35244;P54132;Q13472;Q9H9A7","subunits.Entrez.IDs.":"6118;6117;6119;641;7156;80010","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0051276;GO:0006281;GO:0006974;GO:0005634","GO.description":"chromosome organization;DNA repair;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"42.10.03;10.01.05.01;32.01.09;70.10","FunCat.description":"organization of chromosome structure;DNA repair;DNA damage response;nucleus","PubMed.ID":15775963,"subunits.Protein.name.":"Replication protein A 32 kDa subunit ;Replication protein A 70 kDa DNA-binding subunit;Replication protein A 14 kDa subunit ;Bloom syndrome protein ;DNA topoisomerase 3-alpha ;RecQ-mediated genome instability protein 1","subunits.Gene.name.":"RPA2;RPA1;RPA3;BLM;TOP3A;RMI1","subunits.Gene.name.syn.":"REPA2 RPA32 RPA34;REPA1 RPA70;REPA3 RPA14;RECQ2 RECQL3;TOP3;C9orf76","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"BLAP75 is an integral component of BLM complexes and is essential for their stability.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2223,"ComplexName":"BLM-TOP3A complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P54132;Q13472","subunits.Entrez.IDs.":"641;7156","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0051276;GO:0005634","GO.description":"chromosome organization;nucleus","FunCat.ID":"42.10.03;70.10","FunCat.description":"organization of chromosome structure;nucleus","PubMed.ID":10734115,"subunits.Protein.name.":"Bloom syndrome protein ;DNA topoisomerase 3-alpha","subunits.Gene.name.":"BLM;TOP3A","subunits.Gene.name.syn.":"RECQ2 RECQL3;TOP3","Disease.comment":"BLM is involved in Bloom syndrome (BS).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2224,"ComplexName":"MSH2/6-BLM-p53-RAD51 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04637;P43246;P52701;P54132;Q06609","subunits.Entrez.IDs.":"7157;4436;2956;641;5888","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0006974;GO:0005634","GO.description":"DNA repair;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;32.01.09;70.10","FunCat.description":"DNA repair;DNA damage response;nucleus","PubMed.ID":15064730,"subunits.Protein.name.":"Cellular tumor antigen p53;DNA mismatch repair protein Msh2 ;DNA mismatch repair protein Msh6 ;Bloom syndrome protein ;DNA repair protein RAD51 homolog 1","subunits.Gene.name.":"TP53;MSH2;MSH6;BLM;RAD51","subunits.Gene.name.syn.":"P53;;GTBP;RECQ2 RECQL3;RAD51A RECA","Disease.comment":"BLM is involved in Bloom's syndrome.","Subunits.comment":"None","Complex.comment":"MSH2/6 protein complex stimulates the ability of the Bloom's syndrome gene product, BLM, to process Holliday junctions in vitro, an activity that could also be regulated by p53. MSH6 colocalizes with BLM and p53 in hydroxyurea-induced RAD51 nuclear foci.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2225,"ComplexName":"MutS-alpha-histone H4 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"B-cell","subunits.UniProt.IDs.":"P43247;P54276;P62806","subunits.Entrez.IDs.":"17685;17688;None","Protein.complex.purification.method":"MI:0402-chromatin immunoprecipitation assays","GO.ID":"GO:0006312;GO:0030183","GO.description":"mitotic recombination;B cell differentiation","FunCat.ID":"10.01.05.03.03;43.03.07.02.01.01","FunCat.description":"somatic / mitotic recombination;B-cell","PubMed.ID":15753043,"subunits.Protein.name.":"DNA mismatch repair protein Msh2;DNA mismatch repair protein Msh6;Histone H4","subunits.Gene.name.":"Msh2;Msh6;Hist1h4a;","subunits.Gene.name.syn.":"None;Gtmbp;; H4-53; H4-12; ; ; ; ; ; ; ; Hist2h4;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"MSH2 associates with transcribed S regions in primary murine B cells activated for switch recombination. Electron microscopic imaging reveals that MutSalpha binds in vitro to DNA structures formed within transcribed S regions and mediates their synapsis.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2226,"ComplexName":"MutS-alpha-PK-zeta complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P43246;P52701;Q05513","subunits.Entrez.IDs.":"4436;2956;5590","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0043161;GO:0006511","GO.description":"DNA repair;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process","FunCat.ID":"10.01.05.01;14.13.01.01","FunCat.description":"DNA repair;proteasomal degradation (ubiquitin/proteasomal pathway)","PubMed.ID":15808853,"subunits.Protein.name.":"DNA mismatch repair protein Msh2 ;DNA mismatch repair protein Msh6 ;Protein kinase C zeta type","subunits.Gene.name.":"MSH2;MSH6;PRKCZ","subunits.Gene.name.syn.":";GTBP;PKC2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"PKC zeta protects MutS-alpha protein complex from degradation. PKC zeta interacts with hMSH2 and hMSH6 proteins and phosphorylates both.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2228,"ComplexName":"BLM-RAD51L3-XRCC2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43543;O75771;P54132","subunits.Entrez.IDs.":"7516;5892;641","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0005634","GO.description":"DNA repair;nucleus","FunCat.ID":"10.01.05.01;70.10","FunCat.description":"DNA repair;nucleus","PubMed.ID":12975363,"subunits.Protein.name.":"DNA repair protein XRCC2 ;DNA repair protein RAD51 homolog 4 ;Bloom syndrome protein","subunits.Gene.name.":"XRCC2;RAD51D;BLM","subunits.Gene.name.syn.":";RAD51L3;RECQ2 RECQL3","Disease.comment":"BLM is involved in Bloom's syndrome (BS).","Subunits.comment":"None","Complex.comment":"Interaction between BLM and RAD51L3 is mediated through the N-terminal domain of BLM. RAD51L3-XRCC2 complex stimulates ability of BLM to disrupt Holliday junction structures.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2230,"ComplexName":"PCNA complex","Organism":"Rabbit","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P11387;P11802;P12004;P27694;P38936;Q00535;Q08211","subunits.Entrez.IDs.":"7150;1019;5111;6117;1026;1020;1660","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0071- molecular sieving","GO.ID":"GO:0006260;GO:0007049;GO:0005634","GO.description":"DNA replication;cell cycle;nucleus","FunCat.ID":"10.01.03;10.03;70.10","FunCat.description":"DNA synthesis and replication;cell cycle;nucleus","PubMed.ID":11254741,"subunits.Protein.name.":"DNA topoisomerase 1;Cyclin-dependent kinase 4 ;Proliferating cell nuclear antigen;Replication protein A 70 kDa DNA-binding subunit;Cyclin-dependent kinase inhibitor 1 ;Cyclin-dependent-like kinase 5 ;ATP-dependent RNA helicase A","subunits.Gene.name.":"TOP1;CDK4;PCNA;RPA1;CDKN1A;CDK5;DHX9","subunits.Gene.name.syn.":"None;;None;REPA1 RPA70;CAP20 CDKN1 CIP1 MDA6 PIC1 SDI1 WAF1;CDKN5;DDX9 LKP NDH2","Disease.comment":"None","Subunits.comment":"Since none of the proteins from rabbit were available in the UniProt database at the time of annotation, the orthologous human proteins were used.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2231,"ComplexName":"PCNA homotrimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12004","subunits.Entrez.IDs.":"5111","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0029- cosedimentation through density gradients; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006260;GO:0005634","GO.description":"DNA replication;nucleus","FunCat.ID":"10.01.03;70.10","FunCat.description":"DNA synthesis and replication;nucleus","PubMed.ID":7522248,"subunits.Protein.name.":"Proliferating cell nuclear antigen","subunits.Gene.name.":"PCNA","subunits.Gene.name.syn.":"None","Disease.comment":"PCNA is a target for autoimmunity in systemic lupus erythematosus.","Subunits.comment":"None","Complex.comment":"PCNA exists mainly as homotrimer whose expression increases in the late G1- to S-phase of cell cycle.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":2233,"ComplexName":"Replication-coupled CAF-1-MBD1-ETDB1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q13111;Q15047;Q9UIS9","subunits.Entrez.IDs.":"10036;9869;4152","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0018- two hybrid","GO.ID":"GO:0006260;GO:0006265;GO:0006349;GO:0000084;GO:0018126;GO:0006479;GO:0051276;GO:0005634","GO.description":"DNA replication;DNA topological change;regulation of gene expression by genetic imprinting;mitotic S phase;protein hydroxylation;protein methylation;chromosome organization;nucleus","FunCat.ID":"10.01.03;10.01.09.05;10.01.09.07;10.03.01.01.05;14.07.09;42.10.03;70.10","FunCat.description":"DNA synthesis and replication;DNA conformation modification (e.g. chromatin);DNA imprinting and other epigenetic effects;S phase of mitotic cell cycle;posttranslational modification of amino acids (e.g. hydroxylation, methylation);organization of chromosome structure;nucleus","PubMed.ID":15327775,"subunits.Protein.name.":"Chromatin assembly factor 1 subunit A ;Histone-lysine N-methyltransferase SETDB1;Methyl-CpG-binding domain protein 1","subunits.Gene.name.":"CHAF1A;SETDB1;MBD1","subunits.Gene.name.syn.":"CAF CAF1P150;KIAA0067 KMT1E;CXXC3 PCM1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Formation of CAF-1-MBD1-SETDB1 complex occurs during S phase of cell cycle. This complex facilitates methylation of H3-K9 during replication-coupled chromatin assembly.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2234,"ComplexName":"Chromatin assembly complex (CAF-1 complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q09028;Q13111;Q13112","subunits.Entrez.IDs.":"5928;10036;8208","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006260;GO:0006265;GO:0000084;GO:0051276;GO:0005634","GO.description":"DNA replication;DNA topological change;mitotic S phase;chromosome organization;nucleus","FunCat.ID":"10.01.03;10.01.09.05;10.03.01.01.05;42.10.03;70.10","FunCat.description":"DNA synthesis and replication;DNA conformation modification (e.g. chromatin);S phase of mitotic cell cycle;organization of chromosome structure;nucleus","PubMed.ID":8858152,"subunits.Protein.name.":"Histone-binding protein RBBP4;Chromatin assembly factor 1 subunit A ;Chromatin assembly factor 1 subunit B","subunits.Gene.name.":"RBBP4;CHAF1A;CHAF1B","subunits.Gene.name.syn.":"RBAP48;CAF CAF1P150;CAF1A CAF1P60 MPHOSPH7 MPP7","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Caf-1 complex assembles nucleosomes in a replication-dependent manner.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2235,"ComplexName":"ASF1-interacting protein complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P54198;P68431;Q13111;Q13112;Q9NVP2;Q9Y294","subunits.Entrez.IDs.":"7290;None;10036;8208;55723;25842","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006260;GO:0006265;GO:0051276","GO.description":"DNA replication;DNA topological change;chromosome organization","FunCat.ID":"10.01.03;10.01.09.05;42.10.03","FunCat.description":"DNA synthesis and replication;DNA conformation modification (e.g. chromatin);organization of chromosome structure","PubMed.ID":15664198,"subunits.Protein.name.":"Protein HIRA ;Histone H3.1;Chromatin assembly factor 1 subunit A ;Chromatin assembly factor 1 subunit B ;Histone chaperone ASF1B ;Histone chaperone ASF1A","subunits.Gene.name.":"HIRA;HIST1H3A;;CHAF1A;CHAF1B;ASF1B;ASF1A","subunits.Gene.name.syn.":"DGCR1 HIR TUPLE1;H3FA; H3FL; H3FC; H3FB; H3FD; H3FI; H3FH; H3FK; H3FF; H3FJ;CAF CAF1P150;CAF1A CAF1P60 MPHOSPH7 MPP7;;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Asf1 provides the cells with a buffering system for histone excess generated in response to stalled replication and explains how mammalian cells maintain a critical active histone pool available for deposition during recovery from replication stresses.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2236,"ComplexName":"ASF1-histone containing complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O96017;P49321;P50502;P68431;Q13112;Q9NVP2;Q9Y294","subunits.Entrez.IDs.":"11200;4678;6767;None;8208;55723;25842","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0006260;GO:0006265;GO:0051276","GO.description":"DNA replication;DNA topological change;chromosome organization","FunCat.ID":"10.01.03;10.01.09.05;42.10.03","FunCat.description":"DNA synthesis and replication;DNA conformation modification (e.g. chromatin);organization of chromosome structure","PubMed.ID":15664198,"subunits.Protein.name.":"Serine/threonine-protein kinase Chk2 ;Nuclear autoantigenic sperm protein ;Hsc70-interacting protein ;Histone H3.1;Chromatin assembly factor 1 subunit B ;Histone chaperone ASF1B ;Histone chaperone ASF1A","subunits.Gene.name.":"CHEK2;NASP;ST13;HIST1H3A;;CHAF1B;ASF1B;ASF1A","subunits.Gene.name.syn.":"CDS1 CHK2 RAD53;;AAG2 FAM10A1 HIP SNC6;H3FA; H3FL; H3FC; H3FB; H3FD; H3FI; H3FH; H3FK; H3FF; H3FJ;CAF1A CAF1P60 MPHOSPH7 MPP7;;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Asf1 provides the cells with a buffering system for histone excess generated in response to stalled replication and explains how mammalian cells maintain a critical active histone pool available for deposition during recovery from replication stresses.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2237,"ComplexName":"SP1-MCAF2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P08047;Q5U623","subunits.Entrez.IDs.":"6667;80063","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006265;GO:0006349;GO:0045892;GO:0032774;GO:0051276;GO:0005634","GO.description":"DNA topological change;regulation of gene expression by genetic imprinting;negative regulation of transcription, DNA-templated;RNA biosynthetic process;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;10.01.09.07;11.02.03.04.03;11.02;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);DNA imprinting and other epigenetic effects;transcription repression;RNA synthesis;organization of chromosome structure;nucleus","PubMed.ID":15691849,"subunits.Protein.name.":"Transcription factor Sp1;Activating transcription factor 7-interacting protein 2","subunits.Gene.name.":"SP1;ATF7IP2","subunits.Gene.name.syn.":"TSFP1;MCAF2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"MCAF2 also binds to SETDB1, but more efficiently to SP1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2238,"ComplexName":"MBD1-MCAF1-SETDB1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q15047;Q6VMQ6;Q9UIS9","subunits.Entrez.IDs.":"9869;55729;4152","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006265;GO:0006349;GO:0045892;GO:0032774;GO:0018126;GO:0006479;GO:0051276;GO:0005634","GO.description":"DNA topological change;regulation of gene expression by genetic imprinting;negative regulation of transcription, DNA-templated;RNA biosynthetic process;protein hydroxylation;protein methylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;10.01.09.07;11.02.03.04.03;11.02;14.07.09;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);DNA imprinting and other epigenetic effects;transcription repression;RNA synthesis;posttranslational modification of amino acids (e.g. hydroxylation, methylation);organization of chromosome structure;nucleus","PubMed.ID":15691849,"subunits.Protein.name.":"Histone-lysine N-methyltransferase SETDB1;Activating transcription factor 7-interacting protein 1 ;Methyl-CpG-binding domain protein 1","subunits.Gene.name.":"SETDB1;ATF7IP;MBD1","subunits.Gene.name.syn.":"KIAA0067 KMT1E;MCAF MCAF1;CXXC3 PCM1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"MCAF1 enhances transcriptional repression by MBD1 together with SETDB1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2240,"ComplexName":"Hd-Hap1-Dctn1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P28023;P51111;P54256","subunits.Entrez.IDs.":"29167;29424;29430","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030705;GO:0005737","GO.description":"cytoskeleton-dependent intracellular transport;cytoplasm","FunCat.ID":"20.09.14;70.03","FunCat.description":"cytoskeleton-dependent transport;cytoplasm","PubMed.ID":9454836,"subunits.Protein.name.":"Dynactin subunit 1 ;Huntingtin ;Huntingtin-associated protein 1","subunits.Gene.name.":"Dctn1;Htt;Hap1","subunits.Gene.name.syn.":";Hd Hdh;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This protein complex may take part in dynein-dynactin-associated intracellular transport.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2241,"ComplexName":"HD-RAB8A-OPTN complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P42858;P61006;Q96CV9","subunits.Entrez.IDs.":"3064;4218;10133","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0018- two hybrid","GO.ID":"GO:0016192","GO.description":"vesicle-mediated transport","FunCat.ID":"20.09.07","FunCat.description":"vesicular transport (Golgi network, etc.)","PubMed.ID":11137014,"subunits.Protein.name.":"Huntingtin ;Ras-related protein Rab-8A ;Optineurin","subunits.Gene.name.":"HTT;RAB8A;OPTN","subunits.Gene.name.syn.":"HD IT15;MEL RAB8;FIP2 GLC1E HIP7 HYPL NRP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex probably involved in membrane trafficking and cellular morphogenesis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2242,"ComplexName":"TGM2-HD-CALM1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P21980;P42858;P62158","subunits.Entrez.IDs.":"7052;3064;None","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006461","GO.description":"protein complex assembly","FunCat.ID":"14.1","FunCat.description":"assembly of protein complexes","PubMed.ID":14985437,"subunits.Protein.name.":"Protein-glutamine gamma-glutamyltransferase 2 ;Huntingtin ;Calmodulin","subunits.Gene.name.":"TGM2;HTT;CALM1; CAL","subunits.Gene.name.syn.":";HD IT15;CALM, CAM, CAM1, CAM2, CAMB, CALML2, CAM3, CAMC, CAMIII","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Inhibiting the interaction of calmodulin with transglutaminase and huntingtin protein could decrease cross-linking and diminish huntingtin aggregate formation in the HD brain.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2243,"ComplexName":"TGM2-HD complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P21980;P42858","subunits.Entrez.IDs.":"7052;3064","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006461","GO.description":"protein complex assembly","FunCat.ID":"14.1","FunCat.description":"assembly of protein complexes","PubMed.ID":11442349,"subunits.Protein.name.":"Protein-glutamine gamma-glutamyltransferase 2 ;Huntingtin","subunits.Gene.name.":"TGM2;HTT","subunits.Gene.name.syn.":";HD IT15","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2247,"ComplexName":"Dynactin complex (DCTN1, DCTN2, DCTN3, DCTN4, DCTN6, CAPZA1, CAPZB, ACTR1A)","Organism":"Bovine","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"O00399;O75935;P47756;P52907;P61163;Q13561;Q14203;Q9UJW0","subunits.Entrez.IDs.":"10671;11258;832;829;10121;10540;1639;51164","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies;MI:0029- cosedimentation through density gradients","GO.ID":"GO:0030705","GO.description":"cytoskeleton-dependent intracellular transport","FunCat.ID":"20.09.14","FunCat.description":"cytoskeleton-dependent transport","PubMed.ID":10074429,"subunits.Protein.name.":"Dynactin subunit 6 ;Dynactin subunit 3 ;F-actin-capping protein subunit beta;F-actin-capping protein subunit alpha-1;Alpha-centractin ;Dynactin subunit 2 ;Dynactin subunit 1;Dynactin subunit 4","subunits.Gene.name.":"DCTN6;DCTN3;CAPZB;CAPZA1;ACTR1A;DCTN2;DCTN1;DCTN4","subunits.Gene.name.syn.":"WS3;DCTN22;CAPB, CAPPB, CAPZ;CAPPA1, CAPZ, CAZ1;CTRN1;DCTN50;None;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2254,"ComplexName":"CTGF/Hcs24-actin(beta/gamma) complex","Organism":"Human","Synonyms":"None","Cell.line":"HCS-2/8 cells","subunits.UniProt.IDs.":"P29279;P60709;P63261","subunits.Entrez.IDs.":"1490;60;71","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0004-affinity chromatography technologies","GO.ID":"GO:0030037;GO:0030036;GO:0051216;GO:0005737","GO.description":"actin filament reorganization involved in cell cycle;actin cytoskeleton organization;cartilage development;cytoplasm","FunCat.ID":"10.03.05.03;42.04.03;45.03.05.05;70.03","FunCat.description":"cell cycle dependent actin filament reorganization;actin cytoskeleton;cartilage;cytoplasm","PubMed.ID":12470643,"subunits.Protein.name.":"Connective tissue growth factor;Actin, cytoplasmic 1;Actin, cytoplasmic 2","subunits.Gene.name.":"CTGF;ACTB;ACTG1","subunits.Gene.name.syn.":"CCN2 HCS24 IGFBP8;None;ACTG","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors suggest that binding of CTGF/Hcs24 to actin in chondrocytes may play some important roles in the regulation of cytoskeletal organization and of the cell cycle.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2255,"ComplexName":"Cofilin-actin-CAP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P23528;P60709;Q01518","subunits.Entrez.IDs.":"1072;60;10487","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006928;GO:0030036;GO:0015629","GO.description":"movement of cell or subcellular component;actin cytoskeleton organization;actin cytoskeleton","FunCat.ID":"34.05;42.04.03;70.04.03","FunCat.description":"cell motility;actin cytoskeleton;actin cytoskeleton","PubMed.ID":11950878,"subunits.Protein.name.":"Cofilin-1 ;Actin, cytoplasmic 1;Adenylyl cyclase-associated protein 1","subunits.Gene.name.":"CFL1;ACTB;CAP1","subunits.Gene.name.syn.":"CFL;None;CAP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"As well as full-length CAP1, both CAP1-NT and CAP1-CT enhanced cofilin-induced acceleration of F-actin turnover, whereas their effect was only marginally visible in the absence of cofilin. Localization experiments in fibroblasts demonstrated that CAP1-NT is primarily responsible for accumulating CAP1 with cofilin and actin in dynamic peripheral regions of spreading cells.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2256,"ComplexName":"RIAM-Rap1-GTP complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62834;Q7Z5R6","subunits.Entrez.IDs.":"5906;54518","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0007155;GO:0030036;GO:0005886","GO.description":"cell adhesion;actin cytoskeleton organization;plasma membrane","FunCat.ID":"34.07;42.04.03;70.02","FunCat.description":"cell adhesion;actin cytoskeleton;eukaryotic plasma membrane / membrane attached","PubMed.ID":15469846,"subunits.Protein.name.":"Ras-related protein Rap-1A;Amyloid beta A4 precursor protein-binding family B member 1-interacting protein","subunits.Gene.name.":"RAP1A;APBB1IP","subunits.Gene.name.syn.":"KREV1;PREL1 RARP1 RIAM","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"RIAM preferentially interacted with Rap1-GTP compared to Ras-GTP. The results indicate that RIAM is required for localization of Rap1-GTP at the plasma membrane.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2258,"ComplexName":"VILIP-1-AChR-alpha-4-AChR-beta-2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P17787;P43681;P62760","subunits.Entrez.IDs.":"1141;1137;7447","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0005509;GO:0050789;GO:0005216;GO:0007268","GO.description":"calcium ion binding;regulation of biological process;ion channel activity;synaptic transmission","FunCat.ID":"16.17.01;18;20.03.01.01;34.03.01","FunCat.description":"calcium binding;REGULATION OF METABOLISM AND PROTEIN FUNCTION;ion channels;synaptic transmission","PubMed.ID":12202488,"subunits.Protein.name.":"Neuronal acetylcholine receptor subunit beta-2;Neuronal acetylcholine receptor subunit alpha-4;Visinin-like protein 1","subunits.Gene.name.":"CHRNB2;CHRNA4;VSNL1","subunits.Gene.name.syn.":";NACRA4;VISL1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results suggest a rule for VILIP-1 as an AChR-associated protein that modulates the surface expression levels and functional properties of alpha 4beta 2 AChRs in response to changes in the intracellular levels of calcium.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2261,"ComplexName":"GluR6a-GluR6b heterodimer complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"P39087","subunits.Entrez.IDs.":"14806","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0007268;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;synaptic transmission;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;34.03.01;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;synaptic transmission;eukaryotic plasma membrane / membrane attached","PubMed.ID":16102538,"subunits.Protein.name.":"Glutamate receptor ionotropic, kainate 2","subunits.Gene.name.":"Grik2","subunits.Gene.name.syn.":"Glur6","Disease.comment":"None","Subunits.comment":"The authors show that the two splice variants of the GluR6 subunit, GluR6a and GluR6b, which differ in their C-terminal domains, do not show distinct functional properties, but coassemble as heteromers in vitro and in vivo.","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse)"}
{"ComplexID":2266,"ComplexName":"PPP3CA-PPP3CA-RCAN1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P16298;P53805;Q08209","subunits.Entrez.IDs.":"5532;1827;5530","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0019722","GO.description":"calcium-mediated signaling","FunCat.ID":"30.01.09.03","FunCat.description":"Ca2+ mediated signal transduction","PubMed.ID":12809556,"subunits.Protein.name.":"Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform ;Calcipressin-1 ;Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform","subunits.Gene.name.":"PPP3CB;RCAN1;PPP3CA","subunits.Gene.name.syn.":"CALNA2 CALNB CNA2;ADAPT78 CSP1 DSC1 DSCR1;CALNA CNA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2267,"ComplexName":"Pick1 homodimer complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q9EP80","subunits.Entrez.IDs.":"84591","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006461","GO.description":"protein complex assembly","FunCat.ID":"14.1","FunCat.description":"assembly of protein complexes","PubMed.ID":11466413,"subunits.Protein.name.":"PRKCA-binding protein","subunits.Gene.name.":"Pick1","subunits.Gene.name.syn.":"Prkcabp","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors conclude that PICK1 dimerizes or multimerizes via the coiled coil region or the C-terminal neighboring sequences.","SWISSPROT.organism":"Rattus norvegicus (Rat)"}
{"ComplexID":2268,"ComplexName":"Pick1-Glur2-Pkca complex, TPA (tissue plasminogen activator) treated","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P05696;P19491;Q9EP80","subunits.Entrez.IDs.":"24680;29627;84591","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0007268;GO:0005886","GO.description":"intracellular protein transport;protein targeting;protein transport;synaptic transmission;plasma membrane","FunCat.ID":"14.04;20.01.10;34.03.01;70.02","FunCat.description":"protein targeting, sorting and translocation;protein transport;synaptic transmission;eukaryotic plasma membrane / membrane attached","PubMed.ID":11466413,"subunits.Protein.name.":"Protein kinase C alpha type;Glutamate receptor 2;PRKCA-binding protein","subunits.Gene.name.":"Prkca;Gria2;Pick1","subunits.Gene.name.syn.":"Pkca;Glur2;Prkcabp","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The experiment demonstrates that a heterocomplex, in which a PICK1 dimer or higher multimer is linked simultaneously to the C termini of PKC-alpha  and GluR2, forms by a phorbol ester and PDZ-dependent mechanism. Such a complex could target the activated form of PKC-alpha  to GluR2. Ser880 of GluR2 is a substrate for PKC. To determine whether PICK1 clusters contain GluR2 that has been phosphorylated by PKC, the authors assayed the clusters for GluR2Ser880-PO4 by using an affinity-purified phosphopeptide antiserum. Western blot analysis revealed that TPA (tissue plasminogen activator)  induced a strong increase of GluR2Ser880-PO4 present in protein extracts from neurons, confirming the PKC phosphorylation of GluR2 in vivo.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2270,"ComplexName":"Hippocalcin-beta2-adaptin-Glur2 complex, Ca(2+) dependent","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P19491;P62944;P84076","subunits.Entrez.IDs.":"29627;140670;29177","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005509;GO:0006897;GO:0007268;GO:0005886","GO.description":"calcium ion binding;endocytosis;synaptic transmission;plasma membrane","FunCat.ID":"16.17.01;20.09.18.09.01;34.03.01;70.02","FunCat.description":"calcium binding;endocytosis;synaptic transmission;eukaryotic plasma membrane / membrane attached","PubMed.ID":16102532,"subunits.Protein.name.":"Glutamate receptor 2;AP-2 complex subunit beta ;Neuron-specific calcium-binding protein hippocalcin","subunits.Gene.name.":"Gria2;Ap2b1;Hpca","subunits.Gene.name.syn.":"Glur2;Clapb1;","Disease.comment":"None","Subunits.comment":"The authors state that beta2-adaptin is part of AP2 complex, described in PMID:12086608.","Complex.comment":"The authors describe that in neurons the hippocalcin-AP2 complex binds TfR in a Ca(2+)-independent manner, whereas the complex only binds to AMPARs, like Glur2 in the presence of Ca(2+). Since there is no direct interaction between hippocalcin and GluR2/3, the data indicate that hippocalcin complexes with AMPARs via its interaction with AP2. Hippocalcin binds the beta-2-adaptin subunit of the AP2 adaptor complex.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2271,"ComplexName":"Grip-Glur2/3-liprin-alpha-Lar complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P19491;P19492;P97879;Q64604;Q91Z80","subunits.Entrez.IDs.":"29627;29628;84016;360406;140592","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation;MI:0030-cross-linking studies","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0005886;GO:0007416","GO.description":"intracellular protein transport;protein targeting;protein transport;plasma membrane;synapse assembly","FunCat.ID":"14.04;20.01.10;70.02;41.05.13.01","FunCat.description":"protein targeting, sorting and translocation;protein transport;eukaryotic plasma membrane / membrane attached;synaptogenesis","PubMed.ID":11931740,"subunits.Protein.name.":"Glutamate receptor 2;Glutamate receptor 3;Glutamate receptor-interacting protein 1;Receptor-type tyrosine-protein phosphatase F;Liprin-alpha-4","subunits.Gene.name.":"Gria2;Gria3;Grip1;Ptprf;Ppfia4","subunits.Gene.name.syn.":"Glur2;Glur3;None;Lar;None","Disease.comment":"None","Subunits.comment":"Since the authors did not specify glutamate receptor-interacting protein, we used isoform Grip1.","Complex.comment":"The authors showed that Liprin-alpha and LAR-RPTPs are enriched at synaptic sites, and interfering with the GRIP-liprin-alpha interaction disrupts the synaptic targeting of AMPA receptors.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2272,"ComplexName":"PICK1-GRIP1-GLUR2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P42262;Q9NRD5;Q9Y3R0","subunits.Entrez.IDs.":"2891;9463;23426","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0006897;GO:0005886","GO.description":"intracellular protein transport;protein targeting;protein transport;endocytosis;plasma membrane","FunCat.ID":"14.04;20.01.10;20.09.18.09.01;70.02","FunCat.description":"protein targeting, sorting and translocation;protein transport;endocytosis;eukaryotic plasma membrane / membrane attached","PubMed.ID":16055064,"subunits.Protein.name.":"Glutamate receptor 2 ;PRKCA-binding protein ;Glutamate receptor-interacting protein 1","subunits.Gene.name.":"GRIA2;PICK1;GRIP1","subunits.Gene.name.syn.":"GLUR2;PRKCABP;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex analysed both in vitro and in vivo. This triple complex may function in the presentation of PKC-PICK1 complexes to the ABP/GRIP-GluR2 complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2273,"ComplexName":"Nsg1-Glur2-Grip1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P02683;P19491;P97879","subunits.Entrez.IDs.":"25247;29627;84016","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0096- pull down","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0006897;GO:0005886","GO.description":"intracellular protein transport;protein targeting;protein transport;endocytosis;plasma membrane","FunCat.ID":"14.04;20.01.10;20.09.18.09.01;70.02","FunCat.description":"protein targeting, sorting and translocation;protein transport;endocytosis;eukaryotic plasma membrane / membrane attached","PubMed.ID":16037816,"subunits.Protein.name.":"Neuron-specific protein family member 1 ;Glutamate receptor 2;Glutamate receptor-interacting protein 1","subunits.Gene.name.":"Nsg1;Gria2;Grip1","subunits.Gene.name.syn.":"Bsmrb;Glur2;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results indicate that NEEP21-RIP1 binding is crucial for GluR2-AMPAR sorting through endosomes and their recruitment to the plasma membrane.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2274,"ComplexName":"Beta-catenin-Cadherin-Grip-liprin-alpha-GluR2/3 complex","Organism":"Rat","Synonyms":"None","Cell.line":"cerebral cortex","subunits.UniProt.IDs.":"P19491;P19492;P97879;Q91Z79;Q9WU82;Q9Z1Y3","subunits.Entrez.IDs.":"29627;29628;84016;140591;84353;83501","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0007416","GO.description":"intracellular protein transport;protein targeting;protein transport;synapse assembly","FunCat.ID":"14.04;20.01.10;41.05.13.01","FunCat.description":"protein targeting, sorting and translocation;protein transport;synaptogenesis","PubMed.ID":15750591,"subunits.Protein.name.":"Glutamate receptor 2;Glutamate receptor 3;Glutamate receptor-interacting protein 1;Liprin-alpha-3;Catenin beta-1;Cadherin-2","subunits.Gene.name.":"Gria2;Gria3;Grip1;Ppfia3;Ctnnb1;Cdh2","subunits.Gene.name.syn.":"Glur2;Glur3;None;None;Catnb;None","Disease.comment":"None","Subunits.comment":"Since the authors did not specify liprin-alpha  as well as Grip , we used isoform Ppfia3 and isoform Grip1, respectively.","Complex.comment":"The authors suggest that LAR-RPTPs (Leukocyte common antigen-related (LAR) family receptor protein tyrosine phosphatases) contribute to synapse morphogenesis by regulating the synaptic delivery of a protein complex that is scaffolded by GRIP and liprin-alpha and that includes AMPA receptors and cadherin-beta-catenin.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2275,"ComplexName":"GluR receptor complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P19490;P19491;P19492;P19493","subunits.Entrez.IDs.":"50592;29627;29628;29629","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0071- molecular sieving","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0007215;GO:0007268;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;glutamate receptor signaling pathway;synaptic transmission;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;30.05.02.24.05;34.03.01;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;glutamate signalling pathway;synaptic transmission;eukaryotic plasma membrane / membrane attached","PubMed.ID":1309749,"subunits.Protein.name.":"Glutamate receptor 1;Glutamate receptor 2;Glutamate receptor 3;Glutamate receptor 4","subunits.Gene.name.":"Gria1;Gria2;Gria3;Gria4","subunits.Gene.name.syn.":"Glur1;Glur2;Glur3;Glur4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Immunolabeling done from detergent solubilized rat brain membranes.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2276,"ComplexName":"GluR1 homomer complex","Organism":"Rat","Synonyms":"None","Cell.line":"hippocampal neurons","subunits.UniProt.IDs.":"P19490","subunits.Entrez.IDs.":"50592","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0007268;GO:0007611","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;synaptic transmission;learning or memory","FunCat.ID":"20.01.01.01;20.03.01.01;34.03.01;36.25.03.04.01","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;synaptic transmission;learning and memory","PubMed.ID":15924137,"subunits.Protein.name.":"Glutamate receptor 1","subunits.Gene.name.":"Gria1","subunits.Gene.name.syn.":"Glur1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ser831 phosphorylation of GluR1 by CaMKII enhances the single-channel conductance of GluR1 homomers, and this tightly correlates with the increased channel conductance of synaptic AMPARs during LTP (long-term potentiation).","SWISSPROT.organism":"Rattus norvegicus (Rat)"}
{"ComplexID":2277,"ComplexName":"D2 receptor-GluR2-GluR1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P19490;P19491;P61169","subunits.Entrez.IDs.":"50592;29627;24318","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation;MI:0096- pull down","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0008324;GO:0006812;GO:0005216;GO:0007212;GO:0007268","GO.description":"intracellular protein transport;protein targeting;protein transport;cation transmembrane transporter activity;cation transport;ion channel activity;dopamine receptor signaling pathway;synaptic transmission","FunCat.ID":"14.04;20.01.10;20.01.01.01;20.03.01.01;30.05.02.24.03;34.03.01","FunCat.description":"protein targeting, sorting and translocation;protein transport;cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;dopamine receptor signalling pathway;synaptic transmission","PubMed.ID":15858065,"subunits.Protein.name.":"Glutamate receptor 1;Glutamate receptor 2;D","subunits.Gene.name.":"Gria1;Gria2;Drd2","subunits.Gene.name.syn.":"Glur1;Glur2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors show that D2 receptors interact with the GluR1 subunit only in the presence of the GluR2 subunit, indicating that GluR2 subunit is responsible for D2-AMPA receptor complex formation. In further experiments they show that D2 receptors interact with GluR2 subunit through NSF.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2281,"ComplexName":"Protein kinase A II alpha homodimer complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12367","subunits.Entrez.IDs.":"19087","Protein.complex.purification.method":"MI:0077- nuclear magnetic resonance","GO.ID":"GO:0035556;GO:0019933","GO.description":"intracellular signal transduction;cAMP-mediated signaling","FunCat.ID":"30.01;30.01.09.07","FunCat.description":"cellular signalling;cAMP/cGMP mediated signal transduction","PubMed.ID":11985580,"subunits.Protein.name.":"cAMP-dependent protein kinase type II-alpha regulatory subunit","subunits.Gene.name.":"Prkar2a","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse)"}
{"ComplexID":2294,"ComplexName":"ABI1-WASF2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q8IZP0;Q9Y6W5","subunits.Entrez.IDs.":"10006;10163","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030036","GO.description":"actin cytoskeleton organization","FunCat.ID":"42.04.03","FunCat.description":"actin cytoskeleton","PubMed.ID":16155590,"subunits.Protein.name.":"Abl interactor 1;Wiskott-Aldrich syndrome protein family member 2","subunits.Gene.name.":"ABI1;WASF2","subunits.Gene.name.syn.":"SSH3BP1;WAVE2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2296,"ComplexName":"Abi1-Wasl complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q8CBW3;Q91YD9","subunits.Entrez.IDs.":"11308;73178","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030036","GO.description":"actin cytoskeleton organization","FunCat.ID":"42.04.03","FunCat.description":"actin cytoskeleton","PubMed.ID":16155590,"subunits.Protein.name.":"Abl interactor 1;Neural Wiskott-Aldrich syndrome protein","subunits.Gene.name.":"Abi1;Wasl","subunits.Gene.name.syn.":"Ssh3bp1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2297,"ComplexName":"ABI1-WASL complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00401;Q8IZP0","subunits.Entrez.IDs.":"8976;10006","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0030036","GO.description":"actin cytoskeleton organization","FunCat.ID":"42.04.03","FunCat.description":"actin cytoskeleton","PubMed.ID":16155590,"subunits.Protein.name.":"Neural Wiskott-Aldrich syndrome protein ;Abl interactor 1","subunits.Gene.name.":"WASL;ABI1","subunits.Gene.name.syn.":";SSH3BP1","Disease.comment":"Neural Wiskott-Aldrich syndrome","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2300,"ComplexName":"Profilin 2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75116;P11142;P17600;P35080;P60709;Q05193;Q7L576;Q92777;Q9Y2A7","subunits.Entrez.IDs.":"9475;3312;6853;5217;60;1759;23191;6854;10787","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006461;GO:0006897;GO:0030036","GO.description":"protein complex assembly;endocytosis;actin cytoskeleton organization","FunCat.ID":"14.10;20.09.18.09.01;42.04.03","FunCat.description":"assembly of protein complexes;endocytosis;actin cytoskeleton","PubMed.ID":9463375,"subunits.Protein.name.":"Rho-associated protein kinase 2 ;Heat shock cognate 71 kDa protein;Synapsin-1 ;Profilin-2 ;Actin, cytoplasmic 1;Dynamin-1 ;Cytoplasmic FMR1-interacting protein 1;Synapsin-2 ;Nck-associated protein 1","subunits.Gene.name.":"ROCK2;HSPA8;SYN1;PFN2;ACTB;DNM1;CYFIP1;SYN2;NCKAP1","subunits.Gene.name.syn.":"KIAA0619;HSC70, HSP73, HSPA10;;;None;DNM;KIAA0068;;HEM2 KIAA0587 NAP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2307,"ComplexName":"AP3D1-AP3S2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14617;P59780","subunits.Entrez.IDs.":"8943;10239","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006886;GO:0006605;GO:0015031","GO.description":"intracellular protein transport;protein targeting;protein transport","FunCat.ID":"14.04;20.01.10","FunCat.description":"protein targeting, sorting and translocation;protein transport","PubMed.ID":15469849,"subunits.Protein.name.":"AP-3 complex subunit delta-1;AP-3 complex subunit sigma-2","subunits.Gene.name.":"AP3D1;AP3S2","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2308,"ComplexName":"AP3D1-AP3S1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14617;Q92572","subunits.Entrez.IDs.":"8943;1176","Protein.complex.purification.method":"MI:0018- two hybrid; MI:0004- affinity chromatography technologies","GO.ID":"GO:0006886;GO:0006605;GO:0015031","GO.description":"intracellular protein transport;protein targeting;protein transport","FunCat.ID":"14.04;20.01.10","FunCat.description":"protein targeting, sorting and translocation;protein transport","PubMed.ID":15469849,"subunits.Protein.name.":"AP-3 complex subunit delta-1;AP-3 complex subunit sigma-1","subunits.Gene.name.":"AP3D1;AP3S1","subunits.Gene.name.syn.":"None;CLAPS3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2318,"ComplexName":"ITGA6-ITGB4-Laminin10/12 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"O15230;P07942;P11047;P16144;P23229","subunits.Entrez.IDs.":"3911;3912;3915;3691;3655","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0007155","GO.description":"cell adhesion","FunCat.ID":"34.07","FunCat.description":"cell adhesion","PubMed.ID":10671376,"subunits.Protein.name.":"Laminin subunit alpha-5;Laminin subunit beta-1 ;Laminin subunit gamma-1 ;Integrin beta-4;Integrin alpha-6","subunits.Gene.name.":"LAMA5;LAMB1;LAMC1;ITGB4;ITGA6","subunits.Gene.name.syn.":"KIAA0533 KIAA1907;;LAMB2;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2319,"ComplexName":"ITGA6-ITGB4-Laminin10/12 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"O15230;P11047;P16144;P23229;P55268","subunits.Entrez.IDs.":"3911;3915;3691;3655;3913","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0007155","GO.description":"cell adhesion","FunCat.ID":"34.07","FunCat.description":"cell adhesion","PubMed.ID":10671376,"subunits.Protein.name.":"Laminin subunit alpha-5;Laminin subunit gamma-1 ;Integrin beta-4;Integrin alpha-6;Laminin subunit beta-2","subunits.Gene.name.":"LAMA5;LAMC1;ITGB4;ITGA6;LAMB2","subunits.Gene.name.syn.":"KIAA0533 KIAA1907;LAMB2;None;None;LAMS","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2320,"ComplexName":"ITGA6-ITGB4-CD151 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"skin","subunits.UniProt.IDs.":"P16144;P23229;P48509","subunits.Entrez.IDs.":"3691;3655;977","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005515;GO:0007160","GO.description":"protein binding;cell-matrix adhesion","FunCat.ID":"16.01;34.07.02","FunCat.description":"protein binding;cell-matrix adhesion","PubMed.ID":10811835,"subunits.Protein.name.":"Integrin beta-4;Integrin alpha-6;CD151 antigen","subunits.Gene.name.":"ITGB4;ITGA6;CD151","subunits.Gene.name.syn.":"None;None;TSPAN24","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The recruitment of Cd151 into hemidesmosomes is regulated by the integrin alpha6beta4.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2321,"ComplexName":"ITGA6-ITGB4-FYN complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"skin","subunits.UniProt.IDs.":"P06241;P16144;P23229","subunits.Entrez.IDs.":"2534;3691;3655","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005515;GO:0006921","GO.description":"protein binding;cellular component disassembly involved in execution phase of apoptosis","FunCat.ID":"16.01;40.10.02.02.03","FunCat.description":"protein binding;disassembly of cell structures","PubMed.ID":11684709,"subunits.Protein.name.":"Tyrosine-protein kinase Fyn;Integrin beta-4;Integrin alpha-6","subunits.Gene.name.":"FYN;ITGB4;ITGA6","subunits.Gene.name.syn.":"None;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"EGF-R with  ITGA6-ITGB4 and, through the tyrosine kinase Fyn, induces phosphorylation of the beta4 tail (ITGB4) and disruption of hemidesmosomes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2322,"ComplexName":"ITGA6-ITGB4-LAMA5 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"epithelium, skin","subunits.UniProt.IDs.":"O15230;P16144;P23229","subunits.Entrez.IDs.":"3911;3691;3655","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007155","GO.description":"cell adhesion","FunCat.ID":"34.07","FunCat.description":"cell adhesion","PubMed.ID":7556090,"subunits.Protein.name.":"Laminin subunit alpha-5;Integrin beta-4;Integrin alpha-6","subunits.Gene.name.":"LAMA5;ITGB4;ITGA6","subunits.Gene.name.syn.":"KIAA0533 KIAA1907;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2323,"ComplexName":"ITGA6-ITGB4 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"skin","subunits.UniProt.IDs.":"P16144;P23229","subunits.Entrez.IDs.":"3691;3655","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0030-cross-linking studies","GO.ID":"GO:0023052;GO:0006928","GO.description":"signaling;movement of cell or subcellular component","FunCat.ID":"30.01;34.05","FunCat.description":"cellular signalling;cell motility","PubMed.ID":2649503,"subunits.Protein.name.":"Integrin beta-4;Integrin alpha-6","subunits.Gene.name.":"ITGB4;ITGA6","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2342,"ComplexName":"ITGAV-ITGB8-MMP14-TGFB1 complex","Organism":"Human","Synonyms":"None","Cell.line":"epithelium, nervous tissue","subunits.UniProt.IDs.":"P01137;P06756;P26012;P50281","subunits.Entrez.IDs.":"7040;3685;3696;4323","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies;MI:0019-coimmunoprecipitation","GO.ID":"GO:0051098;GO:0005515;GO:0050789;GO:0005886","GO.description":"regulation of binding;protein binding;regulation of biological process;plasma membrane","FunCat.ID":"18.01.07;16.01;18;70.02","FunCat.description":"regulation by binding / dissociation;protein binding;REGULATION OF METABOLISM AND PROTEIN FUNCTION;eukaryotic plasma membrane / membrane attached","PubMed.ID":11970960,"subunits.Protein.name.":"Transforming growth factor beta-1;Integrin alpha-V;Integrin beta-8;Matrix metalloproteinase-14","subunits.Gene.name.":"TGFB1;ITGAV;ITGB8;MMP14","subunits.Gene.name.syn.":"TGFB;MSK8 VNRA;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SLC binds to alphav-beta8, an integrin expressed by normal epithelial and neuronal cells in vivo. This binding results in the membrane type 1 (MT1)-MMP-dependent release of active TGF-beta, which leads to autocrine and paracrine effects on cell growth and matrix production.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2343,"ComplexName":"ITGAV-ITGB5-PLAUR complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P06756;P18084;Q03405","subunits.Entrez.IDs.":"3685;3693;5329","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016477","GO.description":"cell migration","FunCat.ID":"34.05.01","FunCat.description":"cell migration","PubMed.ID":10537314,"subunits.Protein.name.":"Integrin alpha-V;Integrin beta-5;Urokinase plasminogen activator surface receptor","subunits.Gene.name.":"ITGAV;ITGB5;PLAUR","subunits.Gene.name.syn.":"MSK8 VNRA;;MO3 UPAR","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"uPAR association with alpha(v)beta5 leads to a functional interaction of these receptors and suggests that uPAR directs cytoskeletal rearrangements and cell migration by altering alpha(v)beta5 signaling specificity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2345,"ComplexName":"ITGAV-ITGB5-ICAM4 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P06756;P18084;Q14773","subunits.Entrez.IDs.":"3685;3693;3386","Protein.complex.purification.method":"MI:0401- biochemical","GO.ID":"GO:0005515;GO:0007155","GO.description":"protein binding;cell adhesion","FunCat.ID":"16.01;34.07","FunCat.description":"protein binding;cell adhesion","PubMed.ID":11435317,"subunits.Protein.name.":"Integrin alpha-V;Integrin beta-5;Intercellular adhesion molecule 4","subunits.Gene.name.":"ITGAV;ITGB5;ICAM4","subunits.Gene.name.syn.":"MSK8 VNRA;;LW","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2346,"ComplexName":"ITGAV-ITGB5-ADAM9 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P06756;P18084;Q13443","subunits.Entrez.IDs.":"3685;3693;8754","Protein.complex.purification.method":"MI:0054- fluorescence-activated cell sorting","GO.ID":"GO:0005515;GO:0007155","GO.description":"protein binding;cell adhesion","FunCat.ID":"16.01;34.07","FunCat.description":"protein binding;cell adhesion","PubMed.ID":11162558,"subunits.Protein.name.":"Integrin alpha-V;Integrin beta-5;Disintegrin and metalloproteinase domain-containing protein 9","subunits.Gene.name.":"ITGAV;ITGB5;ADAM9","subunits.Gene.name.syn.":"MSK8 VNRA;;KIAA0021 MCMP MDC9 MLTNG","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"MDC-9 interacts with alpha(v)beta(5) in an RGD-independent manner.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2347,"ComplexName":"ITGAV-ITGB5-SPP1 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P06756;P10451;P18084","subunits.Entrez.IDs.":"3685;6696;3693","Protein.complex.purification.method":"MI:0110- text mining","GO.ID":"GO:0005515;GO:0007155","GO.description":"protein binding;cell adhesion","FunCat.ID":"16.01;34.07","FunCat.description":"protein binding;cell adhesion","PubMed.ID":16005200,"subunits.Protein.name.":"Integrin alpha-V;Osteopontin ;Integrin beta-5","subunits.Gene.name.":"ITGAV;SPP1;ITGB5","subunits.Gene.name.syn.":"MSK8 VNRA;BNSP OPN;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2348,"ComplexName":"ITGAV-ITGB5-CYR61 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"O00622;P06756;P18084","subunits.Entrez.IDs.":"3491;3685;3693","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0005515;GO:0051098;GO:0016477;GO:0007155","GO.description":"protein binding;regulation of binding;cell migration;cell adhesion","FunCat.ID":"16.01;18.01.07;34.05.01;34.07","FunCat.description":"protein binding;regulation by binding / dissociation;cell migration;cell adhesion","PubMed.ID":11287419,"subunits.Protein.name.":"Protein CYR61 ;Integrin alpha-V;Integrin beta-5","subunits.Gene.name.":"CYR61;ITGAV;ITGB5","subunits.Gene.name.syn.":"CCN1 GIG1 IGFBP10;MSK8 VNRA;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"CYR61-dependent chemotaxis is mediated through integrin alpha(v)beta5.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2350,"ComplexName":"ITGAV-ITGB5 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06756;P18084","subunits.Entrez.IDs.":"3685;3693","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0005515;GO:0007155","GO.description":"protein binding;cell adhesion","FunCat.ID":"16.01;34.07","FunCat.description":"protein binding;cell adhesion","PubMed.ID":1694173,"subunits.Protein.name.":"Integrin alpha-V;Integrin beta-5","subunits.Gene.name.":"ITGAV;ITGB5","subunits.Gene.name.syn.":"MSK8 VNRA;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2351,"ComplexName":"ITGB6-FYN-FN1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P02751;P06241;P18564","subunits.Entrez.IDs.":"2335;2534;3694","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0051098;GO:0005515;GO:0035556;GO:0023052","GO.description":"regulation of binding;protein binding;intracellular signal transduction;signaling","FunCat.ID":"18.01.07;16.01;30.01","FunCat.description":"regulation by binding / dissociation;protein binding;cellular signalling","PubMed.ID":12917446,"subunits.Protein.name.":"Fibronectin ;Tyrosine-protein kinase Fyn;Integrin beta-6","subunits.Gene.name.":"FN1;FYN;ITGB6","subunits.Gene.name.syn.":"FN;None;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Integrin beta6 signaling activates Fyn and thus promotes oral cancer progression.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2352,"ComplexName":"ITGAV-ITGB6-SPP1 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P06756;P10451;P18564","subunits.Entrez.IDs.":"3685;6696;3694","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0005515;GO:0007155","GO.description":"protein binding;cell adhesion","FunCat.ID":"16.01;34.07","FunCat.description":"protein binding;cell adhesion","PubMed.ID":16005200,"subunits.Protein.name.":"Integrin alpha-V;Osteopontin ;Integrin beta-6","subunits.Gene.name.":"ITGAV;SPP1;ITGB6","subunits.Gene.name.syn.":"MSK8 VNRA;BNSP OPN;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2353,"ComplexName":"ITGAV-ITGB6-TGFB3 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P06756;P10600;P18564","subunits.Entrez.IDs.":"3685;7043;3694","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0005515;GO:0051098","GO.description":"protein binding;regulation of binding","FunCat.ID":"16.01;18.01.07","FunCat.description":"protein binding;regulation by binding / dissociation","PubMed.ID":11821050,"subunits.Protein.name.":"Integrin alpha-V;Transforming growth factor beta-3 ;Integrin beta-6","subunits.Gene.name.":"ITGAV;TGFB3;ITGB6","subunits.Gene.name.syn.":"MSK8 VNRA;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2354,"ComplexName":"ITGAV-ITGB6 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06756;P18564","subunits.Entrez.IDs.":"3685;3694","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515","GO.description":"protein binding","FunCat.ID":"16.01","FunCat.description":"protein binding","PubMed.ID":8798654,"subunits.Protein.name.":"Integrin alpha-V;Integrin beta-6","subunits.Gene.name.":"ITGAV;ITGB6","subunits.Gene.name.syn.":"MSK8 VNRA;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cells expressing alpha(v)beta6 attach, but less avidly, do not spread, and completely fail to proliferate.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2355,"ComplexName":"ITGAV-ITGB3-CD47-FCER2 complex","Organism":"Human","Synonyms":"None","Cell.line":"blood cell","subunits.UniProt.IDs.":"P05106;P06734;P06756;Q08722","subunits.Entrez.IDs.":"3690;2208;3685;961","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies;MI:0019-coimmunoprecipitation","GO.ID":"GO:0005515;GO:0006954","GO.description":"protein binding;inflammatory response","FunCat.ID":"16.01;36.25.16.07","FunCat.description":"protein binding;inflammatory response","PubMed.ID":10037797,"subunits.Protein.name.":"Integrin beta-3;Low affinity immunoglobulin epsilon Fc receptor;Integrin alpha-V;Leukocyte surface antigen CD47","subunits.Gene.name.":"ITGB3;FCER2;ITGAV;CD47","subunits.Gene.name.syn.":"GP3A;CD23A CLEC4J FCE2 IGEBF;MSK8 VNRA;MER6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Alpha(v)beta3-CD47 mediates proinflammatory cytokine synthesis via interaction with CD23.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2356,"ComplexName":"ITGB3-ITGAV-CD47 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05106;P06756;Q08722","subunits.Entrez.IDs.":"3690;3685;961","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515;GO:0007155;GO:0005886","GO.description":"protein binding;cell adhesion;plasma membrane","FunCat.ID":"16.01;34.07;70.02","FunCat.description":"protein binding;cell adhesion;eukaryotic plasma membrane / membrane attached","PubMed.ID":7691831,"subunits.Protein.name.":"Integrin beta-3;Integrin alpha-V;Leukocyte surface antigen CD47","subunits.Gene.name.":"ITGB3;ITGAV;CD47","subunits.Gene.name.syn.":"GP3A;MSK8 VNRA;MER6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"CD47 interactions with alpha(v)beta3 were found to promote both integrin activation induced by RGD peptide, and alpha(v)beta3 avidity in binding immobilized substrates by enhancing integrin clustering (PMID:14966135).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2358,"ComplexName":"ITGAV-ITGB3-SPP1 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05106;P06756;P10451","subunits.Entrez.IDs.":"3690;3685;6696","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0019- coimmunoprecipitation; MI:0030- cross-linking studies","GO.ID":"GO:0016477;GO:0000902;GO:0016049","GO.description":"cell migration;cell morphogenesis;cell growth","FunCat.ID":"34.05.01;40.01","FunCat.description":"cell migration;cell growth / morphogenesis","PubMed.ID":9256478,"subunits.Protein.name.":"Integrin beta-3;Integrin alpha-V;Osteopontin","subunits.Gene.name.":"ITGB3;ITGAV;SPP1","subunits.Gene.name.syn.":"GP3A;MSK8 VNRA;BNSP OPN","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The interaction of OPN with alpha(v)beta3 integrin, expressed on CASMCs (coronary artery smooth muscle cells), causes migration, extracellular matrix invasion, and proliferation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2359,"ComplexName":"ITGAV-ITGB3-ADAM15 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05106;P06756;Q13444","subunits.Entrez.IDs.":"3690;3685;8751","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0005515;GO:0007155;GO:0005886;GO:0031012","GO.description":"protein binding;cell adhesion;plasma membrane;extracellular matrix","FunCat.ID":"16.01;34.07;70.02;70.27.01","FunCat.description":"protein binding;cell adhesion;eukaryotic plasma membrane / membrane attached;extracellular matrix component","PubMed.ID":11882657,"subunits.Protein.name.":"Integrin beta-3;Integrin alpha-V;Disintegrin and metalloproteinase domain-containing protein 15","subunits.Gene.name.":"ITGB3;ITGAV;ADAM15","subunits.Gene.name.syn.":"GP3A;MSK8 VNRA;MDC15","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"ADAM15/alpha(v)beta3 interactions may be important in the adhesion of tumour cells to endothelium (PMID:9914169).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2360,"ComplexName":"Itgav-Itgb3-Gsn complex","Organism":"Mouse","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"O54890;P13020;P43406","subunits.Entrez.IDs.":"16416;227753;16410","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0005515","GO.description":"protein binding","FunCat.ID":"16.01","FunCat.description":"protein binding","PubMed.ID":11577104,"subunits.Protein.name.":"Integrin beta-3 ;Gelsolin;Integrin alpha-V","subunits.Gene.name.":"Itgb3;Gsn;Itgav","subunits.Gene.name.syn.":";Gsb;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2362,"ComplexName":"ITAGV-ITGB3-F11R complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05106;P06756;Q9Y624","subunits.Entrez.IDs.":"3690;3685;50848","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0051098;GO:0005515;GO:0001568;GO:0001944","GO.description":"regulation of binding;protein binding;blood vessel development;vasculature development","FunCat.ID":"18.01.07;16.01;47.03.03.02","FunCat.description":"regulation by binding / dissociation;protein binding;vessels","PubMed.ID":12750158,"subunits.Protein.name.":"Integrin beta-3;Integrin alpha-V;Junctional adhesion molecule A","subunits.Gene.name.":"ITGB3;ITGAV;F11R","subunits.Gene.name.syn.":"GP3A;MSK8 VNRA;JAM1 JCAM","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"JAM-1/A and alpha(v)beta3 form a complex in the absence of bFGF.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2363,"ComplexName":"ITGAV-ITGB3-PXN-PTK2b complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05106;P06756;P49023;Q14289","subunits.Entrez.IDs.":"3690;3685;5829;2185","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515;GO:0007155","GO.description":"protein binding;cell adhesion","FunCat.ID":"16.01;34.07","FunCat.description":"protein binding;cell adhesion","PubMed.ID":11683411,"subunits.Protein.name.":"Integrin beta-3;Integrin alpha-V;Paxillin;Protein-tyrosine kinase 2-beta","subunits.Gene.name.":"ITGB3;ITGAV;PXN;PTK2B","subunits.Gene.name.syn.":"GP3A;MSK8 VNRA;;FAK2 PYK2 RAFTK","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex could play key role in the regulation of cell adhesion-triggered cytoskeletal organization and signal transduction in podosome-containing cells derived from monocytic lineage.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2364,"ComplexName":"ITGAV-ITGB3-ADAM23 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"O75077;P05106;P06756","subunits.Entrez.IDs.":"8745;3690;3685","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0005515;GO:0007155","GO.description":"protein binding;cell adhesion","FunCat.ID":"16.01;34.07","FunCat.description":"protein binding;cell adhesion","PubMed.ID":10749942,"subunits.Protein.name.":"Disintegrin and metalloproteinase domain-containing protein 23 ;Integrin beta-3;Integrin alpha-V","subunits.Gene.name.":"ADAM23;ITGB3;ITGAV","subunits.Gene.name.syn.":"MDC3;GP3A;MSK8 VNRA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"ADAM 23, through its disintegrin-like domain, may function as an adhesion molecule involved in alpha(v)beta3-mediated cell interactions occurring in normal and pathological processes, including progression of malignant tumors from neural origin.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2365,"ComplexName":"ITGAV-ITGB3-COL4A3 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05106;P06756;Q01955","subunits.Entrez.IDs.":"3690;3685;1285","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006417","GO.description":"regulation of translation","FunCat.ID":"12.07","FunCat.description":"translational control","PubMed.ID":12682293,"subunits.Protein.name.":"Integrin beta-3;Integrin alpha-V;Collagen alpha-3","subunits.Gene.name.":"ITGB3;ITGAV;COL4A3","subunits.Gene.name.syn.":"GP3A;MSK8 VNRA;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Tumstatin binding to alpha(v)beta3 integrin leads to the inhibition of Cap-dependent translation (protein synthesis) mediated by focal adhesion kinase/phosphatidylinositol 3-kinase/Akt/mTOR/4E-BP1 pathway.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2366,"ComplexName":"ITGAV-ITGB3-PPAP2b complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"O14495;P05106;P06756","subunits.Entrez.IDs.":"8613;3690;3685","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0007155;GO:0001568;GO:0001944;GO:0005886","GO.description":"cell adhesion;blood vessel development;vasculature development;plasma membrane","FunCat.ID":"34.07;47.03.03.02;70.02","FunCat.description":"cell adhesion;vessels;eukaryotic plasma membrane / membrane attached","PubMed.ID":16099422,"subunits.Protein.name.":"Phospholipid phosphatase 3 ;Integrin beta-3;Integrin alpha-V","subunits.Gene.name.":"PLPP3;ITGB3;ITGAV","subunits.Gene.name.syn.":"LPP3 PPAP2B;GP3A;MSK8 VNRA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2369,"ComplexName":"ITGAV-ITGB3-EGFR complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P00533;P05106;P06756","subunits.Entrez.IDs.":"1956;3690;3685","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515;GO:0007173;GO:0007229","GO.description":"protein binding;epidermal growth factor receptor signaling pathway;integrin-mediated signaling pathway","FunCat.ID":"16.01;30.05.01.12.01;30.05.02.26","FunCat.description":"protein binding;EGF-receptor signalling pathway;integrin receptor signalling pathway","PubMed.ID":15834425,"subunits.Protein.name.":"Epidermal growth factor receptor;Integrin beta-3;Integrin alpha-V","subunits.Gene.name.":"EGFR;ITGB3;ITGAV","subunits.Gene.name.syn.":"ERBB, ERBB1, HER1;GP3A;MSK8 VNRA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The coordination between EGFR and alpha(v)beta3 is essential for the early events of HCMV infection, including viral entry.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2370,"ComplexName":"ITGA2b-ITGB3-CD9 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"blood cell","subunits.UniProt.IDs.":"P05106;P08514;P21926","subunits.Entrez.IDs.":"3690;3674;928","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0051098;GO:0005515;GO:0007155;GO:0005886","GO.description":"regulation of binding;protein binding;cell adhesion;plasma membrane","FunCat.ID":"18.01.07;16.01;34.07;70.02","FunCat.description":"regulation by binding / dissociation;protein binding;cell adhesion;eukaryotic plasma membrane / membrane attached","PubMed.ID":10429193,"subunits.Protein.name.":"Integrin beta-3;Integrin alpha-IIb;CD9 antigen","subunits.Gene.name.":"ITGB3;ITGA2B;CD9","subunits.Gene.name.syn.":"GP3A;GP2B ITGAB;MIC3 TSPAN29","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"CD9 is part of a protein complex that co-precipitates with aIIb3 under native conditions and provides evidence of CD9 and aIIbb3 associating in resting, inactive platelets (PMID:9355765).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2373,"ComplexName":"ITGAV-ITGB3-SPP1 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05106;P06756;P10451","subunits.Entrez.IDs.":"3690;3685;6696","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016477","GO.description":"cell migration","FunCat.ID":"34.05.01","FunCat.description":"cell migration","PubMed.ID":7532190,"subunits.Protein.name.":"Integrin beta-3;Integrin alpha-V;Osteopontin","subunits.Gene.name.":"ITGB3;ITGAV;SPP1","subunits.Gene.name.syn.":"GP3A;MSK8 VNRA;BNSP OPN","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2374,"ComplexName":"ITGAV-ITGB3-LAMA4 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05106;P06756;Q16363","subunits.Entrez.IDs.":"3690;3685;3910","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0005515;GO:0007155;GO:0031012","GO.description":"protein binding;cell adhesion;extracellular matrix","FunCat.ID":"16.01;34.07;70.27.01","FunCat.description":"protein binding;cell adhesion;extracellular matrix component","PubMed.ID":16824487,"subunits.Protein.name.":"Integrin beta-3;Integrin alpha-V;Laminin subunit alpha-4","subunits.Gene.name.":"ITGB3;ITGAV;LAMA4","subunits.Gene.name.syn.":"GP3A;MSK8 VNRA;","Disease.comment":"The G1121-1139 peptide promotes angiogenesis in vivo.","Subunits.comment":"None","Complex.comment":"The alpha4 laminin subunit mediates endothelial cell-adhesion through alpha(v)beta3 integrin and that the key site is G1121-1139.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2375,"ComplexName":"FN1-TGM2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P02751;P21980","subunits.Entrez.IDs.":"2335;7052","Protein.complex.purification.method":"MI:0030- cross-linking studies","GO.ID":"GO:0005515;GO:0007155","GO.description":"protein binding;cell adhesion","FunCat.ID":"16.01;34.07","FunCat.description":"protein binding;cell adhesion","PubMed.ID":10684262,"subunits.Protein.name.":"Fibronectin ;Protein-glutamine gamma-glutamyltransferase 2","subunits.Gene.name.":"FN1;TGM2","subunits.Gene.name.syn.":"FN;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Overexpression of tTG increases the amount of Fn on the cell surface, enhances adhesion and spreading of fibronectin.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2376,"ComplexName":"ITGA2B-ITGB3-FN1-TGM2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P02751;P05106;P08514;P21980","subunits.Entrez.IDs.":"2335;3690;3674;7052","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515;GO:0007155;GO:0005886","GO.description":"protein binding;cell adhesion;plasma membrane","FunCat.ID":"16.01;34.07;70.02","FunCat.description":"protein binding;cell adhesion;eukaryotic plasma membrane / membrane attached","PubMed.ID":10684262,"subunits.Protein.name.":"Fibronectin ;Integrin beta-3;Integrin alpha-IIb;Protein-glutamine gamma-glutamyltransferase 2","subunits.Gene.name.":"FN1;ITGB3;ITGA2B;TGM2","subunits.Gene.name.syn.":"FN;GP3A;GP2B ITGAB;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The tissue transglutaminase mediates the interaction of integrins with fibronectin, thereby acting as an integrin-associated coreceptor to promote cell adhesion and spreading.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2377,"ComplexName":"ITGA2b-ITGB3-CD47-SRC complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05106;P08514;P12931;Q08722","subunits.Entrez.IDs.":"3690;3674;6714;961","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515;GO:0005886","GO.description":"protein binding;plasma membrane","FunCat.ID":"16.01;70.02","FunCat.description":"protein binding;eukaryotic plasma membrane / membrane attached","PubMed.ID":9169439,"subunits.Protein.name.":"Integrin beta-3;Integrin alpha-IIb;Proto-oncogene tyrosine-protein kinase Src;Leukocyte surface antigen CD47","subunits.Gene.name.":"ITGB3;ITGA2B;SRC;CD47","subunits.Gene.name.syn.":"GP3A;GP2B ITGAB;SRC1;MER6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"At least five members of the Src-type kinase family are expressed in megakaryocytes and platelets (PMID:7545532) but only c-Src could be detected in the alpha IIb-beta 3-IAP complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2378,"ComplexName":"ITGA2b-ITGB3-TLN1 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"blood cell","subunits.UniProt.IDs.":"P05106;P08514;Q9Y490","subunits.Entrez.IDs.":"3690;3674;7094","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0005515","GO.description":"protein binding","FunCat.ID":"16.01","FunCat.description":"protein binding","PubMed.ID":8663236,"subunits.Protein.name.":"Integrin beta-3;Integrin alpha-IIb;Talin-1","subunits.Gene.name.":"ITGB3;ITGA2B;TLN1","subunits.Gene.name.syn.":"GP3A;GP2B ITGAB;KIAA1027 TLN","Disease.comment":"Disrupting the beta3 integrin-talin interaction blocks {alpha}IIb-beta3 activation and has a dramatic antithrombotic effect (PMID:17627302).","Subunits.comment":"None","Complex.comment":"The purified talin binds to the cytoplasmic sequences of both alpha  and beta  subunits of this integrin.The regulated binding of talin to integrin beta tails is a final common element of cellular signaling cascades that control integrin activation (PMID:14526080).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2379,"ComplexName":"ITGA2B-ITGB3-CIB1 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"liver","subunits.UniProt.IDs.":"P05106;P08514;Q99828","subunits.Entrez.IDs.":"3690;3674;10519","Protein.complex.purification.method":"MI:0411-enzyme linked immunosorbent assay;MI:0018-two hybrid","GO.ID":"GO:0005509;GO:0007155","GO.description":"calcium ion binding;cell adhesion","FunCat.ID":"16.17.01;34.07","FunCat.description":"calcium binding;cell adhesion","PubMed.ID":9030514,"subunits.Protein.name.":"Integrin beta-3;Integrin alpha-IIb;Calcium and integrin-binding protein 1","subunits.Gene.name.":"ITGB3;ITGA2B;CIB1","subunits.Gene.name.syn.":"GP3A;GP2B ITGAB;CIB KIP PRKDCIP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"CIB does not regulate alpha-IIb-beta3 inside-out signaling, but rather is involved in an alpha-IIb-beta3 post-receptor occupancy event.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2381,"ComplexName":"ITGA2B-ITGB3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P05106;P08514","subunits.Entrez.IDs.":"3690;3674","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":8132607,"subunits.Protein.name.":"Integrin beta-3;Integrin alpha-IIb","subunits.Gene.name.":"ITGB3;ITGA2B","subunits.Gene.name.syn.":"GP3A;GP2B ITGAB","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2382,"ComplexName":"ITGA2B-ITGB3-F11R complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05106;P08514;Q9Y624","subunits.Entrez.IDs.":"3690;3674;50848","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0007155","GO.description":"cell adhesion","FunCat.ID":"34.07","FunCat.description":"cell adhesion","PubMed.ID":11171323,"subunits.Protein.name.":"Integrin beta-3;Integrin alpha-IIb;Junctional adhesion molecule A","subunits.Gene.name.":"ITGB3;ITGA2B;F11R","subunits.Gene.name.syn.":"GP3A;GP2B ITGAB;JAM1 JCAM","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2383,"ComplexName":"ITGA5-ITGB1-FN1-TGM2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P02751;P05556;P08648;P21980","subunits.Entrez.IDs.":"2335;3688;3678;7052","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515;GO:0007155;GO:0005886","GO.description":"protein binding;cell adhesion;plasma membrane","FunCat.ID":"16.01;34.07;70.02","FunCat.description":"protein binding;cell adhesion;eukaryotic plasma membrane / membrane attached","PubMed.ID":10684262,"subunits.Protein.name.":"Fibronectin ;Integrin beta-1;Integrin alpha-5 ;Protein-glutamine gamma-glutamyltransferase 2","subunits.Gene.name.":"FN1;ITGB1;ITGA5;TGM2","subunits.Gene.name.syn.":"FN;FNRB MDF2 MSK12;FNRA;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The tissue transglutaminase mediates the interaction of integrins with fibronectin, thereby acting as an integrin-associated coreceptor to promote cell adhesion and spreading.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2384,"ComplexName":"ITGA5-ITGB1-ADAM15 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P08648;Q13444","subunits.Entrez.IDs.":"3688;3678;8751","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0005515;GO:0007155","GO.description":"protein binding;cell adhesion","FunCat.ID":"16.01;34.07","FunCat.description":"protein binding;cell adhesion","PubMed.ID":9914169,"subunits.Protein.name.":"Integrin beta-1;Integrin alpha-5 ;Disintegrin and metalloproteinase domain-containing protein 15","subunits.Gene.name.":"ITGB1;ITGA5;ADAM15","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;FNRA;MDC15","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2385,"ComplexName":"ITGA5-ITGB4 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P08648","subunits.Entrez.IDs.":"3688;3678","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007155","GO.description":"cell adhesion","FunCat.ID":"34.07","FunCat.description":"cell adhesion","PubMed.ID":3546305,"subunits.Protein.name.":"Integrin beta-1;Integrin alpha-5","subunits.Gene.name.":"ITGB1;ITGA5","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;FNRA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2386,"ComplexName":"Itga-Itgb1-Ppap2b complex","Organism":"Mouse","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P09055;P11688;Q99JY8","subunits.Entrez.IDs.":"16412;16402;67916","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0007155;GO:0001568;GO:0001944;GO:0005886","GO.description":"cell adhesion;blood vessel development;vasculature development;plasma membrane","FunCat.ID":"34.07;47.03.03.02;70.02","FunCat.description":"cell adhesion;vessels;eukaryotic plasma membrane / membrane attached","PubMed.ID":16099422,"subunits.Protein.name.":"Integrin beta-1 ;Integrin alpha-5;Phospholipid phosphatase 3","subunits.Gene.name.":"Itgb1;Itga5;Plpp3","subunits.Gene.name.syn.":";Vla5;Lpp3 Ppap2b","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2388,"ComplexName":"Itga5-Itgb1-Fn1-Sfrp2 complex","Organism":"Dog","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P08648;Q28275;Q863H1","subunits.Entrez.IDs.":"3688;3678;403845;475471","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0043067","GO.description":"regulation of programmed cell death","FunCat.ID":"40.10.02.04","FunCat.description":"regulation of apoptosis","PubMed.ID":14709558,"subunits.Protein.name.":"Integrin beta-1;Integrin alpha-5 ;Fibronectin ;Secreted frizzled-related protein 2","subunits.Gene.name.":"ITGB1;ITGA5;FN1;SFRP2","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;FNRA;;","Disease.comment":"None","Subunits.comment":"Since ITGA5 and ITGB1 from dog were not available in the UniProt database at the time of annotation, the orthologous proteins from human were used.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Canis lupus familiaris (Dog) (Canis familiaris);Canis lupus familiaris (Dog) (Canis familiaris)"}
{"ComplexID":2390,"ComplexName":"CD98-LAT2-ITGB1 complex","Organism":"Human","Synonyms":"None","Cell.line":"epithelium","subunits.UniProt.IDs.":"P05556;P08195;Q9UHI5","subunits.Entrez.IDs.":"3688;6520;23428","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0016337","GO.description":"single organismal cell-cell adhesion","FunCat.ID":"34.07.01","FunCat.description":"cell-cell adhesion","PubMed.ID":11507094,"subunits.Protein.name.":"Integrin beta-1;4F2 cell-surface antigen heavy chain;Large neutral amino acids transporter small subunit 2","subunits.Gene.name.":"ITGB1;SLC3A2;SLC7A8","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;MDU1;LAT2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The specific molecular ratio between the heterodimer CD98/LAT-2 and beta 1 integrin may be required for the polarity of epithelial cells.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2395,"ComplexName":"ITGA7-ITGB1-CD151 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"muscle","subunits.UniProt.IDs.":"P05556;P48509;Q13683","subunits.Entrez.IDs.":"3688;977;3679","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515;GO:0007155","GO.description":"protein binding;cell adhesion","FunCat.ID":"16.01;34.07","FunCat.description":"protein binding;cell adhesion","PubMed.ID":11884516,"subunits.Protein.name.":"Integrin beta-1;CD151 antigen;Integrin alpha-7 [Cleaved into: Integrin alpha-7 heavy chain; Integrin alpha-7 light chain; Integrin alpha-7 70 kDa form]","subunits.Gene.name.":"ITGB1;CD151;ITGA7","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;TSPAN24;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The expression of alpha7-beta1 in K562 cells results in increased levels of CD151 at its surface.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2396,"ComplexName":"ITGA7-ITGB1-CD9 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P21926;Q13683","subunits.Entrez.IDs.":"3688;928;3679","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007519","GO.description":"skeletal muscle tissue development","FunCat.ID":"41.05.15","FunCat.description":"myogenesis","PubMed.ID":10459022,"subunits.Protein.name.":"Integrin beta-1;CD9 antigen;Integrin alpha-7 [Cleaved into: Integrin alpha-7 heavy chain; Integrin alpha-7 light chain; Integrin alpha-7 70 kDa form]","subunits.Gene.name.":"ITGB1;CD9;ITGA7","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;MIC3 TSPAN29;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2397,"ComplexName":"ITGA7-ITGB1-ITGB1BP3 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;Q13683;Q9NPI5","subunits.Entrez.IDs.":"3688;3679;27231","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007155","GO.description":"cell adhesion","FunCat.ID":"34.07","FunCat.description":"cell adhesion","PubMed.ID":12941630,"subunits.Protein.name.":"Integrin beta-1;Integrin alpha-7 [Cleaved into: Integrin alpha-7 heavy chain; Integrin alpha-7 light chain; Integrin alpha-7 70 kDa form];Nicotinamide riboside kinase 2","subunits.Gene.name.":"ITGB1;ITGA7;NMRK2","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;;ITGB1BP3 NRK2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2398,"ComplexName":"ITGA3-ITGB1-BSG complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P26006;P35613","subunits.Entrez.IDs.":"3688;3675;682","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0050789;GO:0007160","GO.description":"regulation of biological process;cell-matrix adhesion","FunCat.ID":"18;34.07.02","FunCat.description":"REGULATION OF METABOLISM AND PROTEIN FUNCTION;cell-matrix adhesion","PubMed.ID":9360995,"subunits.Protein.name.":"Integrin beta-1;Integrin alpha-3;Basigin","subunits.Gene.name.":"ITGB1;ITGA3;BSG","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;MSK18;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The physical association between EMMPRIN and alpha3-beta1 may play a role in adhesion-induced matrix metalloproteinase production.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2399,"ComplexName":"ITGA3-ITGB1-CD63 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P08962;P26006","subunits.Entrez.IDs.":"3688;967;3675","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006928;GO:0007155","GO.description":"movement of cell or subcellular component;cell adhesion","FunCat.ID":"34.05;34.07","FunCat.description":"cell motility;cell adhesion","PubMed.ID":9360995,"subunits.Protein.name.":"Integrin beta-1;CD63 antigen;Integrin alpha-3","subunits.Gene.name.":"ITGB1;CD63;ITGA3","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;MLA1 TSPAN30;MSK18","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2400,"ComplexName":"ITGA3-ITGB1-CD151 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"skin","subunits.UniProt.IDs.":"P05556;P26006;P48509","subunits.Entrez.IDs.":"3688;3675;977","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0042277;GO:0007160;GO:0005886","GO.description":"peptide binding;cell-matrix adhesion;plasma membrane","FunCat.ID":"16.02;34.07.02;70.02","FunCat.description":"peptide binding;cell-matrix adhesion;eukaryotic plasma membrane / membrane attached","PubMed.ID":10811835,"subunits.Protein.name.":"Integrin beta-1;Integrin alpha-3;CD151 antigen","subunits.Gene.name.":"ITGB1;ITGA3;CD151","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;MSK18;TSPAN24","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"CD151 is colocalized with alpha3-beta1 in pre-hemidesmosomal structures together with laminin-5.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2401,"ComplexName":"ITGA3-ITGB1-THBS1 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P07996;P26006","subunits.Entrez.IDs.":"3688;7057;3675","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0007155","GO.description":"cell adhesion","FunCat.ID":"34.07","FunCat.description":"cell adhesion","PubMed.ID":11358957,"subunits.Protein.name.":"Integrin beta-1;Thrombospondin-1;Integrin alpha-3","subunits.Gene.name.":"ITGB1;THBS1;ITGA3","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;TSP TSP1;MSK18","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2402,"ComplexName":"Itga3-Itgb1-Tgm2 complex","Organism":"Rat","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P49134;Q62470;Q9WVJ6","subunits.Entrez.IDs.":"24511;16400;56083","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515;GO:0007155;GO:0005886","GO.description":"protein binding;cell adhesion;plasma membrane","FunCat.ID":"16.01;34.07;70.02","FunCat.description":"protein binding;cell adhesion;eukaryotic plasma membrane / membrane attached","PubMed.ID":10684262,"subunits.Protein.name.":"Integrin beta-1 ;Integrin alpha-3 ;Protein Tgm2","subunits.Gene.name.":"Itgb1;Itga3;Tgm2","subunits.Gene.name.syn.":";;TgaseII","Disease.comment":"None","Subunits.comment":"Since Itga3 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"Complexes of transglutaminase with integrins are formed inside the cell during biosynthesis and accumulate on the surface and in focal adhesions.","SWISSPROT.organism":"Rattus norvegicus (Rat);Mus musculus (Mouse);Rattus norvegicus (Rat)"}
{"ComplexID":2406,"ComplexName":"ITGA3-ITGB1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P26006","subunits.Entrez.IDs.":"3688;3675","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007155","GO.description":"cell adhesion","FunCat.ID":"34.07","FunCat.description":"cell adhesion","PubMed.ID":3546305,"subunits.Protein.name.":"Integrin beta-1;Integrin alpha-3","subunits.Gene.name.":"ITGB1;ITGA3","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;MSK18","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2411,"ComplexName":"ITGA6-ITGB1-CD151 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P23229;P48509","subunits.Entrez.IDs.":"3688;3655;977","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016477","GO.description":"cell migration","FunCat.ID":"34.05.01","FunCat.description":"cell migration","PubMed.ID":11884516,"subunits.Protein.name.":"Integrin beta-1;Integrin alpha-6;CD151 antigen","subunits.Gene.name.":"ITGB1;ITGA6;CD151","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;None;TSPAN24","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The YXXphi motif-mediated internalization of CD151 promotes integrin-dependent cell migration by modulating the endocytosis and/or vesicular trafficking of its associated integrins (PMID:17716972).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2413,"ComplexName":"ITGA6-ITGB1 complex","Organism":"Human","Synonyms":"Integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P23229","subunits.Entrez.IDs.":"3688;3655","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0007155","GO.description":"cell adhesion","FunCat.ID":"34.07","FunCat.description":"cell adhesion","PubMed.ID":2649503,"subunits.Protein.name.":"Integrin beta-1;Integrin alpha-6","subunits.Gene.name.":"ITGB1;ITGA6","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2415,"ComplexName":"Itgb1-Rap1a-Prkd1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P09055;P62835;Q62101","subunits.Entrez.IDs.":"16412;109905;18760","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0050789","GO.description":"regulation of biological process","FunCat.ID":"18","FunCat.description":"REGULATION OF METABOLISM AND PROTEIN FUNCTION","PubMed.ID":16111639,"subunits.Protein.name.":"Integrin beta-1 ;Ras-related protein Rap-1A ;Serine/threonine-protein kinase D1","subunits.Gene.name.":"Itgb1;Rap1a;Prkd1","subunits.Gene.name.syn.":";Krev-1;Pkcm Pkd Prkcm","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2416,"ComplexName":"ITGB1-RAP1A-PKD1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P62834;P98161","subunits.Entrez.IDs.":"3688;5906;5310","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0050789","GO.description":"regulation of biological process","FunCat.ID":"18","FunCat.description":"REGULATION OF METABOLISM AND PROTEIN FUNCTION","PubMed.ID":16111639,"subunits.Protein.name.":"Integrin beta-1;Ras-related protein Rap-1A;Polycystin-1","subunits.Gene.name.":"ITGB1;RAP1A;PKD1","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;KREV1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2417,"ComplexName":"ITGA4-ITGB1-EMILIN1 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P13612;Q9Y6C2","subunits.Entrez.IDs.":"3688;3676;11117","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006928;GO:0007155","GO.description":"movement of cell or subcellular component;cell adhesion","FunCat.ID":"34.05;34.07","FunCat.description":"cell motility;cell adhesion","PubMed.ID":12456677,"subunits.Protein.name.":"Integrin beta-1;Integrin alpha-4 ;EMILIN-1","subunits.Gene.name.":"ITGB1;ITGA4;EMILIN1","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;CD49D;EMI","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2418,"ComplexName":"ITGA4-ITGB1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P13612","subunits.Entrez.IDs.":"3688;3676","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007155","GO.description":"cell adhesion","FunCat.ID":"34.07","FunCat.description":"cell adhesion","PubMed.ID":3546305,"subunits.Protein.name.":"Integrin beta-1;Integrin alpha-4","subunits.Gene.name.":"ITGB1;ITGA4","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;CD49D","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2419,"ComplexName":"ITGA4-ITGB1-CD81 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P13612;P60033","subunits.Entrez.IDs.":"3688;3676;975","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007155","GO.description":"cell adhesion","FunCat.ID":"34.07","FunCat.description":"cell adhesion","PubMed.ID":10229664,"subunits.Protein.name.":"Integrin beta-1;Integrin alpha-4 ;CD81 antigen","subunits.Gene.name.":"ITGB1;ITGA4;CD81","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;CD49D;TAPA1, TSPAN28","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2420,"ComplexName":"ITGA4-ITGB1-CD53 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P13612;P19397","subunits.Entrez.IDs.":"3688;3676;963","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515","GO.description":"protein binding","FunCat.ID":"16.01","FunCat.description":"protein binding","PubMed.ID":8757325,"subunits.Protein.name.":"Integrin beta-1;Integrin alpha-4 ;Leukocyte surface antigen CD53","subunits.Gene.name.":"ITGB1;ITGA4;CD53","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;CD49D;MOX44 TSPAN25","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2421,"ComplexName":"ITGA4-ITGB1-VCAM1 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P13612;P19320","subunits.Entrez.IDs.":"3688;3676;7412","Protein.complex.purification.method":"MI:0004- affinMI:0030- cross-linking studies","GO.ID":"GO:0007155","GO.description":"cell adhesion","FunCat.ID":"34.07","FunCat.description":"cell adhesion","PubMed.ID":10623819,"subunits.Protein.name.":"Integrin beta-1;Integrin alpha-4 ;Vascular cell adhesion protein 1","subunits.Gene.name.":"ITGB1;ITGA4;VCAM1","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;CD49D;L1CAM","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2422,"ComplexName":"ITGA4-ITGB1-JAM2 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P13612;P57087","subunits.Entrez.IDs.":"3688;3676;58494","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0007155","GO.description":"cell adhesion","FunCat.ID":"34.07","FunCat.description":"cell adhesion","PubMed.ID":12070135,"subunits.Protein.name.":"Integrin beta-1;Integrin alpha-4 ;Junctional adhesion molecule B","subunits.Gene.name.":"ITGB1;ITGA4;JAM2","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;CD49D;C21orf43 VEJAM","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2423,"ComplexName":"ITGA4-ITGB1-CD47 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P13612;Q08722","subunits.Entrez.IDs.":"3688;3676;961","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007155","GO.description":"cell adhesion","FunCat.ID":"34.07","FunCat.description":"cell adhesion","PubMed.ID":15292185,"subunits.Protein.name.":"Integrin beta-1;Integrin alpha-4 ;Leukocyte surface antigen CD47","subunits.Gene.name.":"ITGB1;ITGA4;CD47","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;CD49D;MER6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2424,"ComplexName":"ITGA4-ITGB1-CD63 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P08962;P13612","subunits.Entrez.IDs.":"3688;967;3676","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515","GO.description":"protein binding","FunCat.ID":"16.01","FunCat.description":"protein binding","PubMed.ID":8757325,"subunits.Protein.name.":"Integrin beta-1;CD63 antigen;Integrin alpha-4","subunits.Gene.name.":"ITGB1;CD63;ITGA4","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;MLA1 TSPAN30;CD49D","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2425,"ComplexName":"ITGA4-ITGB1-PXN complex","Organism":"Hamster","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P13612;P49023","subunits.Entrez.IDs.":"3688;3676;5829","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0019- coimmunoprecipitation","GO.ID":"GO:0016477","GO.description":"cell migration","FunCat.ID":"34.05.01","FunCat.description":"cell migration","PubMed.ID":12221126,"subunits.Protein.name.":"Integrin beta-1;Integrin alpha-4 ;Paxillin","subunits.Gene.name.":"ITGB1;ITGA4;PXN","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;CD49D;","Disease.comment":"None","Subunits.comment":"Since ITGA4, ITGB1 and PXN from hamster were not available in the UniProt databaseat the time of annotation, the orthologous human proteins were used.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2426,"ComplexName":"ITGA4-ITGB1-THBS1 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P07996;P13612","subunits.Entrez.IDs.":"3688;7057;3676","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0007155","GO.description":"cell adhesion","FunCat.ID":"34.07","FunCat.description":"cell adhesion","PubMed.ID":11980922,"subunits.Protein.name.":"Integrin beta-1;Thrombospondin-1;Integrin alpha-4","subunits.Gene.name.":"ITGB1;THBS1;ITGA4","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;TSP TSP1;CD49D","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2427,"ComplexName":"Itga4-Itgb1-Adam2 complex","Organism":"Mouse","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P09055;Q00651;Q60718","subunits.Entrez.IDs.":"16412;16401;11495","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0031- protein cross-linking with a bifunctional reagent","GO.ID":"GO:0016337","GO.description":"single organismal cell-cell adhesion","FunCat.ID":"34.07.01","FunCat.description":"cell-cell adhesion","PubMed.ID":9889149,"subunits.Protein.name.":"Integrin beta-1 ;Integrin alpha-4 ;Disintegrin and metalloproteinase domain-containing protein 2","subunits.Gene.name.":"Itgb1;Itga4;Adam2","subunits.Gene.name.syn.":";;Ftnb","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex mediates sperm-egg fusion.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2428,"ComplexName":"ITGA4-ITGB1-THBS2 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P13612;P35442","subunits.Entrez.IDs.":"3688;3676;7058","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0007155","GO.description":"cell adhesion","FunCat.ID":"34.07","FunCat.description":"cell adhesion","PubMed.ID":11980922,"subunits.Protein.name.":"Integrin beta-1;Integrin alpha-4 ;Thrombospondin-2","subunits.Gene.name.":"ITGB1;ITGA4;THBS2","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;CD49D;TSP2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2429,"ComplexName":"ITGA2-ITGB1-CD47 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P17301;Q08722","subunits.Entrez.IDs.":"3688;3673;961","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006935","GO.description":"chemotaxis","FunCat.ID":"34.11.03.03","FunCat.description":"chemotaxis","PubMed.ID":10397731,"subunits.Protein.name.":"Integrin beta-1;Integrin alpha-2 ;Leukocyte surface antigen CD47","subunits.Gene.name.":"ITGB1;ITGA2;CD47","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;CD49B;MER6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Integrin-associated protein (IAP/CD47) augments the function of alpha2-beta1 integrin in smooth muscle cells (SMC), resulting in enhanced chemotaxis toward soluble collagen.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2430,"ComplexName":"ITGA2-ITGB1-CHAD complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"O15335;P05556;P17301","subunits.Entrez.IDs.":"1101;3688;3673","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0019- coimmunoprecipitation","GO.ID":"GO:0007155","GO.description":"cell adhesion","FunCat.ID":"34.07","FunCat.description":"cell adhesion","PubMed.ID":9281592,"subunits.Protein.name.":"Chondroadherin ;Integrin beta-1;Integrin alpha-2","subunits.Gene.name.":"CHAD;ITGB1;ITGA2","subunits.Gene.name.syn.":"SLRR4A;FNRB MDF2 MSK12;CD49B","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2431,"ComplexName":"ITGA2-ITGB1-COL6A3 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P12111;P17301","subunits.Entrez.IDs.":"3688;1293;3673","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0005515;GO:0007155;GO:0005886;GO:0031012","GO.description":"protein binding;cell adhesion;plasma membrane;extracellular matrix","FunCat.ID":"16.01;34.07;70.02;70.27.01","FunCat.description":"protein binding;cell adhesion;eukaryotic plasma membrane / membrane attached;extracellular matrix component","PubMed.ID":8387021,"subunits.Protein.name.":"Integrin beta-1;Collagen alpha-3;Integrin alpha-2","subunits.Gene.name.":"ITGB1;COL6A3;ITGA2","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;;CD49B","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2432,"ComplexName":"ITGA2-ITGB1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P17301","subunits.Entrez.IDs.":"3688;3673","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007155","GO.description":"cell adhesion","FunCat.ID":"34.07","FunCat.description":"cell adhesion","PubMed.ID":3546305,"subunits.Protein.name.":"Integrin beta-1;Integrin alpha-2","subunits.Gene.name.":"ITGB1;ITGA2","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;CD49B","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2433,"ComplexName":"Itga5-Itgb1-Tgm2 complex","Organism":"Rat","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P49134;Q7M074;Q9WVJ6","subunits.Entrez.IDs.":"24511;315346;56083","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515;GO:0007155;GO:0005886","GO.description":"protein binding;cell adhesion;plasma membrane","FunCat.ID":"16.01;34.07;70.02","FunCat.description":"protein binding;cell adhesion;eukaryotic plasma membrane / membrane attached","PubMed.ID":10684262,"subunits.Protein.name.":"Integrin beta-1 ;Fibronectin receptor alpha chain ;Protein Tgm2","subunits.Gene.name.":"Itgb1;Itga5;Tgm2","subunits.Gene.name.syn.":";;TgaseII","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complexes of transglutaminase with integrins are formed inside the cell during biosynthesis and accumulate on the surface and in focal adhesions.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2434,"ComplexName":"ITGA1-ITGB1-COL6A3 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P12111;P56199","subunits.Entrez.IDs.":"3688;1293;3672","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0005515;GO:0007155;GO:0005886;GO:0031012","GO.description":"protein binding;cell adhesion;plasma membrane;extracellular matrix","FunCat.ID":"16.01;34.07;70.02;70.27.01","FunCat.description":"protein binding;cell adhesion;eukaryotic plasma membrane / membrane attached;extracellular matrix component","PubMed.ID":8387021,"subunits.Protein.name.":"Integrin beta-1;Collagen alpha-3;Integrin alpha-1","subunits.Gene.name.":"ITGB1;COL6A3;ITGA1","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2435,"ComplexName":"ITGA1-ITGB1-PTPN2 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P17706;P56199","subunits.Entrez.IDs.":"3688;5771;3672","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007169","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway","FunCat.ID":"30.05.01.12","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways","PubMed.ID":15592458,"subunits.Protein.name.":"Integrin beta-1;Tyrosine-protein phosphatase non-receptor type 2 ;Integrin alpha-1","subunits.Gene.name.":"ITGB1;PTPN2;ITGA1","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;PTPT;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The cytoplasmic tail of alpha(1) integrin selectively interacts with a ubiquitously expressed TCPTP and activates it after cell adhesion to collagen.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2436,"ComplexName":"ITGAV-ITGB1 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P06756","subunits.Entrez.IDs.":"3688;3685","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515;GO:0007155","GO.description":"protein binding;cell adhesion","FunCat.ID":"16.01;34.07","FunCat.description":"protein binding;cell adhesion","PubMed.ID":2138612,"subunits.Protein.name.":"Integrin beta-1;Integrin alpha-V","subunits.Gene.name.":"ITGB1;ITGAV","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;MSK8 VNRA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The cell surface expression level of alphaV-beta1 is dependent on the number of alphaV subunits available after the formation of other alphaV-containing heterodimers (PMID:11997396).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2437,"ComplexName":"ITGA6-ITGB1-CYR61 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"O00622;P05556;P23229","subunits.Entrez.IDs.":"3491;3688;3655","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0007155;GO:0001568;GO:0001944","GO.description":"cell adhesion;blood vessel development;vasculature development","FunCat.ID":"34.07;47.03.03.02","FunCat.description":"cell adhesion;vessels","PubMed.ID":12826661,"subunits.Protein.name.":"Protein CYR61 ;Integrin beta-1;Integrin alpha-6","subunits.Gene.name.":"CYR61;ITGB1;ITGA6","subunits.Gene.name.syn.":"CCN1 GIG1 IGFBP10;FNRB MDF2 MSK12;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The T1 sequence in CCN1 is a novel binding motif for integrin alpha6-beta1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2439,"ComplexName":"ITGA8-ITGB1 complex","Organism":"Human","Synonyms":"integrin","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P53708","subunits.Entrez.IDs.":"3688;8516","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0005515;GO:0007155","GO.description":"protein binding;cell adhesion","FunCat.ID":"16.01;34.07","FunCat.description":"protein binding;cell adhesion","PubMed.ID":7559467,"subunits.Protein.name.":"Integrin beta-1;Integrin alpha-8 [Cleaved into: Integrin alpha-8 heavy chain; Integrin alpha-8 light chain]","subunits.Gene.name.":"ITGB1;ITGA8","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This integrin is receptor for tenascin, fibronectin, and vitronectin.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2440,"ComplexName":"ITGA9-ITGB1-ADAM9 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;Q13443;Q13797","subunits.Entrez.IDs.":"3688;8754;3680","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0005515","GO.description":"protein binding","FunCat.ID":"16.01","FunCat.description":"protein binding","PubMed.ID":11882657,"subunits.Protein.name.":"Integrin beta-1;Disintegrin and metalloproteinase domain-containing protein 9 ;Integrin alpha-9","subunits.Gene.name.":"ITGB1;ADAM9;ITGA9","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;KIAA0021 MCMP MDC9 MLTNG;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Alpha9-eta1-ADAM interactions may have a broad significance in many biological and pathological processes such as fertilization, development, and tissue remodeling.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2441,"ComplexName":"Itga9-Itgb1-Adam2 complex","Organism":"Mammalia","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;Q13797;Q60718","subunits.Entrez.IDs.":"3688;3680;11495","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0005515","GO.description":"protein binding","FunCat.ID":"16.01","FunCat.description":"protein binding","PubMed.ID":11882657,"subunits.Protein.name.":"Integrin beta-1;Integrin alpha-9 ;Disintegrin and metalloproteinase domain-containing protein 2","subunits.Gene.name.":"ITGB1;ITGA9;Adam2","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;;Ftnb","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Alpha9-beta1-ADAM interactions may have a broad significance in many biological and pathological processes such as fertilization, development, and tissue remodeling.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Mus musculus (Mouse)"}
{"ComplexID":2442,"ComplexName":"ITGA9-ITGB1-VCAM1 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P19320;Q13797","subunits.Entrez.IDs.":"3688;7412;3680","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0016477;GO:0007155;GO:0072672","GO.description":"cell migration;cell adhesion;neutrophil extravasation","FunCat.ID":"34.05.01;34.07","FunCat.description":"cell migration;cell adhesion","PubMed.ID":10209034,"subunits.Protein.name.":"Integrin beta-1;Vascular cell adhesion protein 1 ;Integrin alpha-9","subunits.Gene.name.":"ITGB1;VCAM1;ITGA9","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;L1CAM;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2443,"ComplexName":"ITGA9-ITGB1-TNC complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P24821;Q13797","subunits.Entrez.IDs.":"3688;3371;3680","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0005515","GO.description":"protein binding","FunCat.ID":"16.01","FunCat.description":"protein binding","PubMed.ID":9565552,"subunits.Protein.name.":"Integrin beta-1;Tenascin ;Integrin alpha-9","subunits.Gene.name.":"ITGB1;TNC;ITGA9","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;HXB;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2444,"ComplexName":"ITGB1-ITGA9 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P05556;Q13797","subunits.Entrez.IDs.":"3688;3680","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515;GO:0007155;GO:0016049","GO.description":"protein binding;cell adhesion;cell growth","FunCat.ID":"16.01;34.07;40.01","FunCat.description":"protein binding;cell adhesion;cell growth / morphogenesis","PubMed.ID":8798654,"subunits.Protein.name.":"Integrin beta-1;Integrin alpha-9","subunits.Gene.name.":"ITGB1;ITGA9","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cells expressing alpha9-beta1 attach and spread equally well, and also proliferate, but significantly less than do cells expressing alpha(v)beta3.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2445,"ComplexName":"ITGA9-ITGB1-ADAM15 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;Q13444;Q13797","subunits.Entrez.IDs.":"3688;8751;3680","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0005515;GO:0016337","GO.description":"protein binding;single organismal cell-cell adhesion","FunCat.ID":"16.01;34.07.01","FunCat.description":"protein binding;cell-cell adhesion","PubMed.ID":11882657,"subunits.Protein.name.":"Integrin beta-1;Disintegrin and metalloproteinase domain-containing protein 15 ;Integrin alpha-9","subunits.Gene.name.":"ITGB1;ADAM15;ITGA9","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;MDC15;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Alpha9-beta 1-ADAM interactions may have a broad significance in many biological and pathological processes such as fertilization, development, and tissue remodeling.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2446,"ComplexName":"ITGA9-ITGB1-FIGF complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"O43915;P05556;Q13797","subunits.Entrez.IDs.":"2277;3688;3680","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0016477;GO:0007155;GO:0030154","GO.description":"cell migration;cell adhesion;cell differentiation","FunCat.ID":"34.05.01;34.07;40.02","FunCat.description":"cell migration;cell adhesion;cell differentiation","PubMed.ID":15590642,"subunits.Protein.name.":"Vascular endothelial growth factor D ;Integrin beta-1;Integrin alpha-9","subunits.Gene.name.":"VEGFD;ITGB1;ITGA9","subunits.Gene.name.syn.":"FIGF;FNRB MDF2 MSK12;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Alpha9-beta1 directly binds to VEGF-C and -D and contributes to lymphangiogenesis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2447,"ComplexName":"ITGA9-ITGB1-ADAM12 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"O43184;P05556;Q13797","subunits.Entrez.IDs.":"8038;3688;3680","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0016337;GO:0005886","GO.description":"single organismal cell-cell adhesion;plasma membrane","FunCat.ID":"34.07.01;70.02","FunCat.description":"cell-cell adhesion;eukaryotic plasma membrane / membrane attached","PubMed.ID":10944520,"subunits.Protein.name.":"Disintegrin and metalloproteinase domain-containing protein 12 ;Integrin beta-1;Integrin alpha-9","subunits.Gene.name.":"ADAM12;ITGB1;ITGA9","subunits.Gene.name.syn.":"MLTN;FNRB MDF2 MSK12;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2453,"ComplexName":"Multiprotein complex (monoubiquitination)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P00533;Q13191;Q5U5U6;Q96B97","subunits.Entrez.IDs.":"1956;868;7314;30011","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579","GO.description":"protein ubiquitination;protein deubiquitination","FunCat.ID":"14.07.05","FunCat.description":"modification by ubiquitination, deubiquitination","PubMed.ID":12218189,"subunits.Protein.name.":"Epidermal growth factor receptor;E3 ubiquitin-protein ligase CBL-B ;Epididymis secretory protein Li 50 ;SH3 domain-containing kinase-binding protein 1","subunits.Gene.name.":"EGFR;CBLB;UBB;SH3KBP1","subunits.Gene.name.syn.":"ERBB, ERBB1, HER1;RNF56;HEL-S-50;CIN85","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors show that the adaptor protein CIN85 and its homologue CMS are monoubiquitinated by Cbl/Cbl-b after epidermal growth factor (EGF) stimulation. CIN85  has a dual role in controlling EGFR down-regulation, because it both promotes receptor internalization and participates in endosomal sorting and subsequent degradation of activated receptors.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2454,"ComplexName":"CIN85-CBL-SH3GL2-EGFR complex, EGF stimulated","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"P00533;P22681;Q3V639;Q96B97","subunits.Entrez.IDs.":"1956;867;6456;30011","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006900;GO:0016050;GO:0006897;GO:0007173","GO.description":"membrane budding;vesicle organization;endocytosis;epidermal growth factor receptor signaling pathway","FunCat.ID":"20.09.07.25;20.09.18.09.01;30.05.01.12.01","FunCat.description":"vesicle formation;endocytosis;EGF-receptor signalling pathway","PubMed.ID":11894095,"subunits.Protein.name.":"Epidermal growth factor receptor;E3 ubiquitin-protein ligase CBL;Endophilin A1 BAR domain;SH3 domain-containing kinase-binding protein 1","subunits.Gene.name.":"EGFR;CBL;SH3GL2;SH3KBP1","subunits.Gene.name.syn.":"ERBB, ERBB1, HER1;CBL2, RNF55;;CIN85","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cbl rapidly recruits CIN85 and endophilins to form a complex with activated EGF receptors, thus controlling receptor internalization.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2455,"ComplexName":"CIN85-SH3GL2 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"Q96B97;Q99962","subunits.Entrez.IDs.":"30011;6456","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006900;GO:0016050;GO:0006897","GO.description":"membrane budding;vesicle organization;endocytosis","FunCat.ID":"20.09.07.25;20.09.18.09.01","FunCat.description":"vesicle formation;endocytosis","PubMed.ID":11894095,"subunits.Protein.name.":"SH3 domain-containing kinase-binding protein 1;Endophilin-A1","subunits.Gene.name.":"SH3KBP1;SH3GL2","subunits.Gene.name.syn.":"CIN85;CNSA2 SH3D2A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2456,"ComplexName":"MET-CIN85-SH3GL3-CBL complex, HGF stimulated","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"P08581;P22681;Q96B97;Q99963","subunits.Entrez.IDs.":"4233;867;30011;6457","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006900;GO:0016050;GO:0006897;GO:0007169","GO.description":"membrane budding;vesicle organization;endocytosis;transmembrane receptor protein tyrosine kinase signaling pathway","FunCat.ID":"20.09.07.25;20.09.18.09.01;30.05.01.12","FunCat.description":"vesicle formation;endocytosis;transmembrane receptor protein tyrosine kinase signalling pathways","PubMed.ID":11894096,"subunits.Protein.name.":"Hepatocyte growth factor receptor;E3 ubiquitin-protein ligase CBL;SH3 domain-containing kinase-binding protein 1;Endophilin-A3","subunits.Gene.name.":"MET;CBL;SH3KBP1;SH3GL3","subunits.Gene.name.syn.":"None;CBL2, RNF55;CIN85;CNSA3 SH3D2C","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors propose the following model: upon ligand activation, HGF receptor becomes tyrosine phosphorylated, binds and phosphorylates Cbl, which in turn targets the receptor to clathrin-coated pits by recruiting the CIN85\\u2013endophilin complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2457,"ComplexName":"CIN85-SH3GL3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q96B97;Q99963","subunits.Entrez.IDs.":"30011;6457","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0096- pull down; MI:0018- two hybrid","GO.ID":"GO:0006900;GO:0016050;GO:0006897","GO.description":"membrane budding;vesicle organization;endocytosis","FunCat.ID":"20.09.07.25;20.09.18.09.01","FunCat.description":"vesicle formation;endocytosis","PubMed.ID":11894096,"subunits.Protein.name.":"SH3 domain-containing kinase-binding protein 1;Endophilin-A3","subunits.Gene.name.":"SH3KBP1;SH3GL3","subunits.Gene.name.syn.":"CIN85;CNSA3 SH3D2C","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2462,"ComplexName":"Caveolin-1 homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q03135","subunits.Entrez.IDs.":"857","Protein.complex.purification.method":"MI:0030- cross-linking studies","GO.ID":"GO:0042632;GO:0005783","GO.description":"cholesterol homeostasis;endoplasmic reticulum","FunCat.ID":"34.01.07;70.07","FunCat.description":"cholesterol homeostasis;endoplasmic reticulum","PubMed.ID":15782218,"subunits.Protein.name.":"Caveolin-1","subunits.Gene.name.":"CAV1","subunits.Gene.name.syn.":"CAV","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":2470,"ComplexName":"p130Cas-ER-alpha-cSrc-kinase- PI3-kinase p85-subunit complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P03372;P12931;P27986;P56945","subunits.Entrez.IDs.":"2099;6714;5295;9564","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0007049;GO:0006468;GO:0006470;GO:0046777;GO:0023052;GO:0009755","GO.description":"cell cycle;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;signaling;hormone-mediated signaling pathway","FunCat.ID":"10.03;14.07.03;30.01;30.01.09.08","FunCat.description":"cell cycle;modification by phosphorylation, dephosphorylation, autophosphorylation;cellular signalling;hormone mediated signal transduction","PubMed.ID":15020686,"subunits.Protein.name.":"Estrogen receptor;Proto-oncogene tyrosine-protein kinase Src;Phosphatidylinositol 3-kinase regulatory subunit alpha;Breast cancer anti-estrogen resistance protein 1","subunits.Gene.name.":"ESR1;SRC;PIK3R1;BCAR1","subunits.Gene.name.syn.":"ESR, NR3A1;SRC1;GRB1;CAS CASS1 CRKAS","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors suggest that estradiol triggers association of ER-alpha, c-Src, the p85 subunit of PI 3-kinase (PI3K) and p130Cas in a macromolecular complex and activates the c-Src kinase leading to p130Cas-dependent Erk1/2 phosphorylation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2471,"ComplexName":"SRC-PRKCD-CDCP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12931;Q05655;Q9H5V8","subunits.Entrez.IDs.":"6714;5580;64866","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0005515","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;protein binding","FunCat.ID":"14.07.03;16.01","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;protein binding","PubMed.ID":15851033,"subunits.Protein.name.":"Proto-oncogene tyrosine-protein kinase Src;Protein kinase C delta type ;CUB domain-containing protein 1","subunits.Gene.name.":"SRC;PRKCD;CDCP1","subunits.Gene.name.syn.":"SRC1;;TRASK","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2475,"ComplexName":"Cbl-Crkl-Rapgef1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P22682;P47941;Q91ZZ2","subunits.Entrez.IDs.":"12402;12929;107746","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0007229;GO:0016477","GO.description":"integrin-mediated signaling pathway;cell migration","FunCat.ID":"30.05.02.26;34.05.01","FunCat.description":"integrin receptor signalling pathway;cell migration","PubMed.ID":10608804,"subunits.Protein.name.":"E3 ubiquitin-protein ligase CBL;Crk-like protein;Guanine nucleotide exchange factor","subunits.Gene.name.":"Cbl;Crkl;Rapgef1","subunits.Gene.name.syn.":"None;Crkol;Grf2","Disease.comment":"Crkl is one of the major tyrosine phosphoproteins detected in cells from patients with chronic myelogenous leukemia.","Subunits.comment":"None","Complex.comment":"The complex may be involved in migration signaling.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2476,"ComplexName":"CRKL-PDGFRA-CRK-RAPGEF1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P16234;P46108;P46109;Q13905","subunits.Entrez.IDs.":"5156;1398;1399;2889","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0035556","GO.description":"intracellular signal transduction","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":9546424,"subunits.Protein.name.":"Platelet-derived growth factor receptor alpha ;Adapter molecule crk;Crk-like protein;Rap guanine nucleotide exchange factor 1","subunits.Gene.name.":"PDGFRA;CRK;CRKL;RAPGEF1","subunits.Gene.name.syn.":"PDGFR2 RHEPDGFRA;None;;GRF2","Disease.comment":"None","Subunits.comment":"CrkI and CrkII are splice variants of the Crk gene, only variant CrkII has been identified as component of the complex.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2480,"ComplexName":"CIN85 complex (CIN85, CRK, BCAR1, CBL, PIK3R1, GRB2, SOS1)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P22681;P27986;P46108;P56945;P62993;Q07889;Q96B97","subunits.Entrez.IDs.":"867;5295;1398;9564;2885;6654;30011","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007169","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway","FunCat.ID":"30.05.01.12","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways","PubMed.ID":11071869,"subunits.Protein.name.":"E3 ubiquitin-protein ligase CBL;Phosphatidylinositol 3-kinase regulatory subunit alpha;Adapter molecule crk;Breast cancer anti-estrogen resistance protein 1;Growth factor receptor-bound protein 2;Son of sevenless homolog 1;SH3 domain-containing kinase-binding protein 1","subunits.Gene.name.":"CBL;PIK3R1;CRK;BCAR1;GRB2;SOS1;SH3KBP1","subunits.Gene.name.syn.":"CBL2, RNF55;GRB1;None;CAS CASS1 CRKAS;ASH;None;CIN85","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors propose that CIN85 acts as a mediator to couple the c-Cbl signaling pathway with other pathways through its multiple protein complexes, thereby leading to their interplay.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2486,"ComplexName":"GIPC1-LHCGR complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14908;P22888","subunits.Entrez.IDs.":"10755;3973","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0096- pull down; MI:0018- two hybrid","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0006897","GO.description":"intracellular protein transport;protein targeting;protein transport;endocytosis","FunCat.ID":"14.04;20.01.10;20.09.18.09.01","FunCat.description":"protein targeting, sorting and translocation;protein transport;endocytosis","PubMed.ID":14507927,"subunits.Protein.name.":"PDZ domain-containing protein GIPC1 ;Lutropin-choriogonadotropic hormone receptor","subunits.Gene.name.":"GIPC1;LHCGR","subunits.Gene.name.syn.":"C19orf3 GIPC RGS19IP1;LCGR LGR2 LHRHR","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This protein is involved in the post-endocytotic trafficking of the internalized hCG and in maintaining the levels of cell surface hLHR during endocytosis of the bound hormone.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2487,"ComplexName":"GIPC1-NTRK1-RGS19 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14908;P04629;P49795","subunits.Entrez.IDs.":"10755;4914;10287","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000301","GO.description":"retrograde transport, vesicle recycling within Golgi","FunCat.ID":"20.09.07.07","FunCat.description":"retrograde transport","PubMed.ID":11251075,"subunits.Protein.name.":"PDZ domain-containing protein GIPC1 ;High affinity nerve growth factor receptor ;Regulator of G-protein signaling 19","subunits.Gene.name.":"GIPC1;NTRK1;RGS19","subunits.Gene.name.syn.":"C19orf3 GIPC RGS19IP1;MTC TRK TRKA;GAIP GNAI3IP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"GIPC forms a complex with GAIP and the TrkA receptor and colocalizes with phosphoryated TrkA in retrograde transport vesicles.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2489,"ComplexName":"NCR3-CD247 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14931;P20963","subunits.Entrez.IDs.":"259197;919","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006915","GO.description":"apoptotic process","FunCat.ID":"40.10.02","FunCat.description":"apoptosis (type I programmed cell death)","PubMed.ID":15821739,"subunits.Protein.name.":"Natural cytotoxicity triggering receptor 3 ;T-cell surface glycoprotein CD3 zeta chain","subunits.Gene.name.":"NCR3;CD247","subunits.Gene.name.syn.":"1C7 LY117;CD3Z T3Z TCRZ","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"NKp30, similar to other NK triggering receptors including CD16 (34) (35) and NKp46 (23), can transduce activating signals via association with the ITAM-containing CD3{zeta} polypeptides (PMID: 10562324).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2510,"ComplexName":"ZAP70-CRKL-WIPF1-WAS complex","Organism":"Human","Synonyms":"ZAP-70-CrkL-WIP-WASP complex","Cell.line":"None","subunits.UniProt.IDs.":"O43516;P42768;P43403;P46109","subunits.Entrez.IDs.":"7456;7454;7535;1399","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0035556","GO.description":"intracellular signal transduction","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":12504004,"subunits.Protein.name.":"WAS/WASL-interacting protein family member 1;Wiskott-Aldrich syndrome protein;Tyrosine-protein kinase ZAP-70 ;Crk-like protein","subunits.Gene.name.":"WIPF1;WAS;ZAP70;CRKL","subunits.Gene.name.syn.":"WASPIP WIP;IMD2;SRK;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2511,"ComplexName":"CRKL-WIPF1-WAS complex","Organism":"Human","Synonyms":"CrkL-WIP-WASP complex","Cell.line":"None","subunits.UniProt.IDs.":"O43516;P42768;P46109","subunits.Entrez.IDs.":"7456;7454;1399","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0035556","GO.description":"intracellular signal transduction","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":12504004,"subunits.Protein.name.":"WAS/WASL-interacting protein family member 1;Wiskott-Aldrich syndrome protein;Crk-like protein","subunits.Gene.name.":"WIPF1;WAS;CRKL","subunits.Gene.name.syn.":"WASPIP WIP;IMD2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2513,"ComplexName":"N-WASp homomer","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00401","subunits.Entrez.IDs.":"8976","Protein.complex.purification.method":"MI:0031- protein cross-linking with a bifunctional reagent","GO.ID":"GO:0030036","GO.description":"actin cytoskeleton organization","FunCat.ID":"42.04.03","FunCat.description":"actin cytoskeleton","PubMed.ID":10781580,"subunits.Protein.name.":"Neural Wiskott-Aldrich syndrome protein","subunits.Gene.name.":"WASL","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"N-WASp undergoes self-association upon increasing concentration and the monomeric form activates actin polymerization and is favored by Grb2 binding.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":2528,"ComplexName":"ERBB2-MEMO-SHC complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04626;P29353;Q9Y316","subunits.Entrez.IDs.":"2064;6464;51072","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006928;GO:0000226","GO.description":"movement of cell or subcellular component;microtubule cytoskeleton organization","FunCat.ID":"34.05;42.04.05","FunCat.description":"cell motility;microtubule cytoskeleton","PubMed.ID":15156151,"subunits.Protein.name.":"Receptor tyrosine-protein kinase erbB-2;SHC-transforming protein 1;Protein MEMO1","subunits.Gene.name.":"ERBB2;SHC1;MEMO1","subunits.Gene.name.syn.":"HER2, MLN19, NEU, NGL;SHC SHCA;C2orf4 MEMO NS5ATP7","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results suggest that the Shc adaptor protein mediates binding of Memo to the phospho-YD (Tyr 1227) residue of ErbB2.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2529,"ComplexName":"LAT-PLC-gamma-1-p85-GRB2-CBL-VAV-SLP-76 signaling complex, C305 activated","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43561;P15498;P19174;P22681;P27986;P62993;Q13094","subunits.Entrez.IDs.":"27040;7409;5335;867;5295;2885;3937","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007169;GO:0050896;GO:0048015","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway;response to stimulus;phosphatidylinositol-mediated signaling","FunCat.ID":"30.05.01.12;36.25","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways;animal specific systemic sensing and response","PubMed.ID":9489702,"subunits.Protein.name.":"Linker for activation of T-cells family member 1;Proto-oncogene vav;1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 ;E3 ubiquitin-protein ligase CBL;Phosphatidylinositol 3-kinase regulatory subunit alpha;Growth factor receptor-bound protein 2;Lymphocyte cytosolic protein 2","subunits.Gene.name.":"LAT;VAV1;PLCG1;CBL;PIK3R1;GRB2;LCP2","subunits.Gene.name.syn.":"None;VAV;PLC1;CBL2, RNF55;GRB1;ASH;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors show that upon tyrosine phosphorylation, LAT binds Grb2, PLC-gamma1, the p85 subunit of PI3K, and other critical signaling molecules. They provide evidence that LAT plays an important role in linking the TCR to cellular activation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2534,"ComplexName":"Cbl-SLP-76-Grb2 complex, Fc receptor gamma-R1 stimulated","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P22681;P62993;Q13094","subunits.Entrez.IDs.":"867;2885;3937","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007169;GO:0006955","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway;immune response","FunCat.ID":"30.05.01.12;36.25.16","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways;immune response","PubMed.ID":9716598,"subunits.Protein.name.":"E3 ubiquitin-protein ligase CBL;Growth factor receptor-bound protein 2;Lymphocyte cytosolic protein 2","subunits.Gene.name.":"CBL;GRB2;LCP2","subunits.Gene.name.syn.":"CBL2, RNF55;ASH;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors demonstrate that the kinetics of SLP-76 phosphorylation parallels the kinetics of Cbl phosphorylation, suggesting a link between these two adapter proteins in the Fc gamma RI-signaling cascade.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2535,"ComplexName":"SLP-76-Cbl-Grb2-Shc complex, Fc receptor gamma-R1 stimulated","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P22681;P29353;P62993;Q13094","subunits.Entrez.IDs.":"867;6464;2885;3937","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007169;GO:0006955","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway;immune response","FunCat.ID":"30.05.01.12;36.25.16","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways;immune response","PubMed.ID":9716598,"subunits.Protein.name.":"E3 ubiquitin-protein ligase CBL;SHC-transforming protein 1;Growth factor receptor-bound protein 2;Lymphocyte cytosolic protein 2","subunits.Gene.name.":"CBL;SHC1;GRB2;LCP2","subunits.Gene.name.syn.":"CBL2, RNF55;SHC SHCA;ASH;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors propose that the association of Grb2 and Shc with SLP-76 and Cbl may serve as a repository for Grb2 and Shc, regulating their association with Sos and subsequent activation of Ras.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2536,"ComplexName":"PLC-gamma-2-SLP-76-Lyn-Grb2 complex","Organism":"Human","Synonyms":"None","Cell.line":"platelet","subunits.UniProt.IDs.":"P07948;P16885;P62993;Q13094","subunits.Entrez.IDs.":"4067;5336;2885;3937","Protein.complex.purification.method":"MI:0096-pull down","GO.ID":"GO:0007169;GO:0007596;GO:0048015","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway;blood coagulation;phosphatidylinositol-mediated signaling","FunCat.ID":"30.05.01.12;36.25.16.09","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways;blood coagulation","PubMed.ID":10469124,"subunits.Protein.name.":"Tyrosine-protein kinase Lyn;1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2;Growth factor receptor-bound protein 2;Lymphocyte cytosolic protein 2","subunits.Gene.name.":"LYN;PLCG2;GRB2;LCP2","subunits.Gene.name.syn.":"JTK8;None;ASH;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Analyses done with different GST-PLC-gamma-2 fusion proteins from resting and CRP (collagen-related peptide) stimulated platelets.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2537,"ComplexName":"PKC-alpha-PLD1-PLC-gamma-2 signaling complex, lacritin stimulated","Organism":"Human","Synonyms":"None","Cell.line":"epithelium","subunits.UniProt.IDs.":"P16885;P17252;Q13393","subunits.Entrez.IDs.":"5336;5578;5337","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0019722;GO:0030855;GO:0002009;GO:0005794;GO:0048015","GO.description":"calcium-mediated signaling;epithelial cell differentiation;morphogenesis of an epithelium;Golgi apparatus;phosphatidylinositol-mediated signaling","FunCat.ID":"30.01.09.03;45.03.09;70.08","FunCat.description":"Ca2+ mediated signal transduction;epithelium;Golgi","PubMed.ID":16923831,"subunits.Protein.name.":"1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2;Protein kinase C alpha type;Phospholipase D1","subunits.Gene.name.":"PLCG2;PRKCA;PLD1","subunits.Gene.name.syn.":"None;PKCA PRKACA;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Lacritin is described as mitogenic for a small subset of epithelial cell lines derived mainly from the nongermative epithelia that normally contact lacritin during its outward glandular flow. The authors propose that lacritin signaling  stimulates the formation of a transient perinuclear Golgi complex of PKC-alpha, PLD1, and PLC-gamma-2. This activates PLD1 of the mTOR pathway. Some PLC-gamma-2 activation and considerable IP3 generation were detected. Ca(2+) mobilization may then be a consequence.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2539,"ComplexName":"Lab-Grb2 complex, BCR stimulated","Organism":"Mouse","Synonyms":"None","Cell.line":"B-cell","subunits.UniProt.IDs.":"Q60631;Q9JHL0","subunits.Entrez.IDs.":"14784;56743","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0023052;GO:0019724;GO:0030183;GO:0005886","GO.description":"signaling;B cell mediated immunity;B cell differentiation;plasma membrane","FunCat.ID":"30.01;36.25.16.03.01;43.03.07.02.01.01;70.02","FunCat.description":"cellular signalling;humoral response (B-cells);B-cell;eukaryotic plasma membrane / membrane attached","PubMed.ID":12514734,"subunits.Protein.name.":"Growth factor receptor-bound protein 2;Linker for activation of T-cells family member 2","subunits.Gene.name.":"Grb2;Lat2","subunits.Gene.name.syn.":"None;Lab Ntal Wbscr15 Wbscr5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"LAB could be phosphorylated upon stimulation of splenocytes via the BCR by the Syk tyrosine kinase. The authors describe that LAB subsequently associates with Grb2, thereby recruiting Grb2 and Grb2-associated proteins to lipid rafts at the membrane.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2540,"ComplexName":"BCR-ABL (p210 fusion protein)-GRB2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"A1Z199;P62993","subunits.Entrez.IDs.":"None;2885","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0023052;GO:0007186","GO.description":"signaling;G-protein coupled receptor signaling pathway","FunCat.ID":"30.01;30.05.02.24","FunCat.description":"cellular signalling;G-protein coupled receptor signalling pathway","PubMed.ID":8112292,"subunits.Protein.name.":"BCR/ABL p210 fusion protein ;Growth factor receptor-bound protein 2","subunits.Gene.name.":"BCR/ABL fu;GRB2","subunits.Gene.name.syn.":";ASH","Disease.comment":"Chimeric bcr-abl oncogene is involved in Philadelphia chromosome positive (Ph+) chronic myelogenous leukemia (CML) and acute lymphoblastic leukemia (Ph+ ALL).","Subunits.comment":"None","Complex.comment":"It was shown that Grb2 binds to the Tyr177 autophosphorylation site on Bcr-Abl.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2541,"ComplexName":"HGF-Met complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P08581;P14210","subunits.Entrez.IDs.":"4233;3082","Protein.complex.purification.method":"MI:0411- enzyme linked immunosorbent assay","GO.ID":"GO:0007169","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway","FunCat.ID":"30.05.01.12","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways","PubMed.ID":15161915,"subunits.Protein.name.":"Hepatocyte growth factor receptor;Hepatocyte growth factor","subunits.Gene.name.":"MET;HGF","subunits.Gene.name.syn.":"None;HPTA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"HGF interacts with the extracellular domain of Met, resulting in the activation of Met and subsequent downstream functions. The authors demonstrate that that copper(II) inhibits HGF/Met interaction.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2542,"ComplexName":"EGFR-CBL-GRB2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P00533;P22681;P62993","subunits.Entrez.IDs.":"1956;867;2885","Protein.complex.purification.method":"MI:0055- fluorescent resonance energy transfer","GO.ID":"GO:0035556;GO:0005768","GO.description":"intracellular signal transduction;endosome","FunCat.ID":"30.01;70.22","FunCat.description":"cellular signalling;endosome","PubMed.ID":15782196,"subunits.Protein.name.":"Epidermal growth factor receptor;E3 ubiquitin-protein ligase CBL;Growth factor receptor-bound protein 2","subunits.Gene.name.":"EGFR;CBL;GRB2","subunits.Gene.name.syn.":"ERBB, ERBB1, HER1;CBL2, RNF55;ASH","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The energy transfer analysis results prompted the authors to support the previously proposed model that although Cbl is capable of direct binding to EGFR, it preferentially binds receptors indirectly through Grb2.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2545,"ComplexName":"Grb2-mSos1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q60631;Q62245","subunits.Entrez.IDs.":"14784;20662","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0027- cosedimentation","GO.ID":"GO:0035556","GO.description":"intracellular signal transduction","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":8940013,"subunits.Protein.name.":"Growth factor receptor-bound protein 2;Son of sevenless homolog 1","subunits.Gene.name.":"Grb2;Sos1","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The stoichiometry of the Grb2-mSos1 complex was 1:1. Grb2-mSos1 is a stable complex and both proteins can exist in a constitutive complex in unstimulated cells.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2547,"ComplexName":"PLC-gamma-1-SLP-76-SOS1-LAT complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43561;P19174;Q07889;Q13094","subunits.Entrez.IDs.":"27040;5335;6654;3937","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007169;GO:0050896;GO:0048015","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway;response to stimulus;phosphatidylinositol-mediated signaling","FunCat.ID":"30.05.01.12;36.25","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways;animal specific systemic sensing and response","PubMed.ID":15696170,"subunits.Protein.name.":"Linker for activation of T-cells family member 1;1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 ;Son of sevenless homolog 1;Lymphocyte cytosolic protein 2","subunits.Gene.name.":"LAT;PLCG1;SOS1;LCP2","subunits.Gene.name.syn.":"None;PLC1;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In a supplementary figure the authors show that PLC-gamma-1, SLP-76 and Sos1 are effectively recruited to LAT in the absence of Dyn2. The results show further that when Dyn2 was present, several tyrosine-phosphorylated proteins coimmunoprecipitated with Lat, including SLP76, PLC-gamma1 and several other unidentified proteins. PLC-gamma-1 total tyrosine phosphorylation was diminished in the absence of Dyn2.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2548,"ComplexName":"Egfr-Grb2-mSos1 complex, EGF stimulated","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q01279;Q2M4G6;Q60631","subunits.Entrez.IDs.":"13649;20662;14784","Protein.complex.purification.method":"MI:0107- surface plasmon resonance","GO.ID":"GO:0007186;GO:0007173","GO.description":"G-protein coupled receptor signaling pathway;epidermal growth factor receptor signaling pathway","FunCat.ID":"30.05.02.24;30.05.01.12.01","FunCat.description":"G-protein coupled receptor signalling pathway;EGF-receptor signalling pathway","PubMed.ID":8940013,"subunits.Protein.name.":"Epidermal growth factor receptor ;Son of sevenless like-protein 1 ;Growth factor receptor-bound protein 2","subunits.Gene.name.":"Egfr;Sos1;Grb2","subunits.Gene.name.syn.":";;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors analysed the binding of Grb2-mSos1 to different phosphopeptides Shc pYVNV, EGFR1068, IR-PEP. Shc pYVNV showed the highest affinity.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2550,"ComplexName":"Frs2-Grb2-Shp2 complex, FGF stimulated","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P35235;Q60631;Q8C180","subunits.Entrez.IDs.":"19247;14784;327826","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0008543","GO.description":"fibroblast growth factor receptor signaling pathway","FunCat.ID":"30.05.01.12.03","FunCat.description":"FGF-receptor signalling pathway","PubMed.ID":9632781,"subunits.Protein.name.":"Tyrosine-protein phosphatase non-receptor type 11;Growth factor receptor-bound protein 2;Fibroblast growth factor receptor substrate 2","subunits.Gene.name.":"Ptpn11;Grb2;Frs2","subunits.Gene.name.syn.":"None;None;Frs2a","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"On the basis of further experiments the authors conclude that FGF stimulation leads to tyrosine phosphorylation of Shp2 and association with the Grb2-Sos complex.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2551,"ComplexName":"PDGFRA-PLC-gamma-1-PI3K-SHP-2 complex, PDGF stimulated","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P16234;P19174;P27986;Q06124","subunits.Entrez.IDs.":"5156;5335;5295;5781","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007169","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway","FunCat.ID":"30.05.01.12","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways","PubMed.ID":8943348,"subunits.Protein.name.":"Platelet-derived growth factor receptor alpha ;1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 ;Phosphatidylinositol 3-kinase regulatory subunit alpha;Tyrosine-protein phosphatase non-receptor type 11","subunits.Gene.name.":"PDGFRA;PLCG1;PIK3R1;PTPN11","subunits.Gene.name.syn.":"PDGFR2 RHEPDGFRA;PLC1;GRB1;PTP2C SHPTP2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Mutational analysis shows that Y720 of PDGFRA is required for binding of SHP-2 to the PDGFRA but not for the association of PLCg, the p85 subunit of PI3K, or Src. The data strongly suggest that SHP-2 must bind to the PDGFRA to be efficiently tyrosine phosphorylated.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2552,"ComplexName":"Il3rb1-Shc complex, IL-3 stimulated","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P26955;P98083","subunits.Entrez.IDs.":"12983;20416","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":10891441,"subunits.Protein.name.":"Cytokine receptor common subunit beta ;SHC-transforming protein 1","subunits.Gene.name.":"Csf2rb;Shc1","subunits.Gene.name.syn.":"Aic2b Csf2rb1 Il3rb1;Shc ShcA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors describe that Shc-Ship and Shc-Il3rb1 exist as separate complexes. They further propose that the interaction between Shc and the Il3rb1 subunit seems to be transient and of a lower affinity than the association of Shc with Ship.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2553,"ComplexName":"Shc-Grb2-mSos1 complex, EGF stimulated","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P98083;Q2M4G6;Q60631","subunits.Entrez.IDs.":"20416;20662;14784","Protein.complex.purification.method":"MI:0107- surface plasmon resonance","GO.ID":"GO:0007186;GO:0007169","GO.description":"G-protein coupled receptor signaling pathway;transmembrane receptor protein tyrosine kinase signaling pathway","FunCat.ID":"30.05.02.24;30.05.01.12","FunCat.description":"G-protein coupled receptor signalling pathway;transmembrane receptor protein tyrosine kinase signalling pathways","PubMed.ID":8940013,"subunits.Protein.name.":"SHC-transforming protein 1 ;Son of sevenless like-protein 1 ;Growth factor receptor-bound protein 2","subunits.Gene.name.":"Shc1;Sos1;Grb2","subunits.Gene.name.syn.":"Shc ShcA;;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors analysed the binding of Grb2-mSos1 to different phosphopeptides Shc pYVNV, EGFR1068, IR-PEP. Shc pYVNV showed the highest affinity.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2558,"ComplexName":"p56(Lck)-CAML complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06240;P49070","subunits.Entrez.IDs.":"16818;12328","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0007169;GO:0030217","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway;T cell differentiation","FunCat.ID":"30.05.01.12;43.03.07.02.01.02","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways;T-cell","PubMed.ID":16111633,"subunits.Protein.name.":"Proto-oncogene tyrosine-protein kinase LCK ;Calcium signal-modulating cyclophilin ligand","subunits.Gene.name.":"Lck;Camlg","subunits.Gene.name.syn.":"Lsk-t;Caml","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results of the authors suggest that CAML interacts with p56Lck to regulate its subcellular localization and timely activation of the kinase in response to TCR induction. They propose that CAML functions to maintain the proper storage of p56Lck to prevent excessive activation and to ensure carefully measured release of the kinase in response to TCR stimulation, thereby facilitating productive T cell activation with less cell death.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2559,"ComplexName":"p56(LCK)-CAML complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06239;P49069","subunits.Entrez.IDs.":"3932;819","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007169;GO:0030217","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway;T cell differentiation","FunCat.ID":"30.05.01.12;43.03.07.02.01.02","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways;T-cell","PubMed.ID":16111633,"subunits.Protein.name.":"Tyrosine-protein kinase Lck;Calcium signal-modulating cyclophilin ligand","subunits.Gene.name.":"LCK;CAMLG","subunits.Gene.name.syn.":"None;CAML","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results of the authors suggest that CAML interacts with p56Lck to regulate its subcellular localization and timely activation of the kinase in response to TCR induction. They propose that CAML functions to maintain the proper storage of p56Lck to prevent excessive activation and to ensure carefully measured release of the kinase in response to TCR stimulation, thereby facilitating productive T cell activation with less cell death.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2560,"ComplexName":"Nephrin-cadherin complex (Nphs1, Ctnnd1, ZO-1, Cd2ap)","Organism":"Dog","Synonyms":"None","Cell.line":"MDCK cells, epithelium","subunits.UniProt.IDs.":"O97758;P30999;Q9JLQ0;Q9QZS7","subunits.Entrez.IDs.":"403752;12388;12488;54631","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0016337;GO:0005911","GO.description":"single organismal cell-cell adhesion;cell-cell junction","FunCat.ID":"34.07.01;70.06.04","FunCat.description":"cell-cell adhesion;intercellular junction (gap junction/adherens junction)","PubMed.ID":15331416,"subunits.Protein.name.":"Tight junction protein ZO-1 ;Catenin delta-1;CD2-associated protein;Nephrin","subunits.Gene.name.":"TJP1;Ctnnd1;Cd2ap;Nphs1","subunits.Gene.name.syn.":"ZO1;Catns Kiaa0384;Mets1;Nphn","Disease.comment":"None","Subunits.comment":"Since Cd2ap, Ctnnd1 and Nphs1 from dog were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.","Complex.comment":"None","SWISSPROT.organism":"Canis lupus familiaris (Dog) (Canis familiaris);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2561,"ComplexName":"Nephrin-cadherin complex (Nphs1, Cask, Cd2ap)","Organism":"Rat","Synonyms":"None","Cell.line":"kidney epithelium","subunits.UniProt.IDs.":"Q62915;Q80ZE7;Q9R044","subunits.Entrez.IDs.":"29647;316258;64563","Protein.complex.purification.method":"MI:0096-pull down","GO.ID":"GO:0016337;GO:0045216;GO:0007043;GO:0005911","GO.description":"single organismal cell-cell adhesion;cell-cell junction organization;cell-cell junction assembly;cell-cell junction","FunCat.ID":"34.07.01;42.06.04;70.06.04","FunCat.description":"cell-cell adhesion;intercellular junction (gap junction/adherens junction);intercellular junction (gap junction/adherens junction)","PubMed.ID":15331416,"subunits.Protein.name.":"Peripheral plasma membrane protein CASK;CD2AP/CMS;Nephrin","subunits.Gene.name.":"Cask;Cd2ap;Nphs1","subunits.Gene.name.syn.":"None;None;Nphn","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors discuss eight bands stained with GelCode Blue, but describe only the 110kd band analysed by MS as CASK. Immunofluorescence labeling of cryosections from rat kidney lead to the conclusion that CASK is expressed in podocytes and MDCK-nephrin cells in the appropriate location to interact with nephrin.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2562,"ComplexName":"Nephrin-cadherin complex (Nphs1, Ctnnd1, Cdh3, Cd2ap)","Organism":"Dog","Synonyms":"None","Cell.line":"MDCK cells, epithelium","subunits.UniProt.IDs.":"P10287;P30999;Q9JLQ0;Q9QZS7","subunits.Entrez.IDs.":"12560;12388;12488;54631","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016337;GO:0005911","GO.description":"single organismal cell-cell adhesion;cell-cell junction","FunCat.ID":"34.07.01;70.06.04","FunCat.description":"cell-cell adhesion;intercellular junction (gap junction/adherens junction)","PubMed.ID":15331416,"subunits.Protein.name.":"Cadherin-3 ;Catenin delta-1;CD2-associated protein;Nephrin","subunits.Gene.name.":"Cdh3;Ctnnd1;Cd2ap;Nphs1","subunits.Gene.name.syn.":"Cdhp;Catns Kiaa0384;Mets1;Nphn","Disease.comment":"None","Subunits.comment":"Since Cd2ap, Cdh3, Ctnnd1 and Nphs1 from dog were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2563,"ComplexName":"FGFR2-c-Cbl-Lyn-Fyn complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06241;P07948;P21802;P22681","subunits.Entrez.IDs.":"2534;4067;2263;867","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0043161;GO:0006511;GO:0023052;GO:0008543;GO:0001649","GO.description":"proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;signaling;fibroblast growth factor receptor signaling pathway;osteoblast differentiation","FunCat.ID":"14.13.01.01;30.01;30.05.01.12.03;43.03.17","FunCat.description":"proteasomal degradation (ubiquitin/proteasomal pathway);cellular signalling;FGF-receptor signalling pathway;structural cell of tissue (fibroblast, osteoblast, etc.)","PubMed.ID":15190072,"subunits.Protein.name.":"Tyrosine-protein kinase Fyn;Tyrosine-protein kinase Lyn;Fibroblast growth factor receptor 2 ;E3 ubiquitin-protein ligase CBL","subunits.Gene.name.":"FYN;LYN;FGFR2;CBL","subunits.Gene.name.syn.":"None;JTK8;BEK KGFR KSAM;CBL2, RNF55","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results indicate that FGFR2 interacts with Lyn and Fyn and with c-Cbl, which can then mediate proteasome degradation of these three molecules in osteoblasts. The authors propose a mechanism by which constitutive FGFR2 activation in osteoblasts induces c-Cbl-dependent recruitment of FGFR2, Lyn, and Fyn, leading to their proteasome degradation, decreased kinase activity, and hence increased osteoblast differentiation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2564,"ComplexName":"p21(ras)GAP-Fyn-Lyn-Yes complex, thrombin stimulated","Organism":"Human","Synonyms":"None","Cell.line":"platelet","subunits.UniProt.IDs.":"P06241;P07947;P07948;P20936","subunits.Entrez.IDs.":"2534;7525;4067;5921","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0023052;GO:0007596","GO.description":"signaling;blood coagulation","FunCat.ID":"30.01;36.25.16.09","FunCat.description":"cellular signalling;blood coagulation","PubMed.ID":1544885,"subunits.Protein.name.":"Tyrosine-protein kinase Fyn;Tyrosine-protein kinase Yes;Tyrosine-protein kinase Lyn;Ras GTPase-activating protein 1","subunits.Gene.name.":"FYN;YES1;LYN;RASA1","subunits.Gene.name.syn.":"None;YES;JTK8;GAP, RASA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors showed that Fyn, Lyn,and Yes are associated with GAP in thrombin-stimulatedplatelets. They could not distinguish whether this complex is preformed in restingplatelets or whether the kinases associate with GAP followingactivation with thrombin.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2565,"ComplexName":"CD20-LCK-LYN-FYN-p75/80 complex, (Raji human B cell line)","Organism":"Human","Synonyms":"None","Cell.line":"Raji cells","subunits.UniProt.IDs.":"P06239;P06241;P07948;P11836","subunits.Entrez.IDs.":"3932;2534;4067;931","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":7545683,"subunits.Protein.name.":"Tyrosine-protein kinase Lck;Tyrosine-protein kinase Fyn;Tyrosine-protein kinase Lyn;B-lymphocyte antigen CD20","subunits.Gene.name.":"LCK;FYN;LYN;MS4A1","subunits.Gene.name.syn.":"None;None;JTK8;CD20","Disease.comment":"None","Subunits.comment":"At the time of annotation, the identity of the additional member p75/80 of the protein complex was not known.","Complex.comment":"Lyn accounted for most of the PTK activity in the CD20 complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2567,"ComplexName":"NCAM140-p59(fyn)-p125(fak) signaling complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"O35346;P13596;Q62844","subunits.Entrez.IDs.":"25614;24586;25150","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0023052;GO:0007155;GO:0010183","GO.description":"signaling;cell adhesion;pollen tube guidance","FunCat.ID":"30.01;34.07;40.01.03.03","FunCat.description":"cellular signalling;cell adhesion;guidance of longitudinal cell extension (e.g. pollen tube guidance, axonal pathfinding)","PubMed.ID":9079653,"subunits.Protein.name.":"Focal adhesion kinase 1 ;Neural cell adhesion molecule 1 ;Tyrosine-protein kinase Fyn","subunits.Gene.name.":"Ptk2;Ncam1;Fyn","subunits.Gene.name.syn.":"Fak Fak1;Ncam;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"p59 (fyn) appeared to be constitutively bound to NCAM140, either directly or indirectly, whereas p125fak was recruited to the NCAM complex. The authors showed that antibody-mediated ligation of cell surface NCAM140 or stimulation with soluble NCAM fusion protein led to a transient increase in tyrosine phosphorylation of both p125 (fak) and p59 (fyn), suggesting that activation of these nonreceptor tyrosine kinases is a proximal event in the NCAM signal transduction pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2568,"ComplexName":"Slam-SAP-FynT complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O88890;P39688;Q9QUM4","subunits.Entrez.IDs.":"20400;14360;27218","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0023052;GO:0016064;GO:0005125","GO.description":"signaling;immunoglobulin mediated immune response;cytokine activity","FunCat.ID":"30.01;36.25.16.03;40.02.03.01","FunCat.description":"cellular signalling;adaptive immune response (vertebrates);cytokines (interleukines, colony stimulating factors, etc.)","PubMed.ID":11477403,"subunits.Protein.name.":"SH2 domain-containing protein 1A;Tyrosine-protein kinase Fyn;Signaling lymphocytic activation molecule","subunits.Gene.name.":"Sh2d1a;Fyn;Slamf1","subunits.Gene.name.syn.":"Xlp;None;Slam","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"FynT was clearly associated with Tac-SLAM in cells that were coexpressing SAP. The analysis of the role of FynT in SLAM-SAP signaling showed that Fyn was absolutely required for antibody-mediated tyrosine phosphorylation of SLAM in thymocytes. SLAM tyrosine phosphorylation is not required for SAP binding, the association between SLAM and SAP was Fyn-independent.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2569,"ComplexName":"Slam-SAP-SHIP complex","Organism":"Mouse","Synonyms":"None","Cell.line":"lymphocyte","subunits.UniProt.IDs.":"O88890;Q9ES52;Q9QUM4","subunits.Entrez.IDs.":"20400;16331;27218","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0023052;GO:0016064;GO:0005125","GO.description":"signaling;immunoglobulin mediated immune response;cytokine activity","FunCat.ID":"30.01;36.25.16.03;40.02.03.01","FunCat.description":"cellular signalling;adaptive immune response (vertebrates);cytokines (interleukines, colony stimulating factors, etc.)","PubMed.ID":11477403,"subunits.Protein.name.":"SH2 domain-containing protein 1A;Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1;Signaling lymphocytic activation molecule","subunits.Gene.name.":"Sh2d1a;Inpp5d;Slamf1","subunits.Gene.name.syn.":"Xlp;7a33 Ship Ship1;Slam","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors showed that SHIP appeared to be the intermediate molecule that linked SLAM-SAP to Dok-related adaptors and RasGAP.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2570,"ComplexName":"Slam-SAP complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O88890;Q9QUM4","subunits.Entrez.IDs.":"20400;27218","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0023052;GO:0016064;GO:0005125","GO.description":"signaling;immunoglobulin mediated immune response;cytokine activity","FunCat.ID":"30.01;36.25.16.03;40.02.03.01","FunCat.description":"cellular signalling;adaptive immune response (vertebrates);cytokines (interleukines, colony stimulating factors, etc.)","PubMed.ID":11477403,"subunits.Protein.name.":"SH2 domain-containing protein 1A;Signaling lymphocytic activation molecule","subunits.Gene.name.":"Sh2d1a;Slamf1","subunits.Gene.name.syn.":"Xlp;Slam","Disease.comment":"Sh2d1a is involved in X-linked lymphoproliferative syndrome (XLP).","Subunits.comment":"None","Complex.comment":"The authors showed that SLAM was constitutively associated with SAP in thymocytes. The authors deduced that SLAM engagement is capable of triggering a protein tyrosine phosphorylation signal in T cells, and that this signal is strictly dependent on the presence of SAP. SLAM-SAP signaling was able to selectively inhibit IFN-gamma production by activated BI-141 T cells.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2572,"ComplexName":"RAB5-EEA1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P20339;Q15075","subunits.Entrez.IDs.":"5868;8411","Protein.complex.purification.method":"MI:0055- fluorescent resonance energy transfer","GO.ID":"GO:0006897;GO:0005768","GO.description":"endocytosis;endosome","FunCat.ID":"20.09.18.09.01;70.22","FunCat.description":"endocytosis;endosome","PubMed.ID":15782196,"subunits.Protein.name.":"Ras-related protein Rab-5A;Early endosome antigen 1","subunits.Gene.name.":"RAB5A;EEA1","subunits.Gene.name.syn.":"RAB5;ZFYVE2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2573,"ComplexName":"Class C VPS/HOPS complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P20339;Q15075;Q96JC1;Q9H269;Q9H270;Q9P253","subunits.Entrez.IDs.":"5868;8411;23339;64601;55823;57617","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006897;GO:0007032;GO:0005768","GO.description":"endocytosis;endosome organization;endosome","FunCat.ID":"20.09.18.09.01;42.22;70.22","FunCat.description":"endocytosis;endosome;endosome","PubMed.ID":16143105,"subunits.Protein.name.":"Ras-related protein Rab-5A;Early endosome antigen 1 ;Vam6/Vps39-like protein;Vacuolar protein sorting-associated protein 16 homolog;Vacuolar protein sorting-associated protein 11 homolog;Vacuolar protein sorting-associated protein 18 homolog","subunits.Gene.name.":"RAB5A;EEA1;VPS39;VPS16;VPS11;VPS18","subunits.Gene.name.syn.":"RAB5;ZFYVE2;KIAA0770, TLP, VAM6;None;RNF108;KIAA1475","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The class C VPS/HOPS complex, an established GEF for Rab7, interacts with Rab5 and is required for Rab5-to-Rab7 conversion.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2574,"ComplexName":"CD19-Vav-PI 3-kinase (p85 subunit) complex","Organism":"Human","Synonyms":"None","Cell.line":"B-cell","subunits.UniProt.IDs.":"P15391;P15498;P27986","subunits.Entrez.IDs.":"930;7409;5295","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0023052;GO:0019724;GO:0030183","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;signaling;B cell mediated immunity;B cell differentiation","FunCat.ID":"14.07.03;30.01;36.25.16.03.01;43.03.07.02.01.01","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;cellular signalling;humoral response (B-cells);B-cell","PubMed.ID":7528218,"subunits.Protein.name.":"B-lymphocyte antigen CD19;Proto-oncogene vav;Phosphatidylinositol 3-kinase regulatory subunit alpha","subunits.Gene.name.":"CD19;VAV1;PIK3R1","subunits.Gene.name.syn.":"None;VAV;GRB1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors show that cross-linking of CD19 onsurface Ig-negative B cell precursors and surface Ig-positiveimmature B cells results in the rapid tyrosine phosphorylationof Vav and a concomitant physical association of Vav with CD19and PI 3-kinase.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2575,"ComplexName":"PI3-kinase p85-subunit alpha- PI3-kinase p110 complex","Organism":"Bovine","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P23727;P32871","subunits.Entrez.IDs.":"282307;282306","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation;MI:0096- pull down","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0048015","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;phosphatidylinositol-mediated signaling","FunCat.ID":"14.07.03","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation","PubMed.ID":8313896,"subunits.Protein.name.":"Phosphatidylinositol 3-kinase regulatory subunit alpha ;Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform","subunits.Gene.name.":"PIK3R1;PIK3CA","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results demonstrate that p110 is able to form a stable, active PI 3-kinase complex with either of the p85 isoforms.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":2577,"ComplexName":"Sam68-p85 P13K-IRS-1-IR signaling complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06213;P27986;P35568;Q07666","subunits.Entrez.IDs.":"3643;5295;3667;10657","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008286;GO:0005737","GO.description":"insulin receptor signaling pathway;cytoplasm","FunCat.ID":"30.05.01.12.05;70.03","FunCat.description":"insulin receptor signalling pathway;cytoplasm","PubMed.ID":11604231,"subunits.Protein.name.":"Insulin receptor ;Phosphatidylinositol 3-kinase regulatory subunit alpha;Insulin receptor substrate 1 ;KH domain-containing, RNA-binding, signal transduction-associated protein 1","subunits.Gene.name.":"INSR;PIK3R1;IRS1;KHDRBS1","subunits.Gene.name.syn.":";GRB1;;SAM68","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors found that Sam68 is tyrosine phosphorylated and associates with p85 PI3K after insulin stimulation in a complex that also contains IRS-1 and the IR itself. Further they demonstrated that Sam68 relocalizes after insulin stimulation from the nucleus to the cytoplasm. Regarding the association of Sam68 with p120GAP it is concluded that Sam68 is linking p120GAP to P13K signaling pathway.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2578,"ComplexName":"Sam68-p120GAP complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P20936;Q07666","subunits.Entrez.IDs.":"5921;10657","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008286;GO:0005737","GO.description":"insulin receptor signaling pathway;cytoplasm","FunCat.ID":"30.05.01.12.05;70.03","FunCat.description":"insulin receptor signalling pathway;cytoplasm","PubMed.ID":11604231,"subunits.Protein.name.":"Ras GTPase-activating protein 1;KH domain-containing, RNA-binding, signal transduction-associated protein 1","subunits.Gene.name.":"RASA1;KHDRBS1","subunits.Gene.name.syn.":"GAP, RASA;SAM68","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors suggest that Sam68 is associated with p120GAP after insulin stimulation and in this way it links GAP to the PI3K pathway. Further they demonstrated that Sam68 relocalizes after insulin stimulation from the nucleus to the cytoplasm.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2579,"ComplexName":"Chromosomal passenger complex CPC (INCENP, BIRC5, AURKB)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15392;Q96GD4;Q9NQS7","subunits.Entrez.IDs.":"332;9212;3619","Protein.complex.purification.method":"MI:0096- pull down;MI:0416- fluorescence microscopy","GO.ID":"GO:0000278;GO:0051225;GO:0007098;GO:0006468;GO:0006470;GO:0046777;GO:0000775","GO.description":"mitotic cell cycle;spindle assembly;centrosome cycle;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;chromosome, centromeric region","FunCat.ID":"10.03.01.01;10.03.05.01;14.07.03;70.10.04","FunCat.description":"mitotic cell cycle;spindle pole body/centrosome and microtubule cycle;modification by phosphorylation, dephosphorylation, autophosphorylation;centromere / kinetochore","PubMed.ID":12925766,"subunits.Protein.name.":"Baculoviral IAP repeat-containing protein 5;Aurora kinase B;Inner centromere protein","subunits.Gene.name.":"BIRC5;AURKB;INCENP","subunits.Gene.name.syn.":"API4, IAP4;AIK2, AIM1, AIRK2, ARK2 STK1, STK12, STK5;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"All three proteins showed very similar changes in cell cycle progression, low in G1/S, increased during G2 and M. The studies revealed an evolutionarily conserved mechanism for Aurora B activation by INCENP binding and phosphorylation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2580,"ComplexName":"Survivin homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15392","subunits.Entrez.IDs.":"332","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0000279;GO:0007067;GO:0051225;GO:0007098;GO:0043066;GO:0000226;GO:0015630","GO.description":"M phase;mitotic nuclear division;spindle assembly;centrosome cycle;negative regulation of apoptotic process;microtubule cytoskeleton organization;microtubule cytoskeleton","FunCat.ID":"10.03.01.01.11;10.03.05.01;40.10.02.01;42.04.05;70.04.05","FunCat.description":"M phase;spindle pole body/centrosome and microtubule cycle;anti-apoptosis;microtubule cytoskeleton;microtubule cytoskeleton","PubMed.ID":10876248,"subunits.Protein.name.":"Baculoviral IAP repeat-containing protein 5","subunits.Gene.name.":"BIRC5","subunits.Gene.name.syn.":"API4, IAP4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Survivin temporally and spatially localizes to microtubule organizing centers (MTOC) during mitosis (PMID:9859993).","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":2581,"ComplexName":"RasGAP-AURKA-survivin complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O14965;O15392;P20936","subunits.Entrez.IDs.":"6790;332;5921","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0096-pull down","GO.ID":"GO:0000278;GO:0051726;GO:0007186","GO.description":"mitotic cell cycle;regulation of cell cycle;G-protein coupled receptor signaling pathway","FunCat.ID":"10.03.01.01;10.03.01;30.05.02.24","FunCat.description":"mitotic cell cycle;mitotic cell cycle and cell cycle control;G-protein coupled receptor signalling pathway","PubMed.ID":11976319,"subunits.Protein.name.":"Aurora kinase A;Baculoviral IAP repeat-containing protein 5;Ras GTPase-activating protein 1","subunits.Gene.name.":"AURKA;BIRC5;RASA1","subunits.Gene.name.syn.":"AIK, AIRK1, ARK1, AURA, AYK1, BTAK, IAK1, STK15, STK6;API4, IAP4;GAP, RASA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors define this ternary complex by several protein-protein interactions. RasGAP binds to the kinase domain of Aurora and this interaction inhibits the kinase activity of AURKA and AURKB.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2582,"ComplexName":"Chromosomal passenger complex CPC (CDCA8, AURKB, BIRC5)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15392;Q53HL2;Q96GD4","subunits.Entrez.IDs.":"332;55143;9212","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0000278;GO:0051225;GO:0007098;GO:0000775","GO.description":"mitotic cell cycle;spindle assembly;centrosome cycle;chromosome, centromeric region","FunCat.ID":"10.03.01.01;10.03.05.01;70.10.04","FunCat.description":"mitotic cell cycle;spindle pole body/centrosome and microtubule cycle;centromere / kinetochore","PubMed.ID":15260989,"subunits.Protein.name.":"Baculoviral IAP repeat-containing protein 5;Borealin ;Aurora kinase B","subunits.Gene.name.":"BIRC5;CDCA8;AURKB","subunits.Gene.name.syn.":"API4, IAP4;PESCRG3;AIK2, AIM1, AIRK2, ARK2 STK1, STK12, STK5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors propose that Dasra B may act to regulate the stability of Survivin, which, together with Incenp, serves to target Aurora B to chromosomal arms and centromeres.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2583,"ComplexName":"CSK-GAP-A.p62 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P41241;Q60749","subunits.Entrez.IDs.":"12988;20218","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0023052;GO:0005886;GO:0005856","GO.description":"signaling;plasma membrane;cytoskeleton","FunCat.ID":"30.01;70.02;70.04","FunCat.description":"cellular signalling;eukaryotic plasma membrane / membrane attached;cytoskeleton","PubMed.ID":7544435,"subunits.Protein.name.":"Tyrosine-protein kinase CSK ;KH domain-containing, RNA-binding, signal transduction-associated protein 1","subunits.Gene.name.":"Csk;Khdrbs1","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"The authors differentiate between GAP-A.p62 and Sam68, but there is no other corresponding entry than Swiss:Q60749 in SWISS-DB.","Complex.comment":"The interaction requires the SH2 domain of CSK.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2584,"ComplexName":"c-Src-Muc1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P41241;Q02496","subunits.Entrez.IDs.":"12988;17829","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0663- confocal microscopy","GO.ID":"GO:0023052;GO:0005886","GO.description":"signaling;plasma membrane","FunCat.ID":"30.01;70.02","FunCat.description":"cellular signalling;eukaryotic plasma membrane / membrane attached","PubMed.ID":15897873,"subunits.Protein.name.":"Tyrosine-protein kinase CSK ;Mucin-1","subunits.Gene.name.":"Csk;Muc1","subunits.Gene.name.syn.":";Muc-1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors use MMTV-PyV MT (MMTV-driven polyoma middle T-antigen transgenic mice)  as model to characterize the effect of Muc1 expression on c-Src signaling. Muc1 and c-Src colocalize in the MT tumors mainly at the apical membrane.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2585,"ComplexName":"nKHC-KLC1-uKHC kinesin complex","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"O88447;P33175;Q61768","subunits.Entrez.IDs.":"16593;16572;16573","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007018;GO:0050896;GO:0015630","GO.description":"microtubule-based movement;response to stimulus;microtubule cytoskeleton","FunCat.ID":"20.09.14.01;36.25;70.04.05","FunCat.description":"tubulin dependent transport;animal specific systemic sensing and response;microtubule cytoskeleton","PubMed.ID":9624122,"subunits.Protein.name.":"Kinesin light chain 1 ;Kinesin heavy chain isoform 5A;Kinesin-1 heavy chain","subunits.Gene.name.":"Klc1;Kif5a;Kif5b","subunits.Gene.name.syn.":"Kns2;Kiaa4086 Kif5 Nkhc1;Khcs, Kns1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors demonstrate that neither KLC nor KHC form heterodimers in the native complex in brain and that there is no specificity in the interaction of the kinesin light chains with the kinesin heavy chains. Immunprecipitation done from brain lysate with KLC1 antibodies shows nKHC, uKHC and KLC1, but not KLC2.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2586,"ComplexName":"KLC2-nKHC-uKHC kinesin complex","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"O88448;P33175;Q61768","subunits.Entrez.IDs.":"16594;16572;16573","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007018;GO:0050896;GO:0015630","GO.description":"microtubule-based movement;response to stimulus;microtubule cytoskeleton","FunCat.ID":"20.09.14.01;36.25;70.04.05","FunCat.description":"tubulin dependent transport;animal specific systemic sensing and response;microtubule cytoskeleton","PubMed.ID":9624122,"subunits.Protein.name.":"Kinesin light chain 2 ;Kinesin heavy chain isoform 5A;Kinesin-1 heavy chain","subunits.Gene.name.":"Klc2;Kif5a;Kif5b","subunits.Gene.name.syn.":";Kiaa4086 Kif5 Nkhc1;Khcs, Kns1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors demonstrate that neither KLC nor KHC form heterodimers in the native complex in brain and that there is no specificity in the interaction of the kinesin light chains with the kinesin heavy chains. Immunprecipitation done from brain lysate with KLC2 antibodies shows nKHC, uKHC and KLC2, but not KLC1.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2587,"ComplexName":"nKHC-KLC1-KLC2 kinesin complex","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"O88447;O88448;P33175","subunits.Entrez.IDs.":"16593;16594;16572","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007018;GO:0050896;GO:0015630","GO.description":"microtubule-based movement;response to stimulus;microtubule cytoskeleton","FunCat.ID":"20.09.14.01;36.25;70.04.05","FunCat.description":"tubulin dependent transport;animal specific systemic sensing and response;microtubule cytoskeleton","PubMed.ID":9624122,"subunits.Protein.name.":"Kinesin light chain 1 ;Kinesin light chain 2 ;Kinesin heavy chain isoform 5A","subunits.Gene.name.":"Klc1;Klc2;Kif5a","subunits.Gene.name.syn.":"Kns2;;Kiaa4086 Kif5 Nkhc1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Immunoprecipitation done from brain lysate with nKHC antibodies brings down both kinesin light chains.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2589,"ComplexName":"PGC-1-SRp40-SRp55-SRp75 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q08170;Q13243;Q13247;Q9UBK2","subunits.Entrez.IDs.":"6429;6430;6431;10891","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0000398;GO:0006397;GO:0003676;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;mRNA splicing, via spliceosome;mRNA processing;nucleic acid binding;nucleus","FunCat.ID":"11.02.03.04;11.04.03;16.03;70.10","FunCat.description":"transcriptional control;mRNA processing (splicing, 5'-, 3'-end processing);nucleic acid binding;nucleus","PubMed.ID":10983978,"subunits.Protein.name.":"Serine/arginine-rich splicing factor 4 ;Serine/arginine-rich splicing factor 5 ;Serine/arginine-rich splicing factor 6;Peroxisome proliferator-activated receptor gamma coactivator 1-alpha","subunits.Gene.name.":"SRSF4;SRSF5;SRSF6;PPARGC1A","subunits.Gene.name.syn.":"SFRS4 SRP75;HRS SFRS5 SRP40;SFRS6 SRP55;LEM6 PGC1 PGC1A PPARGC1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"PGC-1 is part of both the preinitiation and elongation Pol II complexes, and association with the elongation form of Pol II depends on the C-terminal domain of PGC-1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2590,"ComplexName":"FOXO1-FHL2-SIRT1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q12778;Q14192;Q96EB6","subunits.Entrez.IDs.":"2308;2274;23411","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0045892;GO:0006473;GO:0006476;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;nucleus","FunCat.ID":"11.02.03.04.03;14.07.04;70.10","FunCat.description":"transcription repression;modification by acetylation, deacetylation;nucleus","PubMed.ID":15692560,"subunits.Protein.name.":"Forkhead box protein O1 ;Four and a half LIM domains protein 2 ;NAD-dependent protein deacetylase sirtuin-1","subunits.Gene.name.":"FOXO1;FHL2;SIRT1","subunits.Gene.name.syn.":"FKHR FOXO1A;DRAL SLIM3;SIR2L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors came to the following results: 1. FHL2 colocalizes and interacts with FOXO1 in prostate cancer cells. 2. FHL2 inhibits the activation of an IRS-driven reporter gene by FOXO1 in the presence but not in the absence of SIRT1 activity. 3. SIRT1 binds FOXO1, decreases its acetylation, and inhibits its transcriptional activity. 4. FHL2 interacts with SIRT1 and promotes its interaction with FOXO1. They suggest a model  that FHL2 negates the transcriptional activity of FOXO1 by promoting its deacetylation by SIRT1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2591,"ComplexName":"SIRT1-HNF4-alpha-PGC-1-alpha complex, in response to fasting","Organism":"Mouse","Synonyms":"None","Cell.line":"liver","subunits.UniProt.IDs.":"O70343;P49698;Q923E4","subunits.Entrez.IDs.":"19017;15378;93759","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0006111;GO:0006110;GO:2001141;GO:0006355;GO:0042594;GO:0042593;GO:0005634","GO.description":"regulation of gluconeogenesis;regulation of glycolytic process;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;response to starvation;glucose homeostasis;nucleus","FunCat.ID":"02.01.03;11.02.03.04;32.01.11;34.01.04;70.10","FunCat.description":"regulation of glycolysis and gluconeogenesis;transcriptional control;nutrient starvation response;glucose homeostasis;nucleus","PubMed.ID":15744310,"subunits.Protein.name.":"Peroxisome proliferator-activated receptor gamma coactivator 1-alpha;Hepatocyte nuclear factor 4-alpha;NAD-dependent protein deacetylase sirtuin-1","subunits.Gene.name.":"Ppargc1a;Hnf4a;Sirt1","subunits.Gene.name.syn.":"Pgc1 Pgc1a Ppargc1;Hnf-4 Hnf4 Nr2a1 Tcf14;Sir2l1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Acetylation of PGC-1 alpha by SIRT1 decreases its ability to efficiently coactivate HNF4alpha. In general the results show that PGC-1 alpha and SIRT1 can function together to promote adaptation to nutrient deprivation by regulating the genetic programmes of gluconeogenesis and glycolysis. SIRT1 can act both positively and negatively to control gene expression as a cofactor for PGC-1 alpha.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2592,"ComplexName":"SIRT1 homotrimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q96EB6","subunits.Entrez.IDs.":"23411","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0006473;GO:0006476;GO:0005634","GO.description":"protein acetylation;protein deacetylation;nucleus","FunCat.ID":"14.07.04;70.10","FunCat.description":"modification by acetylation, deacetylation;nucleus","PubMed.ID":15469825,"subunits.Protein.name.":"NAD-dependent protein deacetylase sirtuin-1","subunits.Gene.name.":"SIRT1","subunits.Gene.name.syn.":"SIR2L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SirT1 exists as a trimer and interacts with histone H1.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":2593,"ComplexName":"FOXO3-SIRT1 complex, oxidative stress stimulated","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43524;Q96EB6","subunits.Entrez.IDs.":"2309;23411","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0000302;GO:0006979;GO:0043066;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;response to reactive oxygen species;response to oxidative stress;negative regulation of apoptotic process;nucleus","FunCat.ID":"11.02.03.04;32.01.01;40.10.02.01;70.10","FunCat.description":"transcriptional control;oxidative stress response;anti-apoptosis;nucleus","PubMed.ID":14976264,"subunits.Protein.name.":"Forkhead box protein O3;NAD-dependent protein deacetylase sirtuin-1","subunits.Gene.name.":"FOXO3;SIRT1","subunits.Gene.name.syn.":"FKHRL1, FOXO3A;SIR2L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SIRT1 and  transcription factor FOXO3 formed a complex in cells in response to oxidative stress, and SIRT1 deacetylated FOXO3 in vitro and within cells. SIRT1 increased FOXO3's ability to induce cell cycle arrest and resistance to oxidative stress but inhibited FOXO3's ability to induce cell death.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2598,"ComplexName":"NELF complex (Negative elongation factor complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P18615;Q8IXH7;Q8WX92;Q9H3P2","subunits.Entrez.IDs.":"7936;51497;25920;7469","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006354;GO:0045892;GO:0005515;GO:0003723;GO:0051098;GO:0051090;GO:0005634","GO.description":"DNA-templated transcription, elongation;negative regulation of transcription, DNA-templated;protein binding;RNA binding;regulation of binding;regulation of sequence-specific DNA binding transcription factor activity;nucleus","FunCat.ID":"11.02.03.01.04;11.02.03.04.03;16.01;16.03.03;18.01.07;18.02.09;70.10","FunCat.description":"transcription elongation;transcription repression;protein binding;RNA binding;regulation by binding / dissociation;regulator of transcription factor;nucleus","PubMed.ID":12612062,"subunits.Protein.name.":"Negative elongation factor E ;Negative elongation factor C/D ;Negative elongation factor B ;Negative elongation factor A","subunits.Gene.name.":"NELFE;NELFCD;NELFB;NELFA","subunits.Gene.name.syn.":"RD RDBP;NELFD TH1 TH1L;COBRA1 KIAA1182;WHSC2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"NELF cooperates with DSIF and represses DRB-sensitive RNA-Polymerase II.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2599,"ComplexName":"POLR2A-CCNT1-CDK9-NCL-LEM6-CPSF2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60563;P19338;P24928;P50750;Q9P2I0;Q9UBK2","subunits.Entrez.IDs.":"904;4691;5430;1025;53981;10891","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0000398;GO:0006397;GO:0006468;GO:0006470;GO:0046777;GO:0003676;GO:0006464;GO:0050789;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;mRNA splicing, via spliceosome;mRNA processing;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;nucleic acid binding;cellular protein modification process;regulation of biological process;nucleus","FunCat.ID":"11.02.03.04;11.04.03;14.07.03;16.03;14.07;18;70.10","FunCat.description":"transcriptional control;mRNA processing (splicing, 5'-, 3'-end processing);modification by phosphorylation, dephosphorylation, autophosphorylation;nucleic acid binding;protein modification;REGULATION OF METABOLISM AND PROTEIN FUNCTION;nucleus","PubMed.ID":10983978,"subunits.Protein.name.":"Cyclin-T1;Nucleolin ;DNA-directed RNA polymerase II subunit RPB1;Cyclin-dependent kinase 9;Cleavage and polyadenylation specificity factor subunit 2 ;Peroxisome proliferator-activated receptor gamma coactivator 1-alpha","subunits.Gene.name.":"CCNT1;NCL;POLR2A;CDK9;CPSF2;PPARGC1A","subunits.Gene.name.syn.":"None;;POLR2;CDC2L4, TAK;CPSF100 KIAA1367;LEM6 PGC1 PGC1A PPARGC1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors demonstrate that PGC-1 is part of both the preinitiation and elongation Pol II complexes, and association with the elongation form of Pol II depends on the C-terminal domain of PGC-1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2600,"ComplexName":"BRD4 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60244;O60563;O60885;O75448;P50750;Q15648;Q93074;Q9NVC6","subunits.Entrez.IDs.":"9282;904;23476;9862;1025;5469;9968;9440","Protein.complex.purification.method":"MI:0676- tandem affinity purification","GO.ID":"GO:0006794;GO:0006796;GO:0006354;GO:0045893;GO:0006464;GO:0043085;GO:0008047;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;DNA-templated transcription, elongation;positive regulation of transcription, DNA-templated;cellular protein modification process;positive regulation of catalytic activity;enzyme activator activity;nucleus","FunCat.ID":"01.04;11.02.03.01.04;11.02.03.04.01;14.07;18.02.01.01;70.10","FunCat.description":"phosphate metabolism;transcription elongation;transcription activation;protein modification;enzyme activator;nucleus","PubMed.ID":16109376,"subunits.Protein.name.":"Mediator of RNA polymerase II transcription subunit 14;Cyclin-T1;Bromodomain-containing protein 4 ;Mediator of RNA polymerase II transcription subunit 24;Cyclin-dependent kinase 9;Mediator of RNA polymerase II transcription subunit 1;Mediator of RNA polymerase II transcription subunit 12;Mediator of RNA polymerase II transcription subunit 17","subunits.Gene.name.":"MED14;CCNT1;BRD4;MED24;CDK9;MED1;MED12;MED17","subunits.Gene.name.syn.":"ARC150 CRSP2 CXorf4 DRIP150 EXLM1 RGR1 TRAP170;None;HUNK1;ARC100 CRSP4 DRIP100 KIAA0130 THRAP4 TRAP100;CDC2L4, TAK;ARC205 CRSP1 CRSP200 DRIP205 DRIP230 PBP PPARBP PPARGBP RB18A TRAP220 TRIP2;ARC240 CAGH45 HOPA KIAA0192 TNRC11 TRAP230;ARC77 CRSP6 DRIP77 DRIP80 TRAP80","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2601,"ComplexName":"P-TEFb-BRD4-TRAP220 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60563;O60885;P50750;Q15648","subunits.Entrez.IDs.":"904;23476;1025;5469","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006794;GO:0006796;GO:0006354;GO:0045893;GO:0006464;GO:0043085;GO:0008047;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;DNA-templated transcription, elongation;positive regulation of transcription, DNA-templated;cellular protein modification process;positive regulation of catalytic activity;enzyme activator activity;nucleus","FunCat.ID":"01.04;11.02.03.01.04;11.02.03.04.01;14.07;18.02.01.01;70.10","FunCat.description":"phosphate metabolism;transcription elongation;transcription activation;protein modification;enzyme activator;nucleus","PubMed.ID":16109377,"subunits.Protein.name.":"Cyclin-T1;Bromodomain-containing protein 4 ;Cyclin-dependent kinase 9;Mediator of RNA polymerase II transcription subunit 1","subunits.Gene.name.":"CCNT1;BRD4;CDK9;MED1","subunits.Gene.name.syn.":"None;HUNK1;CDC2L4, TAK;ARC205 CRSP1 CRSP200 DRIP205 DRIP230 PBP PPARBP PPARGBP RB18A TRAP220 TRIP2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Brd4 is necessary to mediate the interaction between P-TEFb and Mediator complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2602,"ComplexName":"P-TEFb-7SKRNA-HEXIM1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60563;O94992;P50750","subunits.Entrez.IDs.":"904;10614;1025","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006794;GO:0006796;GO:0006354;GO:2001141;GO:0006355;GO:0006464;GO:0030234;GO:0050790;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;DNA-templated transcription, elongation;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;cellular protein modification process;enzyme regulator activity;regulation of catalytic activity;nucleus","FunCat.ID":"01.04;11.02.03.01.04;11.02.03.04;14.07;18.02.01;70.10","FunCat.description":"phosphate metabolism;transcription elongation;transcriptional control;protein modification;enzymatic activity regulation / enzyme regulator;nucleus","PubMed.ID":14580347,"subunits.Protein.name.":"Cyclin-T1;Protein HEXIM1 ;Cyclin-dependent kinase 9","subunits.Gene.name.":"CCNT1;HEXIM1;CDK9","subunits.Gene.name.syn.":"None;CLP1 EDG1 HIS1 MAQ1;CDC2L4, TAK","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"7SK RNA is required for HEXIM1 to associate with P-TEFb complex. This allowes HEXIM1 to inhibit transcription. P-TEFb dissociates from HEXIM1 and 7SK in cells undergoing stress response, increasing the level of active P-TEFb for stress-induced transcription.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2603,"ComplexName":"Transcription elongation factor complex (SUPT5H, CDK9, CCNT1)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00267;O60563;P50750","subunits.Entrez.IDs.":"6829;904;1025","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0006794;GO:0006796;GO:0006354;GO:0045893;GO:0006464;GO:0043085;GO:0008047;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;DNA-templated transcription, elongation;positive regulation of transcription, DNA-templated;cellular protein modification process;positive regulation of catalytic activity;enzyme activator activity;nucleus","FunCat.ID":"01.04;11.02.03.01.04;11.02.03.04.01;14.07;18.02.01.01;70.10","FunCat.description":"phosphate metabolism;transcription elongation;transcription activation;protein modification;enzyme activator;nucleus","PubMed.ID":11145967,"subunits.Protein.name.":"Transcription elongation factor SPT5 ;Cyclin-T1;Cyclin-dependent kinase 9","subunits.Gene.name.":"SUPT5H;CCNT1;CDK9","subunits.Gene.name.syn.":"SPT5 SPT5H;None;CDC2L4, TAK","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2604,"ComplexName":"P-TEFb-SKP2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60563;P50750;Q13309","subunits.Entrez.IDs.":"904;1025;6502","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006354;GO:2001141;GO:0006355;GO:0043161;GO:0006511;GO:0006464;GO:0043085;GO:0008047;GO:0005634","GO.description":"DNA-templated transcription, elongation;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;cellular protein modification process;positive regulation of catalytic activity;enzyme activator activity;nucleus","FunCat.ID":"11.02.03.01.04;11.02.03.04;14.13.01.01;14.07;18.02.01.01;70.10","FunCat.description":"transcription elongation;transcriptional control;proteasomal degradation (ubiquitin/proteasomal pathway);protein modification;enzyme activator;nucleus","PubMed.ID":11689688,"subunits.Protein.name.":"Cyclin-T1;Cyclin-dependent kinase 9;S-phase kinase-associated protein 2","subunits.Gene.name.":"CCNT1;CDK9;SKP2","subunits.Gene.name.syn.":"None;CDC2L4, TAK;FBXL1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Binding of SKP2 to P-TEFb requires PEST domain of cyclin T1. CDK9 is ubiquitinated and degraded by the proteasome whereas cyclin T1 is stable.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2605,"ComplexName":"Heterotrimeric complex (CCNT1, CDK9, GRN)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60563;P28799;P50750","subunits.Entrez.IDs.":"904;2896;1025","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0045892","GO.description":"negative regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.03","FunCat.description":"transcription repression","PubMed.ID":12588988,"subunits.Protein.name.":"Cyclin-T1;Granulins ;Cyclin-dependent kinase 9","subunits.Gene.name.":"CCNT1;GRN;CDK9","subunits.Gene.name.syn.":"None;;CDC2L4, TAK","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Granulin is a cellular protein that interacts with cyclin T1 to inhibit transcription.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2608,"ComplexName":"Brd4-P-TEFb complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q99J95;Q9ESU6;Q9QWV9","subunits.Entrez.IDs.":"107951;57261;12455","Protein.complex.purification.method":"MI:0809- bimolecular fluorescence complementation; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006794;GO:0006796;GO:0006354;GO:0045893;GO:0006464;GO:0043085;GO:0008047;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;DNA-templated transcription, elongation;positive regulation of transcription, DNA-templated;cellular protein modification process;positive regulation of catalytic activity;enzyme activator activity;nucleus","FunCat.ID":"01.04;11.02.03.01.04;11.02.03.04.01;14.07;18.02.01.01;70.10","FunCat.description":"phosphate metabolism;transcription elongation;transcription activation;protein modification;enzyme activator;nucleus","PubMed.ID":16109376,"subunits.Protein.name.":"Cyclin-dependent kinase 9 ;Bromodomain-containing protein 4 ;Cyclin-T1","subunits.Gene.name.":"Cdk9;Brd4;Ccnt1","subunits.Gene.name.syn.":";Mcap;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2618,"ComplexName":"TUBA1A-TUBB2A complex","Organism":"Bovine","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P02550;Q148E2","subunits.Entrez.IDs.":"None;281555","Protein.complex.purification.method":"MI:0040- electron microscopy","GO.ID":"GO:0000226","GO.description":"microtubule cytoskeleton organization","FunCat.ID":"42.04.05","FunCat.description":"microtubule cytoskeleton","PubMed.ID":9428769,"subunits.Protein.name.":"Tubulin alpha-1A chain ;Tubulin beta chain","subunits.Gene.name.":"TUBA1A;TUBB2A","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Sus scrofa (Pig);Bos taurus (Bovine)"}
{"ComplexID":2625,"ComplexName":"CDK8-MED6-PARP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75586;P09874;P49336","subunits.Entrez.IDs.":"10001;142;1024","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":15808511,"subunits.Protein.name.":"Mediator of RNA polymerase II transcription subunit 6 ;Poly [ADP-ribose] polymerase 1;Cyclin-dependent kinase 8","subunits.Gene.name.":"MED6;PARP1;CDK8","subunits.Gene.name.syn.":"ARC33;ADPRT PPOL;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2626,"ComplexName":"CCNC-CDK8-MED1-MED6-MED7 xcomplex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43513;O75586;P24863;P49336;Q15648","subunits.Entrez.IDs.":"9443;10001;892;1024;5469","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":15808511,"subunits.Protein.name.":"Mediator of RNA polymerase II transcription subunit 7 ;Mediator of RNA polymerase II transcription subunit 6 ;Cyclin-C;Cyclin-dependent kinase 8;Mediator of RNA polymerase II transcription subunit 1","subunits.Gene.name.":"MED7;MED6;CCNC;CDK8;MED1","subunits.Gene.name.syn.":"ARC34 CRSP9;ARC33;None;None;ARC205 CRSP1 CRSP200 DRIP205 DRIP230 PBP PPARBP PPARGBP RB18A TRAP220 TRIP2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2628,"ComplexName":"CCNC-CDK3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P24863;Q00526","subunits.Entrez.IDs.":"892;1018","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007049","GO.description":"cell cycle","FunCat.ID":"10.03","FunCat.description":"cell cycle","PubMed.ID":15084261,"subunits.Protein.name.":"Cyclin-C;Cyclin-dependent kinase 3","subunits.Gene.name.":"CCNC;CDK3","subunits.Gene.name.syn.":"None;CDKN3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"A non-cdk8-associated cellular pool of cyclin C combines with cdk3 to stimulate pRb phosphorylation at S807/811 during the G0/G1 transition, and that this phosphorylation is required for cells to exit G0 efficiently.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2635,"ComplexName":"BETA2-Cyclin D1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P24385;Q13562","subunits.Entrez.IDs.":"595;4760","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":11788592,"subunits.Protein.name.":"G1/S-specific cyclin-D1;Neurogenic differentiation factor 1","subunits.Gene.name.":"CCND1;NEUROD1","subunits.Gene.name.syn.":"BCL1 PRAD1;BHLHA3 NEUROD","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2638,"ComplexName":"HES1 promoter corepressor complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P24928;P50613;Q06330;Q09472;Q7KZ85;Q92793","subunits.Entrez.IDs.":"5430;1022;3516;2033;6830;1387","Protein.complex.purification.method":"MI:0402- chromatin immunoprecipitation assays","GO.ID":"GO:0045892;GO:0003677;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04.03;16.03.01;70.10","FunCat.description":"transcription repression;DNA binding;nucleus","PubMed.ID":15546612,"subunits.Protein.name.":"DNA-directed RNA polymerase II subunit RPB1;Cyclin-dependent kinase 7 ;Recombining binding protein suppressor of hairless ;Histone acetyltransferase p300;Transcription elongation factor SPT6 ;CREB-binding protein","subunits.Gene.name.":"POLR2A;CDK7;RBPJ;EP300;SUPT6H;CREBBP","subunits.Gene.name.syn.":"POLR2;CAK CAK1 CDKN7 MO15 STK1;IGKJRB IGKJRB1 RBPJK RBPSUH;P300;KIAA0162 SPT6H;CBP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex has been studied on the HES1 promoter (a Notch target gene) in cells without Notch signaling.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2639,"ComplexName":"HES1 promoter-Notch enhancer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60563;P24928;P46531;P49336;P50613;P50750;Q06330;Q09472;Q15648;Q7KZ85;Q92585;Q9BT40;Q9Y5B9","subunits.Entrez.IDs.":"904;5430;4851;1024;1022;1025;3516;2033;5469;6830;9794;51763;11198","Protein.complex.purification.method":"MI:0402- chromatin immunoprecipitation assays","GO.ID":"GO:0045893;GO:0003677;GO:0007219;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;Notch signaling pathway;nucleus","FunCat.ID":"11.02.03.04.01;16.03.01;30.05.02.14;70.10","FunCat.description":"transcription activation;DNA binding;Notch-receptor signalling pathway;nucleus","PubMed.ID":15546612,"subunits.Protein.name.":"Cyclin-T1;DNA-directed RNA polymerase II subunit RPB1;Neurogenic locus notch homolog protein 1 ;Cyclin-dependent kinase 8;Cyclin-dependent kinase 7 ;Cyclin-dependent kinase 9;Recombining binding protein suppressor of hairless ;Histone acetyltransferase p300;Mediator of RNA polymerase II transcription subunit 1;Transcription elongation factor SPT6 ;Mastermind-like protein 1 ;Inositol polyphosphate 5-phosphatase K ;FACT complex subunit SPT16","subunits.Gene.name.":"CCNT1;POLR2A;NOTCH1;CDK8;CDK7;CDK9;RBPJ;EP300;MED1;SUPT6H;MAML1;INPP5K;SUPT16H","subunits.Gene.name.syn.":"None;POLR2;TAN1;None;CAK CAK1 CDKN7 MO15 STK1;CDC2L4, TAK;IGKJRB IGKJRB1 RBPJK RBPSUH;P300;ARC205 CRSP1 CRSP200 DRIP205 DRIP230 PBP PPARBP PPARGBP RB18A TRAP220 TRIP2;KIAA0162 SPT6H;KIAA0200;PPS SKIP;FACT140 FACTP140","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"After Notch signaling endogenous CDK8 is recruited to the HES1 promoter (a Notch target gene) together with Notch and MAM. Signaling also induces binding of SKIP, as well as two transcription elongation factors, P-TEFb and FACT.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2641,"ComplexName":"CREBBP-KAT2B-MYOD1 complex","Organism":"Human","Synonyms":"p300/CBP-PCAF-MyoD complex","Cell.line":"C2C12 myotube","subunits.UniProt.IDs.":"P15172;Q92793;Q92831","subunits.Entrez.IDs.":"4654;1387;8850","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007519;GO:0006351","GO.description":"skeletal muscle tissue development;transcription, DNA-templated","FunCat.ID":"41.05.15;11","FunCat.description":"myogenesis;TRANSCRIPTION","PubMed.ID":9659901,"subunits.Protein.name.":"Myoblast determination protein 1;CREB-binding protein;Histone acetyltransferase KAT2B","subunits.Gene.name.":"MYOD1;CREBBP;KAT2B","subunits.Gene.name.syn.":"BHLHC1 MYF3 MYOD;CBP;PCAF","Disease.comment":"None","Subunits.comment":"The transcriptional coactivators p300 and CBP are considered as functional homologs, the authors refer to them as p300/CBP. We used CBP.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2642,"ComplexName":"SMAD1-P300 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q09472;Q15797","subunits.Entrez.IDs.":"2033;4086","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation; MI:0402- chromatin immunoprecipitation assays","GO.ID":"GO:0006265;GO:0045893;GO:0006473;GO:0006476;GO:0007179;GO:0051276;GO:0005634","GO.description":"DNA topological change;positive regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;transforming growth factor beta receptor signaling pathway;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.01;14.07.04;30.05.01.18.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription activation;modification by acetylation, deacetylation;TGF-beta-receptor signalling pathway;organization of chromosome structure;nucleus","PubMed.ID":10673036,"subunits.Protein.name.":"Histone acetyltransferase p300;Mothers against decapentaplegic homolog 1","subunits.Gene.name.":"EP300;SMAD1","subunits.Gene.name.syn.":"P300;BSP1 MADH1 MADR1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SMAD1 stimulates transcription cooperatively with P300.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2649,"ComplexName":"MYC-DNMT3A-ZBTB17 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P01106;Q13105;Q9Y6K1","subunits.Entrez.IDs.":"4609;None;1788","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0003677","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding","FunCat.ID":"11.02.03.04;16.03.01","FunCat.description":"transcriptional control;DNA binding","PubMed.ID":15616584,"subunits.Protein.name.":"Myc proto-oncogene protein ;Zinc finger and BTB domain-containing protein 17 ;DNA","subunits.Gene.name.":"MYC;ZBTB17;DNMT3A","subunits.Gene.name.syn.":"BHLHE39;MIZ1 ZNF151 ZNF60;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex is involved in a transcriptional silecing of  p21Cip1 promoter.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2650,"ComplexName":"DNMT3B-DNMT3L complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q9UBC3;Q9UJW3","subunits.Entrez.IDs.":"1789;29947","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0006306","GO.description":"DNA methylation","FunCat.ID":"10.01.09.01","FunCat.description":"DNA methylation","PubMed.ID":15105426,"subunits.Protein.name.":"DNA;DNA","subunits.Gene.name.":"DNMT3B;DNMT3L","subunits.Gene.name.syn.":"None;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2651,"ComplexName":"DNMT3L-DNMT3A complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q9UJW3;Q9Y6K1","subunits.Entrez.IDs.":"29947;1788","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0006306","GO.description":"DNA methylation","FunCat.ID":"10.01.09.01","FunCat.description":"DNA methylation","PubMed.ID":15105426,"subunits.Protein.name.":"DNA ;DNA","subunits.Gene.name.":"DNMT3L;DNMT3A","subunits.Gene.name.syn.":";None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2653,"ComplexName":"MYC-MAX-BLOC1S1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P01106;P61244;P78537","subunits.Entrez.IDs.":"4609;4149;2647","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0051098;GO:0005515","GO.description":"regulation of binding;protein binding","FunCat.ID":"18.01.07;16.01","FunCat.description":"regulation by binding / dissociation;protein binding","PubMed.ID":10611234,"subunits.Protein.name.":"Myc proto-oncogene protein ;Protein max ;Biogenesis of lysosome-related organelles complex 1 subunit 1","subunits.Gene.name.":"MYC;MAX;BLOC1S1","subunits.Gene.name.syn.":"BHLHE39;BHLHD4;BLOS1 GCN5L1 RT14","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2655,"ComplexName":"MYC-MAX complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P01106;P61244","subunits.Entrez.IDs.":"4609;4149","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0003677","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding","FunCat.ID":"11.02.03.04;16.03.01","FunCat.description":"transcriptional control;DNA binding","PubMed.ID":12584560,"subunits.Protein.name.":"Myc proto-oncogene protein ;Protein max","subunits.Gene.name.":"MYC;MAX","subunits.Gene.name.syn.":"BHLHE39;BHLHD4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2657,"ComplexName":"ESR1-CDK7-CCNH-MNAT1-MTA1-HDAC2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P03372;P50613;P51946;P51948;Q13330;Q92769","subunits.Entrez.IDs.":"2099;1022;902;4331;9112;3066","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0006468;GO:0006470;GO:0046777;GO:0006464;GO:0050789;GO:0023052;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;cellular protein modification process;regulation of biological process;signaling;nucleus","FunCat.ID":"11.02.03.04;14.07.03;14.07;18;30.01;70.10","FunCat.description":"transcriptional control;modification by phosphorylation, dephosphorylation, autophosphorylation;protein modification;REGULATION OF METABOLISM AND PROTEIN FUNCTION;cellular signalling;nucleus","PubMed.ID":12527756,"subunits.Protein.name.":"Estrogen receptor;Cyclin-dependent kinase 7 ;Cyclin-H ;CDK-activating kinase assembly factor MAT1 ;Metastasis-associated protein MTA1;Histone deacetylase 2","subunits.Gene.name.":"ESR1;CDK7;CCNH;MNAT1;MTA1;HDAC2","subunits.Gene.name.syn.":"ESR, NR3A1;CAK CAK1 CDKN7 MO15 STK1;;CAP35 MAT1 RNF66;None;None","Disease.comment":"MTA1 is involved in metastasis or cancer formation.","Subunits.comment":"None","Complex.comment":"The authors identified MAT1 as a target of corepressor MTA1 and provided new evidence to suggest that the transactivation functions of ER are influenced by the regulatory interactions between CAK and MTA1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2660,"ComplexName":"ERCC2/CAK complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P18074;P50613;P51946;P51948","subunits.Entrez.IDs.":"2068;1022;902;4331","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006281","GO.description":"DNA repair","FunCat.ID":"10.01.05.01","FunCat.description":"DNA repair","PubMed.ID":8692841,"subunits.Protein.name.":"TFIIH basal transcription factor complex helicase XPD subunit ;Cyclin-dependent kinase 7 ;Cyclin-H ;CDK-activating kinase assembly factor MAT1","subunits.Gene.name.":"ERCC2;CDK7;CCNH;MNAT1","subunits.Gene.name.syn.":"XPD XPDC;CAK CAK1 CDKN7 MO15 STK1;;CAP35 MAT1 RNF66","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TFIIH* and ERCC2/CAK interact to form the TFIIH holoenzyme capable of efficiently assembling the pol II transcription initiation complex and directly participating in excision repair reactions.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2670,"ComplexName":"Er-alpha-p53-hdm2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P03372;P04637;Q00987","subunits.Entrez.IDs.":"2099;7157;4193","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0030234;GO:0050790","GO.description":"enzyme regulator activity;regulation of catalytic activity","FunCat.ID":"18.02.01","FunCat.description":"enzymatic activity regulation / enzyme regulator","PubMed.ID":10766163,"subunits.Protein.name.":"Estrogen receptor;Cellular tumor antigen p53;E3 ubiquitin-protein ligase Mdm2","subunits.Gene.name.":"ESR1;TP53;MDM2","subunits.Gene.name.syn.":"ESR, NR3A1;P53;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors demonstrated that ER-alpha protects p53 from being deactivated by hdm2 in a Luc reporter assay.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2678,"ComplexName":"FOXO3-TP53 complex, oxidative stress stimulated","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43524;P04637","subunits.Entrez.IDs.":"2309;7157","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0000302;GO:0006979;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;response to reactive oxygen species;response to oxidative stress;nucleus","FunCat.ID":"11.02.03.04;32.01.01;70.10","FunCat.description":"transcriptional control;oxidative stress response;nucleus","PubMed.ID":14976264,"subunits.Protein.name.":"Forkhead box protein O3;Cellular tumor antigen p53","subunits.Gene.name.":"FOXO3;TP53","subunits.Gene.name.syn.":"FKHRL1, FOXO3A;P53","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2679,"ComplexName":"p53-SP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04637;P08047","subunits.Entrez.IDs.":"7157;6667","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04;16.03.01;70.10","FunCat.description":"transcriptional control;DNA binding;nucleus","PubMed.ID":15674334,"subunits.Protein.name.":"Cellular tumor antigen p53;Transcription factor Sp1","subunits.Gene.name.":"TP53;SP1","subunits.Gene.name.syn.":"P53;TSFP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors provide evidence that p53 repressed the RECQ4 promoter by forming a complex with the transcription factor, SP1, and by regulating promoter occupancy of both itself and SP1 in concert with histone deacetylase 1 (HDAC1). The formation of this complex is camptothecin-dependent.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2681,"ComplexName":"p53 homotetramer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04637","subunits.Entrez.IDs.":"7157","Protein.complex.purification.method":"MI:0031- protein cross-linking with a bifunctional reagent; MI:0276- blue native page","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04;16.03.01;70.10","FunCat.description":"transcriptional control;DNA binding;nucleus","PubMed.ID":15674341,"subunits.Protein.name.":"Cellular tumor antigen p53","subunits.Gene.name.":"TP53","subunits.Gene.name.syn.":"P53","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results demonstrate that Ref-1 (redox factor 1) modulates p53 DNA binding not only as a redox regulator but also as a factor, which facilitates the formation of p53 tetramers from higher oligomeric forms as well as from dimers. Ref-1 mediates de-stacking of higher oligomeric forms into individual tetramers, as well as the assembly of dimers into tetramers. Redox-dependent and redox-independent activation of p53 seem to require different amounts of Ref-1.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":2682,"ComplexName":"Bcl-xL-p53-PUMA complex, DNA damage induced","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P02340;Q64373;Q99ML1","subunits.Entrez.IDs.":"22059;12048;170770","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0006915;GO:0005737","GO.description":"apoptotic process;cytoplasm","FunCat.ID":"40.10.02;70.03","FunCat.description":"apoptosis (type I programmed cell death);cytoplasm","PubMed.ID":16151013,"subunits.Protein.name.":"Cellular tumor antigen p53 ;Bcl-2-like protein 1 ;Bcl-2-binding component 3","subunits.Gene.name.":"Tp53;Bcl2l1;Bbc3","subunits.Gene.name.syn.":"P53 Trp53;Bcl2l Bclx;Puma","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"PUMA appeared to be the major regulator of the p53\\u00b7Bcl-xL complex after UV treatment because no free cytoplasmic p53 was observed in Puma-/- cytosol. The authors support a model of p53-dependent, DNA damage-induced apoptosis that includes both nuclear and cytoplasmic functions of p53.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2683,"ComplexName":"PUMA-Bcl-xL complex, DNA-damage induced","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q64373;Q99ML1","subunits.Entrez.IDs.":"12048;170770","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006915;GO:0005737","GO.description":"apoptotic process;cytoplasm","FunCat.ID":"40.10.02;70.03","FunCat.description":"apoptosis (type I programmed cell death);cytoplasm","PubMed.ID":16151013,"subunits.Protein.name.":"Bcl-2-like protein 1 ;Bcl-2-binding component 3","subunits.Gene.name.":"Bcl2l1;Bbc3","subunits.Gene.name.syn.":"Bcl2l Bclx;Puma","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The p53-Bcl-xL complex was disrupted by incubation with PUMA. The p53 released from Bcl-xL by PUMA still activated BAX and induced mitochondrial cytochrome c release.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2684,"ComplexName":"p53-Bcl-xL complex, DNA-damage induced","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P02340;Q64373","subunits.Entrez.IDs.":"22059;12048","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006915;GO:0005737","GO.description":"apoptotic process;cytoplasm","FunCat.ID":"40.10.02;70.03","FunCat.description":"apoptosis (type I programmed cell death);cytoplasm","PubMed.ID":16151013,"subunits.Protein.name.":"Cellular tumor antigen p53 ;Bcl-2-like protein 1","subunits.Gene.name.":"Tp53;Bcl2l1","subunits.Gene.name.syn.":"P53 Trp53;Bcl2l Bclx","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In the presence of PUMA expression , the amount of p53 associated with Bcl-xL decreased after UV treatment, and this temporally correlated with the induction of apoptosis. PUMA may function to liberate p53 from Bcl-xL.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2685,"ComplexName":"RNA polymerase II (RNAPII)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15514;P13984;P19387;P19388;P24928;P30876;P35269;P36954;P52434;P52435;P53803;P61218;P62487;P62875;Q00403;Q9BWH6;Q9Y5B0","subunits.Entrez.IDs.":"5433;2963;5432;5434;5430;5431;2962;5438;5437;5439;5440;5435;5436;5441;2959;26015;9150","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0006351;GO:0003677;GO:0005634","GO.description":"transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11;16.03.01;70.10","FunCat.description":"TRANSCRIPTION;DNA binding;nucleus","PubMed.ID":15282305,"subunits.Protein.name.":"DNA-directed RNA polymerase II subunit RPB4 ;General transcription factor IIF subunit 2 ;DNA-directed RNA polymerase II subunit RPB3 ;DNA-directed RNA polymerases I, II, and III subunit RPABC1 ;DNA-directed RNA polymerase II subunit RPB1;DNA-directed RNA polymerase II subunit RPB2 ;General transcription factor IIF subunit 1;DNA-directed RNA polymerase II subunit RPB9 ;DNA-directed RNA polymerases I, II, and III subunit RPABC3 ;DNA-directed RNA polymerase II subunit RPB11-a ;DNA-directed RNA polymerases I, II, and III subunit RPABC4 ;DNA-directed RNA polymerases I, II, and III subunit RPABC2 ;DNA-directed RNA polymerase II subunit RPB7 ;DNA-directed RNA polymerases I, II, and III subunit RPABC5 ;Transcription initiation factor IIB;RNA polymerase II-associated protein 1;RNA polymerase II subunit A C-terminal domain phosphatase","subunits.Gene.name.":"POLR2D;GTF2F2;POLR2C;POLR2E;POLR2A;POLR2B;GTF2F1;POLR2I;POLR2H;POLR2J;POLR2K;POLR2F;POLR2G;POLR2L;GTF2B;RPAP1;CTDP1","subunits.Gene.name.syn.":";RAP30;;;POLR2;;RAP74;;;POLR2J1;;POLRF;RPB7;;TF2B TFIIB;KIAA1403;FCP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors demonstrate the purification of a functionally active human RNAPII by the use of doubly tagged subunits expressed in mammalian cells.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2686,"ComplexName":"BRCA1-core RNA polymerase II complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15514;P19387;P19388;P24928;P30876;P36954;P38398;P52434;P52435;P53803;P61218;P62487;P62875","subunits.Entrez.IDs.":"5433;5432;5434;5430;5431;5438;672;5437;5439;5440;5435;5436;5441","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006351;GO:0003677;GO:0005634","GO.description":"transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11;16.03.01;70.10","FunCat.description":"TRANSCRIPTION;DNA binding;nucleus","PubMed.ID":10725406,"subunits.Protein.name.":"DNA-directed RNA polymerase II subunit RPB4 ;DNA-directed RNA polymerase II subunit RPB3 ;DNA-directed RNA polymerases I, II, and III subunit RPABC1 ;DNA-directed RNA polymerase II subunit RPB1;DNA-directed RNA polymerase II subunit RPB2 ;DNA-directed RNA polymerase II subunit RPB9 ;Breast cancer type 1 susceptibility protein;DNA-directed RNA polymerases I, II, and III subunit RPABC3 ;DNA-directed RNA polymerase II subunit RPB11-a ;DNA-directed RNA polymerases I, II, and III subunit RPABC4 ;DNA-directed RNA polymerases I, II, and III subunit RPABC2 ;DNA-directed RNA polymerase II subunit RPB7 ;DNA-directed RNA polymerases I, II, and III subunit RPABC5","subunits.Gene.name.":"POLR2D;POLR2C;POLR2E;POLR2A;POLR2B;POLR2I;BRCA1;POLR2H;POLR2J;POLR2K;POLR2F;POLR2G;POLR2L","subunits.Gene.name.syn.":";;;POLR2;;;RNF53;;POLR2J1;;POLRF;RPB7;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The transcriptional coactivator BRCA1 interacts directly with the core Pol II complex in vitro.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2688,"ComplexName":"MT1-MMP-claudin-1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95832;P50281","subunits.Entrez.IDs.":"9076;4323","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0051098;GO:0005515;GO:0016504","GO.description":"regulation of binding;protein binding;peptidase activator activity","FunCat.ID":"18.01.07;16.01;18.02.01.01.03","FunCat.description":"regulation by binding / dissociation;protein binding;protease activator","PubMed.ID":11382769,"subunits.Protein.name.":"Claudin-1 ;Matrix metalloproteinase-14","subunits.Gene.name.":"CLDN1;MMP14","subunits.Gene.name.syn.":"CLD1 SEMP1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2689,"ComplexName":"Fra1-JunB DNA-protein complex","Organism":"Rat","Synonyms":"None","Cell.line":"heart muscle","subunits.UniProt.IDs.":"P10158;P24898","subunits.Entrez.IDs.":"25445;24517","Protein.complex.purification.method":"MI:0413-electrophoretic mobility shift assay","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04;16.03.01;70.10","FunCat.description":"transcriptional control;DNA binding;nucleus","PubMed.ID":12371906,"subunits.Protein.name.":"Fos-related antigen 1;Transcription factor jun-B","subunits.Gene.name.":"Fosl1;Junb","subunits.Gene.name.syn.":"Fra1;Jun-b","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Examination of the -1410 to -1362 bp promoter sequence of matrix metalloproteinase 2 (MMP-2) revealed apotential AP-1 complex binding site at -1394 to -1384bp.EMSA studies, combined with single and double antibodystudies, indicate the specific binding of Fra1-JunB heterodimersto the AP-1 site using nuclear extracts from fibroblasts culturedunder normoxic conditions. The studies demonstrate that a functional AP-1 site mediates MMP-2 transcription in cardiaccells through the binding of distinctive Fra1-JunB and FosB-JunB heterodimers.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2690,"ComplexName":"Atf2-c-Jun-c-Myc complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P09416;P17325;Q00969","subunits.Entrez.IDs.":"24577;24516;81647","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007049;GO:2001141;GO:0006355;GO:0003677;GO:0006950;GO:0005634","GO.description":"cell cycle;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;response to stress;nucleus","FunCat.ID":"10.03;11.02.03.04;16.03.01;32.01;70.10","FunCat.description":"cell cycle;transcriptional control;DNA binding;stress response;nucleus","PubMed.ID":15990869,"subunits.Protein.name.":"Myc proto-oncogene protein ;Transcription factor AP-1 ;Cyclic AMP-dependent transcription factor ATF-2","subunits.Gene.name.":"Myc;Jun;Atf2","subunits.Gene.name.syn.":";Rjg-9;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"c-Myc forms a ternary complex with ATF2/c-Jun through its direct binding to ATF2. ATF2/c-Jun complex binds the ATF/CRE DNA motif and c-Myc is recruited to the proximal region of the ATF3 promoter. The authors describe a functional link between the stress response gene ATF3 and the proto-oncogene c-myc.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2692,"ComplexName":"SMAD3-SMAD4-cJun-cFos complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P01100;P05412;P84022;Q13485","subunits.Entrez.IDs.":"2353;3725;4088;4089","Protein.complex.purification.method":"MI:0412- electrophoretic mobility supershift assay","GO.ID":"GO:0045893;GO:0003677;GO:0007179;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"11.02.03.04.01;16.03.01;30.05.01.18.01;70.10","FunCat.description":"transcription activation;DNA binding;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":9732876,"subunits.Protein.name.":"Proto-oncogene c-Fos ;Transcription factor AP-1 ;Mothers against decapentaplegic homolog 3;Mothers against decapentaplegic homolog 4","subunits.Gene.name.":"FOS;JUN;SMAD3;SMAD4","subunits.Gene.name.syn.":"G0S7;;MADH3;DPC4 MADH4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2693,"ComplexName":"NFAT-JUN-FOS DNA-protein complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P01100;P05412;Q13469","subunits.Entrez.IDs.":"2353;3725;4773","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0045893;GO:0003677;GO:0006955","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;immune response","FunCat.ID":"11.02.03.04.01;16.03.01;36.25.16","FunCat.description":"transcription activation;DNA binding;immune response","PubMed.ID":9510247,"subunits.Protein.name.":"Proto-oncogene c-Fos ;Transcription factor AP-1 ;Nuclear factor of activated T-cells, cytoplasmic 2","subunits.Gene.name.":"FOS;JUN;NFATC2","subunits.Gene.name.syn.":"G0S7;;NFAT1 NFATP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"NFAT and heterodimer Fos-Jun cooperatively bind a composite DNA site and synergistically activate the expression of many immune-response genes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2694,"ComplexName":"ERG-JUN-FOS DNA-protein complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P01100;P05412;P11308","subunits.Entrez.IDs.":"2353;3725;2078","Protein.complex.purification.method":"MI:0096- pull down; MI:0413- electrophoretic mobility shift assay; MI:0114- x-ray crystallography","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04;16.03.01;70.10","FunCat.description":"transcriptional control;DNA binding;nucleus","PubMed.ID":11278640,"subunits.Protein.name.":"Proto-oncogene c-Fos ;Transcription factor AP-1 ;Transcriptional regulator ERG","subunits.Gene.name.":"FOS;JUN;ERG","subunits.Gene.name.syn.":"G0S7;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors demonstrated that amino acids Arg(367) and Tyr(371) of the ETS domain, but not Asp374, play an important role in the recruitment of the Jun/Fos heterodimer by Erg. The authors propose that interdependent protein-protein and protein-DNA contacts regulate Erg-Jun/Fos-DNA complex assembly.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2695,"ComplexName":"ETS2-FOS-JUN complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P01100;P05412;P15036","subunits.Entrez.IDs.":"2353;3725;2114","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04;16.03.01;70.10","FunCat.description":"transcriptional control;DNA binding;nucleus","PubMed.ID":9334186,"subunits.Protein.name.":"Proto-oncogene c-Fos ;Transcription factor AP-1 ;Protein C-ets-2","subunits.Gene.name.":"FOS;JUN;ETS2","subunits.Gene.name.syn.":"G0S7;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results suggest that stromelysin-1 promoter DNA can enhance the ETS2/Fos/Jun interaction, perhaps by stabilizing protein contacts.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2699,"ComplexName":"ER-alpha-GRIP1-c-Jun complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P03372;P05412;Q9Y3R0","subunits.Entrez.IDs.":"2099;3725;23426","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:2001141;GO:0006355;GO:0023052","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;signaling","FunCat.ID":"11.02.03.04;30.01","FunCat.description":"transcriptional control;cellular signalling","PubMed.ID":11477071,"subunits.Protein.name.":"Estrogen receptor;Transcription factor AP-1 ;Glutamate receptor-interacting protein 1","subunits.Gene.name.":"ESR1;JUN;GRIP1","subunits.Gene.name.syn.":"ESR, NR3A1;;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors showed that ERalpha , c-Jun, and the p160 coactivator GRIP1 can form a multiprotein complex in vitro and in intact cells and that the ERalpha - c-Jun interaction could be crucial for the stability of this complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2700,"ComplexName":"ER-alpha-c-Jun complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P03372;P05412","subunits.Entrez.IDs.":"2099;3725","Protein.complex.purification.method":"MI:0096- pull down; MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0023052","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;signaling","FunCat.ID":"11.02.03.04;16.03.01;30.01","FunCat.description":"transcriptional control;DNA binding;cellular signalling","PubMed.ID":11477071,"subunits.Protein.name.":"Estrogen receptor;Transcription factor AP-1","subunits.Gene.name.":"ESR1;JUN","subunits.Gene.name.syn.":"ESR, NR3A1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"All experiments demonstrated that ER-alpha and c-Jun could interact in mammalian cells in a ligand-dependent manner.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2704,"ComplexName":"Ectodermin-SMAD4 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q13485;Q9UPN9","subunits.Entrez.IDs.":"4089;51592","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0007179;GO:0005634","GO.description":"protein ubiquitination;protein deubiquitination;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"14.07.05;30.05.01.18.01;70.10","FunCat.description":"modification by ubiquitination, deubiquitination;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":15820681,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 4;E3 ubiquitin-protein ligase TRIM33","subunits.Gene.name.":"SMAD4;TRIM33","subunits.Gene.name.syn.":"DPC4 MADH4;KIAA1113 RFG7 TIF1G","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2705,"ComplexName":"SMAD3-SMAD4-CTCF protein-DNA complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P49711;P84022;Q13485","subunits.Entrez.IDs.":"10664;4088;4089","Protein.complex.purification.method":"MI:0413- electrophoretic mobility shift assay","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0007179;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"11.02.03.04;16.03.01;30.05.01.18.01;70.10","FunCat.description":"transcriptional control;DNA binding;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":12099698,"subunits.Protein.name.":"Transcriptional repressor CTCF ;Mothers against decapentaplegic homolog 3;Mothers against decapentaplegic homolog 4","subunits.Gene.name.":"CTCF;SMAD3;SMAD4","subunits.Gene.name.syn.":";MADH3;DPC4 MADH4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors demonstrated that TGF-beta increases APP gene transcription in NHAs (normal human astrocytes) through activation of the proximal APP promoter domain, (-488) base pairs (bp) relative to the transcription start site (+1). In the presence of TGF-beta stimulation, Smads 3 and 4 specifically associated with the CTCF-APBbeta complex, likely enhancing APP gene transcription.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2706,"ComplexName":"SMAD3-SMAD4-SP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P08047;P84022;Q13485","subunits.Entrez.IDs.":"6667;4088;4089","Protein.complex.purification.method":"MI:0413- electrophoretic mobility shift assay; MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0007179;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"11.02.03.04;16.03.01;30.05.01.18.01;70.10","FunCat.description":"transcriptional control;DNA binding;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":11432852,"subunits.Protein.name.":"Transcription factor Sp1;Mothers against decapentaplegic homolog 3;Mothers against decapentaplegic homolog 4","subunits.Gene.name.":"SP1;SMAD3;SMAD4","subunits.Gene.name.syn.":"TSFP1;MADH3;DPC4 MADH4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors demonstrated that Sp1 and Smad3/Smad4 are able to bind the endoglin promoter at positions -50/-29 forming a multiprotein complex, and suggest their cooperation in the transcriptional activity of endoglin.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2707,"ComplexName":"SMAD3-SMAD4-FOXO3-FOXG1 complex","Organism":"Human","Synonyms":"None","Cell.line":"epithelium","subunits.UniProt.IDs.":"O43524;P55316;P84022;Q13485","subunits.Entrez.IDs.":"2309;2290;4088;4089","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0007179;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"11.02.03.04;16.03.01;30.05.01.18.01;70.10","FunCat.description":"transcriptional control;DNA binding;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":15084259,"subunits.Protein.name.":"Forkhead box protein O3;Forkhead box protein G1 ;Mothers against decapentaplegic homolog 3;Mothers against decapentaplegic homolog 4","subunits.Gene.name.":"FOXO3;FOXG1;SMAD3;SMAD4","subunits.Gene.name.syn.":"FKHRL1, FOXO3A;FKH2 FKHL1 FKHL2 FKHL3 FKHL4 FOXG1A FOXG1B FOXG1C;MADH3;DPC4 MADH4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results suggest that FoxG1 is a direct inhibitor of the FoxO-Smad transcriptional complex and a blocker of p21Cip1 induction by TGF-beta signals in neuroepithelial cells.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2708,"ComplexName":"SMAD3-SMAD4-cJUN complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P05412;P84022;Q13485","subunits.Entrez.IDs.":"3725;4088;4089","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:2001141;GO:0006355;GO:0007179;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"11.02.03.04;30.05.01.18.01;70.10","FunCat.description":"transcriptional control;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":10220381,"subunits.Protein.name.":"Transcription factor AP-1 ;Mothers against decapentaplegic homolog 3;Mothers against decapentaplegic homolog 4","subunits.Gene.name.":"JUN;SMAD3;SMAD4","subunits.Gene.name.syn.":";MADH3;DPC4 MADH4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"On TGF-beta  treatment, Smad3 and Smad4 heteromerize and enter the nucleus, where they can associate with TGF-beta-responsive promoters by binding a discreet DNA sequence and/or AP-1 members bound to AP-1 sites on the same promoter.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2709,"ComplexName":"MMP-9-TIMP-1-LRP complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P01033;P14780;Q07954","subunits.Entrez.IDs.":"7076;4318;4035","Protein.complex.purification.method":"MI:0047- far western blotting; MI:0411- enzyme linked immunosorbent assay","GO.ID":"GO:0030234;GO:0050790;GO:0006898;GO:0030198","GO.description":"enzyme regulator activity;regulation of catalytic activity;receptor-mediated endocytosis;extracellular matrix organization","FunCat.ID":"18.02.01;20.09.18.09.01.01;42.27.01","FunCat.description":"enzymatic activity regulation / enzyme regulator;receptor-mediated endocytosis;extracellular matrix","PubMed.ID":11279011,"subunits.Protein.name.":"Metalloproteinase inhibitor 1 ;Matrix metalloproteinase-9 ;Prolow-density lipoprotein receptor-related protein 1","subunits.Gene.name.":"TIMP1;MMP9;LRP1","subunits.Gene.name.syn.":"CLGI TIMP;CLG4B;A2MR APR","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The binding to LRP was blocked when excess RAP (39-kDa receptor-associated protein) was incubated along with MMP-9. Further results indicated that MMP-9 directly binds to LRP even in the absence of TIMP-1 and that reduction of MMP-9 abolishes its ability to bind LRP. The authors summarize that LRP is a functional receptor for MMP-9 and confirm that LRP is capable of mediating the cellular uptake of at least three MMPs (MMP-2, MMP-13, and MMP-9).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2710,"ComplexName":"LRP-1-Alpha-2-M-annexin VI complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P01023;P08133;Q07954","subunits.Entrez.IDs.":"2;309;4035","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006898","GO.description":"receptor-mediated endocytosis","FunCat.ID":"20.09.18.09.01.01","FunCat.description":"receptor-mediated endocytosis","PubMed.ID":15226301,"subunits.Protein.name.":"Alpha-2-macroglobulin ;Annexin A6 ;Prolow-density lipoprotein receptor-related protein 1","subunits.Gene.name.":"A2M;ANXA6;LRP1","subunits.Gene.name.syn.":"CPAMD5;ANX6;A2MR APR","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cell surface annexin VI is involved in the binding of 125I-alpha-2M(activated) to LRP-1 at neutral pH and forms ternary complexes with 125I-alpha-2M(activated) and LRP-1 at neutral pH.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2711,"ComplexName":"Amyloid beta protein oligomer","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P05067","subunits.Entrez.IDs.":"351","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0050896","GO.description":"response to stimulus","FunCat.ID":"36.25","FunCat.description":"animal specific systemic sensing and response","PubMed.ID":15834427,"subunits.Protein.name.":"Amyloid beta A4 protein","subunits.Gene.name.":"APP","subunits.Gene.name.syn.":"A4 AD1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Size fractionation showed that Abeta oligomers, not monomers or fibrils, were responsible for inhibiting long-term potentiation (LTP), and an Abeta antibody again prevented such inhibition.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":2712,"ComplexName":"Aph1a-Psen1-Ncstn complex","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P49769;P57716;Q8BVF7","subunits.Entrez.IDs.":"19164;59287;226548","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0096- pull down;MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0043161;GO:0006511;GO:0007219;GO:0005886","GO.description":"proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;Notch signaling pathway;plasma membrane","FunCat.ID":"14.13.01.01;30.05.02.14;70.02","FunCat.description":"proteasomal degradation (ubiquitin/proteasomal pathway);Notch-receptor signalling pathway;eukaryotic plasma membrane / membrane attached","PubMed.ID":15146195,"subunits.Protein.name.":"Presenilin-1 ;Nicastrin;Gamma-secretase subunit APH-1A","subunits.Gene.name.":"Psen1;Ncstn;Aph1a","subunits.Gene.name.syn.":"Ad3h Psnl1;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Presenilin, nicastrin and mAPH1a are essential components of the gamma-secretase complex that is required for the intramembrane proteolysis of membrane proteins including the amyloid-beta precursor protein (APP) and Notch.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2714,"ComplexName":"Ubiquitin E3 ligase (CHEK1, CUL1)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14757;Q13616","subunits.Entrez.IDs.":"1111;8454","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511;GO:0006974;GO:0005634","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"14.07.05;14.13.01.01;32.01.09;70.10","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway);DNA damage response;nucleus","PubMed.ID":16137618,"subunits.Protein.name.":"Serine/threonine-protein kinase Chk1 ;Cullin-1","subunits.Gene.name.":"CHEK1;CUL1","subunits.Gene.name.syn.":"CHK1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. The Chk1 kinase is a major effector of S phase checkpoint signaling during the cellular response to genotoxic stress. Replicative stress induces the polyubiquitination and degradation of Chk1 in human cells.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2715,"ComplexName":"Ubiquitin E3 ligase (CSN1, CSN8, HRT1, SKP1, SKP2, CUL1, CUL2, CUL3)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62877;P63208;Q13098;Q13309;Q13616;Q13617;Q13618;Q99627","subunits.Entrez.IDs.":"9978;6500;2873;6502;8454;8453;8452;10920","Protein.complex.purification.method":"MI:0047-far western blotting","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":11337588,"subunits.Protein.name.":"E3 ubiquitin-protein ligase RBX1;S-phase kinase-associated protein 1;COP9 signalosome complex subunit 1;S-phase kinase-associated protein 2;Cullin-1;Cullin-2;Cullin-3;COP9 signalosome complex subunit 8","subunits.Gene.name.":"RBX1;SKP1;GPS1;SKP2;CUL1;CUL2;CUL3;COPS8","subunits.Gene.name.syn.":"RNF75, ROC1;EMC19, OCP2, SKP1A, TCEB1L;COPS1, CSN1;FBXL1;None;None;KIAA0617;CSN8","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. SCF ubiquitin ligases consist of at least four subunits: CUL1 and HRT1 (=ROC1, RBX1), which  harbor a core ubiquitin ligase activity; a variable F-box protein that serves as a substrate receptor; and SKP1, which links the two modules together. Because CSN binds all cullins, it might be a global signal integrator that radiates its output onto various associated ubiquitin ligases to modulate their activity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2716,"ComplexName":"Elongator core complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95163;Q6IA86;Q9H9T3","subunits.Entrez.IDs.":"8518;55250;55140","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006354;GO:0005634","GO.description":"DNA-templated transcription, elongation;nucleus","FunCat.ID":"11.02.03.01.04;70.10","FunCat.description":"transcription elongation;nucleus","PubMed.ID":11714725,"subunits.Protein.name.":"Elongator complex protein 1 ;Elongator complex protein 2 ;Elongator complex protein 3","subunits.Gene.name.":"IKBKAP;ELP2;ELP3","subunits.Gene.name.syn.":"ELP1 IKAP;STATIP1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The core-Elongator complex does not have histone acetyltransferase activity despite containing the catalytic Elp3 subunit.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2717,"ComplexName":"Ubiquitin E3 ligase (TRIM25, DDX58)","Organism":"Human","Synonyms":"TRIM25 E3 ubiquitin ligase","Cell.line":"None","subunits.UniProt.IDs.":"O95786;Q14258","subunits.Entrez.IDs.":"23586;7706","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0016567;GO:0016579;GO:0035556;GO:0050896;GO:0005737","GO.description":"protein ubiquitination;protein deubiquitination;intracellular signal transduction;response to stimulus;cytoplasm","FunCat.ID":"14.07.05;30.01;36.25;70.03","FunCat.description":"modification by ubiquitination, deubiquitination;cellular signalling;animal specific systemic sensing and response;cytoplasm","PubMed.ID":17392790,"subunits.Protein.name.":"Probable ATP-dependent RNA helicase DDX58 ;E3 ubiquitin/ISG15 ligase TRIM25","subunits.Gene.name.":"DDX58;TRIM25","subunits.Gene.name.syn.":";EFP RNF147 ZNF147","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TRIM25 E3 ubiquitin ligase induces the Lys 63-linked ubiquitination of RIG-I, which is crucial for the cytosolic RIG-I signalling pathway to elicit host antiviral innate immunity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2718,"ComplexName":"MAD2-CDC20 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q12834;Q13257","subunits.Entrez.IDs.":"991;4085","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0007050;GO:0051098;GO:0005515;GO:0005634","GO.description":"cell cycle arrest;regulation of binding;protein binding;nucleus","FunCat.ID":"10.03.01.02;18.01.07;16.01;70.10","FunCat.description":"cell cycle arrest;regulation by binding / dissociation;protein binding;nucleus","PubMed.ID":10700282,"subunits.Protein.name.":"Cell division cycle protein 20 homolog ;Mitotic spindle assembly checkpoint protein MAD2A","subunits.Gene.name.":"CDC20;MAD2L1","subunits.Gene.name.syn.":";MAD2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The checkpoint protein Mad2 inhibits the activity of the anaphase promoting complex by sequestering Cdc20 until all chromosomes are aligned at the metaphase plate.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2719,"ComplexName":"Casein kinase II-HMG1 complex","Organism":"Human","Synonyms":"FCP1-specific kinase complex","Cell.line":"None","subunits.UniProt.IDs.":"P09429;P19784;P67870;P68400","subunits.Entrez.IDs.":"3146;1459;1460;1457","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006794;GO:0006796;GO:0006468;GO:0006470;GO:0046777;GO:0006464;GO:0030234;GO:0050790","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;cellular protein modification process;enzyme regulator activity;regulation of catalytic activity","FunCat.ID":"01.04;14.07.03;14.07;18.02.01","FunCat.description":"phosphate metabolism;modification by phosphorylation, dephosphorylation, autophosphorylation;protein modification;enzymatic activity regulation / enzyme regulator","PubMed.ID":12591939,"subunits.Protein.name.":"High mobility group protein B1 ;Casein kinase II subunit alpha' ;Casein kinase II subunit beta ;Casein kinase II subunit alpha","subunits.Gene.name.":"HMGB1;CSNK2A2;CSNK2B;CSNK2A1","subunits.Gene.name.syn.":"HMG1;CK2A2;CK2N G5A;CK2A1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"CK2 is comprised of the subunits CK2alpha , CK2alpha ', and CK2beta , and the differences in FCP1 kinase activity among the elution fractions reflect a dose-dependent effect related to the amount of CK2 present but do not depend on the presence of HMG1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2720,"ComplexName":"Casein kinase II complex","Organism":"Human","Synonyms":"CK2 complex; FCP1-specific kinase complex","Cell.line":"None","subunits.UniProt.IDs.":"P19784;P67870;P68400","subunits.Entrez.IDs.":"1459;1460;1457","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006794;GO:0006796;GO:0006468;GO:0006470;GO:0046777;GO:0006464;GO:0030234;GO:0050790","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;cellular protein modification process;enzyme regulator activity;regulation of catalytic activity","FunCat.ID":"01.04;14.07.03;14.07;18.02.01","FunCat.description":"phosphate metabolism;modification by phosphorylation, dephosphorylation, autophosphorylation;protein modification;enzymatic activity regulation / enzyme regulator","PubMed.ID":12591939,"subunits.Protein.name.":"Casein kinase II subunit alpha' ;Casein kinase II subunit beta ;Casein kinase II subunit alpha","subunits.Gene.name.":"CSNK2A2;CSNK2B;CSNK2A1","subunits.Gene.name.syn.":"CK2A2;CK2N G5A;CK2A1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"CK2 phosphorylates FCP1 and RAP74.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2721,"ComplexName":"HCF-1 complex","Organism":"Human","Synonyms":"HCF-1-associated protein complex","Cell.line":"None","subunits.UniProt.IDs.":"O15047;O15294;O75182;O75446;P07900;P08047;P11021;P11142;P34932;P51610;P61964;Q09028;Q13547;Q16576;Q92769;Q96ST3;Q9H7L9;Q9UBL3","subunits.Entrez.IDs.":"9739;8473;23309;8819;3320;6667;3309;3312;3308;3054;11091;5928;3065;5931;3066;25942;64426;9070","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0000910;GO:0000917;GO:2001141;GO:0006355;GO:0000902;GO:0016049;GO:0051276;GO:0005634;GO:0016575;GO:0016571","GO.description":"DNA topological change;cytokinesis;barrier septum assembly;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;cell morphogenesis;cell growth;chromosome organization;nucleus;histone deacetylation;histone methylation","FunCat.ID":"10.01.09.05;10.03.03;11.02.03.04;40.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);cytokinesis (cell division) /septum formation and hydrolysis;transcriptional control;cell growth / morphogenesis;organization of chromosome structure;nucleus","PubMed.ID":12670868,"subunits.Protein.name.":"Histone-lysine N-methyltransferase SETD1A;UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit;Paired amphipathic helix protein Sin3b;Histone deacetylase complex subunit SAP30;Heat shock protein HSP 90-alpha;Transcription factor Sp1;78 kDa glucose-regulated protein;Heat shock cognate 71 kDa protein;Heat shock 70 kDa protein 4;Host cell factor 1;WD repeat-containing protein 5;Histone-binding protein RBBP4;Histone deacetylase 1;Histone-binding protein RBBP7;Histone deacetylase 2;Paired amphipathic helix protein Sin3a;Sin3 histone deacetylase corepressor complex component SDS3;Set1/Ash2 histone methyltransferase complex subunit ASH2","subunits.Gene.name.":"SETD1A;OGT;SIN3B;SAP30;HSP90AA1;SP1;HSPA5;HSPA8;HSPA4;HCFC1;WDR5;RBBP4;HDAC1;RBBP7;HDAC2;SIN3A;SUDS3;ASH2L","subunits.Gene.name.syn.":"KIAA0339, KMT2F, SET1, SET1A;None;KIAA0700;None;HSP90A HSPC1 HSPCA;TSFP1;GRP78;HSC70, HSP73, HSPA10;APG2;HCF1, HFC1;BIG3;RBAP48;RPD3L1;RBAP46;None;None;SAP45 SDS3;ASH2L1","Disease.comment":"None","Subunits.comment":"Since the authors did not specify HSP90A, we used HSP90AA1.","Complex.comment":"HCF-1 can regulate transcription, both positively and negatively, through selective modulation of chromatin structure.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2722,"ComplexName":"Ubiquitin E3 ligase (DDB1, CUL4A, RBX1)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62877;Q13619;Q16531","subunits.Entrez.IDs.":"9978;8451;1642","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511;GO:0006974","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;cellular response to DNA damage stimulus","FunCat.ID":"14.07.05;14.13.01.01;32.01.09","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway);DNA damage response","PubMed.ID":15448697,"subunits.Protein.name.":"E3 ubiquitin-protein ligase RBX1;Cullin-4A;DNA damage-binding protein 1","subunits.Gene.name.":"RBX1;CUL4A;DDB1","subunits.Gene.name.syn.":"RNF75, ROC1;None;XAP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. The ubiquitin E3 ligase (DDB1, CUL4A and RBX1) perfoms targeted ubiquitination of CDT1 in response to DNA damage.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2723,"ComplexName":"ATM-NBS1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60934;Q13315","subunits.Entrez.IDs.":"4683;472","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0007- anti tag coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0000075;GO:0006468;GO:0006470;GO:0046777;GO:0023052;GO:0006974;GO:0009314;GO:0005634","GO.description":"cell cycle checkpoint;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;signaling;cellular response to DNA damage stimulus;response to radiation;nucleus","FunCat.ID":"10.03.01.03;14.07.03;30.01;32.01.09;32.01.13;70.10","FunCat.description":"cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);modification by phosphorylation, dephosphorylation, autophosphorylation;cellular signalling;DNA damage response;electromagnetic waves stress response (e.g. UV, X-ray);nucleus","PubMed.ID":10839544,"subunits.Protein.name.":"Nibrin ;Serine-protein kinase ATM","subunits.Gene.name.":"NBN;ATM","subunits.Gene.name.syn.":"NBS NBS1 P95;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"NBS1 was co-immunoprecipitated by the ATM antibody from untreated cells and in increased quantities from cells treated with ionizing radiation. The results indicate that phosphorylation of Ser 278 and Ser 343 in NBS1 contributes to both cellular resistance to ionizing radiation and formation of foci that contain NBS1 in response to ionizing radiation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2724,"ComplexName":"Ubiquitin E3 ligase (NFKBIA, BTRC, CUL1, SKP1A)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P25963;P63208;Q13616;Q9Y297","subunits.Entrez.IDs.":"4792;6500;8454;8945","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511;GO:0005737","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;cytoplasm","FunCat.ID":"14.07.05;14.13.01.01;70.03","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway);cytoplasm","PubMed.ID":10644755,"subunits.Protein.name.":"NF-kappa-B inhibitor alpha ;S-phase kinase-associated protein 1;Cullin-1;F-box/WD repeat-containing protein 1A","subunits.Gene.name.":"NFKBIA;SKP1;CUL1;BTRC","subunits.Gene.name.syn.":"IKBA MAD3 NFKBI;EMC19, OCP2, SKP1A, TCEB1L;None;BTRCP FBW1A FBXW1A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Ubiquitination-dependent destruction of NF-kappa-B inhibitor alpha is mediated by ubiquitin E3 ligases containing heterdimers and homodimers of beta-TrCP1 (BTRC) and beta-TrCP2 (FBXW11).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2725,"ComplexName":"Ubiquitin E3 ligase (NFKBIA, FBXW11, CUL1, SKP1A)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P25963;P63208;Q13616;Q9UKB1","subunits.Entrez.IDs.":"4792;6500;8454;23291","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511;GO:0005737","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;cytoplasm","FunCat.ID":"14.07.05;14.13.01.01;70.03","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway);cytoplasm","PubMed.ID":10644755,"subunits.Protein.name.":"NF-kappa-B inhibitor alpha ;S-phase kinase-associated protein 1;Cullin-1;F-box/WD repeat-containing protein 11","subunits.Gene.name.":"NFKBIA;SKP1;CUL1;FBXW11","subunits.Gene.name.syn.":"IKBA MAD3 NFKBI;EMC19, OCP2, SKP1A, TCEB1L;None;BTRCP2 FBW1B FBXW1B KIAA0696","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Ubiquitination-dependent destruction of NF-kappa-B inhibitor alpha is mediated by ubiquitin E3 ligases containing heterdimers and homodimers of beta-TrCP1 (BTRC) and beta-TrCP2 (FBXW11).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2726,"ComplexName":"PXN-ITGB5-PTK2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P18084;P49023;Q05397","subunits.Entrez.IDs.":"3693;5829;5747","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007229","GO.description":"integrin-mediated signaling pathway","FunCat.ID":"30.05.02.26","FunCat.description":"integrin receptor signalling pathway","PubMed.ID":11278329,"subunits.Protein.name.":"Integrin beta-5;Paxillin;Focal adhesion kinase 1","subunits.Gene.name.":"ITGB5;PXN;PTK2","subunits.Gene.name.syn.":";;FAK FAK1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The changes in the expression of PAR1 in a cell affect its invasive capabilities. These changes come about through the specific recruitment of the alpha(v)-beta 5 integrin, through cytoskeletal reorganization, and through distinct signaling at FACs.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2727,"ComplexName":"SRC-3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14920;O15111;P10155;Q15596;Q92793;Q9Y6K9;Q9Y6Q9","subunits.Entrez.IDs.":"3551;1147;6738;10499;1387;8517;8202","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0071- molecular sieving; MI:0226- ion exchange chromatography","GO.ID":"GO:0045893;GO:0006473;GO:0006476;GO:0007249;GO:0023052;GO:0006954;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;I-kappaB kinase/NF-kappaB signaling;signaling;inflammatory response;nucleus","FunCat.ID":"11.02.03.04.01;14.07.04;30.01.05.01.04;30.01;36.25.16.07;70.10","FunCat.description":"transcription activation;modification by acetylation, deacetylation;NIK-I-kappaB/NF-kappaB cascade;cellular signalling;inflammatory response;nucleus","PubMed.ID":11971985,"subunits.Protein.name.":"Inhibitor of nuclear factor kappa-B kinase subunit beta;Inhibitor of nuclear factor kappa-B kinase subunit alpha;60 kDa SS-A/Ro ribonucleoprotein ;Nuclear receptor coactivator 2 ;CREB-binding protein;NF-kappa-B essential modulator;Nuclear receptor coactivator 3","subunits.Gene.name.":"IKBKB;CHUK;TROVE2;NCOA2;CREBBP;IKBKG;NCOA3","subunits.Gene.name.syn.":"IKKB;IKKA, TCF16;RO60 SSA2;BHLHE75 SRC2 TIF2;CBP;FIP3, NEMO;AIB1, BHLHE42, RAC3, TRAM1, ACTR","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SRC-3 enhances NF-kappaB-mediated gene expression in concert with IKK.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2728,"ComplexName":"SRC-1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P10155;Q15596;Q15788;Q92793","subunits.Entrez.IDs.":"6738;10499;8648;1387","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0071- molecular sieving; MI:0226- ion exchange chromatography","GO.ID":"GO:0007249;GO:0023052;GO:0005634","GO.description":"I-kappaB kinase/NF-kappaB signaling;signaling;nucleus","FunCat.ID":"30.01.05.01.04;30.01;70.10","FunCat.description":"NIK-I-kappaB/NF-kappaB cascade;cellular signalling;nucleus","PubMed.ID":11971985,"subunits.Protein.name.":"60 kDa SS-A/Ro ribonucleoprotein ;Nuclear receptor coactivator 2 ;Nuclear receptor coactivator 1;CREB-binding protein","subunits.Gene.name.":"TROVE2;NCOA2;NCOA1;CREBBP","subunits.Gene.name.syn.":"RO60 SSA2;BHLHE75 SRC2 TIF2;BHLHE74, SRC1;CBP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2729,"ComplexName":"PIP complex","Organism":"Mouse","Synonyms":"None","Cell.line":"kidney","subunits.UniProt.IDs.":"O55222;Q99JW4;Q9EPC1","subunits.Entrez.IDs.":"16202;110829;57342","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007155;GO:0043067","GO.description":"cell adhesion;regulation of programmed cell death","FunCat.ID":"34.07;40.10.02.04","FunCat.description":"cell adhesion;regulation of apoptosis","PubMed.ID":15872073,"subunits.Protein.name.":"Integrin-linked protein kinase;LIM and senescent cell antigen-like-containing domain protein 1;Alpha-parvin","subunits.Gene.name.":"Ilk;Lims1;Parva","subunits.Gene.name.syn.":"None;Pinch1;Actp","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Disruption of the PINCH-1-ILK-alpha-parvin complex significantly reduced the podocyte-matrix adhesion and foot process formation. The PIP complex promotes glomerular mesangial matrix deposition and protects podocytes from apoptosis.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2730,"ComplexName":"Set1B complex","Organism":"Human","Synonyms":"None","Cell.line":"kidney","subunits.UniProt.IDs.":"P61964;Q15291;Q6UXN9;Q9P0U4;Q9UBL3;Q9UPS6","subunits.Entrez.IDs.":"11091;5929;80335;30827;9070;23067","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation;MI:0029-cosedimentation through density gradients","GO.ID":"GO:0006265;GO:0006349;GO:0018126;GO:0006479;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;regulation of gene expression by genetic imprinting;protein hydroxylation;protein methylation;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;10.01.09.07;14.07.09;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);DNA imprinting and other epigenetic effects;posttranslational modification of amino acids (e.g. hydroxylation, methylation);DNA binding;organization of chromosome structure;nucleus","PubMed.ID":17355966,"subunits.Protein.name.":"WD repeat-containing protein 5;Retinoblastoma-binding protein 5;WD repeat-containing protein 82;CXXC-type zinc finger protein 1;Set1/Ash2 histone methyltransferase complex subunit ASH2;Histone-lysine N-methyltransferase SETD1B","subunits.Gene.name.":"WDR5;RBBP5;WDR82;CXXC1;ASH2L;SETD1B","subunits.Gene.name.syn.":"BIG3;RBQ3;TMEM113, WDR82A;CFP1, CGBP, PCCX1, PHF18;ASH2L1;KIAA1076, KMT2G, SET1B","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The SET1B complex is a methyltransferase that produces trimethylated histone H3 at Lysine 4.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2731,"ComplexName":"Set1A complex","Organism":"Human","Synonyms":"SET1-CFP1 complex","Cell.line":"kidney","subunits.UniProt.IDs.":"O15047;P61964;Q15291;Q6UXN9;Q9P0U4;Q9UBL3","subunits.Entrez.IDs.":"9739;11091;5929;80335;30827;9070","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation;MI:0029-cosedimentation through density gradients","GO.ID":"GO:0006265;GO:0006349;GO:0018126;GO:0006479;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;regulation of gene expression by genetic imprinting;protein hydroxylation;protein methylation;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;10.01.09.07;14.07.09;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);DNA imprinting and other epigenetic effects;posttranslational modification of amino acids (e.g. hydroxylation, methylation);DNA binding;organization of chromosome structure;nucleus","PubMed.ID":17355966,"subunits.Protein.name.":"Histone-lysine N-methyltransferase SETD1A;WD repeat-containing protein 5;Retinoblastoma-binding protein 5;WD repeat-containing protein 82;CXXC-type zinc finger protein 1;Set1/Ash2 histone methyltransferase complex subunit ASH2","subunits.Gene.name.":"SETD1A;WDR5;RBBP5;WDR82;CXXC1;ASH2L","subunits.Gene.name.syn.":"KIAA0339, KMT2F, SET1, SET1A;BIG3;RBQ3;TMEM113, WDR82A;CFP1, CGBP, PCCX1, PHF18;ASH2L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The SET1A complex is a methyltransferase that produces mono-di- and trimethylated histone H3 at Lysine 4.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2732,"ComplexName":"Translocon-associated protein complex (TRAP complex)","Organism":"Dog","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P16967;P23438;P51571;Q9UNL2","subunits.Entrez.IDs.":"403951;403950;6748;6747","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0005509;GO:0005783","GO.description":"intracellular protein transport;protein targeting;protein transport;calcium ion binding;endoplasmic reticulum","FunCat.ID":"14.04;20.01.10;16.17.01;70.07","FunCat.description":"protein targeting, sorting and translocation;protein transport;calcium binding;endoplasmic reticulum","PubMed.ID":7916687,"subunits.Protein.name.":"Translocon-associated protein subunit alpha ;Translocon-associated protein subunit beta ;Translocon-associated protein subunit delta ;Translocon-associated protein subunit gamma","subunits.Gene.name.":"SSR1;SSR2;SSR4;SSR3","subunits.Gene.name.syn.":";;TRAPD;TRAPG","Disease.comment":"None","Subunits.comment":"Since SSR4 and SSR3 from dog were not available in the UniProt database at the time of annotation, the orthologous human protein was used.","Complex.comment":"TRAP complex regulates the retention of ER resident proteins.","SWISSPROT.organism":"Canis lupus familiaris (Dog) (Canis familiaris);Canis lupus familiaris (Dog) (Canis familiaris);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2733,"ComplexName":"Aph1a-pPsen1-nNcstn complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P97887;Q5PQQ3;Q8CGU6","subunits.Entrez.IDs.":"29192;365872;289231","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0043161;GO:0006511;GO:0007219;GO:0005886","GO.description":"proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;Notch signaling pathway;plasma membrane","FunCat.ID":"14.13.01.01;30.05.02.14;70.02","FunCat.description":"proteasomal degradation (ubiquitin/proteasomal pathway);Notch-receptor signalling pathway;eukaryotic plasma membrane / membrane attached","PubMed.ID":12297508,"subunits.Protein.name.":"Presenilin-1;Anterior pharynx defective 1 homolog A ;Nicastrin","subunits.Gene.name.":"Psen1;Aph1a;Ncstn","subunits.Gene.name.syn.":"Psnl1;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Presenilin, nicastrin and mAPH1a are essential components of the gamma-secretase complex that is required for the intramembrane proteolysis of membrane proteins including the amyloid-beta precursor protein (APP) and Notch. The authors use the splice variant mAPH-1a-L for the coimmunoprecipitation experiment. The authors show that endogenous mAPH-1, nicastrin, and the presenilin NTF:CTF heterodimers physically interact with each other in vivo and under the conditions that are compatible with gamma-secretase activity.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2734,"ComplexName":"APH1A-PSEN1-NCSTN complex","Organism":"Human","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P49768;Q92542;Q96BI3","subunits.Entrez.IDs.":"5663;23385;51107","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation;MI:0096- pull down","GO.ID":"GO:0043161;GO:0006511;GO:0007219;GO:0005886","GO.description":"proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;Notch signaling pathway;plasma membrane","FunCat.ID":"14.13.01.01;30.05.02.14;70.02","FunCat.description":"proteasomal degradation (ubiquitin/proteasomal pathway);Notch-receptor signalling pathway;eukaryotic plasma membrane / membrane attached","PubMed.ID":12297508,"subunits.Protein.name.":"Presenilin-1;Nicastrin;Gamma-secretase subunit APH-1A","subunits.Gene.name.":"PSEN1;NCSTN;APH1A","subunits.Gene.name.syn.":"AD3 PS1 PSNL1;KIAA0253;PSF","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Presenilin, nicastrin and mAPH1a are essential components of the gamma-secretase complex that is required for the intramembrane proteolysis of membrane proteins including the amyloid-beta precursor protein (APP) and Notch. The authors use the splice variant mAPH-1a-L for  experiments.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2735,"ComplexName":"APH1A-PSEN2-NCSTN complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P49810;Q92542;Q96BI3","subunits.Entrez.IDs.":"5664;23385;51107","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0043161;GO:0006511;GO:0007219","GO.description":"proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;Notch signaling pathway","FunCat.ID":"14.13.01.01;30.05.02.14","FunCat.description":"proteasomal degradation (ubiquitin/proteasomal pathway);Notch-receptor signalling pathway","PubMed.ID":12297508,"subunits.Protein.name.":"Presenilin-2 ;Nicastrin;Gamma-secretase subunit APH-1A","subunits.Gene.name.":"PSEN2;NCSTN;APH1A","subunits.Gene.name.syn.":"AD4 PS2 PSNL2 STM2;KIAA0253;PSF","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Presenilin, nicastrin and mAPH1a are essential components of the gamma-secretase complex that is required for the intramembrane proteolysis of membrane proteins including the amyloid-beta precursor protein (APP) and Notch. The authors use the splice variant mAPH-1a-L for  experiments. In an additional pull down experiment the authors show the interaction of APH1B with presenilin 2.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2736,"ComplexName":"TAJ-NgR1-LINGO-1 signaling complex","Organism":"Human","Synonyms":"None","Cell.line":"COS-7 cells","subunits.UniProt.IDs.":"Q96FE5;Q9BZR6;Q9NS68","subunits.Entrez.IDs.":"84894;65078;55504","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0051098;GO:0005515;GO:0022008;GO:0048699","GO.description":"regulation of binding;protein binding;neurogenesis;generation of neurons","FunCat.ID":"18.01.07;16.01;41.05.13","FunCat.description":"regulation by binding / dissociation;protein binding;neurogenesis","PubMed.ID":15694322,"subunits.Protein.name.":"Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1 ;Reticulon-4 receptor ;Tumor necrosis factor receptor superfamily member 19","subunits.Gene.name.":"LINGO1;RTN4R;TNFRSF19","subunits.Gene.name.syn.":"LERN1 LRRN6A;NOGOR;TAJ TROY","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors additionally analyzed interactions between TAJ-NgR1 and TAJ-LINGO-1. The authors show that TAJ (an orphan receptor in the TNF family), broadly expressed in postnatal and adult neurons, binds to NgR1 and can replace p75 in the p75/NgR1/LINGO-1 complex to activate RhoA in the presence of myelin inhibitors.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2738,"ComplexName":"BLM complex II","Organism":"Human","Synonyms":"BLM-CII complex","Cell.line":"None","subunits.UniProt.IDs.":"P15927;P27694;P35244;P54132;Q13472;Q9H9A7","subunits.Entrez.IDs.":"6118;6117;6119;641;7156;80010","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0051276;GO:0006281;GO:0006974;GO:0005634","GO.description":"chromosome organization;DNA repair;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"42.10.03;10.01.05.01;32.01.09;70.10","FunCat.description":"organization of chromosome structure;DNA repair;DNA damage response;nucleus","PubMed.ID":12724401,"subunits.Protein.name.":"Replication protein A 32 kDa subunit ;Replication protein A 70 kDa DNA-binding subunit;Replication protein A 14 kDa subunit ;Bloom syndrome protein ;DNA topoisomerase 3-alpha ;RecQ-mediated genome instability protein 1","subunits.Gene.name.":"RPA2;RPA1;RPA3;BLM;TOP3A;RMI1","subunits.Gene.name.syn.":"REPA2 RPA32 RPA34;REPA1 RPA70;REPA3 RPA14;RECQ2 RECQL3;TOP3;C9orf76","Disease.comment":"BLM complex II is involved in Bloom syndrome (BS).","Subunits.comment":"Another subunit of the complex was found in the analysis, which has not been further characterized: BLAPp100.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2739,"ComplexName":"FA complex (Fanconi anemia complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15287;O15360;P27694;P54132;Q00597;Q13472;Q8NB91;Q9H9A7;Q9HB96;Q9NPI8;Q9NW38","subunits.Entrez.IDs.":"2189;2175;6117;641;2176;7156;2187;80010;2178;2188;55120","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0006974;GO:0005634","GO.description":"protein ubiquitination;protein deubiquitination;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"14.07.05;32.01.09;70.10","FunCat.description":"modification by ubiquitination, deubiquitination;DNA damage response;nucleus","PubMed.ID":12724401,"subunits.Protein.name.":"Fanconi anemia group G protein ;Fanconi anemia group A protein ;Replication protein A 70 kDa DNA-binding subunit;Bloom syndrome protein ;Fanconi anemia group C protein ;DNA topoisomerase 3-alpha ;Fanconi anemia group B protein ;RecQ-mediated genome instability protein 1 ;Fanconi anemia group E protein ;Fanconi anemia group F protein ;E3 ubiquitin-protein ligase FANCL","subunits.Gene.name.":"FANCG;FANCA;RPA1;BLM;FANCC;TOP3A;FANCB;RMI1;FANCE;FANCF;FANCL","subunits.Gene.name.syn.":"XRCC9;FAA FACA FANCH;REPA1 RPA70;RECQ2 RECQL3;FAC FACC;TOP3;;C9orf76;FACE;;PHF9","Disease.comment":"FA complex is involved in Fanconi anemia (FA) disease.","Subunits.comment":"None","Complex.comment":"The FA complex contains several other proteins of unknown function, called FAAPs.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2740,"ComplexName":"MutS-alpha complex","Organism":"Human","Synonyms":"MSH2-MSH6 complex","Cell.line":"None","subunits.UniProt.IDs.":"P43246;P52701","subunits.Entrez.IDs.":"4436;2956","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006281;GO:0006974;GO:0005634","GO.description":"DNA repair;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;32.01.09;70.10","FunCat.description":"DNA repair;DNA damage response;nucleus","PubMed.ID":7604264,"subunits.Protein.name.":"DNA mismatch repair protein Msh2 ;DNA mismatch repair protein Msh6","subunits.Gene.name.":"MSH2;MSH6","subunits.Gene.name.syn.":";GTBP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The mismatch DNA repair complex hMSH2-MSH6, regulates BLM helicase activity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2742,"ComplexName":"Gata2-Tal1-Tcf3-Lmo2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O09100;P15806;P22091;P25801","subunits.Entrez.IDs.":"14461;21423;21349;16909","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0018- two hybrid","GO.ID":"GO:2001141;GO:0006355;GO:0030218;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;erythrocyte differentiation;nucleus","FunCat.ID":"11.02.03.04;43.03.07;70.10","FunCat.description":"transcriptional control;blood cell;nucleus","PubMed.ID":7568177,"subunits.Protein.name.":"Endothelial transcription factor GATA-2 ;Transcription factor E2-alpha ;T-cell acute lymphocytic leukemia protein 1 homolog ;Rhombotin-2","subunits.Gene.name.":"Gata2;Tcf3;Tal1;Lmo2","subunits.Gene.name.syn.":";Alf2 Me2 Tcfe2a;Scl Tal-1;Rbtn-2 Rbtn2 Rhom-2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complexes involving RBTN2, TAL1, and GATA1 (or -2), together with E47, the basic helix-loop-helix heterodimerization partner of TAL1, could be demonstrated. Thus, a molecular link exists between three proteins crucial for erythropoiesis, and the data suggest that variations in amounts of complexes involving RBTN2, TAL1, and GATA1 (or -2) could be important for erythroid differentiation.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2743,"ComplexName":"TRAF6-MALT1 complex","Organism":"Human","Synonyms":"None","Cell.line":"lymphocyte","subunits.UniProt.IDs.":"Q9UDY8;Q9Y4K3","subunits.Entrez.IDs.":"10892;7189","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0043085;GO:0008047","GO.description":"positive regulation of catalytic activity;enzyme activator activity","FunCat.ID":"18.02.01.01","FunCat.description":"enzyme activator","PubMed.ID":15125833,"subunits.Protein.name.":"Mucosa-associated lymphoid tissue lymphoma translocation protein 1;TNF receptor-associated factor 6","subunits.Gene.name.":"MALT1;TRAF6","subunits.Gene.name.syn.":"MLT;RNF85","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The CARD domain protein BCL10 and paracaspase MALT1 are essential for the activation of IkappaB kinase (IKK) and NF-kappaB in response to T cell receptor (TCR) stimulation. TRAF6 ubiquitin ligase and TAK1 protein kinase mediate IKK activation by BCL10 and MALT1. MALT1 binds to TRAF6 through the C-terminal binding sites and induces the oligomerization of TRAF6 to activate IKK.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2744,"ComplexName":"TRAF2-MALT1 complex","Organism":"Human","Synonyms":"None","Cell.line":"lymphocyte","subunits.UniProt.IDs.":"Q12933;Q9UDY8","subunits.Entrez.IDs.":"7186;10892","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0043085;GO:0008047","GO.description":"positive regulation of catalytic activity;enzyme activator activity","FunCat.ID":"18.02.01.01","FunCat.description":"enzyme activator","PubMed.ID":15125833,"subunits.Protein.name.":"TNF receptor-associated factor 2;Mucosa-associated lymphoid tissue lymphoma translocation protein 1","subunits.Gene.name.":"TRAF2;MALT1","subunits.Gene.name.syn.":"TRAP3;MLT","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2745,"ComplexName":"Ubiquitin ligase complex (TRAF6, TAB2, MALT1, UEV1A, BCL10)","Organism":"Human","Synonyms":"None","Cell.line":"lymphocyte","subunits.UniProt.IDs.":"O95999;Q13404;Q9NYJ8;Q9UDY8;Q9Y4K3","subunits.Entrez.IDs.":"8915;None;23118;10892;7189","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0043085;GO:0008047","GO.description":"protein ubiquitination;protein deubiquitination;positive regulation of catalytic activity;enzyme activator activity","FunCat.ID":"14.07.05;18.02.01.01","FunCat.description":"modification by ubiquitination, deubiquitination;enzyme activator","PubMed.ID":15125833,"subunits.Protein.name.":"B-cell lymphoma/leukemia 10;Ubiquitin-conjugating enzyme E2 variant 1;TGF-beta-activated kinase 1 and MAP3K7-binding protein 2;Mucosa-associated lymphoid tissue lymphoma translocation protein 1;TNF receptor-associated factor 6","subunits.Gene.name.":"BCL10;UBE2V1;TAB2;MALT1;TRAF6","subunits.Gene.name.syn.":"CIPER CLAP;CROC1 UBE2V UEV1;KIAA0733, MAP3K7IP2;MLT;RNF85","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The TRAF6 ubiquitin ligase and TAK1 kinase mediate IkappaB kinase (IKK) activation by BCL10 and MALT1 in T lymphocytes. NF-kappaB is a ubiquitous transcription factor that plays a central role in many biological processes including innate and adaptive immunity. NF-kappaB is regulated primarily through its association with an inhibitory protein of the IkappaB family, which binds to and retains NF-kappaB in the cytoplasm.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2746,"ComplexName":"NMDA receptor complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P35439;Q00959;Q9R1M7","subunits.Entrez.IDs.":"24408;24409;191573","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0006461;GO:0050789;GO:0005886;GO:0005783","GO.description":"intracellular protein transport;protein targeting;protein transport;protein complex assembly;regulation of biological process;plasma membrane;endoplasmic reticulum","FunCat.ID":"14.04;20.01.10;14.10;18;70.02;70.07","FunCat.description":"protein targeting, sorting and translocation;protein transport;assembly of protein complexes;REGULATION OF METABOLISM AND PROTEIN FUNCTION;eukaryotic plasma membrane / membrane attached;endoplasmic reticulum","PubMed.ID":11160393,"subunits.Protein.name.":"Glutamate receptor ionotropic, NMDA 1 ;Glutamate receptor ionotropic, NMDA 2A ;Glutamate receptor ionotropic, NMDA 3A","subunits.Gene.name.":"Grin1;Grin2a;Grin3a","subunits.Gene.name.syn.":"Nmdar1;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Glutamate receptors of the NMDA subtype are involved in a number of physiological and pathological processes in the brain, including synaptic plasticity, refinement of synaptic connections during development, and excitotoxicity.  Heteromeric combinations of NR1 and NR2 subunits are characterized by a high relative Ca21 permeability.  NR3A associates independently with both NR1-1a and NR2A in the endoplasmic reticulum, but only heteromeric complexes containing the NR1-1a NMDA receptor subunit are targeted to the plasma membrane.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2747,"ComplexName":"Gata1-Fog1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O35615;P17679","subunits.Entrez.IDs.":"22761;14460","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0051098;GO:0005515;GO:0051090;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;regulation of binding;protein binding;regulation of sequence-specific DNA binding transcription factor activity;nucleus","FunCat.ID":"11.02.03.04;18.01.07;16.01;18.02.09;70.10","FunCat.description":"transcriptional control;regulation by binding / dissociation;protein binding;regulator of transcription factor;nucleus","PubMed.ID":15920471,"subunits.Protein.name.":"Zinc finger protein ZFPM1 ;Erythroid transcription factor","subunits.Gene.name.":"Zfpm1;Gata1","subunits.Gene.name.syn.":"Fog Fog1;Gf-1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"GATA-1 functions as both an activator and a repressor. The Gata-1-Fog-1 complex has been shown to repress some genes, such as GATA-2, and activate others, such as beta-globin or the EKLF gene. Fog-1 mediates Gata-1 interactions with the MeCP1 complex, thus providing an explanation for the overlapping functions of these two factors in erythropoiesis.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2749,"ComplexName":"SETDB1-containing HMTase complex","Organism":"Human","Synonyms":"ESET-SETDB1 complex","Cell.line":"None","subunits.UniProt.IDs.":"Q15047;Q6VMQ6","subunits.Entrez.IDs.":"9869;55729","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0071- molecular sieving; MI:0226- ion exchange chromatography","GO.ID":"GO:0006265;GO:0045892;GO:0032774;GO:0018126;GO:0006479;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;RNA biosynthetic process;protein hydroxylation;protein methylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;11.02;14.07.09;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;RNA synthesis;posttranslational modification of amino acids (e.g. hydroxylation, methylation);organization of chromosome structure;nucleus","PubMed.ID":14536086,"subunits.Protein.name.":"Histone-lysine N-methyltransferase SETDB1;Activating transcription factor 7-interacting protein 1","subunits.Gene.name.":"SETDB1;ATF7IP","subunits.Gene.name.syn.":"KIAA0067 KMT1E;MCAF MCAF1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"ATF7IP stimulates the HMTase activity of ESET (SETDB1) through facilitating the ESET-dependent conversion of dimethyl H3-K9 to the trimethyl state.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2750,"ComplexName":"Gata1-Fog1-MeCP1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O09106;O35615;P17679;P70288;Q60972;Q60973;Q6PDQ2;Q8K4B0;Q8VHR5;Q924K8;Q9R190;Q9Z2D8;Q9Z2E1","subunits.Entrez.IDs.":"433759;22761;14460;15182;19646;245688;107932;116870;229542;116871;23942;17192;17191","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;organization of chromosome structure;nucleus","PubMed.ID":15920471,"subunits.Protein.name.":"Histone deacetylase 1;Zinc finger protein ZFPM1 ;Erythroid transcription factor ;Histone deacetylase 2;Histone-binding protein RBBP4 ;Histone-binding protein RBBP7;Chromodomain-helicase-DNA-binding protein 4;Metastasis-associated protein MTA1;Transcriptional repressor p66-beta ;Metastasis-associated protein MTA3;Metastasis-associated protein MTA2 ;Methyl-CpG-binding domain protein 3 ;Methyl-CpG-binding domain protein 2","subunits.Gene.name.":"Hdac1;Zfpm1;Gata1;Hdac2;Rbbp4;Rbbp7;Chd4;Mta1;Gatad2b;Mta3;Mta2;Mbd3;Mbd2","subunits.Gene.name.syn.":"None;Fog Fog1;Gf-1;Yy1bp;Rbap48;Rbap46;None;;;;Mta1l1;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Experiments strongly suggest that GATA-1, FOG-1 and MeCP1 form the repressive complex responsible for GATA-2 silencing.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2752,"ComplexName":"CARMA1-BCL10-MALT1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95999;Q9BXL7;Q9UDY8","subunits.Entrez.IDs.":"8915;84433;10892","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007249;GO:0005886","GO.description":"I-kappaB kinase/NF-kappaB signaling;plasma membrane","FunCat.ID":"30.01.05.01.04;70.02","FunCat.description":"NIK-I-kappaB/NF-kappaB cascade;eukaryotic plasma membrane / membrane attached","PubMed.ID":17478723,"subunits.Protein.name.":"B-cell lymphoma/leukemia 10;Caspase recruitment domain-containing protein 11 ;Mucosa-associated lymphoid tissue lymphoma translocation protein 1","subunits.Gene.name.":"BCL10;CARD11;MALT1","subunits.Gene.name.syn.":"CIPER CLAP;CARMA1;MLT","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The multiprotein complex consisting of the membrane-associated adapter protein CARMA1, the caspase-like protein MALT1, and the adapter protein BCL-10 is critical for TCR-dependent activation of the I{kappa}B kinase complex and subsequent NF-{kappa}B nuclear translocation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2753,"ComplexName":"FYB-CARMA1-BCL-10-MALT1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15117;O95999;Q9BXL7;Q9UDY8","subunits.Entrez.IDs.":"2533;8915;84433;10892","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007249;GO:0005886","GO.description":"I-kappaB kinase/NF-kappaB signaling;plasma membrane","FunCat.ID":"30.01.05.01.04;70.02","FunCat.description":"NIK-I-kappaB/NF-kappaB cascade;eukaryotic plasma membrane / membrane attached","PubMed.ID":17478723,"subunits.Protein.name.":"FYN-binding protein ;B-cell lymphoma/leukemia 10;Caspase recruitment domain-containing protein 11 ;Mucosa-associated lymphoid tissue lymphoma translocation protein 1","subunits.Gene.name.":"FYB;BCL10;CARD11;MALT1","subunits.Gene.name.syn.":"SLAP130;CIPER CLAP;CARMA1;MLT","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"FYB (ADAP) was found to be an integral part of the multiprotein complex consisting of the membrane-associated adapter protein CARMA1, the caspase-like protein MALT1, and the adapter protein BCL-10, which is critical for TCR-dependent activation of the I{kappa}B kinase complex and subsequent NF-{kappa}B nuclear translocation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2754,"ComplexName":"JUND-FOSB-SMAD3-SMAD4 complex","Organism":"Human","Synonyms":"TRE binding complex","Cell.line":"None","subunits.UniProt.IDs.":"P17535;P53539;P84022;Q13485","subunits.Entrez.IDs.":"3727;2354;4088;4089","Protein.complex.purification.method":"MI:0412- electrophoretic mobility supershift assay","GO.ID":"GO:2001141;GO:0006355;GO:0007167;GO:0006915;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;enzyme linked receptor protein signaling pathway;apoptotic process;nucleus","FunCat.ID":"11.02.03.04;30.05.01;40.10.02;70.10","FunCat.description":"transcriptional control;receptor enzyme mediated signalling;apoptosis (type I programmed cell death);nucleus","PubMed.ID":10942775,"subunits.Protein.name.":"Transcription factor jun-D;Protein fosB ;Mothers against decapentaplegic homolog 3;Mothers against decapentaplegic homolog 4","subunits.Gene.name.":"JUND;FOSB;SMAD3;SMAD4","subunits.Gene.name.syn.":";G0S3;MADH3;DPC4 MADH4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors found that only JunD and FosB, but not the other components of the AP-1 complex, are markedly induced during TGF-beta 1-dependent apoptosis. FosB enhanced Smad3\\u00b7Smad4-dependent transcription, and its dominant-negative form blocked TGF-beta 1-dependent apoptosis but not growth inhibition. These results suggest that JunD\\u00b7FosB activates transcription of a putative target gene for TGF-beta 1, which is responsible for apoptosis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2755,"ComplexName":"17S U2 snRNP","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15042;O43143;O75533;O75937;O75940;P08579;P09661;P10809;P14678;P26368;P62304;P62306;P62308;P62314;P62316;P62318;Q01081;Q07955;Q12874;Q12931;Q13435;Q15393;Q15427;Q15428;Q15459;Q7L014;Q7RTV0;Q8IWX8;Q96I25;Q9BWJ5;Q9P0W2;Q9UHX1;Q9Y3B4","subunits.Entrez.IDs.":"23350;1665;23451;22826;10285;6629;6627;3329;6628;11338;6635;6636;6637;6632;6633;6634;7307;6426;10946;10131;10992;23450;10262;8175;10291;9879;84844;10523;84991;83443;10362;22827;51639","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008380;GO:0005634","GO.description":"RNA splicing;nucleus","FunCat.ID":"11.04.03.01;70.10","FunCat.description":"splicing;nucleus","PubMed.ID":12234937,"subunits.Protein.name.":"U2 snRNP-associated SURP motif-containing protein ;Pre-mRNA-splicing factor ATP-dependent RNA helicase DHX15 ;Splicing factor 3B subunit 1 ;DnaJ homolog subfamily C member 8 ;Survival of motor neuron-related-splicing factor 30 ;U2 small nuclear ribonucleoprotein B'' ;U2 small nuclear ribonucleoprotein A' ;60 kDa heat shock protein, mitochondrial ;Small nuclear ribonucleoprotein-associated proteins B and B' ;Splicing factor U2AF 65 kDa subunit ;Small nuclear ribonucleoprotein E ;Small nuclear ribonucleoprotein F ;Small nuclear ribonucleoprotein G ;Small nuclear ribonucleoprotein Sm D1 ;Small nuclear ribonucleoprotein Sm D2 ;Small nuclear ribonucleoprotein Sm D3 ;Splicing factor U2AF 35 kDa subunit ;Serine/arginine-rich splicing factor 1 ;Splicing factor 3A subunit 3 ;Heat shock protein 75 kDa, mitochondrial ;Splicing factor 3B subunit 2 ;Splicing factor 3B subunit 3;Splicing factor 3B subunit 4 ;Splicing factor 3A subunit 2 ;Splicing factor 3A subunit 1 ;Probable ATP-dependent RNA helicase DDX46 ;PHD finger-like domain-containing protein 5A ;Calcium homeostasis endoplasmic reticulum protein ;Splicing factor 45 ;Splicing factor 3B subunit 5 ;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related;Poly;Splicing factor 3B subunit 6","subunits.Gene.name.":"U2SURP;DHX15;SF3B1;DNAJC8;SMNDC1;SNRPB2;SNRPA1;HSPD1;SNRPB;U2AF2;SNRPE;SNRPF;SNRPG;SNRPD1;SNRPD2;SNRPD3;U2AF1;SRSF1;SF3A3;TRAP1;SF3B2;SF3B3;SF3B4;SF3A2;SF3A1;DDX46;PHF5A;CHERP;RBM17;SF3B5;HMG20B;PUF60;SF3B6","subunits.Gene.name.syn.":"KIAA0332 SR140;DBP1 DDX15;SAP155;SPF31;SMNR SPF30;;;HSP60;COD SNRPB1;U2AF65;;PBSCF;PBSCG;;SNRPD1;;U2AF35 U2AFBP;ASF SF2 SF2P33 SFRS1;SAP61;HSP75;SAP145;KIAA0017 SAP130;SAP49;SAP62;SAP114;KIAA0801;;DAN26 SCAF6;SPF45;SF3B10;BRAF35 HMGX2 HMGXB2 SMARCE1R;FIR ROBPI SIAHBP1;SAP14 SF3B14 SF3B14A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Spliceosome assembly is initiated by the interaction of the U1 snRNP with the 5' splice site, forming the E complex. The latter also contains the 17S U2 snRNP, which at this stage associates via a non-base pairing interaction. In a subsequent ATP-dependent step, the U2 snRNA base pairs with the branch site of the pre-mRNA leading to stable association of the U2 snRNP and formation of the so-called A complex or prespliceosome.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2756,"ComplexName":"Ubiquitin-protein-ligase (UBE2N, UBE2V2/MMS2)","Organism":"Human","Synonyms":"TRIKA1","Cell.line":"None","subunits.UniProt.IDs.":"P61088;Q15819","subunits.Entrez.IDs.":"7334;7336","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0006464;GO:0019209;GO:0023052","GO.description":"protein ubiquitination;protein deubiquitination;cellular protein modification process;kinase activator activity;signaling","FunCat.ID":"14.07.05;14.07;18.02.01.01.05;30.01","FunCat.description":"modification by ubiquitination, deubiquitination;protein modification;kinase activator;cellular signalling","PubMed.ID":11460167,"subunits.Protein.name.":"Ubiquitin-conjugating enzyme E2 N;Ubiquitin-conjugating enzyme E2 variant 2","subunits.Gene.name.":"UBE2N;UBE2V2","subunits.Gene.name.syn.":"BLU;MMS2 UEV2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TRAF6 is a signal transducer that activates IkappaB kinase (IKK) and Jun amino-terminal kinase (JNK) in response to pro-inflammatory mediators such as interleukin-1 (IL-1) and lipopolysaccharides (LPS). IKK activation by TRAF6 requires two intermediary factors, TRAF6-regulated IKK activator 1 (TRIKA1) and TRIKA2. TRIKA1 is a dimeric ubiquitin-conjugating enzyme complex composed of UBE2N and UBE2V1 or the functionally equivalent UBE2V2. This Ubiquitin-protein ligase complex, together with TRAF6, catalyses the formation of a Lys 63 (K63)-linked polyubiquitin chain that mediates IKK activation through a unique proteasome-independent mechanism.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2757,"ComplexName":"SMN complex, U7 snRNA specific","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P14678;P62304;P62306;P62308;P62318;P83369;Q969L4","subunits.Entrez.IDs.":"6628;6635;6636;6637;6634;134353;84967","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008380;GO:0032774;GO:0006461;GO:0003723;GO:0005737;GO:0005634","GO.description":"RNA splicing;RNA biosynthetic process;protein complex assembly;RNA binding;cytoplasm;nucleus","FunCat.ID":"11.04.03.01;11.02;14.10;16.03.03;70.03;70.10","FunCat.description":"splicing;RNA synthesis;assembly of protein complexes;RNA binding;cytoplasm;nucleus","PubMed.ID":12975319,"subunits.Protein.name.":"Small nuclear ribonucleoprotein-associated proteins B and B' ;Small nuclear ribonucleoprotein E ;Small nuclear ribonucleoprotein F ;Small nuclear ribonucleoprotein G ;Small nuclear ribonucleoprotein Sm D3 ;U7 snRNA-associated Sm-like protein LSm11;U7 snRNA-associated Sm-like protein LSm10","subunits.Gene.name.":"SNRPB;SNRPE;SNRPF;SNRPG;SNRPD3;LSM11;LSM10","subunits.Gene.name.syn.":"COD SNRPB1;;PBSCF;PBSCG;;;","Disease.comment":"Spinal muscular atrophy (SMA)","Subunits.comment":"None","Complex.comment":"The Lsm11 protein of the U7 snRNA specific SMN complex plays an important role in histone RNA 3' end processing.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2758,"ComplexName":"TAK1 complex","Organism":"Human","Synonyms":"TRIKA2 protein kinase complex (TAK1, TAB1, TAB2)","Cell.line":"HeLa cell line","subunits.UniProt.IDs.":"O43318;Q15750;Q9NYJ8","subunits.Entrez.IDs.":"6885;10454;23118","Protein.complex.purification.method":"MI:0091-chromatography technologies;MI:0019-coimmunoprecipitation","GO.ID":"GO:0006468;GO:0007249;GO:0007254","GO.description":"protein phosphorylation;I-kappaB kinase/NF-kappaB signaling;JNK cascade","FunCat.ID":"14.07.03;30.01.05.01.04;30.01.05.01.02","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;NIK-I-kappaB/NF-kappaB cascade;JNK cascade","PubMed.ID":11460167,"subunits.Protein.name.":"Mitogen-activated protein kinase kinase kinase 7;TGF-beta-activated kinase 1 and MAP3K7-binding protein 1;TGF-beta-activated kinase 1 and MAP3K7-binding protein 2","subunits.Gene.name.":"MAP3K7;TAB1;TAB2","subunits.Gene.name.syn.":"TAK1;MAP3K7IP1;KIAA0733, MAP3K7IP2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TAK1 complex stimulates IKK/NF-kappaB in the presence of UBC13-UEV1A complex and TRAF6.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2759,"ComplexName":"MBD1-MCAF complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q6VMQ6;Q9UIS9","subunits.Entrez.IDs.":"55729;4152","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0006265;GO:0045892;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;organization of chromosome structure;nucleus","PubMed.ID":12665582,"subunits.Protein.name.":"Activating transcription factor 7-interacting protein 1 ;Methyl-CpG-binding domain protein 1","subunits.Gene.name.":"ATF7IP;MBD1","subunits.Gene.name.syn.":"MCAF MCAF1;CXXC3 PCM1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"MBD1 directly prevents transcription from methylated promoters in a histone deacetylation-independent manner, through interacting with MCAF. MBD1 competes with Sp1 for binding to MCAF. MBD1-MCAF complex blocks transcription through affecting Sp1 on methylated promoter regions.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2760,"ComplexName":"SMAD3-SMAD4-FOXO3 complex","Organism":"Human","Synonyms":"None","Cell.line":"epithelium","subunits.UniProt.IDs.":"O43524;P84022;Q13485","subunits.Entrez.IDs.":"2309;4088;4089","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0007179;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"11.02.03.04;16.03.01;30.05.01.18.01;70.10","FunCat.description":"transcriptional control;DNA binding;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":15084259,"subunits.Protein.name.":"Forkhead box protein O3;Mothers against decapentaplegic homolog 3;Mothers against decapentaplegic homolog 4","subunits.Gene.name.":"FOXO3;SMAD3;SMAD4","subunits.Gene.name.syn.":"FKHRL1, FOXO3A;MADH3;DPC4 MADH4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Endogenous FoxO1, FoxO3, and FoxO4 bind to endogenous Smad2/3 and Smad4. Formation of these complexes was absolutely dependent on TGF-beta stimulation, as was the formation of a Smad2/3-Smad4 complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2761,"ComplexName":"SMAD3-SMAD4-FOXO1 complex","Organism":"Human","Synonyms":"None","Cell.line":"epithelium","subunits.UniProt.IDs.":"P84022;Q12778;Q13485","subunits.Entrez.IDs.":"4088;2308;4089","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0007179;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"11.02.03.04;16.03.01;30.05.01.18.01;70.10","FunCat.description":"transcriptional control;DNA binding;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":15084259,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 3;Forkhead box protein O1 ;Mothers against decapentaplegic homolog 4","subunits.Gene.name.":"SMAD3;FOXO1;SMAD4","subunits.Gene.name.syn.":"MADH3;FKHR FOXO1A;DPC4 MADH4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Endogenous FoxO1, FoxO3, and FoxO4 bind to endogenous Smad2/3 and Smad4. Formation of these complexes was absolutely dependent on TGF-beta stimulation, as was the formation of a Smad2/3-Smad4 complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2762,"ComplexName":"SMAD3-SMAD4-FOXO4 complex","Organism":"Human","Synonyms":"None","Cell.line":"epithelium","subunits.UniProt.IDs.":"P84022;P98177;Q13485","subunits.Entrez.IDs.":"4088;4303;4089","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0007179;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"11.02.03.04;16.03.01;30.05.01.18.01;70.10","FunCat.description":"transcriptional control;DNA binding;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":15084259,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 3;Forkhead box protein O4 ;Mothers against decapentaplegic homolog 4","subunits.Gene.name.":"SMAD3;FOXO4;SMAD4","subunits.Gene.name.syn.":"MADH3;AFX AFX1 MLLT7;DPC4 MADH4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Endogenous FoxO1, FoxO3, and FoxO4 bind to endogenous Smad2/3 and Smad4. Formation of these complexes was absolutely dependent on TGF-beta stimulation, as was the formation of a Smad2/3-Smad4 complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2763,"ComplexName":"MBD1-Suv39h1-HP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43463;P45973;Q9UIS9","subunits.Entrez.IDs.":"6839;23468;4152","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0006349;GO:0045892;GO:0018126;GO:0006479;GO:0005634","GO.description":"regulation of gene expression by genetic imprinting;negative regulation of transcription, DNA-templated;protein hydroxylation;protein methylation;nucleus","FunCat.ID":"10.01.09.07;11.02.03.04.03;14.07.09;70.10","FunCat.description":"DNA imprinting and other epigenetic effects;transcription repression;posttranslational modification of amino acids (e.g. hydroxylation, methylation);nucleus","PubMed.ID":12711603,"subunits.Protein.name.":"Histone-lysine N-methyltransferase SUV39H1 ;Chromobox protein homolog 5 ;Methyl-CpG-binding domain protein 1","subunits.Gene.name.":"SUV39H1;CBX5;MBD1","subunits.Gene.name.syn.":"KMT1A SUV39H;HP1A;CXXC3 PCM1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"MBD1 tethers the Suv39h1-HP1 complex to methylated DNA regions. MBD1 interacts with Suv39h1-HP1 complex via MBD domain.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2764,"ComplexName":"PRMT5 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14744","subunits.Entrez.IDs.":"10419","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0018126;GO:0006479;GO:0005737","GO.description":"protein hydroxylation;protein methylation;cytoplasm","FunCat.ID":"14.07.09;70.03","FunCat.description":"posttranslational modification of amino acids (e.g. hydroxylation, methylation);cytoplasm","PubMed.ID":11152681,"subunits.Protein.name.":"Protein arginine N-methyltransferase 5","subunits.Gene.name.":"PRMT5","subunits.Gene.name.syn.":"HRMT1L5 IBP72 JBP1 SKB1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"PRMT5 (protein-arginine methyltransferase) formes distinct homo-oligomeric complexes, including a dimer and tetramer. Recombinant PRMT5 protein methylates myelin basic protein, histone, and the amino terminus of fibrillarin.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":2765,"ComplexName":"PRMT1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q99873","subunits.Entrez.IDs.":"3276","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0018126;GO:0006479;GO:0005634","GO.description":"protein hydroxylation;protein methylation;nucleus","FunCat.ID":"14.07.09;70.10","FunCat.description":"posttranslational modification of amino acids (e.g. hydroxylation, methylation);nucleus","PubMed.ID":11152681,"subunits.Protein.name.":"Protein arginine N-methyltransferase 1","subunits.Gene.name.":"PRMT1","subunits.Gene.name.syn.":"HMT2 HRMT1L2 IR1B4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"PRMT1 (protein-arginine methyltransferase) formes distinct homo-oligomeric complexes, including a dimer and tetramer.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":2766,"ComplexName":"TERF2-RAP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12956;P13010;P49959;Q15554;Q92878;Q9BSI4;Q9NYB0","subunits.Entrez.IDs.":"2547;7520;4361;7014;10111;26277;54386","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0003677;GO:0006974;GO:0051276;GO:0005634","GO.description":"DNA binding;cellular response to DNA damage stimulus;chromosome organization;nucleus","FunCat.ID":"16.03.01;32.01.09;42.10.03;70.10","FunCat.description":"DNA binding;DNA damage response;organization of chromosome structure;nucleus","PubMed.ID":15383534,"subunits.Protein.name.":"X-ray repair cross-complementing protein 6 ;X-ray repair cross-complementing protein 5 ;Double-strand break repair protein MRE11A ;Telomeric repeat-binding factor 2 ;DNA repair protein RAD50 ;TERF1-interacting nuclear factor 2 ;Telomeric repeat-binding factor 2-interacting protein 1","subunits.Gene.name.":"XRCC6;XRCC5;MRE11A;TERF2;RAD50;TINF2;TERF2IP","subunits.Gene.name.syn.":"G22P1;G22P2;HNGS1 MRE11;TRBF2 TRF2;;TIN2;DRIP5 RAP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex is responsible for proper maintenance of telomere length and structure.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2767,"ComplexName":"RAD50-MRE11-NBN-p200-p350 complex","Organism":"Human","Synonyms":"None","Cell.line":"IMR-90 cells","subunits.UniProt.IDs.":"O60934;P49959;Q92878","subunits.Entrez.IDs.":"4683;4361;10111","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006308;GO:0006281;GO:0000075;GO:0003677;GO:0006974;GO:0005634","GO.description":"DNA catabolic process;DNA repair;cell cycle checkpoint;DNA binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"01.03.16.03;10.01.05.01;10.03.01.03;16.03.01;32.01.09;70.10","FunCat.description":"DNA degradation;DNA repair;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA binding;DNA damage response;nucleus","PubMed.ID":8756642,"subunits.Protein.name.":"Nibrin ;Double-strand break repair protein MRE11A ;DNA repair protein RAD50","subunits.Gene.name.":"NBN;MRE11A;RAD50","subunits.Gene.name.syn.":"NBS NBS1 P95;HNGS1 MRE11;","Disease.comment":"None","Subunits.comment":"Two other subunits of the complex were found in the analysis, which have not been further characterized: p350 and p200.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2768,"ComplexName":"IKK complex (NEMO, IKKB)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q6TMG5;Q9QY78","subunits.Entrez.IDs.":"309295;84351","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0003677;GO:0019209","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;DNA binding;kinase activator activity","FunCat.ID":"14.07.03;16.03.01;18.02.01.01.05","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;DNA binding;kinase activator","PubMed.ID":17419723,"subunits.Protein.name.":"NF-kappa-B essential modulator ;Inhibitor of nuclear factor kappa-B kinase subunit beta","subunits.Gene.name.":"Ikbkg;Ikbkb","subunits.Gene.name.syn.":"Nemo;Ikkb","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"NEMO molecules do not form a tripartite IKK complex with an IKKalpha-IKKbeta heterodimer.  NEMO is able to form a complex with the monomeric forms of IKKalpha and IKKbeta.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2769,"ComplexName":"IKK complex (NEMO)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q6TMG5","subunits.Entrez.IDs.":"309295","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0003677;GO:0019209","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;DNA binding;kinase activator activity","FunCat.ID":"14.07.03;16.03.01;18.02.01.01.05","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;DNA binding;kinase activator","PubMed.ID":17419723,"subunits.Protein.name.":"NF-kappa-B essential modulator","subunits.Gene.name.":"Ikbkg","subunits.Gene.name.syn.":"Nemo","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat)"}
{"ComplexID":2770,"ComplexName":"ITGA6-ITGB4-CD9 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"skin","subunits.UniProt.IDs.":"P16144;P21926;P23229","subunits.Entrez.IDs.":"3691;928;3655","Protein.complex.purification.method":"MI:0024-confirmational text mining","GO.ID":"GO:0006928","GO.description":"movement of cell or subcellular component","FunCat.ID":"34.05","FunCat.description":"cell motility","PubMed.ID":10711425,"subunits.Protein.name.":"Integrin beta-4;CD9 antigen;Integrin alpha-6","subunits.Gene.name.":"ITGB4;CD9;ITGA6","subunits.Gene.name.syn.":"None;MIC3 TSPAN29;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2771,"ComplexName":"RAD51-DMC1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q08297;Q61880","subunits.Entrez.IDs.":"19361;13404","Protein.complex.purification.method":"MI:0416- fluorescence microscopy; MI:0040- electron microscopy","GO.ID":"GO:0006281;GO:0007131;GO:0005634","GO.description":"DNA repair;reciprocal meiotic recombination;nucleus","FunCat.ID":"10.01.05.01;10.01.05.03.01;70.10","FunCat.description":"DNA repair;meiotic recombination;nucleus","PubMed.ID":11950880,"subunits.Protein.name.":"DNA repair protein RAD51 homolog 1 ;Meiotic recombination protein DMC1/LIM15 homolog","subunits.Gene.name.":"Rad51;Dmc1","subunits.Gene.name.syn.":"Rad51a Reca;Dmc1h Lim15","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2772,"ComplexName":"Ubiquitin E3 ligase (CRY1, SKP1A, CUL1, FBXL3)","Organism":"Human","Synonyms":"SCF(FBXL3) ubiquitin ligase complex","Cell.line":"None","subunits.UniProt.IDs.":"P63208;Q13616;Q16526;Q9UKT7","subunits.Entrez.IDs.":"6500;8454;1407;26224","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511;GO:0007624;GO:0048511;GO:0005634","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;ultradian rhythm;rhythmic process;nucleus","FunCat.ID":"14.07.05;14.13.01.01;34.11.11;70.10","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway);rhythm (e.g. circadian, ultradian);nucleus","PubMed.ID":17463251,"subunits.Protein.name.":"S-phase kinase-associated protein 1;Cullin-1;Cryptochrome-1;F-box/LRR-repeat protein 3","subunits.Gene.name.":"SKP1;CUL1;CRY1;FBXL3","subunits.Gene.name.syn.":"EMC19, OCP2, SKP1A, TCEB1L;None;PHLL1;FBL3A FBXL3A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Cry1 and Cry2, encode inhibitors of the Clock-Bmal1 complex that establish a negative-feedback loop. Cry1 and Cry2 proteins are ubiquitinated and degraded via the SCF(Fbxl3) ubiquitin ligase complex. This regulation by SCF(Fbxl3) is a prerequisite for the efficient and timely reactivation of Clock-Bmal1 and the consequent expression of Per1 and Per2, two regulators of the circadian clock that display tumor suppressor activity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2773,"ComplexName":"Ubiquitin E3 ligase (CRY2, SKP1A, CUL1, FBXL3)","Organism":"Human","Synonyms":"SCF(FBXL3) ubiquitin ligase complex","Cell.line":"None","subunits.UniProt.IDs.":"P63208;Q13616;Q49AN0;Q9UKT7","subunits.Entrez.IDs.":"6500;8454;1408;26224","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511;GO:0007624;GO:0048511;GO:0005634","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;ultradian rhythm;rhythmic process;nucleus","FunCat.ID":"14.07.05;14.13.01.01;34.11.11;70.10","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway);rhythm (e.g. circadian, ultradian);nucleus","PubMed.ID":17463251,"subunits.Protein.name.":"S-phase kinase-associated protein 1;Cullin-1;Cryptochrome-2;F-box/LRR-repeat protein 3","subunits.Gene.name.":"SKP1;CUL1;CRY2;FBXL3","subunits.Gene.name.syn.":"EMC19, OCP2, SKP1A, TCEB1L;None;KIAA0658;FBL3A FBXL3A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome. Cry1 and Cry2, encode inhibitors of the Clock-Bmal1 complex that establish a negative-feedback loop. Cry1 and Cry2 proteins are ubiquitinated and degraded via the SCF(Fbxl3) ubiquitin ligase complex. This regulation by SCF(Fbxl3) is a prerequisite for the efficient and timely reactivation of Clock-Bmal1 and the consequent expression of Per1 and Per2, two regulators of the circadian clock that display tumor suppressor activity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2774,"ComplexName":"MDC1-H2AFX-TP53BP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P16104;Q12888;Q14676","subunits.Entrez.IDs.":"3014;7158;9656","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0000075;GO:0003677;GO:0006974;GO:0005634","GO.description":"DNA repair;cell cycle checkpoint;DNA binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;10.03.01.03;16.03.01;32.01.09;70.10","FunCat.description":"DNA repair;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA binding;DNA damage response;nucleus","PubMed.ID":12607005,"subunits.Protein.name.":"Histone H2AX ;Tumor suppressor p53-binding protein 1 ;Mediator of DNA damage checkpoint protein 1","subunits.Gene.name.":"H2AFX;TP53BP1;MDC1","subunits.Gene.name.syn.":"H2AX;;KIAA0170 NFBD1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"MDC1 forms complexes with phosporylated H2AFX.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2775,"ComplexName":"MDC1-p53BP1-SMC1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q12888;Q14676;Q14683","subunits.Entrez.IDs.":"7158;9656;8243","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0000075;GO:0003677;GO:0005634","GO.description":"DNA repair;cell cycle checkpoint;DNA binding;nucleus","FunCat.ID":"10.01.05.01;10.03.01.03;16.03.01;70.10","FunCat.description":"DNA repair;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA binding;nucleus","PubMed.ID":12607005,"subunits.Protein.name.":"Tumor suppressor p53-binding protein 1 ;Mediator of DNA damage checkpoint protein 1 ;Structural maintenance of chromosomes protein 1A","subunits.Gene.name.":"TP53BP1;MDC1;SMC1A","subunits.Gene.name.syn.":";KIAA0170 NFBD1;DXS423E KIAA0178 SB1.8 SMC1 SMC1L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Interaction of MDC1 with 53BP1 and SMC1 is unaffected by DNA damage.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2776,"ComplexName":"RAD50-BRCA1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P38398;Q92878","subunits.Entrez.IDs.":"672;10111","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation; MI:0226- ion exchange chromatography","GO.ID":"GO:0006281;GO:0005634","GO.description":"DNA repair;nucleus","FunCat.ID":"10.01.05.01;70.10","FunCat.description":"DNA repair;nucleus","PubMed.ID":11504724,"subunits.Protein.name.":"Breast cancer type 1 susceptibility protein;DNA repair protein RAD50","subunits.Gene.name.":"BRCA1;RAD50","subunits.Gene.name.syn.":"RNF53;","Disease.comment":"BRCA1 is involved in breast cancer.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2777,"ComplexName":"Ecsit complex (Ecsit2-Smad4)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P97471;Q9QZH6","subunits.Entrez.IDs.":"17128;26940","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0007179;GO:0010074","GO.description":"transforming growth factor beta receptor signaling pathway;maintenance of meristem identity","FunCat.ID":"30.05.01.18.01;41.05.04","FunCat.description":"TGF-beta-receptor signalling pathway;embryogenesis","PubMed.ID":14633973,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 4 ;Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial","subunits.Gene.name.":"Smad4;Ecsit","subunits.Gene.name.syn.":"Dpc4 Madh4;Sitpec","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ecsit is a cytosolic adaptor protein essential for inflammatory response and embryonic development via the Toll-like and BMP (bone morphogenetic protein) signal transduction pathways, respectively. A mitochondrial function for Ecsit (an evolutionary conserved signaling intermediate in Toll pathways) in the assembly of mitochondrial complex I (NADH:ubiquinone oxidoreductase) has also been demonstrated.The authors focused on Ecsit isoform 2 because it is the only Ecsit isoform expressed in P19 cells. Ecsit2 could be coprecipitated with Smad4 from both treated and untreated cells, while Smad1 coprecipitated with Ecsit2 only after Bmp4 treatment.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2778,"ComplexName":"Ecsit complex (Ecsit2-Smad1)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P70340;Q9QZH6","subunits.Entrez.IDs.":"17125;26940","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0007179;GO:0010074","GO.description":"transforming growth factor beta receptor signaling pathway;maintenance of meristem identity","FunCat.ID":"30.05.01.18.01;41.05.04","FunCat.description":"TGF-beta-receptor signalling pathway;embryogenesis","PubMed.ID":14633973,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 1;Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial","subunits.Gene.name.":"Smad1;Ecsit","subunits.Gene.name.syn.":"Madh1 Madr1;Sitpec","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ecsit is a cytosolic adaptor protein essential for inflammatory response and embryonic development via the Toll-like and BMP (bone morphogenetic protein) signal transduction pathways, respectively. A mitochondrial function for Ecsit (an evolutionary conserved signaling intermediate in Toll pathways) in the assembly of mitochondrial complex I (NADH:ubiquinone oxidoreductase) has also been demonstrated. The authors focused on Ecsit2 because it is the only Ecsit isoform expressed in P19 cells. Ecsit2 could be coprecipitated with Smad4 from both treated and untreated cells, while Smad1 coprecipitated with Ecsit2 only after Bmp4 treatment. It seems that association of Ecsit2 with Smad1 is dependent on phosphorylation of Smad1 by ligand-activated Bmpr1a.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2779,"ComplexName":"Ecsit complex (Smad1-Smad4-Ecsit2)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P70340;P97471;Q9QZH6","subunits.Entrez.IDs.":"17125;17128;26940","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0007179;GO:0010074;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;transforming growth factor beta receptor signaling pathway;maintenance of meristem identity;nucleus","FunCat.ID":"11.02.03.04;16.03.01;30.05.01.18.01;41.05.04;70.10","FunCat.description":"transcriptional control;DNA binding;TGF-beta-receptor signalling pathway;embryogenesis;nucleus","PubMed.ID":14633973,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 1;Mothers against decapentaplegic homolog 4 ;Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial","subunits.Gene.name.":"Smad1;Smad4;Ecsit","subunits.Gene.name.syn.":"Madh1 Madr1;Dpc4 Madh4;Sitpec","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ecsit is a cytosolic adaptor protein essential for inflammatory response and embryonic development via the Toll-like and BMP (bone morphogenetic protein) signal transduction pathways, respectively. A mitochondrial function for Ecsit (an evolutionary conserved signaling intermediate in Toll pathways) in the assembly of mitochondrial complex I (NADH:ubiquinone oxidoreductase) has also been demonstrated. The authors focused on Ecsit2 because it is the only Ecsit isoform expressed in P19 cells. The authors describe that in resting cells, Ecsit binds constitutively to Smad4 and the Ecsit:Smad4 complex binds to promoters of certain target genes, without activating transcription. When the Bmp pathway is activated, phosphorylated Smad1 translocates to the nucleus and binds to the Ecsit:Smad4 complex to form a higher-order complex containing Ecsit, Smad1, and Smad4.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2780,"ComplexName":"Rab1-GTP-GM130 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q62839;Q6NYB7","subunits.Entrez.IDs.":"64528;81754","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006888;GO:0006900;GO:0016050;GO:0006906;GO:0005794","GO.description":"ER to Golgi vesicle-mediated transport;membrane budding;vesicle organization;vesicle fusion;Golgi apparatus","FunCat.ID":"20.09.07.03;20.09.07.25;20.09.07.27;70.08","FunCat.description":"ER to Golgi transport;vesicle formation;vesicle fusion;Golgi","PubMed.ID":11285137,"subunits.Protein.name.":"Golgin subfamily A member 2 ;Ras-related protein Rab-1A","subunits.Gene.name.":"Golga2;Rab1A","subunits.Gene.name.syn.":";Rab1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Interaction of GM130 was specific for the active GTP-bound conformation of Rab1. Since GM130 can directly interact with p115 the authors demonstrated that immunodepletion of p115 had no effect on Rab1-GM130 interaction.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2781,"ComplexName":"Rab1-GTP-p115 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P41542;Q6NYB7","subunits.Entrez.IDs.":"56042;81754","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006888;GO:0006900;GO:0016050;GO:0006906;GO:0005794","GO.description":"ER to Golgi vesicle-mediated transport;membrane budding;vesicle organization;vesicle fusion;Golgi apparatus","FunCat.ID":"20.09.07.03;20.09.07.25;20.09.07.27;70.08","FunCat.description":"ER to Golgi transport;vesicle formation;vesicle fusion;Golgi","PubMed.ID":11285137,"subunits.Protein.name.":"General vesicular transport factor p115 ;Ras-related protein Rab-1A","subunits.Gene.name.":"Uso1;Rab1A","subunits.Gene.name.syn.":"Vdp;Rab1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors demonstrated that Rab1-GTP interacts with two different tethering factors - p115 and the GM130 complex.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2782,"ComplexName":"Rab1-GTP-GM130-GRASP65 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O35254;Q62839;Q6NYB7","subunits.Entrez.IDs.":"56082;64528;81754","Protein.complex.purification.method":"MI:0096- pull down; MI:0019- coimmunoprecipitation","GO.ID":"GO:0006888;GO:0006900;GO:0016050;GO:0006906;GO:0005794","GO.description":"ER to Golgi vesicle-mediated transport;membrane budding;vesicle organization;vesicle fusion;Golgi apparatus","FunCat.ID":"20.09.07.03;20.09.07.25;20.09.07.27;70.08","FunCat.description":"ER to Golgi transport;vesicle formation;vesicle fusion;Golgi","PubMed.ID":11285137,"subunits.Protein.name.":"Golgi reassembly-stacking protein 1;Golgin subfamily A member 2 ;Ras-related protein Rab-1A","subunits.Gene.name.":"Gorasp1;Golga2;Rab1A","subunits.Gene.name.syn.":"Grasp65;;Rab1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors demonstrate that the cis-Golgi tethering protein GM130 forms a novel Rab1 effector complex that interacts with activated Rab1-GTP in a p115-independent manner and is required for coat protein II vesicle targeting/fusion with the cis-Golgi.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2783,"ComplexName":"BARD1-BRCA1-CSTF64 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P33240;P38398;Q99728","subunits.Entrez.IDs.":"1478;672;580","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0031123;GO:0031124;GO:0006974;GO:0005634","GO.description":"RNA 3'-end processing;mRNA 3'-end processing;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"11.04.03.05;32.01.09;70.10","FunCat.description":"3'-end processing;DNA damage response;nucleus","PubMed.ID":11257228,"subunits.Protein.name.":"Cleavage stimulation factor subunit 2 ;Breast cancer type 1 susceptibility protein;BRCA1-associated RING domain protein 1","subunits.Gene.name.":"CSTF2;BRCA1;BARD1","subunits.Gene.name.syn.":";RNF53;","Disease.comment":"BRCA1 is involved in breast cancer.","Subunits.comment":"None","Complex.comment":"DNA damage increases formation of a CstF-BARD1-BRCA1 inhibitory complex. Complex formation represses polyadenylation of mRNA.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2784,"ComplexName":"Alpha-2-M enhanceosome DNA-protein complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06536;P12841;P17325;P31503;P52631","subunits.Entrez.IDs.":"24413;314322;24516;171068;25125","Protein.complex.purification.method":"MI:0225- chromatin immunoprecipitation array","GO.ID":"GO:0045893;GO:0003677;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04.01;16.03.01;70.10","FunCat.description":"transcription activation;DNA binding;nucleus","PubMed.ID":14522952,"subunits.Protein.name.":"Glucocorticoid receptor ;Proto-oncogene c-Fos ;Transcription factor AP-1 ;POU domain, class 2, transcription factor 1 ;Signal transducer and activator of transcription 3","subunits.Gene.name.":"Nr3c1;Fos;Jun;Pou2f1;Stat3","subunits.Gene.name.syn.":"Grl;;Rjg-9;Oct-1 Otf-1 Otf1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Analysis done after IL-6 and Dex (Dexamethasone) treatment. The authors describe the association of severel proteins with the chromosomal (alpha)2-M enhanceosome and analyze the time course of assembly, disassembly, and stability of the enhanceosome.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2785,"ComplexName":"Alpha-2-M enhanceosome DNA-protein complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06536;P17325;P31503;P52631","subunits.Entrez.IDs.":"24413;24516;171068;25125","Protein.complex.purification.method":"MI:0225- chromatin immunoprecipitation array","GO.ID":"GO:0045893;GO:0003677;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04.01;16.03.01;70.10","FunCat.description":"transcription activation;DNA binding;nucleus","PubMed.ID":14522952,"subunits.Protein.name.":"Glucocorticoid receptor ;Transcription factor AP-1 ;POU domain, class 2, transcription factor 1 ;Signal transducer and activator of transcription 3","subunits.Gene.name.":"Nr3c1;Jun;Pou2f1;Stat3","subunits.Gene.name.syn.":"Grl;Rjg-9;Oct-1 Otf-1 Otf1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Analysis done after IL-6 and Dex (Dexamethasone) treatment. The authors describe the association of severel proteins with the chromosomal (alpha)2-M enhanceosome and analyze the time course of assembly, disassembly, and stability of the enhanceosome. They suggest a model of the sequential formation of complexes leading to the activation of the (alpha)2-M gene. OCT-1 and c-Jun bind constitutively the (alpha)2-M promoter. Dex-activated GR is recruited to the complex, possibly by interacting with c-Jun. IL-6 treatment recruits STAT3 to the complex, and STAT3 alone is competent to recruit Pol II and stimulate low levels of transcription.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2786,"ComplexName":"BRCA1 A complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P38398;Q6UWZ7;Q96RL1;Q99728","subunits.Entrez.IDs.":"672;84142;51720;580","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006281;GO:0000075;GO:0009314;GO:0005634","GO.description":"DNA repair;cell cycle checkpoint;response to radiation;nucleus","FunCat.ID":"10.01.05.01;10.03.01.03;32.01.13;70.10","FunCat.description":"DNA repair;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);electromagnetic waves stress response (e.g. UV, X-ray);nucleus","PubMed.ID":17525340,"subunits.Protein.name.":"Breast cancer type 1 susceptibility protein;BRCA1-A complex subunit Abraxas ;BRCA1-A complex subunit RAP80 ;BRCA1-associated RING domain protein 1","subunits.Gene.name.":"BRCA1;FAM175A;UIMC1;BARD1","subunits.Gene.name.syn.":"RNF53;ABRA1 CCDC98;RAP80 RXRIP110;","Disease.comment":"BRCA1 is involved in breast cancer.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2787,"ComplexName":"BRCA1 C complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P38398;Q96RL1;Q99708;Q99728","subunits.Entrez.IDs.":"672;51720;5932;580","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006310;GO:0000075;GO:0005634","GO.description":"DNA recombination;cell cycle checkpoint;nucleus","FunCat.ID":"10.01.05.03;10.03.01.03;70.10","FunCat.description":"DNA recombination;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);nucleus","PubMed.ID":17525340,"subunits.Protein.name.":"Breast cancer type 1 susceptibility protein;BRCA1-A complex subunit RAP80 ;DNA endonuclease RBBP8 ;BRCA1-associated RING domain protein 1","subunits.Gene.name.":"BRCA1;UIMC1;RBBP8;BARD1","subunits.Gene.name.syn.":"RNF53;RAP80 RXRIP110;CTIP;","Disease.comment":"BRCA1 is involved in breast cancer.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2788,"ComplexName":"BRCA1 B complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14867;P38398;Q99728","subunits.Entrez.IDs.":"571;672;580","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006310;GO:0005634","GO.description":"DNA recombination;nucleus","FunCat.ID":"10.01.05.03;70.10","FunCat.description":"DNA recombination;nucleus","PubMed.ID":17525340,"subunits.Protein.name.":"Transcription regulator protein BACH1 ;Breast cancer type 1 susceptibility protein;BRCA1-associated RING domain protein 1","subunits.Gene.name.":"BACH1;BRCA1;BARD1","subunits.Gene.name.syn.":";RNF53;","Disease.comment":"BRCA1 is involved in breast cancer.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2789,"ComplexName":"ETS2-ERG complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P11308;P15036","subunits.Entrez.IDs.":"2078;2114","Protein.complex.purification.method":"MI:0096- pull down; MI:0018- two hybrid","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04;16.03.01;70.10","FunCat.description":"transcriptional control;DNA binding;nucleus","PubMed.ID":9334186,"subunits.Protein.name.":"Transcriptional regulator ERG ;Protein C-ets-2","subunits.Gene.name.":"ERG;ETS2","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors found that different domains of ETS2 make contacts with the Fos/Jun complex and with other members of the Ets family to form stable heterotrimeric ETS2/Fos/Jun and heterodimeric ETS2/ERG and ETS2/ETS1 complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2790,"ComplexName":"ETS2-ETS1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P14921;P15036","subunits.Entrez.IDs.":"2113;2114","Protein.complex.purification.method":"MI:0096- pull down; MI:0018- two hybrid","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04;16.03.01;70.10","FunCat.description":"transcriptional control;DNA binding;nucleus","PubMed.ID":9334186,"subunits.Protein.name.":"Protein C-ets-1 ;Protein C-ets-2","subunits.Gene.name.":"ETS1;ETS2","subunits.Gene.name.syn.":"EWSR2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors found that different domains of ETS2 make contacts with the Fos/Jun complex and with other members of the Ets family to form stable heterotrimeric ETS2/Fos/Jun and heterodimeric ETS2/ERG and ETS2/ETS1 complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2791,"ComplexName":"MCM4-MCM6-MCM7 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P33991;P33993;Q14566","subunits.Entrez.IDs.":"4173;4176;4175","Protein.complex.purification.method":"MI:0091- chromatography technologies","GO.ID":"GO:0006794;GO:0006796;GO:0051276;GO:0006260;GO:0005524;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;chromosome organization;DNA replication;ATP binding;nucleus","FunCat.ID":"01.04;42.10.03;10.01.03;16.19.03;70.10","FunCat.description":"phosphate metabolism;organization of chromosome structure;DNA synthesis and replication;ATP binding;nucleus","PubMed.ID":9305914,"subunits.Protein.name.":"DNA replication licensing factor MCM4 ;DNA replication licensing factor MCM7 ;DNA replication licensing factor MCM6","subunits.Gene.name.":"MCM4;MCM7;MCM6","subunits.Gene.name.syn.":"CDC21;CDC47 MCM2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex has DNA helicase activity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2792,"ComplexName":"MCM2-MCM4-MCM6-MCM7 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P33991;P33993;P49736;Q14566","subunits.Entrez.IDs.":"4173;4176;4171;4175","Protein.complex.purification.method":"MI:0091- chromatography technologies; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006794;GO:0006796;GO:0051276;GO:0006260;GO:0005524;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;chromosome organization;DNA replication;ATP binding;nucleus","FunCat.ID":"01.04;42.10.03;10.01.03;16.19.03;70.10","FunCat.description":"phosphate metabolism;organization of chromosome structure;DNA synthesis and replication;ATP binding;nucleus","PubMed.ID":9305914,"subunits.Protein.name.":"DNA replication licensing factor MCM4 ;DNA replication licensing factor MCM7 ;DNA replication licensing factor MCM2 ;DNA replication licensing factor MCM6","subunits.Gene.name.":"MCM4;MCM7;MCM2;MCM6","subunits.Gene.name.syn.":"CDC21;CDC47 MCM2;BM28 CCNL1 CDCL1 KIAA0030;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex has DNA helicase activity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2793,"ComplexName":"Brd4-Rfc complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P35601;Q3UI84;Q8R323;Q9D0F6;Q9ESU6;Q9WUK4","subunits.Entrez.IDs.":"19687;106344;69263;72151;57261;19718","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0000278;GO:0051726;GO:0000082;GO:0005634","GO.description":"mitotic cell cycle;regulation of cell cycle;G1/S transition of mitotic cell cycle;nucleus","FunCat.ID":"10.03.01.01;10.03.01;10.03.01.01.03;70.10","FunCat.description":"mitotic cell cycle;mitotic cell cycle and cell cycle control;G1/S transition of mitotic cell cycle;nucleus","PubMed.ID":12192049,"subunits.Protein.name.":"Replication factor C subunit 1 ;Replication factor C subunit 4;Replication factor C subunit 3 ;Replication factor C subunit 5 ;Bromodomain-containing protein 4 ;Replication factor C subunit 2","subunits.Gene.name.":"Rfc1;Rfc4;Rfc3;Rfc5;Brd4;Rfc2","subunits.Gene.name.syn.":"Ibf-1 Recc1;;;;Mcap;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"BRD4 regulates cell cycle progression from G1 to S phase by interacting with RFC1.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2794,"ComplexName":"ATF2-c-Jun complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P17325;Q00969","subunits.Entrez.IDs.":"24516;81647","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0402- chromatin immunoprecipitation assays","GO.ID":"GO:0007049;GO:2001141;GO:0006355;GO:0003677;GO:0006950;GO:0005634","GO.description":"cell cycle;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;response to stress;nucleus","FunCat.ID":"10.03;11.02.03.04;16.03.01;32.01;70.10","FunCat.description":"cell cycle;transcriptional control;DNA binding;stress response;nucleus","PubMed.ID":15990869,"subunits.Protein.name.":"Transcription factor AP-1 ;Cyclic AMP-dependent transcription factor ATF-2","subunits.Gene.name.":"Jun;Atf2","subunits.Gene.name.syn.":"Rjg-9;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors conclude that ATF2 and c-Jun are activated to bind to the ATF/CRE promoter motif in vivo, and c-Myc is also recruited to this region of ATF3 in response to serum.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2796,"ComplexName":"FosB-JunB DNA-protein complex","Organism":"Rat","Synonyms":"None","Cell.line":"heart muscle","subunits.UniProt.IDs.":"P13346;P24898","subunits.Entrez.IDs.":"14282;24517","Protein.complex.purification.method":"MI:0413-electrophoretic mobility shift assay","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04;16.03.01;70.10","FunCat.description":"transcriptional control;DNA binding;nucleus","PubMed.ID":12371906,"subunits.Protein.name.":"Protein fosB;Transcription factor jun-B","subunits.Gene.name.":"Fosb;Junb","subunits.Gene.name.syn.":"None;Jun-b","Disease.comment":"None","Subunits.comment":"Since FosB from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"Examination of the -1410 to -1362 bp promoter sequence of matrix metalloproteinase 2 (MMP-2) revealed a potential AP-1 complex binding site at -1394 to -1384bp. EMSA studies, combined with single and double antibodystudies, indicate the specific binding of FosB-JunB heterodimersto the AP-1 site using nuclear extracts from fibroblasts cultured under hypoxic conditions. The studies demonstrate that a functional AP-1 site mediates MMP-2 transcription in cardiac cells through the binding of distinctive Fra1-JunB and FosB-JunB heterodimers.","SWISSPROT.organism":"Mus musculus (Mouse);Rattus norvegicus (Rat)"}
{"ComplexID":2797,"ComplexName":"PCNA-CHL12-RFC2-5 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12004;P35249;P35250;P40937;P40938;Q8WVB6","subunits.Entrez.IDs.":"5111;5984;5982;5985;5983;63922","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006260;GO:0005634","GO.description":"DNA replication;nucleus","FunCat.ID":"10.01.03;70.10","FunCat.description":"DNA synthesis and replication;nucleus","PubMed.ID":12171929,"subunits.Protein.name.":"Proliferating cell nuclear antigen;Replication factor C subunit 4;Replication factor C subunit 2;Replication factor C subunit 5;Replication factor C subunit 3;Chromosome transmission fidelity protein 18 homolog","subunits.Gene.name.":"PCNA;RFC4;RFC2;RFC5;RFC3;CHTF18","subunits.Gene.name.syn.":"None;None;None;None;None;C16orf41 CTF18","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"CHL12-RFC2-5 functions as a novel clamp loader protein.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2798,"ComplexName":"MMP-2-claudin-1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95832;P08253","subunits.Entrez.IDs.":"9076;4313","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0051098;GO:0005515;GO:0016504","GO.description":"regulation of binding;protein binding;peptidase activator activity","FunCat.ID":"18.01.07;16.01;18.02.01.01.03","FunCat.description":"regulation by binding / dissociation;protein binding;protease activator","PubMed.ID":11382769,"subunits.Protein.name.":"Claudin-1 ;72 kDa type IV collagenase","subunits.Gene.name.":"CLDN1;MMP2","subunits.Gene.name.syn.":"CLD1 SEMP1;CLG4A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2799,"ComplexName":"RFC complex","Organism":"Human","Synonyms":"Replication factor C complex; RF-C complex","Cell.line":"None","subunits.UniProt.IDs.":"P35249;P35250;P35251;P40937;P40938","subunits.Entrez.IDs.":"5984;5982;5981;5985;5983","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006260;GO:0006281;GO:0000075;GO:0003677;GO:0005634","GO.description":"DNA replication;DNA repair;cell cycle checkpoint;DNA binding;nucleus","FunCat.ID":"10.01.03;10.01.05.01;10.03.01.03;16.03.01;70.10","FunCat.description":"DNA synthesis and replication;DNA repair;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA binding;nucleus","PubMed.ID":9488738,"subunits.Protein.name.":"Replication factor C subunit 4;Replication factor C subunit 2;Replication factor C subunit 1;Replication factor C subunit 5;Replication factor C subunit 3","subunits.Gene.name.":"RFC4;RFC2;RFC1;RFC5;RFC3","subunits.Gene.name.syn.":"None;None;RFC140;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Assembly of RFC complex involves distinct subunit interations: RFC5 and RFC3 interact with the RFC4 subunit and RFC2 interacts with RFC5 and RFC4. RFC1 interacts primarily with RFC3 and RFC2. RFC complex functions as clamp loader. The complex is necessary for loading of PCNA onto dsDNA.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2800,"ComplexName":"SNARE complex (STX1A, CPLX2, SNAP-25, VAMP2)","Organism":"Bovine","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P32850;P63026;P84088;Q17QQ3","subunits.Entrez.IDs.":"788566;282116;281711;540853","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":12200427,"subunits.Protein.name.":"Syntaxin-1A ;Vesicle-associated membrane protein 2 ;Complexin-2 ;Synaptosomal-associated protein 25","subunits.Gene.name.":"STX1A;VAMP2;CPLX2;SNAP25","subunits.Gene.name.syn.":";SYB2;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":2801,"ComplexName":"OCT4-SOX2 DNA-protein complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P48431;Q01860","subunits.Entrez.IDs.":"6657;5460","Protein.complex.purification.method":"MI:0413- electrophoretic mobility shift assay","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0009792;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;embryo development ending in birth or egg hatching;nucleus","FunCat.ID":"11.02.03.04;16.03.01;41.05.04.01;70.10","FunCat.description":"transcriptional control;DNA binding;early embryogenesis;nucleus","PubMed.ID":12923055,"subunits.Protein.name.":"Transcription factor SOX-2;POU domain, class 5, transcription factor 1","subunits.Gene.name.":"SOX2;POU5F1","subunits.Gene.name.syn.":";OCT3 OCT4 OTF3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors analyzed the interaction of the two transcription factors Oct4 with Sox2 on the DNA enhancers of FGF4 (fibroblast growth factor 4) and UTF1 (undifferentiated transcription factor 1). The structural models revealed that the FGF4 and the UTF1  enhancers mediate the assembly of distinct POU/HMG-domain complexes, leading to different quaternary arrangements by swapping protein-protein interaction surfaces of Sox2.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2802,"ComplexName":"OCT1-SOX2 DNA-protein complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P14859;P48431","subunits.Entrez.IDs.":"5451;6657","Protein.complex.purification.method":"MI:0413- electrophoretic mobility shift assay; MI:0114- x-ray crystallography","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0009792;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;embryo development ending in birth or egg hatching;nucleus","FunCat.ID":"11.02.03.04;16.03.01;41.05.04.01;70.10","FunCat.description":"transcriptional control;DNA binding;early embryogenesis;nucleus","PubMed.ID":12923055,"subunits.Protein.name.":"POU domain, class 2, transcription factor 1;Transcription factor SOX-2","subunits.Gene.name.":"POU2F1;SOX2","subunits.Gene.name.syn.":"OCT1 OTF1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors analyzed the interaction of the two transcription factors Oct1 with Sox2 on the DNA enhancers of FGF4 (fibroblast growth factor 4) and UTF1 (undifferentiated transcription factor 1). The structural models revealed that the FGF4 and the UTF1  enhancers mediate the assembly of distinct POU/HMG-domain complexes, leading to different quaternary arrangements by swapping protein-protein interaction surfaces of Sox2.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2803,"ComplexName":"PAX6-SOX2 DNA-protein complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P26367;P48431","subunits.Entrez.IDs.":"5080;6657","Protein.complex.purification.method":"MI:0413- electrophoretic mobility shift assay","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0032504;GO:0001654;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;multicellular organism reproduction;eye development;nucleus","FunCat.ID":"11.02.03.04;16.03.01;41.05.04.03;47.03.02.02;70.10","FunCat.description":"transcriptional control;DNA binding;late embryogenesis ;eye;nucleus","PubMed.ID":12923055,"subunits.Protein.name.":"Paired box protein Pax-6 ;Transcription factor SOX-2","subunits.Gene.name.":"PAX6;SOX2","subunits.Gene.name.syn.":"AN2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors analyzed the interaction of the two transcription factors Pax6 with Sox2 on the DNA enhancer of DC5. It was demonstrated that the same Sox2 interface (the C-terminal region of HMG) is required for heterodimer formation with Oct4 on FGF4 and with Pax6 on DC5, although these two Sox2 partners are members of different transcription factor families and, as such, both unrelated in sequence and structure.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2804,"ComplexName":"CTF18-cohesion-RFC complex","Organism":"Human","Synonyms":"CTF18-RFC complex","Cell.line":"None","subunits.UniProt.IDs.":"P0CG13;P35249;P35250;P40937;P40938;Q8WVB6;Q9BVC3","subunits.Entrez.IDs.":"54921;5984;5982;5985;5983;63922;79075","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0006794;GO:0006796;GO:0006260;GO:0007059;GO:0003677;GO:0051276;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;DNA replication;chromosome segregation;DNA binding;chromosome organization;nucleus","FunCat.ID":"01.04;10.01.03;10.03.04.05;16.03.01;42.10.03;70.10","FunCat.description":"phosphate metabolism;DNA synthesis and replication;chromosome segregation/division;DNA binding;organization of chromosome structure;nucleus","PubMed.ID":12930902,"subunits.Protein.name.":"Chromosome transmission fidelity protein 8 homolog;Replication factor C subunit 4;Replication factor C subunit 2;Replication factor C subunit 5;Replication factor C subunit 3;Chromosome transmission fidelity protein 18 homolog;Sister chromatid cohesion protein DCC1","subunits.Gene.name.":"CHTF8;RFC4;RFC2;RFC5;RFC3;CHTF18;DSCC1","subunits.Gene.name.syn.":"CTF8;None;None;None;None;C16orf41 CTF18;DCC1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"CTF18-RFC complex interacts with PCNA homotrimer in the pressence of ATP and loads PCNA onto primed and gapped circular DNA, but not onto nicked or single-stranded circular DNA.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2805,"ComplexName":"CTF8-DCC1 subcomplex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P0CG13;Q9BVC3","subunits.Entrez.IDs.":"54921;79075","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0007059;GO:0005515;GO:0051276;GO:0005634","GO.description":"chromosome segregation;protein binding;chromosome organization;nucleus","FunCat.ID":"10.03.04.05;16.01;42.10.03;70.10","FunCat.description":"chromosome segregation/division;protein binding;organization of chromosome structure;nucleus","PubMed.ID":12930902,"subunits.Protein.name.":"Chromosome transmission fidelity protein 8 homolog;Sister chromatid cohesion protein DCC1","subunits.Gene.name.":"CHTF8;DSCC1","subunits.Gene.name.syn.":"CTF8;DCC1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2806,"ComplexName":"CTF8-CTF18-DCC1 subcomplex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P0CG13;Q8WVB6;Q9BVC3","subunits.Entrez.IDs.":"54921;63922;79075","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0007059;GO:0005515;GO:0051276;GO:0005634","GO.description":"chromosome segregation;protein binding;chromosome organization;nucleus","FunCat.ID":"10.03.04.05;16.01;42.10.03;70.10","FunCat.description":"chromosome segregation/division;protein binding;organization of chromosome structure;nucleus","PubMed.ID":12930902,"subunits.Protein.name.":"Chromosome transmission fidelity protein 8 homolog;Chromosome transmission fidelity protein 18 homolog;Sister chromatid cohesion protein DCC1","subunits.Gene.name.":"CHTF8;CHTF18;DSCC1","subunits.Gene.name.syn.":"CTF8;C16orf41 CTF18;DCC1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2808,"ComplexName":"9-1-1-APE1 complex","Organism":"Human","Synonyms":"RAD9-RAD1-HUS1-APE1 complex","Cell.line":"None","subunits.UniProt.IDs.":"O60671;O60921;P27695;Q99638","subunits.Entrez.IDs.":"5810;3364;328;5883","Protein.complex.purification.method":"MI:0096-pull down;MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0006308;GO:0006401;GO:0006281;GO:0000075;GO:0006974;GO:0005634","GO.description":"DNA catabolic process;RNA catabolic process;DNA repair;cell cycle checkpoint;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"01.03.16.03;01.03.16.01;10.01.05.01;10.03.01.03;32.01.09;70.10","FunCat.description":"DNA degradation;RNA degradation;DNA repair;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA damage response;nucleus","PubMed.ID":17426133,"subunits.Protein.name.":"Cell cycle checkpoint protein RAD1;Checkpoint protein HUS1;DNA-;Cell cycle checkpoint control protein RAD9A","subunits.Gene.name.":"RAD1;HUS1;APEX1;RAD9A","subunits.Gene.name.syn.":"REC1;None;APE APE1 APEX APX HAP1 REF1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The 9-1-1 complex specifically stimulates the endonuclease activity of APEX1 for DNA repair.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2809,"ComplexName":"9-1-1 complex","Organism":"Human","Synonyms":"RAD9-RAD1-HUS1 complex; RHR complex","Cell.line":"None","subunits.UniProt.IDs.":"O60671;O60921;Q99638","subunits.Entrez.IDs.":"5810;3364;5883","Protein.complex.purification.method":"MI:0096-pull down","GO.ID":"GO:0006281;GO:0000075;GO:0006974;GO:0005634","GO.description":"DNA repair;cell cycle checkpoint;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;10.03.01.03;32.01.09;70.10","FunCat.description":"DNA repair;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA damage response;nucleus","PubMed.ID":17426133,"subunits.Protein.name.":"Cell cycle checkpoint protein RAD1;Checkpoint protein HUS1;Cell cycle checkpoint control protein RAD9A","subunits.Gene.name.":"RAD1;HUS1;RAD9A","subunits.Gene.name.syn.":"REC1;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2810,"ComplexName":"Rad17-RFC complex","Organism":"Human","Synonyms":"RSR complex","Cell.line":"None","subunits.UniProt.IDs.":"O75943;P35249;P35250;P40937;P40938","subunits.Entrez.IDs.":"5884;5984;5982;5985;5983","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006794;GO:0006796;GO:0000075;GO:0003677;GO:0005524;GO:0006974;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;cell cycle checkpoint;DNA binding;ATP binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"01.04;10.03.01.03;16.03.01;16.19.03;32.01.09;70.10","FunCat.description":"phosphate metabolism;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA binding;ATP binding;DNA damage response;nucleus","PubMed.ID":14624239,"subunits.Protein.name.":"Cell cycle checkpoint protein RAD17;Replication factor C subunit 4;Replication factor C subunit 2;Replication factor C subunit 5;Replication factor C subunit 3","subunits.Gene.name.":"RAD17;RFC4;RFC2;RFC5;RFC3","subunits.Gene.name.syn.":"R24L;None;None;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The RSR complex works as a clamp loader, loading RHR onto DNA. RSR prefers DNA substrates posessing 5' recessed ends.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2811,"ComplexName":"BRCA1-cABL complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P00519;P38398","subunits.Entrez.IDs.":"25;672","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0006974;GO:0005634","GO.description":"DNA repair;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;32.01.09;70.10","FunCat.description":"DNA repair;DNA damage response;nucleus","PubMed.ID":12024016,"subunits.Protein.name.":"Tyrosine-protein kinase ABL1;Breast cancer type 1 susceptibility protein","subunits.Gene.name.":"ABL1;BRCA1","subunits.Gene.name.syn.":"ABL, JTK7;RNF53","Disease.comment":"BRCA1 is involved in breast cancer.","Subunits.comment":"None","Complex.comment":"BRCA1 controls c-Abl activity. Interaction occurs between th PXXP motif in the C-terminus of BRCA1 and the SH3 domain of c-Abl.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2812,"ComplexName":"RPAP1-RPB2-RPB3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P19387;P30876;Q9BWH6","subunits.Entrez.IDs.":"5432;5431;26015","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006351;GO:0005634","GO.description":"transcription, DNA-templated;nucleus","FunCat.ID":"11;70.10","FunCat.description":"TRANSCRIPTION;nucleus","PubMed.ID":15282305,"subunits.Protein.name.":"DNA-directed RNA polymerase II subunit RPB3 ;DNA-directed RNA polymerase II subunit RPB2 ;RNA polymerase II-associated protein 1","subunits.Gene.name.":"POLR2C;POLR2B;RPAP1","subunits.Gene.name.syn.":";;KIAA1403","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2813,"ComplexName":"BRCA1-SMAD3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P38398;P84022","subunits.Entrez.IDs.":"672;4088","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0006281;GO:0007049;GO:2001141;GO:0006355;GO:0007179;GO:0005634","GO.description":"DNA repair;cell cycle;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"10.01.05.01;10.03;11.02.03.04;30.05.01.18.01;70.10","FunCat.description":"DNA repair;cell cycle;transcriptional control;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":15735739,"subunits.Protein.name.":"Breast cancer type 1 susceptibility protein;Mothers against decapentaplegic homolog 3","subunits.Gene.name.":"BRCA1;SMAD3","subunits.Gene.name.syn.":"RNF53;MADH3","Disease.comment":"BRCA1 is involved in breast cancer.","Subunits.comment":"None","Complex.comment":"Interaction is mediated by the MH1 domain of Smad3 and the C-terminal part of BRCA1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2814,"ComplexName":"BRCA1-HDAC1-HDAC2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P38398;Q13547;Q92769","subunits.Entrez.IDs.":"672;3065;3066","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006281;GO:0006473;GO:0006476;GO:0005634","GO.description":"DNA repair;protein acetylation;protein deacetylation;nucleus","FunCat.ID":"10.01.05.01;14.07.04;70.10","FunCat.description":"DNA repair;modification by acetylation, deacetylation;nucleus","PubMed.ID":10220405,"subunits.Protein.name.":"Breast cancer type 1 susceptibility protein;Histone deacetylase 1;Histone deacetylase 2","subunits.Gene.name.":"BRCA1;HDAC1;HDAC2","subunits.Gene.name.syn.":"RNF53;RPD3L1;None","Disease.comment":"BRCA1 is involved in breast cancer.","Subunits.comment":"None","Complex.comment":"BRCA1 interacts with components of the histone deacetylase complex, and therefore may explain the involvement of BRCA1 in multiple processes such as transcription, DNA repair, and recombination. BRCA1 associates with HDAC1 and HDAC2 via the BRCT domain.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2815,"ComplexName":"BRCA1-BARD1-BACH1-DNA damage complex II","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14867;O60934;P38398;P49959;Q92547;Q92878;Q99708;Q99728","subunits.Entrez.IDs.":"571;4683;672;4361;11073;10111;5932;580","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006260;GO:0006281;GO:0000075;GO:0006974;GO:0005634","GO.description":"DNA replication;DNA repair;cell cycle checkpoint;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.03;10.01.05.01;10.03.01.03;32.01.09;70.10","FunCat.description":"DNA synthesis and replication;DNA repair;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA damage response;nucleus","PubMed.ID":16391231,"subunits.Protein.name.":"Transcription regulator protein BACH1 ;Nibrin ;Breast cancer type 1 susceptibility protein;Double-strand break repair protein MRE11A ;DNA topoisomerase 2-binding protein 1;DNA repair protein RAD50 ;DNA endonuclease RBBP8 ;BRCA1-associated RING domain protein 1","subunits.Gene.name.":"BACH1;NBN;BRCA1;MRE11A;TOPBP1;RAD50;RBBP8;BARD1","subunits.Gene.name.syn.":";NBS NBS1 P95;RNF53;HNGS1 MRE11;KIAA0259;;CTIP;","Disease.comment":"BRCA1 is involved in breast cancer.","Subunits.comment":"None","Complex.comment":"This complex occurs after exposure to UV irradiation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2816,"ComplexName":"ITGAV-ITGB3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P05106;P06756","subunits.Entrez.IDs.":"3690;3685","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515;GO:0016477;GO:0007155;GO:0016049","GO.description":"protein binding;cell migration;cell adhesion;cell growth","FunCat.ID":"16.01;34.05.01;34.07;40.01","FunCat.description":"protein binding;cell migration;cell adhesion;cell growth / morphogenesis","PubMed.ID":8798654,"subunits.Protein.name.":"Integrin beta-3;Integrin alpha-V","subunits.Gene.name.":"ITGB3;ITGAV","subunits.Gene.name.syn.":"GP3A;MSK8 VNRA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Alpha(v)beta3 can differentially activate cell migration and intracellular signaling pathways in a ligand-specific manner (PMID:10835423).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2817,"ComplexName":"BRCA1-BARD1-BACH1-DNA damage complex I","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14867;P38398;P40692;P52701;Q92547;Q99728","subunits.Entrez.IDs.":"571;672;4292;2956;11073;580","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006260;GO:0006281;GO:0000075;GO:0006974;GO:0005634","GO.description":"DNA replication;DNA repair;cell cycle checkpoint;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.03;10.01.05.01;10.03.01.03;32.01.09;70.10","FunCat.description":"DNA synthesis and replication;DNA repair;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA damage response;nucleus","PubMed.ID":16391231,"subunits.Protein.name.":"Transcription regulator protein BACH1 ;Breast cancer type 1 susceptibility protein;DNA mismatch repair protein Mlh1 ;DNA mismatch repair protein Msh6 ;DNA topoisomerase 2-binding protein 1;BRCA1-associated RING domain protein 1","subunits.Gene.name.":"BACH1;BRCA1;MLH1;MSH6;TOPBP1;BARD1","subunits.Gene.name.syn.":";RNF53;COCA2;GTBP;KIAA0259;","Disease.comment":"BRCA1 is involved in breast cancer.","Subunits.comment":"None","Complex.comment":"This complex occurs after exposure to UV irradiation. BRCA1-BARD1-BACH1 complex is required for post-damage interaction with TOPBP1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2818,"ComplexName":"BRCA1-BARD1-BRCA2-DNA damage complex III","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P38398;P51587;Q99728","subunits.Entrez.IDs.":"672;675;580","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006260;GO:0006281;GO:0000075;GO:0006974;GO:0005634","GO.description":"DNA replication;DNA repair;cell cycle checkpoint;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.03;10.01.05.01;10.03.01.03;32.01.09;70.10","FunCat.description":"DNA synthesis and replication;DNA repair;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA damage response;nucleus","PubMed.ID":16391231,"subunits.Protein.name.":"Breast cancer type 1 susceptibility protein;Breast cancer type 2 susceptibility protein ;BRCA1-associated RING domain protein 1","subunits.Gene.name.":"BRCA1;BRCA2;BARD1","subunits.Gene.name.syn.":"RNF53;FACD FANCD1;","Disease.comment":"BRCA1 is involved in breast cancer.","Subunits.comment":"None","Complex.comment":"This complex occurs after exposure to UV irradiation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2819,"ComplexName":"BRCA1-CtIP-CtBP complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P38398;Q13363;Q99708","subunits.Entrez.IDs.":"672;1487;5932","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:2001141;GO:0006355;GO:0006974;GO:0005634","GO.description":"DNA repair;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;11.02.03.04;32.01.09;70.10","FunCat.description":"DNA repair;transcriptional control;DNA damage response;nucleus","PubMed.ID":10196224,"subunits.Protein.name.":"Breast cancer type 1 susceptibility protein;C-terminal-binding protein 1;DNA endonuclease RBBP8","subunits.Gene.name.":"BRCA1;CTBP1;RBBP8","subunits.Gene.name.syn.":"RNF53;CTBP;CTIP","Disease.comment":"BRCA1 is involved in breast cancer.","Subunits.comment":"None","Complex.comment":"BRCA1 binds to CtBP through CtIP. Binding of BRCA1 to CtIP/CtBP is critical in mediating transcriptional regulation of p21 in response to DNA damage.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2820,"ComplexName":"BRCA1-VCP complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P38398;P55072","subunits.Entrez.IDs.":"672;7415","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006281;GO:0005634","GO.description":"DNA repair;nucleus","FunCat.ID":"10.01.05.01;70.10","FunCat.description":"DNA repair;nucleus","PubMed.ID":10855792,"subunits.Protein.name.":"Breast cancer type 1 susceptibility protein;Transitional endoplasmic reticulum ATPase","subunits.Gene.name.":"BRCA1;VCP","subunits.Gene.name.syn.":"RNF53;None","Disease.comment":"BRCA1 is involved in breast cancer.","Subunits.comment":"None","Complex.comment":"VCP participates in the DNA damage-repair function as an ATP transporter, possibly facilitating the transcription-coupled repair.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2821,"ComplexName":"hSIR2-p53 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04637;Q96EB6","subunits.Entrez.IDs.":"7157;23411","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0006473;GO:0006476;GO:0006974;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"11.02.03.04;14.07.04;32.01.09;70.10","FunCat.description":"transcriptional control;modification by acetylation, deacetylation;DNA damage response;nucleus","PubMed.ID":11672523,"subunits.Protein.name.":"Cellular tumor antigen p53;NAD-dependent protein deacetylase sirtuin-1","subunits.Gene.name.":"TP53;SIRT1","subunits.Gene.name.syn.":"P53;SIR2L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors analyzed that hSir2 directly binds the human p53 protein in vivo and specifically deacetylates the K382 residue of p53.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2822,"ComplexName":"BRCA1-BARD1-UbcH5c complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P38398;P61077;Q99728","subunits.Entrez.IDs.":"672;7323;580","Protein.complex.purification.method":"MI:0077- nuclear magnetic resonance","GO.ID":"GO:0016567;GO:0016579;GO:0006974;GO:0005634","GO.description":"protein ubiquitination;protein deubiquitination;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"14.07.05;32.01.09;70.10","FunCat.description":"modification by ubiquitination, deubiquitination;DNA damage response;nucleus","PubMed.ID":12732733,"subunits.Protein.name.":"Breast cancer type 1 susceptibility protein;Ubiquitin-conjugating enzyme E2 D3 ;BRCA1-associated RING domain protein 1","subunits.Gene.name.":"BRCA1;UBE2D3;BARD1","subunits.Gene.name.syn.":"RNF53;UBC5C UBCH5C;","Disease.comment":"BRCA1 is involved in breast cancer.","Subunits.comment":"None","Complex.comment":"UbcH5c binds to BRCA1 RING domain and not to the BARD1 RING.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2823,"ComplexName":"BRCA1-BARD1-UbcH7c complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P38398;P68036;Q99728","subunits.Entrez.IDs.":"672;7332;580","Protein.complex.purification.method":"MI:0077- nuclear magnetic resonance","GO.ID":"GO:0016567;GO:0016579;GO:0006974;GO:0005634","GO.description":"protein ubiquitination;protein deubiquitination;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"14.07.05;32.01.09;70.10","FunCat.description":"modification by ubiquitination, deubiquitination;DNA damage response;nucleus","PubMed.ID":12732733,"subunits.Protein.name.":"Breast cancer type 1 susceptibility protein;Ubiquitin-conjugating enzyme E2 L3 ;BRCA1-associated RING domain protein 1","subunits.Gene.name.":"BRCA1;UBE2L3;BARD1","subunits.Gene.name.syn.":"RNF53;UBCE7 UBCH7;","Disease.comment":"BRCA1 is involved in breast cancer.","Subunits.comment":"None","Complex.comment":"UbcH7c binds to BRCA1 RING domain and not to the BARD1 RING.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2824,"ComplexName":"BRCA1-RAD51 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P38398;Q06609","subunits.Entrez.IDs.":"672;5888","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0006310;GO:0000075;GO:0005634","GO.description":"DNA repair;DNA recombination;cell cycle checkpoint;nucleus","FunCat.ID":"10.01.05.01;10.01.05.03;10.03.01.03;70.10","FunCat.description":"DNA repair;DNA recombination;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);nucleus","PubMed.ID":9008167,"subunits.Protein.name.":"Breast cancer type 1 susceptibility protein;DNA repair protein RAD51 homolog 1","subunits.Gene.name.":"BRCA1;RAD51","subunits.Gene.name.syn.":"RNF53;RAD51A RECA","Disease.comment":"BRCA1 is involved in breast cancer.","Subunits.comment":"None","Complex.comment":"BRCA1 and RAD51 mainly colocalize in S phase cells.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2825,"ComplexName":"BRCA1-RNA polymerase II complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15514;P13984;P18074;P19387;P19388;P19447;P20226;P24928;P29083;P29084;P30876;P32780;P35269;P36954;P38398;P52434;P52435;P53803;P61218;P62487;P62875;Q00403;Q13503;Q13888;Q13889;Q92759","subunits.Entrez.IDs.":"5433;2963;2068;5432;5434;2071;6908;5430;2960;2961;5431;2965;2962;5438;672;5437;5439;5440;5435;5436;5441;2959;9412;2966;2967;2968","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006351;GO:0003677;GO:0005634","GO.description":"transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11;16.03.01;70.10","FunCat.description":"TRANSCRIPTION;DNA binding;nucleus","PubMed.ID":9159119,"subunits.Protein.name.":"DNA-directed RNA polymerase II subunit RPB4 ;General transcription factor IIF subunit 2 ;TFIIH basal transcription factor complex helicase XPD subunit ;DNA-directed RNA polymerase II subunit RPB3 ;DNA-directed RNA polymerases I, II, and III subunit RPABC1 ;TFIIH basal transcription factor complex helicase XPB subunit ;TATA-box-binding protein;DNA-directed RNA polymerase II subunit RPB1;General transcription factor IIE subunit 1;Transcription initiation factor IIE subunit beta ;DNA-directed RNA polymerase II subunit RPB2 ;General transcription factor IIH subunit 1;General transcription factor IIF subunit 1;DNA-directed RNA polymerase II subunit RPB9 ;Breast cancer type 1 susceptibility protein;DNA-directed RNA polymerases I, II, and III subunit RPABC3 ;DNA-directed RNA polymerase II subunit RPB11-a ;DNA-directed RNA polymerases I, II, and III subunit RPABC4 ;DNA-directed RNA polymerases I, II, and III subunit RPABC2 ;DNA-directed RNA polymerase II subunit RPB7 ;DNA-directed RNA polymerases I, II, and III subunit RPABC5 ;Transcription initiation factor IIB;Mediator of RNA polymerase II transcription subunit 21;General transcription factor IIH subunit 2 ;General transcription factor IIH subunit 3 ;General transcription factor IIH subunit 4","subunits.Gene.name.":"POLR2D;GTF2F2;ERCC2;POLR2C;POLR2E;ERCC3;TBP;POLR2A;GTF2E1;GTF2E2;POLR2B;GTF2H1;GTF2F1;POLR2I;BRCA1;POLR2H;POLR2J;POLR2K;POLR2F;POLR2G;POLR2L;GTF2B;MED21;GTF2H2;GTF2H3;GTF2H4","subunits.Gene.name.syn.":";RAP30;XPD XPDC;;;XPB XPBC;GTF2D1 TF2D TFIID;POLR2;TF2E1;TF2E2;;BTF2;RAP74;;RNF53;;POLR2J1;;POLRF;RPB7;;TF2B TFIIB;SRB7 SURB7;BTF2P44;;","Disease.comment":"BRCA1 is involved in breast cancer.","Subunits.comment":"None","Complex.comment":"The Brca1 tumor supressor protein is associated with the transcription process.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2826,"ComplexName":"ITGB3-ITGAV-VTN complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P04004;P05106;P06756","subunits.Entrez.IDs.":"7448;3690;3685","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0050789;GO:0016477","GO.description":"regulation of biological process;cell migration","FunCat.ID":"18;34.05.01","FunCat.description":"REGULATION OF METABOLISM AND PROTEIN FUNCTION;cell migration","PubMed.ID":10835423,"subunits.Protein.name.":"Vitronectin ;Integrin beta-3;Integrin alpha-V","subunits.Gene.name.":"VTN;ITGB3;ITGAV","subunits.Gene.name.syn.":";GP3A;MSK8 VNRA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In beta(3)-LNCaP cells, alpha(v)beta(3) mediates cell migration and PI 3-kinase/AKT pathway activation on vitronectin, whereas adhesion to osteopontin does not support alpha(v)beta(3)-mediated cell migration and PI 3-kinase/AKT pathway activation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2829,"ComplexName":"RSmad complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P51532;P84022;Q13485;Q15796;Q8NFD5;Q8TAQ2;Q92793;Q92922;Q9UPN9;Q9Y6Q9","subunits.Entrez.IDs.":"6597;4088;4089;4087;57492;6601;1387;6599;51592;8202","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:2001141;GO:0006355;GO:0007179;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"11.02.03.04;30.05.01.18.01;70.10","FunCat.description":"transcriptional control;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":16751102,"subunits.Protein.name.":"Transcription activator BRG1;Mothers against decapentaplegic homolog 3;Mothers against decapentaplegic homolog 4;Mothers against decapentaplegic homolog 2;AT-rich interactive domain-containing protein 1B;SWI/SNF complex subunit SMARCC2;CREB-binding protein;SWI/SNF complex subunit SMARCC1;E3 ubiquitin-protein ligase TRIM33;Nuclear receptor coactivator 3","subunits.Gene.name.":"SMARCA4;SMAD3;SMAD4;SMAD2;ARID1B;SMARCC2;CREBBP;SMARCC1;TRIM33;NCOA3","subunits.Gene.name.syn.":"BAF190A BRG1 SNF2B SNF2L4;MADH3;DPC4 MADH4;MADH2, MADR2;BAF250B DAN15 KIAA1235 OSA2;BAF170;CBP;BAF155;KIAA1113 RFG7 TIF1G;AIB1, BHLHE42, RAC3, TRAM1, ACTR","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Affinity purification of proteins that selectively bind to activated RSmads.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2830,"ComplexName":"TIF1gamma-SMAD2-SMAD3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P84022;Q15796;Q9UPN9","subunits.Entrez.IDs.":"4088;4087;51592","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0007179;GO:0030097;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;transforming growth factor beta receptor signaling pathway;hemopoiesis;nucleus","FunCat.ID":"11.02.03.04;30.05.01.18.01;41.05.18;70.10","FunCat.description":"transcriptional control;TGF-beta-receptor signalling pathway;hemopoiesis;nucleus","PubMed.ID":16751102,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 3;Mothers against decapentaplegic homolog 2;E3 ubiquitin-protein ligase TRIM33","subunits.Gene.name.":"SMAD3;SMAD2;TRIM33","subunits.Gene.name.syn.":"MADH3;MADH2, MADR2;KIAA1113 RFG7 TIF1G","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Formation of complex is dependent on TGFbeta. TIF1gamma selectively binds receptor-posphorylated SMAD2 and SMAD3 in competition with SMAD4.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2831,"ComplexName":"TIF1gamma-Smad2-Smad3 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q62432;Q8BUN5;Q99PP7","subunits.Entrez.IDs.":"17126;17127;94093","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0007179;GO:0030097;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;transforming growth factor beta receptor signaling pathway;hemopoiesis;nucleus","FunCat.ID":"11.02.03.04;30.05.01.18.01;41.05.18;70.10","FunCat.description":"transcriptional control;TGF-beta-receptor signalling pathway;hemopoiesis;nucleus","PubMed.ID":16751102,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 2 ;Mothers against decapentaplegic homolog 3;E3 ubiquitin-protein ligase TRIM33","subunits.Gene.name.":"Smad2;Smad3;Trim33","subunits.Gene.name.syn.":"Madh2 Madr2;Madh3;Kiaa1113","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Formation of complex is dependent on TGFbeta. TIF1gamma selectively binds receptor-posphorylated SMAD2 and SMAD3 in competition with SMAD4.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2832,"ComplexName":"Smad4-Smad2-Smad3 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P97471;Q62432;Q8BUN5","subunits.Entrez.IDs.":"17128;17126;17127","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0007179;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"11.02.03.04;30.05.01.18.01;70.10","FunCat.description":"transcriptional control;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":16751102,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 4 ;Mothers against decapentaplegic homolog 2 ;Mothers against decapentaplegic homolog 3","subunits.Gene.name.":"Smad4;Smad2;Smad3","subunits.Gene.name.syn.":"Dpc4 Madh4;Madh2 Madr2;Madh3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Formation of complex is dependent on TGFbeta. TIF1gamma selectively binds receptor-posphorylated SMAD2 and SMAD3 in competition with SMAD4.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2833,"ComplexName":"SRm160-SRm300 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q8IYB3;Q9UQ35","subunits.Entrez.IDs.":"10250;23524","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008380;GO:0003723;GO:0016363","GO.description":"RNA splicing;RNA binding;nuclear matrix","FunCat.ID":"11.04.03.01;16.03.03;70.10.06","FunCat.description":"splicing;RNA binding;nuclear matrix","PubMed.ID":9531537,"subunits.Protein.name.":"Serine/arginine repetitive matrix protein 1 ;Serine/arginine repetitive matrix protein 2","subunits.Gene.name.":"SRRM1;SRRM2","subunits.Gene.name.syn.":"SRM160;KIAA0324 SRL300 SRM300","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors demonstrate that although SRm160/300 can promote splicing in the absence of U1 snRNP, under normal splicing reaction conditions containing endogenous levels of SR family proteins, SRm160/300 associates with pre-mRNA by a U1 snRNP-dependent pathway and its binding to pre-mRNA is further stabilized by U2 snRNP. SRm160/300 also associates preferentially with a subset of specific SR proteins comigrating with SRp40 and SRp75. The results indicate that SRm160/300 and SR family proteins have overlapping but nonreciprocal functions and that cooperative interactions between these factors is critical for the splicing of specific pre-mRNAs.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2834,"ComplexName":"SMAD4-SMAD2-SMAD3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P84022;Q13485;Q15796","subunits.Entrez.IDs.":"4088;4089;4087","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0007179;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"11.02.03.04;30.05.01.18.01;70.10","FunCat.description":"transcriptional control;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":16751102,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 3;Mothers against decapentaplegic homolog 4;Mothers against decapentaplegic homolog 2","subunits.Gene.name.":"SMAD3;SMAD4;SMAD2","subunits.Gene.name.syn.":"MADH3;DPC4 MADH4;MADH2, MADR2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Formation of complex is dependent on TGFbeta. TIF1gamma selectively binds receptor-posphorylated SMAD2 and SMAD3 in competition with SMAD4.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2835,"ComplexName":"Profilin 2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"O88935;P28660;P39053;P60710;P63017;P70336;Q64332;Q7TMB8;Q9JJV2","subunits.Entrez.IDs.":"20964;50884;13429;11461;15481;19878;20965;20430;18645","Protein.complex.purification.method":"MI:0069- mass spectrometry studies of complexes;MI:0004- affinity chromatography technologies","GO.ID":"GO:0006461;GO:0006897;GO:0030036","GO.description":"protein complex assembly;endocytosis;actin cytoskeleton organization","FunCat.ID":"14.10;20.09.18.09.01;42.04.03","FunCat.description":"assembly of protein complexes;endocytosis;actin cytoskeleton","PubMed.ID":9463375,"subunits.Protein.name.":"Synapsin-1;Nck-associated protein 1 ;Dynamin-1;Actin, cytoplasmic 1;Heat shock cognate 71 kDa protein;Rho-associated protein kinase 2 ;Synapsin-2 ;Cytoplasmic FMR1-interacting protein 1 ;Profilin-2","subunits.Gene.name.":"Syn1;Nckap1;Dnm1;Actb;Hspa8;Rock2;Syn2;Cyfip1;Pfn2","subunits.Gene.name.syn.":"Syn-1;Hem2 Kiaa0587 Nap1;Dnm, Kiaa4093;None;Hsc70 Hsc73;;;Kiaa0068 Shyc Sra1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2836,"ComplexName":"Profilin 1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62962;P63017;P63260;Q01853;Q68FD5;Q9CWF2","subunits.Entrez.IDs.":"18643;15481;11465;269523;67300;73710","Protein.complex.purification.method":"MI:0069- mass spectrometry studies of complexes; MI:0004- affinity chromatography technologies","GO.ID":"GO:0006461;GO:0006897;GO:0030036","GO.description":"protein complex assembly;endocytosis;actin cytoskeleton organization","FunCat.ID":"14.10;20.09.18.09.01;42.04.03","FunCat.description":"assembly of protein complexes;endocytosis;actin cytoskeleton","PubMed.ID":9463375,"subunits.Protein.name.":"Profilin-1 ;Heat shock cognate 71 kDa protein;Actin, cytoplasmic 2 ;Transitional endoplasmic reticulum ATPase ;Clathrin heavy chain 1;Tubulin beta-2B chain","subunits.Gene.name.":"Pfn1;Hspa8;Actg1;Vcp;Cltc;Tubb2b","subunits.Gene.name.syn.":";Hsc70 Hsc73;Actg;;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2837,"ComplexName":"Profilin 1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P07737;P11142;P55072;P63261;Q00610;Q9BVA1","subunits.Entrez.IDs.":"5216;3312;7415;71;1213;347733","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006461;GO:0006897;GO:0030036","GO.description":"protein complex assembly;endocytosis;actin cytoskeleton organization","FunCat.ID":"14.10;20.09.18.09.01;42.04.03","FunCat.description":"assembly of protein complexes;endocytosis;actin cytoskeleton","PubMed.ID":9463375,"subunits.Protein.name.":"Profilin-1 ;Heat shock cognate 71 kDa protein;Transitional endoplasmic reticulum ATPase;Actin, cytoplasmic 2;Clathrin heavy chain 1;Tubulin beta-2B chain","subunits.Gene.name.":"PFN1;HSPA8;VCP;ACTG1;CLTC;TUBB2B","subunits.Gene.name.syn.":";HSC70, HSP73, HSPA10;None;ACTG;CLH17, CLTCL2, KIAA0034, CHC;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In brain profilin I complex links the actin cytoskeleton and endocytic membrane flow, directing actin and clathrin assembly to distinct membrane domains.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2838,"ComplexName":"AR coactivator complex","Organism":"Human","Synonyms":"p44-PRMT-ICLN complex","Cell.line":"None","subunits.UniProt.IDs.":"O14744;P54105;Q9BQA1","subunits.Entrez.IDs.":"10419;1207;79084","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045893;GO:0018126;GO:0006479;GO:0003677;GO:0023052;GO:0030850;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;protein hydroxylation;protein methylation;DNA binding;signaling;prostate gland development;nucleus","FunCat.ID":"11.02.03.04.01;14.07.09;16.03.01;30.01;47.03.21.04;70.10","FunCat.description":"transcription activation;posttranslational modification of amino acids (e.g. hydroxylation, methylation);DNA binding;cellular signalling;prostate gland;nucleus","PubMed.ID":12972618,"subunits.Protein.name.":"Protein arginine N-methyltransferase 5;Methylosome subunit pICln ;Methylosome protein 50","subunits.Gene.name.":"PRMT5;CLNS1A;WDR77","subunits.Gene.name.syn.":"HRMT1L5 IBP72 JBP1 SKB1;CLCI ICLN;MEP50 WD45","Disease.comment":"Overexpression of WDR77 (p44) correlates with prostate tumorigenesis.","Subunits.comment":"None","Complex.comment":"This complex enhances AR-driven transcription.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2839,"ComplexName":"ATRX-DAXX complex","Organism":"Human","Synonyms":"ATRX chromatin-remodeling complex","Cell.line":"None","subunits.UniProt.IDs.":"P46100;Q9UER7","subunits.Entrez.IDs.":"546;1616","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0071- molecular sieving","GO.ID":"GO:0006794;GO:0006796;GO:0006265;GO:2001141;GO:0006355;GO:0051276;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;DNA topological change;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;chromosome organization;nucleus","FunCat.ID":"01.04;10.01.09.05;11.02.03.04;42.10.03;70.10","FunCat.description":"phosphate metabolism;DNA conformation modification (e.g. chromatin);transcriptional control;organization of chromosome structure;nucleus","PubMed.ID":12953102,"subunits.Protein.name.":"Transcriptional regulator ATRX ;Death domain-associated protein 6","subunits.Gene.name.":"ATRX;DAXX","subunits.Gene.name.syn.":"RAD54L XH2;BING2 DAP6","Disease.comment":"None","Subunits.comment":"Two other subunits of the complex were found in the analysis, which have not been further characterized: DAP50 and DAP60.","Complex.comment":"ATRX and DAXX colocalize in promyelocytic leukemia nuclear bodies. The level of this complex is significantly decreased in an ATRX patient cell line.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2840,"ComplexName":"uKHC-KLC1-KLC2 kinesin complex","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"O88447;O88448;Q61768","subunits.Entrez.IDs.":"16593;16594;16573","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007018;GO:0050896;GO:0015630","GO.description":"microtubule-based movement;response to stimulus;microtubule cytoskeleton","FunCat.ID":"20.09.14.01;36.25;70.04.05","FunCat.description":"tubulin dependent transport;animal specific systemic sensing and response;microtubule cytoskeleton","PubMed.ID":9624122,"subunits.Protein.name.":"Kinesin light chain 1 ;Kinesin light chain 2 ;Kinesin-1 heavy chain","subunits.Gene.name.":"Klc1;Klc2;Kif5b","subunits.Gene.name.syn.":"Kns2;;Khcs, Kns1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Immunoprecipitation done from brain lysate with uKHC antibodies brings down both kinesin light chains.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2842,"ComplexName":"DAXX-Axin-p53-HIPK2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15169;P04637;Q9H2X6;Q9UER7","subunits.Entrez.IDs.":"8312;7157;28996;1616","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006794;GO:0006796;GO:2001141;GO:0006355;GO:0006468;GO:0006470;GO:0046777;GO:0009314;GO:0006915;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;response to radiation;apoptotic process;nucleus","FunCat.ID":"01.04;11.02.03.04;14.07.03;32.01.13;40.10.02;70.10","FunCat.description":"phosphate metabolism;transcriptional control;modification by phosphorylation, dephosphorylation, autophosphorylation;electromagnetic waves stress response (e.g. UV, X-ray);apoptosis (type I programmed cell death);nucleus","PubMed.ID":17210684,"subunits.Protein.name.":"Axin-1 ;Cellular tumor antigen p53;Homeodomain-interacting protein kinase 2;Death domain-associated protein 6","subunits.Gene.name.":"AXIN1;TP53;HIPK2;DAXX","subunits.Gene.name.syn.":"AXIN;P53;None;BING2 DAP6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Axin tethers DAXX to the tumor suppressor p53. UV induces colocalization of Axin, DAXX and HIPK2 in the nucleus.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2843,"ComplexName":"ATRX-DAXX complex","Organism":"Human","Synonyms":"ATRX chromatin-remodeling complex","Cell.line":"None","subunits.UniProt.IDs.":"P46100;Q9UER7","subunits.Entrez.IDs.":"546;1616","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006794;GO:0006796;GO:0006265;GO:2001141;GO:0006355;GO:0051276;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;DNA topological change;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;chromosome organization;nucleus","FunCat.ID":"01.04;10.01.09.05;11.02.03.04;42.10.03;70.10","FunCat.description":"phosphate metabolism;DNA conformation modification (e.g. chromatin);transcriptional control;organization of chromosome structure;nucleus","PubMed.ID":14990586,"subunits.Protein.name.":"Transcriptional regulator ATRX ;Death domain-associated protein 6","subunits.Gene.name.":"ATRX;DAXX","subunits.Gene.name.syn.":"RAD54L XH2;BING2 DAP6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"DAXX regulates ATRX activity by altering its cellular localization. DAXX targets ATRX to the promyelocytic leukemia protein nuclear bodies.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2844,"ComplexName":"Axin-p53-HIPK2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15169;P04637;Q9H2X6","subunits.Entrez.IDs.":"8312;7157;28996","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0009314;GO:0006915;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;response to radiation;apoptotic process;nucleus","FunCat.ID":"11.02.03.04;32.01.13;40.10.02;70.10","FunCat.description":"transcriptional control;electromagnetic waves stress response (e.g. UV, X-ray);apoptosis (type I programmed cell death);nucleus","PubMed.ID":15526030,"subunits.Protein.name.":"Axin-1 ;Cellular tumor antigen p53;Homeodomain-interacting protein kinase 2","subunits.Gene.name.":"AXIN1;TP53;HIPK2","subunits.Gene.name.syn.":"AXIN;P53;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Axin stimulates the transcriptional activity of p53 selectively toward some of the p53 target genes, and induces p53-dependent cell death through facilitating HIPK2 phosphorylation of Ser(46).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2845,"ComplexName":"BAX-BAK-IRE1alpha complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O08734;Q07813;Q9EQY0","subunits.Entrez.IDs.":"12018;12028;None","Protein.complex.purification.method":"MI:0047- far western blotting; MI:0019- coimmunoprecipitation","GO.ID":"GO:0006950;GO:0097193;GO:0005783","GO.description":"response to stress;intrinsic apoptotic signaling pathway;endoplasmic reticulum","FunCat.ID":"32.01;40.10.02.03.02;70.07","FunCat.description":"stress response;induction of apoptosis by intracellular signals;endoplasmic reticulum","PubMed.ID":16645094,"subunits.Protein.name.":"Bcl-2 homologous antagonist/killer ;Apoptosis regulator BAX;Serine/threonine-protein kinase/endoribonuclease IRE1","subunits.Gene.name.":"Bak1;Bax;Ern1","subunits.Gene.name.syn.":"Bak;;Ire1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Proapoptotic BAX and BAK modulate the unfolded protein response by a direct interaction with IRE1alpha.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2846,"ComplexName":"ITGAV-ITGB3-THBS1 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"blood cell","subunits.UniProt.IDs.":"P05106;P06756;P07996","subunits.Entrez.IDs.":"3690;3685;7057","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0005515","GO.description":"protein binding","FunCat.ID":"16.01","FunCat.description":"protein binding","PubMed.ID":2478219,"subunits.Protein.name.":"Integrin beta-3;Integrin alpha-V;Thrombospondin-1","subunits.Gene.name.":"ITGB3;ITGAV;THBS1","subunits.Gene.name.syn.":"GP3A;MSK8 VNRA;TSP TSP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The alpha(v)beta3 integrin on platelets, endothelial cells, and smooth muscle cells functions as an Arg-Gly-Asp (RGD)-dependent receptor for thrombospondin.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2847,"ComplexName":"ING4 complex (ING4, MYST2, C1orf149, PHF15)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95251;Q9HAF1;Q9NQC1;Q9UNL4","subunits.Entrez.IDs.":"11143;64769;23338;51147","Protein.complex.purification.method":"MI:0069- mass spectrometry studies of complexes; MI:0004- affinity chromatography technologies","GO.ID":"GO:0000278;GO:0051726;GO:0001525","GO.description":"mitotic cell cycle;regulation of cell cycle;angiogenesis","FunCat.ID":"10.03.01.01;10.03.01;41.05.16","FunCat.description":"mitotic cell cycle;mitotic cell cycle and cell cycle control;angiogenesis","PubMed.ID":16387653,"subunits.Protein.name.":"Histone acetyltransferase KAT7 ;Chromatin modification-related protein MEAF6;Protein Jade-2 ;Inhibitor of growth protein 4","subunits.Gene.name.":"KAT7;MEAF6;JADE2;ING4","subunits.Gene.name.syn.":"HBO1 HBOa MYST2;C1orf149 CENP-28 EAF6;KIAA0239 PHF15;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"ING4 associates with the HBO1 HAT required for normal progression through S phase and the majority of histone H4 acetylation in vivo. ING subunits are probably crucial for acetylation of chromatin substrates.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2848,"ComplexName":"ING4 complex (ING4, MYST2, C1orf149, PHF16)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95251;Q92613;Q9HAF1;Q9UNL4","subunits.Entrez.IDs.":"11143;9767;64769;51147","Protein.complex.purification.method":"MI:0069- mass spectrometry studies of complexes; MI:0004- affinity chromatography technologies","GO.ID":"GO:0000278;GO:0051726;GO:0001525","GO.description":"mitotic cell cycle;regulation of cell cycle;angiogenesis","FunCat.ID":"10.03.01.01;10.03.01;41.05.16","FunCat.description":"mitotic cell cycle;mitotic cell cycle and cell cycle control;angiogenesis","PubMed.ID":16387653,"subunits.Protein.name.":"Histone acetyltransferase KAT7 ;Protein Jade-3 ;Chromatin modification-related protein MEAF6;Inhibitor of growth protein 4","subunits.Gene.name.":"KAT7;JADE3;MEAF6;ING4","subunits.Gene.name.syn.":"HBO1 HBOa MYST2;KIAA0215 PHF16;C1orf149 CENP-28 EAF6;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"ING4 associates with the HBO1 HAT required for normal progression through S phase and the majority of histone H4 acetylation in vivo. ING subunits are probably crucial for acetylation of chromatin substrates.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2849,"ComplexName":"ITGAV-ITGB3-NOV complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05106;P06756;P48745","subunits.Entrez.IDs.":"3690;3685;4856","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0005515;GO:0007155","GO.description":"protein binding;cell adhesion","FunCat.ID":"16.01;34.07","FunCat.description":"protein binding;cell adhesion","PubMed.ID":12902636,"subunits.Protein.name.":"Integrin beta-3;Integrin alpha-V;Protein NOV homolog","subunits.Gene.name.":"ITGB3;ITGAV;NOV","subunits.Gene.name.syn.":"GP3A;MSK8 VNRA;CCN3 IGFBP9 NOVH","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The C-terminal domain of NOV is involved in the interaction with integrins.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2850,"ComplexName":"ITGA5-ITGB1-FN-1-NOV complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P02751;P05556;P08648;P48745","subunits.Entrez.IDs.":"2335;3688;3678;4856","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515;GO:0007155","GO.description":"protein binding;cell adhesion","FunCat.ID":"16.01;34.07","FunCat.description":"protein binding;cell adhesion","PubMed.ID":12902636,"subunits.Protein.name.":"Fibronectin ;Integrin beta-1;Integrin alpha-5 ;Protein NOV homolog","subunits.Gene.name.":"FN1;ITGB1;ITGA5;NOV","subunits.Gene.name.syn.":"FN;FNRB MDF2 MSK12;FNRA;CCN3 IGFBP9 NOVH","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The involvement of alpha5-beta1 in the process of endothelial cell adhesion to NOV was mediated by fibronectin.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2851,"ComplexName":"ING2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75446;P29374;Q09028;Q13547;Q16576;Q5PSV4;Q92769;Q96ST3;Q9H0E3;Q9H160;Q9H7L9;Q9HCU9","subunits.Entrez.IDs.":"8819;5926;5928;3065;5931;84312;3066;25942;79595;3622;64426;25855","Protein.complex.purification.method":"MI:0069- mass spectrometry studies of complexes; MI:0004- affinity chromatography technologies","GO.ID":"GO:0006265;GO:0000278;GO:0051726;GO:0006473;GO:0006476;GO:0006915;GO:0001525;GO:0051276;GO:0005634","GO.description":"DNA topological change;mitotic cell cycle;regulation of cell cycle;protein acetylation;protein deacetylation;apoptotic process;angiogenesis;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;10.03.01.01;10.03.01;14.07.04;40.10.02;41.05.16;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);mitotic cell cycle;mitotic cell cycle and cell cycle control;modification by acetylation, deacetylation;apoptosis (type I programmed cell death);angiogenesis;organization of chromosome structure;nucleus","PubMed.ID":16387653,"subunits.Protein.name.":"Histone deacetylase complex subunit SAP30;AT-rich interactive domain-containing protein 4A ;Histone-binding protein RBBP4;Histone deacetylase 1;Histone-binding protein RBBP7;Breast cancer metastasis-suppressor 1-like protein ;Histone deacetylase 2;Paired amphipathic helix protein Sin3a;Histone deacetylase complex subunit SAP130;Inhibitor of growth protein 2 ;Sin3 histone deacetylase corepressor complex component SDS3;Breast cancer metastasis-suppressor 1","subunits.Gene.name.":"SAP30;ARID4A;RBBP4;HDAC1;RBBP7;BRMS1L;HDAC2;SIN3A;SAP130;ING2;SUDS3;BRMS1","subunits.Gene.name.syn.":"None;RBBP1 RBP1;RBAP48;RPD3L1;RBAP46;;None;None;None;ING1L;SAP45 SDS3;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"ING2 is in an HDAC complex similar to ING1. ING subunits are probably crucial for acetylation of chromatin substrates.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2852,"ComplexName":"Brg1-based SWI/SNF chromatin remodeling complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O96019;Q12824;Q8TAQ2;Q92922","subunits.Entrez.IDs.":"86;6598;6601;6599","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0006265;GO:0000278;GO:0051726;GO:2001141;GO:0006355","GO.description":"DNA topological change;mitotic cell cycle;regulation of cell cycle;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated","FunCat.ID":"10.01.09.05;10.03.01.01;10.03.01;11.02.03.04","FunCat.description":"DNA conformation modification (e.g. chromatin);mitotic cell cycle;mitotic cell cycle and cell cycle control;transcriptional control","PubMed.ID":16387653,"subunits.Protein.name.":"Actin-like protein 6A;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;SWI/SNF complex subunit SMARCC2;SWI/SNF complex subunit SMARCC1","subunits.Gene.name.":"ACTL6A;SMARCB1;SMARCC2;SMARCC1","subunits.Gene.name.syn.":"BAF53 BAF53A INO80K;BAF47, INI1, SNF5L1;BAF170;BAF155","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2853,"ComplexName":"ITGA5-ITGB1-CAL4A3 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P08648;P39060","subunits.Entrez.IDs.":"3688;3678;80781","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0019- coimmunoprecipitation","GO.ID":"GO:0006469;GO:0019210","GO.description":"negative regulation of protein kinase activity;kinase inhibitor activity","FunCat.ID":"18.02.01.02.05","FunCat.description":"kinase inhibitior","PubMed.ID":12682293,"subunits.Protein.name.":"Integrin beta-1;Integrin alpha-5 ;Collagen alpha-1","subunits.Gene.name.":"ITGB1;ITGA5;COL18A1","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;FNRA;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Endostatin binding to alpha5-beta1 integrin leads to the inhibition of focal adhesion kinase/c-Raf/MEK1/2/p38/ERK1 mitogen-activated protein kinase pathway, with no effect on phosphatidylinositol 3-kinase/Akt/mTOR/4E-BP1 and Cap-dependent translation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2854,"ComplexName":"PI3-kinase p85-subunit beta- PI3-kinase p110 complex","Organism":"Bovine","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P23726;P32871","subunits.Entrez.IDs.":"282308;282306","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0048015","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;phosphatidylinositol-mediated signaling","FunCat.ID":"14.07.03","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation","PubMed.ID":8313896,"subunits.Protein.name.":"Phosphatidylinositol 3-kinase regulatory subunit beta ;Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform","subunits.Gene.name.":"PIK3R2;PIK3CA","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results demonstrate that p110 is able to form a stable, active PI 3-kinase complex with either of the p85 isoforms.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":2856,"ComplexName":"NuA4/Tip60 HAT complex","Organism":"Human","Synonyms":"ING3 subcomplex","Cell.line":"None","subunits.UniProt.IDs.":"O96019;Q92993;Q96L91;Q9H0E9;Q9H2F5;Q9NPF5;Q9NXR8;Q9UBU8;Q9Y265;Q9Y4A5","subunits.Entrez.IDs.":"86;10524;57634;10902;80314;55929;54556;10933;8607;8295","Protein.complex.purification.method":"MI:0047-far western blotting","GO.ID":"GO:0006794;GO:0006796;GO:0051276;GO:0006281;GO:0006265;GO:0000278;GO:0051726;GO:0006473;GO:0006476;GO:0003677;GO:0006915;GO:0051276;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;chromosome organization;DNA repair;DNA topological change;mitotic cell cycle;regulation of cell cycle;protein acetylation;protein deacetylation;DNA binding;apoptotic process;chromosome organization;nucleus","FunCat.ID":"01.04;42.10.03;10.01.05.01;10.01.09.05;10.03.01.01;10.03.01;14.07.04;16.03.01;40.10.02;70.10","FunCat.description":"phosphate metabolism;organization of chromosome structure;DNA repair;DNA conformation modification (e.g. chromatin);mitotic cell cycle;mitotic cell cycle and cell cycle control;modification by acetylation, deacetylation;DNA binding;apoptosis (type I programmed cell death);nucleus","PubMed.ID":16387653,"subunits.Protein.name.":"Actin-like protein 6A;Histone acetyltransferase KAT5;E1A-binding protein p400;Bromodomain-containing protein 8;Enhancer of polycomb homolog 1;DNA methyltransferase 1-associated protein 1;Inhibitor of growth protein 3;Mortality factor 4-like protein 1;RuvB-like 1;Transformation/transcription domain-associated protein","subunits.Gene.name.":"ACTL6A;KAT5;EP400;BRD8;EPC1;DMAP1;ING3;MORF4L1;RUVBL1;TRRAP","subunits.Gene.name.syn.":"BAF53 BAF53A INO80K;HTATIP TIP60;CAGH32 KIAA1498 KIAA1818 TNRC12;SMAP SMAP2;None;KIAA1425;None;MRG15;INO80H NMP238 TIP49 TIP49A;PAF400","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The NuA4 histone acetyltransferase (HAT) multisubunit complex is responsible for acetylation of histone H4 and H2A N-terminal tails in yeast. The NuA4/Tip60 HAT complex is highly conserved in eukaryotes playing primary roles in transcription, cellular response to DNA damage, and cell cycle control. ING subunits are probably crucial for acetylation of chromatin substrates.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2857,"ComplexName":"NuA4/Tip60 HAT complex","Organism":"Human","Synonyms":"ING3 complex","Cell.line":"None","subunits.UniProt.IDs.":"O95619;O96019;Q52LR7;Q92993;Q96L91;Q9H0E9;Q9H2F5;Q9HAF1;Q9NPF5;Q9NXR8;Q9UBU8;Q9Y230;Q9Y265;Q9Y4A5","subunits.Entrez.IDs.":"8089;86;26122;10524;57634;10902;80314;64769;55929;54556;10933;10856;8607;8295","Protein.complex.purification.method":"MI:0047-far western blotting","GO.ID":"GO:0006794;GO:0006796;GO:0051276;GO:0006281;GO:0006265;GO:0000278;GO:0051726;GO:0006473;GO:0006476;GO:0003677;GO:0006915;GO:0051276;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;chromosome organization;DNA repair;DNA topological change;mitotic cell cycle;regulation of cell cycle;protein acetylation;protein deacetylation;DNA binding;apoptotic process;chromosome organization;nucleus","FunCat.ID":"01.04;42.10.03;10.01.05.01;10.01.09.05;10.03.01.01;10.03.01;14.07.04;16.03.01;40.10.02;70.10","FunCat.description":"phosphate metabolism;organization of chromosome structure;DNA repair;DNA conformation modification (e.g. chromatin);mitotic cell cycle;mitotic cell cycle and cell cycle control;modification by acetylation, deacetylation;DNA binding;apoptosis (type I programmed cell death);nucleus","PubMed.ID":16387653,"subunits.Protein.name.":"YEATS domain-containing protein 4;Actin-like protein 6A;Enhancer of polycomb homolog 2;Histone acetyltransferase KAT5;E1A-binding protein p400;Bromodomain-containing protein 8;Enhancer of polycomb homolog 1;Chromatin modification-related protein MEAF6;DNA methyltransferase 1-associated protein 1;Inhibitor of growth protein 3;Mortality factor 4-like protein 1;RuvB-like 2;RuvB-like 1;Transformation/transcription domain-associated protein","subunits.Gene.name.":"YEATS4;ACTL6A;EPC2;KAT5;EP400;BRD8;EPC1;MEAF6;DMAP1;ING3;MORF4L1;RUVBL2;RUVBL1;TRRAP","subunits.Gene.name.syn.":"GAS41;BAF53 BAF53A INO80K;None;HTATIP TIP60;CAGH32 KIAA1498 KIAA1818 TNRC12;SMAP SMAP2;None;C1orf149 CENP-28 EAF6;KIAA1425;None;MRG15;INO80J TIP48 TIP49B;INO80H NMP238 TIP49 TIP49A;PAF400","Disease.comment":"None","Subunits.comment":"An actin component which was not exactly defined was also found.","Complex.comment":"The NuA4 histone acetyltransferase (HAT) multisubunit complex is responsible for acetylation of histone H4 and H2A N-terminal tails in yeast. The NuA4/Tip60 HAT complex is highly conserved in eukaryotes playing primary roles in transcription, cellular response to DNA damage, and cell cycle control. ING subunits are probably crucial for acetylation of chromatin substrates.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2858,"ComplexName":"HBO1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95251;Q6IE81;Q8WYH8;Q92613;Q9HAF1;Q9NQC1;Q9UNL4","subunits.Entrez.IDs.":"11143;79960;84289;9767;64769;23338;51147","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0000278;GO:0051726;GO:0006915","GO.description":"mitotic cell cycle;regulation of cell cycle;apoptotic process","FunCat.ID":"10.03.01.01;10.03.01;40.10.02","FunCat.description":"mitotic cell cycle;mitotic cell cycle and cell cycle control;apoptosis (type I programmed cell death)","PubMed.ID":16387653,"subunits.Protein.name.":"Histone acetyltransferase KAT7 ;Protein Jade-1 ;Inhibitor of growth protein 5 ;Protein Jade-3 ;Chromatin modification-related protein MEAF6;Protein Jade-2 ;Inhibitor of growth protein 4","subunits.Gene.name.":"KAT7;JADE1;ING5;JADE3;MEAF6;JADE2;ING4","subunits.Gene.name.syn.":"HBO1 HBOa MYST2;KIAA1807 PHF17;;KIAA0215 PHF16;C1orf149 CENP-28 EAF6;KIAA0239 PHF15;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"ING subunits are probably crucial for acetylation of chromatin substrates.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2859,"ComplexName":"ING5 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95251;O95696;P55201;Q6IE81;Q8WYB5;Q8WYH8;Q92613;Q92794;Q9HAF1;Q9NQC1;Q9ULD4","subunits.Entrez.IDs.":"11143;23774;7862;79960;23522;84289;9767;7994;64769;23338;27154","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0000278;GO:0051726;GO:0006915","GO.description":"mitotic cell cycle;regulation of cell cycle;apoptotic process","FunCat.ID":"10.03.01.01;10.03.01;40.10.02","FunCat.description":"mitotic cell cycle;mitotic cell cycle and cell cycle control;apoptosis (type I programmed cell death)","PubMed.ID":16387653,"subunits.Protein.name.":"Histone acetyltransferase KAT7 ;Bromodomain-containing protein 1 ;Peregrin ;Protein Jade-1 ;Histone acetyltransferase KAT6B ;Inhibitor of growth protein 5 ;Protein Jade-3 ;Histone acetyltransferase KAT6A ;Chromatin modification-related protein MEAF6;Protein Jade-2 ;Bromodomain and PHD finger-containing protein 3","subunits.Gene.name.":"KAT7;BRD1;BRPF1;JADE1;KAT6B;ING5;JADE3;KAT6A;MEAF6;JADE2;BRPF3","subunits.Gene.name.syn.":"HBO1 HBOa MYST2;BRL BRPF2;BR140;KIAA1807 PHF17;KIAA0383 MORF MOZ2 MYST4;;KIAA0215 PHF16;MOZ MYST3 RUNXBP2 ZNF220;C1orf149 CENP-28 EAF6;KIAA0239 PHF15;KIAA1286","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"ING5 HAT complexes interact with the MCM helicase and are essential for DNA replication to occur during S phase. ING subunits are probably crucial for acetylation of chromatin substrates.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2860,"ComplexName":"DSIF complex (DRB sensitivity-inducing factor complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00267;P63272","subunits.Entrez.IDs.":"6829;6827","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006354;GO:0045892;GO:0051098;GO:0005515;GO:0030234;GO:0050790;GO:0005634","GO.description":"DNA-templated transcription, elongation;negative regulation of transcription, DNA-templated;regulation of binding;protein binding;enzyme regulator activity;regulation of catalytic activity;nucleus","FunCat.ID":"11.02.03.01.04;11.02.03.04.03;18.01.07;16.01;18.02.01;70.10","FunCat.description":"transcription elongation;transcription repression;regulation by binding / dissociation;protein binding;enzymatic activity regulation / enzyme regulator;nucleus","PubMed.ID":10075709,"subunits.Protein.name.":"Transcription elongation factor SPT5 ;Transcription elongation factor SPT4","subunits.Gene.name.":"SUPT5H;SUPT4H1","subunits.Gene.name.syn.":"SPT5 SPT5H;SPT4H SUPT4H","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"DSIF represses transcription in the presence of DRB (inhibitor of transcription elongation), thereby inducing DRB sensitivity. SPT5 forms a stable complex with SPT4 and interacts directly with the largest subunit of RNA-Polymerase II.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2861,"ComplexName":"DSIF complex (DRB sensitivity-inducing factor complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00267;P63272","subunits.Entrez.IDs.":"6829;6827","Protein.complex.purification.method":"MI:0226- ion exchange chromatography","GO.ID":"GO:0006354;GO:0045892;GO:0051098;GO:0005515;GO:0030234;GO:0050790;GO:0005634","GO.description":"DNA-templated transcription, elongation;negative regulation of transcription, DNA-templated;regulation of binding;protein binding;enzyme regulator activity;regulation of catalytic activity;nucleus","FunCat.ID":"11.02.03.01.04;11.02.03.04.03;18.01.07;16.01;18.02.01;70.10","FunCat.description":"transcription elongation;transcription repression;regulation by binding / dissociation;protein binding;enzymatic activity regulation / enzyme regulator;nucleus","PubMed.ID":9450929,"subunits.Protein.name.":"Transcription elongation factor SPT5 ;Transcription elongation factor SPT4","subunits.Gene.name.":"SUPT5H;SUPT4H1","subunits.Gene.name.syn.":"SPT5 SPT5H;SPT4H SUPT4H","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"DSIF represses transcription in the presence of DRB (inhibitor of transcription elongation), thereby inducing DRB sensitivity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2863,"ComplexName":"Serine-palmitoyltransferase (SPT) complex","Organism":"Human","Synonyms":"None","Cell.line":"Hek293 cells","subunits.UniProt.IDs.":"O15269;O15270;Q9NUV7","subunits.Entrez.IDs.":"10558;9517;55304","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0030-cross-linking studies;MI:0091-chromatography technologies","GO.ID":"GO:0006665;GO:0043085;GO:0008047","GO.description":"sphingolipid metabolic process;positive regulation of catalytic activity;enzyme activator activity","FunCat.ID":"01.06.02.03;18.02.01.01","FunCat.description":"sphingolipid metabolism;enzyme activator","PubMed.ID":19648650,"subunits.Protein.name.":"Serine palmitoyltransferase 1;Serine palmitoyltransferase 2;Serine palmitoyltransferase 3","subunits.Gene.name.":"SPTLC1;SPTLC2;SPTLC3","subunits.Gene.name.syn.":"LCB1;KIAA0526 LCB2;C20orf38 SPTLC2L","Disease.comment":"None","Subunits.comment":"In PMID:26438849 other authors describe SPT as different isoenzymes, which are trimeric proteins composed of two large subunits (SPTLC1 and SPTLC2 or SPTLC3) and a small subunit (SPTssa or SPTssb).","Complex.comment":"By using immunoprecipitation, native gel analysis, cross-linking studies, and size exclusion chromatography, it was demonstrated that the native SPT enzyme contains all three subunits (SPTLC1-3) and forms a protein complex with a molecular mass of about 460 kDa. In PMID:17331073 the same authors confirm by blue-native-PAGE experiments  that all three SPT subunits (SPTLC1-3) are co-localized within a single SPT complex. They conclude that the functional SPT is not a dimer, but a higher organized complex, composed of three distinct subunits (SPTLC1, SPTLC2 and SPTLC3) with a molecular mass of 480 kDa. The stoichiometry of SPTLC2 and SPTLC3 in this complex seems not to be fixed and is probably changed dynamically in dependence of the tissue specific SPTLC2 and SPTLC3 expression levels.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2866,"ComplexName":"TEAD2-YAP DNA-protein complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P46938;P48301","subunits.Entrez.IDs.":"22601;21677","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0045893;GO:0003677;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04.01;16.03.01;70.10","FunCat.description":"transcription activation;DNA binding;nucleus","PubMed.ID":11358867,"subunits.Protein.name.":"Transcriptional coactivator YAP1;Transcriptional enhancer factor TEF-4","subunits.Gene.name.":"Yap1;Tead2","subunits.Gene.name.syn.":"Yap Yap65;Etdf Etf Tef4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors demonstrated that TEAD-1, -2, -3, and -4 each bound YAP with essentially the same efficiency. The authors demonstrated that TEAD-dependent transcription in vivo required YAP protein with a functional TEAD binding domain as well as a TEAD protein with a functional DNA binding domain. Localization experiments showed TEAD proteins and YAP in different cellular compartments, TEAD mainly in the nucleus, YAP mainly in the cytoplasm. It was confirmed that most of the YAP protein existed as a complex with 14-3-3 and T11 (a unidentified protein). YAP can then be transported into and out of the nucleus, where it forms a transcriptionally active complex with TEAD.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2867,"ComplexName":"TEAD1-YAP DNA-protein complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P30051;P46938","subunits.Entrez.IDs.":"21676;22601","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0045893;GO:0003677;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04.01;16.03.01;70.10","FunCat.description":"transcription activation;DNA binding;nucleus","PubMed.ID":11358867,"subunits.Protein.name.":"Transcriptional enhancer factor TEF-1 ;Transcriptional coactivator YAP1","subunits.Gene.name.":"Tead1;Yap1","subunits.Gene.name.syn.":"Tcf13 Tef-1 Tef1;Yap Yap65","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors demonstrated that TEAD-1, -2, -3, and -4 each bound YAP with essentially the same efficiency.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2868,"ComplexName":"TEAD3-YAP DNA-protein complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P46938;P70210","subunits.Entrez.IDs.":"22601;21678","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0045893;GO:0003677;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04.01;16.03.01;70.10","FunCat.description":"transcription activation;DNA binding;nucleus","PubMed.ID":11358867,"subunits.Protein.name.":"Transcriptional coactivator YAP1;Transcriptional enhancer factor TEF-5","subunits.Gene.name.":"Yap1;Tead3","subunits.Gene.name.syn.":"Yap Yap65;Tcf13r2 Tef5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors demonstrated that TEAD-1, -2, -3, and -4 each bound YAP with essentially the same efficiency.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2869,"ComplexName":"TEAD4-YAP DNA-protein complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P46938;Q62296","subunits.Entrez.IDs.":"22601;21679","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0045893;GO:0003677;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04.01;16.03.01;70.10","FunCat.description":"transcription activation;DNA binding;nucleus","PubMed.ID":11358867,"subunits.Protein.name.":"Transcriptional coactivator YAP1;Transcriptional enhancer factor TEF-3","subunits.Gene.name.":"Yap1;Tead4","subunits.Gene.name.syn.":"Yap Yap65;Tcf13r1 Tef3 Tefr1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors demonstrated that TEAD-1, -2, -3, and -4 each bound YAP with essentially the same efficiency.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2870,"ComplexName":"TEAD2-multiprotein complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P46938;P48301;P68254;Q8VBX6","subunits.Entrez.IDs.":"22601;21677;22630;17475","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0029- cosedimentation through density gradients","GO.ID":"GO:2001141;GO:0006355","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":11358867,"subunits.Protein.name.":"Transcriptional coactivator YAP1;Transcriptional enhancer factor TEF-4 ;14-3-3 protein theta ;Multiple PDZ domain protein","subunits.Gene.name.":"Yap1;Tead2;Ywhaq;Mpdz","subunits.Gene.name.syn.":"Yap Yap65;Etdf Etf Tef4;;Mupp1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In pull down experiments the authors analysed 12 proteins (T1-T12). T1/T2 correspond to YAP, T8 to MUPP1, T10 to 14-3-3, the remaining proteins couldn't be identified. Sedimentation experiments revealed that only about 5% of the complex preparation sedimented as TEAD2-multiprotein complex, about 20 % as monomeric TEAD2 protein, about 75% as TEAD2-YAP complex.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2872,"ComplexName":"ITGA2b-ITGB3-CD9-GP1b-CD47 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"blood cell","subunits.UniProt.IDs.":"P05106;P07359;P08514;P21926;Q08722","subunits.Entrez.IDs.":"3690;2811;3674;928;961","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0051098;GO:0005515;GO:0007155;GO:0005886","GO.description":"regulation of binding;protein binding;cell adhesion;plasma membrane","FunCat.ID":"18.01.07;16.01;34.07;70.02","FunCat.description":"regulation by binding / dissociation;protein binding;cell adhesion;eukaryotic plasma membrane / membrane attached","PubMed.ID":10429193,"subunits.Protein.name.":"Integrin beta-3;Platelet glycoprotein Ib alpha chain;Integrin alpha-IIb;CD9 antigen;Leukocyte surface antigen CD47","subunits.Gene.name.":"ITGB3;GP1BA;ITGA2B;CD9;CD47","subunits.Gene.name.syn.":"GP3A;None;GP2B ITGAB;MIC3 TSPAN29;MER6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The isolation of this complex was independent of platelet activation, although a twofold increase in the quantity of CD9 complex was seen after platelet activation by alpha-thrombin in the presence of CaCl2 compared with that present in EDTA.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2873,"ComplexName":"P-TEFb-7SKRNA-HEXIM1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60563;O94992;P50750","subunits.Entrez.IDs.":"904;10614;1025","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006794;GO:0006796;GO:0006354;GO:2001141;GO:0006355;GO:0006464;GO:0030234;GO:0050790;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;DNA-templated transcription, elongation;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;cellular protein modification process;enzyme regulator activity;regulation of catalytic activity;nucleus","FunCat.ID":"01.04;11.02.03.01.04;11.02.03.04;14.07;18.02.01;70.10","FunCat.description":"phosphate metabolism;transcription elongation;transcriptional control;protein modification;enzymatic activity regulation / enzyme regulator;nucleus","PubMed.ID":12832472,"subunits.Protein.name.":"Cyclin-T1;Protein HEXIM1 ;Cyclin-dependent kinase 9","subunits.Gene.name.":"CCNT1;HEXIM1;CDK9","subunits.Gene.name.syn.":"None;CLP1 EDG1 HIS1 MAQ1;CDC2L4, TAK","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"7SK RNA is required for MAQ1 to associate with P-TEFb complex. P-TEFb is inactive when bound to MAQ1 and 7SK. The 7SK RNA/MAQ1 system appears to be a new kind of CDK regulator that may contribute to a feedback loop modulating the activity of RNAP II.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2874,"ComplexName":"Slam-SAP-FynT complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O88890;P39688;Q9QUM4","subunits.Entrez.IDs.":"20400;14360;27218","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0023052;GO:0050896;GO:0005125","GO.description":"signaling;response to stimulus;cytokine activity","FunCat.ID":"30.01;36.25;40.02.03.01","FunCat.description":"cellular signalling;animal specific systemic sensing and response;cytokines (interleukines, colony stimulating factors, etc.)","PubMed.ID":15539156,"subunits.Protein.name.":"SH2 domain-containing protein 1A;Tyrosine-protein kinase Fyn;Signaling lymphocytic activation molecule","subunits.Gene.name.":"Sh2d1a;Fyn;Slamf1","subunits.Gene.name.syn.":"Xlp;None;Slam","Disease.comment":"Sh2d1a is involved in X-linked lymphoproliferative syndrome.","Subunits.comment":"None","Complex.comment":"The mutation of SAP (SAP R78A) did not affect the levels of SAP or the aptitude of SAP to associate with SLAM, a receptor involved in TH2 regulation. However, it eliminated the ability of SAP to recruit FynT and to promote SLAM-mediated protein tyrosine phosphorylation. The authors showed that the SLAM-SAP-FynT cascade is pivotal in TH2 cytokine production.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2875,"ComplexName":"BRD4-P-TEFb complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60563;O60885;P50750","subunits.Entrez.IDs.":"904;23476;1025","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0402- chromatin immunoprecipitation assays; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006794;GO:0006796;GO:0006354;GO:0045893;GO:0006464;GO:0043085;GO:0008047;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;DNA-templated transcription, elongation;positive regulation of transcription, DNA-templated;cellular protein modification process;positive regulation of catalytic activity;enzyme activator activity;nucleus","FunCat.ID":"01.04;11.02.03.01.04;11.02.03.04.01;14.07;18.02.01.01;70.10","FunCat.description":"phosphate metabolism;transcription elongation;transcription activation;protein modification;enzyme activator;nucleus","PubMed.ID":16109376,"subunits.Protein.name.":"Cyclin-T1;Bromodomain-containing protein 4 ;Cyclin-dependent kinase 9","subunits.Gene.name.":"CCNT1;BRD4;CDK9","subunits.Gene.name.syn.":"None;HUNK1;CDC2L4, TAK","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"BRD4 interacts with p-TEFb through its bromodomain. Recruitment of P-TEFb to a promoter was dependent on Brd4 and was enhanced by an increase in chromatin acetylation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2876,"ComplexName":"SNARE complex (Snap25, Vamp3, Vamp2, Napa, Stx12/13)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"G3V7P1;P54921;P60881;P63025;P63045","subunits.Entrez.IDs.":"65033;140673;25012;29528;24803","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":9817754,"subunits.Protein.name.":"Syntaxin-12 ;Alpha-soluble NSF attachment protein;Synaptosomal-associated protein 25;Vesicle-associated membrane protein 3 ;Vesicle-associated membrane protein 2","subunits.Gene.name.":"Stx12;Napa;Snap25;Vamp3;Vamp2","subunits.Gene.name.syn.":"Stx13;Snap Snapa;Snap;Syb3;Syb2","Disease.comment":"None","Subunits.comment":"Entrez Gene says that stx12 is synonym to stx13.","Complex.comment":"SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are responsible for membrane fusion in the secretory pathway.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2877,"ComplexName":"BRD4-P-TEFb complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60563;O60885;P50750","subunits.Entrez.IDs.":"904;23476;1025","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006794;GO:0006796;GO:0006354;GO:0045893;GO:0006464;GO:0043085;GO:0008047;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;DNA-templated transcription, elongation;positive regulation of transcription, DNA-templated;cellular protein modification process;positive regulation of catalytic activity;enzyme activator activity;nucleus","FunCat.ID":"01.04;11.02.03.01.04;11.02.03.04.01;14.07;18.02.01.01;70.10","FunCat.description":"phosphate metabolism;transcription elongation;transcription activation;protein modification;enzyme activator;nucleus","PubMed.ID":16109377,"subunits.Protein.name.":"Cyclin-T1;Bromodomain-containing protein 4 ;Cyclin-dependent kinase 9","subunits.Gene.name.":"CCNT1;BRD4;CDK9","subunits.Gene.name.syn.":"None;HUNK1;CDC2L4, TAK","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2878,"ComplexName":"P-TEFb-7SKRNA-HEXIM1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60563;O94992;P50750","subunits.Entrez.IDs.":"904;10614;1025","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006794;GO:0006796;GO:0006354;GO:2001141;GO:0006355;GO:0006464;GO:0030234;GO:0050790;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;DNA-templated transcription, elongation;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;cellular protein modification process;enzyme regulator activity;regulation of catalytic activity;nucleus","FunCat.ID":"01.04;11.02.03.01.04;11.02.03.04;14.07;18.02.01;70.10","FunCat.description":"phosphate metabolism;transcription elongation;transcriptional control;protein modification;enzymatic activity regulation / enzyme regulator;nucleus","PubMed.ID":16109377,"subunits.Protein.name.":"Cyclin-T1;Protein HEXIM1 ;Cyclin-dependent kinase 9","subunits.Gene.name.":"CCNT1;HEXIM1;CDK9","subunits.Gene.name.syn.":"None;CLP1 EDG1 HIS1 MAQ1;CDC2L4, TAK","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2879,"ComplexName":"CD20-LCK-FYN-p75/80 complex","Organism":"Human","Synonyms":"None","Cell.line":"MOLT-4 cells","subunits.UniProt.IDs.":"P06239;P06241;P11836","subunits.Entrez.IDs.":"3932;2534;931","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":7545683,"subunits.Protein.name.":"Tyrosine-protein kinase Lck;Tyrosine-protein kinase Fyn;B-lymphocyte antigen CD20","subunits.Gene.name.":"LCK;FYN;MS4A1","subunits.Gene.name.syn.":"None;None;CD20","Disease.comment":"None","Subunits.comment":"At the time of annotation, the identity of the additional member p75/80 of the protein complex was not known.","Complex.comment":"Lck accounted for most of the PTK activity in the CD20 complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2880,"ComplexName":"SCF subcomplex (WEE1, SKP2, BTRC)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P30291;Q13309;Q9Y297","subunits.Entrez.IDs.":"7465;6502;8945","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000279;GO:0007067;GO:0006468;GO:0006470;GO:0046777;GO:0016567;GO:0016579;GO:0030163","GO.description":"M phase;mitotic nuclear division;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;protein ubiquitination;protein deubiquitination;protein catabolic process","FunCat.ID":"10.03.01.01.11;14.07.03;14.07.05;14.13","FunCat.description":"M phase;modification by phosphorylation, dephosphorylation, autophosphorylation;modification by ubiquitination, deubiquitination;protein/peptide degradation","PubMed.ID":15070733,"subunits.Protein.name.":"Wee1-like protein kinase ;S-phase kinase-associated protein 2;F-box/WD repeat-containing protein 1A","subunits.Gene.name.":"WEE1;SKP2;BTRC","subunits.Gene.name.syn.":";FBXL1;BTRCP FBW1A FBXW1A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2881,"ComplexName":"Ubiquitin E3 ligase (CUL1, RBX1, SKP1A)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62877;P63208;Q13616","subunits.Entrez.IDs.":"9978;6500;8454","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0000279;GO:0007067;GO:0006468;GO:0006470;GO:0046777;GO:0016567;GO:0016579;GO:0043161;GO:0006511","GO.description":"M phase;mitotic nuclear division;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process","FunCat.ID":"10.03.01.01.11;14.07.03;14.07.05;14.13.01.01","FunCat.description":"M phase;modification by phosphorylation, dephosphorylation, autophosphorylation;modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway)","PubMed.ID":15070733,"subunits.Protein.name.":"E3 ubiquitin-protein ligase RBX1;S-phase kinase-associated protein 1;Cullin-1","subunits.Gene.name.":"RBX1;SKP1;CUL1","subunits.Gene.name.syn.":"RNF75, ROC1;EMC19, OCP2, SKP1A, TCEB1L;None","Disease.comment":"None","Subunits.comment":"Hemagglutinin (HA-)tagged F-box proteins were also found in this study (not further specified).","Complex.comment":"Ubiquitin E3 ligases covalently attach ubiquitin to a lysine residue on a target protein. Polyubiquitination marks proteins for degradation by the proteasome.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2882,"ComplexName":"ITGA5-ITGB3-COL6A3 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05106;P08648;P12111","subunits.Entrez.IDs.":"3690;3678;1293","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0005515;GO:0007155;GO:0005886;GO:0031012","GO.description":"protein binding;cell adhesion;plasma membrane;extracellular matrix","FunCat.ID":"16.01;34.07;70.02;70.27.01","FunCat.description":"protein binding;cell adhesion;eukaryotic plasma membrane / membrane attached;extracellular matrix component","PubMed.ID":8387021,"subunits.Protein.name.":"Integrin beta-3;Integrin alpha-5 ;Collagen alpha-3","subunits.Gene.name.":"ITGB3;ITGA5;COL6A3","subunits.Gene.name.syn.":"GP3A;FNRA;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2883,"ComplexName":"Nephrin-cadherin complex (Nphs1, Ctnnd1, Cdh3, Cd2ap)","Organism":"Rat","Synonyms":"None","Cell.line":"kidney epithelium","subunits.UniProt.IDs.":"F1LRS8;P30999;Q9JIV6;Q9R044","subunits.Entrez.IDs.":"316258;12388;116777;64563","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0096-pull down","GO.ID":"GO:0016337;GO:0045216;GO:0007043;GO:0005911","GO.description":"single organismal cell-cell adhesion;cell-cell junction organization;cell-cell junction assembly;cell-cell junction","FunCat.ID":"34.07.01;42.06.04;70.06.04","FunCat.description":"cell-cell adhesion;intercellular junction (gap junction/adherens junction);intercellular junction (gap junction/adherens junction)","PubMed.ID":15331416,"subunits.Protein.name.":"CD2-associated protein;Catenin delta-1;P-cadherin;Nephrin","subunits.Gene.name.":"Cd2ap;Ctnnd1;Cdh3;Nphs1","subunits.Gene.name.syn.":"None;Catns Kiaa0384;None;Nphn","Disease.comment":"None","Subunits.comment":"Since Ctnnd1 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"Experiments were done in rat glomeruli. The results verify that nephrin, adherens junction proteins, and CD2AP are components of a multiprotein complex in glomeruli as well as in MDCK-nephrin cells.","SWISSPROT.organism":"Rattus norvegicus (Rat);Mus musculus (Mouse);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2884,"ComplexName":"Respiratory chain complex I (early intermediate NDUFAF1 assembly), mitochondrial","Organism":"Human","Synonyms":"NADH:ubiquinone oxidoreductase (EC 1.6.5.3) incomplete intermediate","Cell.line":"None","subunits.UniProt.IDs.":"O75251;O75489;O95139;P03886;P56556;Q16795;Q9Y375","subunits.Entrez.IDs.":"374291;4722;4712;4535;4700;4704;51103","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0276-blue native page","GO.ID":"GO:0006091;GO:0009060;GO:0006461;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;protein complex assembly;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;14.10;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;assembly of protein complexes;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":17557076,"subunits.Protein.name.":"NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6;NADH-ubiquinone oxidoreductase chain 1;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial;Complex I intermediate-associated protein 30, mitochondrial","subunits.Gene.name.":"NDUFS7;NDUFS3;NDUFB6;MT-ND1;NDUFA6;NDUFA9;NDUFAF1","subunits.Gene.name.syn.":"None;None;None;MTND1 NADH1 ND1;LYRM6 NADHB14;NDUFS2L;CIA30","Disease.comment":"Complex I is involved e.g. in mitochondrial diseases, cardioencephalomyopathy (gene CIA30), or deficiency in fibroblasts.","Subunits.comment":"None","Complex.comment":"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone.NDUFAF1 is a crucial component in the early assembly of complex I but not of the mature holoenzyme.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2885,"ComplexName":"ITGAV-ITGB1-SPP1 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P06756;P10451","subunits.Entrez.IDs.":"3688;3685;6696","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0005515;GO:0007155;GO:0005886","GO.description":"protein binding;cell adhesion;plasma membrane","FunCat.ID":"16.01;34.07;70.02","FunCat.description":"protein binding;cell adhesion;eukaryotic plasma membrane / membrane attached","PubMed.ID":7532190,"subunits.Protein.name.":"Integrin beta-1;Integrin alpha-V;Osteopontin","subunits.Gene.name.":"ITGB1;ITGAV;SPP1","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;MSK8 VNRA;BNSP OPN","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2886,"ComplexName":"Respiratory chain complex I (incomplete intermediate ND1, ND2, ND3, CIA30 assembly), mitochondrial","Organism":"Human","Synonyms":"NADH:ubiquinone oxidoreductase (EC 1.6.5.3) incomplete intermediate","Cell.line":"None","subunits.UniProt.IDs.":"P03886;P03891;P03897;Q9Y375","subunits.Entrez.IDs.":"4535;4536;4537;51103","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006091;GO:0009060;GO:0006461;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;protein complex assembly;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;14.10;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;assembly of protein complexes;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":17557076,"subunits.Protein.name.":"NADH-ubiquinone oxidoreductase chain 1;NADH-ubiquinone oxidoreductase chain 2;NADH-ubiquinone oxidoreductase chain 3;Complex I intermediate-associated protein 30, mitochondrial","subunits.Gene.name.":"MT-ND1;MT-ND2;MT-ND3;NDUFAF1","subunits.Gene.name.syn.":"MTND1 NADH1 ND1;MTND2 NADH2 ND2;MTND3 NADH3 ND3;CIA30","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2887,"ComplexName":"Shc-Egfr complex, EGF stimulated","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q9QX70;Q9Z1I0","subunits.Entrez.IDs.":"24329;85385","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0007186;GO:0007173","GO.description":"G-protein coupled receptor signaling pathway;epidermal growth factor receptor signaling pathway","FunCat.ID":"30.05.02.24;30.05.01.12.01","FunCat.description":"G-protein coupled receptor signalling pathway;EGF-receptor signalling pathway","PubMed.ID":7798267,"subunits.Protein.name.":"Receptor protein-tyrosine kinase ;Shc transforming protein","subunits.Gene.name.":"Egfr;Shc1","subunits.Gene.name.syn.":";shc","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"EGF treatment led to rapid tyrosine phosphorylation of Shc. The authors showed that EGFR-Shc complex formation was comparable to the kinetics of Shc phosphorylation.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2888,"ComplexName":"Grb2-Egfr complex, EGF stimulated","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62994;Q9QX70","subunits.Entrez.IDs.":"81504;24329","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0007186;GO:0007173","GO.description":"G-protein coupled receptor signaling pathway;epidermal growth factor receptor signaling pathway","FunCat.ID":"30.05.02.24;30.05.01.12.01","FunCat.description":"G-protein coupled receptor signalling pathway;EGF-receptor signalling pathway","PubMed.ID":7798267,"subunits.Protein.name.":"Growth factor receptor-bound protein 2 ;Receptor protein-tyrosine kinase","subunits.Gene.name.":"Grb2;Egfr","subunits.Gene.name.syn.":"Ash;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Tyrosine-phosphorylated EGFRs were co-precipitated by the anti-Grb2 antibody, but the magnitude of EGFR-Grb2 complex formation was much less than for EGFR-Shc complexes.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2889,"ComplexName":"Grb2-Shc complex, EGF stimulated","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62994;Q9Z1I0","subunits.Entrez.IDs.":"81504;85385","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0007186;GO:0007173","GO.description":"G-protein coupled receptor signaling pathway;epidermal growth factor receptor signaling pathway","FunCat.ID":"30.05.02.24;30.05.01.12.01","FunCat.description":"G-protein coupled receptor signalling pathway;EGF-receptor signalling pathway","PubMed.ID":7798267,"subunits.Protein.name.":"Growth factor receptor-bound protein 2 ;Shc transforming protein","subunits.Gene.name.":"Grb2;Shc1","subunits.Gene.name.syn.":"Ash;shc","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors showed that a substantially larger amount of Grb2 associated with Shc than with EGFR.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2890,"ComplexName":"Notch1-fraction 30 complex","Organism":"Human","Synonyms":"CSL-NotchIC-Mastermind complex","Cell.line":"None","subunits.UniProt.IDs.":"P46531;Q06330;Q92585","subunits.Entrez.IDs.":"4851;3516;9794","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0045893;GO:0003677;GO:0007219;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;Notch signaling pathway;nucleus","FunCat.ID":"11.02.03.04.01;16.03.01;30.05.02.14;70.10","FunCat.description":"transcription activation;DNA binding;Notch-receptor signalling pathway;nucleus","PubMed.ID":11997524,"subunits.Protein.name.":"Neurogenic locus notch homolog protein 1 ;Recombining binding protein suppressor of hairless ;Mastermind-like protein 1","subunits.Gene.name.":"NOTCH1;RBPJ;MAML1","subunits.Gene.name.syn.":"TAN1;IGKJRB IGKJRB1 RBPJK RBPSUH;KIAA0200","Disease.comment":"Notch1 is involved in human cancer.","Subunits.comment":"None","Complex.comment":"Complex formation is required for neoplastic transformation by Notch. MAML1 promotes association between NotchIC (intracellular domain of Notch) and RBPSUH (CSL). NotchIC binding to CSL displaces corepressors from CSL, leading to the binding of the transcriptional coactivator MAML1 to the complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2891,"ComplexName":"Gamma-secretase complex (APH1A, PSEN1, PSENEN, NCSTN)","Organism":"Human","Synonyms":"presenilin complex","Cell.line":"None","subunits.UniProt.IDs.":"P49768;Q92542;Q96BI3;Q9NZ42","subunits.Entrez.IDs.":"5663;23385;51107;55851","Protein.complex.purification.method":"MI:0040- electron microscopy","GO.ID":"GO:0016485;GO:0016485;GO:0051090;GO:0023052;GO:0007219;GO:0005886;GO:0005794","GO.description":"protein processing;protein processing;regulation of sequence-specific DNA binding transcription factor activity;signaling;Notch signaling pathway;plasma membrane;Golgi apparatus","FunCat.ID":"14.07.11;18.02.09;30.01;30.05.02.14;70.02;70.08","FunCat.description":"protein processing (proteolytic);regulator of transcription factor;cellular signalling;Notch-receptor signalling pathway;eukaryotic plasma membrane / membrane attached;Golgi","PubMed.ID":16636269,"subunits.Protein.name.":"Presenilin-1;Nicastrin;Gamma-secretase subunit APH-1A;Gamma-secretase subunit PEN-2","subunits.Gene.name.":"PSEN1;NCSTN;APH1A;PSENEN","subunits.Gene.name.syn.":"AD3 PS1 PSNL1;KIAA0253;PSF;PEN2","Disease.comment":"Gamma-secretase is involved in Alzheimer's disease. In combination with Notch signaling pathway gamma secretase complex is also involved in lung cancer (PMID:17804716).","Subunits.comment":"None","Complex.comment":"Proteolytic cleavage within the hydrophobic transmembrane domains of Notch and APP is intimately associated with a multimeric gamma-secretase complex that contains the presenilin-1 or presenilin-2 and the membrane glycoprotein nicastrin. Three variants of APH1 (APH1A short, APH1A long and APH1B) as well as two presenillin variants (PSEN1 and PSEN2) allow the formation of six different gamma-secretase complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2892,"ComplexName":"BCR-ABL (p185 fusion protein)-GRB2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62993;Q13745","subunits.Entrez.IDs.":"2885;None","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0023052;GO:0007186","GO.description":"signaling;G-protein coupled receptor signaling pathway","FunCat.ID":"30.01;30.05.02.24","FunCat.description":"cellular signalling;G-protein coupled receptor signalling pathway","PubMed.ID":8112292,"subunits.Protein.name.":"Growth factor receptor-bound protein 2;Acute lymphocytic leukemia","subunits.Gene.name.":"GRB2;","subunits.Gene.name.syn.":"ASH;","Disease.comment":"Chimeric bcr-abl oncogene is involved in Philadelphia chromosome positive (Ph+) chronic myelogenous leukemia (CML) and acute lymphoblastic leukemia (Ph+ ALL).","Subunits.comment":"None","Complex.comment":"It was shown that Grb2 binds to the Tyr177 autophosphorylation site on Bcr-Abl.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2893,"ComplexName":"BCR-ABL (p210 fusion protein)-GRB2-SOS1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"A1Z199;P62993;Q07889","subunits.Entrez.IDs.":"None;2885;6654","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0023052;GO:0007186","GO.description":"signaling;G-protein coupled receptor signaling pathway","FunCat.ID":"30.01;30.05.02.24","FunCat.description":"cellular signalling;G-protein coupled receptor signalling pathway","PubMed.ID":8112292,"subunits.Protein.name.":"BCR/ABL p210 fusion protein ;Growth factor receptor-bound protein 2;Son of sevenless homolog 1","subunits.Gene.name.":"BCR/ABL fu;GRB2;SOS1","subunits.Gene.name.syn.":";ASH;None","Disease.comment":"Chimeric bcr-abl oncogene is involved in Philadelphia chromosome positive (Ph+) chronic myelogenous leukemia (CML) and acute lymphoblastic leukemia (Ph+ ALL).","Subunits.comment":"None","Complex.comment":"It was shown that Grb2 binds to the Tyr177 autophosphorylation site on Bcr-Abl.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2894,"ComplexName":"Itga1-Itgb1-Tgm2 complex","Organism":"Rat","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P18614;P49134;Q6P6R6","subunits.Entrez.IDs.":"25118;24511;56083","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515;GO:0007155","GO.description":"protein binding;cell adhesion","FunCat.ID":"16.01;34.07","FunCat.description":"protein binding;cell adhesion","PubMed.ID":10684262,"subunits.Protein.name.":"Integrin alpha-1 ;Integrin beta-1 ;Transglutaminase 2, C polypeptide","subunits.Gene.name.":"Itga1;Itgb1;Tgm2","subunits.Gene.name.syn.":";;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2895,"ComplexName":"SHC-GRB2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P29353;P62993","subunits.Entrez.IDs.":"6464;2885","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":8112292,"subunits.Protein.name.":"SHC-transforming protein 1;Growth factor receptor-bound protein 2","subunits.Gene.name.":"SHC1;GRB2","subunits.Gene.name.syn.":"SHC SHCA;ASH","Disease.comment":"Chimeric bcr-abl oncogene is involved in Philadelphia chromosome positive (Ph+) chronic myelogenous leukemia (CML) and acute lymphoblastic leukemia (Ph+ ALL).","Subunits.comment":"None","Complex.comment":"Bcr-Abl proteins induce the formation of a complex between tyrosine phosphorylated Shc and Grb2. Co-precipitation analysed in R1-p185, R1-p210 and in Ph(+) leucemic cell lines. No co-precipitation seen in parental R1 cells.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2896,"ComplexName":"ITGA2b-ITGB3-CD47-FAK complex","Organism":"Human","Synonyms":"None","Cell.line":"blood cell","subunits.UniProt.IDs.":"P05106;P08514;Q05397;Q08722","subunits.Entrez.IDs.":"3690;3674;5747;961","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies;MI:0019-coimmunoprecipitation","GO.ID":"GO:0005515;GO:0007155","GO.description":"protein binding;cell adhesion","FunCat.ID":"16.01;34.07","FunCat.description":"protein binding;cell adhesion","PubMed.ID":9169439,"subunits.Protein.name.":"Integrin beta-3;Integrin alpha-IIb;Focal adhesion kinase 1;Leukocyte surface antigen CD47","subunits.Gene.name.":"ITGB3;ITGA2B;PTK2;CD47","subunits.Gene.name.syn.":"GP3A;GP2B ITGAB;FAK FAK1;MER6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Activation of platelets with the agonist peptide 4N1K results in the association of FAK with the IAP-alpha-IIb-beta3 complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2897,"ComplexName":"RBPJ-NotchIC-Mastermind complex","Organism":"Human","Synonyms":"Mam1-RBPJ-Notch1IC complex","Cell.line":"None","subunits.UniProt.IDs.":"P46531;Q06330;Q92585","subunits.Entrez.IDs.":"4851;3516;9794","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0045893;GO:0003677;GO:0007219;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;Notch signaling pathway;nucleus","FunCat.ID":"11.02.03.04.01;16.03.01;30.05.02.14;70.10","FunCat.description":"transcription activation;DNA binding;Notch-receptor signalling pathway;nucleus","PubMed.ID":11390662,"subunits.Protein.name.":"Neurogenic locus notch homolog protein 1 ;Recombining binding protein suppressor of hairless ;Mastermind-like protein 1","subunits.Gene.name.":"NOTCH1;RBPJ;MAML1","subunits.Gene.name.syn.":"TAN1;IGKJRB IGKJRB1 RBPJK RBPSUH;KIAA0200","Disease.comment":"Notch1 is involved in human cancer.","Subunits.comment":"None","Complex.comment":"Complex formation is required for neoplastic transformation by Notch. MAML1 promotes association between NotchIC (intracellular domain of Notch) and RBPSUH (CSL). NotchIC binding to CSL displaces corepressors from CSL, leading to the binding of the transcriptional coactivator MAML1 to the complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2898,"ComplexName":"Respiratory chain complex I (intermediate I/200kD and III/250kD), mitochondrial","Organism":"Human","Synonyms":"NADH:ubiquinone oxidoreductase (EC 1.6.5.3) subcomplex I and III","Cell.line":"None","subunits.UniProt.IDs.":"O75306;O75489;Q16795","subunits.Entrez.IDs.":"4720;4722;4704","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0276- blue native page","GO.ID":"GO:0006091;GO:0009060;GO:0006461;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;protein complex assembly;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;14.10;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;assembly of protein complexes;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":12941961,"subunits.Protein.name.":"NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial","subunits.Gene.name.":"NDUFS2;NDUFS3;NDUFA9","subunits.Gene.name.syn.":"None;None;NDUFS2L","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone. Intermediate I and III show the same components (therefore annotated as one entry only) but different molecular weights.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2899,"ComplexName":"PLC-gamma-1-Lab-Blnk complex, BCR stimulated","Organism":"Mouse","Synonyms":"None","Cell.line":"B-cell","subunits.UniProt.IDs.":"Q62077;Q9JHL0;Q9QUN3","subunits.Entrez.IDs.":"18803;56743;17060","Protein.complex.purification.method":"MI:0096-pull down","GO.ID":"GO:0023052;GO:0019724;GO:0030183;GO:0005886","GO.description":"signaling;B cell mediated immunity;B cell differentiation;plasma membrane","FunCat.ID":"30.01;36.25.16.03.01;43.03.07.02.01.01;70.02","FunCat.description":"cellular signalling;humoral response (B-cells);B-cell;eukaryotic plasma membrane / membrane attached","PubMed.ID":12514734,"subunits.Protein.name.":"1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1;Linker for activation of T-cells family member 2;B-cell linker protein","subunits.Gene.name.":"Plcg1;Lat2;Blnk","subunits.Gene.name.syn.":"Plcg-1;Lab Ntal Wbscr15 Wbscr5;Bash Ly57 Slp65","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"LAB could be phosphorylated upon stimulation of splenocytes via the BCR by the Syk tyrosine kinase. The authors propose that BLNK and LAB in B cells are a functionally equivalent pair to SLP-76 and LAT in T cells.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2900,"ComplexName":"PLC-gamma-2-Lab-Blnk complex, BCR stimulated","Organism":"Mouse","Synonyms":"None","Cell.line":"B-cell","subunits.UniProt.IDs.":"Q8CIH5;Q9JHL0;Q9QUN3","subunits.Entrez.IDs.":"234779;56743;17060","Protein.complex.purification.method":"MI:0096-pull down","GO.ID":"GO:0023052;GO:0019724;GO:0030183;GO:0005886","GO.description":"signaling;B cell mediated immunity;B cell differentiation;plasma membrane","FunCat.ID":"30.01;36.25.16.03.01;43.03.07.02.01.01;70.02","FunCat.description":"cellular signalling;humoral response (B-cells);B-cell;eukaryotic plasma membrane / membrane attached","PubMed.ID":12514734,"subunits.Protein.name.":"1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2;Linker for activation of T-cells family member 2;B-cell linker protein","subunits.Gene.name.":"Plcg2;Lat2;Blnk","subunits.Gene.name.syn.":"None;Lab Ntal Wbscr15 Wbscr5;Bash Ly57 Slp65","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"LAB could be phosphorylated upon stimulation of splenocytes via the BCR by the Syk tyrosine kinase. The authors propose that BLNK and LAB in B cells are a functionally equivalent pair to SLP-76 and LAT in T cells.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2901,"ComplexName":"Respiratory chain complex I (intermediate IV/310kD), mitochondrial","Organism":"Human","Synonyms":"NADH:ubiquinone oxidoreductase (EC 1.6.5.3) subcomplex IV","Cell.line":"None","subunits.UniProt.IDs.":"O75306;O75489;P03886;Q16795","subunits.Entrez.IDs.":"4720;4722;4535;4704","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0276- blue native page","GO.ID":"GO:0006091;GO:0009060;GO:0006461;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;protein complex assembly;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;14.10;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;assembly of protein complexes;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":12941961,"subunits.Protein.name.":"NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial;NADH-ubiquinone oxidoreductase chain 1;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial","subunits.Gene.name.":"NDUFS2;NDUFS3;MT-ND1;NDUFA9","subunits.Gene.name.syn.":"None;None;MTND1 NADH1 ND1;NDUFS2L","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2902,"ComplexName":"Grb2-Lab-Blnk complex, BCR stimulated","Organism":"Mouse","Synonyms":"None","Cell.line":"B-cell","subunits.UniProt.IDs.":"Q60631;Q9JHL0;Q9QUN3","subunits.Entrez.IDs.":"14784;56743;17060","Protein.complex.purification.method":"MI:0096-pull down","GO.ID":"GO:0023052;GO:0019724;GO:0030183;GO:0005886","GO.description":"signaling;B cell mediated immunity;B cell differentiation;plasma membrane","FunCat.ID":"30.01;36.25.16.03.01;43.03.07.02.01.01;70.02","FunCat.description":"cellular signalling;humoral response (B-cells);B-cell;eukaryotic plasma membrane / membrane attached","PubMed.ID":12514734,"subunits.Protein.name.":"Growth factor receptor-bound protein 2;Linker for activation of T-cells family member 2;B-cell linker protein","subunits.Gene.name.":"Grb2;Lat2;Blnk","subunits.Gene.name.syn.":"None;Lab Ntal Wbscr15 Wbscr5;Bash Ly57 Slp65","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"LAB could be phosphorylated upon stimulation of splenocytes via the BCR by the Syk tyrosine kinase. LAB subsequently associates with Grb2, thereby recruiting Grb2 and Grb2-associated proteins to lipid rafts at the membrane. The authors propose that BLNK and LAB in B cells are a functionally equivalent pair to SLP-76 and LAT in T cells.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2903,"ComplexName":"Respiratory chain complex I (intermediate V/380kD and VI/480kD), mitochondrial","Organism":"Human","Synonyms":"NADH:ubiquinone oxidoreductase (EC 1.6.5.3) subcomplex V and VI","Cell.line":"None","subunits.UniProt.IDs.":"O43678;O75306;O75489;P03886;Q16795","subunits.Entrez.IDs.":"4695;4720;4722;4535;4704","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0276- blue native page","GO.ID":"GO:0006091;GO:0009060;GO:0006461;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;protein complex assembly;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;14.10;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;assembly of protein complexes;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":12941961,"subunits.Protein.name.":"NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2;NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial;NADH-ubiquinone oxidoreductase chain 1;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial","subunits.Gene.name.":"NDUFA2;NDUFS2;NDUFS3;MT-ND1;NDUFA9","subunits.Gene.name.syn.":"None;None;None;MTND1 NADH1 ND1;NDUFS2L","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone. Intermediate V and VI show the same components (therefore annotated as one entry only) but different molecular weights.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2904,"ComplexName":"Respiratory chain complex I (intermediate VII/650kD), mitochondrial","Organism":"Human","Synonyms":"NADH:ubiquinone oxidoreductase (EC 1.6.5.3) subcomplex VII","Cell.line":"None","subunits.UniProt.IDs.":"O43181;O43678;O43920;O75251;O75306;O75489;P03886;P19404;P56556;Q16795","subunits.Entrez.IDs.":"4724;4695;4725;374291;4720;4722;4535;4729;4700;4704","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0276- blue native page","GO.ID":"GO:0006091;GO:0009060;GO:0006461;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;protein complex assembly;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;14.10;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;assembly of protein complexes;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":12941961,"subunits.Protein.name.":"NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2;NADH dehydrogenase [ubiquinone] iron-sulfur protein 5;NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial;NADH-ubiquinone oxidoreductase chain 1;NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial","subunits.Gene.name.":"NDUFS4;NDUFA2;NDUFS5;NDUFS7;NDUFS2;NDUFS3;MT-ND1;NDUFV2;NDUFA6;NDUFA9","subunits.Gene.name.syn.":"None;None;None;None;None;None;MTND1 NADH1 ND1;None;LYRM6 NADHB14;NDUFS2L","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2905,"ComplexName":"Respiratory chain complex I (holoenzyme), mitochondrial","Organism":"Human","Synonyms":"NADH:ubiquinone oxidoreductase (EC 1.6.5.3) holoenzyme","Cell.line":"None","subunits.UniProt.IDs.":"O43181;O43678;O43920;O75251;O75306;O75489;O95139;P03886;P19404;P56556;Q16795","subunits.Entrez.IDs.":"4724;4695;4725;374291;4720;4722;4712;4535;4729;4700;4704","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0276- blue native page","GO.ID":"GO:0006091;GO:0009060;GO:0006461;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;protein complex assembly;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;14.10;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;assembly of protein complexes;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":12941961,"subunits.Protein.name.":"NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2;NADH dehydrogenase [ubiquinone] iron-sulfur protein 5;NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6;NADH-ubiquinone oxidoreductase chain 1;NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial","subunits.Gene.name.":"NDUFS4;NDUFA2;NDUFS5;NDUFS7;NDUFS2;NDUFS3;NDUFB6;MT-ND1;NDUFV2;NDUFA6;NDUFA9","subunits.Gene.name.syn.":"None;None;None;None;None;None;None;MTND1 NADH1 ND1;None;LYRM6 NADHB14;NDUFS2L","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2906,"ComplexName":"Respiratory chain complex I (intermediate II/230kD), mitochondrial","Organism":"Human","Synonyms":"NADH:ubiquinone oxidoreductase (EC 1.6.5.3) subcomplex II","Cell.line":"None","subunits.UniProt.IDs.":"O43181;O75251;P19404","subunits.Entrez.IDs.":"4724;374291;4729","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0276- blue native page","GO.ID":"GO:0006091;GO:0009060;GO:0006461;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;protein complex assembly;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;14.10;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;assembly of protein complexes;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":12941961,"subunits.Protein.name.":"NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial;NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial","subunits.Gene.name.":"NDUFS4;NDUFS7;NDUFV2","subunits.Gene.name.syn.":"None;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2907,"ComplexName":"RBP-Jkappa-Notch1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P46531;Q06330","subunits.Entrez.IDs.":"4851;3516","Protein.complex.purification.method":"MI:0412- electrophoretic mobility supershift assay","GO.ID":"GO:0045893;GO:0003677;GO:0007219;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;Notch signaling pathway;nucleus","FunCat.ID":"11.02.03.04.01;16.03.01;30.05.02.14;70.10","FunCat.description":"transcription activation;DNA binding;Notch-receptor signalling pathway;nucleus","PubMed.ID":12374742,"subunits.Protein.name.":"Neurogenic locus notch homolog protein 1 ;Recombining binding protein suppressor of hairless","subunits.Gene.name.":"NOTCH1;RBPJ","subunits.Gene.name.syn.":"TAN1;IGKJRB IGKJRB1 RBPJK RBPSUH","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2908,"ComplexName":"RBP-Jkappa-SHARP complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q06330;Q96T58","subunits.Entrez.IDs.":"3516;23013","Protein.complex.purification.method":"MI:0412- electrophoretic mobility supershift assay","GO.ID":"GO:0045892;GO:0003677;GO:0007219;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;DNA binding;Notch signaling pathway;nucleus","FunCat.ID":"11.02.03.04.03;16.03.01;30.05.02.14;70.10","FunCat.description":"transcription repression;DNA binding;Notch-receptor signalling pathway;nucleus","PubMed.ID":12374742,"subunits.Protein.name.":"Recombining binding protein suppressor of hairless ;Msx2-interacting protein","subunits.Gene.name.":"RBPJ;SPEN","subunits.Gene.name.syn.":"IGKJRB IGKJRB1 RBPJK RBPSUH;KIAA0929 MINT SHARP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2909,"ComplexName":"PLC-gamma-2-Syk-LAT-FcR-gamma complex","Organism":"Human","Synonyms":"None","Cell.line":"platelet","subunits.UniProt.IDs.":"O43561;P12314;P16885;P43405","subunits.Entrez.IDs.":"27040;2209;5336;6850","Protein.complex.purification.method":"MI:0096-pull down","GO.ID":"GO:0007169;GO:0007596;GO:0048015","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway;blood coagulation;phosphatidylinositol-mediated signaling","FunCat.ID":"30.05.01.12;36.25.16.09","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways;blood coagulation","PubMed.ID":10469124,"subunits.Protein.name.":"Linker for activation of T-cells family member 1;High affinity immunoglobulin gamma Fc receptor I;1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2;Tyrosine-protein kinase SYK","subunits.Gene.name.":"LAT;FCGR1A;PLCG2;SYK","subunits.Gene.name.syn.":"None;FCG1 FCGR1 IGFR1;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Analyses done with different GST-PLC-gamma-2 fusion proteins from resting and CRP (collagen-related peptide) stimulated platelets.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2910,"ComplexName":"PLC-gamma-2-Lyn-FcR-gamma complex","Organism":"Human","Synonyms":"None","Cell.line":"platelet","subunits.UniProt.IDs.":"P07948;P12314;P16885","subunits.Entrez.IDs.":"4067;2209;5336","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007169;GO:0007596;GO:0048015","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway;blood coagulation;phosphatidylinositol-mediated signaling","FunCat.ID":"30.05.01.12;36.25.16.09","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways;blood coagulation","PubMed.ID":10469124,"subunits.Protein.name.":"Tyrosine-protein kinase Lyn;High affinity immunoglobulin gamma Fc receptor I;1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2","subunits.Gene.name.":"LYN;FCGR1A;PLCG2","subunits.Gene.name.syn.":"JTK8;FCG1 FCGR1 IGFR1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Analyses done with different GST-PLC-gamma-2 fusion proteins from resting and CRP (collagen-related peptide) stimulated platelets. PLC-gamma-2 associates in vivo with Lyn and FcR gamma chain. The identity of Lyn was confirmed by sequential immunoprecipitation after the kinase assay.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2911,"ComplexName":"SMRT-SKIP-CBF1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q06330;Q13573;Q9Y618","subunits.Entrez.IDs.":"3516;22938;9612","Protein.complex.purification.method":"MI:0428- imaging techniques","GO.ID":"GO:2001141;GO:0006355;GO:0006886;GO:0006605;GO:0015031;GO:0007219;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;intracellular protein transport;protein targeting;protein transport;Notch signaling pathway;nucleus","FunCat.ID":"11.02.03.04;14.04;20.01.10;30.05.02.14;70.10","FunCat.description":"transcriptional control;protein targeting, sorting and translocation;protein transport;Notch-receptor signalling pathway;nucleus","PubMed.ID":11509665,"subunits.Protein.name.":"Recombining binding protein suppressor of hairless ;SNW domain-containing protein 1 ;Nuclear receptor corepressor 2","subunits.Gene.name.":"RBPJ;SNW1;NCOR2","subunits.Gene.name.syn.":"IGKJRB IGKJRB1 RBPJK RBPSUH;SKIIP SKIP;CTG26","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"CIR seems to tether SKIP to SMRT.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2912,"ComplexName":"PLC-gamma-2-SLP-76 complex","Organism":"Human","Synonyms":"None","Cell.line":"platelet","subunits.UniProt.IDs.":"P16885;Q13094","subunits.Entrez.IDs.":"5336;3937","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007169;GO:0007596;GO:0048015","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway;blood coagulation;phosphatidylinositol-mediated signaling","FunCat.ID":"30.05.01.12;36.25.16.09","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways;blood coagulation","PubMed.ID":10469124,"subunits.Protein.name.":"1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2;Lymphocyte cytosolic protein 2","subunits.Gene.name.":"PLCG2;LCP2","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Analyses done with  GST-PLC-gamma-2SH2(C) fusion protein from resting and CRP (collagen-related peptide) stimulated platelets. PLC-gamma-2 associates directly with SLP-76 and LAT.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2913,"ComplexName":"PLC-gamma-2-LAT complex","Organism":"Human","Synonyms":"None","Cell.line":"platelet","subunits.UniProt.IDs.":"O43561;P16885","subunits.Entrez.IDs.":"27040;5336","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007169;GO:0007596;GO:0048015","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway;blood coagulation;phosphatidylinositol-mediated signaling","FunCat.ID":"30.05.01.12;36.25.16.09","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways;blood coagulation","PubMed.ID":10469124,"subunits.Protein.name.":"Linker for activation of T-cells family member 1;1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2","subunits.Gene.name.":"LAT;PLCG2","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Analyses done with  GST-PLC-gamma-2SH2(C) fusion protein from resting and CRP (collagen-related peptide) stimulated platelets. PLC-gamma-2 associates directly with SLP-76 and LAT.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2914,"ComplexName":"Respiratory chain complex I (beta subunit) mitochondrial","Organism":"Human","Synonyms":"NADH:ubiquinone oxidoreductase (EC 1.6.5.3) beta subunit","Cell.line":"None","subunits.UniProt.IDs.":"O00483;O14561;O43674;O43676;O75438;O95139;O95168;O95169;O95178;O95298;O96000;P03905;P03915;P17568;Q9NX14;Q9Y6M9","subunits.Entrez.IDs.":"4697;4706;4711;4709;4707;4712;4710;4714;4708;4718;4716;4538;4540;4713;54539;4715","Protein.complex.purification.method":"MI:0276- blue native page; MI:0063- prediction","GO.ID":"GO:0006091;GO:0009060;GO:0006461;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;protein complex assembly;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;14.10;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;assembly of protein complexes;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":15317750,"subunits.Protein.name.":"Cytochrome c oxidase subunit NDUFA4;Acyl carrier protein, mitochondrial;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial;NADH dehydrogenase [ubiquinone] 1 subunit C2;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10;NADH-ubiquinone oxidoreductase chain 4 ;NADH-ubiquinone oxidoreductase chain 5;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9","subunits.Gene.name.":"NDUFA4;NDUFAB1;NDUFB5;NDUFB3;NDUFB1;NDUFB6;NDUFB4;NDUFB8;NDUFB2;NDUFC2;NDUFB10;MT-ND4;MT-ND5;NDUFB7;NDUFB11;NDUFB9","subunits.Gene.name.syn.":"None;None;None;None;None;None;None;None;None;None;None;MTND4 NADH4 ND4;MTND5 NADH5 ND5;None;None;LYRM3 UQOR22","Disease.comment":"None","Subunits.comment":"The authors assume an additional component (homolog to the bovine 10.6K protein).","Complex.comment":"Complex I couples the transfer of two electrons from NADH to ubiquinone to the translocation of four protons across the mitochondrial inner membrane. Complex I  is an L-shaped molecule with one arm embedded in the mitochondrial inner membane and one arm protruding into the matrix, the peripheral arm. The assembly of complex I is a semi-sequential process in which different preassembled subcomplexes are joined to form the holoenzyme.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2915,"ComplexName":"CASK-Caskin1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain, hippocampal neurons","subunits.UniProt.IDs.":"Q62915;Q8VHK2","subunits.Entrez.IDs.":"29647;140722","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation;MI:0096- pull down","GO.ID":"GO:0006461;GO:0007268","GO.description":"protein complex assembly;synaptic transmission","FunCat.ID":"14.10;34.03.01","FunCat.description":"assembly of protein complexes;synaptic transmission","PubMed.ID":12040031,"subunits.Protein.name.":"Peripheral plasma membrane protein CASK;Caskin-1","subunits.Gene.name.":"Cask;Caskin1","subunits.Gene.name.syn.":"None;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Caskin1 and Mint1 bind to the same site on CASK and compete with each other for CASK binding.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2916,"ComplexName":"CASK-Caskin1-Velis complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"Q62915;Q792I0;Q8VHK2;Q9Z250;Q9Z252","subunits.Entrez.IDs.":"29647;60442;140722;85327;60377","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006461;GO:0007268","GO.description":"protein complex assembly;synaptic transmission","FunCat.ID":"14.10;34.03.01","FunCat.description":"assembly of protein complexes;synaptic transmission","PubMed.ID":12040031,"subunits.Protein.name.":"Peripheral plasma membrane protein CASK;Protein lin-7 homolog C ;Caskin-1 ;Protein lin-7 homolog A;Protein lin-7 homolog B","subunits.Gene.name.":"Cask;Lin7c;Caskin1;Lin7a;Lin7b","subunits.Gene.name.syn.":"None;Mals3 Veli3;;Mals1 Veli1;Mals2 Veli1a Veli2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Caskin1 and Mint1 bind to the same site on CASK and compete with each other for CASK binding.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2917,"ComplexName":"Grb2-Sos complex, Fc receptor gamma-R1 stimulated","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62993;Q07889","subunits.Entrez.IDs.":"2885;6654","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007169;GO:0006955","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway;immune response","FunCat.ID":"30.05.01.12;36.25.16","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways;immune response","PubMed.ID":9716598,"subunits.Protein.name.":"Growth factor receptor-bound protein 2;Son of sevenless homolog 1","subunits.Gene.name.":"GRB2;SOS1","subunits.Gene.name.syn.":"ASH;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In literature it has been shown that Grb2 binds to the guanine nucleotide exchange factor Sos, leading to activation of Ras.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2918,"ComplexName":"Ku antigen-YY1-alphaMyHC promoter complex","Organism":"Human","Synonyms":"Ku70-Ku80-YY1-alphaMyHC promoter complex","Cell.line":"None","subunits.UniProt.IDs.":"P12956;P13010;P25490","subunits.Entrez.IDs.":"2547;7520;7528","Protein.complex.purification.method":"MI:0412- electrophoretic mobility supershift assay; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0045892;GO:0003677;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04.03;16.03.01;70.10","FunCat.description":"transcription repression;DNA binding;nucleus","PubMed.ID":15367688,"subunits.Protein.name.":"X-ray repair cross-complementing protein 6 ;X-ray repair cross-complementing protein 5 ;Transcriptional repressor protein YY1","subunits.Gene.name.":"XRCC6;XRCC5;YY1","subunits.Gene.name.syn.":"G22P1;G22P2;INO80S","Disease.comment":"Human heart failure","Subunits.comment":"None","Complex.comment":"Ku complex binds to the human alphaMyHC promoter and represses alphaMyHC expression. Ku70 and YY1 protein levels are increased in patients with heart failure.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2919,"ComplexName":"Respiratory chain complex I (gamma subunit) mitochondrial","Organism":"Human","Synonyms":"NADH:ubiquinone oxidoreductase (EC 1.6.5.3) gamma subunit","Cell.line":"None","subunits.UniProt.IDs.":"O15239;O43677;O43920;O95167;O95299;P03886;P03891;P03897;P03901;P03923;P51970;P56556;Q16795","subunits.Entrez.IDs.":"4694;4717;4725;4696;4705;4535;4536;4537;4539;4541;4702;4700;4704","Protein.complex.purification.method":"MI:0276- blue native page; MI:0063- prediction","GO.ID":"GO:0006091;GO:0009060;GO:0006461;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;protein complex assembly;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;14.10;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;assembly of protein complexes;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":15317750,"subunits.Protein.name.":"NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1;NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 5;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial;NADH-ubiquinone oxidoreductase chain 1;NADH-ubiquinone oxidoreductase chain 2;NADH-ubiquinone oxidoreductase chain 3;NADH-ubiquinone oxidoreductase chain 4L;NADH-ubiquinone oxidoreductase chain 6;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial","subunits.Gene.name.":"NDUFA1;NDUFC1;NDUFS5;NDUFA3;NDUFA10;MT-ND1;MT-ND2;MT-ND3;MT-ND4L;MT-ND6;NDUFA8;NDUFA6;NDUFA9","subunits.Gene.name.syn.":"None;None;None;None;None;MTND1 NADH1 ND1;MTND2 NADH2 ND2;MTND3 NADH3 ND3;MTND4L NADH4L ND4L;MTND6 NADH6 ND6;None;LYRM6 NADHB14;NDUFS2L","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex I couples the transfer of two electrons from NADH to ubiquinone to the translocation of four protons across the mitochondrial inner membrane. Complex I  is an L-shaped molecule with one arm embedded in the mitochondrial inner membane and one arm protruding into the matrix, the peripheral arm. The assembly of complex I is a semi-sequential process in which different preassembled subcomplexes are joined to form the holoenzyme.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2920,"ComplexName":"Respiratory chain complex I (lambda subunit) mitochondrial","Organism":"Human","Synonyms":"NADH:ubiquinone oxidoreductase (EC 1.6.5.3) lambda subunit","Cell.line":"None","subunits.UniProt.IDs.":"O00217;O43181;O43678;O75251;O75306;O75380;O75489;O95182;P19404;P28331;P49821;P56181;Q16718;Q86Y39;Q9P0J0;Q9UI09","subunits.Entrez.IDs.":"4728;4724;4695;374291;4720;4726;4722;4701;4729;4719;4723;4731;4698;126328;51079;55967","Protein.complex.purification.method":"MI:0276- blue native page; MI:0063- prediction","GO.ID":"GO:0006091;GO:0009060;GO:0006461;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;protein complex assembly;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;14.10;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;assembly of protein complexes;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":15317750,"subunits.Protein.name.":"NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2;NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7;NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial;NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial;NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial;NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12","subunits.Gene.name.":"NDUFS8;NDUFS4;NDUFA2;NDUFS7;NDUFS2;NDUFS6;NDUFS3;NDUFA7;NDUFV2;NDUFS1;NDUFV1;NDUFV3;NDUFA5;NDUFA11;NDUFA13;NDUFA12","subunits.Gene.name.syn.":"None;None;None;None;None;None;None;None;None;None;UQOR1;None;None;None;GRIM19;DAP13","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex I couples the transfer of two electrons from NADH to ubiquinone to the translocation of four protons across the mitochondrial inner membrane. Complex I  is an L-shaped molecule with one arm embedded in the mitochondrial inner membane and one arm protruding into the matrix, the peripheral arm. The assembly of complex I is a semi-sequential process in which different preassembled subcomplexes are joined to form the holoenzyme.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2921,"ComplexName":"SHARP-CtBP complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P56545;Q13363;Q96T58","subunits.Entrez.IDs.":"1488;1487;23013","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045892;GO:0003677;GO:0007219;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;DNA binding;Notch signaling pathway;nucleus","FunCat.ID":"11.02.03.04.03;16.03.01;30.05.02.14;70.10","FunCat.description":"transcription repression;DNA binding;Notch-receptor signalling pathway;nucleus","PubMed.ID":16287852,"subunits.Protein.name.":"C-terminal-binding protein 2 ;C-terminal-binding protein 1;Msx2-interacting protein","subunits.Gene.name.":"CTBP2;CTBP1;SPEN","subunits.Gene.name.syn.":";CTBP;KIAA0929 MINT SHARP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"CtBP augments SHARP-mediated repression.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2922,"ComplexName":"LAT-PLC-gamma-1-p85-GRB2-SOS signaling complex, C305 activated","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43561;P19174;P27986;P62993;Q07889","subunits.Entrez.IDs.":"27040;5335;5295;2885;6654","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007169;GO:0050896;GO:0048015","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway;response to stimulus;phosphatidylinositol-mediated signaling","FunCat.ID":"30.05.01.12;36.25","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways;animal specific systemic sensing and response","PubMed.ID":9489702,"subunits.Protein.name.":"Linker for activation of T-cells family member 1;1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 ;Phosphatidylinositol 3-kinase regulatory subunit alpha;Growth factor receptor-bound protein 2;Son of sevenless homolog 1","subunits.Gene.name.":"LAT;PLCG1;PIK3R1;GRB2;SOS1","subunits.Gene.name.syn.":"None;PLC1;GRB1;ASH;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors show that upon tyrosine phosphorylation, LAT binds Grb2, PLC-gamma1, the p85 subunit of PI3K, and other critical signaling molecules. They provide evidence that LAT plays an important role in linking the TCR to cellular activation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2923,"ComplexName":"SHARP-CtBP1-CtIP complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q13363;Q96T58;Q99708","subunits.Entrez.IDs.":"1487;23013;5932","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045892;GO:0003677;GO:0007219;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;DNA binding;Notch signaling pathway;nucleus","FunCat.ID":"11.02.03.04.03;16.03.01;30.05.02.14;70.10","FunCat.description":"transcription repression;DNA binding;Notch-receptor signalling pathway;nucleus","PubMed.ID":16287852,"subunits.Protein.name.":"C-terminal-binding protein 1;Msx2-interacting protein ;DNA endonuclease RBBP8","subunits.Gene.name.":"CTBP1;SPEN;RBBP8","subunits.Gene.name.syn.":"CTBP;KIAA0929 MINT SHARP;CTIP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"CtIP and CtBP augment SHARP-mediated repression.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2924,"ComplexName":"Respiratory chain complex I (beta subunit) mitochondrial","Organism":"Bovine","Synonyms":"NADH:ubiquinone oxidoreductase (EC 1.6.5.3) beta subunit","Cell.line":"None","subunits.UniProt.IDs.":"P03910;P03920;P48305;P52505;Q01321;Q02365;Q02367;Q02368;Q02369;Q02372;Q02373;Q02374;Q02378;Q02380;Q02827;Q8HXG5","subunits.Entrez.IDs.":"3283886;None;None;327702;327704;338073;327665;338065;327660;282517;327701;327713;327690;338061;338046;404161","Protein.complex.purification.method":"MI:0276- blue native page; MI:0063- prediction","GO.ID":"GO:0006091;GO:0009060;GO:0006461;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;protein complex assembly;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;14.10;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;assembly of protein complexes;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":15317750,"subunits.Protein.name.":"NADH-ubiquinone oxidoreductase chain 4;NADH-ubiquinone oxidoreductase chain 5;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4;Acyl carrier protein, mitochondrial;Cytochrome c oxidase subunit NDUFA4;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial;NADH dehydrogenase [ubiquinone] 1 subunit C2;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial","subunits.Gene.name.":"MT-ND4;MT-ND5;NDUFB4;NDUFAB1;NDUFA4;NDUFB3;NDUFB6;NDUFB7;NDUFB9;NDUFB8;NDUFB10;NDUFB2;NDUFB1;NDUFB5;NDUFC2;NDUFB11","subunits.Gene.name.syn.":"MTND4 NADH4 ND4;MTND5 NADH5 ND5;None;None;None;None;None;None;UQOR22;None;None;None;None;None;None;None","Disease.comment":"None","Subunits.comment":"The authors found an additional 10.6K component that could not be identified.","Complex.comment":"Complex I couples the transfer of two electrons from NADH to ubiquinone to the translocation of four protons across the mitochondrial inner membrane. Complex I  is an L-shaped molecule with one arm embedded in the mitochondrial inner membane and one arm protruding into the matrix, the peripheral arm. The assembly of complex I is a semi-sequential process in which different preassembled subcomplexes are joined to form the holoenzyme.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":2925,"ComplexName":"Respiratory chain complex I (lambda subunit) mitochondrial","Organism":"Bovine","Synonyms":"NADH:ubiquinone oxidoreductase (EC 1.6.5.3) lambda subunit","Cell.line":"None","subunits.UniProt.IDs.":"O97725;P04394;P15690;P17694;P23709;P23934;P23935;P25708;P25712;P42026;P42028;Q02370;Q02375;Q05752;Q8HXG6;Q95KV7","subunits.Entrez.IDs.":"281742;None;288380;327697;287327;327691;327714;287014;327717;338079;287027;None;327680;338063;326346;338084","Protein.complex.purification.method":"MI:0276- blue native page; MI:0063- prediction","GO.ID":"GO:0006091;GO:0009060;GO:0006461;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;protein complex assembly;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;14.10;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;assembly of protein complexes;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":15317750,"subunits.Protein.name.":"NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12;NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial;NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5;NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial;NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2;NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13","subunits.Gene.name.":"NDUFA12;NDUFV2;NDUFS1;NDUFS2;NDUFS3;NDUFS6;NDUFA5;NDUFV1;NDUFV3;NDUFS7;NDUFS8;NDUFA2;NDUFS4;NDUFA7;NDUFA11;NDUFA13","subunits.Gene.name.syn.":"None;None;None;None;None;None;None;UQOR1;None;None;None;None;None;CI-B14-5A;None;GRIM19","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex I couples the transfer of two electrons from NADH to ubiquinone to the translocation of four protons across the mitochondrial inner membrane. Complex I  is an L-shaped molecule with one arm embedded in the mitochondrial inner membane and one arm protruding into the matrix, the peripheral arm. The assembly of complex I is a semi-sequential process in which different preassembled subcomplexes are joined to form the holoenzyme.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":2926,"ComplexName":"Respiratory chain complex I (gamma subunit) mitochondrial","Organism":"Bovine","Synonyms":"NADH:ubiquinone oxidoreductase (EC 1.6.5.3) gamma subunit","Cell.line":"None","subunits.UniProt.IDs.":"P03887;P03892;P03898;P03902;P03924;P34942;P34943;P42029;Q02366;Q02371;Q02376;Q02377;Q02379","subunits.Entrez.IDs.":"None;None;3283884;3283885;3283888;338060;404188;327710;327670;338064;282289;None;338057","Protein.complex.purification.method":"MI:0276- blue native page; MI:0063- prediction","GO.ID":"GO:0006091;GO:0009060;GO:0006461;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;protein complex assembly;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;14.10;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;assembly of protein complexes;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":15317750,"subunits.Protein.name.":"NADH-ubiquinone oxidoreductase chain 1;NADH-ubiquinone oxidoreductase chain 2;NADH-ubiquinone oxidoreductase chain 3;NADH-ubiquinone oxidoreductase chain 4L;NADH-ubiquinone oxidoreductase chain 6;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3;NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1;NADH dehydrogenase [ubiquinone] iron-sulfur protein 5","subunits.Gene.name.":"MT-ND1;MT-ND2;MT-ND3;MT-ND4L;MT-ND6;NDUFA10;NDUFA9;NDUFA8;NDUFA6;NDUFA3;NDUFC1;NDUFA1;NDUFS5","subunits.Gene.name.syn.":"MTND1 NADH1 ND1;MTND2 NADH2 ND2;MTND3 NADH3 ND3;MTND4L NADH4L ND4L;MTND6 NADH6 ND6;None;None;None;None;None;None;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex I couples the transfer of two electrons from NADH to ubiquinone to the translocation of four protons across the mitochondrial inner membrane. Complex I  is an L-shaped molecule with one arm embedded in the mitochondrial inner membane and one arm protruding into the matrix, the peripheral arm. The assembly of complex I is a semi-sequential process in which different preassembled subcomplexes are joined to form the holoenzyme.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":2927,"ComplexName":"Respiratory chain complex I (incomplete gamma subunit) mitochondrial","Organism":"Bovine","Synonyms":"NADH:ubiquinone oxidoreductase (EC 1.6.5.3) gamma subunit fragment","Cell.line":"None","subunits.UniProt.IDs.":"P03887;P03892;P03898;P03902;Q02376","subunits.Entrez.IDs.":"None;None;3283884;3283885;282289","Protein.complex.purification.method":"MI:0047- far western blotting; MI:0004- affinity chromatography technologies","GO.ID":"GO:0006091;GO:0009060;GO:0006461;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;protein complex assembly;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;14.10;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;assembly of protein complexes;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":10852722,"subunits.Protein.name.":"NADH-ubiquinone oxidoreductase chain 1;NADH-ubiquinone oxidoreductase chain 2;NADH-ubiquinone oxidoreductase chain 3;NADH-ubiquinone oxidoreductase chain 4L;NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial","subunits.Gene.name.":"MT-ND1;MT-ND2;MT-ND3;MT-ND4L;NDUFC1","subunits.Gene.name.syn.":"MTND1 NADH1 ND1;MTND2 NADH2 ND2;MTND3 NADH3 ND3;MTND4L NADH4L ND4L;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex I couples the transfer of two electrons from NADH to ubiquinone to the translocation of four protons across the mitochondrial inner membrane. Complex I  is an L-shaped molecule with one arm embedded in the mitochondrial inner membane and one arm protruding into the matrix, the peripheral arm. The assembly of complex I is a semi-sequential process in which different preassembled subcomplexes are joined to form the holoenzyme.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":2928,"ComplexName":"Respiratory chain complex I (lambda subunit) mitochondrial","Organism":"Bovine","Synonyms":"NADH:ubiquinone oxidoreductase (EC 1.6.5.3) lambda subunit","Cell.line":"None","subunits.UniProt.IDs.":"P04394;P15690;P17694;P23709;P23934;P23935;P25708;P25712;P42026;P42028;P48305;Q02366;Q02370;Q02375;Q05752","subunits.Entrez.IDs.":"None;288380;327697;287327;327691;327714;287014;327717;338079;287027;None;327670;None;327680;338063","Protein.complex.purification.method":"MI:0047- far western blotting; MI:0004- affinity chromatography technologies","GO.ID":"GO:0006091;GO:0009060;GO:0006461;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;protein complex assembly;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;14.10;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;assembly of protein complexes;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":10852722,"subunits.Protein.name.":"NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial;NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5;NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial;NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2;NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7","subunits.Gene.name.":"NDUFV2;NDUFS1;NDUFS2;NDUFS3;NDUFS6;NDUFA5;NDUFV1;NDUFV3;NDUFS7;NDUFS8;NDUFB4;NDUFA6;NDUFA2;NDUFS4;NDUFA7","subunits.Gene.name.syn.":"None;None;None;None;None;None;UQOR1;None;None;None;None;None;None;None;CI-B14-5A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex I couples the transfer of two electrons from NADH to ubiquinone to the translocation of four protons across the mitochondrial inner membrane. Complex I  is an L-shaped molecule with one arm embedded in the mitochondrial inner membane and one arm protruding into the matrix, the peripheral arm. The assembly of complex I is a semi-sequential process in which different preassembled subcomplexes are joined to form the holoenzyme.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":2929,"ComplexName":"Respiratory chain complex I (beta subunit) mitochondrial","Organism":"Bovine","Synonyms":"NADH:ubiquinone oxidoreductase (EC 1.6.5.3) beta subunit","Cell.line":"None","subunits.UniProt.IDs.":"P03910;P03920;P48305;P52505;Q02367;Q02368;Q02369;Q02372;Q02373;Q02374;Q02378;Q02380","subunits.Entrez.IDs.":"3283886;None;None;327702;327665;338065;327660;282517;327701;327713;327690;338061","Protein.complex.purification.method":"MI:0047- far western blotting; MI:0004- affinity chromatography technologies","GO.ID":"GO:0006091;GO:0009060;GO:0006461;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;protein complex assembly;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;14.10;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;assembly of protein complexes;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":10852722,"subunits.Protein.name.":"NADH-ubiquinone oxidoreductase chain 4;NADH-ubiquinone oxidoreductase chain 5;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4;Acyl carrier protein, mitochondrial;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial","subunits.Gene.name.":"MT-ND4;MT-ND5;NDUFB4;NDUFAB1;NDUFB6;NDUFB7;NDUFB9;NDUFB8;NDUFB10;NDUFB2;NDUFB1;NDUFB5","subunits.Gene.name.syn.":"MTND4 NADH4 ND4;MTND5 NADH5 ND5;None;None;None;None;UQOR22;None;None;None;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex I couples the transfer of two electrons from NADH to ubiquinone to the translocation of four protons across the mitochondrial inner membrane. Complex I  is an L-shaped molecule with one arm embedded in the mitochondrial inner membane and one arm protruding into the matrix, the peripheral arm. The assembly of complex I is a semi-sequential process in which different preassembled subcomplexes are joined to form the holoenzyme.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":2930,"ComplexName":"SHARP-CtIP-RBP-Jkappa complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q06330;Q96T58;Q99708","subunits.Entrez.IDs.":"3516;23013;5932","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045892;GO:0003677;GO:0007219;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;DNA binding;Notch signaling pathway;nucleus","FunCat.ID":"11.02.03.04.03;16.03.01;30.05.02.14;70.10","FunCat.description":"transcription repression;DNA binding;Notch-receptor signalling pathway;nucleus","PubMed.ID":16287852,"subunits.Protein.name.":"Recombining binding protein suppressor of hairless ;Msx2-interacting protein ;DNA endonuclease RBBP8","subunits.Gene.name.":"RBPJ;SPEN;RBBP8","subunits.Gene.name.syn.":"IGKJRB IGKJRB1 RBPJK RBPSUH;KIAA0929 MINT SHARP;CTIP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The ternary complex is formed only when both SHARP and CtIP are expressed.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2931,"ComplexName":"SHARP-CtBP1-CtIP-RBP-Jkappa corepressor complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q06330;Q13363;Q96T58;Q99708","subunits.Entrez.IDs.":"3516;1487;23013;5932","Protein.complex.purification.method":"MI:0232- transcriptional complementation assay; MI:0004- affinity chromatography technologies","GO.ID":"GO:0045892;GO:0003677;GO:0007219;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;DNA binding;Notch signaling pathway;nucleus","FunCat.ID":"11.02.03.04.03;16.03.01;30.05.02.14;70.10","FunCat.description":"transcription repression;DNA binding;Notch-receptor signalling pathway;nucleus","PubMed.ID":16287852,"subunits.Protein.name.":"Recombining binding protein suppressor of hairless ;C-terminal-binding protein 1;Msx2-interacting protein ;DNA endonuclease RBBP8","subunits.Gene.name.":"RBPJ;CTBP1;SPEN;RBBP8","subunits.Gene.name.syn.":"IGKJRB IGKJRB1 RBPJK RBPSUH;CTBP;KIAA0929 MINT SHARP;CTIP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The corepressor complex containing CtIP/CtBP probably facilitates RBP-Jkappa/SHARP-mediated repression of Notch target genes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2932,"ComplexName":"PTF1-L complex (Ptf1a, Tcf12, Rbpjl)","Organism":"Rat","Synonyms":"None","Cell.line":"pancreas","subunits.UniProt.IDs.":"O08674;P51514;Q64305","subunits.Entrez.IDs.":"19668;25720;117034","Protein.complex.purification.method":"MI:0412-electrophoretic mobility supershift assay","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0010074;GO:0031016;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;maintenance of meristem identity;pancreas development;nucleus","FunCat.ID":"11.02.03.04;16.03.01;41.05.04;47.03.11.09;70.10","FunCat.description":"transcriptional control;DNA binding;embryogenesis;pancreas;nucleus","PubMed.ID":16354684,"subunits.Protein.name.":"Recombining binding protein suppressor of hairless-like protein;Transcription factor 12;Pancreas transcription factor 1 subunit alpha","subunits.Gene.name.":"Rbpjl;Tcf12;Ptf1a","subunits.Gene.name.syn.":"Rbpl Rbpsuhl;None;Ptf1p48","Disease.comment":"Mutations in Ptf1a are associated with pancreatic and cerebellar agenesis.","Subunits.comment":"Since Rbpjl from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"Transcriptional activity of PTF1 complex is independent of Notch signaling, because Ptf1a occupies the NotchIC docking site on Rbpj and Rbpl.","SWISSPROT.organism":"Mus musculus (Mouse);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2933,"ComplexName":"PTF1-L complex (Ptf1a, Tcf4, Rbpjl)","Organism":"Rat","Synonyms":"None","Cell.line":"pancreas","subunits.UniProt.IDs.":"O08674;Q62655;Q64305","subunits.Entrez.IDs.":"19668;84382;117034","Protein.complex.purification.method":"MI:0412-electrophoretic mobility supershift assay","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0010074;GO:0031016;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;maintenance of meristem identity;pancreas development;nucleus","FunCat.ID":"11.02.03.04;16.03.01;41.05.04;47.03.11.09;70.10","FunCat.description":"transcriptional control;DNA binding;embryogenesis;pancreas;nucleus","PubMed.ID":16354684,"subunits.Protein.name.":"Recombining binding protein suppressor of hairless-like protein;Transcription factor 4;Pancreas transcription factor 1 subunit alpha","subunits.Gene.name.":"Rbpjl;Tcf4;Ptf1a","subunits.Gene.name.syn.":"Rbpl Rbpsuhl;Itf2 Sef2;Ptf1p48","Disease.comment":"Mutations in Ptf1a are associated with pancreatic and cerebellar agenesis.","Subunits.comment":"Since Rbpjl from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"Transcriptional activity of PTF1 complex is independent of Notch signaling, because Ptf1a occupies the NotchIC docking site on Rbpj and Rbpl.","SWISSPROT.organism":"Mus musculus (Mouse);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2934,"ComplexName":"PTF1-L complex (Ptf1a, Tcf3, Rbpjl)","Organism":"Rat","Synonyms":"None","Cell.line":"pancreas","subunits.UniProt.IDs.":"O08674;P21677;Q64305","subunits.Entrez.IDs.":"19668;171046;117034","Protein.complex.purification.method":"MI:0412-electrophoretic mobility supershift assay","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0010074;GO:0031016;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;maintenance of meristem identity;pancreas development;nucleus","FunCat.ID":"11.02.03.04;16.03.01;41.05.04;47.03.11.09;70.10","FunCat.description":"transcriptional control;DNA binding;embryogenesis;pancreas;nucleus","PubMed.ID":16354684,"subunits.Protein.name.":"Recombining binding protein suppressor of hairless-like protein;Transcription factor E2-alpha;Pancreas transcription factor 1 subunit alpha","subunits.Gene.name.":"Rbpjl;Tcf3;Ptf1a","subunits.Gene.name.syn.":"Rbpl Rbpsuhl;Pan Ptf1c Tcfe2a;Ptf1p48","Disease.comment":"Mutations in Ptf1a are associated with pancreatic and cerebellar agenesis.","Subunits.comment":"Since Rbpjl from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"Transcriptional activity of PTF1 complex is independent of Notch signaling, because Ptf1a occupies the NotchIC docking site on Rbpj and Rbpl.","SWISSPROT.organism":"Mus musculus (Mouse);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2935,"ComplexName":"PTF1 complex (Ptf1a, Tcf12, Rbpj)","Organism":"Rat","Synonyms":"None","Cell.line":"pancreas","subunits.UniProt.IDs.":"P31266;P51514;Q64305","subunits.Entrez.IDs.":"19664;25720;117034","Protein.complex.purification.method":"MI:0402-chromatin immunoprecipitation assays","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0010074;GO:0022008;GO:0048699;GO:0031016;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;maintenance of meristem identity;neurogenesis;generation of neurons;pancreas development;nucleus","FunCat.ID":"11.02.03.04;16.03.01;41.05.04;41.05.13;47.03.11.09;70.10","FunCat.description":"transcriptional control;DNA binding;embryogenesis;neurogenesis;pancreas;nucleus","PubMed.ID":16354684,"subunits.Protein.name.":"Recombining binding protein suppressor of hairless;Transcription factor 12;Pancreas transcription factor 1 subunit alpha","subunits.Gene.name.":"Rbpj;Tcf12;Ptf1a","subunits.Gene.name.syn.":"Igkjrb1 Igkrsbp Rbpsuh;None;Ptf1p48","Disease.comment":"Mutations in Ptf1a are associated with pancreatic and cerebellar agenesis.","Subunits.comment":"Since Rbpj from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"Transcriptional activity of PTF1 complex is independent of Notch signaling, because Ptf1a occupies the NotchIC docking site on Rbpj and Rbpl.","SWISSPROT.organism":"Mus musculus (Mouse);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2936,"ComplexName":"Ecsit complex (ECSIT, MT-CO2, GAPDH, TRAF6, NDUFAF1)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P00403;P04406;Q9BQ95;Q9Y375;Q9Y4K3","subunits.Entrez.IDs.":"4513;2597;51295;51103;7189","Protein.complex.purification.method":"MI:0047-far western blotting","GO.ID":"GO:0006461;GO:0005739","GO.description":"protein complex assembly;mitochondrion","FunCat.ID":"14.10;70.16","FunCat.description":"assembly of protein complexes;mitochondrion","PubMed.ID":17344420,"subunits.Protein.name.":"Cytochrome c oxidase subunit 2;Glyceraldehyde-3-phosphate dehydrogenase;Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial;Complex I intermediate-associated protein 30, mitochondrial;TNF receptor-associated factor 6","subunits.Gene.name.":"MT-CO2;GAPDH;ECSIT;NDUFAF1;TRAF6","subunits.Gene.name.syn.":"COII COXII MTCO2;GAPD;None;CIA30;RNF85","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ecsit is a cytosolic adaptor protein essential for inflammatory response and embryonic development via the Toll-like and BMP (bone morphogenetic protein) signal transduction pathways, respectively. Here, a mitochondrial function for Ecsit (an evolutionary conserved signaling intermediate in Toll pathways) in the assembly of mitochondrial complex I (NADH:ubiquinone oxidoreductase) has also been demonstrated. Ecsit isoform 1 copurifies with tandem affinity-purified NDUFAF1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2937,"ComplexName":"PTF1-bHLH complex","Organism":"Human","Synonyms":"None","Cell.line":"pancreas","subunits.UniProt.IDs.":"Q7RTS3;Q99081","subunits.Entrez.IDs.":"256297;6938","Protein.complex.purification.method":"MI:0412-electrophoretic mobility supershift assay","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0010074;GO:0031016;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;maintenance of meristem identity;pancreas development;nucleus","FunCat.ID":"11.02.03.04;16.03.01;41.05.04;47.03.11.09;70.10","FunCat.description":"transcriptional control;DNA binding;embryogenesis;pancreas;nucleus","PubMed.ID":11562365,"subunits.Protein.name.":"Pancreas transcription factor 1 subunit alpha;Transcription factor 12","subunits.Gene.name.":"PTF1A;TCF12","subunits.Gene.name.syn.":"BHLHA29 PTF1P48;BHLHB20 HEB HTF4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"PTF1, containing P48 and a form of HEB, can bind to and mediate the acinar activity of the A element of the ELA1 gene enhancer.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2938,"ComplexName":"Ecsit complex (ECSIT, NDUFS3, TOM20)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75489;Q15388;Q9BQ95","subunits.Entrez.IDs.":"4722;9804;51295","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006461;GO:0005739","GO.description":"protein complex assembly;mitochondrion","FunCat.ID":"14.10;70.16","FunCat.description":"assembly of protein complexes;mitochondrion","PubMed.ID":17344420,"subunits.Protein.name.":"NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial;Mitochondrial import receptor subunit TOM20 homolog;Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial","subunits.Gene.name.":"NDUFS3;TOMM20;ECSIT","subunits.Gene.name.syn.":"None;KIAA0016;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ecsit is a cytosolic adaptor protein essential for inflammatory response and embryonic development via the Toll-like and BMP (bone morphogenetic protein) signal transduction pathways, respectively. Here, a mitochondrial function for Ecsit (an evolutionary conserved signaling intermediate in Toll pathways) in the assembly of mitochondrial complex I (NADH:ubiquinone oxidoreductase) has also been demonstrated. Ecsit isoform 1 copurifies with tandem affinity-purified NDUFAF1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2939,"ComplexName":"Ecsit complex (ECSIT, MT-CO2, NDUFA1, MT-ND1, TRAF6, NDUFAF1)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15239;P00403;P03886;Q9BQ95;Q9Y375;Q9Y4K3","subunits.Entrez.IDs.":"4694;4513;4535;51295;51103;7189","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006461;GO:0005739","GO.description":"protein complex assembly;mitochondrion","FunCat.ID":"14.10;70.16","FunCat.description":"assembly of protein complexes;mitochondrion","PubMed.ID":17344420,"subunits.Protein.name.":"NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1;Cytochrome c oxidase subunit 2;NADH-ubiquinone oxidoreductase chain 1;Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial;Complex I intermediate-associated protein 30, mitochondrial;TNF receptor-associated factor 6","subunits.Gene.name.":"NDUFA1;MT-CO2;MT-ND1;ECSIT;NDUFAF1;TRAF6","subunits.Gene.name.syn.":"None;COII COXII MTCO2;MTND1 NADH1 ND1;None;CIA30;RNF85","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ecsit is a cytosolic adaptor protein essential for inflammatory response and embryonic development via the Toll-like and BMP (bone morphogenetic protein) signal transduction pathways, respectively. Here, a mitochondrial function for Ecsit (an evolutionary conserved signaling intermediate in Toll pathways) in the assembly of mitochondrial complex I (NADH:ubiquinone oxidoreductase) has also been demonstrated. Ecsit isoform 1 copurifies with tandem affinity-purified NDUFAF1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2940,"ComplexName":"Acinar cell-specific C complex","Organism":"Mouse","Synonyms":"PDX1-PBX1b-MEIS2 complex","Cell.line":"pancreas","subunits.UniProt.IDs.":"P41778;P52946;P97367","subunits.Entrez.IDs.":"18514;18609;17536","Protein.complex.purification.method":"MI:0412-electrophoretic mobility supershift assay","GO.ID":"GO:0045893;GO:0010074;GO:0031016;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;maintenance of meristem identity;pancreas development;nucleus","FunCat.ID":"11.02.03.04.01;41.05.04;47.03.11.09;70.10","FunCat.description":"transcription activation;embryogenesis;pancreas;nucleus","PubMed.ID":9710595,"subunits.Protein.name.":"Pre-B-cell leukemia transcription factor 1;Pancreas/duodenum homeobox protein 1;Homeobox protein Meis2","subunits.Gene.name.":"Pbx1;Pdx1;Meis2","subunits.Gene.name.syn.":"Pbx-1;Ipf1;Mrg1 Stra10","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The association with PBX and MEIS partners controls the nature of the transcriptional activity of the organ-specific PDX1 transcription factor in exocrine versus endocrine cells.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2941,"ComplexName":"Acinar cell-specific C complex","Organism":"Mouse","Synonyms":"PDX1-PBX1b-MEIS2 complex","Cell.line":"pancreas","subunits.UniProt.IDs.":"P41778;P52946;P97367","subunits.Entrez.IDs.":"18514;18609;17536","Protein.complex.purification.method":"MI:0412-electrophoretic mobility supershift assay","GO.ID":"GO:0045893;GO:0010074;GO:0031016;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;maintenance of meristem identity;pancreas development;nucleus","FunCat.ID":"11.02.03.04.01;41.05.04;47.03.11.09;70.10","FunCat.description":"transcription activation;embryogenesis;pancreas;nucleus","PubMed.ID":11279116,"subunits.Protein.name.":"Pre-B-cell leukemia transcription factor 1;Pancreas/duodenum homeobox protein 1;Homeobox protein Meis2","subunits.Gene.name.":"Pbx1;Pdx1;Meis2","subunits.Gene.name.syn.":"Pbx-1;Ipf1;Mrg1 Stra10","Disease.comment":"None","Subunits.comment":"MEIS2b isoform and possibly also MEIS2d isoform are present in the complex, but MEIS2a and MEIS2c isoforms are not.","Complex.comment":"This complex cooperates with PTF1-bHLH complex to activate transcription in pancreatic acinar cells.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2942,"ComplexName":"Ecsit complex (ECSIT, NDUFS3, NDUFAF1)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75489;Q9BQ95;Q9Y375","subunits.Entrez.IDs.":"4722;51295;51103","Protein.complex.purification.method":"MI:0047-far western blotting","GO.ID":"GO:0006461;GO:0005739","GO.description":"protein complex assembly;mitochondrion","FunCat.ID":"14.10;70.16","FunCat.description":"assembly of protein complexes;mitochondrion","PubMed.ID":17344420,"subunits.Protein.name.":"NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial;Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial;Complex I intermediate-associated protein 30, mitochondrial","subunits.Gene.name.":"NDUFS3;ECSIT;NDUFAF1","subunits.Gene.name.syn.":"None;None;CIA30","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ecsit is a cytosolic adaptor protein essential for inflammatory response and embryonic development via the Toll-like and BMP (bone morphogenetic protein) signal transduction pathways, respectively. Here, a mitochondrial function for Ecsit (an evolutionary conserved signaling intermediate in Toll pathways) in the assembly of mitochondrial complex I (NADH:ubiquinone oxidoreductase) has also been demonstrated. Ecsit isoform 1 copurifies with tandem affinity-purified NDUFAF1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2943,"ComplexName":"Respiratory chain complex I (incomplete NDUFAF1 assembly), mitochondrial","Organism":"Human","Synonyms":"NADH:ubiquinone oxidoreductase (EC 1.6.5.3) incomplete intermediate","Cell.line":"None","subunits.UniProt.IDs.":"P03886;Q9Y375","subunits.Entrez.IDs.":"4535;51103","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0047- far western blotting","GO.ID":"GO:0006091;GO:0009060;GO:0006461;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;protein complex assembly;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;14.10;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;assembly of protein complexes;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":16218961,"subunits.Protein.name.":"NADH-ubiquinone oxidoreductase chain 1;Complex I intermediate-associated protein 30, mitochondrial","subunits.Gene.name.":"MT-ND1;NDUFAF1","subunits.Gene.name.syn.":"MTND1 NADH1 ND1;CIA30","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone. NDUFAF1 is a crucial component in the early assembly/stability of complex I.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2944,"ComplexName":"Notch1-p56lck-PI3K complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06239;P27986;P46531","subunits.Entrez.IDs.":"3932;5295;4851","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045893;GO:0007219;GO:0043066;GO:0030217","GO.description":"positive regulation of transcription, DNA-templated;Notch signaling pathway;negative regulation of apoptotic process;T cell differentiation","FunCat.ID":"11.02.03.04.01;30.05.02.14;40.10.02.01;43.03.07.02.01.02","FunCat.description":"transcription activation;Notch-receptor signalling pathway;anti-apoptosis;T-cell","PubMed.ID":14583609,"subunits.Protein.name.":"Tyrosine-protein kinase Lck;Phosphatidylinositol 3-kinase regulatory subunit alpha;Neurogenic locus notch homolog protein 1","subunits.Gene.name.":"LCK;PIK3R1;NOTCH1","subunits.Gene.name.syn.":"None;GRB1;TAN1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Anti-apoptotic function may result from elevated expression of anti-apoptotic genes like IAP-2, Bcl-xl or FLIP.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2945,"ComplexName":"RBP-Jkappa-RING1-KyoT2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q06330;Q06587;Q13642","subunits.Entrez.IDs.":"3516;6015;2273","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045892;GO:0003677;GO:0051098;GO:0005515;GO:0051090;GO:0007219;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;DNA binding;regulation of binding;protein binding;regulation of sequence-specific DNA binding transcription factor activity;Notch signaling pathway;nucleus","FunCat.ID":"11.02.03.04.03;16.03.01;18.01.07;16.01;18.02.09;30.05.02.14;70.10","FunCat.description":"transcription repression;DNA binding;regulation by binding / dissociation;protein binding;regulator of transcription factor;Notch-receptor signalling pathway;nucleus","PubMed.ID":14999091,"subunits.Protein.name.":"Recombining binding protein suppressor of hairless ;E3 ubiquitin-protein ligase RING1;Four and a half LIM domains protein 1","subunits.Gene.name.":"RBPJ;RING1;FHL1","subunits.Gene.name.syn.":"IGKJRB IGKJRB1 RBPJK RBPSUH;RNF1;SLIM1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Overexpression of RING1 And KyoT2 inhibits transactivation of RBP-Jkappa by Notch.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2946,"ComplexName":"YY1-Notch1-RBP-Jkappa complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P25490;P46531;Q06330","subunits.Entrez.IDs.":"7528;4851;3516","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0006- anti bait coimmunoprecipitation; MI:0402- chromatin immunoprecipitation assays","GO.ID":"GO:0045893;GO:0003677;GO:0007219;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;Notch signaling pathway;nucleus","FunCat.ID":"11.02.03.04.01;16.03.01;30.05.02.14;70.10","FunCat.description":"transcription activation;DNA binding;Notch-receptor signalling pathway;nucleus","PubMed.ID":12913000,"subunits.Protein.name.":"Transcriptional repressor protein YY1;Neurogenic locus notch homolog protein 1 ;Recombining binding protein suppressor of hairless","subunits.Gene.name.":"YY1;NOTCH1;RBPJ","subunits.Gene.name.syn.":"INO80S;TAN1;IGKJRB IGKJRB1 RBPJK RBPSUH","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"YY1 indirectly binds to CBF1-response element via association with the intracellular domain of Notch1 (N1IC). N1IC interacts directly with CBF1(RBP-Jkappa).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2947,"ComplexName":"YY1-Notch1 complex","Organism":"Human","Synonyms":"None","Cell.line":"K562 cells","subunits.UniProt.IDs.":"P25490;P46531","subunits.Entrez.IDs.":"7528;4851","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0006- anti bait coimmunoprecipitation; MI:0402- chromatin immunoprecipitation assays","GO.ID":"GO:0003677;GO:0007219;GO:0005634","GO.description":"DNA binding;Notch signaling pathway;nucleus","FunCat.ID":"16.03.01;30.05.02.14;70.10","FunCat.description":"DNA binding;Notch-receptor signalling pathway;nucleus","PubMed.ID":12913000,"subunits.Protein.name.":"Transcriptional repressor protein YY1;Neurogenic locus notch homolog protein 1","subunits.Gene.name.":"YY1;NOTCH1","subunits.Gene.name.syn.":"INO80S;TAN1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Transcription factor Ying Yang 1 (YY1) is associated with exogenous N1IC in human K562 erythroleukemic cells. The ankyrin (ANK) domain of N1IC and zinc finger domains of YY1 are essential for the association of N1IC and YY1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2948,"ComplexName":"Respiratory chain complex I (incomplete intermediate), mitochondrial","Organism":"Human","Synonyms":"NADH:ubiquinone oxidoreductase (EC 1.6.5.3) incomplete intermediate","Cell.line":"None","subunits.UniProt.IDs.":"O43181;O75251;O75306;O75380;O95169;O95299;P19404;P28331;P49821;P56181;Q16795","subunits.Entrez.IDs.":"4724;374291;4720;4726;4714;4705;4729;4719;4723;4731;4704","Protein.complex.purification.method":"MI:0276- blue native page; MI:0047- far western blotting","GO.ID":"GO:0006091;GO:0009060;GO:0006461;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;protein complex assembly;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;14.10;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;assembly of protein complexes;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":17438127,"subunits.Protein.name.":"NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial;NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial;NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial;NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial;NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial","subunits.Gene.name.":"NDUFS4;NDUFS7;NDUFS2;NDUFS6;NDUFB8;NDUFA10;NDUFV2;NDUFS1;NDUFV1;NDUFV3;NDUFA9","subunits.Gene.name.syn.":"None;None;None;None;None;None;None;None;UQOR1;None;NDUFS2L","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2949,"ComplexName":"MAML1-RBP-Jkappa-Notch1 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"P31266;Q01705;Q6T264","subunits.Entrez.IDs.":"19664;18128;103806","Protein.complex.purification.method":"MI:0428- imaging techniques; MI:0412- electrophoretic mobility supershift assay; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045893;GO:0003677;GO:0007219;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;Notch signaling pathway;nucleus","FunCat.ID":"11.02.03.04.01;16.03.01;30.05.02.14;70.10","FunCat.description":"transcription activation;DNA binding;Notch-receptor signalling pathway;nucleus","PubMed.ID":11101851,"subunits.Protein.name.":"Recombining binding protein suppressor of hairless;Neurogenic locus notch homolog protein 1;Mastermind-like protein 1","subunits.Gene.name.":"Rbpj;Notch1;Maml1","subunits.Gene.name.syn.":"Igkjrb1 Igkrsbp Rbpsuh;Motch;Kiaa0200","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Binding of Notch 1 to MAML1 is enhanced in the presence of RBP-Jkappa. MAML1 stabilizes the association of Notch1 with RBP-Jkappa.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2950,"ComplexName":"MAML1-RBP-Jkappa-Notch2 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"O35516;P31266;Q6T264","subunits.Entrez.IDs.":"18129;19664;103806","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045893;GO:0003677;GO:0007219;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;Notch signaling pathway;nucleus","FunCat.ID":"11.02.03.04.01;16.03.01;30.05.02.14;70.10","FunCat.description":"transcription activation;DNA binding;Notch-receptor signalling pathway;nucleus","PubMed.ID":11101851,"subunits.Protein.name.":"Neurogenic locus notch homolog protein 2 ;Recombining binding protein suppressor of hairless;Mastermind-like protein 1","subunits.Gene.name.":"Notch2;Rbpj;Maml1","subunits.Gene.name.syn.":";Igkjrb1 Igkrsbp Rbpsuh;Kiaa0200","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"MAML1 binds to the ankyrin repeat domain of all four mammalian NOTCH receptors, forms a DNA-binding complex with intracellular domain of Notch and RBP-Jkappa, and amplifies NOTCH-induced transcription of HES1.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2951,"ComplexName":"MAML1-RBP-Jkappa-Notch3 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"P31266;Q61982;Q6T264","subunits.Entrez.IDs.":"19664;18131;103806","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045893;GO:0003677;GO:0007219;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;Notch signaling pathway;nucleus","FunCat.ID":"11.02.03.04.01;16.03.01;30.05.02.14;70.10","FunCat.description":"transcription activation;DNA binding;Notch-receptor signalling pathway;nucleus","PubMed.ID":11101851,"subunits.Protein.name.":"Recombining binding protein suppressor of hairless;Neurogenic locus notch homolog protein 3 ;Mastermind-like protein 1","subunits.Gene.name.":"Rbpj;Notch3;Maml1","subunits.Gene.name.syn.":"Igkjrb1 Igkrsbp Rbpsuh;;Kiaa0200","Disease.comment":"Notch3 is involved in lung cancer (PMID:17804716)","Subunits.comment":"None","Complex.comment":"MAML1 binds to the ankyrin repeat domain of all four mammalian NOTCH receptors, forms a DNA-binding complex with intracellular domain of Notch and RBP-Jkappa, and amplifies NOTCH-induced transcription of HES1.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2952,"ComplexName":"MAML1-RBP-Jkappa-Notch4 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"P31266;P31695;Q6T264","subunits.Entrez.IDs.":"19664;18132;103806","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045893;GO:0003677;GO:0007219;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;Notch signaling pathway;nucleus","FunCat.ID":"11.02.03.04.01;16.03.01;30.05.02.14;70.10","FunCat.description":"transcription activation;DNA binding;Notch-receptor signalling pathway;nucleus","PubMed.ID":11101851,"subunits.Protein.name.":"Recombining binding protein suppressor of hairless;Neurogenic locus notch homolog protein 4 ;Mastermind-like protein 1","subunits.Gene.name.":"Rbpj;Notch4;Maml1","subunits.Gene.name.syn.":"Igkjrb1 Igkrsbp Rbpsuh;Int-3 Int3;Kiaa0200","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"MAML1 binds to the ankyrin repeat domain of all four mammalian NOTCH receptors, forms a DNA-binding complex with intracellular domain of Notch and RBP-Jkappa, and amplifies NOTCH-induced transcription of HES1.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2953,"ComplexName":"Respiratory chain complex I (nuclear encoded subunits), mitochondrial","Organism":"Bovine","Synonyms":"NADH:ubiquinone oxidoreductase (EC 1.6.5.3) nuclear encoded subunits;","Cell.line":"heart muscle","subunits.UniProt.IDs.":"O97725;P04394;P15690;P17694;P23709;P23934;P23935;P25708;P25712;P34942;P34943;P42026;P42028;P42029;P48305;P52505;Q01321;Q02365;Q02366;Q02367;Q02368;Q02369;Q02370;Q02371;Q02372;Q02373;Q02374;Q02375;Q02376;Q02377;Q02378;Q02379;Q02380;Q02827;Q05752;Q8HXG5;Q8HXG6;Q95KV7","subunits.Entrez.IDs.":"281742;None;288380;327697;287327;327691;327714;287014;327717;338060;404188;338079;287027;327710;None;327702;327704;338073;327670;327665;338065;327660;None;338064;282517;327701;327713;327680;282289;None;327690;338057;338061;338046;338063;404161;326346;338084","Protein.complex.purification.method":"MI:0047-far western blotting","GO.ID":"GO:0006091;GO:0009060;GO:0006818;GO:0022904;GO:0005743","GO.description":"generation of precursor metabolites and energy;aerobic respiration;hydrogen transport;respiratory electron transport chain;mitochondrial inner membrane","FunCat.ID":"01;02.13.03;20.01.15;02.11.07;70.16.05","FunCat.description":"METABOLISM;aerobic respiration;electron transport;regulation of electron transport and membrane-associated energy conservation;mitochondrial inner membrane","PubMed.ID":12837546,"subunits.Protein.name.":"NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12;NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial;NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5;NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial;NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4;Acyl carrier protein, mitochondrial;Cytochrome c oxidase subunit NDUFA4;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial;NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial;NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1;NADH dehydrogenase [ubiquinone] iron-sulfur protein 5;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial;NADH dehydrogenase [ubiquinone] 1 subunit C2;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7;NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11;NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13","subunits.Gene.name.":"NDUFA12;NDUFV2;NDUFS1;NDUFS2;NDUFS3;NDUFS6;NDUFA5;NDUFV1;NDUFV3;NDUFA10;NDUFA9;NDUFS7;NDUFS8;NDUFA8;NDUFB4;NDUFAB1;NDUFA4;NDUFB3;NDUFA6;NDUFB6;NDUFB7;NDUFB9;NDUFA2;NDUFA3;NDUFB8;NDUFB10;NDUFB2;NDUFS4;NDUFC1;NDUFA1;NDUFB1;NDUFS5;NDUFB5;NDUFC2;NDUFA7;NDUFB11;NDUFA11;NDUFA13","subunits.Gene.name.syn.":"None;None;None;None;None;None;None;UQOR1;None;None;None;None;None;None;None;None;None;None;None;None;None;UQOR22;None;None;None;None;None;None;None;None;None;None;None;None;CI-B14-5A;None;None;GRIM19","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex I is the first multiprotein complex of the OXPHOS system and participates in the formation of a proton gradient across the inner mitochondrial membrane coupled to transfer of electrons from NADH to ubiquinone.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":2954,"ComplexName":"Smad1-Notch1-p300-Pcaf complex","Organism":"Mouse","Synonyms":"None","Cell.line":"nervous tissue","subunits.UniProt.IDs.":"P70340;Q01705;Q09472;Q92831","subunits.Entrez.IDs.":"17125;18128;2033;8850","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0045893;GO:0006473;GO:0006476;GO:0003677;GO:0051098;GO:0005515;GO:0051090;GO:0007219;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;DNA binding;regulation of binding;protein binding;regulation of sequence-specific DNA binding transcription factor activity;Notch signaling pathway;nucleus","FunCat.ID":"11.02.03.04.01;14.07.04;16.03.01;18.01.07;16.01;18.02.09;30.05.02.14;70.10","FunCat.description":"transcription activation;modification by acetylation, deacetylation;DNA binding;regulation by binding / dissociation;protein binding;regulator of transcription factor;Notch-receptor signalling pathway;nucleus","PubMed.ID":14500836,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 1;Neurogenic locus notch homolog protein 1;Histone acetyltransferase p300;Histone acetyltransferase KAT2B","subunits.Gene.name.":"Smad1;Notch1;EP300;KAT2B","subunits.Gene.name.syn.":"Madh1 Madr1;Motch;P300;PCAF","Disease.comment":"None","Subunits.comment":"Since p300 and P/CAF from mouse were not available in the UniProt database at the time of annotation, the orthologous human proteins were used.","Complex.comment":"Interaction of SMAD1 and Notch1 was enhanced in the presence of p300 and PCAF.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2955,"ComplexName":"LCK-SLP76-PLC-gamma-1-LAT complex, pervanadate-activated","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43561;P06239;P19174;Q13094","subunits.Entrez.IDs.":"27040;3932;5335;3937","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007169;GO:0050896","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway;response to stimulus","FunCat.ID":"30.05.01.12;36.25","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways;animal specific systemic sensing and response","PubMed.ID":16938345,"subunits.Protein.name.":"Linker for activation of T-cells family member 1;Tyrosine-protein kinase Lck;1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 ;Lymphocyte cytosolic protein 2","subunits.Gene.name.":"LAT;LCK;PLCG1;LCP2","subunits.Gene.name.syn.":"None;None;PLC1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors show that in pervanadate-treated Jurkat cells, but not in J.CaM1.6 cells, three tyrosine-phosphorylated proteins with molecular weights about 59, 76 and 150 Kd, corresponding to Lck, SLP76, PLC-gamma-1 were co-precipitated with LAT.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2956,"ComplexName":"PLC-gamma-1-LAT-c-CBL complex, OKT3 stimulated","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43561;P19174;P22681","subunits.Entrez.IDs.":"27040;5335;867","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007169;GO:0050896","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway;response to stimulus","FunCat.ID":"30.05.01.12;36.25","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways;animal specific systemic sensing and response","PubMed.ID":16938345,"subunits.Protein.name.":"Linker for activation of T-cells family member 1;1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 ;E3 ubiquitin-protein ligase CBL","subunits.Gene.name.":"LAT;PLCG1;CBL","subunits.Gene.name.syn.":"None;PLC1;CBL2, RNF55","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors show that  upon OKT3 stimulation, an extensive phosphorylation of LAT was seen in J2.LAT cells, but the phosphorylation of LAT F171F191 was barely detectable.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2957,"ComplexName":"LAT-GRB2 complex, Fyn-mLck(KA) or Syk kinase activated","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43561;P62993","subunits.Entrez.IDs.":"27040;2885","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007169;GO:0050896","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway;response to stimulus","FunCat.ID":"30.05.01.12;36.25","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways;animal specific systemic sensing and response","PubMed.ID":16938345,"subunits.Protein.name.":"Linker for activation of T-cells family member 1;Growth factor receptor-bound protein 2","subunits.Gene.name.":"LAT;GRB2","subunits.Gene.name.syn.":"None;ASH","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors show that in the absence of a kinase, the association of LAT and Grb2 was not detected. Grb2 was co-precipitated with LAT, but not with LATF171F191, in the presence of Fyn, mLck(KA) or Syk kinases.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2958,"ComplexName":"SMAD1-CBP complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q15797;Q92793","subunits.Entrez.IDs.":"4086;1387","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045893;GO:0006473;GO:0006476;GO:0007179;GO:0051276;GO:0005634","GO.description":"DNA topological change;positive regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;transforming growth factor beta receptor signaling pathway;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.01;14.07.04;30.05.01.18.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription activation;modification by acetylation, deacetylation;TGF-beta-receptor signalling pathway;organization of chromosome structure;nucleus","PubMed.ID":10673036,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 1 ;CREB-binding protein","subunits.Gene.name.":"SMAD1;CREBBP","subunits.Gene.name.syn.":"BSP1 MADH1 MADR1;CBP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SMAD1 stimulates transcription cooperatively with CBP.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2959,"ComplexName":"SMAD1-OAZ-HsN3 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"P28070;P54368;Q15797","subunits.Entrez.IDs.":"5692;4946;4086","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0043161;GO:0006511;GO:0003677;GO:0007179;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;DNA binding;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"11.02.03.04;14.13.01.01;16.03.01;30.05.01.18.01;70.10","FunCat.description":"transcriptional control;proteasomal degradation (ubiquitin/proteasomal pathway);DNA binding;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":12097147,"subunits.Protein.name.":"Proteasome subunit beta type-4 ;Ornithine decarboxylase antizyme 1;Mothers against decapentaplegic homolog 1","subunits.Gene.name.":"PSMB4;OAZ1;SMAD1","subunits.Gene.name.syn.":"PROS26;OAZ;BSP1 MADH1 MADR1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The interaction of the subunits is enhanced upon BMP type I receptor activation and occur prior to the incorporation of HsN3 into the mature 20S proteasome. Furthermore, BMPs trigger the translocation of the complex to the nucleus.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2960,"ComplexName":"SLP-76-PLC-gamma-1-ITK complex, alpha-TCR stimulated","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P19174;Q08881;Q13094","subunits.Entrez.IDs.":"5335;3702;3937","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0023052;GO:0048015","GO.description":"signaling;phosphatidylinositol-mediated signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":17148460,"subunits.Protein.name.":"1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 ;Tyrosine-protein kinase ITK/TSK ;Lymphocyte cytosolic protein 2","subunits.Gene.name.":"PLCG1;ITK;LCP2","subunits.Gene.name.syn.":"PLC1;EMT LYK;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors speculate that SLP-76 may activate PLC-gamma-1 by regulating the ITK-mediated phosphorylation of PLC-gamma-1 at Tyr783.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2961,"ComplexName":"SLP-76-PLC-gamma-1-VAV complex, alpha-TCR stimulated","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P15498;P19174;Q13094","subunits.Entrez.IDs.":"7409;5335;3937","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0023052;GO:0048015","GO.description":"signaling;phosphatidylinositol-mediated signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":17148460,"subunits.Protein.name.":"Proto-oncogene vav;1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 ;Lymphocyte cytosolic protein 2","subunits.Gene.name.":"VAV1;PLCG1;LCP2","subunits.Gene.name.syn.":"VAV;PLC1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SLP-76 inducibly associated with both Vav and catalytically active ITK, which efficiently phosphorylated a PLC-gamma1 fragment at Tyr783 in vitro.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2962,"ComplexName":"CRK-BCAR1-DOCK1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P46108;P56945;Q14185","subunits.Entrez.IDs.":"1398;9564;1793","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007229;GO:0006909;GO:0043067","GO.description":"integrin-mediated signaling pathway;phagocytosis;regulation of programmed cell death","FunCat.ID":"30.05.02.26;36.25.16.01.03;40.10.02.04","FunCat.description":"integrin receptor signalling pathway;phagocyte response (e.g. macrophages, dendritic cells, granulocytes);regulation of apoptosis","PubMed.ID":11146654,"subunits.Protein.name.":"Adapter molecule crk;Breast cancer anti-estrogen resistance protein 1;Dedicator of cytokinesis protein 1","subunits.Gene.name.":"CRK;BCAR1;DOCK1","subunits.Gene.name.syn.":"None;CAS CASS1 CRKAS;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Alpha(v)beta5 integrin binds to the apoptotic cell for recruitment of this complex to the membrane.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2963,"ComplexName":"ITK-SLP-76 complex, anti-TCR stimulated","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q08881;Q13094","subunits.Entrez.IDs.":"3702;3937","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation;MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0023052;GO:0050896;GO:0048015","GO.description":"signaling;response to stimulus;phosphatidylinositol-mediated signaling","FunCat.ID":"30.01;36.25","FunCat.description":"cellular signalling;animal specific systemic sensing and response","PubMed.ID":17420479,"subunits.Protein.name.":"Tyrosine-protein kinase ITK/TSK ;Lymphocyte cytosolic protein 2","subunits.Gene.name.":"ITK;LCP2","subunits.Gene.name.syn.":"EMT LYK;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors show that catalytically active ITK is found primarily in complex with SLP-76. Further they demonstrate that a continued interaction with SLP-76 is required to maintain ITK in an active state.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2964,"ComplexName":"ITGA9-ITGB1-ADAM1 complex","Organism":"Mammalia","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;Q13797;Q60813","subunits.Entrez.IDs.":"3688;3680;280668","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0005515","GO.description":"protein binding","FunCat.ID":"16.01","FunCat.description":"protein binding","PubMed.ID":11882657,"subunits.Protein.name.":"Integrin beta-1;Integrin alpha-9 ;Disintegrin and metalloproteinase domain-containing protein 1a","subunits.Gene.name.":"ITGB1;ITGA9;Adam1a","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;;Adam1 Ftna","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Alpha9-beta1-ADAM interactions may have a broad significance in many biological and pathological processes such as fertilization, development, and tissue remodeling.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Mus musculus (Mouse)"}
{"ComplexID":2965,"ComplexName":"ITGA9-ITGB1-ADAM3 complex","Organism":"Mammalia","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;Q13797;Q810R6","subunits.Entrez.IDs.":"3688;3680;11497","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0005515","GO.description":"protein binding","FunCat.ID":"16.01","FunCat.description":"protein binding","PubMed.ID":11882657,"subunits.Protein.name.":"Integrin beta-1;Integrin alpha-9 ;Adam3 protein","subunits.Gene.name.":"ITGB1;ITGA9;Adam3","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Alpha9-beta1-ADAM interactions may have a broad significance in many biological and pathological processes such as fertilization, development, and tissue remodeling.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Mus musculus (Mouse)"}
{"ComplexID":2966,"ComplexName":"NuMA-LGN-G-alpha-i-1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P63096;P81274;Q14980","subunits.Entrez.IDs.":"2770;29899;4926","Protein.complex.purification.method":"MI:0096- pull down;MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0000278;GO:0051726;GO:0051225;GO:0007098","GO.description":"mitotic cell cycle;regulation of cell cycle;spindle assembly;centrosome cycle","FunCat.ID":"10.03.01.01;10.03.01;10.03.05.01","FunCat.description":"mitotic cell cycle;mitotic cell cycle and cell cycle control;spindle pole body/centrosome and microtubule cycle","PubMed.ID":15537540,"subunits.Protein.name.":"Guanine nucleotide-binding protein G;G-protein-signaling modulator 2 ;Nuclear mitotic apparatus protein 1","subunits.Gene.name.":"GNAI1;GPSM2;NUMA1","subunits.Gene.name.syn.":";LGN;NMP22 NUMA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors propose that the trimeric NuMA-LGN-G-alpha complex regulates the interaction of aster MTs with the cell cortex. They analyzed with a FRET biosensor that LGN behaves as a conformational switch: in its closed state, the N and C termini interact, but NuMA or G-alpha-i can disrupt this association, allowing LGN to interact simultaneously with both proteins, resulting in their cortical localization.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2967,"ComplexName":"Itga9-Itgb1-Thbs1 complex","Organism":"Mouse","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P09055;P35441;Q91YD5","subunits.Entrez.IDs.":"16412;21825;104099","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0001525","GO.description":"angiogenesis","FunCat.ID":"41.05.16","FunCat.description":"angiogenesis","PubMed.ID":17413041,"subunits.Protein.name.":"Integrin beta-1 ;Thrombospondin-1;Integrin alpha 9 protein","subunits.Gene.name.":"Itgb1;Thbs1;Itga9","subunits.Gene.name.syn.":";Tsp1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Alpha9-beta1 integrin expressed in microvascular endothelial cells interacts with thrombospondin-1, and this interaction is involved in modulation of angiogenesis.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2968,"ComplexName":"Axin-SMAD3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15169;P84022","subunits.Entrez.IDs.":"8312;4088","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0007179;GO:0005737","GO.description":"transforming growth factor beta receptor signaling pathway;cytoplasm","FunCat.ID":"30.05.01.18.01;70.03","FunCat.description":"TGF-beta-receptor signalling pathway;cytoplasm","PubMed.ID":11438668,"subunits.Protein.name.":"Axin-1 ;Mothers against decapentaplegic homolog 3","subunits.Gene.name.":"AXIN1;SMAD3","subunits.Gene.name.syn.":"AXIN;MADH3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Phosphorylation of SMAD3 by T(beta)R-I is faciliated in the presence of Axin. In the absence of ligand stimulation, Axin was colocalized with Smad3 in the cytoplasm in vivo. Upon receptor activation, Smad3 was strongly phosphorylated by TGF-beta type I receptor (TbetaR-I) in the presence of Axin, and dissociated from TbetaR-I and Axin.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2969,"ComplexName":"mTORC2 complex (mTOR/FRAP1, LST8, mAVO3/RICTOR)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P42345;Q6R327;Q9BVC4","subunits.Entrez.IDs.":"2475;253260;64223","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000902;GO:0016049;GO:0030036","GO.description":"cell morphogenesis;cell growth;actin cytoskeleton organization","FunCat.ID":"40.01;42.04.03","FunCat.description":"cell growth / morphogenesis;actin cytoskeleton","PubMed.ID":15467718,"subunits.Protein.name.":"Serine/threonine-protein kinase mTOR ;Rapamycin-insensitive companion of mTOR ;Target of rapamycin complex subunit LST8","subunits.Gene.name.":"MTOR;RICTOR;MLST8","subunits.Gene.name.syn.":"FRAP FRAP1 FRAP2 RAFT1 RAPT1;KIAA1999;GBL LST8","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"mTORC1 and mTORC2 constitute a primordial signalling network conserved in eukaryotic evolution to control the fundamental process of cell growth.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2970,"ComplexName":"mTORC1 complex (mTOR/FRAP1, LST8, RAPTOR)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P42345;Q8N122;Q9BVC4","subunits.Entrez.IDs.":"2475;57521;64223","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000902;GO:0016049","GO.description":"cell morphogenesis;cell growth","FunCat.ID":"40.01","FunCat.description":"cell growth / morphogenesis","PubMed.ID":15467718,"subunits.Protein.name.":"Serine/threonine-protein kinase mTOR ;Regulatory-associated protein of mTOR ;Target of rapamycin complex subunit LST8","subunits.Gene.name.":"MTOR;RPTOR;MLST8","subunits.Gene.name.syn.":"FRAP FRAP1 FRAP2 RAFT1 RAPT1;KIAA1303 RAPTOR;GBL LST8","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"mTORC1 and mTORC2 constitute a primordial signalling network conserved in eukaryotic evolution to control the fundamental process of cell growth.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2971,"ComplexName":"ITGA9-ITGB1-VEGFC complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P49767;Q13797","subunits.Entrez.IDs.":"3688;7424;3680","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0016477;GO:0007155;GO:0030154","GO.description":"cell migration;cell adhesion;cell differentiation","FunCat.ID":"34.05.01;34.07;40.02","FunCat.description":"cell migration;cell adhesion;cell differentiation","PubMed.ID":15590642,"subunits.Protein.name.":"Integrin beta-1;Vascular endothelial growth factor C ;Integrin alpha-9","subunits.Gene.name.":"ITGB1;VEGFC;ITGA9","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Alpha9-beta1 directly binds to VEGF-C and -D and contributes to lymphangiogenesis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2972,"ComplexName":"ITGA9-ITGB1-VEGFA complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P15692;Q13797","subunits.Entrez.IDs.":"3688;7422;3680","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0001525","GO.description":"angiogenesis","FunCat.ID":"41.05.16","FunCat.description":"angiogenesis","PubMed.ID":15590642,"subunits.Protein.name.":"Integrin beta-1;Vascular endothelial growth factor A ;Integrin alpha-9","subunits.Gene.name.":"ITGB1;VEGFA;ITGA9","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;VEGF;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Alpha9-beta1 integrin binds the VEGF121 isoform of VEGF-A.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2973,"ComplexName":"Ccd1-Dvl2-Rac complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P63001;Q60838;Q80Y83","subunits.Entrez.IDs.":"19353;13543;330938","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0007254","GO.description":"JNK cascade","FunCat.ID":"30.01.05.01.02","FunCat.description":"JNK cascade","PubMed.ID":15262978,"subunits.Protein.name.":"Ras-related C3 botulinum toxin substrate 1;Segment polarity protein dishevelled homolog DVL-2;Dixin","subunits.Gene.name.":"Rac1;Dvl2;Dixdc1","subunits.Gene.name.syn.":"None;None;Ccd1 Kiaa1735","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors showed that although Ccd1 could not interact directly with Rac, Ccd1, Dvl, and Rac could coexist in the same complex, indicating that Ccd1 inhibited Dvl-mediated JNK activation by forming a ternary complex of Ccd1\\u00b7Dvl\\u00b7Rac, in which Dvl\\u00b7Rac is somehow blocked from further activating JNK. The authors do not exactly describe the Rac GTPase.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2974,"ComplexName":"Dvl2-Rac complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P63001;Q60838","subunits.Entrez.IDs.":"19353;13543","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0007254","GO.description":"JNK cascade","FunCat.ID":"30.01.05.01.02","FunCat.description":"JNK cascade","PubMed.ID":15262978,"subunits.Protein.name.":"Ras-related C3 botulinum toxin substrate 1;Segment polarity protein dishevelled homolog DVL-2","subunits.Gene.name.":"Rac1;Dvl2","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors showed that although Ccd1 could not interact directly with Rac, Ccd1, Dvl, and Rac could coexist in the same complex, indicating that Ccd1 inhibited Dvl-mediated JNK activation by forming a ternary complex of Ccd1\\u00b7Dvl\\u00b7Rac, in which Dvl\\u00b7Rac is somehow blocked from further activating JNK. The authors do not exactly describe the Rac GTPase.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2975,"ComplexName":"SMAD3-E2F4/5-p107-DP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P28749;P84022;Q14186;Q15329;Q16254","subunits.Entrez.IDs.":"5933;4088;7027;1875;1874","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0007179;GO:0005737","GO.description":"transforming growth factor beta receptor signaling pathway;cytoplasm","FunCat.ID":"30.05.01.18.01;70.03","FunCat.description":"TGF-beta-receptor signalling pathway;cytoplasm","PubMed.ID":12150994,"subunits.Protein.name.":"Retinoblastoma-like protein 1;Mothers against decapentaplegic homolog 3;Transcription factor Dp-1;Transcription factor E2F5 ;Transcription factor E2F4","subunits.Gene.name.":"RBL1;SMAD3;TFDP1;E2F5;E2F4","subunits.Gene.name.syn.":"PRB1, p107, CP107;MADH3;DP1;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex preexists in the cytoplasm. In response to TGF-beta, this complex moves to the nucleus and associates with SMAD4.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2976,"ComplexName":"Ccd1-Dvl2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q60838;Q80Y83","subunits.Entrez.IDs.":"13543;330938","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0007254","GO.description":"JNK cascade","FunCat.ID":"30.01.05.01.02","FunCat.description":"JNK cascade","PubMed.ID":15262978,"subunits.Protein.name.":"Segment polarity protein dishevelled homolog DVL-2;Dixin","subunits.Gene.name.":"Dvl2;Dixdc1","subunits.Gene.name.syn.":"None;Ccd1 Kiaa1735","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors showed that Ccd1\\u00b7Dvl complex formation is required for Ccd1 inhibition of Dvl-mediated JNK activation.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2977,"ComplexName":"Ccd1-Axin complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O35625;Q80Y83","subunits.Entrez.IDs.":"12005;330938","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0007254","GO.description":"JNK cascade","FunCat.ID":"30.01.05.01.02","FunCat.description":"JNK cascade","PubMed.ID":15262978,"subunits.Protein.name.":"Axin-1 ;Dixin","subunits.Gene.name.":"Axin1;Dixdc1","subunits.Gene.name.syn.":"Axin Fu;Ccd1 Kiaa1735","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors showed that Ccd1 competes against MEKK1 binding to Axin in a dose-dependent manner, although MEKK1 and Ccd1 bind to separate regions far apart in Axin.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2978,"ComplexName":"Mekk1-Axin complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O35625;P53349","subunits.Entrez.IDs.":"12005;26401","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0007254","GO.description":"JNK cascade","FunCat.ID":"30.01.05.01.02","FunCat.description":"JNK cascade","PubMed.ID":15262978,"subunits.Protein.name.":"Axin-1 ;Mitogen-activated protein kinase kinase kinase 1","subunits.Gene.name.":"Axin1;Map3k1","subunits.Gene.name.syn.":"Axin Fu;Mekk Mekk1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors showed that Ccd1 competes against MEKK1 binding to Axin in a dose-dependent manner, although MEKK1 and Ccd1 bind to separate regions far apart in Axin.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2979,"ComplexName":"Axin-Mekk4 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O08648;O35625","subunits.Entrez.IDs.":"26407;12005","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0007254","GO.description":"JNK cascade","FunCat.ID":"30.01.05.01.02","FunCat.description":"JNK cascade","PubMed.ID":15262978,"subunits.Protein.name.":"Mitogen-activated protein kinase kinase kinase 4 ;Axin-1","subunits.Gene.name.":"Map3k4;Axin1","subunits.Gene.name.syn.":"Mekk4;Axin Fu","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors showed that Ccd1 did not disrupt the Axin-MEKK4 complex. They showed further that Ccd1 physically interacted with MEKK4 in their physiological concentrations and prevented MEKK4 from binding to Axin.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2980,"ComplexName":"Ccd1-Mekk4 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O08648;Q80Y83","subunits.Entrez.IDs.":"26407;330938","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0007254","GO.description":"JNK cascade","FunCat.ID":"30.01.05.01.02","FunCat.description":"JNK cascade","PubMed.ID":15262978,"subunits.Protein.name.":"Mitogen-activated protein kinase kinase kinase 4 ;Dixin","subunits.Gene.name.":"Map3k4;Dixdc1","subunits.Gene.name.syn.":"Mekk4;Ccd1 Kiaa1735","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors showed that Ccd1 did not disrupt the Axin-MEKK4 complex. They showed further that Ccd1 physically interacted with MEKK4 in their physiological concentrations and prevented MEKK4 from binding to Axin.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2981,"ComplexName":"Nkx3.2-SMAD1 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"P70340;P97503","subunits.Entrez.IDs.":"17125;12020","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0007178;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;transmembrane receptor protein serine/threonine kinase signaling pathway;nucleus","FunCat.ID":"11.02.03.04;30.05.01.18;70.10","FunCat.description":"transcriptional control;transmembrane receptor protein serine/threonine kinase signalling pathways;nucleus","PubMed.ID":14612411,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 1;Homeobox protein Nkx-3.2","subunits.Gene.name.":"Smad1;Nkx3-2","subunits.Gene.name.syn.":"Madh1 Madr1;Bapx1 Nkx-3.2 Nkx3b","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex formation is enhanced in the presence of BMP signalling.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2982,"ComplexName":"Nkx3.2-SMAD1-SMAD4 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"P70340;P97471;P97503","subunits.Entrez.IDs.":"17125;17128;12020","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0007178;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;transmembrane receptor protein serine/threonine kinase signaling pathway;nucleus","FunCat.ID":"11.02.03.04;30.05.01.18;70.10","FunCat.description":"transcriptional control;transmembrane receptor protein serine/threonine kinase signalling pathways;nucleus","PubMed.ID":14612411,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 1;Mothers against decapentaplegic homolog 4 ;Homeobox protein Nkx-3.2","subunits.Gene.name.":"Smad1;Smad4;Nkx3-2","subunits.Gene.name.syn.":"Madh1 Madr1;Dpc4 Madh4;Bapx1 Nkx-3.2 Nkx3b","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex formation is enhanced in the presence of BMP signalling.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2983,"ComplexName":"Nkx3.2-SMAD1-SMAD4-HDAC1 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"O09106;P70340;P97471;P97503","subunits.Entrez.IDs.":"433759;17125;17128;12020","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0007178;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;transmembrane receptor protein serine/threonine kinase signaling pathway;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;30.05.01.18;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;transmembrane receptor protein serine/threonine kinase signalling pathways;organization of chromosome structure;nucleus","PubMed.ID":14612411,"subunits.Protein.name.":"Histone deacetylase 1;Mothers against decapentaplegic homolog 1;Mothers against decapentaplegic homolog 4 ;Homeobox protein Nkx-3.2","subunits.Gene.name.":"Hdac1;Smad1;Smad4;Nkx3-2","subunits.Gene.name.syn.":"None;Madh1 Madr1;Dpc4 Madh4;Bapx1 Nkx-3.2 Nkx3b","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex formation is enhanced in the presence of BMP signalling. HDAC activity is necessary for transcriptional repression of Nkx3.2.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2984,"ComplexName":"Nkx3.2-SMAD1-SMAD4-HDAC-Sin3A complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"O09106;P70340;P97471;P97503;Q60520;Q60972;Q60973","subunits.Entrez.IDs.":"433759;17125;17128;12020;20466;19646;245688","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0007178;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;transmembrane receptor protein serine/threonine kinase signaling pathway;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;30.05.01.18;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;transmembrane receptor protein serine/threonine kinase signalling pathways;organization of chromosome structure;nucleus","PubMed.ID":14612411,"subunits.Protein.name.":"Histone deacetylase 1;Mothers against decapentaplegic homolog 1;Mothers against decapentaplegic homolog 4 ;Homeobox protein Nkx-3.2 ;Paired amphipathic helix protein Sin3a;Histone-binding protein RBBP4 ;Histone-binding protein RBBP7","subunits.Gene.name.":"Hdac1;Smad1;Smad4;Nkx3-2;Sin3a;Rbbp4;Rbbp7","subunits.Gene.name.syn.":"None;Madh1 Madr1;Dpc4 Madh4;Bapx1 Nkx-3.2 Nkx3b;Kiaa4126;Rbap48;Rbap46","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complex formation is enhanced in the presence of BMP signalling. HDAC activity is necessary for transcriptional repression of Nkx3.2.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":2985,"ComplexName":"mTOR-signaling complex","Organism":"Human","Synonyms":"Nutrient-sensitive complex NSC","Cell.line":"None","subunits.UniProt.IDs.":"P42345;Q8N122","subunits.Entrez.IDs.":"2475;57521","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000902;GO:0016049","GO.description":"cell morphogenesis;cell growth","FunCat.ID":"40.01","FunCat.description":"cell growth / morphogenesis","PubMed.ID":12150925,"subunits.Protein.name.":"Serine/threonine-protein kinase mTOR ;Regulatory-associated protein of mTOR","subunits.Gene.name.":"MTOR;RPTOR","subunits.Gene.name.syn.":"FRAP FRAP1 FRAP2 RAFT1 RAPT1;KIAA1303 RAPTOR","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"mTOR/RAFT1/FRAP is the target  of the immunosuppressive drug  rapamycin and the central  component of a nutrient- and hormone-sensitive signaling pathway that regulates cell growth.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2989,"ComplexName":"ITGA9-ITGB1-ADAM8 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P78325;Q13797","subunits.Entrez.IDs.":"3688;101;3680","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0005515;GO:0007155;GO:0001503;GO:0030316","GO.description":"protein binding;cell adhesion;ossification;osteoclast differentiation","FunCat.ID":"16.01;34.07;41.05.17;45.03.05.07","FunCat.description":"protein binding;cell adhesion;osteogenesis;bone","PubMed.ID":16995821,"subunits.Protein.name.":"Integrin beta-1;Disintegrin and metalloproteinase domain-containing protein 8 ;Integrin alpha-9","subunits.Gene.name.":"ITGB1;ADAM8;ITGA9","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;MS2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2990,"ComplexName":"mTOR-signaling complex (FRAP1/mTOR, GBL, RAPTOR)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P42345;Q8N122;Q9BVC4","subunits.Entrez.IDs.":"2475;57521;64223","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000902;GO:0016049","GO.description":"cell morphogenesis;cell growth","FunCat.ID":"40.01","FunCat.description":"cell growth / morphogenesis","PubMed.ID":12718876,"subunits.Protein.name.":"Serine/threonine-protein kinase mTOR ;Regulatory-associated protein of mTOR ;Target of rapamycin complex subunit LST8","subunits.Gene.name.":"MTOR;RPTOR;MLST8","subunits.Gene.name.syn.":"FRAP FRAP1 FRAP2 RAFT1 RAPT1;KIAA1303 RAPTOR;GBL LST8","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2991,"ComplexName":"mTOR-signaling complex (mTOR/FRAP1, RAPTOR)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P42345;Q8N122","subunits.Entrez.IDs.":"2475;57521","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000902;GO:0016049","GO.description":"cell morphogenesis;cell growth","FunCat.ID":"40.01","FunCat.description":"cell growth / morphogenesis","PubMed.ID":12150926,"subunits.Protein.name.":"Serine/threonine-protein kinase mTOR ;Regulatory-associated protein of mTOR","subunits.Gene.name.":"MTOR;RPTOR","subunits.Gene.name.syn.":"FRAP FRAP1 FRAP2 RAFT1 RAPT1;KIAA1303 RAPTOR","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2992,"ComplexName":"SMAD7-SMURF2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15105;Q9HAU4","subunits.Entrez.IDs.":"4092;64750","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511;GO:0051098;GO:0005515;GO:0030545;GO:0005737;GO:0005634","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;regulation of binding;protein binding;receptor regulator activity;cytoplasm;nucleus","FunCat.ID":"14.07.05;14.13.01.01;18.01.07;16.01;18.02.07;70.03;70.10","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway);regulation by binding / dissociation;protein binding;regulator of receptor activity;cytoplasm;nucleus","PubMed.ID":11163210,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 7 ;E3 ubiquitin-protein ligase SMURF2","subunits.Gene.name.":"SMAD7;SMURF2","subunits.Gene.name.syn.":"MADH7 MADH8;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SMURF is localized in the nucleus, but binding to SMAD7 induces export to the cytoplasm.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2993,"ComplexName":"Axin-GSK-3-beta complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"O70239;P18266","subunits.Entrez.IDs.":"79257;84027","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016055","GO.description":"Wnt signaling pathway","FunCat.ID":"30.05.02.20","FunCat.description":"Wnt signalling pathway","PubMed.ID":9482734,"subunits.Protein.name.":"Axin-1 ;Glycogen synthase kinase-3 beta","subunits.Gene.name.":"Axin1;Gsk3b","subunits.Gene.name.syn.":"Axin;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Endogenous Axin forms a complex with and is phosphorylated by GSK-3b.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2994,"ComplexName":"Axin-GSK-3-alpha complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"O70239;P18265","subunits.Entrez.IDs.":"79257;50686","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016055","GO.description":"Wnt signaling pathway","FunCat.ID":"30.05.02.20","FunCat.description":"Wnt signalling pathway","PubMed.ID":9482734,"subunits.Protein.name.":"Axin-1 ;Glycogen synthase kinase-3 alpha","subunits.Gene.name.":"Axin1;Gsk3a","subunits.Gene.name.syn.":"Axin;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Endogenous Axin forms a complex with and is phosphorylated by GSK-3a.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2995,"ComplexName":"Axin-beta-catenin complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"O70239;Q9WU82","subunits.Entrez.IDs.":"79257;84353","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation; MI:0096- pull down; MI:0018- two hybrid","GO.ID":"GO:0016055","GO.description":"Wnt signaling pathway","FunCat.ID":"30.05.02.20","FunCat.description":"Wnt signalling pathway","PubMed.ID":9482734,"subunits.Protein.name.":"Axin-1 ;Catenin beta-1","subunits.Gene.name.":"Axin1;Ctnnb1","subunits.Gene.name.syn.":"Axin;Catnb","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Residues 298-506 of rAxin are sufficient and necessary to form a complex with b-catenin.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":2996,"ComplexName":"SMAD7-SMURF1 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"O15105;Q9HCE7","subunits.Entrez.IDs.":"4092;57154","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511;GO:0051098;GO:0005515;GO:0030545;GO:0005737;GO:0005634","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;regulation of binding;protein binding;receptor regulator activity;cytoplasm;nucleus","FunCat.ID":"14.07.05;14.13.01.01;18.01.07;16.01;18.02.07;70.03;70.10","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway);regulation by binding / dissociation;protein binding;regulator of receptor activity;cytoplasm;nucleus","PubMed.ID":11278251,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 7 ;E3 ubiquitin-protein ligase SMURF1","subunits.Gene.name.":"SMAD7;SMURF1","subunits.Gene.name.syn.":"MADH7 MADH8;KIAA1625","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SMAD7 associates with SMURF1 in the nucleus and is exported to the cytoplasm.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2997,"ComplexName":"SMAD7-SMURF1-TGF-beta receptor complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"O15105;P36897;P37173;Q9HCE7","subunits.Entrez.IDs.":"4092;7046;7048;57154","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511;GO:0007179;GO:0005737","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;transforming growth factor beta receptor signaling pathway;cytoplasm","FunCat.ID":"14.07.05;14.13.01.01;30.05.01.18.01;70.03","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway);TGF-beta-receptor signalling pathway;cytoplasm","PubMed.ID":11278251,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 7 ;TGF-beta receptor type-1;TGF-beta receptor type-2;E3 ubiquitin-protein ligase SMURF1","subunits.Gene.name.":"SMAD7;TGFBR1;TGFBR2;SMURF1","subunits.Gene.name.syn.":"MADH7 MADH8;ALK5 SKR4;None;KIAA1625","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SMAD7 enhances the interaction between SMURF1 and the TGF-beta receptor complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2998,"ComplexName":"Axin-PP2A A-PP2A C-GSK3-beta-beta-catenin complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15169;P35222;P49841;Q15172","subunits.Entrez.IDs.":"8312;1499;2932;5525","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016055","GO.description":"Wnt signaling pathway","FunCat.ID":"30.05.02.20","FunCat.description":"Wnt signalling pathway","PubMed.ID":11818547,"subunits.Protein.name.":"Axin-1 ;Catenin beta-1;Glycogen synthase kinase-3 beta;Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform","subunits.Gene.name.":"AXIN1;CTNNB1;GSK3B;PPP2R5A","subunits.Gene.name.syn.":"AXIN;CTNNB;None;","Disease.comment":"None","Subunits.comment":"The authors describe as additional component of the complex protein phosphatase PP2A C, that couldn't be identified.","Complex.comment":"The incubation of the lysates with casein kinase I isoform epsilon decreases the association of PP2A C and A with the beta-catenin degradation complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":2999,"ComplexName":"Smad2 homotrimer complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"Q62432","subunits.Entrez.IDs.":"17126","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation; MI:0030- crosslink; MI:0071- molecular sieving","GO.ID":"GO:0045893;GO:0007179","GO.description":"positive regulation of transcription, DNA-templated;transforming growth factor beta receptor signaling pathway","FunCat.ID":"11.02.03.04.01;30.05.01.18.01","FunCat.description":"transcription activation;TGF-beta-receptor signalling pathway","PubMed.ID":9670020,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 2","subunits.Gene.name.":"Smad2","subunits.Gene.name.syn.":"Madh2 Madr2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Smad2 exists as monomer and forms homotrimers after phosphorylation by TGF-beta I receptor.","SWISSPROT.organism":"Mus musculus (Mouse)"}
{"ComplexID":3000,"ComplexName":"Smad2-Smad3 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"Q62432;Q8BUN5","subunits.Entrez.IDs.":"17126;17127","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045893;GO:0007179","GO.description":"positive regulation of transcription, DNA-templated;transforming growth factor beta receptor signaling pathway","FunCat.ID":"11.02.03.04.01;30.05.01.18.01","FunCat.description":"transcription activation;TGF-beta-receptor signalling pathway","PubMed.ID":9670020,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 2 ;Mothers against decapentaplegic homolog 3","subunits.Gene.name.":"Smad2;Smad3","subunits.Gene.name.syn.":"Madh2 Madr2;Madh3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3001,"ComplexName":"Smad2-Smad4 heteromer complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"P97471;Q62432","subunits.Entrez.IDs.":"17128;17126","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0045893;GO:0007179","GO.description":"positive regulation of transcription, DNA-templated;transforming growth factor beta receptor signaling pathway","FunCat.ID":"11.02.03.04.01;30.05.01.18.01","FunCat.description":"transcription activation;TGF-beta-receptor signalling pathway","PubMed.ID":9670020,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 4 ;Mothers against decapentaplegic homolog 2","subunits.Gene.name.":"Smad4;Smad2","subunits.Gene.name.syn.":"Dpc4 Madh4;Madh2 Madr2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Complexes with two molecules of Smad4 and only one molecule of Smad2 also exist.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3002,"ComplexName":"Smad3-Smad4 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"P97471;Q8BUN5","subunits.Entrez.IDs.":"17128;17127","Protein.complex.purification.method":"MI:0412- electrophoretic mobility supershift assay","GO.ID":"GO:0045893;GO:0003677;GO:0007179;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"11.02.03.04.01;16.03.01;30.05.01.18.01;70.10","FunCat.description":"transcription activation;DNA binding;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":9670020,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 4 ;Mothers against decapentaplegic homolog 3","subunits.Gene.name.":"Smad4;Smad3","subunits.Gene.name.syn.":"Dpc4 Madh4;Madh3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3003,"ComplexName":"Smad3 homotrimer complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"Q8BUN5","subunits.Entrez.IDs.":"17127","Protein.complex.purification.method":"MI:0412- electrophoretic mobility supershift assay","GO.ID":"GO:0045893;GO:0003677;GO:0007179","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;transforming growth factor beta receptor signaling pathway","FunCat.ID":"11.02.03.04.01;16.03.01;30.05.01.18.01","FunCat.description":"transcription activation;DNA binding;TGF-beta-receptor signalling pathway","PubMed.ID":9670020,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 3","subunits.Gene.name.":"Smad3","subunits.Gene.name.syn.":"Madh3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In the absence of Smad4, Smad3 can form homomers.","SWISSPROT.organism":"Mus musculus (Mouse)"}
{"ComplexID":3004,"ComplexName":"APC-Axin-1-beta-catenin complex","Organism":"Human","Synonyms":"23S APC-containing complex","Cell.line":"None","subunits.UniProt.IDs.":"O15169;P25054;P35222","subunits.Entrez.IDs.":"8312;324;1499","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0016055","GO.description":"Wnt signaling pathway","FunCat.ID":"30.05.02.20","FunCat.description":"Wnt signalling pathway","PubMed.ID":16188939,"subunits.Protein.name.":"Axin-1 ;Adenomatous polyposis coli protein;Catenin beta-1","subunits.Gene.name.":"AXIN1;APC;CTNNB1","subunits.Gene.name.syn.":"AXIN;DP2.5;CTNNB","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3005,"ComplexName":"TGF-beta-receptor type I homodimer complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P80204","subunits.Entrez.IDs.":"29591","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0005515;GO:0007179;GO:0005783","GO.description":"protein binding;transforming growth factor beta receptor signaling pathway;endoplasmic reticulum","FunCat.ID":"16.01;30.05.01.18.01;70.07","FunCat.description":"protein binding;TGF-beta-receptor signalling pathway;endoplasmic reticulum","PubMed.ID":9472030,"subunits.Protein.name.":"TGF-beta receptor type-1","subunits.Gene.name.":"Tgfbr1","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"T-beta-RI can bind TGF-beta only in the presence of T-beta RII.","SWISSPROT.organism":"Rattus norvegicus (Rat)"}
{"ComplexID":3006,"ComplexName":"TGF-beta-receptor type II homodimer complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"Q62312","subunits.Entrez.IDs.":"21813","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0005515;GO:0007179;GO:0005783","GO.description":"protein binding;transforming growth factor beta receptor signaling pathway;endoplasmic reticulum","FunCat.ID":"16.01;30.05.01.18.01;70.07","FunCat.description":"protein binding;TGF-beta-receptor signalling pathway;endoplasmic reticulum","PubMed.ID":9472030,"subunits.Protein.name.":"TGF-beta receptor type-2","subunits.Gene.name.":"Tgfbr2","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The type II receptor can bind TGF-beta in the absence of T-beta-RI.","SWISSPROT.organism":"Mus musculus (Mouse)"}
{"ComplexID":3007,"ComplexName":"TGF-beta-receptor type I homodimer complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"Q64729","subunits.Entrez.IDs.":"21812","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0005515;GO:0007179;GO:0005783","GO.description":"protein binding;transforming growth factor beta receptor signaling pathway;endoplasmic reticulum","FunCat.ID":"16.01;30.05.01.18.01;70.07","FunCat.description":"protein binding;TGF-beta-receptor signalling pathway;endoplasmic reticulum","PubMed.ID":9472030,"subunits.Protein.name.":"TGF-beta receptor type-1","subunits.Gene.name.":"Tgfbr1","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"T-beta-RI can bind TGF-beta only in the presence of T-beta RII.","SWISSPROT.organism":"Mus musculus (Mouse)"}
{"ComplexID":3008,"ComplexName":"60S APC containing complex","Organism":"Human","Synonyms":"None","Cell.line":"epithelium","subunits.UniProt.IDs.":"P23258;P25054;P46940;Q71U36","subunits.Entrez.IDs.":"7283;324;8826;7846","Protein.complex.purification.method":"MI:0029-cosedimentation through density gradients;MI:0226-ion exchange chromatography","GO.ID":"GO:0030036;GO:0005737","GO.description":"actin cytoskeleton organization;cytoplasm","FunCat.ID":"42.04.03;70.03","FunCat.description":"actin cytoskeleton;cytoplasm","PubMed.ID":17126424,"subunits.Protein.name.":"Tubulin gamma-1 chain;Adenomatous polyposis coli protein;Ras GTPase-activating-like protein IQGAP1;Tubulin alpha-1A chain","subunits.Gene.name.":"TUBG1;APC;IQGAP1;TUBA1A","subunits.Gene.name.syn.":"TUBG;DP2.5;KIAA0051;TUBA3","Disease.comment":"None","Subunits.comment":"Since the authors did not specify tubulin alpha as well as tubulin gamma, we used isoform tubulin alpha-1A chain  and isoform tubulin gamma-1 chain  , respectively.","Complex.comment":"The authors propose that 60S APC is a discrete high molecular weight complex with a novel function in cytoskeletal regulation in epithelial cells apart from its well established role in targeting catenin destruction or its proposed role in microtubule plus end stabilization.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3009,"ComplexName":"TFIID complex","Organism":"Human","Synonyms":"TFIID holoenzyme complex","Cell.line":"None","subunits.UniProt.IDs.":"O00268;P20226;P21675;P49848;Q15542;Q15544;Q16514;Q16594;Q6P1X5","subunits.Entrez.IDs.":"6874;6908;6872;6878;6877;6882;6883;6880;6873","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006352;GO:2001141;GO:0006355;GO:0003677;GO:0005634","GO.description":"DNA-templated transcription, initiation;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.01.01;11.02.03.04;16.03.01;70.10","FunCat.description":"transcription initiation;transcriptional control;DNA binding;nucleus","PubMed.ID":16895980,"subunits.Protein.name.":"Transcription initiation factor TFIID subunit 4;TATA-box-binding protein;Transcription initiation factor TFIID subunit 1;Transcription initiation factor TFIID subunit 6;Transcription initiation factor TFIID subunit 5;Transcription initiation factor TFIID subunit 11;Transcription initiation factor TFIID subunit 12;Transcription initiation factor TFIID subunit 9;Transcription initiation factor TFIID subunit 2","subunits.Gene.name.":"TAF4;TBP;TAF1;TAF6;TAF5;TAF11;TAF12;TAF9;TAF2","subunits.Gene.name.syn.":"TAF2C TAF2C1 TAF4A TAFII130 TAFII135;GTF2D1 TF2D TFIID;BA2R CCG1 CCGS TAF2A;TAF2E TAFII70;TAF2D;TAF2I;TAF15 TAF2J TAFII20;TAF2G TAFII31;CIF150 TAF2B","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The subunit stoichiometry is predicted by Sanders et al. (PMID:12138208).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3010,"ComplexName":"TFIID subcomplex","Organism":"Human","Synonyms":"TFIID (stable core) subcomplex","Cell.line":"None","subunits.UniProt.IDs.":"O00268;P49848;Q15542;Q16514;Q16594","subunits.Entrez.IDs.":"6874;6878;6877;6883;6880","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006352;GO:2001141;GO:0006355;GO:0003677;GO:0005634","GO.description":"DNA-templated transcription, initiation;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.01.01;11.02.03.04;16.03.01;70.10","FunCat.description":"transcription initiation;transcriptional control;DNA binding;nucleus","PubMed.ID":16895980,"subunits.Protein.name.":"Transcription initiation factor TFIID subunit 4;Transcription initiation factor TFIID subunit 6;Transcription initiation factor TFIID subunit 5;Transcription initiation factor TFIID subunit 12;Transcription initiation factor TFIID subunit 9","subunits.Gene.name.":"TAF4;TAF6;TAF5;TAF12;TAF9","subunits.Gene.name.syn.":"TAF2C TAF2C1 TAF4A TAFII130 TAFII135;TAF2E TAFII70;TAF2D;TAF15 TAF2J TAFII20;TAF2G TAFII31","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The subunit stoichiometry is predicted by Sanders et al. (PMID:12138208).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3011,"ComplexName":"APC-IQGAP1-Rac1 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"P25054;P46940;P63000","subunits.Entrez.IDs.":"324;8826;5879","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0016477;GO:0007010;GO:0005856","GO.description":"cell migration;cytoskeleton organization;cytoskeleton","FunCat.ID":"34.05.01;42.04;70.04","FunCat.description":"cell migration;cytoskeleton/structural proteins;cytoskeleton","PubMed.ID":15572129,"subunits.Protein.name.":"Adenomatous polyposis coli protein;Ras GTPase-activating-like protein IQGAP1;Ras-related C3 botulinum toxin substrate 1","subunits.Gene.name.":"APC;IQGAP1;RAC1","subunits.Gene.name.syn.":"DP2.5;KIAA0051;TC25","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"When EGFP-APC-M1 (aa221-968) was immunoprecipitated from the cells expressing EGFP-APC-M1 and constitutively active Rac1 (Rac1V12), both Rac1V12 and IQGAP1 were coimmunoprecipitated. The authors showed that activated Rac1 and Cdc42 formed a tripartite complex with IQGAP1 and APC.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3012,"ComplexName":"APC-IQGAP1-Cdc42 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"Vero cells","subunits.UniProt.IDs.":"P25054;P46940;P60953","subunits.Entrez.IDs.":"324;8826;998","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0016477;GO:0007010;GO:0005856","GO.description":"cell migration;cytoskeleton organization;cytoskeleton","FunCat.ID":"34.05.01;42.04;70.04","FunCat.description":"cell migration;cytoskeleton/structural proteins;cytoskeleton","PubMed.ID":15572129,"subunits.Protein.name.":"Adenomatous polyposis coli protein;Ras GTPase-activating-like protein IQGAP1;Cell division control protein 42 homolog","subunits.Gene.name.":"APC;IQGAP1;CDC42","subunits.Gene.name.syn.":"DP2.5;KIAA0051;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"When EGFP-APC-M1 (aa221-968) was immunoprecipitated from the cells expressing EGFP-APC-M1 and constitutively active Cdc42 (Cdc42V12), both Cdc42V12 and IQGAP1 were coimmunoprecipitated. The authors showed that activated Rac1 and Cdc42 formed a tripartite complex with IQGAP1 and APC.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3013,"ComplexName":"EB1-APC-mDia1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"O08808;Q61166;Q61315","subunits.Entrez.IDs.":"13367;13589;11789","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0016477;GO:0000226;GO:0015630","GO.description":"cell migration;microtubule cytoskeleton organization;microtubule cytoskeleton","FunCat.ID":"34.05.01;42.04.05;70.04.05","FunCat.description":"cell migration;microtubule cytoskeleton;microtubule cytoskeleton","PubMed.ID":15311282,"subunits.Protein.name.":"Protein diaphanous homolog 1 ;Microtubule-associated protein RP/EB family member 1 ;Adenomatous polyposis coli protein","subunits.Gene.name.":"Diaph1;Mapre1;Apc","subunits.Gene.name.syn.":"Diap1;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors showed that EB1 and APC interacted with mDia directly, through domains that were distinct from those that interact with each other.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3014,"ComplexName":"Cohesin complex, incomplete (Stag3, Scp1, Ss181)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O70576;Q62209;Q8BW22","subunits.Entrez.IDs.":"50878;20957;269397","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0000279;GO:0007067;GO:0007059;GO:0003677;GO:0051276;GO:0005694","GO.description":"M phase;mitotic nuclear division;chromosome segregation;DNA binding;chromosome organization;chromosome","FunCat.ID":"10.03.01.01.11;10.03.04.05;16.03.01;42.10.03;70.10.03","FunCat.description":"M phase;chromosome segregation/division;DNA binding;organization of chromosome structure;chromosome","PubMed.ID":15870106,"subunits.Protein.name.":"Cohesin subunit SA-3 ;Synaptonemal complex protein 1 ;Calcium-responsive transactivator","subunits.Gene.name.":"Stag3;Sycp1;Ss18l1","subunits.Gene.name.syn.":";Scp1;Crest Kiaa0693","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cohesin-complex proteins ensure that sister chomatids remain paired during meiosis.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3015,"ComplexName":"p27-cyclinE-Cdk2 - Ubiquitin E3 ligase (SKP1A, SKP2, CUL1, CKS1B, RBX1) complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P24864;P24941;P46527;P61024;P62877;P63208;Q13309;Q13616","subunits.Entrez.IDs.":"898;1017;1027;1163;9978;6500;6502;8454","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0000278;GO:0006468;GO:0006470;GO:0046777;GO:0016567;GO:0016579;GO:0050789","GO.description":"mitotic cell cycle;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;protein ubiquitination;protein deubiquitination;regulation of biological process","FunCat.ID":"10.03.01.01;14.07.03;14.07.05;18","FunCat.description":"mitotic cell cycle;modification by phosphorylation, dephosphorylation, autophosphorylation;modification by ubiquitination, deubiquitination;REGULATION OF METABOLISM AND PROTEIN FUNCTION","PubMed.ID":17409098,"subunits.Protein.name.":"G1/S-specific cyclin-E1;Cyclin-dependent kinase 2;Cyclin-dependent kinase inhibitor 1B ;Cyclin-dependent kinases regulatory subunit 1 ;E3 ubiquitin-protein ligase RBX1;S-phase kinase-associated protein 1;S-phase kinase-associated protein 2;Cullin-1","subunits.Gene.name.":"CCNE1;CDK2;CDKN1B;CKS1B;RBX1;SKP1;SKP2;CUL1","subunits.Gene.name.syn.":"CCNE;CDKN2;KIP1;CKS1;RNF75, ROC1;EMC19, OCP2, SKP1A, TCEB1L;FBXL1;None","Disease.comment":"Overexpression of p27 in certain cancer cells prevents DNA replication and tumor formation in nude mice, whereas the loss of p27 has been reported in many human cancers and predicts a poor prognosis in breast, prostate, colon, gastric, lung, and esophageal cancers. In several types of cancers, there is a strong correlation between the loss of p27 and induction of Skp2, a subunit of the SCFSkp2/Cks1 (Skp1, Cul1, Roc1, Skp2, Cks1 complex) ubiquitin E3 ligase that targets p27 for ubiquitination and degradation.","Subunits.comment":"None","Complex.comment":"p27, an important cell cycle regulator, blocks the G1/S transition in cells by binding and inhibiting Cdk2/cyclin A and Cdk2/cyclin E complexes. Ubiquitination and subsequent degradation play a critical role in regulating the levels of p27 during cell cycle progression.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3016,"ComplexName":"Cohesin complex, incomplete (Stag3, Sycp3)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O70576;P70281","subunits.Entrez.IDs.":"50878;20962","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0000279;GO:0007067;GO:0007059;GO:0003677;GO:0051276;GO:0005694","GO.description":"M phase;mitotic nuclear division;chromosome segregation;DNA binding;chromosome organization;chromosome","FunCat.ID":"10.03.01.01.11;10.03.04.05;16.03.01;42.10.03;70.10.03","FunCat.description":"M phase;chromosome segregation/division;DNA binding;organization of chromosome structure;chromosome","PubMed.ID":15870106,"subunits.Protein.name.":"Cohesin subunit SA-3 ;Synaptonemal complex protein 3","subunits.Gene.name.":"Stag3;Sycp3","subunits.Gene.name.syn.":";Scp3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cohesin-complex proteins ensure that sister chomatids remain paired during meiosis.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3017,"ComplexName":"Cohesin complex, incomplete (Stag3, Crest/Ss18I1)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O70576;Q8BW22","subunits.Entrez.IDs.":"50878;269397","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0000279;GO:0007067;GO:0007059;GO:0003677;GO:0051276;GO:0005694","GO.description":"M phase;mitotic nuclear division;chromosome segregation;DNA binding;chromosome organization;chromosome","FunCat.ID":"10.03.01.01.11;10.03.04.05;16.03.01;42.10.03;70.10.03","FunCat.description":"M phase;chromosome segregation/division;DNA binding;organization of chromosome structure;chromosome","PubMed.ID":15870106,"subunits.Protein.name.":"Cohesin subunit SA-3 ;Calcium-responsive transactivator","subunits.Gene.name.":"Stag3;Ss18l1","subunits.Gene.name.syn.":";Crest Kiaa0693","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cohesin-complex proteins ensure that sister chomatids remain paired during meiosis.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3018,"ComplexName":"Cohesin complex, incomplete (Sycp2, Crest/Ss18I1)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q8BW22;Q9CUU3","subunits.Entrez.IDs.":"269397;320558","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0000279;GO:0007067;GO:0007059;GO:0003677;GO:0051276;GO:0005694","GO.description":"M phase;mitotic nuclear division;chromosome segregation;DNA binding;chromosome organization;chromosome","FunCat.ID":"10.03.01.01.11;10.03.04.05;16.03.01;42.10.03;70.10.03","FunCat.description":"M phase;chromosome segregation/division;DNA binding;organization of chromosome structure;chromosome","PubMed.ID":15870106,"subunits.Protein.name.":"Calcium-responsive transactivator ;Synaptonemal complex protein 2","subunits.Gene.name.":"Ss18l1;Sycp2","subunits.Gene.name.syn.":"Crest Kiaa0693;Scp2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cohesin-complex proteins ensure that sister chomatids remain paired during meiosis.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3019,"ComplexName":"Cohesin complex, incomplete (Smc4, Crest/Ss18I1)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q8BW22;Q8CG47","subunits.Entrez.IDs.":"269397;70099","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0000279;GO:0007067;GO:0007059;GO:0003677;GO:0051276;GO:0005694","GO.description":"M phase;mitotic nuclear division;chromosome segregation;DNA binding;chromosome organization;chromosome","FunCat.ID":"10.03.01.01.11;10.03.04.05;16.03.01;42.10.03;70.10.03","FunCat.description":"M phase;chromosome segregation/division;DNA binding;organization of chromosome structure;chromosome","PubMed.ID":15870106,"subunits.Protein.name.":"Calcium-responsive transactivator ;Structural maintenance of chromosomes protein 4","subunits.Gene.name.":"Ss18l1;Smc4","subunits.Gene.name.syn.":"Crest Kiaa0693;Capc Smc4l1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cohesin-complex proteins ensure that sister chomatids remain paired during meiosis.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3020,"ComplexName":"Cohesin complex, incomplete (Rec8, Crest/Ss18I1)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q8BW22;Q8C5S7","subunits.Entrez.IDs.":"269397;56739","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0000279;GO:0007067;GO:0007059;GO:0003677;GO:0051276;GO:0005694","GO.description":"M phase;mitotic nuclear division;chromosome segregation;DNA binding;chromosome organization;chromosome","FunCat.ID":"10.03.01.01.11;10.03.04.05;16.03.01;42.10.03;70.10.03","FunCat.description":"M phase;chromosome segregation/division;DNA binding;organization of chromosome structure;chromosome","PubMed.ID":15870106,"subunits.Protein.name.":"Calcium-responsive transactivator ;Meiotic recombination protein REC8 homolog","subunits.Gene.name.":"Ss18l1;Rec8","subunits.Gene.name.syn.":"Crest Kiaa0693;Mei8 Rec8L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cohesin-complex proteins ensure that sister chomatids remain paired during meiosis.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3021,"ComplexName":"Cohesin complex, incomplete (Smc1b, Crest/Ss18I1)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q8BW22;Q920F6","subunits.Entrez.IDs.":"269397;140557","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0000279;GO:0007067;GO:0007059;GO:0003677;GO:0051276;GO:0005694","GO.description":"M phase;mitotic nuclear division;chromosome segregation;DNA binding;chromosome organization;chromosome","FunCat.ID":"10.03.01.01.11;10.03.04.05;16.03.01;42.10.03;70.10.03","FunCat.description":"M phase;chromosome segregation/division;DNA binding;organization of chromosome structure;chromosome","PubMed.ID":15870106,"subunits.Protein.name.":"Calcium-responsive transactivator ;Structural maintenance of chromosomes protein 1B","subunits.Gene.name.":"Ss18l1;Smc1b","subunits.Gene.name.syn.":"Crest Kiaa0693;Smc1l2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cohesin-complex proteins ensure that sister chomatids remain paired during meiosis.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3022,"ComplexName":"Cohesin complex, incomplete (Sycp1, Crest/Ss18I1, Rec8)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q62209;Q8BW22;Q8C5S7","subunits.Entrez.IDs.":"20957;269397;56739","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0000279;GO:0007067;GO:0007059;GO:0003677;GO:0051276;GO:0005694","GO.description":"M phase;mitotic nuclear division;chromosome segregation;DNA binding;chromosome organization;chromosome","FunCat.ID":"10.03.01.01.11;10.03.04.05;16.03.01;42.10.03;70.10.03","FunCat.description":"M phase;chromosome segregation/division;DNA binding;organization of chromosome structure;chromosome","PubMed.ID":15870106,"subunits.Protein.name.":"Synaptonemal complex protein 1 ;Calcium-responsive transactivator ;Meiotic recombination protein REC8 homolog","subunits.Gene.name.":"Sycp1;Ss18l1;Rec8","subunits.Gene.name.syn.":"Scp1;Crest Kiaa0693;Mei8 Rec8L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cohesin-complex proteins ensure that sister chomatids remain paired during meiosis.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3023,"ComplexName":"Cohesin complex, incomplete (Smc1b, Sycp1, Crest/Ss18I1)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q62209;Q8BW22;Q920F6","subunits.Entrez.IDs.":"20957;269397;140557","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0000279;GO:0007067;GO:0007059;GO:0003677;GO:0051276;GO:0005694","GO.description":"M phase;mitotic nuclear division;chromosome segregation;DNA binding;chromosome organization;chromosome","FunCat.ID":"10.03.01.01.11;10.03.04.05;16.03.01;42.10.03;70.10.03","FunCat.description":"M phase;chromosome segregation/division;DNA binding;organization of chromosome structure;chromosome","PubMed.ID":15870106,"subunits.Protein.name.":"Synaptonemal complex protein 1 ;Calcium-responsive transactivator ;Structural maintenance of chromosomes protein 1B","subunits.Gene.name.":"Sycp1;Ss18l1;Smc1b","subunits.Gene.name.syn.":"Scp1;Crest Kiaa0693;Smc1l2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cohesin-complex proteins ensure that sister chomatids remain paired during meiosis.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3024,"ComplexName":"Cohesin complex, incomplete (Smc3, Sycp1, Crest/Ss18I1)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q62209;Q8BW22;Q9CW03","subunits.Entrez.IDs.":"20957;269397;13006","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0000279;GO:0007067;GO:0007059;GO:0003677;GO:0051276;GO:0005694","GO.description":"M phase;mitotic nuclear division;chromosome segregation;DNA binding;chromosome organization;chromosome","FunCat.ID":"10.03.01.01.11;10.03.04.05;16.03.01;42.10.03;70.10.03","FunCat.description":"M phase;chromosome segregation/division;DNA binding;organization of chromosome structure;chromosome","PubMed.ID":15870106,"subunits.Protein.name.":"Synaptonemal complex protein 1 ;Calcium-responsive transactivator ;Structural maintenance of chromosomes protein 3","subunits.Gene.name.":"Sycp1;Ss18l1;Smc3","subunits.Gene.name.syn.":"Scp1;Crest Kiaa0693;Bam Bmh Cspg6 Mmip1 Smc3l1 Smcd","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cohesin-complex proteins ensure that sister chomatids remain paired during meiosis.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3025,"ComplexName":"TGF-beta receptor II-TGF-beta3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P10600;P37173","subunits.Entrez.IDs.":"7043;7048","Protein.complex.purification.method":"MI:0404- comigration in non denaturing gel electrophoresis","GO.ID":"GO:0006461;GO:0005515;GO:0007179;GO:0005886","GO.description":"protein complex assembly;protein binding;transforming growth factor beta receptor signaling pathway;plasma membrane","FunCat.ID":"14.10;16.01;30.05.01.18.01;70.02","FunCat.description":"assembly of protein complexes;protein binding;TGF-beta-receptor signalling pathway;eukaryotic plasma membrane / membrane attached","PubMed.ID":16289576,"subunits.Protein.name.":"Transforming growth factor beta-3 ;TGF-beta receptor type-2","subunits.Gene.name.":"TGFB3;TGFBR2","subunits.Gene.name.syn.":";None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TGF-beta 3 binds to TGF-beta receptor type II sequentially.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3026,"ComplexName":"TGF-beta receptor II-TGF-beta1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P01137;P37173","subunits.Entrez.IDs.":"7040;7048","Protein.complex.purification.method":"MI:0404- comigration in non denaturing gel electrophoresis","GO.ID":"GO:0006461;GO:0005515;GO:0007179;GO:0005886","GO.description":"protein complex assembly;protein binding;transforming growth factor beta receptor signaling pathway;plasma membrane","FunCat.ID":"14.10;16.01;30.05.01.18.01;70.02","FunCat.description":"assembly of protein complexes;protein binding;TGF-beta-receptor signalling pathway;eukaryotic plasma membrane / membrane attached","PubMed.ID":16289576,"subunits.Protein.name.":"Transforming growth factor beta-1;TGF-beta receptor type-2","subunits.Gene.name.":"TGFB1;TGFBR2","subunits.Gene.name.syn.":"TGFB;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TGF-beta 1 binds to TGF-beta receptor type II sequentially.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3027,"ComplexName":"TGF-beta receptor II-TGF-beta receptor I-TGF-beta1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P01137;P36897;P37173","subunits.Entrez.IDs.":"7040;7046;7048","Protein.complex.purification.method":"MI:0404- comigration in non denaturing gel electrophoresis","GO.ID":"GO:0007179;GO:0005886","GO.description":"transforming growth factor beta receptor signaling pathway;plasma membrane","FunCat.ID":"30.05.01.18.01;70.02","FunCat.description":"TGF-beta-receptor signalling pathway;eukaryotic plasma membrane / membrane attached","PubMed.ID":16289576,"subunits.Protein.name.":"Transforming growth factor beta-1;TGF-beta receptor type-1;TGF-beta receptor type-2","subunits.Gene.name.":"TGFB1;TGFBR1;TGFBR2","subunits.Gene.name.syn.":"TGFB;ALK5 SKR4;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TGF-beta receptor I does not bind TGF-beta in the absence of TGF-beta receptor II.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3028,"ComplexName":"TGF-beta receptor II-TGF-beta receptor I-TGF-beta3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P10600;P36897;P37173","subunits.Entrez.IDs.":"7043;7046;7048","Protein.complex.purification.method":"MI:0404- comigration in non denaturing gel electrophoresis","GO.ID":"GO:0007179;GO:0005886","GO.description":"transforming growth factor beta receptor signaling pathway;plasma membrane","FunCat.ID":"30.05.01.18.01;70.02","FunCat.description":"TGF-beta-receptor signalling pathway;eukaryotic plasma membrane / membrane attached","PubMed.ID":16289576,"subunits.Protein.name.":"Transforming growth factor beta-3 ;TGF-beta receptor type-1;TGF-beta receptor type-2","subunits.Gene.name.":"TGFB3;TGFBR1;TGFBR2","subunits.Gene.name.syn.":";ALK5 SKR4;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TGF-beta receptor I does not bind TGF-beta in the absence of TGF-beta receptor II.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3029,"ComplexName":"Drosha complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O35286;O35737;Q501J6;Q5HZJ0;Q61656;Q921F2;Q9D0E1;Q9EQM6","subunits.Entrez.IDs.":"13204;59013;67040;14000;13207;230908;76936;94223","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0029- cosedimentation through density gradients; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006396;GO:0003723;GO:0005634","GO.description":"RNA processing;RNA binding;nucleus","FunCat.ID":"11.04;16.03.03;70.10","FunCat.description":"RNA processing;RNA binding;nucleus","PubMed.ID":17435748,"subunits.Protein.name.":"Pre-mRNA-splicing factor ATP-dependent RNA helicase DHX15 ;Heterogeneous nuclear ribonucleoprotein H ;Probable ATP-dependent RNA helicase DDX17 ;Ribonuclease 3 ;Probable ATP-dependent RNA helicase DDX5 ;TAR DNA-binding protein 43 ;Heterogeneous nuclear ribonucleoprotein M ;Microprocessor complex subunit DGCR8","subunits.Gene.name.":"Dhx15;Hnrnph1;Ddx17;Drosha;Ddx5;Tardbp;Hnrnpm;Dgcr8","subunits.Gene.name.syn.":"Ddx15 Deah9;Hnrph Hnrph1;;Etohi2 Rn3 Rnasen;Tnz2;Tdp43;Hnrpm;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors purified the large complex of mouse Drosha and showed its function in pre-miRNA and 5.8S rRNA generation in vitro. They speculate that p68 and p72 DEAD-box RNA helicase subunits may function to specifically recognize and stably bind to certain structures of pri-miRNAs and 12S pre-rRNA, and to initiate cleavage at precise RNA sites by Drosha.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3030,"ComplexName":"TGF-beta receptor II-TGF-beta receptor I-TGF-beta1 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"Mv1Lu cells; lung","subunits.UniProt.IDs.":"P01137;P36897;P37173","subunits.Entrez.IDs.":"7040;7046;7048","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0007179;GO:0005886","GO.description":"transforming growth factor beta receptor signaling pathway;plasma membrane","FunCat.ID":"30.05.01.18.01;70.02","FunCat.description":"TGF-beta-receptor signalling pathway;eukaryotic plasma membrane / membrane attached","PubMed.ID":8051105,"subunits.Protein.name.":"Transforming growth factor beta-1;TGF-beta receptor type-1;TGF-beta receptor type-2","subunits.Gene.name.":"TGFB1;TGFBR1;TGFBR2","subunits.Gene.name.syn.":"TGFB;ALK5 SKR4;None","Disease.comment":"None","Subunits.comment":"Since TGFBR1/2 and TGF-beta1 from mink were not available in the UniProt database at the time of annotation, the orthologous human proteins were used.","Complex.comment":"TGF-beta receptor I does not bind TGF-beta in the absence of TGF-beta receptor II.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3031,"ComplexName":"TGF-beta receptor II-TGF-beta receptor I-TGF-beta1 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells; lung","subunits.UniProt.IDs.":"P01137;P36897;P37173","subunits.Entrez.IDs.":"7040;7046;7048","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0007179;GO:0005886","GO.description":"transforming growth factor beta receptor signaling pathway;plasma membrane","FunCat.ID":"30.05.01.18.01;70.02","FunCat.description":"TGF-beta-receptor signalling pathway;eukaryotic plasma membrane / membrane attached","PubMed.ID":8051105,"subunits.Protein.name.":"Transforming growth factor beta-1;TGF-beta receptor type-1;TGF-beta receptor type-2","subunits.Gene.name.":"TGFB1;TGFBR1;TGFBR2","subunits.Gene.name.syn.":"TGFB;ALK5 SKR4;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TGF-beta receptor I does not bind TGF-beta in the absence of TGF-beta receptor II.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3032,"ComplexName":"RNA-induced silencing complex, RISC","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P08238;Q15633;Q9UKV8;Q9UPY3","subunits.Entrez.IDs.":"3326;6895;27161;23405","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0032774;GO:0006396;GO:0003723;GO:0005737","GO.description":"RNA biosynthetic process;RNA processing;RNA binding;cytoplasm","FunCat.ID":"11.02;11.04;16.03.03;70.03","FunCat.description":"RNA synthesis;RNA processing;RNA binding;cytoplasm","PubMed.ID":16357216,"subunits.Protein.name.":"Heat shock protein HSP 90-beta;RISC-loading complex subunit TARBP2 ;Protein argonaute-2 ;Endoribonuclease Dicer","subunits.Gene.name.":"HSP90AB1;TARBP2;AGO2;DICER1","subunits.Gene.name.syn.":"HSP90B HSPC2 HSPCB;TRBP;EIF2C2;DICER HERNA KIAA0928","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3033,"ComplexName":"PAC3-PAC4 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q5JS54;Q9BT73","subunits.Entrez.IDs.":"389362;84262","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006461","GO.description":"protein complex assembly","FunCat.ID":"14.1","FunCat.description":"assembly of protein complexes","PubMed.ID":17707236,"subunits.Protein.name.":"Proteasome assembly chaperone 4 ;Proteasome assembly chaperone 3","subunits.Gene.name.":"PSMG4;PSMG3","subunits.Gene.name.syn.":"C6orf86 PAC4;C7orf48 PAC3","Disease.comment":"None","Subunits.comment":"Since human PAC4 was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"20S proteasome assembly is orchestrated by two distinct pairs of chaperones in mammals, the PAC1-PAC2 complex and the PAC3-PAC4 complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3034,"ComplexName":"PAC1-PAC2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95456;Q969U7","subunits.Entrez.IDs.":"8624;56984","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0050821;GO:0006457;GO:0006461","GO.description":"protein stabilization;protein folding;protein complex assembly","FunCat.ID":"14.01;14.10","FunCat.description":"protein folding and stabilization;assembly of protein complexes","PubMed.ID":16251969,"subunits.Protein.name.":"Proteasome assembly chaperone 1 ;Proteasome assembly chaperone 2","subunits.Gene.name.":"PSMG1;PSMG2","subunits.Gene.name.syn.":"C21LRP DSCR2 PAC1;HCCA3 PAC2 TNFSF5IP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"20S proteasome assembly is orchestrated by two distinct pairs of chaperones in mammals, the PAC1-PAC2 complex and the PAC3-PAC4 complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3035,"ComplexName":"LAT2-ITGB1 complex","Organism":"Human","Synonyms":"None","Cell.line":"epithelium","subunits.UniProt.IDs.":"P05556;Q9UHI5","subunits.Entrez.IDs.":"3688;23428","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016337","GO.description":"single organismal cell-cell adhesion","FunCat.ID":"34.07.01","FunCat.description":"cell-cell adhesion","PubMed.ID":11507094,"subunits.Protein.name.":"Integrin beta-1;Large neutral amino acids transporter small subunit 2","subunits.Gene.name.":"ITGB1;SLC7A8","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;LAT2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"CD98-beta1 integrin association is required for focal adhesion kinase-dependent phosphoinositol 3-hydroxykinase activation and cellular transformation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3036,"ComplexName":"Ubiquitin E3 ligase (SKP1A, SKP2, CUL1, CKS1B, RBX1)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P61024;P62877;P63208;Q13309;Q13616","subunits.Entrez.IDs.":"1163;9978;6500;6502;8454","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0000278;GO:0051726;GO:0016567;GO:0016579","GO.description":"mitotic cell cycle;regulation of cell cycle;protein ubiquitination;protein deubiquitination","FunCat.ID":"10.03.01.01;10.03.01;14.07.05","FunCat.description":"mitotic cell cycle;mitotic cell cycle and cell cycle control;modification by ubiquitination, deubiquitination","PubMed.ID":17409098,"subunits.Protein.name.":"Cyclin-dependent kinases regulatory subunit 1 ;E3 ubiquitin-protein ligase RBX1;S-phase kinase-associated protein 1;S-phase kinase-associated protein 2;Cullin-1","subunits.Gene.name.":"CKS1B;RBX1;SKP1;SKP2;CUL1","subunits.Gene.name.syn.":"CKS1;RNF75, ROC1;EMC19, OCP2, SKP1A, TCEB1L;FBXL1;None","Disease.comment":"Overexpression of p27 in certain cancer cells prevents DNA replication and tumor formation in nude mice, whereas the loss of p27 has been reported in many human cancers and predicts a poor prognosis in breast, prostate, colon, gastric, lung, and esophageal cancers. In several types of cancers, there is a strong correlation between the loss of p27 and induction of Skp2, a subunit of the SCFSkp2/Cks1 (Skp1, Cul1, Roc1, Skp2, Cks1 complex) ubiquitin E3 ligase that targets p27 for ubiquitination and degradation.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3037,"ComplexName":"Ubiquitin E3 ligase (Fbxl20, Skp1, Cul1)","Organism":"Mouse","Synonyms":"SCRAPPER","Cell.line":"nervous tissue","subunits.UniProt.IDs.":"Q9CZV8;Q9WTX5;Q9WTX6","subunits.Entrez.IDs.":"72194;21402;26965","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation;MI:0019-coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0007268;GO:0005886","GO.description":"protein ubiquitination;protein deubiquitination;synaptic transmission;plasma membrane","FunCat.ID":"14.07.05;34.03.01;70.02","FunCat.description":"modification by ubiquitination, deubiquitination;synaptic transmission;eukaryotic plasma membrane / membrane attached","PubMed.ID":17803915,"subunits.Protein.name.":"F-box/LRR-repeat protein 20;S-phase kinase-associated protein 1;Cullin-1","subunits.Gene.name.":"Fbxl20;Skp1;Cul1","subunits.Gene.name.syn.":"Fbl2;Skp1a;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SCRAPPER-dependent ubiquitination of active zone protein RIM1 regulates synaptic vesicle release.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3038,"ComplexName":"SMAD2-SMAD4-FAST1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75593;Q13485;Q15796","subunits.Entrez.IDs.":"8928;4089;4087","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045893;GO:0003677;GO:0007179;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"11.02.03.04.01;16.03.01;30.05.01.18.01;70.10","FunCat.description":"transcription activation;DNA binding;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":9389648,"subunits.Protein.name.":"Forkhead box protein H1 ;Mothers against decapentaplegic homolog 4;Mothers against decapentaplegic homolog 2","subunits.Gene.name.":"FOXH1;SMAD4;SMAD2","subunits.Gene.name.syn.":"FAST1 FAST2;DPC4 MADH4;MADH2, MADR2","Disease.comment":"SMAD4 is involved in pancreatic carcinoma.","Subunits.comment":"None","Complex.comment":"This complex is built only in the presence of TGF-beta signaling.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3039,"ComplexName":"SMAD2-FAST1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75593;Q15796","subunits.Entrez.IDs.":"8928;4087","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0003677;GO:0007179;GO:0005634","GO.description":"DNA binding;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"16.03.01;30.05.01.18.01;70.10","FunCat.description":"DNA binding;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":9389648,"subunits.Protein.name.":"Forkhead box protein H1 ;Mothers against decapentaplegic homolog 2","subunits.Gene.name.":"FOXH1;SMAD2","subunits.Gene.name.syn.":"FAST1 FAST2;MADH2, MADR2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TGF-beta induces formation of the SMAD2-FAST1 complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3040,"ComplexName":"Multisynthetase complex","Organism":"Human","Synonyms":"Aminoacyl tRNAsynthetase multienzyme complex","Cell.line":"None","subunits.UniProt.IDs.":"O43324;P07814;P14868;P41252;P47897;P54136;P56192;Q12904;Q13155;Q15046;Q9P2J5","subunits.Entrez.IDs.":"9521;2058;1615;3376;5859;5917;4141;9255;7965;3735;51520","Protein.complex.purification.method":"MI:0028- cosedimentation in solution; MI:0226- ion exchange chromatography","GO.ID":"GO:0004812;GO:0005737;GO:0005634","GO.description":"aminoacyl-tRNA ligase activity;cytoplasm;nucleus","FunCat.ID":"12.10;70.03;70.10","FunCat.description":"aminoacyl-tRNA-synthetases;cytoplasm;nucleus","PubMed.ID":16169847,"subunits.Protein.name.":"Eukaryotic translation elongation factor 1 epsilon-1 ;Bifunctional glutamate/proline--tRNA ligase ;Aspartate--tRNA ligase, cytoplasmic ;Isoleucine--tRNA ligase, cytoplasmic ;Glutamine--tRNA ligase ;Arginine--tRNA ligase, cytoplasmic ;Methionine--tRNA ligase, cytoplasmic ;Aminoacyl tRNA synthase complex-interacting multifunctional protein 1 ;Aminoacyl tRNA synthase complex-interacting multifunctional protein 2 ;Lysine--tRNA ligase ;Leucine--tRNA ligase, cytoplasmic","subunits.Gene.name.":"EEF1E1;EPRS;DARS;IARS;QARS;RARS;MARS;AIMP1;AIMP2;KARS;LARS","subunits.Gene.name.syn.":"AIMP3 P18;GLNS PARS QARS QPRS;;;;;;EMAP2 SCYE1;JTV1;KIAA0070;KIAA1352","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The characteristic core complex of aminoacyl tRNAsynthetase in higher eukaryotes is composed of nine synthetase activities. These are specific for arginine, aspartate, glutamate, glutamine, isoleucine, leucine, lysine, methionine, and proline. There are also three auxiliary proteins in the multisynthetase complex: p43, p38, and p18. These are involved in protein-protein interactions within the particle and with other protein synthesis factors.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3041,"ComplexName":"TGF-beta-receptor type II homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P37173","subunits.Entrez.IDs.":"7048","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0005515;GO:0007179;GO:0005886","GO.description":"protein binding;transforming growth factor beta receptor signaling pathway;plasma membrane","FunCat.ID":"16.01;30.05.01.18.01;70.02","FunCat.description":"protein binding;TGF-beta-receptor signalling pathway;eukaryotic plasma membrane / membrane attached","PubMed.ID":7521335,"subunits.Protein.name.":"TGF-beta receptor type-2","subunits.Gene.name.":"TGFBR2","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TGF-beta receptor type II forms a homomeric complex in the absence of the ligand TGF-beta.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":3042,"ComplexName":"TGF-beta-receptor II-TGF-beta1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P01137;P37173","subunits.Entrez.IDs.":"7040;7048","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006461;GO:0005515;GO:0007179;GO:0005886","GO.description":"protein complex assembly;protein binding;transforming growth factor beta receptor signaling pathway;plasma membrane","FunCat.ID":"14.10;16.01;30.05.01.18.01;70.02","FunCat.description":"assembly of protein complexes;protein binding;TGF-beta-receptor signalling pathway;eukaryotic plasma membrane / membrane attached","PubMed.ID":7521335,"subunits.Protein.name.":"Transforming growth factor beta-1;TGF-beta receptor type-2","subunits.Gene.name.":"TGFB1;TGFBR2","subunits.Gene.name.syn.":"TGFB;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3043,"ComplexName":"BMP2-BRIA complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12643;P12644;P36894","subunits.Entrez.IDs.":"650;652;657","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0007179;GO:0010074;GO:0051216;GO:0001503;GO:0030316","GO.description":"transforming growth factor beta receptor signaling pathway;maintenance of meristem identity;cartilage development;ossification;osteoclast differentiation","FunCat.ID":"30.05.01.18.01;41.05.04;45.03.05.05;41.05.17;45.03.05.07","FunCat.description":"TGF-beta-receptor signalling pathway;embryogenesis;cartilage;osteogenesis;bone","PubMed.ID":10881198,"subunits.Protein.name.":"Bone morphogenetic protein 2 ;Bone morphogenetic protein 4 ;Bone morphogenetic protein receptor type-1A","subunits.Gene.name.":"BMP2;BMP4;BMPR1A","subunits.Gene.name.syn.":"BMP2A;BMP2B DVR4;ACVRLK3 ALK3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3044,"ComplexName":"SKI-NCOR1-SIN3A-HDAC1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75376;P12755;Q13547;Q96ST3","subunits.Entrez.IDs.":"9611;6497;3065;25942","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;DNA binding;organization of chromosome structure;nucleus","PubMed.ID":10049357,"subunits.Protein.name.":"Nuclear receptor corepressor 1;Ski oncogene ;Histone deacetylase 1;Paired amphipathic helix protein Sin3a","subunits.Gene.name.":"NCOR1;SKI;HDAC1;SIN3A","subunits.Gene.name.syn.":"KIAA1047;;RPD3L1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The oncogenic form of Ski, v-Ski, which lacks the mSin3A binding domain, abrogates transcriptional repression.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3045,"ComplexName":"hs4 enhancer complex (faster migrating complex)","Organism":"Human","Synonyms":"None","Cell.line":"B-cell","subunits.UniProt.IDs.":"P09086;P14859;P19838;P25490;Q04206","subunits.Entrez.IDs.":"5452;5451;4790;7528;5970","Protein.complex.purification.method":"MI:0412-electrophoretic mobility supershift assay","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0007249;GO:0030183;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;I-kappaB kinase/NF-kappaB signaling;B cell differentiation;nucleus","FunCat.ID":"11.02.03.04;16.03.01;30.01.05.01.04;43.03.07.02.01.01;70.10","FunCat.description":"transcriptional control;DNA binding;NIK-I-kappaB/NF-kappaB cascade;B-cell;nucleus","PubMed.ID":14707079,"subunits.Protein.name.":"POU domain, class 2, transcription factor 2;POU domain, class 2, transcription factor 1;Nuclear factor NF-kappa-B p105 subunit;Transcriptional repressor protein YY1;Transcription factor p65","subunits.Gene.name.":"POU2F2;POU2F1;NFKB1;YY1;RELA","subunits.Gene.name.syn.":"OCT2 OTF2;OCT1 OTF1;None;INO80S;NFKB3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex exists in healthy and malignant B-cell lines.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3046,"ComplexName":"hs4 enhancer complex (slow migrating complex)","Organism":"Human","Synonyms":"None","Cell.line":"B-cell","subunits.UniProt.IDs.":"P25490;Q01201","subunits.Entrez.IDs.":"7528;5971","Protein.complex.purification.method":"MI:0412-electrophoretic mobility supershift assay;MI:0402-chromatin immunoprecipitation assays;MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0007249;GO:0043066;GO:0030183;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;I-kappaB kinase/NF-kappaB signaling;negative regulation of apoptotic process;B cell differentiation;nucleus","FunCat.ID":"11.02.03.04;16.03.01;30.01.05.01.04;40.10.02.01;43.03.07.02.01.01;70.10","FunCat.description":"transcriptional control;DNA binding;NIK-I-kappaB/NF-kappaB cascade;anti-apoptosis;B-cell;nucleus","PubMed.ID":14707079,"subunits.Protein.name.":"Transcriptional repressor protein YY1;Transcription factor RelB","subunits.Gene.name.":"YY1;RELB","subunits.Gene.name.syn.":"INO80S;None","Disease.comment":"This complex was observed only in patients with diffuse large B cell lymphoma (DLBCA).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3047,"ComplexName":"Parvulin-associated pre-rRNP complex","Organism":"Mouse","Synonyms":"Parvulin-associated preribosomal ribonucleoprotein complex","Cell.line":"None","subunits.UniProt.IDs.":"O09167;O43143;O76021;O95995;P09405;P11276;P12970;P14148;P14869;P19253;P21127;P27635;P27659;P35550;P35980;P46781;P47911;P47962;P47963;P53569;P56183;P61255;P62242;P62702;P62717;P62754;P62906;P62908;P62918;P68363;P84099;P97351;P97452;P99024;Q61656;Q6DFW4;Q7TPV4;Q8K363;Q91VE6;Q921N6;Q922K7;Q99LH1;Q99ME9;Q9BWT6;Q9CR57;Q9CYH6;Q9CZM2;Q9D0I8;Q9D0R4;Q9D6Z1;Q9D8E6;Q9D8N0;Q9D903;Q9DBE9;Q9EQ61;Q9ESV0;Q9JIK5;Q9JJ80;Q9JJA4;Q9NW13;Q9ULW0;Q9Y237","subunits.Entrez.IDs.":"19933;1665;26156;2622;17975;14268;27176;19989;11837;22121;984;6134;27367;14113;19899;6203;19988;19983;270106;12607;18114;19941;20116;20102;76808;20104;4736;27050;26961;10376;19921;20091;12181;22154;13207;55989;18432;66942;67949;228889;110109;230737;69237;84057;67115;59014;66480;69902;52513;67134;67891;67160;69072;56095;64934;27225;56200;67239;57750;55131;22974;5303","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation; MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0042254;GO:0005634","GO.description":"ribosome biogenesis;nucleus","FunCat.ID":"12.01;70.10","FunCat.description":"ribosome biogenesis;nucleus","PubMed.ID":11960984,"subunits.Protein.name.":"60S ribosomal protein L21;Pre-mRNA-splicing factor ATP-dependent RNA helicase DHX15 ;Ribosomal L1 domain-containing protein 1 ;Growth arrest-specific protein 8 ;Nucleolin;Fibronectin ;60S ribosomal protein L7a ;60S ribosomal protein L7;60S acidic ribosomal protein P0 ;60S ribosomal protein L13a ;Cyclin-dependent kinase 11B ;60S ribosomal protein L10;60S ribosomal protein L3 ;rRNA 2'-O-methyltransferase fibrillarin ;60S ribosomal protein L18;40S ribosomal protein S9;60S ribosomal protein L6 ;60S ribosomal protein L5;60S ribosomal protein L13 ;CCAAT/enhancer-binding protein zeta ;Ribosomal RNA processing protein 1 homolog A ;60S ribosomal protein L26 ;40S ribosomal protein S8;40S ribosomal protein S4, X isoform;60S ribosomal protein L18a;40S ribosomal protein S6 ;60S ribosomal protein L10a;40S ribosomal protein S3 ;60S ribosomal protein L8;Tubulin alpha-1B chain ;60S ribosomal protein L19;40S ribosomal protein S3a ;Ribosome biogenesis protein BOP1 ;Tubulin beta-5 chain;Probable ATP-dependent RNA helicase DDX5 ;Nucleolar protein 58 ;Myb-binding protein 1A ;ATP-dependent RNA helicase DDX18 ;MKI67 FHA domain-interacting nucleolar phosphoprotein ;Probable ATP-dependent RNA helicase DDX27 ;Probable 28S rRNA ;Nucleolar GTP-binding protein 2;Nucleolar GTP-binding protein 1 ;Meiotic nuclear division protein 1 homolog;60S ribosomal protein L14;Ribosome biogenesis regulatory protein homolog;60S ribosomal protein L15;mRNA turnover protein 4 homolog ;Probable ATP-dependent RNA helicase DDX56 ;Nucleolar protein 56 ;60S ribosomal protein L4;Elongation factor 1-gamma ;Probable rRNA-processing protein EBP2;pre-rRNA processing protein FTSJ3 ;Pescadillo homolog;ATP-dependent RNA helicase DDX24 ;Nucleolar RNA helicase 2 ;Ribosome production factor 2 homolog ;Ribosome biogenesis protein WDR12 ;RNA-binding protein 28 ;Targeting protein for Xklp2 ;Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4","subunits.Gene.name.":"Rpl21;DHX15;RSL1D1;GAS8;Ncl;Fn1;Rpl7a;Rpl7;Rplp0;Rpl13a;CDK11B;RPL10;Rpl3;Fbl;Rpl18;RPS9;Rpl6;Rpl5;Rpl13;Cebpz;Rrp1;Rpl26;Rps8;Rps4x;Rpl18a;Rps6;RPL10A;Rps3;Rpl8;TUBA1B;Rpl19;Rps3a;Bop1;Tubb5;Ddx5;Nop58;Mybbp1a;Ddx18;Nifk;Ddx27;Nop2;Gnl2;Gtpbp4;MND1;Rpl14;Rrs1;Rpl15;Mrto4;Ddx56;Nop56;Rpl4;Eef1g;Ebna1bp2;Ftsj3;Pes1;Ddx24;Ddx21;Rpf2;Wdr12;RBM28;TPX2;PIN4","subunits.Gene.name.syn.":";DBP1 DDX15;CATX11 CSIG PBK1;GAS11;Nuc;;Surf-3 Surf3;;Arbp;P198 Tstap198-7;CDC2L1 CDK11 PITSLREA PK58;DXS648E QM;;;;None;;;;Cbf2 Cebpa-rs1;Nnp1;;;Rps4;;;NEDD6;;;;;Rps3a1;Kiaa0124;;Tnz2;Nol5;P160;;Mki67ip;;Nol1;;Crfg Nog1;GAJ;;Rrr;;Mrt4;D11Ertd619e Noh61;Nol5a;;;Ebp2;;Pes;;;Bxdc1;;;C20orf1 C20orf2 DIL2 HCA519;","Disease.comment":"None","Subunits.comment":"Since human and mouse cell lines were investigated, not all of the identified protein are from mouse.","Complex.comment":"The authors propose that the hParvulin-associating rRNP complexes isolated represent those formed during postmitotic nucleolar reformation before rDNA transcription or premitotic nucleolar disassembly.","SWISSPROT.organism":"Mus musculus (Mouse);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Homo sapiens (Human);Homo sapiens (Human);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Homo sapiens (Human);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Homo sapiens (Human);Mus musculus (Mouse);Mus musculus (Mouse);Homo sapiens (Human);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Homo sapiens (Human);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3048,"ComplexName":"mSin3A complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q09028;Q13547;Q16576;Q92769;Q96ST3","subunits.Entrez.IDs.":"5928;3065;5931;3066;25942","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;DNA binding;organization of chromosome structure;nucleus","PubMed.ID":9150133,"subunits.Protein.name.":"Histone-binding protein RBBP4;Histone deacetylase 1;Histone-binding protein RBBP7;Histone deacetylase 2;Paired amphipathic helix protein Sin3a","subunits.Gene.name.":"RBBP4;HDAC1;RBBP7;HDAC2;SIN3A","subunits.Gene.name.syn.":"RBAP48;RPD3L1;RBAP46;None;None","Disease.comment":"None","Subunits.comment":"Three other subunits of the complex were found in the analysis, which have not been further characterized: p250, p180, p30.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3049,"ComplexName":"Mad-Max-mSin3a complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P28574;P50538;Q60520","subunits.Entrez.IDs.":"17187;17119;20466","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0045892;GO:0003677;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04.03;16.03.01;70.10","FunCat.description":"transcription repression;DNA binding;nucleus","PubMed.ID":7889570,"subunits.Protein.name.":"Protein max ;Max dimerization protein 1 ;Paired amphipathic helix protein Sin3a","subunits.Gene.name.":"Max;Mxd1;Sin3a","subunits.Gene.name.syn.":"Myn;Mad Mad1;Kiaa4126","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Mad-Max represses transcription by tethering mSin3 to DNA as a corepressor.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3050,"ComplexName":"Mad-Max-mSin3B complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P28574;P50538;Q62141","subunits.Entrez.IDs.":"17187;17119;20467","Protein.complex.purification.method":"MI:0412- electrophoretic mobility supershift assay","GO.ID":"GO:0045892;GO:0003677;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04.03;16.03.01;70.10","FunCat.description":"transcription repression;DNA binding;nucleus","PubMed.ID":7889570,"subunits.Protein.name.":"Protein max ;Max dimerization protein 1 ;Paired amphipathic helix protein Sin3b","subunits.Gene.name.":"Max;Mxd1;Sin3b","subunits.Gene.name.syn.":"Myn;Mad Mad1;Kiaa0700","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Mad-Max represses transcription by tethering mSin3 to DNA as a corepressor.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3051,"ComplexName":"MAD-MAX complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P61244;Q05195","subunits.Entrez.IDs.":"4149;4084","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0045892;GO:0003677;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04.03;16.03.01;70.10","FunCat.description":"transcription repression;DNA binding;nucleus","PubMed.ID":8224841,"subunits.Protein.name.":"Protein max ;Max dimerization protein 1","subunits.Gene.name.":"MAX;MXD1","subunits.Gene.name.syn.":"BHLHD4;MAD","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cell differentiation is accompanied by a change from MYC-MAX complexes (undifferentiated cells) to MAD-MAX complexes (differentiated cells). The ability of MAD to compete with MYC for binding to MAX and to repress MYC transcriptional activation suggests that MAD opposes the function of MYC.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3052,"ComplexName":"MYC-MAX complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P01106;P61244","subunits.Entrez.IDs.":"4609;4149","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0045893;GO:0003677;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04.01;16.03.01;70.10","FunCat.description":"transcription activation;DNA binding;nucleus","PubMed.ID":8224841,"subunits.Protein.name.":"Myc proto-oncogene protein ;Protein max","subunits.Gene.name.":"MYC;MAX","subunits.Gene.name.syn.":"BHLHE39;BHLHD4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cell differentiation is accompanied by a change from MYC-MAX complexes (undifferentiated cells) to MAD-MAX complexes (differentiated cells). The ability of MAD to compete with MYC for binding to MAX and to repress MYC transcriptional activation suggests that MAD opposes the function of MYC.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3053,"ComplexName":"mSin3A-HDAC1-HDAC2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q13547;Q92769;Q96ST3","subunits.Entrez.IDs.":"3065;3066;25942","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;organization of chromosome structure;nucleus","PubMed.ID":9150134,"subunits.Protein.name.":"Histone deacetylase 1;Histone deacetylase 2;Paired amphipathic helix protein Sin3a","subunits.Gene.name.":"HDAC1;HDAC2;SIN3A","subunits.Gene.name.syn.":"RPD3L1;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3054,"ComplexName":"MAD1-mSin3A-HDAC2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q05195;Q92769;Q96ST3","subunits.Entrez.IDs.":"4084;3066;25942","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:2001141;GO:0006355;GO:0006473;GO:0006476;GO:0051276;GO:0005634","GO.description":"DNA topological change;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04;14.07.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcriptional control;modification by acetylation, deacetylation;organization of chromosome structure;nucleus","PubMed.ID":9150134,"subunits.Protein.name.":"Max dimerization protein 1 ;Histone deacetylase 2;Paired amphipathic helix protein Sin3a","subunits.Gene.name.":"MXD1;HDAC2;SIN3A","subunits.Gene.name.syn.":"MAD;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"MAD-MAX complex functions as transcriptional repressor by recruiting the mSin3A-HDAC complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3055,"ComplexName":"Nop56p-associated pre-rRNA complex","Organism":"Human","Synonyms":"Nop56p-associated pre-ribosomal ribonucleoprotein complex","Cell.line":"None","subunits.UniProt.IDs.":"O00567;O76021;P05141;P05386;P05387;P05388;P06748;P08708;P09651;P11387;P13639;P15880;P16402;P18077;P18124;P18621;P19338;P22087;P25398;P26368;P26373;P27635;P30050;P32969;P35268;P36578;P37108;P39023;P40429;P42766;P46776;P46777;P46778;P46779;P46781;P47914;P49411;P50914;P52272;P55209;P55769;P61247;P61254;P61313;P61353;P61513;P62081;P62241;P62244;P62249;P62263;P62266;P62269;P62273;P62277;P62280;P62424;P62736;P62750;P62753;P62829;P62841;P62847;P62888;P62891;P62899;P62906;P62910;P62913;P62917;P63267;P67809;P68104;P83731;P83881;P84098;Q00839;Q01081;Q02543;Q02878;Q07020;Q08211;Q12905;Q12906;Q13428;Q13610;Q14978;Q6P3W7;Q71U36;Q8TDN6;Q92522;Q96SB4;Q99848;Q99879;Q9BQG0;Q9BVP2;Q9H4B7;Q9NR30;Q9NW13;Q9NX58;Q9NZI8;Q9Y2X3;Q9Y383;Q9Y3U8","subunits.Entrez.IDs.":"10528;26156;292;6176;6181;6175;4869;6218;3178;7150;1938;6187;3007;6165;6129;6139;4691;2091;6206;11338;6137;6134;6136;6133;6146;6124;6727;6122;23521;11224;6157;6125;6144;6158;6203;6159;7284;9045;4670;4673;4809;6189;6154;6138;6155;6168;6201;6202;6210;6217;6208;6228;6222;6235;6207;6205;6130;59;6147;6194;9349;6209;6229;6156;6170;6160;4736;6161;6135;6132;72;4904;1915;6152;6173;6143;3192;7307;6142;6128;6141;1660;3608;3609;6949;11137;9221;55681;7846;55299;8971;6732;10969;8342;10514;26354;81027;9188;55131;55646;10642;51602;51631;25873","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation; MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0042254;GO:0005634","GO.description":"ribosome biogenesis;nucleus","FunCat.ID":"12.01;70.10","FunCat.description":"ribosome biogenesis;nucleus","PubMed.ID":12777385,"subunits.Protein.name.":"Nucleolar protein 56 ;Ribosomal L1 domain-containing protein 1 ;ADP/ATP translocase 2;60S acidic ribosomal protein P1;60S acidic ribosomal protein P2;60S acidic ribosomal protein P0;Nucleophosmin ;40S ribosomal protein S17;Heterogeneous nuclear ribonucleoprotein A1 ;DNA topoisomerase 1;Elongation factor 2 ;40S ribosomal protein S2;Histone H1.3 ;60S ribosomal protein L35a;60S ribosomal protein L7;60S ribosomal protein L17;Nucleolin ;rRNA 2'-O-methyltransferase fibrillarin;40S ribosomal protein S12;Splicing factor U2AF 65 kDa subunit ;60S ribosomal protein L13;60S ribosomal protein L10;60S ribosomal protein L12;60S ribosomal protein L9;60S ribosomal protein L22;60S ribosomal protein L4;Signal recognition particle 14 kDa protein ;60S ribosomal protein L3;60S ribosomal protein L13a;60S ribosomal protein L35;60S ribosomal protein L27a;60S ribosomal protein L5;60S ribosomal protein L21;60S ribosomal protein L28;40S ribosomal protein S9;60S ribosomal protein L29;Elongation factor Tu, mitochondrial ;60S ribosomal protein L14;Heterogeneous nuclear ribonucleoprotein M ;Nucleosome assembly protein 1-like 1 ;NHP2-like protein 1 ;40S ribosomal protein S3a;60S ribosomal protein L26;60S ribosomal protein L15;60S ribosomal protein L27;60S ribosomal protein L37a;40S ribosomal protein S7;40S ribosomal protein S8;40S ribosomal protein S15a;40S ribosomal protein S16;40S ribosomal protein S14;40S ribosomal protein S23;40S ribosomal protein S18;40S ribosomal protein S29;40S ribosomal protein S13;40S ribosomal protein S11;60S ribosomal protein L7a;Actin, aortic smooth muscle ;60S ribosomal protein L23a;40S ribosomal protein S6;60S ribosomal protein L23;40S ribosomal protein S15;40S ribosomal protein S24;60S ribosomal protein L30;60S ribosomal protein L39;60S ribosomal protein L31;60S ribosomal protein L10a;60S ribosomal protein L32;60S ribosomal protein L11;60S ribosomal protein L8;Actin, gamma-enteric smooth muscle ;Nuclease-sensitive element-binding protein 1 ;Elongation factor 1-alpha 1 ;60S ribosomal protein L24;60S ribosomal protein L36a;60S ribosomal protein L19;Heterogeneous nuclear ribonucleoprotein U ;Splicing factor U2AF 35 kDa subunit ;60S ribosomal protein L18a;60S ribosomal protein L6;60S ribosomal protein L18;ATP-dependent RNA helicase A ;Interleukin enhancer-binding factor 2 ;Interleukin enhancer-binding factor 3 ;Treacle protein ;Periodic tryptophan protein 1 homolog ;Nucleolar and coiled-body phosphoprotein 1 ;SCY1-like protein 2 ;Tubulin alpha-1A chain;Ribosome biogenesis protein BRX1 homolog ;Histone H1x;SRSF protein kinase 1 ;Probable rRNA-processing protein EBP2 ;Histone H2B type 1-M ;Myb-binding protein 1A;Guanine nucleotide-binding protein-like 3 ;Tubulin beta-1 chain;Nucleolar RNA helicase 2 ;RNA-binding protein 28 ;Cell growth-regulating nucleolar protein;Insulin-like growth factor 2 mRNA-binding protein 1 ;Nucleolar protein 58 ;Putative RNA-binding protein Luc7-like 2;60S ribosomal protein L36","subunits.Gene.name.":"NOP56;RSL1D1;SLC25A5;RPLP1;RPLP2;RPLP0;NPM1;RPS17;HNRNPA1;TOP1;EEF2;RPS2;HIST1H1D;RPL35A;RPL7;RPL17;NCL;FBL;RPS12;U2AF2;RPL13;RPL10;RPL12;RPL9; RPL9;RPL22;RPL4;SRP14;RPL3;RPL13A;RPL35;RPL27A;RPL5;RPL21;RPL28;RPS9;RPL29;TUFM;RPL14;HNRNPM;NAP1L1;SNU13;RPS3A;RPL26;RPL15;RPL27;RPL37A;RPS7;RPS8;RPS15A;RPS16;RPS14;RPS23;RPS18;RPS29;RPS13;RPS11;RPL7A;ACTA2;RPL23A;RPS6;RPL23;RPS15;RPS24;RPL30;RPL39;RPL31;RPL10A;RPL32;RPL11;RPL8;ACTG2;YBX1;EEF1A1;RPL24;RPL36A;RPL19;HNRNPU;U2AF1;RPL18A;RPL6;RPL18;DHX9;ILF2;ILF3;TCOF1;PWP1;NOLC1;SCYL2;TUBA1A;BRIX1;H1FX;SRPK1;EBNA1BP2;HIST1H2BM;MYBBP1A;GNL3;TUBB1;DDX21;RBM28;LYAR;IGF2BP1;NOP58;LUC7L2;RPL36","subunits.Gene.name.syn.":"NOL5A;CATX11 CSIG PBK1;ANT2;RRP1;D11S2243E RPP2;None;NPM;RPS17L;HNRPA1;None;EF2;RPS4;H1F3;None;None;None;;FIB1 FLRN;None;U2AF65;BBC1;DXS648E QM;None;; ; ;;None;RPL1;;None;None;None;None;None;None;None;None;None;;None;HNRPM NAGR1;NRP;NHP2L1;FTE1 MFTL;None;EC45;None;None;None;None;None;None;None;None;D6S218E;None;None;None;SURF-3 SURF3;ACTSA ACTVS;None;None;None;RIG;None;None;None;None;NEDD6;None;None;None;ACTA3 ACTL3 ACTSG;NSEP1 YB1;EEF1A EF1A LENG7;None;RPL44;None;HNRPU SAFA U21.1;U2AF35 U2AFBP;None;TXREB1;None;DDX9 LKP NDH2;NF45;DRBF MPHOSPH4 NF90;;;KIAA0035 NS5ATP13;CVAK104 KIAA1360;TUBA3;BRIX BXDC2;;;EBP2;H2BFE;P160;E2IG3 NS;None;;;;CRDBP VICKZ1 ZBP1;NOL5 NOP5;;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Identification of pre-rRNA species within hNop56p-associated pre-ribosomal ribonucleoprotein complexes, coupled with the known functions of yeast orthologs of the probable trans-acting factors identified in man, demonstrated that hNop56p functions in the early to middle stages of 60 S subunit synthesis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3056,"ComplexName":"Microprocessor complex","Organism":"Human","Synonyms":"small Drosha complex (DGCR8-DROSHA)","Cell.line":"None","subunits.UniProt.IDs.":"Q8WYQ5;Q9NRR4","subunits.Entrez.IDs.":"54487;29102","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation; MI:0071- molecular sieving","GO.ID":"GO:0006396;GO:0003723;GO:0005634","GO.description":"RNA processing;RNA binding;nucleus","FunCat.ID":"11.04;16.03.03;70.10","FunCat.description":"RNA processing;RNA binding;nucleus","PubMed.ID":15531877,"subunits.Protein.name.":"Microprocessor complex subunit DGCR8 ;Ribonuclease 3","subunits.Gene.name.":"DGCR8;DROSHA","subunits.Gene.name.syn.":"C22orf12 DGCRK6;RN3 RNASE3L RNASEN","Disease.comment":"DGCR8 is deleted in DiGeorge syndrome.","Subunits.comment":"None","Complex.comment":"This complex is responsible for pre-miRNA processing.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3057,"ComplexName":"ITGA10-ITGB1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75578;P05556","subunits.Entrez.IDs.":"8515;3688","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0019- coimmunoprecipitation","GO.ID":"GO:0051211","GO.description":"anisotropic cell growth","FunCat.ID":"40.01.03","FunCat.description":"directional cell growth (morphogenesis)","PubMed.ID":9685391,"subunits.Protein.name.":"Integrin alpha-10;Integrin beta-1","subunits.Gene.name.":"ITGA10;ITGB1","subunits.Gene.name.syn.":";FNRB MDF2 MSK12","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3058,"ComplexName":"ITGA11-ITGB1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P05556;Q9UKX5","subunits.Entrez.IDs.":"3688;22801","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515;GO:0016477","GO.description":"protein binding;cell migration","FunCat.ID":"16.01;34.05.01","FunCat.description":"protein binding;cell migration","PubMed.ID":10464311,"subunits.Protein.name.":"Integrin beta-1;Integrin alpha-11","subunits.Gene.name.":"ITGB1;ITGA11","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3059,"ComplexName":"ITGA11-ITGB1-COL1A1 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P02452;P05556;Q9UKX5","subunits.Entrez.IDs.":"1277;3688;22801","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0004- affinity chromatography technologies","GO.ID":"GO:0007229","GO.description":"integrin-mediated signaling pathway","FunCat.ID":"30.05.02.26","FunCat.description":"integrin receptor signalling pathway","PubMed.ID":10464311,"subunits.Protein.name.":"Collagen alpha-1;Integrin beta-1;Integrin alpha-11","subunits.Gene.name.":"COL1A1;ITGB1;ITGA11","subunits.Gene.name.syn.":";FNRB MDF2 MSK12;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3060,"ComplexName":"RNA polymerase II complex (RPB1, RAP74, CDK8, CYCC, SRB7, BAF190, BAF47), chromatin structure modifying","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"P24863;P24928;P35269;P49336;P51531;Q12824;Q13503","subunits.Entrez.IDs.":"892;5430;2962;1024;6595;6598;9412","Protein.complex.purification.method":"MI:0047-far western blotting","GO.ID":"GO:0006265;GO:0006351;GO:0003677;GO:0005634","GO.description":"DNA topological change;transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"10.01.09.05;11;16.03.01;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);TRANSCRIPTION;DNA binding;nucleus","PubMed.ID":9710619,"subunits.Protein.name.":"Cyclin-C;DNA-directed RNA polymerase II subunit RPB1;General transcription factor IIF subunit 1;Cyclin-dependent kinase 8;Probable global transcription activator SNF2L2;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;Mediator of RNA polymerase II transcription subunit 21","subunits.Gene.name.":"CCNC;POLR2A;GTF2F1;CDK8;SMARCA2;SMARCB1;MED21","subunits.Gene.name.syn.":"None;POLR2;RAP74;None;BAF190B, BRM, SNF2A, SNF2L2;BAF47, INI1, SNF5L1;SRB7 SURB7","Disease.comment":"None","Subunits.comment":"Since the authors did not specify SNF2 (= SMARCA), we used isoform SNF2A (=SMARCA2).","Complex.comment":"RNA polymerase II complex contains chromatin structure remodeling activity and histone acetyltransferase activity.Notably, the general transcription factors are absent from this complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3061,"ComplexName":"RNA polymerase II complex (CBP, PCAF, RPB1, BAF47, CYCC, CDK8), chromatin structure modifying","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"P24863;P24928;P49336;Q12824;Q92793;Q92831","subunits.Entrez.IDs.":"892;5430;1024;6598;1387;8850","Protein.complex.purification.method":"MI:0226- ion exchange chromatography","GO.ID":"GO:0006265;GO:0006351;GO:0003677;GO:0005634","GO.description":"DNA topological change;transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"10.01.09.05;11;16.03.01;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);TRANSCRIPTION;DNA binding;nucleus","PubMed.ID":9710619,"subunits.Protein.name.":"Cyclin-C;DNA-directed RNA polymerase II subunit RPB1;Cyclin-dependent kinase 8;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;CREB-binding protein;Histone acetyltransferase KAT2B","subunits.Gene.name.":"CCNC;POLR2A;CDK8;SMARCB1;CREBBP;KAT2B","subunits.Gene.name.syn.":"None;POLR2;None;BAF47, INI1, SNF5L1;CBP;PCAF","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"RNA polymerase II complex contains chromatin structure remodeling activity and histone acetyltransferase activity. Notably, the general transcription factors are absent from this complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3062,"ComplexName":"RNA polymerase II complex, incomplete (CBP, RPBI, PCAF, BAF47), chromatin structure modifying","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"P24928;Q12824;Q92793;Q92831","subunits.Entrez.IDs.":"5430;6598;1387;8850","Protein.complex.purification.method":"MI:0047- far western blotting; MI:0019- coimmunoprecipitation","GO.ID":"GO:0006265;GO:0006351;GO:0003677;GO:0005634","GO.description":"DNA topological change;transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"10.01.09.05;11;16.03.01;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);TRANSCRIPTION;DNA binding;nucleus","PubMed.ID":9710619,"subunits.Protein.name.":"DNA-directed RNA polymerase II subunit RPB1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;CREB-binding protein;Histone acetyltransferase KAT2B","subunits.Gene.name.":"POLR2A;SMARCB1;CREBBP;KAT2B","subunits.Gene.name.syn.":"POLR2;BAF47, INI1, SNF5L1;CBP;PCAF","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"RNA polymerase II complex contains chromatin structure remodeling activity and histone acetyltransferase activity. Notably, the general transcription factors are absent from this complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3063,"ComplexName":"Brg1-associated complex II","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14497;O14744;O96019;P51532;Q12824;Q8TAQ2;Q92922","subunits.Entrez.IDs.":"8289;10419;86;6597;6598;6601;6599","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006265;GO:2001141;GO:0006355;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcriptional control;DNA binding;organization of chromosome structure;nucleus","PubMed.ID":11238380,"subunits.Protein.name.":"AT-rich interactive domain-containing protein 1A;Protein arginine N-methyltransferase 5;Actin-like protein 6A;Transcription activator BRG1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;SWI/SNF complex subunit SMARCC2;SWI/SNF complex subunit SMARCC1","subunits.Gene.name.":"ARID1A;PRMT5;ACTL6A;SMARCA4;SMARCB1;SMARCC2;SMARCC1","subunits.Gene.name.syn.":"BAF250 BAF250A C1orf4 OSA1 SMARCF1;HRMT1L5 IBP72 JBP1 SKB1;BAF53 BAF53A INO80K;BAF190A BRG1 SNF2B SNF2L4;BAF47, INI1, SNF5L1;BAF170;BAF155","Disease.comment":"None","Subunits.comment":"In a following paper (PMID:14559996) p66 has been identified as PRMT5.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3064,"ComplexName":"RNA polymerase II complex, chromatin structure modifying","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"P20226;P24863;P24928;P29083;P32780;P35269;P49336;P51531;Q00403;Q12824;Q13503;Q14919;Q6UW60;Q8TAQ2;Q92922;Q96GM5","subunits.Entrez.IDs.":"6908;892;5430;2960;2965;2962;1024;6595;2959;6598;9412;10589;54760;6601;6599;6602","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0006265;GO:0006351;GO:0003677;GO:0005634","GO.description":"DNA topological change;transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"10.01.09.05;11;16.03.01;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);TRANSCRIPTION;DNA binding;nucleus","PubMed.ID":9710619,"subunits.Protein.name.":"TATA-box-binding protein;Cyclin-C;DNA-directed RNA polymerase II subunit RPB1;General transcription factor IIE subunit 1;General transcription factor IIH subunit 1;General transcription factor IIF subunit 1;Cyclin-dependent kinase 8;Probable global transcription activator SNF2L2;Transcription initiation factor IIB;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;Mediator of RNA polymerase II transcription subunit 21;Dr1-associated corepressor;Proprotein convertase subtilisin/kexin type 4;SWI/SNF complex subunit SMARCC2;SWI/SNF complex subunit SMARCC1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","subunits.Gene.name.":"TBP;CCNC;POLR2A;GTF2E1;GTF2H1;GTF2F1;CDK8;SMARCA2;GTF2B;SMARCB1;MED21;DRAP1;PCSK4;SMARCC2;SMARCC1;SMARCD1","subunits.Gene.name.syn.":"GTF2D1 TF2D TFIID;None;POLR2;TF2E1;BTF2;RAP74;None;BAF190B, BRM, SNF2A, SNF2L2;TF2B TFIIB;BAF47, INI1, SNF5L1;SRB7 SURB7;None;PC4;BAF170;BAF155;BAF60A","Disease.comment":"None","Subunits.comment":"Since the authors did not specify SNF2 (= SMARCA) and BAF60 (=SMARCD), we used isoform SNF2A (=SMARCA2) and BAF60A (=SMARCD1).","Complex.comment":"RNA polymerase II complex contains chromatin structure remodeling activity and histone acetyltransferase activity.Notably, the general transcription factors are absent from this complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3065,"ComplexName":"RNA polymerase II complex, chromatin structure modifying","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O96019;P24863;P49336;Q12824;Q13503;Q8TAQ2;Q92922;Q969G3;Q96GM5","subunits.Entrez.IDs.":"86;892;1024;6598;9412;6601;6599;6605;6602","Protein.complex.purification.method":"MI:0047-far western blotting","GO.ID":"GO:0006265;GO:0006351;GO:0003677;GO:0005634","GO.description":"DNA topological change;transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"10.01.09.05;11;16.03.01;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);TRANSCRIPTION;DNA binding;nucleus","PubMed.ID":9710619,"subunits.Protein.name.":"Actin-like protein 6A;Cyclin-C;Cyclin-dependent kinase 8;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;Mediator of RNA polymerase II transcription subunit 21;SWI/SNF complex subunit SMARCC2;SWI/SNF complex subunit SMARCC1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","subunits.Gene.name.":"ACTL6A;CCNC;CDK8;SMARCB1;MED21;SMARCC2;SMARCC1;SMARCE1;SMARCD1","subunits.Gene.name.syn.":"BAF53 BAF53A INO80K;None;None;BAF47, INI1, SNF5L1;SRB7 SURB7;BAF170;BAF155;BAF57;BAF60A","Disease.comment":"None","Subunits.comment":"Since the authors did not specify BAF60, we used isoform BAF60A.","Complex.comment":"RNA polymerase II complex contains chromatin structure remodeling activity and histone acetyltransferase activity. Notably, the general transcription factors are absent from this complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3066,"ComplexName":"RNA polymerase II complex, chromatin structure modifying","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"P19447;P24863;P24928;P35269;P49336;P51531;P51532;Q00403;Q12824;Q13503;Q13889;Q92793;Q92831","subunits.Entrez.IDs.":"2071;892;5430;2962;1024;6595;6597;2959;6598;9412;2967;1387;8850","Protein.complex.purification.method":"MI:0047- far western blotting; MI:0226- ion exchange chromatography","GO.ID":"GO:0006265;GO:0006351;GO:0003677;GO:0005634","GO.description":"DNA topological change;transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"10.01.09.05;11;16.03.01;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);TRANSCRIPTION;DNA binding;nucleus","PubMed.ID":9710619,"subunits.Protein.name.":"TFIIH basal transcription factor complex helicase XPB subunit ;Cyclin-C;DNA-directed RNA polymerase II subunit RPB1;General transcription factor IIF subunit 1;Cyclin-dependent kinase 8;Probable global transcription activator SNF2L2;Transcription activator BRG1;Transcription initiation factor IIB;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;Mediator of RNA polymerase II transcription subunit 21;General transcription factor IIH subunit 3 ;CREB-binding protein;Histone acetyltransferase KAT2B","subunits.Gene.name.":"ERCC3;CCNC;POLR2A;GTF2F1;CDK8;SMARCA2;SMARCA4;GTF2B;SMARCB1;MED21;GTF2H3;CREBBP;KAT2B","subunits.Gene.name.syn.":"XPB XPBC;None;POLR2;RAP74;None;BAF190B, BRM, SNF2A, SNF2L2;BAF190A BRG1 SNF2B SNF2L4;TF2B TFIIB;BAF47, INI1, SNF5L1;SRB7 SURB7;;CBP;PCAF","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"RNA polymerase II complex contains chromatin structure remodeling activity and histone acetyltransferase activity. Notably, the general transcription factors are absent from this complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3067,"ComplexName":"RNA polymerase II complex, incomplete (CDK8 complex), chromatin structure modifying","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"P24863;P35269;P49336;P51946;Q12824;Q13503;Q8TAQ2;Q92922","subunits.Entrez.IDs.":"892;2962;1024;902;6598;9412;6601;6599","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0006265;GO:0006351;GO:0003677;GO:0005634","GO.description":"DNA topological change;transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"10.01.09.05;11;16.03.01;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);TRANSCRIPTION;DNA binding;nucleus","PubMed.ID":9710619,"subunits.Protein.name.":"Cyclin-C;General transcription factor IIF subunit 1;Cyclin-dependent kinase 8;Cyclin-H ;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;Mediator of RNA polymerase II transcription subunit 21;SWI/SNF complex subunit SMARCC2;SWI/SNF complex subunit SMARCC1","subunits.Gene.name.":"CCNC;GTF2F1;CDK8;CCNH;SMARCB1;MED21;SMARCC2;SMARCC1","subunits.Gene.name.syn.":"None;RAP74;None;;BAF47, INI1, SNF5L1;SRB7 SURB7;BAF170;BAF155","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"RNA polymerase II complex contains chromatin structure remodeling activity and histone acetyltransferase activity. Notably, the general transcription factors are absent from this complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3068,"ComplexName":"Fertilin complex (Adam1a, Adam2)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q60718;Q60813","subunits.Entrez.IDs.":"11495;280668","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0015031;GO:0008565","GO.description":"protein transport;protein transporter activity","FunCat.ID":"20.01.10","FunCat.description":"protein transport","PubMed.ID":15194697,"subunits.Protein.name.":"Disintegrin and metalloproteinase domain-containing protein 2 ;Disintegrin and metalloproteinase domain-containing protein 1a","subunits.Gene.name.":"Adam2;Adam1a","subunits.Gene.name.syn.":"Ftnb;Adam1 Ftna","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"ADAM1a/ADAM2 fertilin may be implicated in the selective transport of specific sperm proteins including ADAM3 from the endoplasmic reticulum of testicular germ cells onto the cell surface.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3069,"ComplexName":"Rich1-Amot-Par-3 polarity complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"Q8VHG2;Q99N37;Q9Z340","subunits.Entrez.IDs.":"27494;63994;81918","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation;MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0008104;GO:0005096;GO:0043547;GO:0007186;GO:0051211;GO:0009798;GO:0007043;GO:0030054","GO.description":"protein localization;GTPase activator activity;positive regulation of GTPase activity;G-protein coupled receptor signaling pathway;anisotropic cell growth;axis specification;cell-cell junction assembly;cell junction","FunCat.ID":"18.01.03;18.02.01.01.01;30.05.02.24;40.01.03;41.05.19;42.06.04;70.06","FunCat.description":"regulation by localization;GTPase activator (GAP);G-protein coupled receptor signalling pathway;directional cell growth (morphogenesis);asymmetries and axis determination;intercellular junction (gap junction/adherens junction);cell junction","PubMed.ID":16678097,"subunits.Protein.name.":"Angiomotin;Rho GTPase-activating protein 17 ;Partitioning defective 3 homolog","subunits.Gene.name.":"Amot;Arhgap17;Pard3","subunits.Gene.name.syn.":"Kiaa1071;;Par3","Disease.comment":"None","Subunits.comment":"Since Amot from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"The results confirm that Rich1, Amot, and Par-3 associate in vivo.","SWISSPROT.organism":"Mus musculus (Mouse);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":3070,"ComplexName":"CTF18-cohesion-RFC-POLH complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P0CG13;P35249;P35250;P40937;P40938;Q8WVB6;Q9BVC3;Q9Y253","subunits.Entrez.IDs.":"54921;5984;5982;5985;5983;63922;79075;5429","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies;MI:0027-cosedimentation;MI:0019-coimmunoprecipitation","GO.ID":"GO:0006260;GO:0006310;GO:0006281;GO:0003677;GO:0005634","GO.description":"DNA replication;DNA recombination;DNA repair;DNA binding;nucleus","FunCat.ID":"10.01.03;10.01.05.03;10.01.05.01;16.03.01;70.10","FunCat.description":"DNA synthesis and replication;DNA recombination;DNA repair;DNA binding;nucleus","PubMed.ID":17545166,"subunits.Protein.name.":"Chromosome transmission fidelity protein 8 homolog;Replication factor C subunit 4;Replication factor C subunit 2;Replication factor C subunit 5;Replication factor C subunit 3;Chromosome transmission fidelity protein 18 homolog;Sister chromatid cohesion protein DCC1;DNA polymerase eta","subunits.Gene.name.":"CHTF8;RFC4;RFC2;RFC5;RFC3;CHTF18;DSCC1;POLH","subunits.Gene.name.syn.":"CTF8;None;None;None;None;C16orf41 CTF18;DCC1;RAD30 RAD30A XPV","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The interaction of CTF18-cohesion-RFC complex  with  DNA-polymerase eta allows DNA replication fork to overcome interference by various template structures, including damaged DNA and DNA-protein complexes that maintain chromosome cohesion.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3071,"ComplexName":"CTLH complex","Organism":"Human","Synonyms":"RANBPM-MKLN1-MAEA-RMND5A-ARMC8 complex","Cell.line":"None","subunits.UniProt.IDs.":"Q7L5Y9;Q8IUR7;Q96S59;Q9H871;Q9UL63","subunits.Entrez.IDs.":"10296;25852;10048;64795;4289","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007059;GO:0016477;GO:0000226;GO:0005737;GO:0005634","GO.description":"chromosome segregation;cell migration;microtubule cytoskeleton organization;cytoplasm;nucleus","FunCat.ID":"10.03.04.05;34.05.01;42.04.05;70.03;70.10","FunCat.description":"chromosome segregation/division;cell migration;microtubule cytoskeleton;cytoplasm;nucleus","PubMed.ID":17467196,"subunits.Protein.name.":"Macrophage erythroblast attacher ;Armadillo repeat-containing protein 8;Ran-binding protein 9 ;Protein RMD5 homolog A;Muskelin","subunits.Gene.name.":"MAEA;ARMC8;RANBP9;RMND5A;MKLN1","subunits.Gene.name.syn.":"EMP;;RANBPM;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex might be involved in the regulation of microtubule dynamics, cell migration , nucleokinesis and chromosome segregation. CTHL complex contains alpha and beta splice variants of ARMC8.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3072,"ComplexName":"CCT complex (chaperonin containing TCP1 complex), testis specific","Organism":"Mouse","Synonyms":"TRiC","Cell.line":"None","subunits.UniProt.IDs.":"P11983;P42932;P80313;P80314;P80315;P80316;P80318;Q61390","subunits.Entrez.IDs.":"21454;12469;12468;12461;12464;12465;12462;12467","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0091- chromatography technologies","GO.ID":"GO:0050821;GO:0006457;GO:0005515;GO:0005524;GO:0005737","GO.description":"protein stabilization;protein folding;protein binding;ATP binding;cytoplasm","FunCat.ID":"14.01;16.01;16.19.03;70.03","FunCat.description":"protein folding and stabilization;protein binding;ATP binding;cytoplasm","PubMed.ID":9013858,"subunits.Protein.name.":"T-complex protein 1 subunit alpha;T-complex protein 1 subunit theta;T-complex protein 1 subunit eta;T-complex protein 1 subunit beta;T-complex protein 1 subunit delta;T-complex protein 1 subunit epsilon;T-complex protein 1 subunit gamma;T-complex protein 1 subunit zeta-2","subunits.Gene.name.":"Tcp1;Cct8;Cct7;Cct2;Cct4;Cct5;Cct3;Cct6b","subunits.Gene.name.syn.":"Cct1 Ccta;Cctq;Ccth;Cctb;Cctd;Ccte Kiaa0098;Cctg;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The chaperonins are a family of molecular chaperones involved in protein folding, assembly and transport. The chaperonin-containing TCP-1 (CCT) is abundant in eukaryotic cytosol. The gene product of Cct6b has only been detected in testis, whereas the other Cctz gene, Cctz-1, is expressed in all tissues investigated. Sequence analysis of the TriC subunits was shown in PMID:9013858, PMID:2377466, PMID:7953530, and PMID:7890169.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3073,"ComplexName":"CCT complex (chaperonin containing TCP1 complex)","Organism":"Bovine","Synonyms":"TRiC","Cell.line":"None","subunits.UniProt.IDs.":"Q2NKZ1;Q2T9X2;Q32L40;Q3MHL7;Q3T0K2;Q3T115;Q3ZBH0;Q3ZCI9","subunits.Entrez.IDs.":"514355;613336;512043;521540;504735;533784;505313;281047","Protein.complex.purification.method":"MI:0027-cosedimentation;MI:0091-chromatography technologies","GO.ID":"GO:0050821;GO:0006457;GO:0005515;GO:0005524;GO:0005737","GO.description":"protein stabilization;protein folding;protein binding;ATP binding;cytoplasm","FunCat.ID":"14.01;16.01;16.19.03;70.03","FunCat.description":"protein folding and stabilization;protein binding;ATP binding;cytoplasm","PubMed.ID":12456645,"subunits.Protein.name.":"T-complex protein 1 subunit eta;T-complex protein 1 subunit delta;T-complex protein 1 subunit alpha;T-complex protein 1 subunit zeta;T-complex protein 1 subunit gamma;Chaperonin containing TCP1, subunit 5;T-complex protein 1 subunit beta;T-complex protein 1 subunit theta","subunits.Gene.name.":"CCT7;CCT4;TCP1;CCT6A;CCT3;CCT5;CCT2;CCT8","subunits.Gene.name.syn.":"None;None;CCT1;None;None;None;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The chaperonins are a family of molecular chaperones involved in protein folding, assembly and transport. The chaperonin-containing TCP-1 (CCT) is abundant in eukaryotic cytosol. The gene product of Cct6b has only been detected in testis, whereas the other Cctz gene, Cctz-1, is expressed in all tissues investigated.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":3074,"ComplexName":"CCT:PFD complex, testis specific","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15212;O60925;P61758;Q2NKZ1;Q2T9X2;Q32L40;Q3T084;Q3T0K2;Q3T115;Q3ZBH0;Q3ZCI9;Q99471;Q9NQP4;Q9UHV9","subunits.Entrez.IDs.":"10471;5201;7411;514355;613336;512043;538090;504735;533784;505313;281047;5204;5203;5202","Protein.complex.purification.method":"MI:0040-electron microscopy;MI:0028-cosedimentation in solution;MI:0226-ion exchange chromatography","GO.ID":"GO:0050821;GO:0006457;GO:0005515","GO.description":"protein stabilization;protein folding;protein binding","FunCat.ID":"14.01;16.01","FunCat.description":"protein folding and stabilization;protein binding","PubMed.ID":12456645,"subunits.Protein.name.":"Prefoldin subunit 6;Prefoldin subunit 1;Prefoldin subunit 3;T-complex protein 1 subunit eta;T-complex protein 1 subunit delta;T-complex protein 1 subunit alpha;T-complex protein 1 subunit zeta-2;T-complex protein 1 subunit gamma;Chaperonin containing TCP1, subunit 5;T-complex protein 1 subunit beta;T-complex protein 1 subunit theta;Prefoldin subunit 5;Prefoldin subunit 4;Prefoldin subunit 2","subunits.Gene.name.":"PFDN6;PFDN1;VBP1;CCT7;CCT4;TCP1;CCT6B;CCT3;CCT5;CCT2;CCT8;PFDN5;PFDN4;PFDN2","subunits.Gene.name.syn.":"HKE2 PFD6;PFD1;PFDN3;None;None;CCT1;None;None;None;None;None;MM1 PFD5;PFD4;PFD2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The biogenesis of the cytoskeletal proteins actin and tubulin involves interaction of nascent chains of each of the two proteins with the oligomeric protein prefoldin (PFD) and their subsequent transfer to the cytosolic chaperonin CCT (chaperonin containing TCP-1). Three-dimensional reconstruction of the CCT:PFD complex based on cryoelectron microscopy reveals that PFD binds to each of the two CCT rings. The gene product of Cct6b has only been detected in testis, whereas the other Cctz gene, Cctz-1, is expressed in all tissues investigated.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3075,"ComplexName":"UTX-MLL2/3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14686;O15550;P61964;Q14686;Q15291;Q5H9R7;Q6ZW49;Q86UW6;Q86XN7;Q8NEZ4;Q9UBL3;Q9Y2X9","subunits.Entrez.IDs.":"8085;7403;11091;23054;5929;55291;22976;55728;80209;58508;9070;23528","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045893;GO:0018126;GO:0006479;GO:0006464;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;protein hydroxylation;protein methylation;cellular protein modification process;nucleus","FunCat.ID":"11.02.03.04.01;14.07.09;14.07;70.10","FunCat.description":"transcription activation;posttranslational modification of amino acids (e.g. hydroxylation, methylation);protein modification;nucleus","PubMed.ID":17761849,"subunits.Protein.name.":"Histone-lysine N-methyltransferase 2D;Lysine-specific demethylase 6A;WD repeat-containing protein 5;Nuclear receptor coactivator 6;Retinoblastoma-binding protein 5;Serine/threonine-protein phosphatase 6 regulatory subunit 3 ;PAX-interacting protein 1;NEDD4-binding protein 2 ;Proline and serine-rich protein 1;Histone-lysine N-methyltransferase 2C;Set1/Ash2 histone methyltransferase complex subunit ASH2;Zinc finger protein 281","subunits.Gene.name.":"KMT2D;KDM6A;WDR5;NCOA6;RBBP5;PPP6R3;PAXIP1;N4BP2;PROSER1;KMT2C;ASH2L;ZNF281","subunits.Gene.name.syn.":"ALR, MLL2, MLL4;UTX;BIG3;AIB3, KIAA0181, RAP250, TRBP;RBQ3;C11orf23 KIAA1558 PP6R3 SAPL SAPS3;PAXIP1L, PTIP;B3BP KIAA1413;C13orf23 KIAA2032;HALR, KIAA1506, MLL3;ASH2L1;GZP1 ZBP99","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Methylation of histone H3 lysine 27 (H3K27) is a post-translational modification highly correlated with genomic silencing. UTX, a member of JmjC-family proteins, is a di- and trimethyl H3K27 demethylase. Results uncover a concerted mechanism for transcriptional activation in which cycles of H3K4 methylation by MLL2/3 are linked with demethylation of H3K27 through UTX.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3076,"ComplexName":"Srf-Elk1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"A4GTP4;Q9JM73","subunits.Entrez.IDs.":"314436;20807","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0045892;GO:0048745","GO.description":"negative regulation of transcription, DNA-templated;smooth muscle tissue development","FunCat.ID":"11.02.03.04.03;45.03.12.02","FunCat.description":"transcription repression;smooth muscle","PubMed.ID":15014501,"subunits.Protein.name.":"ETS domain-containing protein Elk-1;Serum response factor","subunits.Gene.name.":"Elk1;Srf","subunits.Gene.name.syn.":";None","Disease.comment":"None","Subunits.comment":"Since Srf from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"The authors demonstrate that myocardin and Elk-1 compete for interaction with a common docking site on SRF and that Elk-1 acts as a signal-responsive repressor of smooth muscle gene expression by displacing myocardin from SRF within the context of native chromatin.","SWISSPROT.organism":"Rattus norvegicus (Rat);Mus musculus (Mouse)"}
{"ComplexID":3077,"ComplexName":"Srf-Myocd complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q8R5I7;Q9JM73","subunits.Entrez.IDs.":"246297;20807","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0045893;GO:0048745","GO.description":"positive regulation of transcription, DNA-templated;smooth muscle tissue development","FunCat.ID":"11.02.03.04.01;45.03.12.02","FunCat.description":"transcription activation;smooth muscle","PubMed.ID":15014501,"subunits.Protein.name.":"Myocardin;Serum response factor","subunits.Gene.name.":"Myocd;Srf","subunits.Gene.name.syn.":"Mycd;None","Disease.comment":"None","Subunits.comment":"Since Srf from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"The authors demonstrate that myocardin and Elk-1 compete for interaction with a common docking site on SRF and that Elk-1 acts as a signal-responsive repressor of smooth muscle gene expression by displacing myocardin from SRF within the context of native chromatin.","SWISSPROT.organism":"Rattus norvegicus (Rat);Mus musculus (Mouse)"}
{"ComplexID":3078,"ComplexName":"DGCR8-NCL complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P19338;Q8WYQ5","subunits.Entrez.IDs.":"4691;54487","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation; MI:0416- fluorescence microscopy","GO.ID":"GO:0006396;GO:0003723;GO:0005730","GO.description":"RNA processing;RNA binding;nucleolus","FunCat.ID":"11.04;16.03.03;70.10.07","FunCat.description":"RNA processing;RNA binding;nucleolus","PubMed.ID":17765891,"subunits.Protein.name.":"Nucleolin ;Microprocessor complex subunit DGCR8","subunits.Gene.name.":"NCL;DGCR8","subunits.Gene.name.syn.":";C22orf12 DGCRK6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors demonstrated that certain RNA may be involved in the interaction between DGCR8 and Nucleolin, and removal of RNA induces dissociation of these two proteins. The results suggest that DGCR8 may be involved in maturation of miRNA at the nucleolus and nucleoplasm with Nucleolin.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3079,"ComplexName":"DGCR8-ILF3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q12906;Q8WYQ5","subunits.Entrez.IDs.":"3609;54487","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006396;GO:0003723;GO:0005730","GO.description":"RNA processing;RNA binding;nucleolus","FunCat.ID":"11.04;16.03.03;70.10.07","FunCat.description":"RNA processing;RNA binding;nucleolus","PubMed.ID":17765891,"subunits.Protein.name.":"Interleukin enhancer-binding factor 3 ;Microprocessor complex subunit DGCR8","subunits.Gene.name.":"ILF3;DGCR8","subunits.Gene.name.syn.":"DRBF MPHOSPH4 NF90;C22orf12 DGCRK6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors found that ILF3 is associated with both DGCR8 and Exportin5 (XPO5), although DGCR8 is not associated with XPO5.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3080,"ComplexName":"ILF3-XPO5 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q12906;Q9HAV4","subunits.Entrez.IDs.":"3609;57510","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006396;GO:0003723;GO:0050658;GO:0051033;GO:0005634","GO.description":"RNA processing;RNA binding;RNA transport;RNA transmembrane transporter activity;nucleus","FunCat.ID":"11.04;16.03.03;20.01.21;70.10","FunCat.description":"RNA processing;RNA binding;RNA transport;nucleus","PubMed.ID":17765891,"subunits.Protein.name.":"Interleukin enhancer-binding factor 3 ;Exportin-5","subunits.Gene.name.":"ILF3;XPO5","subunits.Gene.name.syn.":"DRBF MPHOSPH4 NF90;KIAA1291 RANBP21","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors found that ILF3 is associated with both DGCR8 and Exportin5 (XPO5), although DGCR8 is not associated with XPO5.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3081,"ComplexName":"Microprocessor complex","Organism":"Human","Synonyms":"small Drosha complex (DGCR8-DROSHA)","Cell.line":"None","subunits.UniProt.IDs.":"Q8WYQ5;Q9NRR4","subunits.Entrez.IDs.":"54487;29102","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation; MI:0416- fluorescence microscopy","GO.ID":"GO:0006396;GO:0003723;GO:0005730","GO.description":"RNA processing;RNA binding;nucleolus","FunCat.ID":"11.04;16.03.03;70.10.07","FunCat.description":"RNA processing;RNA binding;nucleolus","PubMed.ID":17765891,"subunits.Protein.name.":"Microprocessor complex subunit DGCR8 ;Ribonuclease 3","subunits.Gene.name.":"DGCR8;DROSHA","subunits.Gene.name.syn.":"C22orf12 DGCRK6;RN3 RNASE3L RNASEN","Disease.comment":"DGCR8 is deleted in DiGeorge syndrome.","Subunits.comment":"None","Complex.comment":"The authors speculate that DGCR8 might play a significant role in the pri-miRNA recognition before interacting with DROSHA. In the coimmunoprecipitation assay DROSHA is seen as three isoforms (DROSHA-a, -b, -c).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3082,"ComplexName":"DGCR8 multiprotein complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43390;P11021;P17844;P19338;P31943;P35637;Q00839;Q08211;Q12906;Q8WYQ5;Q92841","subunits.Entrez.IDs.":"10236;3309;1655;4691;3187;2521;3192;1660;3609;54487;10521","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation; MI:0416- fluorescence microscopy","GO.ID":"GO:0006396;GO:0005634","GO.description":"RNA processing;nucleus","FunCat.ID":"11.04;70.10","FunCat.description":"RNA processing;nucleus","PubMed.ID":17765891,"subunits.Protein.name.":"Heterogeneous nuclear ribonucleoprotein R ;78 kDa glucose-regulated protein;Probable ATP-dependent RNA helicase DDX5 ;Nucleolin ;Heterogeneous nuclear ribonucleoprotein H ;RNA-binding protein FUS ;Heterogeneous nuclear ribonucleoprotein U ;ATP-dependent RNA helicase A ;Interleukin enhancer-binding factor 3 ;Microprocessor complex subunit DGCR8 ;Probable ATP-dependent RNA helicase DDX17","subunits.Gene.name.":"HNRNPR;HSPA5;DDX5;NCL;HNRNPH1;FUS;HNRNPU;DHX9;ILF3;DGCR8;DDX17","subunits.Gene.name.syn.":"HNRPR;GRP78;G17P1 HELR HLR1;;HNRPH HNRPH1;TLS;HNRPU SAFA U21.1;DDX9 LKP NDH2;DRBF MPHOSPH4 NF90;C22orf12 DGCRK6;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3083,"ComplexName":"Nucleic and chromatin Fanconi complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15287;O15360;Q00597;Q9HB96;Q9NPI8","subunits.Entrez.IDs.":"2189;2175;2176;2178;2188","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006974;GO:0005634","GO.description":"cellular response to DNA damage stimulus;nucleus","FunCat.ID":"32.01.09;70.10","FunCat.description":"DNA damage response;nucleus","PubMed.ID":15082718,"subunits.Protein.name.":"Fanconi anemia group G protein ;Fanconi anemia group A protein ;Fanconi anemia group C protein ;Fanconi anemia group E protein ;Fanconi anemia group F protein","subunits.Gene.name.":"FANCG;FANCA;FANCC;FANCE;FANCF","subunits.Gene.name.syn.":"XRCC9;FAA FACA FANCH;FAC FACC;FACE;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3084,"ComplexName":"CCND1-CDK4 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P11802;P24385","subunits.Entrez.IDs.":"1019;595","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000278;GO:0006468;GO:0006470;GO:0046777;GO:0006464;GO:0050789;GO:0005634","GO.description":"mitotic cell cycle;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;cellular protein modification process;regulation of biological process;nucleus","FunCat.ID":"10.03.01.01;14.07.03;14.07;18;70.10","FunCat.description":"mitotic cell cycle;modification by phosphorylation, dephosphorylation, autophosphorylation;protein modification;REGULATION OF METABOLISM AND PROTEIN FUNCTION;nucleus","PubMed.ID":9447971,"subunits.Protein.name.":"Cyclin-dependent kinase 4 ;G1/S-specific cyclin-D1","subunits.Gene.name.":"CDK4;CCND1","subunits.Gene.name.syn.":";BCL1 PRAD1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Endogenous D-type cyclins, acting with cdk4/6, are able to phosphorylate pRb only partially, a process that is likely to be completed by cyclin E-cdk2 complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3085,"ComplexName":"CCND2-CDK4 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P11802;P30279","subunits.Entrez.IDs.":"1019;894","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000278;GO:0006468;GO:0006470;GO:0046777;GO:0006464;GO:0050789;GO:0005634","GO.description":"mitotic cell cycle;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;cellular protein modification process;regulation of biological process;nucleus","FunCat.ID":"10.03.01.01;14.07.03;14.07;18;70.10","FunCat.description":"mitotic cell cycle;modification by phosphorylation, dephosphorylation, autophosphorylation;protein modification;REGULATION OF METABOLISM AND PROTEIN FUNCTION;nucleus","PubMed.ID":9447971,"subunits.Protein.name.":"Cyclin-dependent kinase 4 ;G1/S-specific cyclin-D2","subunits.Gene.name.":"CDK4;CCND2","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Endogenous D-type cyclins, acting with cdk4/6, are able to phosphorylate pRb only partially, a process that is likely to be completed by cyclin E-cdk2 complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3086,"ComplexName":"CCND3-CDK4 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P11802;P30281","subunits.Entrez.IDs.":"1019;896","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000278;GO:0006468;GO:0006470;GO:0046777;GO:0006464;GO:0050789;GO:0005634","GO.description":"mitotic cell cycle;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;cellular protein modification process;regulation of biological process;nucleus","FunCat.ID":"10.03.01.01;14.07.03;14.07;18;70.10","FunCat.description":"mitotic cell cycle;modification by phosphorylation, dephosphorylation, autophosphorylation;protein modification;REGULATION OF METABOLISM AND PROTEIN FUNCTION;nucleus","PubMed.ID":9447971,"subunits.Protein.name.":"Cyclin-dependent kinase 4 ;G1/S-specific cyclin-D3","subunits.Gene.name.":"CDK4;CCND3","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Endogenous D-type cyclins, acting with cdk4/6, are able to phosphorylate pRb only partially, a process that is likely to be completed by cyclin E-cdk2 complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3087,"ComplexName":"CCND1-CDK6 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P24385;Q00534","subunits.Entrez.IDs.":"595;1021","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000278;GO:0006468;GO:0006470;GO:0046777;GO:0006464;GO:0050789;GO:0005634","GO.description":"mitotic cell cycle;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;cellular protein modification process;regulation of biological process;nucleus","FunCat.ID":"10.03.01.01;14.07.03;14.07;18;70.10","FunCat.description":"mitotic cell cycle;modification by phosphorylation, dephosphorylation, autophosphorylation;protein modification;REGULATION OF METABOLISM AND PROTEIN FUNCTION;nucleus","PubMed.ID":9447971,"subunits.Protein.name.":"G1/S-specific cyclin-D1;Cyclin-dependent kinase 6","subunits.Gene.name.":"CCND1;CDK6","subunits.Gene.name.syn.":"BCL1 PRAD1;CDKN6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Endogenous D-type cyclins, acting with cdk4/6, are able to phosphorylate pRb only partially, a process that is likely to be completed by cyclin E-cdk2 complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3088,"ComplexName":"CCND2-CDK6 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P30279;Q00534","subunits.Entrez.IDs.":"894;1021","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000278;GO:0006468;GO:0006470;GO:0046777;GO:0006464;GO:0050789;GO:0005634","GO.description":"mitotic cell cycle;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;cellular protein modification process;regulation of biological process;nucleus","FunCat.ID":"10.03.01.01;14.07.03;14.07;18;70.10","FunCat.description":"mitotic cell cycle;modification by phosphorylation, dephosphorylation, autophosphorylation;protein modification;REGULATION OF METABOLISM AND PROTEIN FUNCTION;nucleus","PubMed.ID":9447971,"subunits.Protein.name.":"G1/S-specific cyclin-D2;Cyclin-dependent kinase 6","subunits.Gene.name.":"CCND2;CDK6","subunits.Gene.name.syn.":";CDKN6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Endogenous D-type cyclins, acting with cdk4/6, are able to phosphorylate pRb only partially, a process that is likely to be completed by cyclin E-cdk2 complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3089,"ComplexName":"CCND3-CDK6 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P30281;Q00534","subunits.Entrez.IDs.":"896;1021","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000278;GO:0006468;GO:0006470;GO:0046777;GO:0006464;GO:0050789;GO:0005634","GO.description":"mitotic cell cycle;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;cellular protein modification process;regulation of biological process;nucleus","FunCat.ID":"10.03.01.01;14.07.03;14.07;18;70.10","FunCat.description":"mitotic cell cycle;modification by phosphorylation, dephosphorylation, autophosphorylation;protein modification;REGULATION OF METABOLISM AND PROTEIN FUNCTION;nucleus","PubMed.ID":9447971,"subunits.Protein.name.":"G1/S-specific cyclin-D3;Cyclin-dependent kinase 6","subunits.Gene.name.":"CCND3;CDK6","subunits.Gene.name.syn.":";CDKN6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Endogenous D-type cyclins, acting with cdk4/6, are able to phosphorylate pRb only partially, a process that is likely to be completed by cyclin E-cdk2 complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3090,"ComplexName":"Kv4.2-Kchip4 channel complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain, hippocampal membranes","subunits.UniProt.IDs.":"Q63881;Q99MG9","subunits.Entrez.IDs.":"65180;259243","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0001508;GO:0019227;GO:0019228;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;action potential;neuronal action potential propagation;neuronal action potential;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;34.03.03;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;regulation, generation and propagation of action potential;eukaryotic plasma membrane / membrane attached","PubMed.ID":15356203,"subunits.Protein.name.":"Potassium voltage-gated channel subfamily D member 2;Kv channel-interacting protein 4","subunits.Gene.name.":"Kcnd2;Kcnip4","subunits.Gene.name.syn.":"None;Kchip4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Immunohistochemical and immunofluorescence data show that there is preferential codistribution of Kv4.2 with KChIPs 2, 3, and 4 and preferential codistribution of Kv4.3 with KChIP1.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":3091,"ComplexName":"Kv4.3-Kchip1 channel complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain, hippocampal membranes","subunits.UniProt.IDs.":"Q62897;Q8R426","subunits.Entrez.IDs.":"65195;65023","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0001508;GO:0019227;GO:0019228;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;action potential;neuronal action potential propagation;neuronal action potential;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;34.03.03;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;regulation, generation and propagation of action potential;eukaryotic plasma membrane / membrane attached","PubMed.ID":15356203,"subunits.Protein.name.":"Potassium voltage-gated channel subfamily D member 3 ;Kv channel-interacting protein 1","subunits.Gene.name.":"Kcnd3;Kcnip1","subunits.Gene.name.syn.":";Kchip1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Immunohistochemical and immunofluorescence data show that there is preferential codistribution of Kv4.2 with KChIPs 2, 3, and 4 and preferential codistribution of Kv4.3 with KChIP1.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":3092,"ComplexName":"APP-TOM40 complex","Organism":"Human","Synonyms":"APP-TOMM40 complex","Cell.line":"brain","subunits.UniProt.IDs.":"O96008;P05067","subunits.Entrez.IDs.":"10452;351","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0047-far western blotting","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0005739","GO.description":"intracellular protein transport;protein targeting;protein transport;mitochondrion","FunCat.ID":"14.04;20.01.10;70.16","FunCat.description":"protein targeting, sorting and translocation;protein transport;mitochondrion","PubMed.ID":16943564,"subunits.Protein.name.":"Mitochondrial import receptor subunit TOM40 homolog;Amyloid beta A4 protein","subunits.Gene.name.":"TOMM40;APP","subunits.Gene.name.syn.":"C19orf1 PEREC1 TOM40;A4 AD1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Mitochondrial accumulation of APP is associated with decreased cytochrome c oxidase activity and increased levels of H2O2 in mitochondria. Reduced mitochondrial cytochrome c oxidase activity and increased oxidative stress have been associated with the pathogenesis of AD.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3093,"ComplexName":"APP-TIM23 complex","Organism":"Human","Synonyms":"APP-TIMM23 complex","Cell.line":"brain","subunits.UniProt.IDs.":"O14925;P05067","subunits.Entrez.IDs.":"100287932;351","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0047-far western blotting","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0005739","GO.description":"intracellular protein transport;protein targeting;protein transport;mitochondrion","FunCat.ID":"14.04;20.01.10;70.16","FunCat.description":"protein targeting, sorting and translocation;protein transport;mitochondrion","PubMed.ID":16943564,"subunits.Protein.name.":"Mitochondrial import inner membrane translocase subunit Tim23;Amyloid beta A4 protein","subunits.Gene.name.":"TIMM23;APP","subunits.Gene.name.syn.":"TIM23;A4 AD1","Disease.comment":"APP is involved in Alzheimer disease.","Subunits.comment":"None","Complex.comment":"Mitochondrial accumulation of APP is associated with decreased cytochrome coxidase activity and increased levels of H2O2 in mitochondria. Reduced mitochondrial cytochrome c oxidase activity and increased oxidative stress have been associated with the pathogenesis of AD.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3094,"ComplexName":"Metaxin complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O88441;P47802","subunits.Entrez.IDs.":"53375;17827","Protein.complex.purification.method":"MI:0018- two hybrid","GO.ID":"GO:0015031;GO:0008565;GO:0009793;GO:0005741","GO.description":"protein transport;protein transporter activity;embryo development ending in seed dormancy;mitochondrial outer membrane","FunCat.ID":"20.01.10;41.03.03;70.16.01","FunCat.description":"protein transport;embryonal development;mitochondrial outer membrane","PubMed.ID":10381257,"subunits.Protein.name.":"Metaxin-2 ;Metaxin-1","subunits.Gene.name.":"Mtx2;Mtx1","subunits.Gene.name.syn.":";Mtx Mtxn","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3095,"ComplexName":"Itgav-Itgb3-Tgm2 complex","Organism":"Rat","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P43406;Q8R2H2;Q9WVJ6","subunits.Entrez.IDs.":"16410;29302;56083","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515;GO:0007155;GO:0005886","GO.description":"protein binding;cell adhesion;plasma membrane","FunCat.ID":"16.01;34.07;70.02","FunCat.description":"protein binding;cell adhesion;eukaryotic plasma membrane / membrane attached","PubMed.ID":10684262,"subunits.Protein.name.":"Integrin alpha-V;Integrin beta;Protein Tgm2","subunits.Gene.name.":"Itgav;Itgb3;Tgm2","subunits.Gene.name.syn.":"None;itgb3;TgaseII","Disease.comment":"None","Subunits.comment":"Since Itgav from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"Complexes of transglutaminase with integrins are formed inside the cell during biosynthesis and accumulate on the surface and in focal adhesions.","SWISSPROT.organism":"Mus musculus (Mouse);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":3096,"ComplexName":"ITGA6-ITGB4-SHC1-GRB2 complex","Organism":"Human","Synonyms":"None","Cell.line":"epithelium, skin","subunits.UniProt.IDs.":"P16144;P23229;P29353;P62993","subunits.Entrez.IDs.":"3691;3655;6464;2885","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0096-pull down","GO.ID":"GO:0023052;GO:0007010","GO.description":"signaling;cytoskeleton organization","FunCat.ID":"30.01;42.04","FunCat.description":"cellular signalling;cytoskeleton/structural proteins","PubMed.ID":7556090,"subunits.Protein.name.":"Integrin beta-4;Integrin alpha-6;SHC-transforming protein 1;Growth factor receptor-bound protein 2","subunits.Gene.name.":"ITGB4;ITGA6;SHC1;GRB2","subunits.Gene.name.syn.":"None;None;SHC SHCA;ASH","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The signal transduction by the alpha6beta4 integrin is mediated by an associated tyrosine kinase and that phosphorylation of distinct sites in the beta 4 tail mediates assembly of the hemidesmosomal cytoskeleton and recruitment of Shc/Grb2.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3097,"ComplexName":"TIM17A-TIM23 complex","Organism":"Human","Synonyms":"TIMM17A-TIMM23 complex","Cell.line":"None","subunits.UniProt.IDs.":"O14925;Q99595","subunits.Entrez.IDs.":"100287932;10440","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0005743","GO.description":"intracellular protein transport;protein targeting;protein transport;mitochondrial inner membrane","FunCat.ID":"14.04;20.01.10;70.16.05","FunCat.description":"protein targeting, sorting and translocation;protein transport;mitochondrial inner membrane","PubMed.ID":8893850,"subunits.Protein.name.":"Mitochondrial import inner membrane translocase subunit Tim23;Mitochondrial import inner membrane translocase subunit Tim17-A","subunits.Gene.name.":"TIMM23;TIMM17A","subunits.Gene.name.syn.":"TIM23;MIMT17, TIM17, TIM17A TIMM17","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The Tim17 proteins of distinct organisms were indistinguishable, indicating a high evolutionary conservation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3098,"ComplexName":"TIM50-SMN1 complex","Organism":"Human","Synonyms":"TIMM50-SMN1 complex","Cell.line":"None","subunits.UniProt.IDs.":"Q16637;Q3ZCQ8","subunits.Entrez.IDs.":"None;92609","Protein.complex.purification.method":"MI:0018-two hybrid","GO.ID":"GO:0008380;GO:0032774;GO:0006461;GO:0003723;GO:0050658;GO:0051033;GO:0051169;GO:0005634","GO.description":"RNA splicing;RNA biosynthetic process;protein complex assembly;RNA binding;RNA transport;RNA transmembrane transporter activity;nuclear transport;nucleus","FunCat.ID":"11.04.03.01;11.02;14.10;16.03.03;20.01.21;20.09.01;70.10","FunCat.description":"splicing;RNA synthesis;assembly of protein complexes;RNA binding;RNA transport;nuclear transport;nucleus","PubMed.ID":16008839,"subunits.Protein.name.":"Survival motor neuron protein;Mitochondrial import inner membrane translocase subunit TIM50","subunits.Gene.name.":"SMN1; SMN2;TIMM50","subunits.Gene.name.syn.":"SMN; SMNT; SMNC;TIM50","Disease.comment":"Spinal muscular atrophy","Subunits.comment":"None","Complex.comment":"There are two isoforms of TIM50:The nuclear isoform, TIM50a, participates in the release of snRNPs and SMN from the Cajal body (this complex), the mitochondrial isoform is an essential component of the TIM23 complex and regulates mitochondrial integrity and cell death.TIM50a is 103 aa longer (N-terminal) than TIM50.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3099,"ComplexName":"TIM50-COIL complex","Organism":"Human","Synonyms":"TIMM50-CLN80 complex","Cell.line":"None","subunits.UniProt.IDs.":"P38432;Q3ZCQ8","subunits.Entrez.IDs.":"8161;92609","Protein.complex.purification.method":"MI:0018-two hybrid","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":16008839,"subunits.Protein.name.":"Coilin;Mitochondrial import inner membrane translocase subunit TIM50","subunits.Gene.name.":"COIL;TIMM50","subunits.Gene.name.syn.":"CLN80;TIM50","Disease.comment":"Spinal muscular atrophy","Subunits.comment":"None","Complex.comment":"There are two isoforms of TIM50:The nuclear isoform, TIM50a, participates in the release of snRNPs and SMN from the Cajal body (this complex), the mitochondrial isoform is an essential component of the TIM23 complex and regulates mitochondrial integrity and cell death.TIM50a is 103 aa longer (N-terminal) than TIM50.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3100,"ComplexName":"Yy1-Ppargc1a complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O70343;Q00899","subunits.Entrez.IDs.":"19017;22632","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0045893;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;nucleus","FunCat.ID":"11.02.03.04.01;70.10","FunCat.description":"transcription activation;nucleus","PubMed.ID":18046414,"subunits.Protein.name.":"Peroxisome proliferator-activated receptor gamma coactivator 1-alpha;Transcriptional repressor protein YY1","subunits.Gene.name.":"Ppargc1a;Yy1","subunits.Gene.name.syn.":"Pgc1 Pgc1a Ppargc1;Ucrbp","Disease.comment":"Cells treated with amTOR inhibitor developed symptoms of diabetes.","Subunits.comment":"None","Complex.comment":"mTOR controls mitochondrial oxidative function to maintain energy homeostasis in response to nutrient and hormonal signals through a YY1-Ppargc1a transcriptional complex. Results indicate that the nutrient sensor mTOR (Frap1) controls mitochondrial respiration by regulating the transcriptional function of the Yy1-Ppargc1a complex by directly altering the physical interaction of the two subunits.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3101,"ComplexName":"Yy1-Ppargc1a-Frap1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O70343;Q00899;Q9JLN9","subunits.Entrez.IDs.":"19017;22632;56717","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0045893;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;nucleus","FunCat.ID":"11.02.03.04.01;70.10","FunCat.description":"transcription activation;nucleus","PubMed.ID":18046414,"subunits.Protein.name.":"Peroxisome proliferator-activated receptor gamma coactivator 1-alpha;Transcriptional repressor protein YY1 ;Serine/threonine-protein kinase mTOR","subunits.Gene.name.":"Ppargc1a;Yy1;Mtor","subunits.Gene.name.syn.":"Pgc1 Pgc1a Ppargc1;Ucrbp;Frap Frap1","Disease.comment":"Cells treated with amTOR inhibitor developed symptoms of diabetes.","Subunits.comment":"None","Complex.comment":"mTOR controls mitochondrial oxidative function to maintain energy homeostasis in response to nutrient and hormonal signals through a YY1-Ppargc1a transcriptional complex. Results indicate that the nutrient sensor mTOR (Frap1) controls mitochondrial respiration by regulating the transcriptional function of the Yy1-Ppargc1a complex by directly altering the physical interaction of the two subunits.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3102,"ComplexName":"DHX9-ADAR-vigilin-DNA-PK-Ku antigen complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12956;P13010;P55265;P78527;Q00341;Q08211","subunits.Entrez.IDs.":"2547;7520;103;5591;3069;1660","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0007059;GO:0016556;GO:0003723;GO:0051276;GO:0005634","GO.description":"DNA topological change;chromosome segregation;mRNA modification;RNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;10.03.04.05;11.06.03;16.03.03;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);chromosome segregation/division;mRNA modification;RNA binding;organization of chromosome structure;nucleus","PubMed.ID":15723802,"subunits.Protein.name.":"X-ray repair cross-complementing protein 6 ;X-ray repair cross-complementing protein 5 ;Double-stranded RNA-specific adenosine deaminase ;DNA-dependent protein kinase catalytic subunit ;Vigilin ;ATP-dependent RNA helicase A","subunits.Gene.name.":"XRCC6;XRCC5;ADAR;PRKDC;HDLBP;DHX9","subunits.Gene.name.syn.":"G22P1;G22P2;ADAR1 DSRAD G1P1 IFI4;HYRC HYRC1;HBP VGL;DDX9 LKP NDH2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Vigilin and DDP1 bind specifically to Inosine-containing RNAs.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3103,"ComplexName":"ITGAV-ITGB3-SLC3A2 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05106;P06756;P08195","subunits.Entrez.IDs.":"3690;3685;6520","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006928;GO:0007155;GO:0005886","GO.description":"movement of cell or subcellular component;cell adhesion;plasma membrane","FunCat.ID":"34.05;34.07;70.02","FunCat.description":"cell motility;cell adhesion;eukaryotic plasma membrane / membrane attached","PubMed.ID":18032696,"subunits.Protein.name.":"Integrin beta-3;Integrin alpha-V;4F2 cell-surface antigen heavy chain","subunits.Gene.name.":"ITGB3;ITGAV;SLC3A2","subunits.Gene.name.syn.":"GP3A;MSK8 VNRA;MDU1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3104,"ComplexName":"ITGB1-NRP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14786;P05556","subunits.Entrez.IDs.":"8829;3688","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007155;GO:0005886","GO.description":"cell adhesion;plasma membrane","FunCat.ID":"34.07;70.02","FunCat.description":"cell adhesion;eukaryotic plasma membrane / membrane attached","PubMed.ID":17726369,"subunits.Protein.name.":"Neuropilin-1;Integrin beta-1","subunits.Gene.name.":"NRP1;ITGB1","subunits.Gene.name.syn.":"NRP VEGF165R;FNRB MDF2 MSK12","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"NP-1 interacts with integrin beta1 to coordinate signaling events that promote cell adherence and invasiveness.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3105,"ComplexName":"Itga7-Itgb11-Lama2 complex","Organism":"Rat","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P49134;Q60675;Q63258","subunits.Entrez.IDs.":"24511;16773;81008","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007155;GO:0005886","GO.description":"cell adhesion;plasma membrane","FunCat.ID":"34.07;70.02","FunCat.description":"cell adhesion;eukaryotic plasma membrane / membrane attached","PubMed.ID":17598176,"subunits.Protein.name.":"Integrin beta-1 ;Laminin subunit alpha-2 ;Integrin alpha-7","subunits.Gene.name.":"Itgb1;Lama2;Itga7","subunits.Gene.name.syn.":";;","Disease.comment":"None","Subunits.comment":"Since Lama2 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"Alpha7-beta1 integrin is a Schwann cell receptor for laminin-2 that provides transmembrane linkage between the Schwann cell basal lamina and cytoskeleton.","SWISSPROT.organism":"Rattus norvegicus (Rat);Mus musculus (Mouse);Rattus norvegicus (Rat)"}
{"ComplexID":3106,"ComplexName":"Itga7-Itgb11-Ptk2 complex","Organism":"Rat","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"O35346;P49134;Q63258","subunits.Entrez.IDs.":"25614;24511;81008","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007229;GO:0005886","GO.description":"integrin-mediated signaling pathway;plasma membrane","FunCat.ID":"30.05.02.26;70.02","FunCat.description":"integrin receptor signalling pathway;eukaryotic plasma membrane / membrane attached","PubMed.ID":17598176,"subunits.Protein.name.":"Focal adhesion kinase 1 ;Integrin beta-1 ;Integrin alpha-7","subunits.Gene.name.":"Ptk2;Itgb1;Itga7","subunits.Gene.name.syn.":"Fak Fak1;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Alpha7-beta1 integrin, but not alpha6-beta1 integrin or dystroglycan, associates with the intracellular signaling protein focal adhesion kinase (FAK) in Schwann cells.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":3110,"ComplexName":"ITGAV-P2RY2-GNA12 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06756;P41231;Q03113","subunits.Entrez.IDs.":"3685;5029;2768","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016477;GO:0005886","GO.description":"cell migration;plasma membrane","FunCat.ID":"34.05.01;70.02","FunCat.description":"cell migration;eukaryotic plasma membrane / membrane attached","PubMed.ID":17452627,"subunits.Protein.name.":"Integrin alpha-V;P2Y purinoceptor 2 ;Guanine nucleotide-binding protein subunit alpha-12","subunits.Gene.name.":"ITGAV;P2RY2;GNA12","subunits.Gene.name.syn.":"MSK8 VNRA;P2RU1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Alpha(v) integrin complexes provide the P2Y2R with access to G12, thereby allowing activation of this heterotrimeric G protein that controls actin cytoskeletal rearrangements required for chemotaxis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3111,"ComplexName":"ITGA9-ITGB1-SPP1 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P10451;Q13797","subunits.Entrez.IDs.":"3688;6696;3680","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0005515;GO:0007155","GO.description":"protein binding;cell adhesion","FunCat.ID":"16.01;34.07","FunCat.description":"protein binding;cell adhesion","PubMed.ID":16005200,"subunits.Protein.name.":"Integrin beta-1;Osteopontin ;Integrin alpha-9","subunits.Gene.name.":"ITGB1;SPP1;ITGA9","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;BNSP OPN;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3112,"ComplexName":"ITGA5-ITGB1-SPP1 complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P05556;P08648;P10451","subunits.Entrez.IDs.":"3688;3678;6696","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0005515;GO:0007155","GO.description":"protein binding;cell adhesion","FunCat.ID":"16.01;34.07","FunCat.description":"protein binding;cell adhesion","PubMed.ID":16005200,"subunits.Protein.name.":"Integrin beta-1;Integrin alpha-5 ;Osteopontin","subunits.Gene.name.":"ITGB1;ITGA5;SPP1","subunits.Gene.name.syn.":"FNRB MDF2 MSK12;FNRA;BNSP OPN","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3113,"ComplexName":"MAML1-RBP-Jkappa-Notch1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P46531;Q06330;Q92585","subunits.Entrez.IDs.":"4851;3516;9794","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0045893;GO:0003677;GO:0007219;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;Notch signaling pathway;nucleus","FunCat.ID":"11.02.03.04.01;16.03.01;30.05.02.14;70.10","FunCat.description":"transcription activation;DNA binding;Notch-receptor signalling pathway;nucleus","PubMed.ID":16530044,"subunits.Protein.name.":"Neurogenic locus notch homolog protein 1 ;Recombining binding protein suppressor of hairless ;Mastermind-like protein 1","subunits.Gene.name.":"NOTCH1;RBPJ;MAML1","subunits.Gene.name.syn.":"TAN1;IGKJRB IGKJRB1 RBPJK RBPSUH;KIAA0200","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"RBPJ and the Ankyrin domain of Notch1 create a groove to bin MAML-1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3114,"ComplexName":"Itgax-Itgb2-Icam4 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P11835;Q9ERM2;Q9QXH4","subunits.Entrez.IDs.":"16414;78369;16411","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0007155","GO.description":"cell adhesion","FunCat.ID":"34.07","FunCat.description":"cell adhesion","PubMed.ID":16985175,"subunits.Protein.name.":"Integrin beta-2 ;Intercellular adhesion molecule 4 ;Integrin alpha-X","subunits.Gene.name.":"Itgb2;Icam4;Itgax","subunits.Gene.name.syn.":";;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Inhibition of erythrophagocytosis by anti-ICAM-4 and anti-integrin antibodies suggests a role for these interactions in removal of senescent red cells.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3115,"ComplexName":"ITGA2B-ITGB3-ICAM4 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P05106;P08514;Q14773","subunits.Entrez.IDs.":"3690;3674;3386","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0007155","GO.description":"cell adhesion","FunCat.ID":"34.07","FunCat.description":"cell adhesion","PubMed.ID":12477717,"subunits.Protein.name.":"Integrin beta-3;Integrin alpha-IIb;Intercellular adhesion molecule 4","subunits.Gene.name.":"ITGB3;ITGA2B;ICAM4","subunits.Gene.name.syn.":"GP3A;GP2B ITGAB;LW","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3116,"ComplexName":"Rab27a-melanophilin-myosin-Va complex","Organism":"Mouse","Synonyms":"None","Cell.line":"B16 cells","subunits.UniProt.IDs.":"Q91V27;Q99104;Q9ERI2","subunits.Entrez.IDs.":"171531;17918;11891","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0050931;GO:0070285;GO:0005886","GO.description":"pigment cell differentiation;pigment cell development;plasma membrane","FunCat.ID":"43.03.03;70.02","FunCat.description":"pigment cell;eukaryotic plasma membrane / membrane attached","PubMed.ID":12531900,"subunits.Protein.name.":"Melanophilin ;Unconventional myosin-Va ;Ras-related protein Rab-27A","subunits.Gene.name.":"Mlph;Myo5a;Rab27a","subunits.Gene.name.syn.":"Ln Slac2a;Dilute;","Disease.comment":"Rab27a is involved in Griscelli syndrome.","Subunits.comment":"None","Complex.comment":"This complex is responsible for melanosome transport.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3117,"ComplexName":"ITGB5-ITGAV-VTN complex","Organism":"Human","Synonyms":"integrin complex","Cell.line":"None","subunits.UniProt.IDs.":"P04004;P06756;P18084","subunits.Entrez.IDs.":"7448;3685;3693","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515;GO:0007155","GO.description":"protein binding;cell adhesion","FunCat.ID":"16.01;34.07","FunCat.description":"protein binding;cell adhesion","PubMed.ID":1694173,"subunits.Protein.name.":"Vitronectin ;Integrin alpha-V;Integrin beta-5","subunits.Gene.name.":"VTN;ITGAV;ITGB5","subunits.Gene.name.syn.":";MSK8 VNRA;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In purified form, alpha(v)-beta5 preferentially binds to vitronectin.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3118,"ComplexName":"SMN1-SIP1-SNRP complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14893;P14678;P62304;P62314;P62316;P62318;Q16637","subunits.Entrez.IDs.":"8487;6628;6635;6632;6633;6634;None","Protein.complex.purification.method":"MI:0018- two hybrid; MI:0019- coimmunoprecipitation; MI:0047- far western blotting","GO.ID":"GO:0005737;GO:0005634","GO.description":"cytoplasm;nucleus","FunCat.ID":"70.03;70.10","FunCat.description":"cytoplasm;nucleus","PubMed.ID":9323129,"subunits.Protein.name.":"Gem-associated protein 2 ;Small nuclear ribonucleoprotein-associated proteins B and B' ;Small nuclear ribonucleoprotein E ;Small nuclear ribonucleoprotein Sm D1 ;Small nuclear ribonucleoprotein Sm D2 ;Small nuclear ribonucleoprotein Sm D3 ;Survival motor neuron protein","subunits.Gene.name.":"GEMIN2;SNRPB;SNRPE;SNRPD1;SNRPD2;SNRPD3;SMN1; SMN2","subunits.Gene.name.syn.":"SIP1;COD SNRPB1;;;SNRPD1;;SMN; SMNT; SMNC","Disease.comment":"Spinal muscular atrophy (SMA)","Subunits.comment":"None","Complex.comment":"SMN (Survival of Motor Neurons) and its associated protein SIP1 are in  a complex with spliceosomal snRNP proteins. The SMN/SIP1 complex is very stable.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3119,"ComplexName":"Kif17-Lin10-Lin2-Lin7-NR2B complex","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"B2RUJ5;O70589;Q01097;Q8JZS0;Q99PW8","subunits.Entrez.IDs.":"319924;12361;14812;108030;16559","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0030705;GO:0050896;GO:0022008;GO:0048699;GO:0030182","GO.description":"cytoskeleton-dependent intracellular transport;response to stimulus;neurogenesis;generation of neurons;neuron differentiation","FunCat.ID":"20.09.14;36.25;41.05.13;43.03.13","FunCat.description":"cytoskeleton-dependent transport;animal specific systemic sensing and response;neurogenesis;neuron","PubMed.ID":10846156,"subunits.Protein.name.":"Amyloid beta A4 precursor protein-binding family A member 1;Peripheral plasma membrane protein CASK;Glutamate receptor ionotropic, NMDA 2B;Protein lin-7 homolog A;Kinesin-like protein KIF17","subunits.Gene.name.":"Apba1;Cask;Grin2b;Lin7a;Kif17","subunits.Gene.name.syn.":"Mint1, X11, Lin-10;mLin-2;NR2B;Mals1, Veli1;None","Disease.comment":"None","Subunits.comment":"Since the authors did not specify Lin-7, we used isoform Lin7a.","Complex.comment":"The authors suggest that KIF17, a neuron-specific molecular motor with microtubule plus-end-directed motility interacts directly with a mLin-10 PDZ domain, resulting in the transport of NR2B in dendrites. They propose this motor-cargo complex as the sorting machinery for NR2B.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3120,"ComplexName":"OCT1-OBF1-DNA-TLE1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293A cells","subunits.UniProt.IDs.":"P14859;Q04724;Q16633","subunits.Entrez.IDs.":"5451;7088;5450","Protein.complex.purification.method":"MI:0412- electrophoretic mobility supershift assay","GO.ID":"GO:0045892;GO:0003677;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04.03;16.03.01;70.10","FunCat.description":"transcription repression;DNA binding;nucleus","PubMed.ID":16103132,"subunits.Protein.name.":"POU domain, class 2, transcription factor 1;Transducin-like enhancer protein 1;POU domain class 2-associating factor 1","subunits.Gene.name.":"POU2F1;TLE1;POU2AF1","subunits.Gene.name.syn.":"OCT1 OTF1;None;OBF1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Transcription activation by Oct1 in conjunction with OBF1 can be prevented by TLE1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3121,"ComplexName":"OCT2-TLE4 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293A cells","subunits.UniProt.IDs.":"P09086;Q04727","subunits.Entrez.IDs.":"5452;7091","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0045892;GO:0003677;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04.03;16.03.01;70.10","FunCat.description":"transcription repression;DNA binding;nucleus","PubMed.ID":16103132,"subunits.Protein.name.":"POU domain, class 2, transcription factor 2;Transducin-like enhancer protein 4","subunits.Gene.name.":"POU2F2;TLE4","subunits.Gene.name.syn.":"OCT2 OTF2;GRG4 KIAA1261","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3122,"ComplexName":"OCT1-OBF1-DNA complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293A cells","subunits.UniProt.IDs.":"P14859;Q16633","subunits.Entrez.IDs.":"5451;5450","Protein.complex.purification.method":"MI:0412- electrophoretic mobility supershift assay","GO.ID":"GO:0045893;GO:0003677;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04.01;16.03.01;70.10","FunCat.description":"transcription activation;DNA binding;nucleus","PubMed.ID":16103132,"subunits.Protein.name.":"POU domain, class 2, transcription factor 1;POU domain class 2-associating factor 1","subunits.Gene.name.":"POU2F1;POU2AF1","subunits.Gene.name.syn.":"OCT1 OTF1;OBF1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3123,"ComplexName":"TLE2 homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q04725","subunits.Entrez.IDs.":"7089","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0045892;GO:0005515;GO:0051098;GO:0051090;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;protein binding;regulation of binding;regulation of sequence-specific DNA binding transcription factor activity;nucleus","FunCat.ID":"11.02.03.04.03;16.01;18.01.07;18.02.09;70.10","FunCat.description":"transcription repression;protein binding;regulation by binding / dissociation;regulator of transcription factor;nucleus","PubMed.ID":9874198,"subunits.Protein.name.":"Transducin-like enhancer protein 2","subunits.Gene.name.":"TLE2","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TLE2 dimer has no DNA-binding ability but can be recuited to specific DNA sites through interaction with DNA-binding proteins.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":3124,"ComplexName":"TLE1-TLE2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q04724;Q04725","subunits.Entrez.IDs.":"7088;7089","Protein.complex.purification.method":"MI:0096- pull down; MI:0018- two hybrid","GO.ID":"GO:0045892;GO:0005515;GO:0051098;GO:0051090;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;protein binding;regulation of binding;regulation of sequence-specific DNA binding transcription factor activity;nucleus","FunCat.ID":"11.02.03.04.03;16.01;18.01.07;18.02.09;70.10","FunCat.description":"transcription repression;protein binding;regulation by binding / dissociation;regulator of transcription factor;nucleus","PubMed.ID":9874198,"subunits.Protein.name.":"Transducin-like enhancer protein 1;Transducin-like enhancer protein 2","subunits.Gene.name.":"TLE1;TLE2","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TLE1/2 heterodimer has no DNA-binding ability but can be recuited to specific DNA sites through interaction with DNA-binding proteins.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3125,"ComplexName":"TLE1 homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q04724","subunits.Entrez.IDs.":"7088","Protein.complex.purification.method":"MI:0018- two hybrid","GO.ID":"GO:0045892;GO:0005515;GO:0051098;GO:0051090;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;protein binding;regulation of binding;regulation of sequence-specific DNA binding transcription factor activity;nucleus","FunCat.ID":"11.02.03.04.03;16.01;18.01.07;18.02.09;70.10","FunCat.description":"transcription repression;protein binding;regulation by binding / dissociation;regulator of transcription factor;nucleus","PubMed.ID":9874198,"subunits.Protein.name.":"Transducin-like enhancer protein 1","subunits.Gene.name.":"TLE1","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TLE1 dimer has no DNA-binding ability but can be recuited to specific DNA sites through interaction with DNA-binding proteins.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":3126,"ComplexName":"Tle2-Hes1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"ROS 17/2.8 cells","subunits.UniProt.IDs.":"Q04666;Q496Z7","subunits.Entrez.IDs.":"29577;299636","Protein.complex.purification.method":"MI:0096- pull down; MI:0018- two hybrid","GO.ID":"GO:0045892;GO:0003677;GO:0007219;GO:0022008;GO:0048699;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;DNA binding;Notch signaling pathway;neurogenesis;generation of neurons;nucleus","FunCat.ID":"11.02.03.04.03;16.03.01;30.05.02.14;41.05.13;70.10","FunCat.description":"transcription repression;DNA binding;Notch-receptor signalling pathway;neurogenesis;nucleus","PubMed.ID":9874198,"subunits.Protein.name.":"Transcription factor HES-1 ;Transducin-like enhancer of split 2","subunits.Gene.name.":"Hes1;Tle2","subunits.Gene.name.syn.":"Hes-1 Hl;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":3127,"ComplexName":"TLE-Histone H3 complex","Organism":"Human","Synonyms":"None","Cell.line":"Jurkat cells","subunits.UniProt.IDs.":"P68431;Q04724","subunits.Entrez.IDs.":"None;7088","Protein.complex.purification.method":"MI:0047-far western blotting","GO.ID":"GO:0006265;GO:0045892;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;organization of chromosome structure;nucleus","PubMed.ID":9334241,"subunits.Protein.name.":"Histone H3.1;Transducin-like enhancer protein 1","subunits.Gene.name.":"HIST1H3A;;TLE1","subunits.Gene.name.syn.":"H3FA; H3FL; H3FC; H3FB; H3FD; H3FI; H3FH; H3FK; H3FF; H3FJ;None","Disease.comment":"None","Subunits.comment":"Since the authors did not specify histone H3 and TLE, we used HIST1H3A and TLE1.","Complex.comment":"The authors postulate that TLEs regulate gene expression by interacting with nucleosomes through associations with the N-terminus of H3 proteins.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3128,"ComplexName":"Gamma-secretase complex (APH1B, PSEN1, PSENEN, NCSTN)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P49768;Q8WW43;Q92542;Q9NZ42","subunits.Entrez.IDs.":"5663;83464;23385;55851","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016485;GO:0016485;GO:0051090;GO:0023052;GO:0007219;GO:0005886;GO:0005794","GO.description":"protein processing;protein processing;regulation of sequence-specific DNA binding transcription factor activity;signaling;Notch signaling pathway;plasma membrane;Golgi apparatus","FunCat.ID":"14.07.11;18.02.09;30.01;30.05.02.14;70.02;70.08","FunCat.description":"protein processing (proteolytic);regulator of transcription factor;cellular signalling;Notch-receptor signalling pathway;eukaryotic plasma membrane / membrane attached;Golgi","PubMed.ID":15286082,"subunits.Protein.name.":"Presenilin-1;Gamma-secretase subunit APH-1B ;Nicastrin;Gamma-secretase subunit PEN-2","subunits.Gene.name.":"PSEN1;APH1B;NCSTN;PSENEN","subunits.Gene.name.syn.":"AD3 PS1 PSNL1;PSFL;KIAA0253;PEN2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"A multimeric gamma-secretase complex that contains the presenilin-1 or presenilin-2 and the membrane glycoprotein nicastrin processes a number of type I transmembrane proteins such as the beta-amyloid precursor protein and the cell surface receptor notch-1. Three variants of APH1 (APH1A short, APH1A long and APH1B) as well as two presenillin variants (PSEN1 and PSEN2) allow the formation of six different gamma-secretase complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3129,"ComplexName":"STAT6-p100-RHA complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P42226;Q08211;Q7KZF4","subunits.Entrez.IDs.":"6778;1660;27044","Protein.complex.purification.method":"MI:0402- chromatin immunoprecipitation assays","GO.ID":"GO:0051276;GO:0006265;GO:0045893;GO:0003677;GO:0005634","GO.description":"chromosome organization;DNA topological change;positive regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"42.10.03;10.01.09.05;11.02.03.04.01;16.03.01;70.10","FunCat.description":"organization of chromosome structure;DNA conformation modification (e.g. chromatin);transcription activation;DNA binding;nucleus","PubMed.ID":16914450,"subunits.Protein.name.":"Signal transducer and activator of transcription 6 ;ATP-dependent RNA helicase A ;Staphylococcal nuclease domain-containing protein 1","subunits.Gene.name.":"STAT6;DHX9;SND1","subunits.Gene.name.syn.":";DDX9 LKP NDH2;TDRD11","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Experiments show that p100 protein mediates the assembly of the ternary complex  STAT6-p100-RHA. Chromatin immunoprecipitation studies show that RHA together with p100 enhance the binding of STAT6 on the human Ig-epsilon promoter after IL-4 stimulation. The authors propose that the ternary protein complex may facilitate the unwinding of the chromatin structure and accessibility of the promoter.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3130,"ComplexName":"Tle3-Aes complex","Organism":"Mouse","Synonyms":"Grg3b-Grg5 complex","Cell.line":"None","subunits.UniProt.IDs.":"P63002;Q08122","subunits.Entrez.IDs.":"14797;21887","Protein.complex.purification.method":"MI:0096- pull down; MI:0018- two hybrid","GO.ID":"GO:0045892;GO:0005515;GO:0051098;GO:0051090;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;protein binding;regulation of binding;regulation of sequence-specific DNA binding transcription factor activity;nucleus","FunCat.ID":"11.02.03.04.03;16.01;18.01.07;18.02.09;70.10","FunCat.description":"transcription repression;protein binding;regulation by binding / dissociation;regulator of transcription factor;nucleus","PubMed.ID":8955148,"subunits.Protein.name.":"Amino-terminal enhancer of split ;Transducin-like enhancer protein 3","subunits.Gene.name.":"Aes;Tle3","subunits.Gene.name.syn.":"Esp1 Grg Grg5;Esg","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Tle3/Grg3 and Aes/Grg5 heterodimer represses transcription by interacting with transcription factors, thereby regulating cell proliferation and differentiation.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3131,"ComplexName":"Hes1-TLE1 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q04666;Q04724","subunits.Entrez.IDs.":"29577;7088","Protein.complex.purification.method":"MI:0018- two hybrid; MI:0096- pull down","GO.ID":"GO:0045892;GO:0003677;GO:0007219;GO:0022008;GO:0048699;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;DNA binding;Notch signaling pathway;neurogenesis;generation of neurons;nucleus","FunCat.ID":"11.02.03.04.03;16.03.01;30.05.02.14;41.05.13;70.10","FunCat.description":"transcription repression;DNA binding;Notch-receptor signalling pathway;neurogenesis;nucleus","PubMed.ID":8687460,"subunits.Protein.name.":"Transcription factor HES-1 ;Transducin-like enhancer protein 1","subunits.Gene.name.":"Hes1;TLE1","subunits.Gene.name.syn.":"Hes-1 Hl;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Homo sapiens (Human)"}
{"ComplexID":3132,"ComplexName":"OCT1-OBF1-DNA complex","Organism":"Human","Synonyms":"None","Cell.line":"B-cell","subunits.UniProt.IDs.":"P14859;Q16633","subunits.Entrez.IDs.":"5451;5450","Protein.complex.purification.method":"MI:0412-electrophoretic mobility supershift assay","GO.ID":"GO:0045893;GO:0003677;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04.01;16.03.01;70.10","FunCat.description":"transcription activation;DNA binding;nucleus","PubMed.ID":12727885,"subunits.Protein.name.":"POU domain, class 2, transcription factor 1;POU domain class 2-associating factor 1","subunits.Gene.name.":"POU2F1;POU2AF1","subunits.Gene.name.syn.":"OCT1 OTF1;OBF1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The OCT1 dimer is a better substrate for OBF1 than the monomer. OBF1 stabilizes the OCT1 dimer DNA complex by reducing its dissociation rate.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3133,"ComplexName":"Phosphatidylinositol 3-kinase (PIK3CA, PIK3R1)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P27986;P42336","subunits.Entrez.IDs.":"5295;5290","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0005524;GO:0007169;GO:0005886","GO.description":"ATP binding;transmembrane receptor protein tyrosine kinase signaling pathway;plasma membrane","FunCat.ID":"16.19.03;30.05.01.12;70.02","FunCat.description":"ATP binding;transmembrane receptor protein tyrosine kinase signalling pathways;eukaryotic plasma membrane / membrane attached","PubMed.ID":18079394,"subunits.Protein.name.":"Phosphatidylinositol 3-kinase regulatory subunit alpha;Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform","subunits.Gene.name.":"PIK3R1;PIK3CA","subunits.Gene.name.syn.":"GRB1;","Disease.comment":"In different types of cancer PIK3CA was found to be mutated. Defects in the phosphatidylinositol 3-kinase pathway contribute to type II diabetes.","Subunits.comment":"None","Complex.comment":"Phosphatidylinositol 3-kinases (PI3Ks) are lipid kinases that phosphorylate phosphatidylinositol 4,5-bisphosphate at the 3-position of the inositol ring, and thus generate phosphatidylinositol 3,4,5-trisphosphate (PIP3 ), which, in turn, initiates a vast array of signaling events. PI3Ks are heterodimers, composed of catalytic and regulatory subunits, that are activated by growth factor-receptor tyrosine kinases.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3134,"ComplexName":"Na(+)/K(+) ATPase","Organism":"Pig","Synonyms":"None","Cell.line":"kidney","subunits.UniProt.IDs.":"P05024;P05027;Q04646","subunits.Entrez.IDs.":"397481;396898;11936","Protein.complex.purification.method":"MI:0114-x-ray crystallography","GO.ID":"GO:0005524;GO:0008324;GO:0006812;GO:0042626;GO:0005886","GO.description":"ATP binding;cation transmembrane transporter activity;cation transport;ATPase activity, coupled to transmembrane movement of substances;plasma membrane","FunCat.ID":"16.19.03;20.01.01.01;20.03.22;70.02","FunCat.description":"ATP binding;cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);transport ATPases;eukaryotic plasma membrane / membrane attached","PubMed.ID":18075585,"subunits.Protein.name.":"Sodium/potassium-transporting ATPase subunit alpha-1;Sodium/potassium-transporting ATPase subunit beta-1;Sodium/potassium-transporting ATPase subunit gamma","subunits.Gene.name.":"ATP1A1;ATP1B1;Fxyd2","subunits.Gene.name.syn.":"None;None;Atp1c Atp1g1","Disease.comment":"None","Subunits.comment":"Since ATP1G1 from pig was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"None","SWISSPROT.organism":"Sus scrofa (Pig);Sus scrofa (Pig);Mus musculus (Mouse)"}
{"ComplexID":3135,"ComplexName":"TLE1 corepressor complex (MASH1 promoter-corepressor complex)","Organism":"Human","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P06748;P09874;P19338;P34932;Q02880;Q04724;Q15233;Q92878","subunits.Entrez.IDs.":"4869;142;4691;3308;7155;7088;4841;10111","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0045892;GO:0005515;GO:0003677;GO:0051098;GO:0051090;GO:0030182;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;protein binding;DNA binding;regulation of binding;regulation of sequence-specific DNA binding transcription factor activity;neuron differentiation;nucleus","FunCat.ID":"11.02.03.04.03;16.01;16.03.01;18.01.07;18.02.09;43.03.13;70.10","FunCat.description":"transcription repression;protein binding;DNA binding;regulation by binding / dissociation;regulator of transcription factor;neuron;nucleus","PubMed.ID":15607978,"subunits.Protein.name.":"Nucleophosmin ;Poly [ADP-ribose] polymerase 1;Nucleolin ;Heat shock 70 kDa protein 4;DNA topoisomerase 2-beta ;Transducin-like enhancer protein 1;Non-POU domain-containing octamer-binding protein;DNA repair protein RAD50","subunits.Gene.name.":"NPM1;PARP1;NCL;HSPA4;TOP2B;TLE1;NONO;RAD50","subunits.Gene.name.syn.":"NPM;ADPRT PPOL;;APG2;;None;NRB54;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The TLE1 complex is required for HES1-mediated transcription repression. PARP1 is inactive in the TLE1 complex. After Ca(2+) induction, kinase CaMKII-delta activates PARP1 leading to dismissal of the TLE1 corepresspor complex from HES1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3136,"ComplexName":"Hes1-Tle1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q04666;Q62440","subunits.Entrez.IDs.":"29577;21885","Protein.complex.purification.method":"MI:0402- chromatin immunoprecipitation assays","GO.ID":"GO:0045892;GO:0003677;GO:0007219;GO:0022008;GO:0048699;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;DNA binding;Notch signaling pathway;neurogenesis;generation of neurons;nucleus","FunCat.ID":"11.02.03.04.03;16.03.01;30.05.02.14;41.05.13;70.10","FunCat.description":"transcription repression;DNA binding;Notch-receptor signalling pathway;neurogenesis;nucleus","PubMed.ID":15607978,"subunits.Protein.name.":"Transcription factor HES-1 ;Transducin-like enhancer protein 1","subunits.Gene.name.":"Hes1;Tle1","subunits.Gene.name.syn.":"Hes-1 Hl;Grg1","Disease.comment":"None","Subunits.comment":"Since Tle1 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Mus musculus (Mouse)"}
{"ComplexID":3137,"ComplexName":"MASH1 promoter-coactivator complex","Organism":"Human","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P09874;P12931;P24928;P62805;P68431;Q14469;Q15233;Q92793;Q92831","subunits.Entrez.IDs.":"142;6714;5430;None;None;3280;4841;1387;8850","Protein.complex.purification.method":"MI:0402-chromatin immunoprecipitation assays","GO.ID":"GO:0045893;GO:0003677;GO:0051098;GO:0051090;GO:0007219;GO:0030182;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;regulation of binding;regulation of sequence-specific DNA binding transcription factor activity;Notch signaling pathway;neuron differentiation;nucleus","FunCat.ID":"11.02.03.04.01;16.03.01;18.01.07;18.02.09;30.05.02.14;43.03.13;70.10","FunCat.description":"transcription activation;DNA binding;regulation by binding / dissociation;regulator of transcription factor;Notch-receptor signalling pathway;neuron;nucleus","PubMed.ID":15607978,"subunits.Protein.name.":"Poly [ADP-ribose] polymerase 1;Proto-oncogene tyrosine-protein kinase Src;DNA-directed RNA polymerase II subunit RPB1;Histone H4;Histone H3.1;Transcription factor HES-1;Non-POU domain-containing octamer-binding protein;CREB-binding protein;Histone acetyltransferase KAT2B","subunits.Gene.name.":"PARP1;SRC;POLR2A;HIST1H4A;;HIST1H3A;;HES1;NONO;CREBBP;KAT2B","subunits.Gene.name.syn.":"ADPRT PPOL;SRC1;POLR2;H4/A H4FA; H4/I H4FI; H4/G H4FG; H4/B H4FB; H4/J H4FJ; H4/C H4FC; H4/H H4FH; H4/M H4FM; H4/E H4FE; H;H3FA; H3FL; H3FC; H3FB; H3FD; H3FI; H3FH; H3FK; H3FF; H3FJ;BHLHB39 HL HRY;NRB54;CBP;PCAF","Disease.comment":"None","Subunits.comment":"Since the authors did not specify histone H3, we used HIST1H3A.","Complex.comment":"Poly(ADP-ribosyl)ation activity of PARP1 is required for dismissal of the TLE1-corepressor complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3138,"ComplexName":"POSH-AKT2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P31751;Q7Z6J0","subunits.Entrez.IDs.":"208;57630","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007254","GO.description":"JNK cascade","FunCat.ID":"30.01.05.01.02","FunCat.description":"JNK cascade","PubMed.ID":14504284,"subunits.Protein.name.":"RAC-beta serine/threonine-protein kinase ;E3 ubiquitin-protein ligase SH3RF1","subunits.Gene.name.":"AKT2;SH3RF1","subunits.Gene.name.syn.":";KIAA1494 POSH RNF142 SH3MD2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"A POSH mutant unable to bind to Akt2 exhibits increased binding to MLK3. This increased binding of MLK3 to POSH is accompanied by increased activation of the JNK signaling pathway. The results suggest that Akt2 negatively regulates the POSH/JNK signaling complex by phosphorylating MLK3 and promoting the disassembly of the JNK signaling complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3139,"ComplexName":"CRLR-RAMP1-ARRB2 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"O60894;P29067;Q16602","subunits.Entrez.IDs.":"10267;25388;10203","Protein.complex.purification.method":"MI:0663- confocal microscopy","GO.ID":"GO:0007186;GO:0005886","GO.description":"G-protein coupled receptor signaling pathway;plasma membrane","FunCat.ID":"30.05.02.24;70.02","FunCat.description":"G-protein coupled receptor signalling pathway;eukaryotic plasma membrane / membrane attached","PubMed.ID":11535606,"subunits.Protein.name.":"Receptor activity-modifying protein 1 ;Beta-arrestin-2 ;Calcitonin gene-related peptide type 1 receptor","subunits.Gene.name.":"RAMP1;Arrb2;CALCRL","subunits.Gene.name.syn.":";;CGRPR","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"When RAMP1 is expressed with CRLR, it is targeted to the cell surface as a 1:1 heterodimer. CGRP (calcitonin gene-related peptide) binding and receptor activation lead to the phosphorylation of CRLR and the internalization of the receptor as a stable complex. The authers describe that upon a 30-min CGRP treatment, the beta-arrestin2-YFP was redistributed into endocytic vesicles where it co-localized with myc-RAMP1 and HA-CRLR.","SWISSPROT.organism":"Homo sapiens (Human);Rattus norvegicus (Rat);Homo sapiens (Human)"}
{"ComplexID":3140,"ComplexName":"CRLR-RAMP2 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"O60895;Q16602","subunits.Entrez.IDs.":"10266;10203","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007186;GO:0005886","GO.description":"G-protein coupled receptor signaling pathway;plasma membrane","FunCat.ID":"30.05.02.24;70.02","FunCat.description":"G-protein coupled receptor signalling pathway;eukaryotic plasma membrane / membrane attached","PubMed.ID":11387328,"subunits.Protein.name.":"Receptor activity-modifying protein 2 ;Calcitonin gene-related peptide type 1 receptor","subunits.Gene.name.":"RAMP2;CALCRL","subunits.Gene.name.syn.":";CGRPR","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results demonstrate that RAMP2 and RAMP3 and not only RAMP1 can promote the full maturation of CRLR, leading to its terminal glycosylation, and only the fully processed receptors were found to bind AM (adrenomedullin) and CGRP (calcitonin gene-related peptide).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3141,"ComplexName":"CRLR-RAMP3 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"O60896;Q16602","subunits.Entrez.IDs.":"10268;10203","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007186;GO:0005886","GO.description":"G-protein coupled receptor signaling pathway;plasma membrane","FunCat.ID":"30.05.02.24;70.02","FunCat.description":"G-protein coupled receptor signalling pathway;eukaryotic plasma membrane / membrane attached","PubMed.ID":11387328,"subunits.Protein.name.":"Receptor activity-modifying protein 3 ;Calcitonin gene-related peptide type 1 receptor","subunits.Gene.name.":"RAMP3;CALCRL","subunits.Gene.name.syn.":";CGRPR","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results demonstrate that RAMP2 and RAMP3 and not only RAMP1 can promote the full maturation of CRLR, leading to its terminal glycosylation, and only the fully processed receptors were found to bind AM (adrenomedullin) and CGRP (calcitonin gene-related peptide).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3142,"ComplexName":"CAMK2-delta-MASH1 promoter-coactivator complex","Organism":"Human","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P09874;P12931;P24928;Q13557;Q14469;Q15233;Q92793;Q92831","subunits.Entrez.IDs.":"142;6714;5430;817;3280;4841;1387;8850","Protein.complex.purification.method":"MI:0402- chromatin immunoprecipitation assays","GO.ID":"GO:0045893;GO:0005515;GO:0003677;GO:0051098;GO:0051090;GO:0007219;GO:0030182;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;protein binding;DNA binding;regulation of binding;regulation of sequence-specific DNA binding transcription factor activity;Notch signaling pathway;neuron differentiation;nucleus","FunCat.ID":"11.02.03.04.01;16.01;16.03.01;18.01.07;18.02.09;30.05.02.14;43.03.13;70.10","FunCat.description":"transcription activation;protein binding;DNA binding;regulation by binding / dissociation;regulator of transcription factor;Notch-receptor signalling pathway;neuron;nucleus","PubMed.ID":15607978,"subunits.Protein.name.":"Poly [ADP-ribose] polymerase 1;Proto-oncogene tyrosine-protein kinase Src;DNA-directed RNA polymerase II subunit RPB1;Calcium/calmodulin-dependent protein kinase type II subunit delta ;Transcription factor HES-1;Non-POU domain-containing octamer-binding protein;CREB-binding protein;Histone acetyltransferase KAT2B","subunits.Gene.name.":"PARP1;SRC;POLR2A;CAMK2D;HES1;NONO;CREBBP;KAT2B","subunits.Gene.name.syn.":"ADPRT PPOL;SRC1;POLR2;CAMKD;BHLHB39 HL HRY;NRB54;CBP;PCAF","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"HES1 is phosphorylated by CAMKII-delta during neural stem cell differentiation. This phosphorylation is linked to recruitment of coactivator complexes on the MASH1 promoter.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3143,"ComplexName":"Sos1-Abi1-Eps8 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q08509;Q62245;Q8CBW3","subunits.Entrez.IDs.":"13860;20662;11308","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0007264;GO:0007169","GO.description":"small GTPase mediated signal transduction;transmembrane receptor protein tyrosine kinase signaling pathway","FunCat.ID":"30.01.05.05.01;30.05.01.12","FunCat.description":"small GTPase mediated signal transduction;transmembrane receptor protein tyrosine kinase signalling pathways","PubMed.ID":11777939,"subunits.Protein.name.":"Epidermal growth factor receptor kinase substrate 8;Son of sevenless homolog 1;Abl interactor 1","subunits.Gene.name.":"Eps8;Sos1;Abi1","subunits.Gene.name.syn.":"None;None;Ssh3bp1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors describe the formation of either a Sos-1-Grb2 (S/G) or a Sos-1-E3b1-Eps8 (S/E/E8) complex, endowed with Ras- and Rac-specific GEF activities, respectively. Sos-1-Grb2 complex is disrupted upon RTKs (receptor tyrosine kinases) activation, whereas the S/E/E8 complex is not.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3144,"ComplexName":"Sos1-Grb2 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"P62993;Q07889","subunits.Entrez.IDs.":"2885;6654","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0007264;GO:0007169","GO.description":"small GTPase mediated signal transduction;transmembrane receptor protein tyrosine kinase signaling pathway","FunCat.ID":"30.01.05.05.01;30.05.01.12","FunCat.description":"small GTPase mediated signal transduction;transmembrane receptor protein tyrosine kinase signalling pathways","PubMed.ID":11777939,"subunits.Protein.name.":"Growth factor receptor-bound protein 2;Son of sevenless homolog 1","subunits.Gene.name.":"GRB2;SOS1","subunits.Gene.name.syn.":"ASH;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors describe the formation of either a Sos-1-Grb2 (S/G) or a Sos-1-E3b1-Eps8 (S/E/E8) complex, endowed with Ras- and Rac-specific GEF activities, respectively. Sos-1-Grb2 complex is disrupted upon RTKs (receptor tyrosine kinases) activation, whereas the S/E/E8 complex is not.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3145,"ComplexName":"Coatomer complex","Organism":"Rabbit","Synonyms":"None","Cell.line":"liver","subunits.UniProt.IDs.":"O55029;O89079;P61924;Q5XJY5;Q8CIE6;Q9JIF7;Q9QZE5","subunits.Entrez.IDs.":"50797;59042;56447;213827;12847;70349;54161","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies;MI:0019-coimmunoprecipitation;MI:0029-cosedimentation through density gradients","GO.ID":"GO:0015031;GO:0008565;GO:0006900;GO:0016050;GO:0030133;GO:0005737","GO.description":"protein transport;protein transporter activity;membrane budding;vesicle organization;transport vesicle;cytoplasm","FunCat.ID":"20.01.10;20.09.07.25;70.09;70.03","FunCat.description":"protein transport;vesicle formation;intracellular transport vesicles;cytoplasm","PubMed.ID":9482852,"subunits.Protein.name.":"Coatomer subunit beta';Coatomer subunit epsilon;Coatomer subunit zeta-1;Coatomer subunit delta;Coatomer subunit alpha;Coatomer subunit beta;Coatomer subunit gamma-1","subunits.Gene.name.":"Copb2;Cope;Copz1;Arcn1;Copa;Copb1;Copg1","subunits.Gene.name.syn.":"None;Cope1;Copz;Copd;None;Copb;Copg","Disease.comment":"None","Subunits.comment":"Since the proteins from rabbit were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.","Complex.comment":"The coatomer complex is described as a cytosolic complex of seven subunits alpha- to zeta-coat proteins (COPs), that with ADP ribosylation factor (ARF1) cover the surface of COPI-coated vesicles.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3146,"ComplexName":"Coatomer-Arf1 complex","Organism":"Rabbit","Synonyms":"None","Cell.line":"liver","subunits.UniProt.IDs.":"O55029;O89079;P61924;P84078;Q5XJY5;Q8CIE6;Q9JIF7;Q9QZE5","subunits.Entrez.IDs.":"50797;59042;56447;11840;213827;12847;70349;54161","Protein.complex.purification.method":"MI:0029-cosedimentation through density gradients","GO.ID":"GO:0015031;GO:0008565;GO:0006900;GO:0016050;GO:0030133;GO:0005794","GO.description":"protein transport;protein transporter activity;membrane budding;vesicle organization;transport vesicle;Golgi apparatus","FunCat.ID":"20.01.10;20.09.07.25;70.09;70.08","FunCat.description":"protein transport;vesicle formation;intracellular transport vesicles;Golgi","PubMed.ID":9482852,"subunits.Protein.name.":"Coatomer subunit beta';Coatomer subunit epsilon;Coatomer subunit zeta-1;ADP-ribosylation factor 1;Coatomer subunit delta;Coatomer subunit alpha;Coatomer subunit beta;Coatomer subunit gamma-1","subunits.Gene.name.":"Copb2;Cope;Copz1;Arf1;Arcn1;Copa;Copb1;Copg1","subunits.Gene.name.syn.":"None;Cope1;Copz;None;Copd;None;Copb;Copg","Disease.comment":"None","Subunits.comment":"Since the proteins from rabbit were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.","Complex.comment":"The authors describe that ARF1-GTP is tightly bound to the membrane and coatomer can be recruited from the cytosol to the Golgi membrane only after binding ARF1-GTP.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3147,"ComplexName":"Beta/delta-coat protein subcomplex","Organism":"Rabbit","Synonyms":"None","Cell.line":"liver","subunits.UniProt.IDs.":"Q5XJY5;Q9JIF7","subunits.Entrez.IDs.":"213827;70349","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0226-ion exchange chromatography","GO.ID":"GO:0015031;GO:0008565;GO:0006900;GO:0016050;GO:0030133;GO:0005737","GO.description":"protein transport;protein transporter activity;membrane budding;vesicle organization;transport vesicle;cytoplasm","FunCat.ID":"20.01.10;20.09.07.25;70.09;70.03","FunCat.description":"protein transport;vesicle formation;intracellular transport vesicles;cytoplasm","PubMed.ID":9482852,"subunits.Protein.name.":"Coatomer subunit delta;Coatomer subunit beta","subunits.Gene.name.":"Arcn1;Copb1","subunits.Gene.name.syn.":"Copd;Copb","Disease.comment":"None","Subunits.comment":"Since the proteins from rabbit were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.","Complex.comment":"After dissociation/reassociation of the coatomer  with DMMA the authors isolated a subcomplex of coatomer consisting of beta- and delta-COPs that is able to bind to Golgi membranes in an ARF1- and GTP-dependent manner.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3148,"ComplexName":"Arf1-beta/delta-coat protein subcomplex","Organism":"Rabbit","Synonyms":"None","Cell.line":"liver","subunits.UniProt.IDs.":"P84078;Q5XJY5;Q9JIF7","subunits.Entrez.IDs.":"11840;213827;70349","Protein.complex.purification.method":"MI:0029-cosedimentation through density gradients","GO.ID":"GO:0015031;GO:0008565;GO:0006900;GO:0016050;GO:0030133;GO:0005794","GO.description":"protein transport;protein transporter activity;membrane budding;vesicle organization;transport vesicle;Golgi apparatus","FunCat.ID":"20.01.10;20.09.07.25;70.09;70.08","FunCat.description":"protein transport;vesicle formation;intracellular transport vesicles;Golgi","PubMed.ID":9482852,"subunits.Protein.name.":"ADP-ribosylation factor 1;Coatomer subunit delta;Coatomer subunit beta","subunits.Gene.name.":"Arf1;Arcn1;Copb1","subunits.Gene.name.syn.":"None;Copd;Copb","Disease.comment":"None","Subunits.comment":"Since the proteins from rabbit were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.","Complex.comment":"After dissociation/reassociation of the coatomer  with DMMA the authors isolated a subcomplex of coatomer consisting of beta- and delta-COPs that is able to bind to Golgi membranes in an ARF1- and GTP-dependent manner.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3149,"ComplexName":"NK-3-Groucho-HIPK2-SIN3A-RbpA48-HDAC1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q04724;Q09028;Q13547;Q96ST3;Q99801;Q9H2X6","subunits.Entrez.IDs.":"7088;5928;3065;25942;4824;28996","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation;MI:0096-pull down","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;organization of chromosome structure;nucleus","PubMed.ID":10559189,"subunits.Protein.name.":"Transducin-like enhancer protein 1;Histone-binding protein RBBP4;Histone deacetylase 1;Paired amphipathic helix protein Sin3a;Homeobox protein Nkx-3.1;Homeodomain-interacting protein kinase 2","subunits.Gene.name.":"TLE1;RBBP4;HDAC1;SIN3A;NKX3-1;HIPK2","subunits.Gene.name.syn.":"None;RBAP48;RPD3L1;None;NKX3.1 NKX3A;None","Disease.comment":"None","Subunits.comment":"Since the authors did not specify NKX3 and TLE, we used NKX3-1 and TLE1.","Complex.comment":"The authors postulate that the Nk-3 homeodomain protein recruits a corepressor complex containing Groucho protein, HIPK2 and a histone deacetylase complex to repress transcription.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3150,"ComplexName":"NK-3-Groucho complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q04724;Q99801","subunits.Entrez.IDs.":"7088;4824","Protein.complex.purification.method":"MI:0096-pull down","GO.ID":"GO:0045892;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;nucleus","FunCat.ID":"11.02.03.04.03;70.10","FunCat.description":"transcription repression;nucleus","PubMed.ID":10559189,"subunits.Protein.name.":"Transducin-like enhancer protein 1;Homeobox protein Nkx-3.1","subunits.Gene.name.":"TLE1;NKX3-1","subunits.Gene.name.syn.":"None;NKX3.1 NKX3A","Disease.comment":"None","Subunits.comment":"Since the authors did not specify NKX3 and TLE, we used NKX3-1 and TLE1.","Complex.comment":"NK-3 homeodomain protein can associate wih the human Groucho homolog TLE in the absence of DNA. This interaction translocates Groucho proteins from the cytoplasm into the nucleus.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3151,"ComplexName":"Sulphiredoxin-peroxiredoxin complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q06830;Q9BYN0","subunits.Entrez.IDs.":"5052;140809","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0005524;GO:0007165;GO:0005737","GO.description":"ATP binding;signal transduction;cytoplasm","FunCat.ID":"16.19.03;30;70.03","FunCat.description":"ATP binding;CELLULAR COMMUNICATION/SIGNAL TRANSDUCTION MECHANISM;cytoplasm","PubMed.ID":18172504,"subunits.Protein.name.":"Peroxiredoxin-1;Sulfiredoxin-1","subunits.Gene.name.":"PRDX1;SRXN1","subunits.Gene.name.syn.":"PAGA, PAGB, TDPX2;C20orf139 SRX","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Typical 2-Cys peroxiredoxins (Prxs) have an important role in regulating hydrogen peroxide-mediated cell signalling. In this process, Prxs can become inactivated through the hyperoxidation of an active site Cys residue to Cys sulphinic acid. The unique repair of this moiety by sulphiredoxin (Srx) restores peroxidase activity and terminates the signal.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3152,"ComplexName":"Notch1(N-TM)-Notch1(N-EC) heterodimer complex","Organism":"Mouse","Synonyms":"Notch1(p120)-Notch1(p200) heterodimer","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"Q01705","subunits.Entrez.IDs.":"18128","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0005515;GO:0007219","GO.description":"protein binding;Notch signaling pathway","FunCat.ID":"16.01;30.05.02.14","FunCat.description":"protein binding;Notch-receptor signalling pathway","PubMed.ID":9653148,"subunits.Protein.name.":"Neurogenic locus notch homolog protein 1","subunits.Gene.name.":"Notch1","subunits.Gene.name.syn.":"Motch","Disease.comment":"None","Subunits.comment":"The Furine-like protease proteolytically processes Notch 1 precursor (p300) into an intracellular part (N-TM or p120) bound to the plasma membrane and into an extracellular part, N-EC or p200. Both parts form a heterodimeric complex able to bind the ligand Delta.","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse)"}
{"ComplexID":3153,"ComplexName":"GNAQ-GEFT-RHOA complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P50148;P61586;Q86VW2","subunits.Entrez.IDs.":"2776;387;115557","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0005525","GO.description":"GTP binding","FunCat.ID":"16.19.05","FunCat.description":"GTP binding","PubMed.ID":18096806,"subunits.Protein.name.":"Guanine nucleotide-binding protein G;Transforming protein RhoA ;Rho guanine nucleotide exchange factor 25","subunits.Gene.name.":"GNAQ;RHOA;ARHGEF25","subunits.Gene.name.syn.":"GAQ;ARH12 ARHA RHO12;GEFT","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"It is assumed that the complex is involved in signal transduction.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3154,"ComplexName":"Notch2(N-TM)-Notch2(N-EC)-Delta complex","Organism":"Human","Synonyms":"None","Cell.line":"SJ-NB5 cells","subunits.UniProt.IDs.":"O00548;Q04721","subunits.Entrez.IDs.":"28514;4853","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0007219;GO:0005886","GO.description":"Notch signaling pathway;plasma membrane","FunCat.ID":"30.05.02.14;70.02","FunCat.description":"Notch-receptor signalling pathway;eukaryotic plasma membrane / membrane attached","PubMed.ID":9244302,"subunits.Protein.name.":"Delta-like protein 1;Neurogenic locus notch homolog protein 2","subunits.Gene.name.":"DLL1;NOTCH2","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"Since the authors did not specify DLL, we used DLL1.","Complex.comment":"In the trans-Golgi-network Notch2 is cleaved into the transmembrane Notch2(N-TM) subunit and into the extracellular Notch2(N-EC) subunit. Both subunits form a heterodimeric complex. The ligand Delta binds only to the heterodimeric form of Notch.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3155,"ComplexName":"Bipartite complex (TFC4, CTNNB1)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P35222;Q9NQB0","subunits.Entrez.IDs.":"1499;6934","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006351;GO:0016055","GO.description":"transcription, DNA-templated;Wnt signaling pathway","FunCat.ID":"11;30.05.02.20","FunCat.description":"TRANSCRIPTION;Wnt signalling pathway","PubMed.ID":17072303,"subunits.Protein.name.":"Catenin beta-1;Transcription factor 7-like 2","subunits.Gene.name.":"CTNNB1;TCF7L2","subunits.Gene.name.syn.":"CTNNB;TCF4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"As a consequence of engaging the canonical Wnt pathway, a beta-catenin-T-cell factor (TCF) transcriptional complex is generated, which has been postulated to trigger the epithelial-mesenchymal transition (EMT) that characterizes the tissue-invasive phenotype of breast cancer.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3156,"ComplexName":"CBF1-HDAC1-SMRT complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q06330;Q13547;Q9Y618","subunits.Entrez.IDs.":"3516;3065;9612","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;organization of chromosome structure;nucleus","PubMed.ID":9694793,"subunits.Protein.name.":"Recombining binding protein suppressor of hairless ;Histone deacetylase 1;Nuclear receptor corepressor 2","subunits.Gene.name.":"RBPJ;HDAC1;NCOR2","subunits.Gene.name.syn.":"IGKJRB IGKJRB1 RBPJK RBPSUH;RPD3L1;CTG26","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"CBF1 interacts with a corepressor complex containing HDAC1 and SMRT. Activation of Notch disrupts the formation of the repressor complex by competing of SMRT and Notch for binding with CBF1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3157,"ComplexName":"PR -PRLR complex","Organism":"Human","Synonyms":"H1:R2 complex; Prolactin-PRL receptor complex","Cell.line":"None","subunits.UniProt.IDs.":"P01236;P16471","subunits.Entrez.IDs.":"5617;5618","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":16556730,"subunits.Protein.name.":"Prolactin;Prolactin receptor","subunits.Gene.name.":"PRL;PRLR","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"H1:R2 complex consists of one prolactin molecule and one receptor dimer. The process of receptor dimerization can be either constitutive or ligand dependent.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3158,"ComplexName":"RIAM-Rap1-GTP-profilin complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"P07737;P62834;Q7Z5R6","subunits.Entrez.IDs.":"5216;5906;54518","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0007155;GO:0030036","GO.description":"cell adhesion;actin cytoskeleton organization","FunCat.ID":"34.07;42.04.03","FunCat.description":"cell adhesion;actin cytoskeleton","PubMed.ID":15469846,"subunits.Protein.name.":"Profilin-1 ;Ras-related protein Rap-1A;Amyloid beta A4 precursor protein-binding family B member 1-interacting protein","subunits.Gene.name.":"PFN1;RAP1A;APBB1IP","subunits.Gene.name.syn.":";KREV1;PREL1 RARP1 RIAM","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results indicate that RIAM can function as a link between Rap1-GTP and the actin regulator Profilin either by direct RIAM binding to Profilin or by RIAM recruitment of Ena/VASP-Profilin complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3159,"ComplexName":"RIAM-profilin complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P07737;Q7Z5R6","subunits.Entrez.IDs.":"5216;54518","Protein.complex.purification.method":"MI:0018- two hybrid","GO.ID":"GO:0007155;GO:0030036","GO.description":"cell adhesion;actin cytoskeleton organization","FunCat.ID":"34.07;42.04.03","FunCat.description":"cell adhesion;actin cytoskeleton","PubMed.ID":15469846,"subunits.Protein.name.":"Profilin-1 ;Amyloid beta A4 precursor protein-binding family B member 1-interacting protein","subunits.Gene.name.":"PFN1;APBB1IP","subunits.Gene.name.syn.":";PREL1 RARP1 RIAM","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"RIAM  interacts with Profilin and Ena/VASP proteins, molecules that regulate actin dynamics.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3160,"ComplexName":"RIAM-VASP complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P50552;Q7Z5R6","subunits.Entrez.IDs.":"7408;54518","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0007155;GO:0030036","GO.description":"cell adhesion;actin cytoskeleton organization","FunCat.ID":"34.07;42.04.03","FunCat.description":"cell adhesion;actin cytoskeleton","PubMed.ID":15469846,"subunits.Protein.name.":"Vasodilator-stimulated phosphoprotein;Amyloid beta A4 precursor protein-binding family B member 1-interacting protein","subunits.Gene.name.":"VASP;APBB1IP","subunits.Gene.name.syn.":"None;PREL1 RARP1 RIAM","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"RIAM  interacts with Profilin and Ena/VASP proteins, molecules that regulate actin dynamics.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3161,"ComplexName":"PRL receptor (PRLR) dimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P16471","subunits.Entrez.IDs.":"5618","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":16556730,"subunits.Protein.name.":"Prolactin receptor","subunits.Gene.name.":"PRLR","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The process of receptor dimerization can be either constitutive or ligand dependent. The receptor dimer appears in variant (alternatively spliced) forms: As heterodimer long form (LF) - short form (SF) S1a/S1b and homodimers LF - LF, SF - SF.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":3162,"ComplexName":"TF-FVIIa-FXa-TFPI complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P00742;P08709;P10646;P13726","subunits.Entrez.IDs.":"2159;2155;7035;2152","Protein.complex.purification.method":"MI:0017- classical fluorescence spectroscopy","GO.ID":"GO:0007596","GO.description":"blood coagulation","FunCat.ID":"36.25.16.09","FunCat.description":"blood coagulation","PubMed.ID":12787023,"subunits.Protein.name.":"Coagulation factor X ;Coagulation factor VII ;Tissue factor pathway inhibitor ;Tissue factor","subunits.Gene.name.":"F10;F7;TFPI;F3","subunits.Gene.name.syn.":";;LACI TFPI1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors describe that the FXa-dependent inhibition of TF-FVIIa activity by TFPI leads to formation of the quaternary complex TF-FVIIa-FXa-TFPI.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3163,"ComplexName":"VILIP-1-AChR-alpha-4-AChR-beta-2 complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P09483;P12390;P62762","subunits.Entrez.IDs.":"25590;54239;24877","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0005509;GO:0050789;GO:0005216;GO:0007268","GO.description":"calcium ion binding;regulation of biological process;ion channel activity;synaptic transmission","FunCat.ID":"16.17.01;18;20.03.01.01;34.03.01","FunCat.description":"calcium binding;REGULATION OF METABOLISM AND PROTEIN FUNCTION;ion channels;synaptic transmission","PubMed.ID":12202488,"subunits.Protein.name.":"Neuronal acetylcholine receptor subunit alpha-4;Neuronal acetylcholine receptor subunit beta-2 ;Visinin-like protein 1","subunits.Gene.name.":"Chrna4;Chrnb2;Vsnl1","subunits.Gene.name.syn.":"Acra4;Acrb2;Visl1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results suggest a rule for VILIP-1 as an AChR-associated protein that modulates the surface expression levels and functional properties of alpha 4-beta 2 AChRs in response to changes in the intracellular levels of calcium.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":3164,"ComplexName":"HESX1-TLE1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q04724;Q9UBX0","subunits.Entrez.IDs.":"7088;8820","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies;MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045892;GO:0003677;GO:0007219;GO:0005634;GO:0021983","GO.description":"negative regulation of transcription, DNA-templated;DNA binding;Notch signaling pathway;nucleus;pituitary gland development","FunCat.ID":"11.02.03.04.03;16.03.01;30.05.02.14;70.10","FunCat.description":"transcription repression;DNA binding;Notch-receptor signalling pathway;nucleus","PubMed.ID":11731482,"subunits.Protein.name.":"Transducin-like enhancer protein 1;Homeobox expressed in ES cells 1","subunits.Gene.name.":"TLE1;HESX1","subunits.Gene.name.syn.":"None;HANF","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"HESX1 recruits the TLE1 corepressor to specific promoters during pituitary organogenesis. This complex completely abolishes transcriptional activation mediated by PROP1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3166,"ComplexName":"AXIN-APC-betaCatenin-GSK3B complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15169;P25054;P35222;P49841","subunits.Entrez.IDs.":"8312;324;1499;2932","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0016055","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;Wnt signaling pathway","FunCat.ID":"14.07.03;30.05.02.20","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;Wnt signalling pathway","PubMed.ID":10906131,"subunits.Protein.name.":"Axin-1 ;Adenomatous polyposis coli protein;Catenin beta-1;Glycogen synthase kinase-3 beta","subunits.Gene.name.":"AXIN1;APC;CTNNB1;GSK3B","subunits.Gene.name.syn.":"AXIN;DP2.5;CTNNB;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Interactions:  The RGS domains of Axin and conductin interact directly with the region containing the third to seventh 20-aa repeats of APC. The interaction of APC with Axin is important for regulating the stability of b-catenin. APC promotes a GSK-3b-dependent phosphorylation of b-catenin by interacting with Axin, thereby down-regulating b-catenin. APC binds not to GSK-3b but forms a complex with GSK-3b when Axin is present.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3167,"ComplexName":"NCOR-SIN3-HDAC-HESX1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75182;Q13547;Q92769;Q96ST3;Q9UBX0;Q9Y618","subunits.Entrez.IDs.":"23309;3065;3066;25942;8820;9612","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0003677;GO:0007219;GO:0051276;GO:0005634;GO:0021983","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;DNA binding;Notch signaling pathway;chromosome organization;nucleus;pituitary gland development","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;16.03.01;30.05.02.14;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;DNA binding;Notch-receptor signalling pathway;organization of chromosome structure;nucleus","PubMed.ID":11731482,"subunits.Protein.name.":"Paired amphipathic helix protein Sin3b;Histone deacetylase 1;Histone deacetylase 2;Paired amphipathic helix protein Sin3a;Homeobox expressed in ES cells 1 ;Nuclear receptor corepressor 2","subunits.Gene.name.":"SIN3B;HDAC1;HDAC2;SIN3A;HESX1;NCOR2","subunits.Gene.name.syn.":"KIAA0700;RPD3L1;None;None;HANF;CTG26","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"HESX1 recruits the N-Cor-SIN3-HDAC complex to specific promoters during pituitary organogenesis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3168,"ComplexName":"DAXX-AXIN complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"O15169;Q9UER7","subunits.Entrez.IDs.":"8312;1616","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0051098;GO:0005515;GO:0019209;GO:0051090;GO:0009314;GO:0006915","GO.description":"regulation of binding;protein binding;kinase activator activity;regulation of sequence-specific DNA binding transcription factor activity;response to radiation;apoptotic process","FunCat.ID":"18.01.07;16.01;18.02.01.01.05;18.02.09;32.01.13;40.10.02","FunCat.description":"regulation by binding / dissociation;protein binding;kinase activator;regulator of transcription factor;electromagnetic waves stress response (e.g. UV, X-ray);apoptosis (type I programmed cell death)","PubMed.ID":17210684,"subunits.Protein.name.":"Axin-1 ;Death domain-associated protein 6","subunits.Gene.name.":"AXIN1;DAXX","subunits.Gene.name.syn.":"AXIN;BING2 DAP6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The Daxx-Axin complex formation is enhanced by UV-irradiation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3169,"ComplexName":"Daxx-Axin complex","Organism":"Mouse","Synonyms":"None","Cell.line":"293T cells","subunits.UniProt.IDs.":"O35613;O35625","subunits.Entrez.IDs.":"13163;12005","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0051098;GO:0005515;GO:0019209;GO:0051090;GO:0006915","GO.description":"regulation of binding;protein binding;kinase activator activity;regulation of sequence-specific DNA binding transcription factor activity;apoptotic process","FunCat.ID":"18.01.07;16.01;18.02.01.01.05;18.02.09;40.10.02","FunCat.description":"regulation by binding / dissociation;protein binding;kinase activator;regulator of transcription factor;apoptosis (type I programmed cell death)","PubMed.ID":17210684,"subunits.Protein.name.":"Death domain-associated protein 6 ;Axin-1","subunits.Gene.name.":"Daxx;Axin1","subunits.Gene.name.syn.":";Axin Fu","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The Daxx-Axin complex formation is enhanced by UV-irradiation.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3170,"ComplexName":"Daxx-Axin-p53 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"O15169;P04637;Q9UER7","subunits.Entrez.IDs.":"8312;7157;1616","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0009314;GO:0006915;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;response to radiation;apoptotic process;nucleus","FunCat.ID":"11.02.03.04;32.01.13;40.10.02;70.10","FunCat.description":"transcriptional control;electromagnetic waves stress response (e.g. UV, X-ray);apoptosis (type I programmed cell death);nucleus","PubMed.ID":17210684,"subunits.Protein.name.":"Axin-1 ;Cellular tumor antigen p53;Death domain-associated protein 6","subunits.Gene.name.":"AXIN1;TP53;DAXX","subunits.Gene.name.syn.":"AXIN;P53;BING2 DAP6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Axin enhances the interaction between DAXX and p53 in a dose-dependent manner. DAXX does not directly interact with p53, but through a bridge by Axin. DAXX-Axin-p53 complex promotes HIPK2 phosphorylation of p53 at Ser(46).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3171,"ComplexName":"GluR6a-GluR6b-KA2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P39087;Q61626","subunits.Entrez.IDs.":"14806;14809","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0007268;GO:0005886","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;synaptic transmission;plasma membrane","FunCat.ID":"20.01.01.01;20.03.01.01;34.03.01;70.02","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;synaptic transmission;eukaryotic plasma membrane / membrane attached","PubMed.ID":16102538,"subunits.Protein.name.":"Glutamate receptor ionotropic, kainate 2 ;Glutamate receptor ionotropic, kainate 5","subunits.Gene.name.":"Grik2;Grik5","subunits.Gene.name.syn.":"Glur6;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The splice variants GluR6a and GluR6b which differ in their C-terminal domains can assemble in vivo within the same KAR complex, together with KA2.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3172,"ComplexName":"NUMB-TP53-MDM2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04637;P49757;Q00987","subunits.Entrez.IDs.":"7157;8650;4193","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515;GO:0007219;GO:0023052","GO.description":"protein binding;Notch signaling pathway;signaling","FunCat.ID":"16.01;30.05.02.14;30.01","FunCat.description":"protein binding;Notch-receptor signalling pathway;cellular signalling","PubMed.ID":18172499,"subunits.Protein.name.":"Cellular tumor antigen p53;Protein numb homolog;E3 ubiquitin-protein ligase Mdm2","subunits.Gene.name.":"TP53;NUMB;MDM2","subunits.Gene.name.syn.":"P53;None;","Disease.comment":"In breast cancers, loss of NUMB expression causes increased activity of the receptor NOTCH. Thus, in these cancers, a single event-loss of NUMB expression determines activation of an oncogene (NOTCH) and attenuation of the p53 tumour suppressor pathway.","Subunits.comment":"None","Complex.comment":"NUMB enters in a tricomplex with p53 and the E3 ubiquitin ligase MDM2, thereby preventing ubiquitination and degradation of p53. This results in increased p53 protein levels and activity, and in regulation of p53-dependent phenotypes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3173,"ComplexName":"CIN85 homotetramer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q96B97","subunits.Entrez.IDs.":"30011","Protein.complex.purification.method":"MI:0031- protein cross-linking with a bifunctional reagent","GO.ID":"GO:0007169","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway","FunCat.ID":"30.05.01.12","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways","PubMed.ID":11071869,"subunits.Protein.name.":"SH3 domain-containing kinase-binding protein 1","subunits.Gene.name.":"SH3KBP1","subunits.Gene.name.syn.":"CIN85","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"CIN85 interacted with itself via its coiledcoil region, regardless of EGF stimulation.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":3174,"ComplexName":"CIN85-BLNK complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q8WV28;Q96B97","subunits.Entrez.IDs.":"29760;30011","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007169;GO:0005737","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway;cytoplasm","FunCat.ID":"30.05.01.12;70.03","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways;cytoplasm","PubMed.ID":11071869,"subunits.Protein.name.":"B-cell linker protein ;SH3 domain-containing kinase-binding protein 1","subunits.Gene.name.":"BLNK;SH3KBP1","subunits.Gene.name.syn.":"BASH SLP65;CIN85","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors suggest a novel mechanism in regulation of the B cell signaling events in which CIN85 plays a specific role by association with BLNK or c-Cbl.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3175,"ComplexName":"CIN85-c-CBL complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P22681;Q96B97","subunits.Entrez.IDs.":"867;30011","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007169;GO:0005737","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway;cytoplasm","FunCat.ID":"30.05.01.12;70.03","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways;cytoplasm","PubMed.ID":11071869,"subunits.Protein.name.":"E3 ubiquitin-protein ligase CBL;SH3 domain-containing kinase-binding protein 1","subunits.Gene.name.":"CBL;SH3KBP1","subunits.Gene.name.syn.":"CBL2, RNF55;CIN85","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors suggest a novel mechanism in regulation of the B cell signaling events in which CIN85 plays a specific role by association with BLNK or c-Cbl.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3176,"ComplexName":"USP1-UAF1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O94782;Q8TAF3","subunits.Entrez.IDs.":"7398;57599","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies;MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0016579;GO:0006974;GO:0005634","GO.description":"protein deubiquitination;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"14.07.05;32.01.09;70.10","FunCat.description":"modification by ubiquitination, deubiquitination;DNA damage response;nucleus","PubMed.ID":18082604,"subunits.Protein.name.":"Ubiquitin carboxyl-terminal hydrolase 1;WD repeat-containing protein 48","subunits.Gene.name.":"USP1;WDR48","subunits.Gene.name.syn.":"UBP;KIAA1449, UAF1","Disease.comment":"This complex regulates the Fanconi anemia (OMIM:227646) pathway by deubiquitinating FANCD2.","Subunits.comment":"None","Complex.comment":"The active USP1-UAF1 complex deubiquitinates FANCD2 both as a dimeric complex and a ternary complex containing autocleaved USP1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3177,"ComplexName":"GNA14-p115RhoGEF complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95837;Q92888","subunits.Entrez.IDs.":"9630;9138","Protein.complex.purification.method":"MI:0114- x-ray crystallography; MI:0019- coimmunoprecipitation","GO.ID":"GO:0000902;GO:0016049","GO.description":"cell morphogenesis;cell growth","FunCat.ID":"40.01","FunCat.description":"cell growth / morphogenesis","PubMed.ID":15735747,"subunits.Protein.name.":"Guanine nucleotide-binding protein subunit alpha-14 ;Rho guanine nucleotide exchange factor 1","subunits.Gene.name.":"GNA14;ARHGEF1","subunits.Gene.name.syn.":";None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The G-protein alpha subunit a13 regulates cell growth and differentiation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3178,"ComplexName":"Frs2-Shp2 complex, FGF stimulated","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P35235;Q8C180","subunits.Entrez.IDs.":"19247;327826","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0008543","GO.description":"fibroblast growth factor receptor signaling pathway","FunCat.ID":"30.05.01.12.03","FunCat.description":"FGF-receptor signalling pathway","PubMed.ID":9632781,"subunits.Protein.name.":"Tyrosine-protein phosphatase non-receptor type 11;Fibroblast growth factor receptor substrate 2","subunits.Gene.name.":"Ptpn11;Frs2","subunits.Gene.name.syn.":"None;Frs2a","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3179,"ComplexName":"Grb2-Shp2 complex, FGF stimulated","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P35235;Q60631","subunits.Entrez.IDs.":"19247;14784","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0008543","GO.description":"fibroblast growth factor receptor signaling pathway","FunCat.ID":"30.05.01.12.03","FunCat.description":"FGF-receptor signalling pathway","PubMed.ID":9632781,"subunits.Protein.name.":"Tyrosine-protein phosphatase non-receptor type 11;Growth factor receptor-bound protein 2","subunits.Gene.name.":"Ptpn11;Grb2","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"On the basis of further experiments the authors conclude that FGF stimulation leads to tyrosine phosphorylation of Shp2 and association with the Grb2-Sos complex.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3180,"ComplexName":"Shp2-Sos complex, FGF stimulated","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P35235;Q62245","subunits.Entrez.IDs.":"19247;20662","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0008543","GO.description":"fibroblast growth factor receptor signaling pathway","FunCat.ID":"30.05.01.12.03","FunCat.description":"FGF-receptor signalling pathway","PubMed.ID":9632781,"subunits.Protein.name.":"Tyrosine-protein phosphatase non-receptor type 11;Son of sevenless homolog 1","subunits.Gene.name.":"Ptpn11;Sos1","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"On the basis of further experiments the authors conclude that FGF stimulation leads to tyrosine phosphorylation of Shp2 and association with the Grb2-Sos complex.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3181,"ComplexName":"LMO4-CREB complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"P16220;P61968","subunits.Entrez.IDs.":"1385;8543","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0045893;GO:0019722;GO:0022008;GO:0048699","GO.description":"positive regulation of transcription, DNA-templated;calcium-mediated signaling;neurogenesis;generation of neurons","FunCat.ID":"11.02.03.04.01;30.01.09.03;41.05.13","FunCat.description":"transcription activation;Ca2+ mediated signal transduction;neurogenesis","PubMed.ID":16899735,"subunits.Protein.name.":"Cyclic AMP-responsive element-binding protein 1;LIM domain transcription factor LMO4","subunits.Gene.name.":"CREB1;LMO4","subunits.Gene.name.syn.":"None;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Most probably homodimerization of LMO4 and interaction with CREB is necessary for full Ca(2+)-dependent transcription activation. This complex plays a key role in patterning thalamocortical connections during development.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3182,"ComplexName":"FHL2 homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q14192","subunits.Entrez.IDs.":"2274","Protein.complex.purification.method":"MI:0018- two hybrid","GO.ID":"GO:2001141;GO:0006355;GO:0051098;GO:0005515;GO:0051090","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;regulation of binding;protein binding;regulation of sequence-specific DNA binding transcription factor activity","FunCat.ID":"11.02.03.04;18.01.07;16.01;18.02.09","FunCat.description":"transcriptional control;regulation by binding / dissociation;protein binding;regulator of transcription factor","PubMed.ID":11046156,"subunits.Protein.name.":"Four and a half LIM domains protein 2","subunits.Gene.name.":"FHL2","subunits.Gene.name.syn.":"DRAL SLIM3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"FHL2 protein forms homodimer complexes.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":3183,"ComplexName":"PDGFRA-SHP-2 complex, PDGF stimulated","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P16234;Q06124","subunits.Entrez.IDs.":"5156;5781","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007169","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway","FunCat.ID":"30.05.01.12","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways","PubMed.ID":8943348,"subunits.Protein.name.":"Platelet-derived growth factor receptor alpha ;Tyrosine-protein phosphatase non-receptor type 11","subunits.Gene.name.":"PDGFRA;PTPN11","subunits.Gene.name.syn.":"PDGFR2 RHEPDGFRA;PTP2C SHPTP2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The data demonstrate that SHP-2 does not need to be tyrosine phosphorylated in order to bind to the phosphorylated PDGFRA and are consistent with the idea that SHP-2 binds to the PDGFRA directly.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3184,"ComplexName":"FHL3 homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q13643","subunits.Entrez.IDs.":"2275","Protein.complex.purification.method":"MI:0018- two hybrid","GO.ID":"GO:2001141;GO:0006355;GO:0051098;GO:0005515;GO:0051090","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;regulation of binding;protein binding;regulation of sequence-specific DNA binding transcription factor activity","FunCat.ID":"11.02.03.04;18.01.07;16.01;18.02.09","FunCat.description":"transcriptional control;regulation by binding / dissociation;protein binding;regulator of transcription factor","PubMed.ID":11046156,"subunits.Protein.name.":"Four and a half LIM domains protein 3","subunits.Gene.name.":"FHL3","subunits.Gene.name.syn.":"SLIM2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"FHL3 protein forms homodimer complexes.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":3185,"ComplexName":"ACT homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q5TD97","subunits.Entrez.IDs.":"9457","Protein.complex.purification.method":"MI:0018- two hybrid","GO.ID":"GO:2001141;GO:0006355;GO:0051098;GO:0005515;GO:0051090","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;regulation of binding;protein binding;regulation of sequence-specific DNA binding transcription factor activity","FunCat.ID":"11.02.03.04;18.01.07;16.01;18.02.09","FunCat.description":"transcriptional control;regulation by binding / dissociation;protein binding;regulator of transcription factor","PubMed.ID":11046156,"subunits.Protein.name.":"Four and a half LIM domains protein 5","subunits.Gene.name.":"FHL5","subunits.Gene.name.syn.":"ACT","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"ACT protein forms homodimer complexes.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":3186,"ComplexName":"GRB2-SHP-2 complex, PDGF stimulated","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62993;Q06124","subunits.Entrez.IDs.":"2885;5781","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007169","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway","FunCat.ID":"30.05.01.12","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways","PubMed.ID":8943348,"subunits.Protein.name.":"Growth factor receptor-bound protein 2;Tyrosine-protein phosphatase non-receptor type 11","subunits.Gene.name.":"GRB2;PTPN11","subunits.Gene.name.syn.":"ASH;PTP2C SHPTP2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In summary, the data demonstrate that activation of the PDGFRA leads to phosphorylation of SHP-2 at Y580, which appears to trigger the formation of a complex between Grb2 and SHP-2. In addition, SHP-2 binds the activated PDGFRA directly, whereas Grb2 binds indirectly, via SHP-2.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3187,"ComplexName":"FHL2-FHL3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q13643;Q14192","subunits.Entrez.IDs.":"2275;2274","Protein.complex.purification.method":"MI:0018- two hybrid","GO.ID":"GO:2001141;GO:0006355;GO:0051098;GO:0005515;GO:0051090","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;regulation of binding;protein binding;regulation of sequence-specific DNA binding transcription factor activity","FunCat.ID":"11.02.03.04;18.01.07;16.01;18.02.09","FunCat.description":"transcriptional control;regulation by binding / dissociation;protein binding;regulator of transcription factor","PubMed.ID":11046156,"subunits.Protein.name.":"Four and a half LIM domains protein 3 ;Four and a half LIM domains protein 2","subunits.Gene.name.":"FHL3;FHL2","subunits.Gene.name.syn.":"SLIM2;DRAL SLIM3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3188,"ComplexName":"FHL2-ACT complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q14192;Q5TD97","subunits.Entrez.IDs.":"2274;9457","Protein.complex.purification.method":"MI:0018- two hybrid","GO.ID":"GO:2001141;GO:0006355;GO:0051098;GO:0005515;GO:0051090","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;regulation of binding;protein binding;regulation of sequence-specific DNA binding transcription factor activity","FunCat.ID":"11.02.03.04;18.01.07;16.01;18.02.09","FunCat.description":"transcriptional control;regulation by binding / dissociation;protein binding;regulator of transcription factor","PubMed.ID":11046156,"subunits.Protein.name.":"Four and a half LIM domains protein 2 ;Four and a half LIM domains protein 5","subunits.Gene.name.":"FHL2;FHL5","subunits.Gene.name.syn.":"DRAL SLIM3;ACT","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3189,"ComplexName":"FHL2-CREB complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P16220;Q14192","subunits.Entrez.IDs.":"1385;2274","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045893;GO:0003677;GO:0051098;GO:0005515;GO:0051090","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;regulation of binding;protein binding;regulation of sequence-specific DNA binding transcription factor activity","FunCat.ID":"11.02.03.04.01;16.03.01;18.01.07;16.01;18.02.09","FunCat.description":"transcription activation;DNA binding;regulation by binding / dissociation;protein binding;regulator of transcription factor","PubMed.ID":11046156,"subunits.Protein.name.":"Cyclic AMP-responsive element-binding protein 1;Four and a half LIM domains protein 2","subunits.Gene.name.":"CREB1;FHL2","subunits.Gene.name.syn.":"None;DRAL SLIM3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"FHL proteins differentially modulate CRE-dependent transcription in mammalian cells.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3190,"ComplexName":"FHL3-CREB complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P16220;Q13643","subunits.Entrez.IDs.":"1385;2275","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045893;GO:0003677;GO:0051098;GO:0005515;GO:0051090","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;regulation of binding;protein binding;regulation of sequence-specific DNA binding transcription factor activity","FunCat.ID":"11.02.03.04.01;16.03.01;18.01.07;16.01;18.02.09","FunCat.description":"transcription activation;DNA binding;regulation by binding / dissociation;protein binding;regulator of transcription factor","PubMed.ID":11046156,"subunits.Protein.name.":"Cyclic AMP-responsive element-binding protein 1;Four and a half LIM domains protein 3","subunits.Gene.name.":"CREB1;FHL3","subunits.Gene.name.syn.":"None;SLIM2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"FHL proteins differentially modulate CRE-dependent transcription in mammalian cells.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3191,"ComplexName":"ACT-CREB complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P16220;Q5TD97","subunits.Entrez.IDs.":"1385;9457","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045893;GO:0003677;GO:0051098;GO:0005515;GO:0051090","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;regulation of binding;protein binding;regulation of sequence-specific DNA binding transcription factor activity","FunCat.ID":"11.02.03.04.01;16.03.01;18.01.07;16.01;18.02.09","FunCat.description":"transcription activation;DNA binding;regulation by binding / dissociation;protein binding;regulator of transcription factor","PubMed.ID":11046156,"subunits.Protein.name.":"Cyclic AMP-responsive element-binding protein 1;Four and a half LIM domains protein 5","subunits.Gene.name.":"CREB1;FHL5","subunits.Gene.name.syn.":"None;ACT","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"FHL proteins differentially modulate CRE-dependent transcription in mammalian cells.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3192,"ComplexName":"G protein complex (Hdac4, Gnb1, Gng2)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62874;P63213;Q6NZM9","subunits.Entrez.IDs.":"14688;14702;208727","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0018- two hybrid","GO.ID":"GO:0045892;GO:0007186","GO.description":"negative regulation of transcription, DNA-templated;G-protein coupled receptor signaling pathway","FunCat.ID":"11.02.03.04.03;30.05.02.24","FunCat.description":"transcription repression;G-protein coupled receptor signalling pathway","PubMed.ID":16221676,"subunits.Protein.name.":"Guanine nucleotide-binding protein G;Guanine nucleotide-binding protein G;Histone deacetylase 4","subunits.Gene.name.":"Gnb1;Gng2;Hdac4","subunits.Gene.name.syn.":";;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The class II HDAC4 binds to GNB1/GNG2 via its C-terminal domain. The transcriptional co-repression activity is then inhibited.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3193,"ComplexName":"G protein complex (Hdac5, Gnb1, Gng2)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62874;P63213;Q9Z2V6","subunits.Entrez.IDs.":"14688;14702;15184","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0018- two hybrid","GO.ID":"GO:0045892;GO:0007186","GO.description":"negative regulation of transcription, DNA-templated;G-protein coupled receptor signaling pathway","FunCat.ID":"11.02.03.04.03;30.05.02.24","FunCat.description":"transcription repression;G-protein coupled receptor signalling pathway","PubMed.ID":16221676,"subunits.Protein.name.":"Guanine nucleotide-binding protein G;Guanine nucleotide-binding protein G;Histone deacetylase 5","subunits.Gene.name.":"Gnb1;Gng2;Hdac5","subunits.Gene.name.syn.":";;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The class II HDAC5 binds to GNB1/GNG2 via its C-terminal domain. The transcriptional co-repression activity is then inhibited.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3194,"ComplexName":"G protein complex (HDAC5, GNB1, GNG2)","Organism":"Bovine","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62871;P63212;Q2T9N9","subunits.Entrez.IDs.":"281201;281203;504242","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0018- two hybrid","GO.ID":"GO:0045892;GO:0007186","GO.description":"negative regulation of transcription, DNA-templated;G-protein coupled receptor signaling pathway","FunCat.ID":"11.02.03.04.03;30.05.02.24","FunCat.description":"transcription repression;G-protein coupled receptor signalling pathway","PubMed.ID":16221676,"subunits.Protein.name.":"Guanine nucleotide-binding protein G;Guanine nucleotide-binding protein G;Histone deacetylase","subunits.Gene.name.":"GNB1;GNG2;HDAC5","subunits.Gene.name.syn.":";;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The class II HDAC5 binds to GNB1/GNG2 via its C-terminal domain. The transcriptional co-repression activity is then inhibited.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":3195,"ComplexName":"G protein complex (Btk, Gng2, Gnb1)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P35991;P62874;P63213","subunits.Entrez.IDs.":"12229;14688;14702","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0007186;GO:0030154","GO.description":"G-protein coupled receptor signaling pathway;cell differentiation","FunCat.ID":"30.05.02.24;40.02","FunCat.description":"G-protein coupled receptor signalling pathway;cell differentiation","PubMed.ID":7972043,"subunits.Protein.name.":"Tyrosine-protein kinase BTK ;Guanine nucleotide-binding protein G;Guanine nucleotide-binding protein G","subunits.Gene.name.":"Btk;Gnb1;Gng2","subunits.Gene.name.syn.":"Bpk;;","Disease.comment":"Deficient expression or function of Bruton tyrosine kinase (Btk) causes human X chromosome-linked agammaglobulinemia (XLA) ormurine X chromosome-linked immunodeficiency (XID).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3196,"ComplexName":"FHL4/STX11-ACT complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75558;Q5TD97","subunits.Entrez.IDs.":"8676;9457","Protein.complex.purification.method":"MI:0018- two hybrid","GO.ID":"GO:2001141;GO:0006355;GO:0051098;GO:0005515;GO:0051090","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;regulation of binding;protein binding;regulation of sequence-specific DNA binding transcription factor activity","FunCat.ID":"11.02.03.04;18.01.07;16.01;18.02.09","FunCat.description":"transcriptional control;regulation by binding / dissociation;protein binding;regulator of transcription factor","PubMed.ID":11046156,"subunits.Protein.name.":"Syntaxin-11;Four and a half LIM domains protein 5","subunits.Gene.name.":"STX11;FHL5","subunits.Gene.name.syn.":";ACT","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3197,"ComplexName":"SMAD4-SNO-SKI complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"P12755;P12757;Q13485","subunits.Entrez.IDs.":"6497;6498;4089","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0007179;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"11.02.03.04;16.03.01;30.05.01.18.01;70.10","FunCat.description":"transcriptional control;DNA binding;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":10485843,"subunits.Protein.name.":"Ski oncogene ;Ski-like protein ;Mothers against decapentaplegic homolog 4","subunits.Gene.name.":"SKI;SKIL;SMAD4","subunits.Gene.name.syn.":";SNO;DPC4 MADH4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ski and Sno associate predominantly with the MH2 domain of SMAD4.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3198,"ComplexName":"SMAD2-SKI complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"P12755;Q15796","subunits.Entrez.IDs.":"6497;4087","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045892;GO:0003677;GO:0007179;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;DNA binding;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"11.02.03.04.03;16.03.01;30.05.01.18.01;70.10","FunCat.description":"transcription repression;DNA binding;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":10485843,"subunits.Protein.name.":"Ski oncogene ;Mothers against decapentaplegic homolog 2","subunits.Gene.name.":"SKI;SMAD2","subunits.Gene.name.syn.":";MADH2, MADR2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Smad proteins are the DNA-binding partners of Ski. Ski represses TGF(beta)-induced and SMAD-dependent transcriptional activation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3199,"ComplexName":"SMAD3-SKI complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"P12755;P84022","subunits.Entrez.IDs.":"6497;4088","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045892;GO:0003677;GO:0007179;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;DNA binding;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"11.02.03.04.03;16.03.01;30.05.01.18.01;70.10","FunCat.description":"transcription repression;DNA binding;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":10485843,"subunits.Protein.name.":"Ski oncogene ;Mothers against decapentaplegic homolog 3","subunits.Gene.name.":"SKI;SMAD3","subunits.Gene.name.syn.":";MADH3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Smad proteins are the DNA-binding partners of Ski. Ski represses TGF(beta)-induced and SMAD-dependent transcriptional activation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3200,"ComplexName":"SMAD4-SKI complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"P12755;Q13485","subunits.Entrez.IDs.":"6497;4089","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0045892;GO:0003677;GO:0007179;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;DNA binding;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"11.02.03.04.03;16.03.01;30.05.01.18.01;70.10","FunCat.description":"transcription repression;DNA binding;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":10485843,"subunits.Protein.name.":"Ski oncogene ;Mothers against decapentaplegic homolog 4","subunits.Gene.name.":"SKI;SMAD4","subunits.Gene.name.syn.":";DPC4 MADH4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Smad proteins are the DNA-binding partners of Ski. Ski represses TGF(beta)-induced and SMAD-dependent transcriptional activation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3201,"ComplexName":"Ship-Shc complex, IL-3 stimulated","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P98083;Q9ES52","subunits.Entrez.IDs.":"20416;16331","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":10891441,"subunits.Protein.name.":"SHC-transforming protein 1 ;Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1","subunits.Gene.name.":"Shc1;Inpp5d","subunits.Gene.name.syn.":"Shc ShcA;7a33 Ship Ship1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors describe that Shc-SHIP and Shc-Il3rb1 exist as separate complexes. They further propose that the interaction between Shc and the Il3rb1 subunit seems to be transient and of a lower affinity than the association of Shc with SHIP.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3202,"ComplexName":"Il3rb1-Shc-Ship complex, IL-3 stimulated","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P26955;P98083;Q9ES52","subunits.Entrez.IDs.":"12983;20416;16331","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":10891441,"subunits.Protein.name.":"Cytokine receptor common subunit beta ;SHC-transforming protein 1 ;Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1","subunits.Gene.name.":"Csf2rb;Shc1;Inpp5d","subunits.Gene.name.syn.":"Aic2b Csf2rb1 Il3rb1;Shc ShcA;7a33 Ship Ship1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3203,"ComplexName":"Shc-Ship-Grb2 complex, IL-3 stimulated","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P98083;Q60631;Q9ES52","subunits.Entrez.IDs.":"20416;14784;16331","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":10891441,"subunits.Protein.name.":"SHC-transforming protein 1 ;Growth factor receptor-bound protein 2;Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1","subunits.Gene.name.":"Shc1;Grb2;Inpp5d","subunits.Gene.name.syn.":"Shc ShcA;None;7a33 Ship Ship1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors conclude that although both Y239 and Y317 of Shc can associate with Grb2, the latter is the principal site for Grb2 binding in IL-3-stimulated IC2 cells. The data reported here indicate that Shc phosphorylation in IL-3-stimulated mast cells depends on binding of the PTB domain to the IL-3 receptor and that Shc pTyr sites subsequently bind SH2 proteins involved in different signaling pathways.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3204,"ComplexName":"SMAD2-SKI-NCOR complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"O75376;P12755;Q15796","subunits.Entrez.IDs.":"9611;6497;4087","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045892;GO:0003677;GO:0007179;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;DNA binding;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"11.02.03.04.03;16.03.01;30.05.01.18.01;70.10","FunCat.description":"transcription repression;DNA binding;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":10485843,"subunits.Protein.name.":"Nuclear receptor corepressor 1;Ski oncogene ;Mothers against decapentaplegic homolog 2","subunits.Gene.name.":"NCOR1;SKI;SMAD2","subunits.Gene.name.syn.":"KIAA1047;;MADH2, MADR2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ski recruits the corepressor N-Cor to the SMAD proteins.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3205,"ComplexName":"SMAD3-SKI-NCOR complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"O75376;P12755;P84022","subunits.Entrez.IDs.":"9611;6497;4088","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045892;GO:0003677;GO:0007179;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;DNA binding;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"11.02.03.04.03;16.03.01;30.05.01.18.01;70.10","FunCat.description":"transcription repression;DNA binding;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":10485843,"subunits.Protein.name.":"Nuclear receptor corepressor 1;Ski oncogene ;Mothers against decapentaplegic homolog 3","subunits.Gene.name.":"NCOR1;SKI;SMAD3","subunits.Gene.name.syn.":"KIAA1047;;MADH3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ski recruits the corepressor N-Cor to the SMAD proteins.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3206,"ComplexName":"SMAD4-SKI-NCOR complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"O75376;P12755;Q13485","subunits.Entrez.IDs.":"9611;6497;4089","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045892;GO:0003677;GO:0007179;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;DNA binding;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"11.02.03.04.03;16.03.01;30.05.01.18.01;70.10","FunCat.description":"transcription repression;DNA binding;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":10485843,"subunits.Protein.name.":"Nuclear receptor corepressor 1;Ski oncogene ;Mothers against decapentaplegic homolog 4","subunits.Gene.name.":"NCOR1;SKI;SMAD4","subunits.Gene.name.syn.":"KIAA1047;;DPC4 MADH4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ski recruits the corepressor N-Cor to the SMAD proteins.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3207,"ComplexName":"LIN2-LIN7-SAP97-MINT1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells , MDCK cells, epithelium","subunits.UniProt.IDs.":"O14910;O14936;Q02410;Q12959","subunits.Entrez.IDs.":"8825;8573;320;1739","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0051211;GO:0009798;GO:0030855;GO:0002009","GO.description":"intracellular protein transport;protein targeting;protein transport;anisotropic cell growth;axis specification;epithelial cell differentiation;morphogenesis of an epithelium","FunCat.ID":"14.04;20.01.10;40.01.03;41.05.19;45.03.09","FunCat.description":"protein targeting, sorting and translocation;protein transport;directional cell growth (morphogenesis);asymmetries and axis determination;epithelium","PubMed.ID":11865057,"subunits.Protein.name.":"Protein lin-7 homolog A;Peripheral plasma membrane protein CASK ;Amyloid beta A4 precursor protein-binding family A member 1 ;Disks large homolog 1","subunits.Gene.name.":"LIN7A;CASK;APBA1;DLG1","subunits.Gene.name.syn.":"MALS1 VELI1;LIN2;MINT1 X11;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3208,"ComplexName":"LIN2-LIN7 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells, epithelium","subunits.UniProt.IDs.":"O14910;O14936","subunits.Entrez.IDs.":"8825;8573","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0051211;GO:0009798;GO:0030855;GO:0002009","GO.description":"intracellular protein transport;protein targeting;protein transport;anisotropic cell growth;axis specification;epithelial cell differentiation;morphogenesis of an epithelium","FunCat.ID":"14.04;20.01.10;40.01.03;41.05.19;45.03.09","FunCat.description":"protein targeting, sorting and translocation;protein transport;directional cell growth (morphogenesis);asymmetries and axis determination;epithelium","PubMed.ID":11865057,"subunits.Protein.name.":"Protein lin-7 homolog A;Peripheral plasma membrane protein CASK","subunits.Gene.name.":"LIN7A;CASK","subunits.Gene.name.syn.":"MALS1 VELI1;LIN2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"It was earlier described that LIN-2/CASK and LIN-7 form a complex and localize to the basolateral surfaces of renal epithelia and MDCK (Madin-Darby canine kidney) cells (PMID:10710551).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3209,"ComplexName":"LIN2-SAP97 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"MDCK cells, epithelium","subunits.UniProt.IDs.":"O14936;Q12959","subunits.Entrez.IDs.":"8573;1739","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0051211;GO:0009798;GO:0030855;GO:0002009","GO.description":"intracellular protein transport;protein targeting;protein transport;anisotropic cell growth;axis specification;epithelial cell differentiation;morphogenesis of an epithelium","FunCat.ID":"14.04;20.01.10;40.01.03;41.05.19;45.03.09","FunCat.description":"protein targeting, sorting and translocation;protein transport;directional cell growth (morphogenesis);asymmetries and axis determination;epithelium","PubMed.ID":11865057,"subunits.Protein.name.":"Peripheral plasma membrane protein CASK ;Disks large homolog 1","subunits.Gene.name.":"CASK;DLG1","subunits.Gene.name.syn.":"LIN2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Association of SAP97 with LIN-2/CASK is crucial for lateral localization of SAP97 in MDCK cells.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3210,"ComplexName":"Dlg3-SAP97 complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"Q62696;Q62936","subunits.Entrez.IDs.":"25252;58948","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0051211;GO:0009798","GO.description":"intracellular protein transport;protein targeting;protein transport;anisotropic cell growth;axis specification","FunCat.ID":"14.04;20.01.10;40.01.03;41.05.19","FunCat.description":"protein targeting, sorting and translocation;protein transport;directional cell growth (morphogenesis);asymmetries and axis determination","PubMed.ID":12351654,"subunits.Protein.name.":"Disks large homolog 1;Disks large homolog 3","subunits.Gene.name.":"Dlg1;Dlg3","subunits.Gene.name.syn.":"Dlgh1;Dlgh3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Both Myc-DLG3 and Myc-mLIN-2 bound SAP97 via its MRE domain (found in a pull down experiment using MDCK cells). Immunoprecipitation in rat brain showed that endogenous DLG3 and SAP97 interact in rat brain.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":3211,"ComplexName":"Lin2/CASK-SAP97 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"MDCK cells, epithelium","subunits.UniProt.IDs.":"O70589;Q811D0","subunits.Entrez.IDs.":"12361;13383","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0051211;GO:0009798","GO.description":"intracellular protein transport;protein targeting;protein transport;anisotropic cell growth;axis specification","FunCat.ID":"14.04;20.01.10;40.01.03;41.05.19","FunCat.description":"protein targeting, sorting and translocation;protein transport;directional cell growth (morphogenesis);asymmetries and axis determination","PubMed.ID":12351654,"subunits.Protein.name.":"Peripheral plasma membrane protein CASK;Disks large homolog 1","subunits.Gene.name.":"Cask;Dlg1","subunits.Gene.name.syn.":"mLin-2;Dlgh1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Both Myc-DLG3 and Myc-mLIN-2 bound SAP97 via its MRE domain.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3212,"ComplexName":"Pax7-HMT complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O08550;P47239;P61965;Q91X20","subunits.Entrez.IDs.":"None;18509;140858;23808","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045893;GO:0018126;GO:0006479;GO:0007519;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;protein hydroxylation;protein methylation;skeletal muscle tissue development;nucleus","FunCat.ID":"11.02.03.04.01;14.07.09;41.05.15;70.10","FunCat.description":"transcription activation;posttranslational modification of amino acids (e.g. hydroxylation, methylation);myogenesis;nucleus","PubMed.ID":18066051,"subunits.Protein.name.":"Histone-lysine N-methyltransferase 2B ;Paired box protein Pax-7;WD repeat-containing protein 5 ;Set1/Ash2 histone methyltransferase complex subunit ASH2","subunits.Gene.name.":"Kmt2b;Pax7;Wdr5;Ash2l","subunits.Gene.name.syn.":"Mll2 Trx2 Wbp7;Pax-7;Big Big3;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Pax7 associates with the Wdr5-Ash2L-MLL2 histone methyltransferase (HMT) complex. Binding of the Pax7-HMT complex to Myf5 resulted in H3K4 tri-methylation of surrounding chromatin. Thus, Pax7 induces chromatin modifications that stimulate transcriptional activation of target genes to regulate entry into the myogenic developmental programme.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3213,"ComplexName":"ULBP1-KLRK1-HCST complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P26718;Q9BZM6;Q9UBK5","subunits.Entrez.IDs.":"22914;80329;10870","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006955","GO.description":"immune response","FunCat.ID":"36.25.16","FunCat.description":"immune response","PubMed.ID":11239445,"subunits.Protein.name.":"NKG2-D type II integral membrane protein ;NKG2D ligand 1 ;Hematopoietic cell signal transducer","subunits.Gene.name.":"KLRK1;ULBP1;HCST","subunits.Gene.name.syn.":"D12S2489E NKG2D;N2DL1 RAET1I;DAP10 KAP10 PIK3AP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The ULBPs and the MICs share the property of binding to the NKG2D/DAP10 receptor and provide a positive signal for NK cell activation and cytotoxicity that can override the negative signal mediated by MHC class I/KIR engagement.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3214,"ComplexName":"G protein complex (Mcf2l, Gnb1, Gng2)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P54311;Q45QK6;Q63406","subunits.Entrez.IDs.":"24400;80850;117020","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007186","GO.description":"G-protein coupled receptor signaling pathway","FunCat.ID":"30.05.02.24","FunCat.description":"G-protein coupled receptor signalling pathway","PubMed.ID":10518015,"subunits.Protein.name.":"Guanine nucleotide-binding protein G;Guanine nucleotide-binding protein subunit gamma ;Guanine nucleotide exchange factor DBS","subunits.Gene.name.":"Gnb1;Gng2;Mcf2l","subunits.Gene.name.syn.":";;Ost","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":3215,"ComplexName":"G protein complex (Kalrn, Gnb1, Gng2)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P54311;P97924;Q45QK6","subunits.Entrez.IDs.":"24400;84009;80850","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007186","GO.description":"G-protein coupled receptor signaling pathway","FunCat.ID":"30.05.02.24","FunCat.description":"G-protein coupled receptor signalling pathway","PubMed.ID":10518015,"subunits.Protein.name.":"Guanine nucleotide-binding protein G;Kalirin ;Guanine nucleotide-binding protein subunit gamma","subunits.Gene.name.":"Gnb1;Kalrn;Gng2","subunits.Gene.name.syn.":";Duo Hapip;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":3216,"ComplexName":"G protein complex (CACNA1A, GNB1, GNG2)","Organism":"Bovine","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"A5ACB9;P62871;P63212","subunits.Entrez.IDs.":"282648;281201;281203","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0007186","GO.description":"G-protein coupled receptor signaling pathway","FunCat.ID":"30.05.02.24","FunCat.description":"G-protein coupled receptor signalling pathway","PubMed.ID":9238069,"subunits.Protein.name.":"Calcium channel, voltage-dependent, P/Q type, Cav2.1 alpha 1A subunit ;Guanine nucleotide-binding protein G;Guanine nucleotide-binding protein G","subunits.Gene.name.":"CACNA1A;GNB1;GNG2","subunits.Gene.name.syn.":";;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The direct interaction of the G proteins (beta, gamma) with the Ca-channel alpha 1 subunit  is responsible for the channel inhibition by  G protein-coupled receptors.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":3217,"ComplexName":"MAML2-RBP-Jkappa-Notch2 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P31266;Q04721;Q7TPU6","subunits.Entrez.IDs.":"19664;4853;270118","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0007219;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;Notch signaling pathway;nucleus","FunCat.ID":"11.02.03.04;16.03.01;30.05.02.14;70.10","FunCat.description":"transcriptional control;DNA binding;Notch-receptor signalling pathway;nucleus","PubMed.ID":12370315,"subunits.Protein.name.":"Recombining binding protein suppressor of hairless;Neurogenic locus notch homolog protein 2;Maml2 protein","subunits.Gene.name.":"Rbpj;NOTCH2;Maml2","subunits.Gene.name.syn.":"Igkjrb1 Igkrsbp Rbpsuh;None;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Homo sapiens (Human);Mus musculus (Mouse)"}
{"ComplexID":3218,"ComplexName":"MAML2-RBP-Jkappa-Notch3 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P31266;Q61982;Q7TPU6","subunits.Entrez.IDs.":"19664;18131;270118","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0007219;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;Notch signaling pathway;nucleus","FunCat.ID":"11.02.03.04;16.03.01;30.05.02.14;70.10","FunCat.description":"transcriptional control;DNA binding;Notch-receptor signalling pathway;nucleus","PubMed.ID":12370315,"subunits.Protein.name.":"Recombining binding protein suppressor of hairless;Neurogenic locus notch homolog protein 3 ;Maml2 protein","subunits.Gene.name.":"Rbpj;Notch3;Maml2","subunits.Gene.name.syn.":"Igkjrb1 Igkrsbp Rbpsuh;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3219,"ComplexName":"MAML2-RBP-Jkappa-Notch4 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P31266;Q7TPU6;Q99466","subunits.Entrez.IDs.":"19664;270118;4855","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0007219;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;Notch signaling pathway;nucleus","FunCat.ID":"11.02.03.04;16.03.01;30.05.02.14;70.10","FunCat.description":"transcriptional control;DNA binding;Notch-receptor signalling pathway;nucleus","PubMed.ID":12370315,"subunits.Protein.name.":"Recombining binding protein suppressor of hairless;Maml2 protein;Neurogenic locus notch homolog protein 4","subunits.Gene.name.":"Rbpj;Maml2;NOTCH4","subunits.Gene.name.syn.":"Igkjrb1 Igkrsbp Rbpsuh;;INT3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Homo sapiens (Human)"}
{"ComplexID":3220,"ComplexName":"MAML3-RBP-Jkappa-Notch1 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P31266;P46531;Q96JK9","subunits.Entrez.IDs.":"19664;4851;55534","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0007219;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;Notch signaling pathway;nucleus","FunCat.ID":"11.02.03.04;16.03.01;30.05.02.14;70.10","FunCat.description":"transcriptional control;DNA binding;Notch-receptor signalling pathway;nucleus","PubMed.ID":12370315,"subunits.Protein.name.":"Recombining binding protein suppressor of hairless;Neurogenic locus notch homolog protein 1 ;Mastermind-like protein 3","subunits.Gene.name.":"Rbpj;NOTCH1;MAML3","subunits.Gene.name.syn.":"Igkjrb1 Igkrsbp Rbpsuh;TAN1;KIAA1816","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3221,"ComplexName":"MAML3-RBP-Jkappa-Notch2 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P31266;Q04721;Q96JK9","subunits.Entrez.IDs.":"19664;4853;55534","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0007219;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;Notch signaling pathway;nucleus","FunCat.ID":"11.02.03.04;16.03.01;30.05.02.14;70.10","FunCat.description":"transcriptional control;DNA binding;Notch-receptor signalling pathway;nucleus","PubMed.ID":12370315,"subunits.Protein.name.":"Recombining binding protein suppressor of hairless;Neurogenic locus notch homolog protein 2;Mastermind-like protein 3","subunits.Gene.name.":"Rbpj;NOTCH2;MAML3","subunits.Gene.name.syn.":"Igkjrb1 Igkrsbp Rbpsuh;None;KIAA1816","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3222,"ComplexName":"MAML3-RBP-Jkappa-Notch3 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P31266;Q61982;Q69Z97","subunits.Entrez.IDs.":"19664;18131;433586","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0007219;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;Notch signaling pathway;nucleus","FunCat.ID":"11.02.03.04;16.03.01;30.05.02.14;70.10","FunCat.description":"transcriptional control;DNA binding;Notch-receptor signalling pathway;nucleus","PubMed.ID":12370315,"subunits.Protein.name.":"Recombining binding protein suppressor of hairless;Neurogenic locus notch homolog protein 3 ;MKIAA1816 protein","subunits.Gene.name.":"Rbpj;Notch3;Maml3","subunits.Gene.name.syn.":"Igkjrb1 Igkrsbp Rbpsuh;;BC049812 mKIAA1816","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3223,"ComplexName":"MAML3-RBP-Jkappa-Notch4 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P31266;Q96JK9;Q99466","subunits.Entrez.IDs.":"19664;55534;4855","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0007219;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;Notch signaling pathway;nucleus","FunCat.ID":"11.02.03.04;16.03.01;30.05.02.14;70.10","FunCat.description":"transcriptional control;DNA binding;Notch-receptor signalling pathway;nucleus","PubMed.ID":12370315,"subunits.Protein.name.":"Recombining binding protein suppressor of hairless;Mastermind-like protein 3 ;Neurogenic locus notch homolog protein 4","subunits.Gene.name.":"Rbpj;MAML3;NOTCH4","subunits.Gene.name.syn.":"Igkjrb1 Igkrsbp Rbpsuh;KIAA1816;INT3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3224,"ComplexName":"G protein complex (NME2, GNB1, GNGT1)","Organism":"Bovine","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P02698;P62871;Q3T0Q4","subunits.Entrez.IDs.":"281796;281201;615447","Protein.complex.purification.method":"MI:0047- far western blotting; MI:0004- affinity chromatography technologies; MI:0019- coimmunoprecipitation","GO.ID":"GO:0007186","GO.description":"G-protein coupled receptor signaling pathway","FunCat.ID":"30.05.02.24","FunCat.description":"G-protein coupled receptor signalling pathway","PubMed.ID":12486123,"subunits.Protein.name.":"Guanine nucleotide-binding protein G;Guanine nucleotide-binding protein G;Nucleoside diphosphate kinase B","subunits.Gene.name.":"GNGT1;GNB1;NME2","subunits.Gene.name.syn.":";;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"NDPK B (=NME2) contributes to G protein activation by increasing the high energetic phosphate transfer onto GDP via intermediately phosphorylated His-266 in Gbeta1 subunits.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":3225,"ComplexName":"NMDA receptor complex (NR2A, NR2B, NR1, PSD-95)","Organism":"Rat","Synonyms":"None","Cell.line":"mature hippocampal neurons","subunits.UniProt.IDs.":"P31016;P35439;Q00959;Q00960","subunits.Entrez.IDs.":"29495;24408;24409;24410","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0005216;GO:0007264;GO:0007215;GO:0023052;GO:0050896;GO:0005886","GO.description":"intracellular protein transport;protein targeting;protein transport;ion channel activity;small GTPase mediated signal transduction;glutamate receptor signaling pathway;signaling;response to stimulus;plasma membrane","FunCat.ID":"14.04;20.01.10;20.03.01.01;30.01.05.05.01;30.05.02.24.05;30.01;36.25;70.02","FunCat.description":"protein targeting, sorting and translocation;protein transport;ion channels;small GTPase mediated signal transduction;glutamate signalling pathway;cellular signalling;animal specific systemic sensing and response;eukaryotic plasma membrane / membrane attached","PubMed.ID":15924861,"subunits.Protein.name.":"Disks large homolog 4;Glutamate receptor ionotropic, NMDA 1 ;Glutamate receptor ionotropic, NMDA 2A ;Glutamate receptor ionotropic, NMDA 2B","subunits.Gene.name.":"Dlg4;Grin1;Grin2a;Grin2b","subunits.Gene.name.syn.":"Dlgh4, Psd95;Nmdar1;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors analyse the links between NMDAR subtypes, Ras-ERK signaling, and AMPAR trafficking. They find that NR2A and NR2B have antagonistic actions on Ras-ERK activation and AMPAR distribution in mature neurons. NR2A-NMDARs promote, whereas NR2B-NMDARs inhibit, the surface expression of GluR1 - primarily by regulating GluR1 surface insertion.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":3226,"ComplexName":"Cd74-Cd44 receptor complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04441;P15379","subunits.Entrez.IDs.":"16149;12505","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007165;GO:0009987","GO.description":"signal transduction;cellular process","FunCat.ID":"30;40","FunCat.description":"CELLULAR COMMUNICATION/SIGNAL TRANSDUCTION MECHANISM;CELL FATE","PubMed.ID":18056708,"subunits.Protein.name.":"H-2 class II histocompatibility antigen gamma chain ;CD44 antigen","subunits.Gene.name.":"Cd74;Cd44","subunits.Gene.name.syn.":"Ii;Ly-24","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cd74 forms a complex with Cd44 on the B cell surface, and the Macrophage migration inhibitory factor (MIF) protein can serve as a ligand for the Cd74-Cd44 receptor complex. This complex is essential for the MIF-induced signaling cascade that results in B cell survival.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3227,"ComplexName":"Pick1-Pkca complex, TPA (tissue plasminogen activator) treated","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P05696;Q9EP80","subunits.Entrez.IDs.":"24680;84591","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0007268;GO:0005886","GO.description":"intracellular protein transport;protein targeting;protein transport;synaptic transmission;plasma membrane","FunCat.ID":"14.04;20.01.10;34.03.01;70.02","FunCat.description":"protein targeting, sorting and translocation;protein transport;synaptic transmission;eukaryotic plasma membrane / membrane attached","PubMed.ID":11466413,"subunits.Protein.name.":"Protein kinase C alpha type;PRKCA-binding protein","subunits.Gene.name.":"Prkca;Pick1","subunits.Gene.name.syn.":"Pkca;Prkcabp","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"A strong complex of Pick1-Pkca was observed when the cells were treated with TPA to activate PKC-alpha. In contrast to PKC-alpha , the binding of PICK1 to GluR2 was constitutive and did not require TPA treatment.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":3228,"ComplexName":"Pick1-Glur2 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P19491;Q9EP80","subunits.Entrez.IDs.":"29627;84591","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0007268;GO:0005886","GO.description":"intracellular protein transport;protein targeting;protein transport;synaptic transmission;plasma membrane","FunCat.ID":"14.04;20.01.10;34.03.01;70.02","FunCat.description":"protein targeting, sorting and translocation;protein transport;synaptic transmission;eukaryotic plasma membrane / membrane attached","PubMed.ID":11466413,"subunits.Protein.name.":"Glutamate receptor 2;PRKCA-binding protein","subunits.Gene.name.":"Gria2;Pick1","subunits.Gene.name.syn.":"Glur2;Prkcabp","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In contrast to the formation of the complex Pick1-PKCa, which affords treatment with TPA to activate PKC-alpha, the binding of PICK1 to GluR2 was constitutive and did not require TPA treatment.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":3229,"ComplexName":"Heterodimer complex (CDK9, IL6ST)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P40189;P50750","subunits.Entrez.IDs.":"3572;1025","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0023052;GO:0005737","GO.description":"signaling;cytoplasm","FunCat.ID":"30.01;70.03","FunCat.description":"cellular signalling;cytoplasm","PubMed.ID":12386808,"subunits.Protein.name.":"Interleukin-6 receptor subunit beta ;Cyclin-dependent kinase 9","subunits.Gene.name.":"IL6ST;CDK9","subunits.Gene.name.syn.":";CDC2L4, TAK","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The pleiotropic activities of the gp130-utilizing cytokines point to an extensive role for Cdk9 as a regulator of immune response, inflammation and cell differentiation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3230,"ComplexName":"Heterodimer complex (Cdk9, Il6st)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q00560;Q99J95","subunits.Entrez.IDs.":"16195;107951","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0047- far western blotting","GO.ID":"GO:0023052;GO:0005737","GO.description":"signaling;cytoplasm","FunCat.ID":"30.01;70.03","FunCat.description":"cellular signalling;cytoplasm","PubMed.ID":12386808,"subunits.Protein.name.":"Interleukin-6 receptor subunit beta ;Cyclin-dependent kinase 9","subunits.Gene.name.":"Il6st;Cdk9","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The pleiotropic activities of the gp130-utilizing cytokines point to an extensive role for Cdk9 as a regulator of immune response, inflammation and cell differentiation.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3231,"ComplexName":"Eps15-stonin2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P42566;Q8WXE9","subunits.Entrez.IDs.":"2060;85439","Protein.complex.purification.method":"MI:0077- nuclear magnetic resonance","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0016192","GO.description":"intracellular protein transport;protein targeting;protein transport;vesicle-mediated transport","FunCat.ID":"14.04;20.01.10;20.09.07","FunCat.description":"protein targeting, sorting and translocation;protein transport;vesicular transport (Golgi network, etc.)","PubMed.ID":18200045,"subunits.Protein.name.":"Epidermal growth factor receptor substrate 15;Stonin-2","subunits.Gene.name.":"EPS15;STON2","subunits.Gene.name.syn.":"AF1P;STN2 STNB","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Eps15 and stonin2 have both been shown to directly associate with the clathrin adaptor complex AP-2 and to localize to clathrin-coated pits (CCPs).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3232,"ComplexName":"Hippocalcin-beta2-adaptin complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62944;P84076","subunits.Entrez.IDs.":"140670;29177","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0005509","GO.description":"intracellular protein transport;protein targeting;protein transport;calcium ion binding","FunCat.ID":"14.04;20.01.10;16.17.01","FunCat.description":"protein targeting, sorting and translocation;protein transport;calcium binding","PubMed.ID":16102532,"subunits.Protein.name.":"AP-2 complex subunit beta ;Neuron-specific calcium-binding protein hippocalcin","subunits.Gene.name.":"Ap2b1;Hpca","subunits.Gene.name.syn.":"Clapb1;","Disease.comment":"None","Subunits.comment":"The authors state that beta2-adaptin is part of AP2 complex, described in PMID:12086608.","Complex.comment":"The authors describe that in neurons the hippocalcin-AP2 complex binds TfR in a Ca(2+)-independent manner, whereas the complex only binds to AMPARs, like Glur2 in the presence of Ca(2+).  Hippocalcin binds the beta-2-adaptin subunit of the AP2 adaptor complex.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":3233,"ComplexName":"SMAD2-SMAD4-FAST1-TGIF complex, TGF(beta) induced","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS-1 cells","subunits.UniProt.IDs.":"O75593;Q13485;Q15583;Q15796","subunits.Entrez.IDs.":"8928;4089;7050;4087","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045892;GO:0003677;GO:0007179;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;DNA binding;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"11.02.03.04.03;16.03.01;30.05.01.18.01;70.10","FunCat.description":"transcription repression;DNA binding;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":9389648,"subunits.Protein.name.":"Forkhead box protein H1 ;Mothers against decapentaplegic homolog 4;Homeobox protein TGIF1 ;Mothers against decapentaplegic homolog 2","subunits.Gene.name.":"FOXH1;SMAD4;TGIF1;SMAD2","subunits.Gene.name.syn.":"FAST1 FAST2;DPC4 MADH4;TGIF;MADH2, MADR2","Disease.comment":"None","Subunits.comment":"The orthologous human proteins are used.","Complex.comment":"This complex is only present in TGF(beta)-treated cells.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3234,"ComplexName":"SMAD2-SMAD4-FAST1-TGIF-HDAC1 complex, TGF(beta) induced","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS-1 cells","subunits.UniProt.IDs.":"O75593;Q13485;Q13547;Q15583;Q15796","subunits.Entrez.IDs.":"8928;4089;3065;7050;4087","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0003677;GO:0007179;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;DNA binding;transforming growth factor beta receptor signaling pathway;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;16.03.01;30.05.01.18.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;DNA binding;TGF-beta-receptor signalling pathway;organization of chromosome structure;nucleus","PubMed.ID":10199400,"subunits.Protein.name.":"Forkhead box protein H1 ;Mothers against decapentaplegic homolog 4;Histone deacetylase 1;Homeobox protein TGIF1 ;Mothers against decapentaplegic homolog 2","subunits.Gene.name.":"FOXH1;SMAD4;HDAC1;TGIF1;SMAD2","subunits.Gene.name.syn.":"FAST1 FAST2;DPC4 MADH4;RPD3L1;TGIF;MADH2, MADR2","Disease.comment":"None","Subunits.comment":"The orthologous human proteins are used.","Complex.comment":"This complex is only present in TGF(beta)-treated cells. Interaction of TGIF with HDAC1 is necessary for silencing of TGF(beta) transcriptional responses.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3235,"ComplexName":"PTF1 complex (Ptf1a, Tcf12, Rbpj)","Organism":"Mouse","Synonyms":"None","Cell.line":"pancreas","subunits.UniProt.IDs.":"P31266;Q61286;Q9QX98","subunits.Entrez.IDs.":"19664;21406;19213","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0010074;GO:0022008;GO:0048699;GO:0031016;GO:0005634;GO:0021510","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;maintenance of meristem identity;neurogenesis;generation of neurons;pancreas development;nucleus;spinal cord development","FunCat.ID":"11.02.03.04;16.03.01;41.05.04;41.05.13;47.03.11.09;70.10","FunCat.description":"transcriptional control;DNA binding;embryogenesis;neurogenesis;pancreas;nucleus","PubMed.ID":18198335,"subunits.Protein.name.":"Recombining binding protein suppressor of hairless;Transcription factor 12;Pancreas transcription factor 1 subunit alpha","subunits.Gene.name.":"Rbpj;Tcf12;Ptf1a","subunits.Gene.name.syn.":"Igkjrb1 Igkrsbp Rbpsuh;Alf1 Meb;Ptf1p48","Disease.comment":"Mutations in Ptf1a are associated with pancreatic and cerebellar agenesis.","Subunits.comment":"None","Complex.comment":"Transcriptional activity of PTF1 complex is independent of Notch signaling. The PTF1 transcription factor complex determines neuronal identity by inducing GABAergic-specific genes and suppressing glutamergic-specific genes.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3240,"ComplexName":"Nsg1-Glur2-Grip1-Stx13 complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P02683;P19491;P97879;Q9ER00","subunits.Entrez.IDs.":"25247;29627;84016;100226","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0071- molecular sieving","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0006897;GO:0005886","GO.description":"intracellular protein transport;protein targeting;protein transport;endocytosis;plasma membrane","FunCat.ID":"14.04;20.01.10;20.09.18.09.01;70.02","FunCat.description":"protein targeting, sorting and translocation;protein transport;endocytosis;eukaryotic plasma membrane / membrane attached","PubMed.ID":16037816,"subunits.Protein.name.":"Neuron-specific protein family member 1 ;Glutamate receptor 2;Glutamate receptor-interacting protein 1;Syntaxin-12","subunits.Gene.name.":"Nsg1;Gria2;Grip1;Stx12","subunits.Gene.name.syn.":"Bsmrb;Glur2;None;","Disease.comment":"None","Subunits.comment":"Since Stx12 (Stx13) from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"The results indicate that NEEP21-GRIP1 binding is crucial for GluR2-AMPAR sorting through endosomes and their recruitment to the plasma membrane.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Mus musculus (Mouse)"}
{"ComplexID":3262,"ComplexName":"SCAMP1-SCAMP2-SCAMP3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14828;O15126;O15127","subunits.Entrez.IDs.":"10067;9522;10066","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0015031;GO:0008565;GO:0006892","GO.description":"protein transport;protein transporter activity;post-Golgi vesicle-mediated transport","FunCat.ID":"20.01.10;20.09.07.06","FunCat.description":"protein transport;post Golgi transport","PubMed.ID":9224770,"subunits.Protein.name.":"Secretory carrier-associated membrane protein 3 ;Secretory carrier-associated membrane protein 1 ;Secretory carrier-associated membrane protein 2","subunits.Gene.name.":"SCAMP3;SCAMP1;SCAMP2","subunits.Gene.name.syn.":"C1orf3 PROPIN1;SCAMP;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3263,"ComplexName":"HERP1/HEY2-NCOR-SIN3A complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q13547;Q96ST3;Q9UBP5;Q9Y618","subunits.Entrez.IDs.":"3065;25942;23493;9612","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;DNA binding;organization of chromosome structure;nucleus","PubMed.ID":11486045,"subunits.Protein.name.":"Histone deacetylase 1;Paired amphipathic helix protein Sin3a;Hairy/enhancer-of-split related with YRPW motif protein 2 ;Nuclear receptor corepressor 2","subunits.Gene.name.":"HDAC1;SIN3A;HEY2;NCOR2","subunits.Gene.name.syn.":"RPD3L1;None;BHLHB32 CHF1 GRL HERP HERP1 HRT2;CTG26","Disease.comment":"None","Subunits.comment":"The authors state that SIN3A is part of the SIN3A complex, described in PMID:11784859.","Complex.comment":"HERP1/HEY2 associates with the SIN3A complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3269,"ComplexName":"RB1-HDAC1-BRG1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06400;P51532;Q13547","subunits.Entrez.IDs.":"5925;6597;3065","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0007050;GO:0045892;GO:0051276;GO:0005634","GO.description":"DNA topological change;cell cycle arrest;negative regulation of transcription, DNA-templated;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;10.03.01.02;11.02.03.04.03;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);cell cycle arrest;transcription repression;organization of chromosome structure;nucleus","PubMed.ID":10778858,"subunits.Protein.name.":"Retinoblastoma-associated protein ;Transcription activator BRG1;Histone deacetylase 1","subunits.Gene.name.":"RB1;SMARCA4;HDAC1","subunits.Gene.name.syn.":";BAF190A BRG1 SNF2B SNF2L4;RPD3L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Rb forms a repressor containing histone deacetylase (HDAC) and the hSWI/SNF nucleosome remodeling complex, which inhibits transcription of genes for cyclins E and A and arrests cells in the G1 phase of the cell cycle.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3270,"ComplexName":"Delta1 homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"O00548","subunits.Entrez.IDs.":"28514","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0007219","GO.description":"Notch signaling pathway","FunCat.ID":"30.05.02.14","FunCat.description":"Notch-receptor signalling pathway","PubMed.ID":12794186,"subunits.Protein.name.":"Delta-like protein 1","subunits.Gene.name.":"DLL1","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":3271,"ComplexName":"Gamma-secretase-Delta1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00548;P49768;Q92542;Q96BI3;Q9NZ42","subunits.Entrez.IDs.":"28514;5663;23385;51107;55851","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0007219","GO.description":"Notch signaling pathway","FunCat.ID":"30.05.02.14","FunCat.description":"Notch-receptor signalling pathway","PubMed.ID":12794186,"subunits.Protein.name.":"Delta-like protein 1;Presenilin-1;Nicastrin;Gamma-secretase subunit APH-1A;Gamma-secretase subunit PEN-2","subunits.Gene.name.":"DLL1;PSEN1;NCSTN;APH1A;PSENEN","subunits.Gene.name.syn.":"None;AD3 PS1 PSNL1;KIAA0253;PSF;PEN2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3276,"ComplexName":"GluR1-GluR2 complex","Organism":"Rat","Synonyms":"None","Cell.line":"hippocampal neurons","subunits.UniProt.IDs.":"P19490;P19491","subunits.Entrez.IDs.":"50592;29627","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0005216;GO:0007268;GO:0007611","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity;synaptic transmission;learning or memory","FunCat.ID":"20.01.01.01;20.03.01.01;34.03.01;36.25.03.04.01","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;synaptic transmission;learning and memory","PubMed.ID":15924137,"subunits.Protein.name.":"Glutamate receptor 1;Glutamate receptor 2","subunits.Gene.name.":"Gria1;Gria2","subunits.Gene.name.syn.":"Glur1;Glur2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results demonstrate a dominant role of the GluR2 subunit in signaling mediated by CaMKII at AMPARs.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":3277,"ComplexName":"D2 receptor-Nsf-GluR2 complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P19491;P61169;Q9QUL6","subunits.Entrez.IDs.":"29627;24318;60355","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation;MI:0096- pull down","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0008324;GO:0006812;GO:0005216;GO:0007212;GO:0007268","GO.description":"intracellular protein transport;protein targeting;protein transport;cation transmembrane transporter activity;cation transport;ion channel activity;dopamine receptor signaling pathway;synaptic transmission","FunCat.ID":"14.04;20.01.10;20.01.01.01;20.03.01.01;30.05.02.24.03;34.03.01","FunCat.description":"protein targeting, sorting and translocation;protein transport;cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels;dopamine receptor signalling pathway;synaptic transmission","PubMed.ID":15858065,"subunits.Protein.name.":"Glutamate receptor 2;D;Vesicle-fusing ATPase","subunits.Gene.name.":"Gria2;Drd2;Nsf","subunits.Gene.name.syn.":"Glur2;;Erg1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results indicate that D2 receptor interacts with GluR2 indirectly through NSF.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":3284,"ComplexName":"SMN complex (GEMIN5,2,3,4, SMN)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14893;P57678;Q16637;Q8TEQ6;Q9UHI6","subunits.Entrez.IDs.":"8487;50628;None;25929;11218","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0008380;GO:0032774;GO:0006461;GO:0003723;GO:0006811;GO:0005737;GO:0005634","GO.description":"RNA splicing;RNA biosynthetic process;protein complex assembly;RNA binding;ion transport;cytoplasm;nucleus","FunCat.ID":"11.04.03.01;11.02;14.10;16.03.03;20.01.01;70.03;70.10","FunCat.description":"splicing;RNA synthesis;assembly of protein complexes;RNA binding;ion transport;cytoplasm;nucleus","PubMed.ID":11714716,"subunits.Protein.name.":"Gem-associated protein 2 ;Gem-associated protein 4 ;Survival motor neuron protein;Gem-associated protein 5 ;Probable ATP-dependent RNA helicase DDX20","subunits.Gene.name.":"GEMIN2;GEMIN4;SMN1; SMN2;GEMIN5;DDX20","subunits.Gene.name.syn.":"SIP1;;SMN; SMNT; SMNC;;DP103 GEMIN3","Disease.comment":"Spinal muscular atrophy","Subunits.comment":"None","Complex.comment":"Gemin5 interacts with several of the snRNP core proteins including SmB, SmD1, SmD2, SmD3, and SmE, suggesting that it participates in the activities of the SMN complex in snRNP assembly.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3289,"ComplexName":"Ng2-Grip1-Glur2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"primary oligodendrocytes","subunits.UniProt.IDs.":"P23819;Q8VHY0;Q925T6","subunits.Entrez.IDs.":"14800;121021;74053","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0007268;GO:0010183","GO.description":"intracellular protein transport;protein targeting;protein transport;synaptic transmission;pollen tube guidance","FunCat.ID":"14.04;20.01.10;34.03.01;40.01.03.03","FunCat.description":"protein targeting, sorting and translocation;protein transport;synaptic transmission;guidance of longitudinal cell extension (e.g. pollen tube guidance, axonal pathfinding)","PubMed.ID":12458226,"subunits.Protein.name.":"Glutamate receptor 2 ;Chondroitin sulfate proteoglycan 4 ;Glutamate receptor-interacting protein 1","subunits.Gene.name.":"Gria2;Cspg4;Grip1","subunits.Gene.name.syn.":"Glur2;An2 Kiaa4232 Ng2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors propose that GRIP1 acts as a scaffolding molecule clustering NG2 and AMPA receptors in immature glia.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3296,"ComplexName":"SMN complex (GEMIN5,4,3), SMN-independent intermediate","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P57678;Q8TEQ6;Q9UHI6","subunits.Entrez.IDs.":"50628;25929;11218","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0008380;GO:0032774;GO:0006461;GO:0003723;GO:0005737;GO:0005634","GO.description":"RNA splicing;RNA biosynthetic process;protein complex assembly;RNA binding;cytoplasm;nucleus","FunCat.ID":"11.04.03.01;11.02;14.10;16.03.03;70.03;70.10","FunCat.description":"splicing;RNA synthesis;assembly of protein complexes;RNA binding;cytoplasm;nucleus","PubMed.ID":17640873,"subunits.Protein.name.":"Gem-associated protein 4 ;Gem-associated protein 5 ;Probable ATP-dependent RNA helicase DDX20","subunits.Gene.name.":"GEMIN4;GEMIN5;DDX20","subunits.Gene.name.syn.":";;DP103 GEMIN3","Disease.comment":"Reduced levels of SMN cause the motor neuron degenerative disease, spinal muscular atrophy.","Subunits.comment":"None","Complex.comment":"The survival of motor neurons (SMN) complex is essential for the biogenesis of small nuclear ribonucleoprotein (snRNP) complexes in eukaryotic cells.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3297,"ComplexName":"SMN complex (GEMIN6,7, UNRIP), SMN-independent intermediate","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q8WXD5;Q9H840;Q9Y3F4","subunits.Entrez.IDs.":"79833;79760;11171","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0008380;GO:0032774;GO:0006461;GO:0003723;GO:0005737;GO:0005634","GO.description":"RNA splicing;RNA biosynthetic process;protein complex assembly;RNA binding;cytoplasm;nucleus","FunCat.ID":"11.04.03.01;11.02;14.10;16.03.03;70.03;70.10","FunCat.description":"splicing;RNA synthesis;assembly of protein complexes;RNA binding;cytoplasm;nucleus","PubMed.ID":17640873,"subunits.Protein.name.":"Gem-associated protein 6 ;Gem-associated protein 7 ;Serine-threonine kinase receptor-associated protein","subunits.Gene.name.":"GEMIN6;GEMIN7;STRAP","subunits.Gene.name.syn.":";;MAWD UNRIP","Disease.comment":"Reduced levels of SMN cause the motor neuron degenerative disease, spinal muscular atrophy.","Subunits.comment":"None","Complex.comment":"The survival of motor neurons (SMN) complex is essential for the biogenesis of small nuclear ribonucleoprotein (snRNP) complexes in eukaryotic cells.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3298,"ComplexName":"SMN complex (GEMIN2,5, SMN)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14893;Q16637;Q8TEQ6","subunits.Entrez.IDs.":"8487;None;25929","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0008380;GO:0032774;GO:0006461;GO:0003723;GO:0005737;GO:0005634","GO.description":"RNA splicing;RNA biosynthetic process;protein complex assembly;RNA binding;cytoplasm;nucleus","FunCat.ID":"11.04.03.01;11.02;14.10;16.03.03;70.03;70.10","FunCat.description":"splicing;RNA synthesis;assembly of protein complexes;RNA binding;cytoplasm;nucleus","PubMed.ID":17640873,"subunits.Protein.name.":"Gem-associated protein 2 ;Survival motor neuron protein;Gem-associated protein 5","subunits.Gene.name.":"GEMIN2;SMN1; SMN2;GEMIN5","subunits.Gene.name.syn.":"SIP1;SMN; SMNT; SMNC;","Disease.comment":"Reduced levels of SMN cause the motor neuron degenerative disease, spinal muscular atrophy.","Subunits.comment":"None","Complex.comment":"The survival of motor neurons (SMN) complex is essential for the biogenesis of small nuclear ribonucleoprotein (snRNP) complexes in eukaryotic cells.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3335,"ComplexName":"Homotetrameric complex NIAP","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q13075","subunits.Entrez.IDs.":"4671","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0043067","GO.description":"regulation of programmed cell death","FunCat.ID":"40.10.02.04","FunCat.description":"regulation of apoptosis","PubMed.ID":15280366,"subunits.Protein.name.":"Baculoviral IAP repeat-containing protein 1","subunits.Gene.name.":"NAIP","subunits.Gene.name.syn.":"BIRC1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The expression of NAIP in macrophages and the structural organization of the NAIP raise the possibility that the protein function may be activated by pathogen-associated molecular patterns concomitant with proinflammatory caspases. The authors propose therefore that a key role of NAIP may therefore be to allow caspase-1 activation while suppressing unintentional activation of caspase-3/7 and -9.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":3439,"ComplexName":"CCT:PhLP complex","Organism":"Bovine","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P19632;Q3T115;Q58DJ8","subunits.Entrez.IDs.":"287007;533784;504735","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0040- electron microscopy","GO.ID":"GO:0050821;GO:0006457","GO.description":"protein stabilization;protein folding","FunCat.ID":"14.01","FunCat.description":"protein folding and stabilization","PubMed.ID":15583139,"subunits.Protein.name.":"Phosducin ;Chaperonin containing TCP1, subunit 5;T-complex protein 1 subunit gamma","subunits.Gene.name.":"PDC;CCT5;CCT3","subunits.Gene.name.syn.":";None;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"PhLP seems to interact with different isoforms of CCT. Complex models:  Model 1: CCT(gamma and delta) on one side of PhLP and CCT (alpha, epsilon, and zeta) on the other side. Model 2: CCT (delta and eta) on one side. and CCT (zeta, beta, and gamma) on the other side. With the exception of CCT isoforms epsilon and gamma,  no other isoforms could be found in the Uniprot database.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":3457,"ComplexName":"B23-NPM3 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q61937;Q9CPP0","subunits.Entrez.IDs.":"18148;18150","Protein.complex.purification.method":"MI:0018- two hybrid","GO.ID":"GO:0042254","GO.description":"ribosome biogenesis","FunCat.ID":"12.01","FunCat.description":"ribosome biogenesis","PubMed.ID":15596447,"subunits.Protein.name.":"Nucleophosmin;Nucleoplasmin-3","subunits.Gene.name.":"Npm1;Npm3","subunits.Gene.name.syn.":"None;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"NPM3 interacts with Nucleophosmin to inhibit ribosome biogenesis.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3458,"ComplexName":"B23-NPM3 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"CMT3 cells","subunits.UniProt.IDs.":"Q61937;Q9CPP0","subunits.Entrez.IDs.":"18148;18150","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0042254","GO.description":"ribosome biogenesis","FunCat.ID":"12.01","FunCat.description":"ribosome biogenesis","PubMed.ID":15596447,"subunits.Protein.name.":"Nucleophosmin;Nucleoplasmin-3","subunits.Gene.name.":"Npm1;Npm3","subunits.Gene.name.syn.":"None;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"NPM3 interacts with Nucleophosmin to inhibit ribosome biogenesis.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3489,"ComplexName":"Klf5-Pias1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O88907;Q9Z0Z7","subunits.Entrez.IDs.":"56469;12224","Protein.complex.purification.method":"MI:0018- two hybrid; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045893;GO:0003677;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04.01;16.03.01;70.10","FunCat.description":"transcription activation;DNA binding;nucleus","PubMed.ID":17178721,"subunits.Protein.name.":"E3 SUMO-protein ligase PIAS1 ;Krueppel-like factor 5","subunits.Gene.name.":"Pias1;Klf5","subunits.Gene.name.syn.":"Ddxbp1;Bteb2 Iklf","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors demonstrate that Pias1 is a functional partner of Klf5 and enhances the ability of KLF5 to promote proliferation.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3492,"ComplexName":"Bax homooligomeric complex, after apoptotic stimulation","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q07812","subunits.Entrez.IDs.":"581","Protein.complex.purification.method":"MI:0030- cross-linking studies","GO.ID":"GO:0006915;GO:0005739","GO.description":"apoptotic process;mitochondrion","FunCat.ID":"40.10.02;70.16","FunCat.description":"apoptosis (type I programmed cell death);mitochondrion","PubMed.ID":15757910,"subunits.Protein.name.":"Apoptosis regulator BAX","subunits.Gene.name.":"BAX","subunits.Gene.name.syn.":"BCL2L4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In unstimulated cells BAX normally exists as monomer. After apoptotic stimulation Bax is oligomerized.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":3522,"ComplexName":"COG complex","Organism":"Human","Synonyms":"Conserved oligomeric golgi tethering complex","Cell.line":"None","subunits.UniProt.IDs.":"P83436;Q14746;Q8WTW3;Q96JB2;Q96MW5;Q9H9E3;Q9UP83;Q9Y2V7","subunits.Entrez.IDs.":"91949;22796;9382;83548;84342;25839;10466;57511","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016192;GO:0007030;GO:0005794","GO.description":"vesicle-mediated transport;Golgi organization;Golgi apparatus","FunCat.ID":"20.09.07;42.08;70.08","FunCat.description":"vesicular transport (Golgi network, etc.);Golgi;Golgi","PubMed.ID":15047703,"subunits.Protein.name.":"Conserved oligomeric Golgi complex subunit 7;Conserved oligomeric Golgi complex subunit 2 ;Conserved oligomeric Golgi complex subunit 1 ;Conserved oligomeric Golgi complex subunit 3 ;Conserved oligomeric Golgi complex subunit 8;Conserved oligomeric Golgi complex subunit 4 ;Conserved oligomeric Golgi complex subunit 5;Conserved oligomeric Golgi complex subunit 6","subunits.Gene.name.":"COG7;COG2;COG1;COG3;COG8;COG4;COG5;COG6","subunits.Gene.name.syn.":"None;LDLC;KIAA1381 LDLB;SEC34;None;;GOLTC1 GTC90;KIAA1134","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The COG complex plays important roles in Golgi structure and function.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3525,"ComplexName":"Tetrameric COG subcomplex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P83436;Q96MW5;Q9UP83;Q9Y2V7","subunits.Entrez.IDs.":"91949;84342;10466;57511","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0016192;GO:0007030;GO:0005737","GO.description":"vesicle-mediated transport;Golgi organization;cytoplasm","FunCat.ID":"20.09.07;42.08;70.03","FunCat.description":"vesicular transport (Golgi network, etc.);Golgi;cytoplasm","PubMed.ID":15047703,"subunits.Protein.name.":"Conserved oligomeric Golgi complex subunit 7;Conserved oligomeric Golgi complex subunit 8;Conserved oligomeric Golgi complex subunit 5;Conserved oligomeric Golgi complex subunit 6","subunits.Gene.name.":"COG7;COG8;COG5;COG6","subunits.Gene.name.syn.":"None;None;GOLTC1 GTC90;KIAA1134","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The COG complex plays important roles in Golgi structure and function.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3529,"ComplexName":"Ternary COG subcomplex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P83436;Q9UP83;Q9Y2V7","subunits.Entrez.IDs.":"91949;10466;57511","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016192;GO:0007030;GO:0005794","GO.description":"vesicle-mediated transport;Golgi organization;Golgi apparatus","FunCat.ID":"20.09.07;42.08;70.08","FunCat.description":"vesicular transport (Golgi network, etc.);Golgi;Golgi","PubMed.ID":15047703,"subunits.Protein.name.":"Conserved oligomeric Golgi complex subunit 7;Conserved oligomeric Golgi complex subunit 5;Conserved oligomeric Golgi complex subunit 6","subunits.Gene.name.":"COG7;COG5;COG6","subunits.Gene.name.syn.":"None;GOLTC1 GTC90;KIAA1134","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The COG complex plays important roles in Golgi structure and function. COG6 interacts with a binary COG5-COG7 subcomplex.  Similarly, it was shown that COG8 interacts with a ternary COG5-COG6-COG7 subcomplex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3530,"ComplexName":"Binary COG subcomplex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P83436;Q9UP83","subunits.Entrez.IDs.":"91949;10466","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016192;GO:0007030;GO:0005794","GO.description":"vesicle-mediated transport;Golgi organization;Golgi apparatus","FunCat.ID":"20.09.07;42.08;70.08","FunCat.description":"vesicular transport (Golgi network, etc.);Golgi;Golgi","PubMed.ID":15047703,"subunits.Protein.name.":"Conserved oligomeric Golgi complex subunit 7;Conserved oligomeric Golgi complex subunit 5","subunits.Gene.name.":"COG7;COG5","subunits.Gene.name.syn.":"None;GOLTC1 GTC90","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The COG complex plays important roles in Golgi structure and function. COG6 interacts with a binary COG5-COG7 subcomplex.  Similarly, it was shown that COG8 interacts with a ternary COG5-COG6-COG7 subcomplex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3532,"ComplexName":"COG1-COG8 subcomplex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q8WTW3;Q96MW5","subunits.Entrez.IDs.":"9382;84342","Protein.complex.purification.method":"MI:0018- two hybrid; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0015031;GO:0008565;GO:0000301;GO:0007030","GO.description":"protein transport;protein transporter activity;retrograde transport, vesicle recycling within Golgi;Golgi organization","FunCat.ID":"20.01.10;20.09.07.07;42.08","FunCat.description":"protein transport;retrograde transport;Golgi","PubMed.ID":16020545,"subunits.Protein.name.":"Conserved oligomeric Golgi complex subunit 1 ;Conserved oligomeric Golgi complex subunit 8","subunits.Gene.name.":"COG1;COG8","subunits.Gene.name.syn.":"KIAA1381 LDLB;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"COG1-COG8 subcomplex constitutes a bridge linking COG2-COG3-COG4 subcomplex to COG5-COG6-COG7 subcomplex. For defining the complex composition the authors combined in vitro co-translation assay with co-immunoprecipitation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3539,"ComplexName":"Limd1-p62-Traf6-Prkcz complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P70196;Q02956;Q64337;Q9QXD8","subunits.Entrez.IDs.":"22034;18762;18412;29806","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0001503;GO:0030316","GO.description":"ossification;osteoclast differentiation","FunCat.ID":"41.05.17;45.03.05.07","FunCat.description":"osteogenesis;bone","PubMed.ID":17092936,"subunits.Protein.name.":"TNF receptor-associated factor 6 ;Protein kinase C zeta type ;Sequestosome-1 ;LIM domain-containing protein 1","subunits.Gene.name.":"Traf6;Prkcz;Sqstm1;Limd1","subunits.Gene.name.syn.":";Pkcz;A170 STAP;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors discuss the potential role of Limd1 as a positive regulator of Traf6 activity, only during states of osteoclastogenic stress.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3544,"ComplexName":"COG2-COG3-COG4 subcomplex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q14746;Q96JB2;Q9H9E3","subunits.Entrez.IDs.":"22796;83548;25839","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0015031;GO:0008565;GO:0000301;GO:0007030","GO.description":"protein transport;protein transporter activity;retrograde transport, vesicle recycling within Golgi;Golgi organization","FunCat.ID":"20.01.10;20.09.07.07;42.08","FunCat.description":"protein transport;retrograde transport;Golgi","PubMed.ID":16020545,"subunits.Protein.name.":"Conserved oligomeric Golgi complex subunit 2 ;Conserved oligomeric Golgi complex subunit 3 ;Conserved oligomeric Golgi complex subunit 4","subunits.Gene.name.":"COG2;COG3;COG4","subunits.Gene.name.syn.":"LDLC;SEC34;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"For defining the complex composition the authors combined in vitro co-translation assay with co-immunoprecipitation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3545,"ComplexName":"COG5-COG6-COG7 subcomplex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P83436;Q9UP83;Q9Y2V7","subunits.Entrez.IDs.":"91949;10466;57511","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0015031;GO:0008565;GO:0000301;GO:0007030","GO.description":"protein transport;protein transporter activity;retrograde transport, vesicle recycling within Golgi;Golgi organization","FunCat.ID":"20.01.10;20.09.07.07;42.08","FunCat.description":"protein transport;retrograde transport;Golgi","PubMed.ID":16020545,"subunits.Protein.name.":"Conserved oligomeric Golgi complex subunit 7;Conserved oligomeric Golgi complex subunit 5;Conserved oligomeric Golgi complex subunit 6","subunits.Gene.name.":"COG7;COG5;COG6","subunits.Gene.name.syn.":"None;GOLTC1 GTC90;KIAA1134","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"For defining the complex composition the authors combined in vitro co-translation assay with co-immunoprecipitation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3551,"ComplexName":"COG1-COG8-COG2-COG3-COG4 subcomplex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q14746;Q8WTW3;Q96JB2;Q96MW5;Q9H9E3","subunits.Entrez.IDs.":"22796;9382;83548;84342;25839","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0015031;GO:0008565;GO:0000301;GO:0007030","GO.description":"protein transport;protein transporter activity;retrograde transport, vesicle recycling within Golgi;Golgi organization","FunCat.ID":"20.01.10;20.09.07.07;42.08","FunCat.description":"protein transport;retrograde transport;Golgi","PubMed.ID":16020545,"subunits.Protein.name.":"Conserved oligomeric Golgi complex subunit 2 ;Conserved oligomeric Golgi complex subunit 1 ;Conserved oligomeric Golgi complex subunit 3 ;Conserved oligomeric Golgi complex subunit 8;Conserved oligomeric Golgi complex subunit 4","subunits.Gene.name.":"COG2;COG1;COG3;COG8;COG4","subunits.Gene.name.syn.":"LDLC;KIAA1381 LDLB;SEC34;None;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"COG1 mediates the interaction between COG1-COG8 and COG2-COG3-COG4. For defining the complex composition the authors combined in vitro co-translation assay with co-immunoprecipitation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3552,"ComplexName":"COG1-COG8-COG5-COG6-COG7 subcomplex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P83436;Q8WTW3;Q96MW5;Q9UP83;Q9Y2V7","subunits.Entrez.IDs.":"91949;9382;84342;10466;57511","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0015031;GO:0008565;GO:0000301;GO:0007030","GO.description":"protein transport;protein transporter activity;retrograde transport, vesicle recycling within Golgi;Golgi organization","FunCat.ID":"20.01.10;20.09.07.07;42.08","FunCat.description":"protein transport;retrograde transport;Golgi","PubMed.ID":16020545,"subunits.Protein.name.":"Conserved oligomeric Golgi complex subunit 7;Conserved oligomeric Golgi complex subunit 1 ;Conserved oligomeric Golgi complex subunit 8;Conserved oligomeric Golgi complex subunit 5;Conserved oligomeric Golgi complex subunit 6","subunits.Gene.name.":"COG7;COG1;COG8;COG5;COG6","subunits.Gene.name.syn.":"None;KIAA1381 LDLB;None;GOLTC1 GTC90;KIAA1134","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"COG8 mediates interaction between COG1-COG8 subcomplex and COG5-COG6-COG7 subcomplex. For defining the complex composition the authors combined in vitro co-translation assay with co-immunoprecipitation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3553,"ComplexName":"Traf6-p62-aPKC complex, RANK-L stimulated","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P70196;Q62074;Q64337","subunits.Entrez.IDs.":"22034;18759;18412","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0002573","GO.description":"myeloid leukocyte differentiation","FunCat.ID":"43.03.21","FunCat.description":"extracellular matrix degrading cell (chondroclast, osteoclast)","PubMed.ID":14960283,"subunits.Protein.name.":"TNF receptor-associated factor 6 ;Protein kinase C iota type;Sequestosome-1","subunits.Gene.name.":"Traf6;Prkci;Sqstm1","subunits.Gene.name.syn.":";Pkcl, aPKClambda;A170 STAP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results indicate that the activation of the RANK pathway promotes the formation of a TRAF6-p62-aPKC complex required for  NF-kappa-B activation, NFATc1 synthesis, and osteoclast differentiation.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3556,"ComplexName":"COG complex","Organism":"Human","Synonyms":"COG1-COG8-COG2-COG3-COG4-COG5-COG6-COG7 complex","Cell.line":"None","subunits.UniProt.IDs.":"P83436;Q14746;Q8WTW3;Q96JB2;Q96MW5;Q9H9E3;Q9UP83;Q9Y2V7","subunits.Entrez.IDs.":"91949;22796;9382;83548;84342;25839;10466;57511","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0015031;GO:0008565;GO:0000301;GO:0007030","GO.description":"protein transport;protein transporter activity;retrograde transport, vesicle recycling within Golgi;Golgi organization","FunCat.ID":"20.01.10;20.09.07.07;42.08","FunCat.description":"protein transport;retrograde transport;Golgi","PubMed.ID":16020545,"subunits.Protein.name.":"Conserved oligomeric Golgi complex subunit 7;Conserved oligomeric Golgi complex subunit 2 ;Conserved oligomeric Golgi complex subunit 1 ;Conserved oligomeric Golgi complex subunit 3 ;Conserved oligomeric Golgi complex subunit 8;Conserved oligomeric Golgi complex subunit 4 ;Conserved oligomeric Golgi complex subunit 5;Conserved oligomeric Golgi complex subunit 6","subunits.Gene.name.":"COG7;COG2;COG1;COG3;COG8;COG4;COG5;COG6","subunits.Gene.name.syn.":"None;LDLC;KIAA1381 LDLB;SEC34;None;;GOLTC1 GTC90;KIAA1134","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"COG1 mediates the interaction between COG1-COG8 and COG2-COG3-COG4. For defining the complex composition the authors combined in vitro co-translation assay with co-immunoprecipitation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3558,"ComplexName":"Fgf2-Ck2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P15655;P67871","subunits.Entrez.IDs.":"14173;13001","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000082;GO:0006468;GO:0006470;GO:0046777;GO:0005634","GO.description":"G1/S transition of mitotic cell cycle;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;nucleus","FunCat.ID":"10.03.01.01.03;14.07.03;70.10","FunCat.description":"G1/S transition of mitotic cell cycle;modification by phosphorylation, dephosphorylation, autophosphorylation;nucleus","PubMed.ID":10657989,"subunits.Protein.name.":"Fibroblast growth factor 2 ;Casein kinase II subunit beta","subunits.Gene.name.":"Fgf2;Csnk2b","subunits.Gene.name.syn.":"Fgf-2;Ck2n","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3559,"ComplexName":"Fgf2-Ck2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P15655;P67871","subunits.Entrez.IDs.":"14173;13001","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0000082;GO:0006468;GO:0006470;GO:0046777;GO:0005634","GO.description":"G1/S transition of mitotic cell cycle;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;nucleus","FunCat.ID":"10.03.01.01.03;14.07.03;70.10","FunCat.description":"G1/S transition of mitotic cell cycle;modification by phosphorylation, dephosphorylation, autophosphorylation;nucleus","PubMed.ID":15879597,"subunits.Protein.name.":"Fibroblast growth factor 2 ;Casein kinase II subunit beta","subunits.Gene.name.":"Fgf2;Csnk2b","subunits.Gene.name.syn.":"Fgf-2;Ck2n","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3563,"ComplexName":"Fgf2-Rsk2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P15655;P18654","subunits.Entrez.IDs.":"14173;None","Protein.complex.purification.method":"MI:0096- pull down; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0005634","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;nucleus","FunCat.ID":"14.07.03;70.10","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;nucleus","PubMed.ID":15879597,"subunits.Protein.name.":"Fibroblast growth factor 2 ;Ribosomal protein S6 kinase alpha-3","subunits.Gene.name.":"Fgf2;Rps6ka3","subunits.Gene.name.syn.":"Fgf-2;Mapkapk1b Rps6ka-rs1 Rsk2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Fgf2-Rsk2 complex phosphorylates histone H3 as well as several other proteins.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3569,"ComplexName":"Angiomotin isoform p80-Angiostatin complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P20918;Q8VHG2-2","subunits.Entrez.IDs.":"18815;27494","Protein.complex.purification.method":"MI:0096-pull down","GO.ID":"GO:0006928;GO:0001568;GO:0001944","GO.description":"movement of cell or subcellular component;blood vessel development;vasculature development","FunCat.ID":"34.05;47.03.03.02","FunCat.description":"cell motility;vessels","PubMed.ID":16043488,"subunits.Protein.name.":"Plasminogen;Angiomotin","subunits.Gene.name.":"Plg;Amot","subunits.Gene.name.syn.":"None;Kiaa1071","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The complex is larger than 175 kDa, indicating that the complex consists of more than one angiostatin (38 kDa) and one p80 angiomotin (80 kDa) molecule.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3618,"ComplexName":"GammaH2AFX-NDHII-Ku70-DNA complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12956;P16104;Q08211","subunits.Entrez.IDs.":"2547;3014;1660","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0006974;GO:0005634","GO.description":"DNA repair;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;32.01.09;70.10","FunCat.description":"DNA repair;DNA damage response;nucleus","PubMed.ID":15613478,"subunits.Protein.name.":"X-ray repair cross-complementing protein 6 ;Histone H2AX ;ATP-dependent RNA helicase A","subunits.Gene.name.":"XRCC6;H2AFX;DHX9","subunits.Gene.name.syn.":"G22P1;H2AX;DDX9 LKP NDH2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"NDH II directly bound to gammaH2AX, whereas association of Ku70 with gammaH2AX was mediated by chromosomal DNA.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3634,"ComplexName":"NR3C2-UBC9-SRC-1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"P08235;P63279;Q15788","subunits.Entrez.IDs.":"4306;7329;8648","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0402- chromatin immunoprecipitation assays","GO.ID":"GO:0045893;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;nucleus","FunCat.ID":"11.02.03.04.01;70.10","FunCat.description":"transcription activation;nucleus","PubMed.ID":17105732,"subunits.Protein.name.":"Mineralocorticoid receptor ;SUMO-conjugating enzyme UBC9 ;Nuclear receptor coactivator 1","subunits.Gene.name.":"NR3C2;UBE2I;NCOA1","subunits.Gene.name.syn.":"MCR MLR;UBC9 UBCE9;BHLHE74, SRC1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results support a physiological role of Ubc9 as a transcriptional MR coactivator, beyond the known SUMO E2-conjugating enzyme.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3677,"ComplexName":"RIN1-STAM2-HRS complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O14964;O75886;Q13671","subunits.Entrez.IDs.":"9146;10254;9610","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0005768","GO.description":"intracellular protein transport;protein targeting;protein transport;endosome","FunCat.ID":"14.04;20.01.10;70.22","FunCat.description":"protein targeting, sorting and translocation;protein transport;endosome","PubMed.ID":17403676,"subunits.Protein.name.":"Hepatocyte growth factor-regulated tyrosine kinase substrate;Signal transducing adapter molecule 2 ;Ras and Rab interactor 1","subunits.Gene.name.":"HGS;STAM2;RIN1","subunits.Gene.name.syn.":"HRS;HBP;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3678,"ComplexName":"RIN1-STAM2-EGFR complex, EGF stimulated","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"O75886;P00533;Q13671","subunits.Entrez.IDs.":"10254;1956;9610","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0006897;GO:0007173;GO:0005768","GO.description":"intracellular protein transport;protein targeting;protein transport;endocytosis;epidermal growth factor receptor signaling pathway;endosome","FunCat.ID":"14.04;20.01.10;20.09.18.09.01;30.05.01.12.01;70.22","FunCat.description":"protein targeting, sorting and translocation;protein transport;endocytosis;EGF-receptor signalling pathway;endosome","PubMed.ID":17403676,"subunits.Protein.name.":"Signal transducing adapter molecule 2 ;Epidermal growth factor receptor;Ras and Rab interactor 1","subunits.Gene.name.":"STAM2;EGFR;RIN1","subunits.Gene.name.syn.":"HBP;ERBB, ERBB1, HER1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"It seems that Rin1 plays dual roles, one facilitating cytoskeletal-dependent cellular movement and a second facilitating vesicle trafficking and receptor degradation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3710,"ComplexName":"CHL2-BMP2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12643;Q6WN34","subunits.Entrez.IDs.":"650;25884","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0007178;GO:0001503;GO:0030316","GO.description":"transmembrane receptor protein serine/threonine kinase signaling pathway;ossification;osteoclast differentiation","FunCat.ID":"30.05.01.18;41.05.17;45.03.05.07","FunCat.description":"transmembrane receptor protein serine/threonine kinase signalling pathways;osteogenesis;bone","PubMed.ID":17483092,"subunits.Protein.name.":"Bone morphogenetic protein 2 ;Chordin-like protein 2","subunits.Gene.name.":"BMP2;CHRDL2","subunits.Gene.name.syn.":"BMP2A;BNF1 CHL2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3711,"ComplexName":"CHL2-BMP2-TSG complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12643;Q6WN34;Q9GZX9","subunits.Entrez.IDs.":"650;25884;57045","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0007178;GO:0001503;GO:0030316","GO.description":"transmembrane receptor protein serine/threonine kinase signaling pathway;ossification;osteoclast differentiation","FunCat.ID":"30.05.01.18;41.05.17;45.03.05.07","FunCat.description":"transmembrane receptor protein serine/threonine kinase signalling pathways;osteogenesis;bone","PubMed.ID":17483092,"subunits.Protein.name.":"Bone morphogenetic protein 2 ;Chordin-like protein 2 ;Twisted gastrulation protein homolog 1","subunits.Gene.name.":"BMP2;CHRDL2;TWSG1","subunits.Gene.name.syn.":"BMP2A;BNF1 CHL2;TSG","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3712,"ComplexName":"Smad2-Smad4 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P97471;Q62432","subunits.Entrez.IDs.":"17128;17126","Protein.complex.purification.method":"MI:0065- isothermal titration calorimetry; MI:0114- x-ray crystallography; MI:0226- ion exchange chromatography","GO.ID":"GO:2001141;GO:0006355;GO:0007179;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"11.02.03.04;30.05.01.18.01;70.10","FunCat.description":"transcriptional control;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":15350224,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 4 ;Mothers against decapentaplegic homolog 2","subunits.Gene.name.":"Smad4;Smad2","subunits.Gene.name.syn.":"Dpc4 Madh4;Madh2 Madr2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Preferential formation of the R-Smad/Smad4 heterotrimer over the R-Smad homotrimer is largely enthalpy driven, contributed by the unique presence of strong electrostatic interactions within the heterotrimeric interfaces.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3713,"ComplexName":"Smad3-Smad4 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P97471;Q8BUN5","subunits.Entrez.IDs.":"17128;17127","Protein.complex.purification.method":"MI:0065- isothermal titration calorimetry; MI:0114- x-ray crystallography; MI:0226- ion exchange chromatography","GO.ID":"GO:2001141;GO:0006355;GO:0007179;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"11.02.03.04;30.05.01.18.01;70.10","FunCat.description":"transcriptional control;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":15350224,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 4 ;Mothers against decapentaplegic homolog 3","subunits.Gene.name.":"Smad4;Smad3","subunits.Gene.name.syn.":"Dpc4 Madh4;Madh3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Preferential formation of the R-Smad/Smad4 heterotrimer over the R-Smad homotrimer is largely enthalpy driven, contributed by the unique presence of strong electrostatic interactions within the heterotrimeric interfaces.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3714,"ComplexName":"Pericentrin-GCP complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95613;Q96CW5;Q9BSJ2","subunits.Entrez.IDs.":"5116;10426;10844","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0018- two hybrid;MI:0047- far western blotting","GO.ID":"GO:0000278;GO:0051726;GO:0051225;GO:0007098;GO:0005813","GO.description":"mitotic cell cycle;regulation of cell cycle;spindle assembly;centrosome cycle;centrosome","FunCat.ID":"10.03.01.01;10.03.01;10.03.05.01;70.05","FunCat.description":"mitotic cell cycle;mitotic cell cycle and cell cycle control;spindle pole body/centrosome and microtubule cycle;centrosome","PubMed.ID":15146056,"subunits.Protein.name.":"Pericentrin ;Gamma-tubulin complex component 3 ;Gamma-tubulin complex component 2","subunits.Gene.name.":"PCNT;TUBGCP3;TUBGCP2","subunits.Gene.name.syn.":"KIAA0402 PCNT2;GCP3;GCP2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors show that the centrosomal coiled-coil protein pericentrin anchors gamma TuRCsat spindle poles through an interaction with gamma tubulin complex proteins 2 and 3 (GCP2/3).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3715,"ComplexName":"Pericentrin-GCP complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P48725;P58854;Q921G8","subunits.Entrez.IDs.":"18541;259279;74237","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0018- two hybrid;MI:0047- far western blotting","GO.ID":"GO:0000278;GO:0051726;GO:0051225;GO:0007098;GO:0005813","GO.description":"mitotic cell cycle;regulation of cell cycle;spindle assembly;centrosome cycle;centrosome","FunCat.ID":"10.03.01.01;10.03.01;10.03.05.01;70.05","FunCat.description":"mitotic cell cycle;mitotic cell cycle and cell cycle control;spindle pole body/centrosome and microtubule cycle;centrosome","PubMed.ID":15146056,"subunits.Protein.name.":"Pericentrin;Gamma-tubulin complex component 3 ;Gamma-tubulin complex component 2","subunits.Gene.name.":"Pcnt;Tubgcp3;Tubgcp2","subunits.Gene.name.syn.":"Pcnt2;Gcp3;Gcp2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors show that the centrosomal coiled-coil protein pericentrin anchors gamma TuRCsat spindle poles through an interaction with gamma tubulin complex proteins 2 and 3 (GCP2/3).","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3729,"ComplexName":"SKI-SMAD2 hexameric complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12755;Q15796","subunits.Entrez.IDs.":"6497;4087","Protein.complex.purification.method":"MI:0065- isothermal titration calorimetry; MI:0071- molecular sieving","GO.ID":"GO:2001141;GO:0006355;GO:0007179","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;transforming growth factor beta receptor signaling pathway","FunCat.ID":"11.02.03.04;30.05.01.18.01","FunCat.description":"transcriptional control;TGF-beta-receptor signalling pathway","PubMed.ID":17283070,"subunits.Protein.name.":"Ski oncogene ;Mothers against decapentaplegic homolog 2","subunits.Gene.name.":"SKI;SMAD2","subunits.Gene.name.syn.":";MADH2, MADR2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results suggest that Ski negatively regulates TGF-beta signaling by replacing CBP in R-Smad complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3733,"ComplexName":"SKI-SMAD3 hexameric complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12755;P84022","subunits.Entrez.IDs.":"6497;4088","Protein.complex.purification.method":"MI:0065- isothermal titration calorimetry; MI:0071- molecular sieving","GO.ID":"GO:2001141;GO:0006355;GO:0007179","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;transforming growth factor beta receptor signaling pathway","FunCat.ID":"11.02.03.04;30.05.01.18.01","FunCat.description":"transcriptional control;TGF-beta-receptor signalling pathway","PubMed.ID":17283070,"subunits.Protein.name.":"Ski oncogene ;Mothers against decapentaplegic homolog 3","subunits.Gene.name.":"SKI;SMAD3","subunits.Gene.name.syn.":";MADH3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results suggest that Ski negatively regulates TGF-beta signaling by replacing CBP in R-Smad complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3739,"ComplexName":"SKI-SMAD2-SMAD4  pentameric complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12755;Q13485;Q15796","subunits.Entrez.IDs.":"6497;4089;4087","Protein.complex.purification.method":"MI:0065- isothermal titration calorimetry; MI:0071- molecular sieving","GO.ID":"GO:2001141;GO:0006355;GO:0007179","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;transforming growth factor beta receptor signaling pathway","FunCat.ID":"11.02.03.04;30.05.01.18.01","FunCat.description":"transcriptional control;TGF-beta-receptor signalling pathway","PubMed.ID":17283070,"subunits.Protein.name.":"Ski oncogene ;Mothers against decapentaplegic homolog 4;Mothers against decapentaplegic homolog 2","subunits.Gene.name.":"SKI;SMAD4;SMAD2","subunits.Gene.name.syn.":";DPC4 MADH4;MADH2, MADR2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results suggest that Ski negatively regulates TGF-beta signaling by replacing CBP in R-Smad complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3740,"ComplexName":"SKI-SMAD3-SMAD4  pentameric complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12755;P84022;Q13485","subunits.Entrez.IDs.":"6497;4088;4089","Protein.complex.purification.method":"MI:0065- isothermal titration calorimetry; MI:0071- molecular sieving","GO.ID":"GO:2001141;GO:0006355;GO:0007179","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;transforming growth factor beta receptor signaling pathway","FunCat.ID":"11.02.03.04;30.05.01.18.01","FunCat.description":"transcriptional control;TGF-beta-receptor signalling pathway","PubMed.ID":17283070,"subunits.Protein.name.":"Ski oncogene ;Mothers against decapentaplegic homolog 3;Mothers against decapentaplegic homolog 4","subunits.Gene.name.":"SKI;SMAD3;SMAD4","subunits.Gene.name.syn.":";MADH3;DPC4 MADH4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results suggest that Ski negatively regulates TGF-beta signaling by replacing CBP in R-Smad complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3741,"ComplexName":"Slp5-Rab27A complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q80T23;Q9ERI2","subunits.Entrez.IDs.":"236643;11891","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0016192","GO.description":"vesicle-mediated transport","FunCat.ID":"20.09.07","FunCat.description":"vesicular transport (Golgi network, etc.)","PubMed.ID":12051743,"subunits.Protein.name.":"Synaptotagmin-like protein 5;Ras-related protein Rab-27A","subunits.Gene.name.":"Sytl5;Rab27a","subunits.Gene.name.syn.":"Slp5;","Disease.comment":"Rab27A is involved in Griscelli syndrome (human hemophagocytic syndrome).","Subunits.comment":"None","Complex.comment":"Slp5-Rab27A complex is formed in liver but not in heart.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3749,"ComplexName":"CREBBP-SMAD2 hexameric complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q15796;Q92793","subunits.Entrez.IDs.":"4087;1387","Protein.complex.purification.method":"MI:0065- isothermal titration calorimetry; MI:0071- molecular sieving","GO.ID":"GO:2001141;GO:0006355;GO:0007179","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;transforming growth factor beta receptor signaling pathway","FunCat.ID":"11.02.03.04;30.05.01.18.01","FunCat.description":"transcriptional control;TGF-beta-receptor signalling pathway","PubMed.ID":17283070,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 2;CREB-binding protein","subunits.Gene.name.":"SMAD2;CREBBP","subunits.Gene.name.syn.":"MADH2, MADR2;CBP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results suggest that Ski negatively regulates TGF-beta signaling by replacing CBP in R-Smad complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3750,"ComplexName":"CREBBP-SMAD3 hexameric complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P84022;Q92793","subunits.Entrez.IDs.":"4088;1387","Protein.complex.purification.method":"MI:0065- isothermal titration calorimetry; MI:0071- molecular sieving","GO.ID":"GO:2001141;GO:0006355;GO:0007179","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;transforming growth factor beta receptor signaling pathway","FunCat.ID":"11.02.03.04;30.05.01.18.01","FunCat.description":"transcriptional control;TGF-beta-receptor signalling pathway","PubMed.ID":17283070,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 3;CREB-binding protein","subunits.Gene.name.":"SMAD3;CREBBP","subunits.Gene.name.syn.":"MADH3;CBP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results suggest that Ski negatively regulates TGF-beta signaling by replacing CBP in R-Smad complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3753,"ComplexName":"CREBBP-SMAD2-SMAD4 pentameric complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q13485;Q15796;Q92793","subunits.Entrez.IDs.":"4089;4087;1387","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:2001141;GO:0006355;GO:0007179","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;transforming growth factor beta receptor signaling pathway","FunCat.ID":"11.02.03.04;30.05.01.18.01","FunCat.description":"transcriptional control;TGF-beta-receptor signalling pathway","PubMed.ID":17283070,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 4;Mothers against decapentaplegic homolog 2;CREB-binding protein","subunits.Gene.name.":"SMAD4;SMAD2;CREBBP","subunits.Gene.name.syn.":"DPC4 MADH4;MADH2, MADR2;CBP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results suggest that Ski negatively regulates TGF-beta signaling by replacing CBP in R-Smad complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3754,"ComplexName":"CREBBP-SMAD3-SMAD4 pentameric complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P84022;Q13485;Q92793","subunits.Entrez.IDs.":"4088;4089;1387","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:2001141;GO:0006355;GO:0007179","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;transforming growth factor beta receptor signaling pathway","FunCat.ID":"11.02.03.04;30.05.01.18.01","FunCat.description":"transcriptional control;TGF-beta-receptor signalling pathway","PubMed.ID":17283070,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 3;Mothers against decapentaplegic homolog 4;CREB-binding protein","subunits.Gene.name.":"SMAD3;SMAD4;CREBBP","subunits.Gene.name.syn.":"MADH3;DPC4 MADH4;CBP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results suggest that Ski negatively regulates TGF-beta signaling by replacing CBP in R-Smad complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3828,"ComplexName":"DRIP78-PHLP complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q13371;Q6Y2X3","subunits.Entrez.IDs.":"5082;85406","Protein.complex.purification.method":"MI:0012- bioluminescence resonance energy transfer;MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:1902605","GO.description":"intracellular protein transport;protein targeting;protein transport;heterotrimeric G-protein complex assembly","FunCat.ID":"14.04;20.01.10","FunCat.description":"protein targeting, sorting and translocation;protein transport","PubMed.ID":17363375,"subunits.Protein.name.":"Phosducin-like protein ;DnaJ homolog subfamily C member 14","subunits.Gene.name.":"PDCL;DNAJC14","subunits.Gene.name.syn.":"PHLOP1 PhLP1;DRIP78 HDJ3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors suggest that the DRiP78\\u00b7PhLP complex is important in selective formation of different G-beta-gamma pairs.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3830,"ComplexName":"ADRB2 homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P07550","subunits.Entrez.IDs.":"154","Protein.complex.purification.method":"MI:0012- bioluminescence resonance energy transfer","GO.ID":"GO:0007186","GO.description":"G-protein coupled receptor signaling pathway","FunCat.ID":"30.05.02.24","FunCat.description":"G-protein coupled receptor signalling pathway","PubMed.ID":17363375,"subunits.Protein.name.":"Beta-2 adrenergic receptor","subunits.Gene.name.":"ADRB2","subunits.Gene.name.syn.":"ADRB2R B2AR","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":3837,"ComplexName":"SP1-E2F1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O89090;Q61501","subunits.Entrez.IDs.":"20683;13555","Protein.complex.purification.method":"MI:0096- pull down; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0045893","GO.description":"positive regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.01","FunCat.description":"transcription activation","PubMed.ID":8657141,"subunits.Protein.name.":"Transcription factor Sp1;Transcription factor E2F1","subunits.Gene.name.":"Sp1;E2f1","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3838,"ComplexName":"SP1-E2F2 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P08047;P56931","subunits.Entrez.IDs.":"6667;242705","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0045893","GO.description":"positive regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.01","FunCat.description":"transcription activation","PubMed.ID":8657141,"subunits.Protein.name.":"Transcription factor Sp1;Transcription factor E2F2","subunits.Gene.name.":"SP1;E2f2","subunits.Gene.name.syn.":"TSFP1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Mus musculus (Mouse)"}
{"ComplexID":3839,"ComplexName":"SP1-E2F3 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O35261;P08047","subunits.Entrez.IDs.":"13557;6667","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0045893","GO.description":"positive regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.01","FunCat.description":"transcription activation","PubMed.ID":8657141,"subunits.Protein.name.":"Transcription factor E2F3 ;Transcription factor Sp1","subunits.Gene.name.":"E2f3;SP1","subunits.Gene.name.syn.":";TSFP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Homo sapiens (Human)"}
{"ComplexID":3847,"ComplexName":"TCL1(trimer)-AKT1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"P31749;P56279","subunits.Entrez.IDs.":"207;8115","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0018- two hybrid","GO.ID":"GO:0019209","GO.description":"kinase activator activity","FunCat.ID":"18.02.01.01.05","FunCat.description":"kinase activator","PubMed.ID":10983986,"subunits.Protein.name.":"RAC-alpha serine/threonine-protein kinase;T-cell leukemia/lymphoma protein 1A","subunits.Gene.name.":"AKT1;TCL1A","subunits.Gene.name.syn.":"PKB, RAC;TCL1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TCL1 forms trimers which associate with AKT1 and binds to AKT PH domain. TCL1 increases Akt kinase activity and as a consequence enhances substrate phosphorylation. It stabilizes the mitochondrial transmembrane potential and enhances cell proliferation and survival.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3848,"ComplexName":"TCL1(trimer)-AKT2 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"P31751;P56279","subunits.Entrez.IDs.":"208;8115","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0018- two hybrid","GO.ID":"GO:0019209","GO.description":"kinase activator activity","FunCat.ID":"18.02.01.01.05","FunCat.description":"kinase activator","PubMed.ID":10983986,"subunits.Protein.name.":"RAC-beta serine/threonine-protein kinase ;T-cell leukemia/lymphoma protein 1A","subunits.Gene.name.":"AKT2;TCL1A","subunits.Gene.name.syn.":";TCL1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TCL1 forms trimers which associate with AKT1 and binds to AKT PH domain. TCL1 increases Akt kinase activity and as a consequence enhances substrate phosphorylation. It stabilizes the mitochondrial transmembrane potential and enhances cell proliferation and survival.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3849,"ComplexName":"TCL1(homotrimer) complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"P56279","subunits.Entrez.IDs.":"8115","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0095- proteinchip(r) on a surface-enhanced laser desorption/ionization","GO.ID":"GO:0019209","GO.description":"kinase activator activity","FunCat.ID":"18.02.01.01.05","FunCat.description":"kinase activator","PubMed.ID":10983986,"subunits.Protein.name.":"T-cell leukemia/lymphoma protein 1A","subunits.Gene.name.":"TCL1A","subunits.Gene.name.syn.":"TCL1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TCL1 forms trimers which associate with AKT1 and binds to AKT PH domain. TCL1 increases Akt kinase activity and as a consequence enhances substrate phosphorylation. It stabilizes the mitochondrial transmembrane potential and enhances cell proliferation and survival.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":3852,"ComplexName":"Rb-HDAC1 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"CV-1 cells","subunits.UniProt.IDs.":"P06400;Q13547","subunits.Entrez.IDs.":"5925;3065","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006265;GO:0000082;GO:0045892;GO:0006473;GO:0006476;GO:0051276;GO:0005634","GO.description":"DNA topological change;G1/S transition of mitotic cell cycle;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;10.03.01.01.03;11.02.03.04.03;14.07.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);G1/S transition of mitotic cell cycle;transcription repression;modification by acetylation, deacetylation;organization of chromosome structure;nucleus","PubMed.ID":9491888,"subunits.Protein.name.":"Retinoblastoma-associated protein ;Histone deacetylase 1","subunits.Gene.name.":"RB1;HDAC1","subunits.Gene.name.syn.":";RPD3L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The interaction was analyzed in CV-1 cells expressing a mixture of endogenous and transfected proteins. H. sapiens is used as model organism for annotation of the subunits.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3853,"ComplexName":"Rb-HDAC1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06400;Q13547","subunits.Entrez.IDs.":"5925;3065","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0000082;GO:0045892;GO:0006473;GO:0006476;GO:0051276;GO:0005634","GO.description":"DNA topological change;G1/S transition of mitotic cell cycle;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;10.03.01.01.03;11.02.03.04.03;14.07.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);G1/S transition of mitotic cell cycle;transcription repression;modification by acetylation, deacetylation;organization of chromosome structure;nucleus","PubMed.ID":9491888,"subunits.Protein.name.":"Retinoblastoma-associated protein ;Histone deacetylase 1","subunits.Gene.name.":"RB1;HDAC1","subunits.Gene.name.syn.":";RPD3L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3867,"ComplexName":"Xin-Cdh2-Ctnnb1-Ctnnd1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"heart muscle","subunits.UniProt.IDs.":"O70373;P15116;P30999;Q02248","subunits.Entrez.IDs.":"22437;12558;12388;12387","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0007155;GO:0030036","GO.description":"cell adhesion;actin cytoskeleton organization","FunCat.ID":"34.07;42.04.03","FunCat.description":"cell adhesion;actin cytoskeleton","PubMed.ID":17925400,"subunits.Protein.name.":"Xin actin-binding repeat-containing protein 1;Cadherin-2;Catenin delta-1;Catenin beta-1","subunits.Gene.name.":"Xirp1;Cdh2;Ctnnd1;Ctnnb1","subunits.Gene.name.syn.":"Cmya1 Xin;None;Catns Kiaa0384;Catnb","Disease.comment":"Xirp1 is involved in cardiac hypertrophy and cardiomyopathy (PMID:17766470).","Subunits.comment":"None","Complex.comment":"The authors found that the actin binding and bundling activity of mXinalpha was enhanced in the presence of beta-catenin.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3882,"ComplexName":"Abcg5-Abcg8 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"liver","subunits.UniProt.IDs.":"Q99PE8;Q9DBM0","subunits.Entrez.IDs.":"27409;67470","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006869;GO:0005319;GO:0006810","GO.description":"lipid transport;lipid transporter activity;transport","FunCat.ID":"20.01.13;20","FunCat.description":"lipid/fatty acid transport;CELLULAR TRANSPORT, TRANSPORT FACILITIES AND TRANSPORT ROUTES","PubMed.ID":14504269,"subunits.Protein.name.":"ATP-binding cassette sub-family G member 5;ATP-binding cassette sub-family G member 8","subunits.Gene.name.":"Abcg5;Abcg8","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results indicate that G5 and G8 are obligate heterodimers and are dependent on one another for transport out of the ER and for the excretion of hepatic sterols into bile. None of the other G subfamily members supported movement of G5 or G8 out of the ER in these cells.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3883,"ComplexName":"Abcg5-Abcg1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q64343;Q99PE8","subunits.Entrez.IDs.":"11307;27409","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005783","GO.description":"endoplasmic reticulum","FunCat.ID":"70.07","FunCat.description":"endoplasmic reticulum","PubMed.ID":14504269,"subunits.Protein.name.":"ATP-binding cassette sub-family G member 1 ;ATP-binding cassette sub-family G member 5","subunits.Gene.name.":"Abcg1;Abcg5","subunits.Gene.name.syn.":"Abc8 Wht1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Any complex formed between G5 and G1, G2, or G4  was retained in the ER.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3884,"ComplexName":"Abcg5-Abcg2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q7TMS5;Q99PE8","subunits.Entrez.IDs.":"26357;27409","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005783","GO.description":"endoplasmic reticulum","FunCat.ID":"70.07","FunCat.description":"endoplasmic reticulum","PubMed.ID":14504269,"subunits.Protein.name.":"ATP-binding cassette sub-family G member 2 ;ATP-binding cassette sub-family G member 5","subunits.Gene.name.":"Abcg2;Abcg5","subunits.Gene.name.syn.":"Abcp Bcrp1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Any complex formed between G5 and G1, G2, or G4  was retained in the ER.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3886,"ComplexName":"Abcg5-Abcg4 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q91WA9;Q99PE8","subunits.Entrez.IDs.":"192663;27409","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005783","GO.description":"endoplasmic reticulum","FunCat.ID":"70.07","FunCat.description":"endoplasmic reticulum","PubMed.ID":14504269,"subunits.Protein.name.":"ATP-binding cassette transporter ABCG4 ;ATP-binding cassette sub-family G member 5","subunits.Gene.name.":"Abcg4;Abcg5","subunits.Gene.name.syn.":"ABCG4;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Any complex formed between G5 and G1, G2, or G4  was retained in the ER.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3888,"ComplexName":"Abcg8-Abcg4 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q91WA9;Q9DBM0","subunits.Entrez.IDs.":"192663;67470","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005783","GO.description":"endoplasmic reticulum","FunCat.ID":"70.07","FunCat.description":"endoplasmic reticulum","PubMed.ID":14504269,"subunits.Protein.name.":"ATP-binding cassette transporter ABCG4 ;ATP-binding cassette sub-family G member 8","subunits.Gene.name.":"Abcg4;Abcg8","subunits.Gene.name.syn.":"ABCG4;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Any complex formed between G5 and G1, G2, or G4 or between G8 and G4 was retained in the ER.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3900,"ComplexName":"GABP(gamma)1-E2F1-DP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"Saos-2 cells","subunits.UniProt.IDs.":"Q01094;Q14186;Q8TAK5","subunits.Entrez.IDs.":"1869;7027;126626","Protein.complex.purification.method":"MI:0412- electrophoretic mobility supershift assay","GO.ID":"GO:0000082;GO:0045893;GO:0003677;GO:0006915;GO:0005634","GO.description":"G1/S transition of mitotic cell cycle;positive regulation of transcription, DNA-templated;DNA binding;apoptotic process;nucleus","FunCat.ID":"10.03.01.01.03;11.02.03.04.01;16.03.01;40.10.02;70.10","FunCat.description":"G1/S transition of mitotic cell cycle;transcription activation;DNA binding;apoptosis (type I programmed cell death);nucleus","PubMed.ID":11884602,"subunits.Protein.name.":"Transcription factor E2F1;Transcription factor Dp-1;GA-binding protein subunit beta-2","subunits.Gene.name.":"E2F1;TFDP1;GABPB2","subunits.Gene.name.syn.":"RBBP3;DP1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3903,"ComplexName":"Grip-Glur2/3-liprin-alpha complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P19491;P19492;P97879;Q91Z80","subunits.Entrez.IDs.":"29627;29628;84016;140592","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0005886;GO:0007416","GO.description":"intracellular protein transport;protein targeting;protein transport;plasma membrane;synapse assembly","FunCat.ID":"14.04;20.01.10;70.02;41.05.13.01","FunCat.description":"protein targeting, sorting and translocation;protein transport;eukaryotic plasma membrane / membrane attached;synaptogenesis","PubMed.ID":11931740,"subunits.Protein.name.":"Glutamate receptor 2;Glutamate receptor 3;Glutamate receptor-interacting protein 1;Liprin-alpha-4","subunits.Gene.name.":"Gria2;Gria3;Grip1;Ppfia4","subunits.Gene.name.syn.":"Glur2;Glur3;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":3917,"ComplexName":"Ternary complex (GATA4, SRF, MYOCD)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P11831;P43694;Q8IZQ8","subunits.Entrez.IDs.":"6722;2626;93649","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":15367672,"subunits.Protein.name.":"Serum response factor ;Transcription factor GATA-4 ;Myocardin","subunits.Gene.name.":"SRF;GATA4;MYOCD","subunits.Gene.name.syn.":";;MYCD","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3929,"ComplexName":"Ternary complex (CCD1, Dvl, Rac)","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P31750;P51141;Q155Q3","subunits.Entrez.IDs.":"11651;13542;85458","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007254","GO.description":"JNK cascade","FunCat.ID":"30.01.05.01.02","FunCat.description":"JNK cascade","PubMed.ID":15262978,"subunits.Protein.name.":"RAC-alpha serine/threonine-protein kinase;Segment polarity protein dishevelled homolog DVL-1;Dixin","subunits.Gene.name.":"Akt1;Dvl1;DIXDC1","subunits.Gene.name.syn.":"Akt, Rac;Dvl;CCD1 KIAA1735","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Homo sapiens (Human)"}
{"ComplexID":3930,"ComplexName":"CCD1-Axin complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O35625;Q155Q3","subunits.Entrez.IDs.":"12005;85458","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007254","GO.description":"JNK cascade","FunCat.ID":"30.01.05.01.02","FunCat.description":"JNK cascade","PubMed.ID":15262978,"subunits.Protein.name.":"Axin-1 ;Dixin","subunits.Gene.name.":"Axin1;DIXDC1","subunits.Gene.name.syn.":"Axin Fu;CCD1 KIAA1735","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ccd1 drastically inhibits JNK activation both by Axin and by Dvl.","SWISSPROT.organism":"Mus musculus (Mouse);Homo sapiens (Human)"}
{"ComplexID":3941,"ComplexName":"RCP-Rab11 complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"P62491;Q6WKZ4","subunits.Entrez.IDs.":"8766;80223","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0047- far western blotting","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0030545","GO.description":"intracellular protein transport;protein targeting;protein transport;receptor regulator activity","FunCat.ID":"14.04;20.01.10;18.02.07","FunCat.description":"protein targeting, sorting and translocation;protein transport;regulator of receptor activity","PubMed.ID":15181150,"subunits.Protein.name.":"Ras-related protein Rab-11A;Rab11 family-interacting protein 1","subunits.Gene.name.":"RAB11A;RAB11FIP1","subunits.Gene.name.syn.":"RAB11;RCP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The RCP-Rab11 complex regulates the sorting of transferrin receptors from the degradative to the recycling pathway.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3942,"ComplexName":"Beta-catenin-Cadherin-LAR complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"Q64604;Q9WU82;Q9Z1Y3","subunits.Entrez.IDs.":"360406;84353;83501","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0007416","GO.description":"synapse assembly","FunCat.ID":"41.05.13.01","FunCat.description":"synaptogenesis","PubMed.ID":15750591,"subunits.Protein.name.":"Receptor-type tyrosine-protein phosphatase F;Catenin beta-1;Cadherin-2","subunits.Gene.name.":"Ptprf;Ctnnb1;Cdh2","subunits.Gene.name.syn.":"Lar;Catnb;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors suggest that one pool of cadherin-beta-catenin is associated with the GRIP-liprin-alpha complex independently of LAR-RPTP, and another pool of beta-catenin-cadherin is associated with LAR-RPTP independently of GRIP-liprin-alpha.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":3943,"ComplexName":"MondoA-Mlx complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O08609;Q3UPW8","subunits.Entrez.IDs.":"21428;208104","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0047- far western blotting; MI:0412- electrophoretic mobility supershift assay","GO.ID":"GO:0045893;GO:0003677;GO:0005737;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;cytoplasm;nucleus","FunCat.ID":"11.02.03.04.01;16.03.01;70.03;70.10","FunCat.description":"transcription activation;DNA binding;cytoplasm;nucleus","PubMed.ID":11073985,"subunits.Protein.name.":"Max-like protein X ;Putative uncharacterized protein","subunits.Gene.name.":"Mlx;Mlxip","subunits.Gene.name.syn.":"Tcfl4;AW228700","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"MondoA-Mlx complexes activate transcription when targeted to the nucleus.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3952,"ComplexName":"Mlx-Mad1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"NIH 3T3 cells","subunits.UniProt.IDs.":"O08609;P50538","subunits.Entrez.IDs.":"21428;17119","Protein.complex.purification.method":"MI:0412- electrophoretic mobility supershift assay","GO.ID":"GO:0045892;GO:0003677;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04.03;16.03.01;70.10","FunCat.description":"transcription repression;DNA binding;nucleus","PubMed.ID":10593926,"subunits.Protein.name.":"Max-like protein X ;Max dimerization protein 1","subunits.Gene.name.":"Mlx;Mxd1","subunits.Gene.name.syn.":"Tcfl4;Mad Mad1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3959,"ComplexName":"SMAD3-SMAD4-cSKI, TGF(beta)-dependent","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12755;P84022;Q13485","subunits.Entrez.IDs.":"6497;4088;4089","Protein.complex.purification.method":"MI:0412- electrophoretic mobility supershift assay","GO.ID":"GO:0045892;GO:0007179;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"11.02.03.04.03;30.05.01.18.01;70.10","FunCat.description":"transcription repression;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":10575014,"subunits.Protein.name.":"Ski oncogene ;Mothers against decapentaplegic homolog 3;Mothers against decapentaplegic homolog 4","subunits.Gene.name.":"SKI;SMAD3;SMAD4","subunits.Gene.name.syn.":";MADH3;DPC4 MADH4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"c-SKI interacts with SMAD in a TGF(beta)-dependent manner.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3961,"ComplexName":"SMAD3-cSKI-SIN3A-HDAC1 complex","Organism":"Human","Synonyms":"None","Cell.line":"COS-7 cells","subunits.UniProt.IDs.":"P12755;P84022;Q13547;Q96ST3","subunits.Entrez.IDs.":"6497;4088;3065;25942","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045892;GO:0006473;GO:0006476;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;negative regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.03;14.07.04;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription repression;modification by acetylation, deacetylation;DNA binding;organization of chromosome structure;nucleus","PubMed.ID":10575014,"subunits.Protein.name.":"Ski oncogene ;Mothers against decapentaplegic homolog 3;Histone deacetylase 1;Paired amphipathic helix protein Sin3a","subunits.Gene.name.":"SKI;SMAD3;HDAC1;SIN3A","subunits.Gene.name.syn.":";MADH3;RPD3L1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3967,"ComplexName":"SMURF2-SMAD2 complex, TGF(beta)-dependent","Organism":"MINK","Synonyms":"None","Cell.line":"Mv1Lu cells","subunits.UniProt.IDs.":"Q15796;Q9HAU4","subunits.Entrez.IDs.":"4087;64750","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0016567;GO:0016579;GO:0007179;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein ubiquitination;protein deubiquitination;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"11.02.03.04;14.07.05;30.05.01.18.01;70.10","FunCat.description":"transcriptional control;modification by ubiquitination, deubiquitination;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":11389444,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 2;E3 ubiquitin-protein ligase SMURF2","subunits.Gene.name.":"SMAD2;SMURF2","subunits.Gene.name.syn.":"MADH2, MADR2;","Disease.comment":"None","Subunits.comment":"Since SMURF2 and SMAD2 from mink were not available in the UniProt database at the time of annotation, the orthologous human proteins were used.","Complex.comment":"SMURF2 interacts stably with phosphorylated SMAD2 in response to TGF(beta) signaling.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3971,"ComplexName":"SMURF2-SMAD3 complex, TGF(beta)-dependent","Organism":"Mammalia","Synonyms":"None","Cell.line":"Mv1Lu cells","subunits.UniProt.IDs.":"P84022;Q9HAU4","subunits.Entrez.IDs.":"4088;64750","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0016567;GO:0016579;GO:0007179;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein ubiquitination;protein deubiquitination;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"11.02.03.04;14.07.05;30.05.01.18.01;70.10","FunCat.description":"transcriptional control;modification by ubiquitination, deubiquitination;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":11389444,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 3;E3 ubiquitin-protein ligase SMURF2","subunits.Gene.name.":"SMAD3;SMURF2","subunits.Gene.name.syn.":"MADH3;","Disease.comment":"None","Subunits.comment":"Since SMURF2 and SMAD3 from mink were not available in the UniProt database at the time of annotation, the orthologous human proteins were used.","Complex.comment":"SMURF2 interacts stably with phosphorylated SMAD3 in response to TGF(beta) signaling.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3972,"ComplexName":"SMURF2-SMAD3-SnoN complex, TGF(beta)-dependent","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"P12757;P84022;Q9HAU4","subunits.Entrez.IDs.":"6498;4088;64750","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0045892;GO:0016567;GO:0016579;GO:0007179;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;protein ubiquitination;protein deubiquitination;transforming growth factor beta receptor signaling pathway;nucleus","FunCat.ID":"11.02.03.04.03;14.07.05;30.05.01.18.01;70.10","FunCat.description":"transcription repression;modification by ubiquitination, deubiquitination;TGF-beta-receptor signalling pathway;nucleus","PubMed.ID":11389444,"subunits.Protein.name.":"Ski-like protein ;Mothers against decapentaplegic homolog 3;E3 ubiquitin-protein ligase SMURF2","subunits.Gene.name.":"SKIL;SMAD3;SMURF2","subunits.Gene.name.syn.":"SNO;MADH3;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex allows SMURF2 to target SnoN for ubiquitin-mediated degradation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3979,"ComplexName":"mTORC2 complex (mTOR/FRAP1, LST8, mAVO3/RICTOR, SIN1)","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"P42345;Q6R327;Q9BPZ7;Q9BVC4","subunits.Entrez.IDs.":"2475;253260;79109;64223","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0071- molecular sieving","GO.ID":"GO:0035556;GO:0000902;GO:0016049;GO:0030036","GO.description":"intracellular signal transduction;cell morphogenesis;cell growth;actin cytoskeleton organization","FunCat.ID":"30.01;40.01;42.04.03","FunCat.description":"cellular signalling;cell growth / morphogenesis;actin cytoskeleton","PubMed.ID":17043309,"subunits.Protein.name.":"Serine/threonine-protein kinase mTOR ;Rapamycin-insensitive companion of mTOR ;Target of rapamycin complex 2 subunit MAPKAP1 ;Target of rapamycin complex subunit LST8","subunits.Gene.name.":"MTOR;RICTOR;MAPKAP1;MLST8","subunits.Gene.name.syn.":"FRAP FRAP1 FRAP2 RAFT1 RAPT1;KIAA1999;MIP1 SIN1;GBL LST8","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors showed that hSin1, similar to Rictor, is selectively required for the phosphorylation and activation of the TORC2 substrate Akt, but not the TORC1 substrate S6K and that it plays an important role in the regulation of Akt activity and the phosphorylation of Akt substrates in vivo. They mentioned LST8 as a conserved component of the complex but did not show it in the experiments.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3980,"ComplexName":"mTOR-RAPTOR complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"P42345;Q8N122;Q9BVC4","subunits.Entrez.IDs.":"2475;57521;64223","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0035556;GO:0000902;GO:0016049","GO.description":"intracellular signal transduction;cell morphogenesis;cell growth","FunCat.ID":"30.01;40.01","FunCat.description":"cellular signalling;cell growth / morphogenesis","PubMed.ID":15268862,"subunits.Protein.name.":"Serine/threonine-protein kinase mTOR ;Regulatory-associated protein of mTOR ;Target of rapamycin complex subunit LST8","subunits.Gene.name.":"MTOR;RPTOR;MLST8","subunits.Gene.name.syn.":"FRAP FRAP1 FRAP2 RAFT1 RAPT1;KIAA1303 RAPTOR;GBL LST8","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The raptor-mTOR complex regulates by phosphorylating the ribosomal S6 Kinase (S6K) in a  rapamycin-sensitive manner.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":3988,"ComplexName":"ClpP complex, heptameric","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q16740","subunits.Entrez.IDs.":"8192","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0005515;GO:0005739","GO.description":"protein binding;mitochondrion","FunCat.ID":"16.01;70.16","FunCat.description":"protein binding;mitochondrion","PubMed.ID":16115876,"subunits.Protein.name.":"ATP-dependent Clp protease proteolytic subunit, mitochondrial","subunits.Gene.name.":"CLPP","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"ClpP occurs as a stable heptamer in solution. Heptameric hClpP has no proteolytic activity and very low peptidase activity.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":3989,"ComplexName":"ClpP complex, heptameric","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O88696","subunits.Entrez.IDs.":"53895","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0005515;GO:0005739","GO.description":"protein binding;mitochondrion","FunCat.ID":"16.01;70.16","FunCat.description":"protein binding;mitochondrion","PubMed.ID":16115876,"subunits.Protein.name.":"ATP-dependent Clp protease proteolytic subunit, mitochondrial","subunits.Gene.name.":"Clpp","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"Since ClpP from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"ClpP occurs as a stable heptamer in solution. Heptameric hClpP has no proteolytic activity and very low peptidase activity.","SWISSPROT.organism":"Mus musculus (Mouse)"}
{"ComplexID":3990,"ComplexName":"ClpXP complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O88696;Q9JHS4","subunits.Entrez.IDs.":"53895;270166","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0030163;GO:0005515;GO:0005739","GO.description":"protein catabolic process;protein binding;mitochondrion","FunCat.ID":"14.13;16.01;70.16","FunCat.description":"protein/peptide degradation;protein binding;mitochondrion","PubMed.ID":16115876,"subunits.Protein.name.":"ATP-dependent Clp protease proteolytic subunit, mitochondrial ;ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial","subunits.Gene.name.":"Clpp;Clpx","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"Since ClpP and ClpX from rat were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.","Complex.comment":"In the presence of ATP, ClpX promotes interaction between two ClpP rings, forming a proteolytic active ClpXP complex.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":3991,"ComplexName":"ClpX complex, hexameric","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O76031","subunits.Entrez.IDs.":"10845","Protein.complex.purification.method":"MI:0028- cosedimentation in solution","GO.ID":"GO:0005515;GO:0005739","GO.description":"protein binding;mitochondrion","FunCat.ID":"16.01;70.16","FunCat.description":"protein binding;mitochondrion","PubMed.ID":16115876,"subunits.Protein.name.":"ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial","subunits.Gene.name.":"CLPX","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":3992,"ComplexName":"ClpXP complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O76031;Q16740","subunits.Entrez.IDs.":"10845;8192","Protein.complex.purification.method":"MI:0040- electron microscopy","GO.ID":"GO:0030163;GO:0005515;GO:0005739","GO.description":"protein catabolic process;protein binding;mitochondrion","FunCat.ID":"14.13;16.01;70.16","FunCat.description":"protein/peptide degradation;protein binding;mitochondrion","PubMed.ID":16115876,"subunits.Protein.name.":"ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial;ATP-dependent Clp protease proteolytic subunit, mitochondrial","subunits.Gene.name.":"CLPX;CLPP","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In the presence of ATP, ClpX promotes interaction between two ClpP rings, forming a proteolytic active ClpXP complex: two rings of ClpP heptamers bind to two ClpX hexamers.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":4025,"ComplexName":"Affixin-actinin(alpha) complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12814;Q9HBI1","subunits.Entrez.IDs.":"87;29780","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0018- two hybrid","GO.ID":"GO:0007229;GO:0015629","GO.description":"integrin-mediated signaling pathway;actin cytoskeleton","FunCat.ID":"30.05.02.26;70.04.03","FunCat.description":"integrin receptor signalling pathway;actin cytoskeleton","PubMed.ID":15159419,"subunits.Protein.name.":"Alpha-actinin-1 ;Beta-parvin","subunits.Gene.name.":"ACTN1;PARVB","subunits.Gene.name.syn.":";None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Affixin interacts with alpha-actinin and mediates integrin signaling for reorganization of F-actin induced by initial cell\\u2013substrate interaction.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":4039,"ComplexName":"PAR4-BACE1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P56817;Q96IZ0","subunits.Entrez.IDs.":"23621;5074","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0030163","GO.description":"protein catabolic process","FunCat.ID":"14.13","FunCat.description":"protein/peptide degradation","PubMed.ID":15671026,"subunits.Protein.name.":"Beta-secretase 1 ;PRKC apoptosis WT1 regulator protein","subunits.Gene.name.":"BACE1;PAWR","subunits.Gene.name.syn.":"BACE KIAA1149;PAR4","Disease.comment":"This complex is involved in the pathogenesis of Alzheimer disease.","Subunits.comment":"None","Complex.comment":"The C-terminal domain of PAR-4 is necessary for forming a complex with the cytosolic tail of BACE1. PAR-4 may be directly involved in regulating the APP cleavage activity of BACE1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":4043,"ComplexName":"NEMO-HIF2(alpha)-ARNT complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P27540;Q99814;Q9Y6K9","subunits.Entrez.IDs.":"405;2034;8517","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0007249","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;I-kappaB kinase/NF-kappaB signaling","FunCat.ID":"11.02.03.04;30.01.05.01.04","FunCat.description":"transcriptional control;NIK-I-kappaB/NF-kappaB cascade","PubMed.ID":15653678,"subunits.Protein.name.":"Aryl hydrocarbon receptor nuclear translocator ;Endothelial PAS domain-containing protein 1 ;NF-kappa-B essential modulator","subunits.Gene.name.":"ARNT;EPAS1;IKBKG","subunits.Gene.name.syn.":"BHLHE2;BHLHE73 HIF2A MOP2 PASD2;FIP3, NEMO","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"During hypoxia HIF(alpha) proteins migrate into the nucleus and heterodimerize with the aryl hydrocarbon nuclear translocator ARNT (also called HIF-1(beta)).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":4055,"ComplexName":"Axin-Dvl-Gsk complex","Organism":"Mouse","Synonyms":"None","Cell.line":"COS-7 cells","subunits.UniProt.IDs.":"O35625;P51141;Q9WV60","subunits.Entrez.IDs.":"12005;13542;56637","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016055","GO.description":"Wnt signaling pathway","FunCat.ID":"30.05.02.20","FunCat.description":"Wnt signalling pathway","PubMed.ID":10428961,"subunits.Protein.name.":"Axin-1 ;Segment polarity protein dishevelled homolog DVL-1;Glycogen synthase kinase-3 beta","subunits.Gene.name.":"Axin1;Dvl1;Gsk3b","subunits.Gene.name.syn.":"Axin Fu;Dvl;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Gsk, Dvl and Axin form a complex, which is probably bridged by Axin in the absence of Wnt-signaling.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":4056,"ComplexName":"Axin-Dvl-Gsk-Frat1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"COS-7 cells","subunits.UniProt.IDs.":"O35625;P51141;P70339;Q9WV60","subunits.Entrez.IDs.":"12005;13542;14296;56637","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016055","GO.description":"Wnt signaling pathway","FunCat.ID":"30.05.02.20","FunCat.description":"Wnt signalling pathway","PubMed.ID":10428961,"subunits.Protein.name.":"Axin-1 ;Segment polarity protein dishevelled homolog DVL-1;Proto-oncogene FRAT1 ;Glycogen synthase kinase-3 beta","subunits.Gene.name.":"Axin1;Dvl1;Frat1;Gsk3b","subunits.Gene.name.syn.":"Axin Fu;Dvl;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Wnt may promote the disintegration of the Axin-Dvl-Gsk-Frat1 complex.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":4062,"ComplexName":"NRP1-VEGFR2-VEGF(165) complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14786;P15692;P35968","subunits.Entrez.IDs.":"8829;7422;3791","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0107- surface plasmon resonance","GO.ID":"GO:0007155;GO:0001525","GO.description":"cell adhesion;angiogenesis","FunCat.ID":"34.07;41.05.16","FunCat.description":"cell adhesion;angiogenesis","PubMed.ID":17575273,"subunits.Protein.name.":"Neuropilin-1;Vascular endothelial growth factor A ;Vascular endothelial growth factor receptor 2","subunits.Gene.name.":"NRP1;VEGFA;KDR","subunits.Gene.name.syn.":"NRP VEGF165R;VEGF;FLK1, VEGFR2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"VEGF165 mediates the formation of complexes containing VEGFR2 and NRP1, which enhances the affinity of VEGF165 for VEGFR2 and therefore VEGFR2 signaling. VEGF121 does not promote VEGFR2\\u00b7NRP1 complex formation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":4072,"ComplexName":"Heterotrimeric SKP1-CUL1-ROC1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62877;P63208;Q13616","subunits.Entrez.IDs.":"9978;6500;8454","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0051276;GO:0016567;GO:0016579;GO:0043161;GO:0006511","GO.description":"chromosome organization;protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process","FunCat.ID":"42.10.03;14.07.05;14.13.01.01","FunCat.description":"organization of chromosome structure;modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway)","PubMed.ID":15118074,"subunits.Protein.name.":"E3 ubiquitin-protein ligase RBX1;S-phase kinase-associated protein 1;Cullin-1","subunits.Gene.name.":"RBX1;SKP1;CUL1","subunits.Gene.name.syn.":"RNF75, ROC1;EMC19, OCP2, SKP1A, TCEB1L;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SCFhFBH1 (=SKP1/CUL1/ROC1 - human F-box DNA helicase) can act as helicase and E3 ubiquitin ligase.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":4081,"ComplexName":"Ku70/Ku86 complex","Organism":"Human","Synonyms":"Ku complex","Cell.line":"None","subunits.UniProt.IDs.":"P12956;P13010","subunits.Entrez.IDs.":"2547;7520","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006281;GO:0003677;GO:0006974;GO:0005634","GO.description":"DNA repair;DNA binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;16.03.01;32.01.09;70.10","FunCat.description":"DNA repair;DNA binding;DNA damage response;nucleus","PubMed.ID":10783163,"subunits.Protein.name.":"X-ray repair cross-complementing protein 6 ;X-ray repair cross-complementing protein 5","subunits.Gene.name.":"XRCC6;XRCC5","subunits.Gene.name.syn.":"G22P1;G22P2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ku complex interacts with and stimulates the Werner protein.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":4082,"ComplexName":"Ku70/Ku86/Werner complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12956;P13010;Q14191","subunits.Entrez.IDs.":"2547;7520;7486","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006281;GO:0003677;GO:0006974;GO:0005634","GO.description":"DNA repair;DNA binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;16.03.01;32.01.09;70.10","FunCat.description":"DNA repair;DNA binding;DNA damage response;nucleus","PubMed.ID":10783163,"subunits.Protein.name.":"X-ray repair cross-complementing protein 6 ;X-ray repair cross-complementing protein 5 ;Werner syndrome ATP-dependent helicase","subunits.Gene.name.":"XRCC6;XRCC5;WRN","subunits.Gene.name.syn.":"G22P1;G22P2;RECQ3 RECQL2","Disease.comment":"Werner syndrome (=is the hallmark premature aging disorder in which affected humans appear older than their chronological age).","Subunits.comment":"None","Complex.comment":"Ku complex interacts with and stimulates the Werner protein.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":4089,"ComplexName":"SMAD6-HOXC8 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43541;P31273","subunits.Entrez.IDs.":"4091;3224","Protein.complex.purification.method":"MI:0018- two hybrid; MI:0019- coimmunoprecipitation; MI:0413- electrophoretic mobility shift assay","GO.ID":"GO:0045892;GO:0003677","GO.description":"negative regulation of transcription, DNA-templated;DNA binding","FunCat.ID":"11.02.03.04.03;16.03.01","FunCat.description":"transcription repression;DNA binding","PubMed.ID":10722652,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 6 ;Homeobox protein Hox-C8","subunits.Gene.name.":"SMAD6;HOXC8","subunits.Gene.name.syn.":"MADH6;HOX3A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The Smad6-Hoxc8 complex inhibits interaction of Smad1 with Hoxc-8- and Smad1-induced transcription activity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":4090,"ComplexName":"SMAD6-HOXA9 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43541;P31269","subunits.Entrez.IDs.":"4091;3205","Protein.complex.purification.method":"MI:0413- electrophoretic mobility shift assay","GO.ID":"GO:0003677","GO.description":"DNA binding","FunCat.ID":"16.03.01","FunCat.description":"DNA binding","PubMed.ID":10722652,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 6 ;Homeobox protein Hox-A9","subunits.Gene.name.":"SMAD6;HOXA9","subunits.Gene.name.syn.":"MADH6;HOX1G","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":4095,"ComplexName":"Catulin (alpha) - catenin (beta) complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P35222;Q9UBT7","subunits.Entrez.IDs.":"1499;8727","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0023052;GO:0007155","GO.description":"signaling;cell adhesion","FunCat.ID":"30.01;34.07","FunCat.description":"cellular signalling;cell adhesion","PubMed.ID":14993280,"subunits.Protein.name.":"Catenin beta-1;Alpha-catulin","subunits.Gene.name.":"CTNNB1;CTNNAL1","subunits.Gene.name.syn.":"CTNNB;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":4096,"ComplexName":"Catenin (alpha) - catenin (beta) complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P35221;P35222","subunits.Entrez.IDs.":"1495;1499","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0023052;GO:0007155","GO.description":"signaling;cell adhesion","FunCat.ID":"30.01;34.07","FunCat.description":"cellular signalling;cell adhesion","PubMed.ID":14993280,"subunits.Protein.name.":"Catenin alpha-1 ;Catenin beta-1","subunits.Gene.name.":"CTNNA1;CTNNB1","subunits.Gene.name.syn.":";CTNNB","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":4149,"ComplexName":"5'-AMP-activated protein kinase complex (AMPK)","Organism":"Mammalia","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"O54950;Q09137;Q6PAM0","subunits.Entrez.IDs.":"19082;78975;108097","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006720;GO:0006633;GO:0008299;GO:0009062;GO:0016042;GO:0008300;GO:0006629;GO:0006631;GO:0008610","GO.description":"isoprenoid metabolic process;fatty acid biosynthetic process;isoprenoid biosynthetic process;fatty acid catabolic process;lipid catabolic process;isoprenoid catabolic process;lipid metabolic process;fatty acid metabolic process;lipid biosynthetic process","FunCat.ID":"01.06;01.06.05;01.06.06","FunCat.description":"lipid, fatty acid and isoprenoid metabolism;fatty acid metabolism;isoprenoid metabolism","PubMed.ID":17012231,"subunits.Protein.name.":"5'-AMP-activated protein kinase subunit gamma-1 ;5'-AMP-activated protein kinase catalytic subunit alpha-2 ;5'-AMP-activated protein kinase subunit beta-2","subunits.Gene.name.":"Prkag1;Prkaa2;Prkab2","subunits.Gene.name.syn.":"Prkaac;Ampk Ampk2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Rattus norvegicus (Rat);Mus musculus (Mouse)"}
{"ComplexID":4151,"ComplexName":"TSC complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O70239;P18265;P49816;Q9Z136","subunits.Entrez.IDs.":"79257;50686;24855;60445","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006417","GO.description":"regulation of translation","FunCat.ID":"12.07","FunCat.description":"translational control","PubMed.ID":15972957,"subunits.Protein.name.":"Axin-1 ;Glycogen synthase kinase-3 alpha ;Tuberin ;Hamartin","subunits.Gene.name.":"Axin1;Gsk3a;Tsc2;Tsc1","subunits.Gene.name.syn.":"Axin;;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TSC1/TSC2 complex associated with GSK3 and Axin  promotes beta-catenin degradation to inhibit Wnt-stimulated TCF/LEF-dependent transcription.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":4158,"ComplexName":"HSP90-FKBP38-CAM-Ca(2+) complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P07900;P62158;Q14318","subunits.Entrez.IDs.":"3320;None;23770","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0017-classical fluorescence spectroscopy","GO.ID":"GO:0043067","GO.description":"regulation of programmed cell death","FunCat.ID":"40.10.02.04","FunCat.description":"regulation of apoptosis","PubMed.ID":17379601,"subunits.Protein.name.":"Heat shock protein HSP 90-alpha;Calmodulin;Peptidyl-prolyl cis-trans isomerase FKBP8","subunits.Gene.name.":"HSP90AA1;CALM1; CAL;FKBP8","subunits.Gene.name.syn.":"HSP90A HSPC1 HSPCA;CALM, CAM, CAM1, CAM2, CAMB, CALML2, CAM3, CAMC, CAMIII;FKBP38","Disease.comment":"None","Subunits.comment":"Since the authors did not specify HSP90, we used isoform HSP90A.","Complex.comment":"The authors show that the TPR domain of FKBP38 interacts with the C-terminal domain of Hsp90, but only if the FKBP38-CaM-Ca(2+) complex is preformed. The resulting ternary complex is enzymatically inactive, and the association of Bcl-2 and the PPIase site of FKBP38 is prevented.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":4200,"ComplexName":"DLP1-hFIS1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00429;Q9Y3D6","subunits.Entrez.IDs.":"10059;51024","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0055 fluorescent resonance energy transfer","GO.ID":"GO:0007005","GO.description":"mitochondrion organization","FunCat.ID":"42.16","FunCat.description":"mitochondrion","PubMed.ID":12861026,"subunits.Protein.name.":"Dynamin-1-like protein ;Mitochondrial fission 1 protein","subunits.Gene.name.":"DNM1L;FIS1","subunits.Gene.name.syn.":"DLP1 DRP1;TTC11","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors suggest that hFis1 participates in mitochondrial fission through an interaction that recruits DLP1 from the cytosol.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":4216,"ComplexName":"GR-hnRNP U complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04150;Q00839","subunits.Entrez.IDs.":"2908;3192","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0004- affinity chromatography technologies","GO.ID":"GO:2001141;GO:0006355","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":9353307,"subunits.Protein.name.":"Glucocorticoid receptor ;Heterogeneous nuclear ribonucleoprotein U","subunits.Gene.name.":"NR3C1;HNRNPU","subunits.Gene.name.syn.":"GRL;HNRPU SAFA U21.1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The glucocorticoid receptor (GR) is a ligand-dependent transcription factor that is able to modulate gene activity by binding to its response element, interacting with other transcription factors (here = GRIP120 = hnRNP U), and contacting several accessory proteins such as coactivators.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":4389,"ComplexName":"EIF3 core complex (EIF3A, EIF3B, EIF3G, EIF3I)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75821;P55884;Q13347;Q14152","subunits.Entrez.IDs.":"8666;8662;8668;8661","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006413","GO.description":"translational initiation","FunCat.ID":"12.04.01","FunCat.description":"translation initiation","PubMed.ID":14688252,"subunits.Protein.name.":"Eukaryotic translation initiation factor 3 subunit G ;Eukaryotic translation initiation factor 3 subunit B;Eukaryotic translation initiation factor 3 subunit I ;Eukaryotic translation initiation factor 3 subunit A","subunits.Gene.name.":"EIF3G;EIF3B;EIF3I;EIF3A","subunits.Gene.name.syn.":"EIF3S4;EIF3S9;EIF3S2 TRIP1;EIF3S10 KIAA0139","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"EIF3b appears to be a central scaffolding subunit.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":4392,"ComplexName":"EIF3 complex (EIF3A, EIF3B, EIF3G, EIF3I, EIF3C)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75821;P55884;Q13347;Q14152;Q99613","subunits.Entrez.IDs.":"8666;8662;8668;8661;8663","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006413","GO.description":"translational initiation","FunCat.ID":"12.04.01","FunCat.description":"translation initiation","PubMed.ID":14688252,"subunits.Protein.name.":"Eukaryotic translation initiation factor 3 subunit G ;Eukaryotic translation initiation factor 3 subunit B;Eukaryotic translation initiation factor 3 subunit I ;Eukaryotic translation initiation factor 3 subunit A ;Eukaryotic translation initiation factor 3 subunit C","subunits.Gene.name.":"EIF3G;EIF3B;EIF3I;EIF3A;EIF3C","subunits.Gene.name.syn.":"EIF3S4;EIF3S9;EIF3S2 TRIP1;EIF3S10 KIAA0139;EIF3S8","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"EIF3b appears to be a central scaffolding subunit. EIF3c is able to associate with the four-subunit eIF3 subcomplex, but does so only weakly under these expression and purification conditions.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":4395,"ComplexName":"EIF3 complex (EIF3B, EIF3G, EIF3I)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75821;P55884;Q13347","subunits.Entrez.IDs.":"8666;8662;8668","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006413","GO.description":"translational initiation","FunCat.ID":"12.04.01","FunCat.description":"translation initiation","PubMed.ID":14688252,"subunits.Protein.name.":"Eukaryotic translation initiation factor 3 subunit G ;Eukaryotic translation initiation factor 3 subunit B;Eukaryotic translation initiation factor 3 subunit I","subunits.Gene.name.":"EIF3G;EIF3B;EIF3I","subunits.Gene.name.syn.":"EIF3S4;EIF3S9;EIF3S2 TRIP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":4399,"ComplexName":"EIF3 complex (EIF3B, EIF3J, EIF3I)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75822;P55884;Q13347","subunits.Entrez.IDs.":"8669;8662;8668","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006413","GO.description":"translational initiation","FunCat.ID":"12.04.01","FunCat.description":"translation initiation","PubMed.ID":14688252,"subunits.Protein.name.":"Eukaryotic translation initiation factor 3 subunit J ;Eukaryotic translation initiation factor 3 subunit B;Eukaryotic translation initiation factor 3 subunit I","subunits.Gene.name.":"EIF3J;EIF3B;EIF3I","subunits.Gene.name.syn.":"EIF3S1;EIF3S9;EIF3S2 TRIP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":4403,"ComplexName":"EIF3 complex (EIF3A, EIF3B, EIF3G, EIF3I, EIF3J)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75821;O75822;P55884;Q13347;Q14152","subunits.Entrez.IDs.":"8666;8669;8662;8668;8661","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006413","GO.description":"translational initiation","FunCat.ID":"12.04.01","FunCat.description":"translation initiation","PubMed.ID":14688252,"subunits.Protein.name.":"Eukaryotic translation initiation factor 3 subunit G ;Eukaryotic translation initiation factor 3 subunit J ;Eukaryotic translation initiation factor 3 subunit B;Eukaryotic translation initiation factor 3 subunit I ;Eukaryotic translation initiation factor 3 subunit A","subunits.Gene.name.":"EIF3G;EIF3J;EIF3B;EIF3I;EIF3A","subunits.Gene.name.syn.":"EIF3S4;EIF3S1;EIF3S9;EIF3S2 TRIP1;EIF3S10 KIAA0139","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"EIF3b appears to be a central scaffolding subunit. The authors conclude that EIF3J promotes the stable association of EIF3 subcomplexes to the 40S ribosomal subunit.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":4478,"ComplexName":"CBF-DNA complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"P23511;P25208;Q13952","subunits.Entrez.IDs.":"4800;4801;4802","Protein.complex.purification.method":"MI:0413- electrophoretic mobility shift assay; MI:0096- pull down","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04;16.03.01;70.10","FunCat.description":"transcriptional control;DNA binding;nucleus","PubMed.ID":15243141,"subunits.Protein.name.":"Nuclear transcription factor Y subunit alpha ;Nuclear transcription factor Y subunit beta ;Nuclear transcription factor Y subunit gamma","subunits.Gene.name.":"NFYA;NFYB;NFYC","subunits.Gene.name.syn.":";HAP3;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":4498,"ComplexName":"p32-CBF-DNA complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"P23511;P25208;Q07021;Q13952","subunits.Entrez.IDs.":"4800;4801;708;4802","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0045892;GO:0003677;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;DNA binding;nucleus","FunCat.ID":"11.02.03.04.03;16.03.01;70.10","FunCat.description":"transcription repression;DNA binding;nucleus","PubMed.ID":15243141,"subunits.Protein.name.":"Nuclear transcription factor Y subunit alpha ;Nuclear transcription factor Y subunit beta ;Complement component 1 Q subcomponent-binding protein, mitochondrial;Nuclear transcription factor Y subunit gamma","subunits.Gene.name.":"NFYA;NFYB;C1QBP;NFYC","subunits.Gene.name.syn.":";HAP3;GC1QBP HABP1 SF2P32;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"p32 interacts specifically with CBF-B subunit and also associates with CBF-DNA complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":4869,"ComplexName":"beta(1)-AR receptosome (ADRB1-SAP97-AKAP79-PRKAR2A)","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"P08588;P13861;P24588;Q12959","subunits.Entrez.IDs.":"153;5576;9495;1739","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0055- fluorescent resonance energy transfer","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0006468;GO:0006470;GO:0046777;GO:0007186","GO.description":"intracellular protein transport;protein targeting;protein transport;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;G-protein coupled receptor signaling pathway","FunCat.ID":"14.04;20.01.10;14.07.03;30.05.02.24","FunCat.description":"protein targeting, sorting and translocation;protein transport;modification by phosphorylation, dephosphorylation, autophosphorylation;G-protein coupled receptor signalling pathway","PubMed.ID":17170109,"subunits.Protein.name.":"Beta-1 adrenergic receptor;cAMP-dependent protein kinase type II-alpha regulatory subunit;A-kinase anchor protein 5;Disks large homolog 1","subunits.Gene.name.":"ADRB1;PRKAR2A;AKAP5;DLG1","subunits.Gene.name.syn.":"ADRB1R, B1AR;PKR2, PRKAR2;AKAP79;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SAP97 siRNA abolished the ability of the beta(1)-AR to co-immunoprecipitate AKAP79 and SAP97. This indicates that SAP97 probably serves as a bridging molecule between the beta1-AR and the AKAP79-PKA complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":4976,"ComplexName":"SVIP-p97/VCP-DERL1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"P55072;Q8NHG7;Q9BUN8","subunits.Entrez.IDs.":"7415;258010;79139","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0030968;GO:0005783","GO.description":"endoplasmic reticulum unfolded protein response;endoplasmic reticulum","FunCat.ID":"32.01.07;70.07","FunCat.description":"unfolded protein response (e.g. ER quality control);endoplasmic reticulum","PubMed.ID":17872946,"subunits.Protein.name.":"Transitional endoplasmic reticulum ATPase;Small VCP/p97-interacting protein;Derlin-1","subunits.Gene.name.":"VCP;SVIP;DERL1","subunits.Gene.name.syn.":"None;;DER1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors identified SVIP as the first endogenous inhibitor of ERAD (ER-associated degradation) that uses a novel mechanism through inhibiting the assembly of the gp78-p97/VCP-Derlin1 complex. The data suggest that p97/VCP and Derlin1 can form a complex with either gp78 or SVIP. The gp78 complex facilitates ERAD, whereas the SVIP complex inhibits ERAD.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":4977,"ComplexName":"gp78-p97/VCP-DERL1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"P55072;Q9BUN8;Q9UKV5","subunits.Entrez.IDs.":"7415;79139;267","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0043161;GO:0006511;GO:0030968;GO:0005783","GO.description":"proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;endoplasmic reticulum unfolded protein response;endoplasmic reticulum","FunCat.ID":"14.13.01.01;32.01.07;70.07","FunCat.description":"proteasomal degradation (ubiquitin/proteasomal pathway);unfolded protein response (e.g. ER quality control);endoplasmic reticulum","PubMed.ID":17872946,"subunits.Protein.name.":"Transitional endoplasmic reticulum ATPase;Derlin-1 ;E3 ubiquitin-protein ligase AMFR","subunits.Gene.name.":"VCP;DERL1;AMFR","subunits.Gene.name.syn.":"None;DER1;RNF45","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors identified SVIP as the first endogenous inhibitor of ERAD (ER-associated degradation) that uses a novel mechanism through inhibiting the assembly of the gp78-p97/VCP-Derlin1 complex. The data suggest that p97/VCP and Derlin1 can form a complex with either gp78 or SVIP. The gp78 complex facilitates ERAD, whereas the SVIP complex inhibits ERAD.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":4997,"ComplexName":"p97/VCP-VIMP-DERL1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P55072;Q9BQE4;Q9BUN8","subunits.Entrez.IDs.":"7415;55829;79139","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030968;GO:0005783","GO.description":"endoplasmic reticulum unfolded protein response;endoplasmic reticulum","FunCat.ID":"32.01.07;70.07","FunCat.description":"unfolded protein response (e.g. ER quality control);endoplasmic reticulum","PubMed.ID":16186509,"subunits.Protein.name.":"Transitional endoplasmic reticulum ATPase;Selenoprotein S ;Derlin-1","subunits.Gene.name.":"VCP;VIMP;DERL1","subunits.Gene.name.syn.":"None;SELS;DER1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":4998,"ComplexName":"p97/VCP-VIMP-DERL2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P55072;Q9BQE4;Q9GZP9","subunits.Entrez.IDs.":"7415;55829;51009","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030968;GO:0005783","GO.description":"endoplasmic reticulum unfolded protein response;endoplasmic reticulum","FunCat.ID":"32.01.07;70.07","FunCat.description":"unfolded protein response (e.g. ER quality control);endoplasmic reticulum","PubMed.ID":16186509,"subunits.Protein.name.":"Transitional endoplasmic reticulum ATPase;Selenoprotein S ;Derlin-2","subunits.Gene.name.":"VCP;VIMP;DERL2","subunits.Gene.name.syn.":"None;SELS;DER2 FLANA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":4999,"ComplexName":"p97/VCP-VIMP-DERL1-DERL2-HRD1-SEL1L complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P55072;Q86TM6;Q9BQE4;Q9BUN8;Q9GZP9;Q9UBV2","subunits.Entrez.IDs.":"7415;84447;55829;79139;51009;6400","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030968;GO:0005783","GO.description":"endoplasmic reticulum unfolded protein response;endoplasmic reticulum","FunCat.ID":"32.01.07;70.07","FunCat.description":"unfolded protein response (e.g. ER quality control);endoplasmic reticulum","PubMed.ID":16186509,"subunits.Protein.name.":"Transitional endoplasmic reticulum ATPase;E3 ubiquitin-protein ligase synoviolin ;Selenoprotein S ;Derlin-1 ;Derlin-2 ;Protein sel-1 homolog 1","subunits.Gene.name.":"VCP;SYVN1;VIMP;DERL1;DERL2;SEL1L","subunits.Gene.name.syn.":"None;HRD1 KIAA1810;SELS;DER1;DER2 FLANA;TSA305","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cell lin: U373.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5000,"ComplexName":"p47-p97 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O35987;P46462","subunits.Entrez.IDs.":"83809;116643","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0006906","GO.description":"intracellular protein transport;protein targeting;protein transport;vesicle fusion","FunCat.ID":"14.04;20.01.10;20.09.07.27","FunCat.description":"protein targeting, sorting and translocation;protein transport;vesicle fusion","PubMed.ID":10811609,"subunits.Protein.name.":"NSFL1 cofactor p47;Transitional endoplasmic reticulum ATPase","subunits.Gene.name.":"Nsfl1c;Vcp","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ufd1/Npl4 and p47 compete for p97 binding and form alternative complexes in.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5001,"ComplexName":"p97-Ufd1-Npl4 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P46462;Q9ES53;Q9ES54","subunits.Entrez.IDs.":"116643;84478;140639","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0043161;GO:0006511;GO:0030968;GO:0005783","GO.description":"proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;endoplasmic reticulum unfolded protein response;endoplasmic reticulum","FunCat.ID":"14.13.01.01;32.01.07;70.07","FunCat.description":"proteasomal degradation (ubiquitin/proteasomal pathway);unfolded protein response (e.g. ER quality control);endoplasmic reticulum","PubMed.ID":11740563,"subunits.Protein.name.":"Transitional endoplasmic reticulum ATPase;Ubiquitin fusion degradation protein 1 homolog;Nuclear protein localization protein 4 homolog","subunits.Gene.name.":"Vcp;Ufd1l;Nploc4","subunits.Gene.name.syn.":"None;None;Npl4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ufd1/Npl4 and p47 compete for p97 binding and form alternative complexes.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5002,"ComplexName":"p47-p97 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O35987;P46462","subunits.Entrez.IDs.":"83809;116643","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0006906","GO.description":"intracellular protein transport;protein targeting;protein transport;vesicle fusion","FunCat.ID":"14.04;20.01.10;20.09.07.27","FunCat.description":"protein targeting, sorting and translocation;protein transport;vesicle fusion","PubMed.ID":11740563,"subunits.Protein.name.":"NSFL1 cofactor p47;Transitional endoplasmic reticulum ATPase","subunits.Gene.name.":"Nsfl1c;Vcp","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ufd1/Npl4 and p47 compete for p97 binding and form alternative complexes in cytosol.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5003,"ComplexName":"p97/VCP homohexamer complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q01853","subunits.Entrez.IDs.":"269523","Protein.complex.purification.method":"MI:0114- x-ray crystallography; MI:0040- electron microscopy","GO.ID":"GO:0043161;GO:0006511;GO:0000301;GO:0006906;GO:0030968","GO.description":"proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;retrograde transport, vesicle recycling within Golgi;vesicle fusion;endoplasmic reticulum unfolded protein response","FunCat.ID":"14.13.01.01;20.09.07.07;20.09.07.27;32.01.07","FunCat.description":"proteasomal degradation (ubiquitin/proteasomal pathway);retrograde transport;vesicle fusion;unfolded protein response (e.g. ER quality control)","PubMed.ID":12949490,"subunits.Protein.name.":"Transitional endoplasmic reticulum ATPase","subunits.Gene.name.":"Vcp","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse)"}
{"ComplexID":5092,"ComplexName":"Cdk5-p39-CaMKII(alpha)-(alpha)actinin1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"O35926;P11275;Q03114;Q9Z1P2","subunits.Entrez.IDs.":"12570;25400;140908;81634","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0000278;GO:0051726;GO:0035556;GO:0016477;GO:0022008;GO:0048699;GO:0030182;GO:0007420","GO.description":"mitotic cell cycle;regulation of cell cycle;intracellular signal transduction;cell migration;neurogenesis;generation of neurons;neuron differentiation;brain development","FunCat.ID":"10.03.01.01;10.03.01;30.01;34.05.01;41.05.13;43.03.13;47.03.01.01.01","FunCat.description":"mitotic cell cycle;mitotic cell cycle and cell cycle control;cellular signalling;cell migration;neurogenesis;neuron;brain","PubMed.ID":12223541,"subunits.Protein.name.":"Cyclin-dependent kinase 5 activator 2 ;Calcium/calmodulin-dependent protein kinase type II subunit alpha ;Cyclin-dependent-like kinase 5 ;Alpha-actinin-1","subunits.Gene.name.":"Cdk5r2;Camk2a;Cdk5;Actn1","subunits.Gene.name.syn.":"Nck5ai;;Cdkn5;None","Disease.comment":"Cdk5 might be a potential drug target for the treatment of neurodegenerative diseases.","Subunits.comment":"Since Cdk5r2 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5099,"ComplexName":"RB1(hypophosphorylated)-E2F4 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06400;Q16254","subunits.Entrez.IDs.":"5925;1874","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0000082;GO:0045892","GO.description":"G1/S transition of mitotic cell cycle;negative regulation of transcription, DNA-templated","FunCat.ID":"10.03.01.01.03;11.02.03.04.03","FunCat.description":"G1/S transition of mitotic cell cycle;transcription repression","PubMed.ID":9380698,"subunits.Protein.name.":"Retinoblastoma-associated protein ;Transcription factor E2F4","subunits.Gene.name.":"RB1;E2F4","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Hypo-phosphorylated Rb interacts with E2F4 in the early G1 phase of the cell cyclus. Inactivation of Rb by hyper-phosphorylation in late G1 phase causes release of E2F, allowing transcription of genes important for DNA synthesis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5100,"ComplexName":"CyclinD3-CDK4-CDK6 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P11802;P30281;Q00534","subunits.Entrez.IDs.":"1019;896;1021","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0000278;GO:0000082;GO:0035556;GO:0007519","GO.description":"mitotic cell cycle;G1/S transition of mitotic cell cycle;intracellular signal transduction;skeletal muscle tissue development","FunCat.ID":"10.03.01.01;10.03.01.01.03;30.01;41.05.15","FunCat.description":"mitotic cell cycle;G1/S transition of mitotic cell cycle;cellular signalling;myogenesis","PubMed.ID":8930396,"subunits.Protein.name.":"Cyclin-dependent kinase 4 ;G1/S-specific cyclin-D3;Cyclin-dependent kinase 6","subunits.Gene.name.":"CDK4;CCND3;CDK6","subunits.Gene.name.syn.":";;CDKN6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Upon myocyte differentiation subunit composition of the CDK4/6 complex is altered. Interaction with cyclinD1 is reduced but interaction with cyclinD3 and p21 is enhanced thus inhibiting the kinase activity of CDK4/6.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5101,"ComplexName":"CyclinD3-CDK4-CDK6-p21 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P11802;P30281;P38936;Q00534","subunits.Entrez.IDs.":"1019;896;1026;1021","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0000278;GO:0000082;GO:0035556;GO:0007519","GO.description":"mitotic cell cycle;G1/S transition of mitotic cell cycle;intracellular signal transduction;skeletal muscle tissue development","FunCat.ID":"10.03.01.01;10.03.01.01.03;30.01;41.05.15","FunCat.description":"mitotic cell cycle;G1/S transition of mitotic cell cycle;cellular signalling;myogenesis","PubMed.ID":8930396,"subunits.Protein.name.":"Cyclin-dependent kinase 4 ;G1/S-specific cyclin-D3;Cyclin-dependent kinase inhibitor 1 ;Cyclin-dependent kinase 6","subunits.Gene.name.":"CDK4;CCND3;CDKN1A;CDK6","subunits.Gene.name.syn.":";;CAP20 CDKN1 CIP1 MDA6 PIC1 SDI1 WAF1;CDKN6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Upon myocyte differentiation subunit composition of the CDK4/6 complex is altered. Interaction with cyclinD1 is reduced but interaction with cyclinD3 and p21 is enhanced thus inhibiting the kinase activity of CDK4/6.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5107,"ComplexName":"p34(SEI-1)-CDK4-CyclinD2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P11802;P30279;Q9UHV2","subunits.Entrez.IDs.":"1019;894;29950","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006260;GO:0035556","GO.description":"DNA replication;intracellular signal transduction","FunCat.ID":"10.01.03;30.01","FunCat.description":"DNA synthesis and replication;cellular signalling","PubMed.ID":15065884,"subunits.Protein.name.":"Cyclin-dependent kinase 4 ;G1/S-specific cyclin-D2;SERTA domain-containing protein 1","subunits.Gene.name.":"CDK4;CCND2;SERTAD1","subunits.Gene.name.syn.":";;SEI1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"p34(SEI1) binds to the CDK4-CyclinD2 complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5115,"ComplexName":"Trip(Br1)-Dp1-E2F1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q08639;Q61501;Q9JL10","subunits.Entrez.IDs.":"21781;13555;55942","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0045893","GO.description":"positive regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.01","FunCat.description":"transcription activation","PubMed.ID":11331592,"subunits.Protein.name.":"Transcription factor Dp-1;Transcription factor E2F1 ;SERTA domain-containing protein 1","subunits.Gene.name.":"Tfdp1;E2f1;Sertad1","subunits.Gene.name.syn.":"None;;Sei1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Trip-Br proteins interact with Dp1 thus stimulating the E2F1-Dp1 transcriptional activity.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5116,"ComplexName":"Trip(Br2)-Dp1-E2F1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q08639;Q61501;Q9JJG5","subunits.Entrez.IDs.":"21781;13555;58172","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0045893","GO.description":"positive regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.01","FunCat.description":"transcription activation","PubMed.ID":11331592,"subunits.Protein.name.":"Transcription factor Dp-1;Transcription factor E2F1 ;SERTA domain-containing protein 2","subunits.Gene.name.":"Tfdp1;E2f1;Sertad2","subunits.Gene.name.syn.":"None;;Kiaa0127","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5117,"ComplexName":"pRb2/p130-multimolecular complex (DNMT1, E2F4, SuV39H1, HDAC1, RBL2)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43463;P26358;Q08999;Q13547;Q16254","subunits.Entrez.IDs.":"6839;1786;5934;3065;1874","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0047- far western blotting","GO.ID":"GO:0006351","GO.description":"transcription, DNA-templated","FunCat.ID":"11","FunCat.description":"TRANSCRIPTION","PubMed.ID":12789259,"subunits.Protein.name.":"Histone-lysine N-methyltransferase SUV39H1 ;DNA ;Retinoblastoma-like protein 2;Histone deacetylase 1;Transcription factor E2F4","subunits.Gene.name.":"SUV39H1;DNMT1;RBL2;HDAC1;E2F4","subunits.Gene.name.syn.":"KMT1A SUV39H;AIM CXXC9 DNMT;RB2, P130;RPD3L1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5118,"ComplexName":"pRb2/p130-multimolecular complex (RB2, E2F4, HDAC1, SUV39H1, P300)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43463;Q08999;Q09472;Q13547;Q16254","subunits.Entrez.IDs.":"6839;5934;2033;3065;1874","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0047- far western blotting","GO.ID":"GO:0006351","GO.description":"transcription, DNA-templated","FunCat.ID":"11","FunCat.description":"TRANSCRIPTION","PubMed.ID":12789259,"subunits.Protein.name.":"Histone-lysine N-methyltransferase SUV39H1 ;Retinoblastoma-like protein 2;Histone acetyltransferase p300;Histone deacetylase 1;Transcription factor E2F4","subunits.Gene.name.":"SUV39H1;RBL2;EP300;HDAC1;E2F4","subunits.Gene.name.syn.":"KMT1A SUV39H;RB2, P130;P300;RPD3L1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5119,"ComplexName":"p19-Cdk4 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P30285;Q60773","subunits.Entrez.IDs.":"12567;12581","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0000278;GO:0051726;GO:0051098;GO:0005515;GO:0006469;GO:0019210;GO:0035556","GO.description":"mitotic cell cycle;regulation of cell cycle;regulation of binding;protein binding;negative regulation of protein kinase activity;kinase inhibitor activity;intracellular signal transduction","FunCat.ID":"10.03.01.01;10.03.01;18.01.07;16.01;18.02.01.02.05;30.01","FunCat.description":"mitotic cell cycle;mitotic cell cycle and cell cycle control;regulation by binding / dissociation;protein binding;kinase inhibitior;cellular signalling","PubMed.ID":7739547,"subunits.Protein.name.":"Cyclin-dependent kinase 4 ;Cyclin-dependent kinase 4 inhibitor D","subunits.Gene.name.":"Cdk4;Cdkn2d","subunits.Gene.name.syn.":"Crk3;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5120,"ComplexName":"p19-Cdk6 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q60773;Q64261","subunits.Entrez.IDs.":"12581;12571","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0000278;GO:0051726;GO:0051098;GO:0005515;GO:0006469;GO:0019210;GO:0035556","GO.description":"mitotic cell cycle;regulation of cell cycle;regulation of binding;protein binding;negative regulation of protein kinase activity;kinase inhibitor activity;intracellular signal transduction","FunCat.ID":"10.03.01.01;10.03.01;18.01.07;16.01;18.02.01.02.05;30.01","FunCat.description":"mitotic cell cycle;mitotic cell cycle and cell cycle control;regulation by binding / dissociation;protein binding;kinase inhibitior;cellular signalling","PubMed.ID":7739547,"subunits.Protein.name.":"Cyclin-dependent kinase 4 inhibitor D ;Cyclin-dependent kinase 6","subunits.Gene.name.":"Cdkn2d;Cdk6","subunits.Gene.name.syn.":";Cdkn6 Crk2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5127,"ComplexName":"p18-Cdk4 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P30285;Q60772","subunits.Entrez.IDs.":"12567;12580","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0000278;GO:0051726;GO:0051098;GO:0005515;GO:0006469;GO:0019210;GO:0035556","GO.description":"mitotic cell cycle;regulation of cell cycle;regulation of binding;protein binding;negative regulation of protein kinase activity;kinase inhibitor activity;intracellular signal transduction","FunCat.ID":"10.03.01.01;10.03.01;18.01.07;16.01;18.02.01.02.05;30.01","FunCat.description":"mitotic cell cycle;mitotic cell cycle and cell cycle control;regulation by binding / dissociation;protein binding;kinase inhibitior;cellular signalling","PubMed.ID":7739547,"subunits.Protein.name.":"Cyclin-dependent kinase 4 ;Cyclin-dependent kinase 4 inhibitor C","subunits.Gene.name.":"Cdk4;Cdkn2c","subunits.Gene.name.syn.":"Crk3;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5128,"ComplexName":"p18-Cdk6 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q60772;Q64261","subunits.Entrez.IDs.":"12580;12571","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0000278;GO:0051726;GO:0051098;GO:0005515;GO:0006469;GO:0019210;GO:0035556","GO.description":"mitotic cell cycle;regulation of cell cycle;regulation of binding;protein binding;negative regulation of protein kinase activity;kinase inhibitor activity;intracellular signal transduction","FunCat.ID":"10.03.01.01;10.03.01;18.01.07;16.01;18.02.01.02.05;30.01","FunCat.description":"mitotic cell cycle;mitotic cell cycle and cell cycle control;regulation by binding / dissociation;protein binding;kinase inhibitior;cellular signalling","PubMed.ID":7739547,"subunits.Protein.name.":"Cyclin-dependent kinase 4 inhibitor C ;Cyclin-dependent kinase 6","subunits.Gene.name.":"Cdkn2c;Cdk6","subunits.Gene.name.syn.":";Cdkn6 Crk2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5142,"ComplexName":"DCS complex (Ptbp1, Ptbp2, Hnrph1, Hnrpf)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O35737;P17225;Q91Z31;Q9Z2X1","subunits.Entrez.IDs.":"59013;19205;56195;98758","Protein.complex.purification.method":"MI:0226- ion exchange chromatography; MI:0019- coimmunoprecipitation; MI:0004- affinity chromatography technologies","GO.ID":"GO:0043484;GO:0048024;GO:0003723;GO:0005634","GO.description":"regulation of RNA splicing;regulation of mRNA splicing, via spliceosome;RNA binding;nucleus","FunCat.ID":"11.04.03.01.10;16.03.03;70.10","FunCat.description":"regulation of splicing;RNA binding;nucleus","PubMed.ID":11003644,"subunits.Protein.name.":"Heterogeneous nuclear ribonucleoprotein H ;Polypyrimidine tract-binding protein 1 ;Polypyrimidine tract-binding protein 2 ;Heterogeneous nuclear ribonucleoprotein F","subunits.Gene.name.":"Hnrnph1;Ptbp1;Ptbp2;Hnrnpf","subunits.Gene.name.syn.":"Hnrph Hnrph1;Ptb;Brptb Nptb;Hnrpf","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5143,"ComplexName":"E2F1-Rb complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06400;Q01094","subunits.Entrez.IDs.":"5925;1869","Protein.complex.purification.method":"MI:0412- electrophoretic mobility supershift assay; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0000080;GO:2001141;GO:0006355","GO.description":"mitotic G1 phase;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated","FunCat.ID":"10.03.01.01.01;11.02.03.04","FunCat.description":"G1 phase of mitotic cell cycle;transcriptional control","PubMed.ID":1531040,"subunits.Protein.name.":"Retinoblastoma-associated protein ;Transcription factor E2F1","subunits.Gene.name.":"RB1;E2F1","subunits.Gene.name.syn.":";RBBP3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Rb forms a complex with E2F1 in the G1 phase of the cell cycle.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5144,"ComplexName":"E2F1-p107-cyclinA complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P20248;P28749;Q01094","subunits.Entrez.IDs.":"890;5933;1869","Protein.complex.purification.method":"MI:0412- electrophoretic mobility supershift assay; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0000084;GO:2001141;GO:0006355","GO.description":"mitotic S phase;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated","FunCat.ID":"10.03.01.01.05;11.02.03.04","FunCat.description":"S phase of mitotic cell cycle;transcriptional control","PubMed.ID":1531040,"subunits.Protein.name.":"Cyclin-A2 ;Retinoblastoma-like protein 1;Transcription factor E2F1","subunits.Gene.name.":"CCNA2;RBL1;E2F1","subunits.Gene.name.syn.":"CCN1 CCNA;PRB1, p107, CP107;RBBP3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"p107 forms a complex with E2F1 and cyclin A in the S phase of the cell cycle.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5145,"ComplexName":"p19-Cdk4-cyclinD2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P30280;P30285;Q60773","subunits.Entrez.IDs.":"12444;12567;12581","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0000278;GO:0051726;GO:0035556","GO.description":"mitotic cell cycle;regulation of cell cycle;intracellular signal transduction","FunCat.ID":"10.03.01.01;10.03.01;30.01","FunCat.description":"mitotic cell cycle;mitotic cell cycle and cell cycle control;cellular signalling","PubMed.ID":7739547,"subunits.Protein.name.":"G1/S-specific cyclin-D2;Cyclin-dependent kinase 4 ;Cyclin-dependent kinase 4 inhibitor D","subunits.Gene.name.":"Ccnd2;Cdk4;Cdkn2d","subunits.Gene.name.syn.":"Cyl-2;Crk3;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"p19 binds to preassembled cyclinD-CDK complex in vitro and inhibits their activity without replacing Cyclin D. However, affinity for p19 to the uncomplexed CDK4 is higher.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5146,"ComplexName":"RB1-TFAP2A complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P05549;P06400","subunits.Entrez.IDs.":"7020;5925","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0045893","GO.description":"positive regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.01","FunCat.description":"transcription activation","PubMed.ID":9632747,"subunits.Protein.name.":"Transcription factor AP-2-alpha ;Retinoblastoma-associated protein","subunits.Gene.name.":"TFAP2A;RB1","subunits.Gene.name.syn.":"AP2TF TFAP2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5151,"ComplexName":"Nsf-Stx1a-Napa complex","Organism":"Rat","Synonyms":"None","Cell.line":"liver","subunits.UniProt.IDs.":"P32851;P54921;Q9QUL6","subunits.Entrez.IDs.":"116470;140673;60355","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":1315316,"subunits.Protein.name.":"Syntaxin-1A;Alpha-soluble NSF attachment protein;Vesicle-fusing ATPase","subunits.Gene.name.":"Stx1a;Napa;Nsf","subunits.Gene.name.syn.":"Sap;Snap Snapa;Erg1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5152,"ComplexName":"Nsf-Stx1a-NAPG complex","Organism":"Rat","Synonyms":"None","Cell.line":"liver","subunits.UniProt.IDs.":"P32851;Q99747;Q9QUL6","subunits.Entrez.IDs.":"116470;8774;60355","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006906;GO:0048489;GO:0016079","GO.description":"vesicle fusion;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.05","FunCat.description":"vesicle fusion;synaptic vesicle exocytosis","PubMed.ID":1315316,"subunits.Protein.name.":"Syntaxin-1A;Gamma-soluble NSF attachment protein;Vesicle-fusing ATPase","subunits.Gene.name.":"Stx1a;NAPG;Nsf","subunits.Gene.name.syn.":"Sap;SNAPG;Erg1","Disease.comment":"None","Subunits.comment":"Since Napg from rat was not available in the UniProt database at the time of annotation, the orthologous human protein was used.","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Homo sapiens (Human);Rattus norvegicus (Rat)"}
{"ComplexID":5153,"ComplexName":"CTFC-TAF1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P49711;Q01105","subunits.Entrez.IDs.":"10664;6418","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0004- affinity chromatography technologies","GO.ID":"GO:2001141;GO:0006355","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":14759373,"subunits.Protein.name.":"Transcriptional repressor CTCF ;Protein SET","subunits.Gene.name.":"CTCF;SET","subunits.Gene.name.syn.":";TAF-I","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5154,"ComplexName":"CTCF-nucleophosmin complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06748;P49711","subunits.Entrez.IDs.":"4869;10664","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0029- cosedimentation through density gradients; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;nucleus","FunCat.ID":"11.02.03.04;70.10","FunCat.description":"transcriptional control;nucleus","PubMed.ID":14759373,"subunits.Protein.name.":"Nucleophosmin ;Transcriptional repressor CTCF","subunits.Gene.name.":"NPM1;CTCF","subunits.Gene.name.syn.":"NPM;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"CTCF and nucleophosmin work together as insularors blocking enhancer activity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5158,"ComplexName":"SMARCA2/BRM-BAF57-MECP2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P51531;P51608;Q969G3","subunits.Entrez.IDs.":"6595;4204;6605","Protein.complex.purification.method":"MI:0047- far western blotting; MI:0019- coimmunoprecipitation","GO.ID":"GO:0045892","GO.description":"negative regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.03","FunCat.description":"transcription repression","PubMed.ID":15696166,"subunits.Protein.name.":"Probable global transcription activator SNF2L2;Methyl-CpG-binding protein 2 ;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","subunits.Gene.name.":"SMARCA2;MECP2;SMARCE1","subunits.Gene.name.syn.":"BAF190B, BRM, SNF2A, SNF2L2;;BAF57","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5159,"ComplexName":"E2F4-p107-cyclinE complex","Organism":"Human","Synonyms":"None","Cell.line":"MCF-7 cells","subunits.UniProt.IDs.":"P24864;P28749;Q16254","subunits.Entrez.IDs.":"898;5933;1874","Protein.complex.purification.method":"MI:0412- electrophoretic mobility supershift assay","GO.ID":"GO:0000082;GO:0005634","GO.description":"G1/S transition of mitotic cell cycle;nucleus","FunCat.ID":"10.03.01.01.03;70.10","FunCat.description":"G1/S transition of mitotic cell cycle;nucleus","PubMed.ID":12096339,"subunits.Protein.name.":"G1/S-specific cyclin-E1;Retinoblastoma-like protein 1;Transcription factor E2F4","subunits.Gene.name.":"CCNE1;RBL1;E2F4","subunits.Gene.name.syn.":"CCNE;PRB1, p107, CP107;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In proliferating MCF-7 cells the complex contains mostly cyclin A. After overexpression of cyclin E most of the complexes contain cyclin E.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5160,"ComplexName":"E2F4-p130 complex","Organism":"Human","Synonyms":"None","Cell.line":"MCF-7 cells","subunits.UniProt.IDs.":"Q08999;Q16254","subunits.Entrez.IDs.":"5934;1874","Protein.complex.purification.method":"MI:0412- electrophoretic mobility supershift assay","GO.ID":"GO:0000082;GO:0005634","GO.description":"G1/S transition of mitotic cell cycle;nucleus","FunCat.ID":"10.03.01.01.03;70.10","FunCat.description":"G1/S transition of mitotic cell cycle;nucleus","PubMed.ID":12096339,"subunits.Protein.name.":"Retinoblastoma-like protein 2;Transcription factor E2F4","subunits.Gene.name.":"RBL2;E2F4","subunits.Gene.name.syn.":"RB2, P130;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"After tamoxifen treatment p107 is replaced by p130.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5162,"ComplexName":"ELK1-SRF-ELK3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P11831;P19419;P41970","subunits.Entrez.IDs.":"6722;2002;2004","Protein.complex.purification.method":"MI:0413- electrophoretic mobility shift assay","GO.ID":"GO:2001141;GO:0006355","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":7540136,"subunits.Protein.name.":"Serum response factor ;ETS domain-containing protein Elk-1;ETS domain-containing protein Elk-3","subunits.Gene.name.":"SRF;ELK1;ELK3","subunits.Gene.name.syn.":";;NET SAP2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5165,"ComplexName":"AP1G1-PACS1-FURIN complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43747;P09958;Q6VY07","subunits.Entrez.IDs.":"164;5045;55690","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0016192","GO.description":"intracellular protein transport;protein targeting;protein transport;vesicle-mediated transport","FunCat.ID":"14.04;20.01.10;20.09.07","FunCat.description":"protein targeting, sorting and translocation;protein transport;vesicular transport (Golgi network, etc.)","PubMed.ID":11331585,"subunits.Protein.name.":"AP-1 complex subunit gamma-1;Furin ;Phosphofurin acidic cluster sorting protein 1","subunits.Gene.name.":"AP1G1;FURIN;PACS1","subunits.Gene.name.syn.":"ADTG CLAPG1;FUR PACE PCSK3;KIAA1175","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The data suggest that PACS-1 functions in a connector capacity by linking acidic cluster motifs to adaptor complexes and their associated vesicle-generating machinery.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5166,"ComplexName":"C3G-Crkl-Shp2 complex","Organism":"Rat","Synonyms":"None","Cell.line":"PC12 cells","subunits.UniProt.IDs.":"P41499;Q5U2U2;Q9QYV3","subunits.Entrez.IDs.":"25622;287942;63881","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0007169","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway","FunCat.ID":"30.05.01.12","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways","PubMed.ID":11466412,"subunits.Protein.name.":"Tyrosine-protein phosphatase non-receptor type 11 ;Crk-like protein;C3G protein","subunits.Gene.name.":"Ptpn11;Crkl;Rapgef1","subunits.Gene.name.syn.":";;c3g Grf2 Grf2_v1 Grf2_v2 Rapgef1_v1 Rapgef1_v2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In untreated cells C3G is tyrosine phosphorylated constitutively and formes a stable complex with CrkL and Shp2.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5167,"ComplexName":"C3G-Crkl-Shp2-Cbl-Egfr complex","Organism":"Rat","Synonyms":"None","Cell.line":"PC12 cells","subunits.UniProt.IDs.":"P22682;P41499;Q5U2U2;Q9QX70;Q9QYV3","subunits.Entrez.IDs.":"12402;25622;287942;24329;63881","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0007169","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway","FunCat.ID":"30.05.01.12","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways","PubMed.ID":11466412,"subunits.Protein.name.":"E3 ubiquitin-protein ligase CBL;Tyrosine-protein phosphatase non-receptor type 11 ;Crk-like protein;Receptor protein-tyrosine kinase ;C3G protein","subunits.Gene.name.":"Cbl;Ptpn11;Crkl;Egfr;Rapgef1","subunits.Gene.name.syn.":"None;;;;c3g Grf2 Grf2_v1 Grf2_v2 Rapgef1_v1 Rapgef1_v2","Disease.comment":"None","Subunits.comment":"Since Cbl from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"After EGF treatment, C3G is dephosphorylated and a protein complex that includes C3G/CrkL/Shp2/Cbl/Egfr is formed transiently.","SWISSPROT.organism":"Mus musculus (Mouse);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5168,"ComplexName":"C3G-Crkl-Shp2-Gab2-TrkA complex","Organism":"Rat","Synonyms":"None","Cell.line":"PC12 cells","subunits.UniProt.IDs.":"P35739;P41499;Q5U2U2;Q9EQH1;Q9QYV3","subunits.Entrez.IDs.":"59109;25622;287942;84477;63881","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0007169","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway","FunCat.ID":"30.05.01.12","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways","PubMed.ID":11466412,"subunits.Protein.name.":"High affinity nerve growth factor receptor ;Tyrosine-protein phosphatase non-receptor type 11 ;Crk-like protein;GRB2-associated-binding protein 2 ;C3G protein","subunits.Gene.name.":"Ntrk1;Ptpn11;Crkl;Gab2;Rapgef1","subunits.Gene.name.syn.":"Trk Trka;;;;c3g Grf2 Grf2_v1 Grf2_v2 Rapgef1_v1 Rapgef1_v2","Disease.comment":"None","Subunits.comment":"Since Cbl from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"After NGF treatment of the cell, C3G remains tyrosine-phosphorylated and the C3G-CrkL-Shp2 complex becomes stably associated with Gab2 and TrkA.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5171,"ComplexName":"SH3KBP1-CBLB-EGFR complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells, HeLa cells","subunits.UniProt.IDs.":"P00533;Q13191;Q96B97","subunits.Entrez.IDs.":"1956;868;30011","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006898;GO:0007169","GO.description":"receptor-mediated endocytosis;transmembrane receptor protein tyrosine kinase signaling pathway","FunCat.ID":"20.09.18.09.01.01;30.05.01.12","FunCat.description":"receptor-mediated endocytosis;transmembrane receptor protein tyrosine kinase signalling pathways","PubMed.ID":12177062,"subunits.Protein.name.":"Epidermal growth factor receptor;E3 ubiquitin-protein ligase CBL-B ;SH3 domain-containing kinase-binding protein 1","subunits.Gene.name.":"EGFR;CBLB;SH3KBP1","subunits.Gene.name.syn.":"ERBB, ERBB1, HER1;RNF56;CIN85","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Growth factor stimulation led to a complex formation between endogenous SH3KBP1, Cbl-b and EGF or PDGF receptors in several cell lines. The results suggested that SH3KBP1 binding to Cbl-b is important for EGF receptor internalization, although it has no effect on Cbl-b-induced receptor ubiquitination.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5172,"ComplexName":"Sh3kbp1-Cblb-Egfr complex","Organism":"Mouse","Synonyms":"None","Cell.line":"NIH 3T3 cells","subunits.UniProt.IDs.":"Q01279;Q3TTA7;Q8R550","subunits.Entrez.IDs.":"13649;208650;58194","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006898;GO:0007169","GO.description":"receptor-mediated endocytosis;transmembrane receptor protein tyrosine kinase signaling pathway","FunCat.ID":"20.09.18.09.01.01;30.05.01.12","FunCat.description":"receptor-mediated endocytosis;transmembrane receptor protein tyrosine kinase signalling pathways","PubMed.ID":12177062,"subunits.Protein.name.":"Epidermal growth factor receptor ;E3 ubiquitin-protein ligase CBL-B ;SH3 domain-containing kinase-binding protein 1","subunits.Gene.name.":"Egfr;Cblb;Sh3kbp1","subunits.Gene.name.syn.":";;Ruk Seta","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Growth factor stimulation led to a complex formation between endogenous Sh3kbp1, Cbl-b and EGF or PDGF receptors in several cell lines. The results suggested that Sh3kbp1 binding to Cbl-b is important for EGF receptor internalization, although it has no effect on Cbl-b-induced receptor ubiquitination.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5173,"ComplexName":"Sh3kbp1-Cblb-Pdgfrb complex","Organism":"Mouse","Synonyms":"None","Cell.line":"NIH 3T3 cells","subunits.UniProt.IDs.":"P05622;Q3TTA7;Q8R550","subunits.Entrez.IDs.":"18596;208650;58194","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006898;GO:0007169","GO.description":"receptor-mediated endocytosis;transmembrane receptor protein tyrosine kinase signaling pathway","FunCat.ID":"20.09.18.09.01.01;30.05.01.12","FunCat.description":"receptor-mediated endocytosis;transmembrane receptor protein tyrosine kinase signalling pathways","PubMed.ID":12177062,"subunits.Protein.name.":"Platelet-derived growth factor receptor beta ;E3 ubiquitin-protein ligase CBL-B ;SH3 domain-containing kinase-binding protein 1","subunits.Gene.name.":"Pdgfrb;Cblb;Sh3kbp1","subunits.Gene.name.syn.":"Pdgfr Pdgfr1;;Ruk Seta","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Growth factor stimulation led to a complex formation between endogenous Sh3kbp1, Cbl-b and EGF or PDGF receptors in several cell lines. The results suggested that Sh3kbp1 binding to Cbl-b is important for  receptor internalization, although it has no effect on Cbl-b-induced receptor ubiquitination.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5174,"ComplexName":"Smarcb1/Ini1-Smarca2-Mecp2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q99KH6;Q9Z0H3;Q9Z2D6","subunits.Entrez.IDs.":"67155;20587;17257","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0045892","GO.description":"negative regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.03","FunCat.description":"transcription repression","PubMed.ID":15696166,"subunits.Protein.name.":"Smarca2 protein;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;Methyl-CpG-binding protein 2","subunits.Gene.name.":"Smarca2;Smarcb1;Mecp2","subunits.Gene.name.syn.":";Baf47 Ini1 Snf5l1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5175,"ComplexName":"SWI/SNF-related complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O54941;P70288;P97496;Q3UX55;Q60520;Q9Z0H3;Q9Z2D6","subunits.Entrez.IDs.":"57376;15182;20588;67155;20466;20587;17257","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0045892","GO.description":"negative regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.03","FunCat.description":"transcription repression","PubMed.ID":15696166,"subunits.Protein.name.":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;Histone deacetylase 2;SWI/SNF complex subunit SMARCC1;Putative uncharacterized protein ;Paired amphipathic helix protein Sin3a;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;Methyl-CpG-binding protein 2","subunits.Gene.name.":"Smarce1;Hdac2;Smarcc1;Smarca2;Sin3a;Smarcb1;Mecp2","subunits.Gene.name.syn.":"Baf57;Yy1bp;Baf155 Srg3;;Kiaa4126;Baf47 Ini1 Snf5l1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5176,"ComplexName":"MGC1-DNA-PKcs-Ku complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12956;P13010;P78527;Q14676","subunits.Entrez.IDs.":"2547;7520;5591;9656","Protein.complex.purification.method":"MI:0096- pull down; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0000075;GO:0006974;GO:0005634","GO.description":"DNA repair;cell cycle checkpoint;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;10.03.01.03;32.01.09;70.10","FunCat.description":"DNA repair;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);DNA damage response;nucleus","PubMed.ID":15377652,"subunits.Protein.name.":"X-ray repair cross-complementing protein 6 ;X-ray repair cross-complementing protein 5 ;DNA-dependent protein kinase catalytic subunit ;Mediator of DNA damage checkpoint protein 1","subunits.Gene.name.":"XRCC6;XRCC5;PRKDC;MDC1","subunits.Gene.name.syn.":"G22P1;G22P2;HYRC HYRC1;KIAA0170 NFBD1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"MDC1 directly interacts with the DNA-PKc-Ku complex and this interaction is required for efficient DNA-PK autophosphorylation and DNA damage repair.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5177,"ComplexName":"Polycystin-1 multiprotein complex (ACTN1, CDH1, SRC, JUP, VCL, CTNNB1, PXN, BCAR1, PKD1, PTK2, TLN1)","Organism":"Human","Synonyms":"None","Cell.line":"epithelium","subunits.UniProt.IDs.":"P12814;P12830;P12931;P14923;P18206;P35222;P49023;P56945;P98161;Q05397;Q9Y490","subunits.Entrez.IDs.":"87;999;6714;3728;7414;1499;5829;9564;5310;5747;7094","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0007155;GO:0030855;GO:0002009;GO:0001822","GO.description":"cell adhesion;epithelial cell differentiation;morphogenesis of an epithelium;kidney development","FunCat.ID":"34.07;45.03.09;47.03.07.01","FunCat.description":"cell adhesion;epithelium;kidney","PubMed.ID":11113628,"subunits.Protein.name.":"Alpha-actinin-1 ;Cadherin-1;Proto-oncogene tyrosine-protein kinase Src;Junction plakoglobin ;Vinculin ;Catenin beta-1;Paxillin;Breast cancer anti-estrogen resistance protein 1;Polycystin-1;Focal adhesion kinase 1;Talin-1","subunits.Gene.name.":"ACTN1;CDH1;SRC;JUP;VCL;CTNNB1;PXN;BCAR1;PKD1;PTK2;TLN1","subunits.Gene.name.syn.":";CDHE UVO;SRC1;CTNNG DP3;;CTNNB;;CAS CASS1 CRKAS;None;FAK FAK1;KIAA1027 TLN","Disease.comment":"PKD1 is involved in autosomal dominant polycystic kidney disease (ADPKD).","Subunits.comment":"None","Complex.comment":"The results suggest that polycystin-1 complexes are present in focal adhesions in subconfluent cells  and in both focal adhesions and cell\\u2013cell adherens complexes in confluent cells.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5178,"ComplexName":"JAK2-PAFR-TYK2 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS-7 cells, Mono Mac 1 cells","subunits.UniProt.IDs.":"O60674;P25105;P29597","subunits.Entrez.IDs.":"3717;5724;7297","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0007259","GO.description":"JAK-STAT cascade","FunCat.ID":"30.01.05.01.01","FunCat.description":"JAK-STAT cascade","PubMed.ID":14500680,"subunits.Protein.name.":"Tyrosine-protein kinase JAK2 ;Platelet-activating factor receptor ;Non-receptor tyrosine-protein kinase TYK2","subunits.Gene.name.":"JAK2;PTAFR;TYK2","subunits.Gene.name.syn.":";PAFR;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5179,"ComplexName":"NCOA6-DNA-PK-Ku-PARP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P09874;P12956;P13010;P78527;Q14686","subunits.Entrez.IDs.":"142;2547;7520;5591;23054","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006281;GO:0005634","GO.description":"DNA repair;nucleus","FunCat.ID":"10.01.05.01;70.10","FunCat.description":"DNA repair;nucleus","PubMed.ID":12519782,"subunits.Protein.name.":"Poly [ADP-ribose] polymerase 1;X-ray repair cross-complementing protein 6 ;X-ray repair cross-complementing protein 5 ;DNA-dependent protein kinase catalytic subunit ;Nuclear receptor coactivator 6","subunits.Gene.name.":"PARP1;XRCC6;XRCC5;PRKDC;NCOA6","subunits.Gene.name.syn.":"ADPRT PPOL;G22P1;G22P2;HYRC HYRC1;AIB3, KIAA0181, RAP250, TRBP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TRBP (NCOA6) stimulates DNA-PK kinase activity in the absence of DNA.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5182,"ComplexName":"DNA-PK-Ku complex","Organism":"Human","Synonyms":"DNA-PK-Ku70-Ku80 complex","Cell.line":"None","subunits.UniProt.IDs.":"P12956;P13010;P78527","subunits.Entrez.IDs.":"2547;7520;5591","Protein.complex.purification.method":"MI:0412- electrophoretic mobility supershift assay","GO.ID":"GO:0006281;GO:0006468;GO:0006470;GO:0046777;GO:0003677;GO:0006464;GO:0043085;GO:0008047;GO:0005634","GO.description":"DNA repair;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;DNA binding;cellular protein modification process;positive regulation of catalytic activity;enzyme activator activity;nucleus","FunCat.ID":"10.01.05.01;14.07.03;16.03.01;14.07;18.02.01.01;70.10","FunCat.description":"DNA repair;modification by phosphorylation, dephosphorylation, autophosphorylation;DNA binding;protein modification;enzyme activator;nucleus","PubMed.ID":9442054,"subunits.Protein.name.":"X-ray repair cross-complementing protein 6 ;X-ray repair cross-complementing protein 5 ;DNA-dependent protein kinase catalytic subunit","subunits.Gene.name.":"XRCC6;XRCC5;PRKDC","subunits.Gene.name.syn.":"G22P1;G22P2;HYRC HYRC1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"For assembly of the DNA-PK-Ku70-Ku80 complex presence of DNA is necessary.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5183,"ComplexName":"DNA-PK-Ku-eIF2-NF90-NF45 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P05198;P12956;P13010;P20042;P41091;P78527;Q12905;Q12906","subunits.Entrez.IDs.":"1965;2547;7520;8894;1968;5591;3608;3609","Protein.complex.purification.method":"MI:0412- electrophoretic mobility supershift assay; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281;GO:0006468;GO:0006470;GO:0046777;GO:0003677;GO:0006464;GO:0043085;GO:0008047;GO:0005634","GO.description":"DNA repair;protein phosphorylation;protein dephosphorylation;protein autophosphorylation;DNA binding;cellular protein modification process;positive regulation of catalytic activity;enzyme activator activity;nucleus","FunCat.ID":"10.01.05.01;14.07.03;16.03.01;14.07;18.02.01.01;70.10","FunCat.description":"DNA repair;modification by phosphorylation, dephosphorylation, autophosphorylation;DNA binding;protein modification;enzyme activator;nucleus","PubMed.ID":9442054,"subunits.Protein.name.":"Eukaryotic translation initiation factor 2 subunit 1 ;X-ray repair cross-complementing protein 6 ;X-ray repair cross-complementing protein 5 ;Eukaryotic translation initiation factor 2 subunit 2 ;Eukaryotic translation initiation factor 2 subunit 3 ;DNA-dependent protein kinase catalytic subunit ;Interleukin enhancer-binding factor 2 ;Interleukin enhancer-binding factor 3","subunits.Gene.name.":"EIF2S1;XRCC6;XRCC5;EIF2S2;EIF2S3;PRKDC;ILF2;ILF3","subunits.Gene.name.syn.":"EIF2A;G22P1;G22P2;EIF2B;EIF2G;HYRC HYRC1;NF45;DRBF MPHOSPH4 NF90","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"NF90, in complex with NF45, interacts with DNA-PKcs and Ku and promotes formation of a complex on DNA.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5184,"ComplexName":"SWI/SNF chromatin-remodeling complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P51531;P51608;Q13547;Q969G3;Q96ST3","subunits.Entrez.IDs.":"6595;4204;3065;6605;25942","Protein.complex.purification.method":"MI:0402- chromatin immunoprecipitation assays","GO.ID":"GO:0045892","GO.description":"negative regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.03","FunCat.description":"transcription repression","PubMed.ID":15696166,"subunits.Protein.name.":"Probable global transcription activator SNF2L2;Methyl-CpG-binding protein 2 ;Histone deacetylase 1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;Paired amphipathic helix protein Sin3a","subunits.Gene.name.":"SMARCA2;MECP2;HDAC1;SMARCE1;SIN3A","subunits.Gene.name.syn.":"BAF190B, BRM, SNF2A, SNF2L2;;RPD3L1;BAF57;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5185,"ComplexName":"SWI/SNF chromatin-remodeling complex (Mecp2, Smarc)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O54941;P70288;Q3UX55;Q60520;Q9Z0H3;Q9Z2D6","subunits.Entrez.IDs.":"57376;15182;67155;20466;20587;17257","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0045892","GO.description":"negative regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.03","FunCat.description":"transcription repression","PubMed.ID":15696166,"subunits.Protein.name.":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;Histone deacetylase 2;Putative uncharacterized protein ;Paired amphipathic helix protein Sin3a;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;Methyl-CpG-binding protein 2","subunits.Gene.name.":"Smarce1;Hdac2;Smarca2;Sin3a;Smarcb1;Mecp2","subunits.Gene.name.syn.":"Baf57;Yy1bp;;Kiaa4126;Baf47 Ini1 Snf5l1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5189,"ComplexName":"YWHAQ-CALM1-CABIN1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P27348;P62158;Q9Y6J0","subunits.Entrez.IDs.":"10971;None;23523","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":15902271,"subunits.Protein.name.":"14-3-3 protein theta;Calmodulin;Calcineurin-binding protein cabin-1","subunits.Gene.name.":"YWHAQ;CALM1; CAL;CABIN1","subunits.Gene.name.syn.":"None;CALM, CAM, CAM1, CAM2, CAMB, CALML2, CAM3, CAMC, CAMIII;KIAA0330","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5190,"ComplexName":"TIAM1-EFNB1-EPHA2 complex","Organism":"Human","Synonyms":"None","Cell.line":"COS-1 cells","subunits.UniProt.IDs.":"P29317;P98172;Q13009","subunits.Entrez.IDs.":"1969;1947;7074","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0010183;GO:0022008;GO:0048699","GO.description":"pollen tube guidance;neurogenesis;generation of neurons","FunCat.ID":"40.01.03.03;41.05.13","FunCat.description":"guidance of longitudinal cell extension (e.g. pollen tube guidance, axonal pathfinding);neurogenesis","PubMed.ID":14988728,"subunits.Protein.name.":"Ephrin type-A receptor 2 ;Ephrin-B1 ;T-lymphoma invasion and metastasis-inducing protein 1","subunits.Gene.name.":"EPHA2;EFNB1;TIAM1","subunits.Gene.name.syn.":"ECK;EFL3 EPLG2 LERK2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5191,"ComplexName":"Ezh2 methyltransferase complex, cytosolic","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75530;Q15022;Q61188","subunits.Entrez.IDs.":"8726;23512;14056","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0018126;GO:0006479;GO:0005737","GO.description":"protein hydroxylation;protein methylation;cytoplasm","FunCat.ID":"14.07.09;70.03","FunCat.description":"posttranslational modification of amino acids (e.g. hydroxylation, methylation);cytoplasm","PubMed.ID":15882624,"subunits.Protein.name.":"Polycomb protein EED;Polycomb protein SUZ12;Histone-lysine N-methyltransferase EZH2","subunits.Gene.name.":"EED;SUZ12;Ezh2","subunits.Gene.name.syn.":"None;CHET9 JJAZ1 KIAA0160;Enx1h","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Mus musculus (Mouse)"}
{"ComplexID":5192,"ComplexName":"Tiam1-Efnb1-Epha2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P52795;Q03145;Q60610","subunits.Entrez.IDs.":"13641;13836;21844","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0010183;GO:0022008;GO:0048699","GO.description":"pollen tube guidance;neurogenesis;generation of neurons","FunCat.ID":"40.01.03.03;41.05.13","FunCat.description":"guidance of longitudinal cell extension (e.g. pollen tube guidance, axonal pathfinding);neurogenesis","PubMed.ID":14988728,"subunits.Protein.name.":"Ephrin-B1 ;Ephrin type-A receptor 2 ;T-lymphoma invasion and metastasis-inducing protein 1","subunits.Gene.name.":"Efnb1;Epha2;Tiam1","subunits.Gene.name.syn.":"Epl2 Eplg2 Lerk2 Stra1;Eck Myk2 Sek2;Tiam-1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Tiam1 physiologically interacts with ephrin-B1 and EphA2 in the brain of an E14 mouse embryo.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5193,"ComplexName":"TNF-alpha/NF-kappa B signaling complex (CHUK, KPNA3, NFKB2, NFKBIB, REL, IKBKG,  NFKB1, NFKBIE, RELB,  NFKBIA, RELA, TNIP2)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00221;O00505;O15111;P19838;P25963;Q00653;Q01201;Q04206;Q04864;Q15653;Q8NFZ5;Q9Y6K9","subunits.Entrez.IDs.":"4794;None;1147;4790;4792;4791;5971;5970;5966;4793;79155;8517","Protein.complex.purification.method":"MI:0676- tandem affinity purification","GO.ID":"GO:0007249;GO:0005125","GO.description":"I-kappaB kinase/NF-kappaB signaling;cytokine activity","FunCat.ID":"30.01.05.01.04;40.02.03.01","FunCat.description":"NIK-I-kappaB/NF-kappaB cascade;cytokines (interleukines, colony stimulating factors, etc.)","PubMed.ID":14743216,"subunits.Protein.name.":"NF-kappa-B inhibitor epsilon ;Importin subunit alpha-4 ;Inhibitor of nuclear factor kappa-B kinase subunit alpha;Nuclear factor NF-kappa-B p105 subunit;NF-kappa-B inhibitor alpha ;Nuclear factor NF-kappa-B p100 subunit ;Transcription factor RelB;Transcription factor p65;Proto-oncogene c-Rel;NF-kappa-B inhibitor beta ;TNFAIP3-interacting protein 2 ;NF-kappa-B essential modulator","subunits.Gene.name.":"NFKBIE;KPNA3;CHUK;NFKB1;NFKBIA;NFKB2;RELB;RELA;REL;NFKBIB;TNIP2;IKBKG","subunits.Gene.name.syn.":"IKBE;QIP2;IKKA, TCF16;None;IKBA MAD3 NFKBI;LYT10;None;NFKB3;;IKBB TRIP9;ABIN2 FLIP1;FIP3, NEMO","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5194,"ComplexName":"TNF-alpha/NF-kappa B signaling complex (SEC16A, CHUK, IKBKB, NFKB2, REL, IKBKG, MAP3K14, RELA, FBXW7, USP2)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14920;O15027;O15111;O75604;Q00653;Q04206;Q04864;Q969H0;Q99558;Q9Y6K9","subunits.Entrez.IDs.":"3551;9919;1147;9099;4791;5970;5966;55294;9020;8517","Protein.complex.purification.method":"MI:0676- tandem affinity purification","GO.ID":"GO:0007249;GO:0005125","GO.description":"I-kappaB kinase/NF-kappaB signaling;cytokine activity","FunCat.ID":"30.01.05.01.04;40.02.03.01","FunCat.description":"NIK-I-kappaB/NF-kappaB cascade;cytokines (interleukines, colony stimulating factors, etc.)","PubMed.ID":14743216,"subunits.Protein.name.":"Inhibitor of nuclear factor kappa-B kinase subunit beta;Protein transport protein Sec16A ;Inhibitor of nuclear factor kappa-B kinase subunit alpha;Ubiquitin carboxyl-terminal hydrolase 2 ;Nuclear factor NF-kappa-B p100 subunit ;Transcription factor p65;Proto-oncogene c-Rel;F-box/WD repeat-containing protein 7;Mitogen-activated protein kinase kinase kinase 14 ;NF-kappa-B essential modulator","subunits.Gene.name.":"IKBKB;SEC16A;CHUK;USP2;NFKB2;RELA;REL;FBXW7;MAP3K14;IKBKG","subunits.Gene.name.syn.":"IKKB;KIAA0310 SEC16 SEC16L;IKKA, TCF16;UBP41;LYT10;NFKB3;;FBW7, FBX30, SEL10;NIK;FIP3, NEMO","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5195,"ComplexName":"PTIP-HMT complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15550;P61964;Q14686;Q15291;Q6ZW49;Q8NEZ4;Q9BTK6;Q9C005;Q9UBL3;Q9UMN6","subunits.Entrez.IDs.":"7403;11091;23054;5929;22976;58508;79447;84661;9070;None","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation; MI:0071- molecular sieving","GO.ID":"GO:0006265;GO:2001141;GO:0006355;GO:0018126;GO:0006479;GO:0003677;GO:0051276;GO:0005634","GO.description":"DNA topological change;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein hydroxylation;protein methylation;DNA binding;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04;14.07.09;16.03.01;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcriptional control;posttranslational modification of amino acids (e.g. hydroxylation, methylation);DNA binding;organization of chromosome structure;nucleus","PubMed.ID":17500065,"subunits.Protein.name.":"Lysine-specific demethylase 6A;WD repeat-containing protein 5;Nuclear receptor coactivator 6;Retinoblastoma-binding protein 5;PAX-interacting protein 1;Histone-lysine N-methyltransferase 2C;PAXIP1-associated glutamate-rich protein 1;Protein dpy-30 homolog;Set1/Ash2 histone methyltransferase complex subunit ASH2;Histone-lysine N-methyltransferase 2B","subunits.Gene.name.":"KDM6A;WDR5;NCOA6;RBBP5;PAXIP1;KMT2C;PAGR1;DPY30;ASH2L;KMT2B","subunits.Gene.name.syn.":"UTX;BIG3;AIB3, KIAA0181, RAP250, TRBP;RBQ3;PAXIP1L, PTIP;HALR, KIAA1506, MLL3;C16orf53, PA1;None;ASH2L1;HRX2 KIAA0304 MLL2 MLL4 TRX2 WBP7","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In cells without DNA damage PTIP associates with proteins involved in regulation of gene expression.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5196,"ComplexName":"TNF-alpha/NF-kappa B signaling complex (CHUK, BTRC, NFKB2, PPP6C, REL, CUL1, IKBKE, SAPS2, SAPS1, ANKRD28, RELA, SKP1)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00743;O15084;O15111;O75170;P63208;Q00653;Q04206;Q04864;Q13616;Q14164;Q9UPN7;Q9Y297","subunits.Entrez.IDs.":"5537;23243;1147;9701;6500;4791;5970;5966;8454;9641;22870;8945","Protein.complex.purification.method":"MI:0676- tandem affinity purification","GO.ID":"GO:0007249;GO:0005125","GO.description":"I-kappaB kinase/NF-kappaB signaling;cytokine activity","FunCat.ID":"30.01.05.01.04;40.02.03.01","FunCat.description":"NIK-I-kappaB/NF-kappaB cascade;cytokines (interleukines, colony stimulating factors, etc.)","PubMed.ID":14743216,"subunits.Protein.name.":"Serine/threonine-protein phosphatase 6 catalytic subunit ;Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit A ;Inhibitor of nuclear factor kappa-B kinase subunit alpha;Serine/threonine-protein phosphatase 6 regulatory subunit 2 ;S-phase kinase-associated protein 1;Nuclear factor NF-kappa-B p100 subunit ;Transcription factor p65;Proto-oncogene c-Rel;Cullin-1;Inhibitor of nuclear factor kappa-B kinase subunit epsilon ;Serine/threonine-protein phosphatase 6 regulatory subunit 1 ;F-box/WD repeat-containing protein 1A","subunits.Gene.name.":"PPP6C;ANKRD28;CHUK;PPP6R2;SKP1;NFKB2;RELA;REL;CUL1;IKBKE;PPP6R1;BTRC","subunits.Gene.name.syn.":"PPP6;KIAA0379;IKKA, TCF16;KIAA0685 PP6R2 SAPS2;EMC19, OCP2, SKP1A, TCEB1L;LYT10;NFKB3;;None;IKKE IKKI KIAA0151;KIAA1115 PP6R1 SAPS1;BTRCP FBW1A FBXW1A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5197,"ComplexName":"PTIP-DNA damage response complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60934;P49959;P54132;Q12888;Q6ZW49;Q92878","subunits.Entrez.IDs.":"4683;4361;641;7158;22976;10111","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation; MI:0071- molecular sieving","GO.ID":"GO:0006281;GO:0003677;GO:0006974;GO:0005634","GO.description":"DNA repair;DNA binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;16.03.01;32.01.09;70.10","FunCat.description":"DNA repair;DNA binding;DNA damage response;nucleus","PubMed.ID":17500065,"subunits.Protein.name.":"Nibrin ;Double-strand break repair protein MRE11A ;Bloom syndrome protein ;Tumor suppressor p53-binding protein 1 ;PAX-interacting protein 1;DNA repair protein RAD50","subunits.Gene.name.":"NBN;MRE11A;BLM;TP53BP1;PAXIP1;RAD50","subunits.Gene.name.syn.":"NBS NBS1 P95;HNGS1 MRE11;RECQ2 RECQL3;;PAXIP1L, PTIP;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In cells treated with DNA damage agents, PTIP associates with proteins involved in DNA damage response and DNA repair.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5198,"ComplexName":"CBP-RARA-RXRA-DNA complex, ligand stimulated","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P10276;P19793;Q92793","subunits.Entrez.IDs.":"5914;6256;1387","Protein.complex.purification.method":"MI:0413- electrophoretic mobility shift assay","GO.ID":"GO:0045893;GO:0023052;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;signaling;nucleus","FunCat.ID":"11.02.03.04.01;30.01;70.10","FunCat.description":"transcription activation;cellular signalling;nucleus","PubMed.ID":8616895,"subunits.Protein.name.":"Retinoic acid receptor alpha ;Retinoic acid receptor RXR-alpha ;CREB-binding protein","subunits.Gene.name.":"RARA;RXRA;CREBBP","subunits.Gene.name.syn.":"NR1B1;NR2B1;CBP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors suggest that CBP/p300 serves as an integrator of multiple signal transduction pathways within the nucleus.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5199,"ComplexName":"Kinase maturation complex 1","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P07900;P08238;P27348;P31946;P34932;P61981;P62258;P63104;Q04917;Q13163;Q16543;Q6Q0C0;Q7KZI7;Q99759;Q9NUG6;Q9UHV9","subunits.Entrez.IDs.":"3320;3326;10971;7529;3308;7532;7531;7534;7533;5607;11140;84231;2011;4215;81572;5202","Protein.complex.purification.method":"MI:0676- tandem affinity purification","GO.ID":"GO:0035556","GO.description":"intracellular signal transduction","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":14743216,"subunits.Protein.name.":"Heat shock protein HSP 90-alpha;Heat shock protein HSP 90-beta;14-3-3 protein theta;14-3-3 protein beta/alpha ;Heat shock 70 kDa protein 4;14-3-3 protein gamma;14-3-3 protein epsilon ;14-3-3 protein zeta/delta;14-3-3 protein eta ;Dual specificity mitogen-activated protein kinase kinase 5 ;Hsp90 co-chaperone Cdc37;E3 ubiquitin-protein ligase TRAF7 ;Serine/threonine-protein kinase MARK2 ;Mitogen-activated protein kinase kinase kinase 3 ;p53 and DNA damage-regulated protein 1;Prefoldin subunit 2","subunits.Gene.name.":"HSP90AA1;HSP90AB1;YWHAQ;YWHAB;HSPA4;YWHAG;YWHAE;YWHAZ;YWHAH;MAP2K5;CDC37;TRAF7;MARK2;MAP3K3;PDRG1;PFDN2","subunits.Gene.name.syn.":"HSP90A HSPC1 HSPCA;HSP90B HSPC2 HSPCB;None;;APG2;None;;None;YWHA1;MEK5 MKK5 PRKMK5;CDC37A;RFWD1 RNF119;EMK1;MAPKKK3 MEKK3;C20orf126 PDRG;PFD2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5206,"ComplexName":"Pentraxin complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O35764;P47971;P97738;Q62703","subunits.Entrez.IDs.":"81005;266777;288475;29218","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0019- coimmunoprecipitation","GO.ID":"GO:0007268","GO.description":"synaptic transmission","FunCat.ID":"34.03.01","FunCat.description":"synaptic transmission","PubMed.ID":10748068,"subunits.Protein.name.":"Neuronal pentraxin receptor;Neuronal pentraxin-1 ;Neuronal pentraxin-2 ;Reticulocalbin-2","subunits.Gene.name.":"Nptxr;Nptx1;Nptx2;Rcn2","subunits.Gene.name.syn.":"Npr;;Narp;Erc55","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"NP1 and NP2 are secreted, exist as higher order multimers (probably pentamers), and interact with taipoxin and taipoxin-associated calcium-binding protein 49 (TCBP49).  NPR is expressed on the cell membrane and does not bind taipoxin or TCBP49 by itself, but it can form heteropentamers with NP1 and NP2 that can be released from cell membranes.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5209,"ComplexName":"Ubiquilin-proteasome complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P25786;P25787;P60900;Q05086;Q9UHD9;Q9UMX0","subunits.Entrez.IDs.":"5682;5683;5687;7337;29978;29979","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0043161;GO:0006511","GO.description":"proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process","FunCat.ID":"14.13.01.01","FunCat.description":"proteasomal degradation (ubiquitin/proteasomal pathway)","PubMed.ID":10983987,"subunits.Protein.name.":"Proteasome subunit alpha type-1 ;Proteasome subunit alpha type-2 ;Proteasome subunit alpha type-6 ;Ubiquitin-protein ligase E3A ;Ubiquilin-2 ;Ubiquilin-1","subunits.Gene.name.":"PSMA1;PSMA2;PSMA6;UBE3A;UBQLN2;UBQLN1","subunits.Gene.name.syn.":"HC2 NU PROS30 PSC2;HC3 PSC3;PROS27;E6AP EPVE6AP HPVE6A;N4BP4 PLIC2;DA41, PLIC1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5210,"ComplexName":"TANK-TRAF2-TRAF3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q12933;Q13114;Q92844","subunits.Entrez.IDs.":"7186;7187;10010","Protein.complex.purification.method":"MI:0676- tandem affinity purification","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":14743216,"subunits.Protein.name.":"TNF receptor-associated factor 2;TNF receptor-associated factor 3 ;TRAF family member-associated NF-kappa-B activator","subunits.Gene.name.":"TRAF2;TRAF3;TANK","subunits.Gene.name.syn.":"TRAP3;CAP1 CRAF1;ITRAF TRAF2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5211,"ComplexName":"RAF1-PPP2-PIN1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04049;P30153;P62714;P63151;Q13526","subunits.Entrez.IDs.":"5894;5518;5516;5520;5300","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0047- far western blotting","GO.ID":"GO:0007178","GO.description":"transmembrane receptor protein serine/threonine kinase signaling pathway","FunCat.ID":"30.05.01.18","FunCat.description":"transmembrane receptor protein serine/threonine kinase signalling pathways","PubMed.ID":15664191,"subunits.Protein.name.":"RAF proto-oncogene serine/threonine-protein kinase;Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform;Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform;Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform ;Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1","subunits.Gene.name.":"RAF1;PPP2R1A;PPP2CB;PPP2R2A;PIN1","subunits.Gene.name.syn.":"RAF;None;None;;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The Raf-1 kinase is an important signaling molecule, functioning in the Ras pathway to transmit mitogenic, differentiative, and oncogenic signals to the downstream kinases MEK and ERK.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5212,"ComplexName":"Kinase maturation complex 2","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"A7MCY6;P07900;P08238;Q12933;Q16543;Q92844;Q9H6S1;Q9UHD2","subunits.Entrez.IDs.":"9755;3320;3326;7186;11140;10010;64343;29110","Protein.complex.purification.method":"MI:0676- tandem affinity purification","GO.ID":"GO:0035556","GO.description":"intracellular signal transduction","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":14743216,"subunits.Protein.name.":"TANK-binding kinase 1-binding protein 1 ;Heat shock protein HSP 90-alpha;Heat shock protein HSP 90-beta;TNF receptor-associated factor 2;Hsp90 co-chaperone Cdc37;TRAF family member-associated NF-kappa-B activator ;5-azacytidine-induced protein 2 ;Serine/threonine-protein kinase TBK1","subunits.Gene.name.":"TBKBP1;HSP90AA1;HSP90AB1;TRAF2;CDC37;TANK;AZI2;TBK1","subunits.Gene.name.syn.":"KIAA0775 SINTBAD;HSP90A HSPC1 HSPCA;HSP90B HSPC2 HSPCB;TRAP3;CDC37A;ITRAF TRAF2;NAP1 TBKBP2;NAK","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5213,"ComplexName":"Pex26-Pex6-Pex1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells, CHO cells","subunits.UniProt.IDs.":"O43933;Q13608;Q7Z412","subunits.Entrez.IDs.":"5189;5190;55670","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0007031;GO:0005777","GO.description":"peroxisome organization;peroxisome","FunCat.ID":"42.19;70.19","FunCat.description":"peroxisome;peroxisome","PubMed.ID":12717447,"subunits.Protein.name.":"Peroxisome biogenesis factor 1 ;Peroxisome assembly factor 2 ;Peroxisome assembly protein 26","subunits.Gene.name.":"PEX1;PEX6;PEX26","subunits.Gene.name.syn.":";PXAAA1;","Disease.comment":"The complex is involved in peroxisome biogenesis disorders (PBDs), such as Zellweger syndrome and neonatal adrenoleukodystrophy.","Subunits.comment":"None","Complex.comment":"The results indicate that Pex26 anchors Pex6 and Pex1 through Pex26-Pex6 and Pex6-Pex1 interactions.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5215,"ComplexName":"CS-MAP3K7IP1-MAP3K7IP2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75390;Q15750;Q9NYJ8","subunits.Entrez.IDs.":"1431;10454;23118","Protein.complex.purification.method":"MI:0676- tandem affinity purification","GO.ID":"GO:0035556","GO.description":"intracellular signal transduction","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":14743216,"subunits.Protein.name.":"Citrate synthase, mitochondrial ;TGF-beta-activated kinase 1 and MAP3K7-binding protein 1;TGF-beta-activated kinase 1 and MAP3K7-binding protein 2","subunits.Gene.name.":"CS;TAB1;TAB2","subunits.Gene.name.syn.":";MAP3K7IP1;KIAA0733, MAP3K7IP2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5216,"ComplexName":"Casein kinase II (beta-dimer, alpha-dimer)","Organism":"Bovine","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P67868;P68399","subunits.Entrez.IDs.":"539235;282419","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0016055","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;Wnt signaling pathway","FunCat.ID":"14.07.03;30.05.02.20","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;Wnt signalling pathway","PubMed.ID":7768894,"subunits.Protein.name.":"Casein kinase II subunit beta ;Casein kinase II subunit alpha","subunits.Gene.name.":"CSNK2B;CSNK2A1","subunits.Gene.name.syn.":"CK2N;CK2A1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":5217,"ComplexName":"Calreticulin oligomer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P27797","subunits.Entrez.IDs.":"811","Protein.complex.purification.method":"MI:0047- far western blotting; MI:0019- coimmunoprecipitation","GO.ID":"GO:0009408","GO.description":"response to heat","FunCat.ID":"32.01.05","FunCat.description":"heat shock response","PubMed.ID":15383281,"subunits.Protein.name.":"Calreticulin","subunits.Gene.name.":"CALR","subunits.Gene.name.syn.":"CRTC","Disease.comment":"None","Subunits.comment":"The protein complex consists of several  identical subunits (oligomerization).","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":5218,"ComplexName":"Casein kinase II (beta-dimer, alpha, alpha')","Organism":"Bovine","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P20427;P67868;P68399","subunits.Entrez.IDs.":"282420;539235;282419","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0016055","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;Wnt signaling pathway","FunCat.ID":"14.07.03;30.05.02.20","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;Wnt signalling pathway","PubMed.ID":7768894,"subunits.Protein.name.":"Casein kinase II subunit alpha' ;Casein kinase II subunit beta ;Casein kinase II subunit alpha","subunits.Gene.name.":"CSNK2A2;CSNK2B;CSNK2A1","subunits.Gene.name.syn.":";CK2N;CK2A1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":5219,"ComplexName":"Casein kinase II (beta-dimer, alpha'-dimer)","Organism":"Bovine","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P20427;P67868","subunits.Entrez.IDs.":"282420;539235","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0016055","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;Wnt signaling pathway","FunCat.ID":"14.07.03;30.05.02.20","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;Wnt signalling pathway","PubMed.ID":7768894,"subunits.Protein.name.":"Casein kinase II subunit alpha' ;Casein kinase II subunit beta","subunits.Gene.name.":"CSNK2A2;CSNK2B","subunits.Gene.name.syn.":";CK2N","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":5220,"ComplexName":"CHUK-IQGAP2-AKAP8L-RELA-TNIP2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15111;Q04206;Q13576;Q8NFZ5;Q9ULX6","subunits.Entrez.IDs.":"1147;5970;10788;79155;26993","Protein.complex.purification.method":"MI:0676- tandem affinity purification","GO.ID":"GO:0035556","GO.description":"intracellular signal transduction","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":14743216,"subunits.Protein.name.":"Inhibitor of nuclear factor kappa-B kinase subunit alpha;Transcription factor p65;Ras GTPase-activating-like protein IQGAP2;TNFAIP3-interacting protein 2 ;A-kinase anchor protein 8-like","subunits.Gene.name.":"CHUK;RELA;IQGAP2;TNIP2;AKAP8L","subunits.Gene.name.syn.":"IKKA, TCF16;NFKB3;;ABIN2 FLIP1;NAKAP NAKAP95","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5222,"ComplexName":"p14-Mp1-MEK1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"Q02750;Q9UHA4;Q9Y2Q5","subunits.Entrez.IDs.":"5604;8649;28956","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0000165","GO.description":"MAPK cascade","FunCat.ID":"30.01.05.01.03","FunCat.description":"MAPKKK cascade","PubMed.ID":11266467,"subunits.Protein.name.":"Dual specificity mitogen-activated protein kinase kinase 1;Ragulator complex protein LAMTOR3 ;Ragulator complex protein LAMTOR2","subunits.Gene.name.":"MAP2K1;LAMTOR3;LAMTOR2","subunits.Gene.name.syn.":"MEK1, PRKMK1;MAP2K1IP1 MAPKSP1;MAPBPIP ROBLD3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5223,"ComplexName":"Casein kinase II (beta-dimer, alpha'-dimer)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P19784;P67870","subunits.Entrez.IDs.":"1459;1460","Protein.complex.purification.method":"MI:0018- two hybrid","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0016055","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;Wnt signaling pathway","FunCat.ID":"14.07.03;30.05.02.20","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;Wnt signalling pathway","PubMed.ID":7768894,"subunits.Protein.name.":"Casein kinase II subunit alpha' ;Casein kinase II subunit beta","subunits.Gene.name.":"CSNK2A2;CSNK2B","subunits.Gene.name.syn.":"CK2A2;CK2N G5A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5224,"ComplexName":"Casein kinase II (beta-dimer, alpha, alpha')","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P19784;P67870;P68400","subunits.Entrez.IDs.":"1459;1460;1457","Protein.complex.purification.method":"MI:0018- two hybrid","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0016055","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;Wnt signaling pathway","FunCat.ID":"14.07.03;30.05.02.20","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;Wnt signalling pathway","PubMed.ID":7768894,"subunits.Protein.name.":"Casein kinase II subunit alpha' ;Casein kinase II subunit beta ;Casein kinase II subunit alpha","subunits.Gene.name.":"CSNK2A2;CSNK2B;CSNK2A1","subunits.Gene.name.syn.":"CK2A2;CK2N G5A;CK2A1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5225,"ComplexName":"Casein kinase II (beta-dimer, alpha-dimer)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P67870;P68400","subunits.Entrez.IDs.":"1460;1457","Protein.complex.purification.method":"MI:0018- two hybrid","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0016055","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;Wnt signaling pathway","FunCat.ID":"14.07.03;30.05.02.20","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;Wnt signalling pathway","PubMed.ID":7768894,"subunits.Protein.name.":"Casein kinase II subunit beta ;Casein kinase II subunit alpha","subunits.Gene.name.":"CSNK2B;CSNK2A1","subunits.Gene.name.syn.":"CK2N G5A;CK2A1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5226,"ComplexName":"p14-Mp1-ERK2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P28482;Q9UHA4;Q9Y2Q5","subunits.Entrez.IDs.":"5594;8649;28956","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0000165","GO.description":"MAPK cascade","FunCat.ID":"30.01.05.01.03","FunCat.description":"MAPKKK cascade","PubMed.ID":11266467,"subunits.Protein.name.":"Mitogen-activated protein kinase 1;Ragulator complex protein LAMTOR3 ;Ragulator complex protein LAMTOR2","subunits.Gene.name.":"MAPK1;LAMTOR3;LAMTOR2","subunits.Gene.name.syn.":"ERK2, PRKM1, PRKM2;MAP2K1IP1 MAPKSP1;MAPBPIP ROBLD3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5227,"ComplexName":"p14-Mp1-Erk1/2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"EpH4 cells","subunits.UniProt.IDs.":"O88653;P63085;Q63844;Q9JHS3","subunits.Entrez.IDs.":"56692;26413;26417;83409","Protein.complex.purification.method":"MI:0029-cosedimentation through density gradients","GO.ID":"GO:0000165;GO:0005886","GO.description":"MAPK cascade;plasma membrane","FunCat.ID":"30.01.05.01.03;70.02","FunCat.description":"MAPKKK cascade;eukaryotic plasma membrane / membrane attached","PubMed.ID":11266467,"subunits.Protein.name.":"Ragulator complex protein LAMTOR3;Mitogen-activated protein kinase 1;Mitogen-activated protein kinase 3;Ragulator complex protein LAMTOR2","subunits.Gene.name.":"Lamtor3;Mapk1;Mapk3;Lamtor2","subunits.Gene.name.syn.":"Map2k1ip1, Mapbp, Mapksp1;Erk2, Mapk, Prkm1;Erk1, Prkm3;Mapbpip, Robld3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5228,"ComplexName":"REL-MAP3K8-RELA-TNIP2-PAPOLA complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P41279;P51003;Q04206;Q04864;Q8NFZ5","subunits.Entrez.IDs.":"1326;10914;5970;5966;79155","Protein.complex.purification.method":"MI:0676- tandem affinity purification","GO.ID":"GO:0007249","GO.description":"I-kappaB kinase/NF-kappaB signaling","FunCat.ID":"30.01.05.01.04","FunCat.description":"NIK-I-kappaB/NF-kappaB cascade","PubMed.ID":14743216,"subunits.Protein.name.":"Mitogen-activated protein kinase kinase kinase 8 ;Poly;Transcription factor p65;Proto-oncogene c-Rel;TNFAIP3-interacting protein 2","subunits.Gene.name.":"MAP3K8;PAPOLA;RELA;REL;TNIP2","subunits.Gene.name.syn.":"COT ESTF;PAP;NFKB3;;ABIN2 FLIP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5229,"ComplexName":"RPA complex","Organism":"Human","Synonyms":"replication complex","Cell.line":"None","subunits.UniProt.IDs.":"P15927;P27694;P35244","subunits.Entrez.IDs.":"6118;6117;6119","Protein.complex.purification.method":"MI:0091- chromatography technologies; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006260;GO:0003677","GO.description":"DNA replication;DNA binding","FunCat.ID":"10.01.03;16.03.01","FunCat.description":"DNA synthesis and replication;DNA binding","PubMed.ID":2833742,"subunits.Protein.name.":"Replication protein A 32 kDa subunit ;Replication protein A 70 kDa DNA-binding subunit;Replication protein A 14 kDa subunit","subunits.Gene.name.":"RPA2;RPA1;RPA3","subunits.Gene.name.syn.":"REPA2 RPA32 RPA34;REPA1 RPA70;REPA3 RPA14","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"RPA facilitates unwinding of dsDNA.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5230,"ComplexName":"CHUK-NFKB2-REL-IKBKG-SPAG9-NFKB1-NFKBIE-COPB2-TNIP1-NFKBIA-RELA-TNIP2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00221;O15111;O60271;P19838;P25963;P35606;Q00653;Q04206;Q04864;Q15025;Q8NFZ5;Q9Y6K9","subunits.Entrez.IDs.":"4794;1147;9043;4790;4792;9276;4791;5970;5966;10318;79155;8517","Protein.complex.purification.method":"MI:0676- tandem affinity purification","GO.ID":"GO:0007249","GO.description":"I-kappaB kinase/NF-kappaB signaling","FunCat.ID":"30.01.05.01.04","FunCat.description":"NIK-I-kappaB/NF-kappaB cascade","PubMed.ID":14743216,"subunits.Protein.name.":"NF-kappa-B inhibitor epsilon ;Inhibitor of nuclear factor kappa-B kinase subunit alpha;C-Jun-amino-terminal kinase-interacting protein 4 ;Nuclear factor NF-kappa-B p105 subunit;NF-kappa-B inhibitor alpha ;Coatomer subunit beta' ;Nuclear factor NF-kappa-B p100 subunit ;Transcription factor p65;Proto-oncogene c-Rel;TNFAIP3-interacting protein 1;TNFAIP3-interacting protein 2 ;NF-kappa-B essential modulator","subunits.Gene.name.":"NFKBIE;CHUK;SPAG9;NFKB1;NFKBIA;COPB2;NFKB2;RELA;REL;TNIP1;TNIP2;IKBKG","subunits.Gene.name.syn.":"IKBE;IKKA, TCF16;HSS KIAA0516 MAPK8IP4 SYD1;None;IKBA MAD3 NFKBI;;LYT10;NFKB3;;KIAA0113, NAF1;ABIN2 FLIP1;FIP3, NEMO","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5231,"ComplexName":"53BP1-containing complex","Organism":"Human","Synonyms":"53BP1-Ku70-Ku80-RPA1-RPA2 complex","Cell.line":"None","subunits.UniProt.IDs.":"P12956;P13010;P15927;P27694;Q12888","subunits.Entrez.IDs.":"2547;7520;6118;6117;7158","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006281;GO:0003677;GO:0006974","GO.description":"DNA repair;DNA binding;cellular response to DNA damage stimulus","FunCat.ID":"10.01.05.01;16.03.01;32.01.09","FunCat.description":"DNA repair;DNA binding;DNA damage response","PubMed.ID":15856006,"subunits.Protein.name.":"X-ray repair cross-complementing protein 6 ;X-ray repair cross-complementing protein 5 ;Replication protein A 32 kDa subunit ;Replication protein A 70 kDa DNA-binding subunit;Tumor suppressor p53-binding protein 1","subunits.Gene.name.":"XRCC6;XRCC5;RPA2;RPA1;TP53BP1","subunits.Gene.name.syn.":"G22P1;G22P2;REPA2 RPA32 RPA34;REPA1 RPA70;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"53BP1 is involved in DNA damage-induced RPA2 phosphorylation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5232,"ComplexName":"TNF-alpha/Nf-kappa B signaling complex (RPL6, RPL30, RPS13, CHUK, DDX3X, NFKB2, NFKBIB, REL, IKBKG, NFKB1, MAP3K8, RELB, GLG1, NFKBIA, RELA, TNIP2,  GTF2I)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00571;O15111;P19838;P25963;P41279;P62277;P62888;P78347;Q00653;Q01201;Q02878;Q04206;Q04864;Q15653;Q8NFZ5;Q92896;Q9Y6K9","subunits.Entrez.IDs.":"1654;1147;4790;4792;1326;6207;6156;2969;4791;5971;6128;5970;5966;4793;79155;2734;8517","Protein.complex.purification.method":"MI:0676- tandem affinity purification","GO.ID":"GO:0007249;GO:0005125","GO.description":"I-kappaB kinase/NF-kappaB signaling;cytokine activity","FunCat.ID":"30.01.05.01.04;40.02.03.01","FunCat.description":"NIK-I-kappaB/NF-kappaB cascade;cytokines (interleukines, colony stimulating factors, etc.)","PubMed.ID":14743216,"subunits.Protein.name.":"ATP-dependent RNA helicase DDX3X ;Inhibitor of nuclear factor kappa-B kinase subunit alpha;Nuclear factor NF-kappa-B p105 subunit;NF-kappa-B inhibitor alpha ;Mitogen-activated protein kinase kinase kinase 8 ;40S ribosomal protein S13;60S ribosomal protein L30;General transcription factor II-I;Nuclear factor NF-kappa-B p100 subunit ;Transcription factor RelB;60S ribosomal protein L6;Transcription factor p65;Proto-oncogene c-Rel;NF-kappa-B inhibitor beta ;TNFAIP3-interacting protein 2 ;Golgi apparatus protein 1 ;NF-kappa-B essential modulator","subunits.Gene.name.":"DDX3X;CHUK;NFKB1;NFKBIA;MAP3K8;RPS13;RPL30;GTF2I;NFKB2;RELB;RPL6;RELA;REL;NFKBIB;TNIP2;GLG1;IKBKG","subunits.Gene.name.syn.":"DBX DDX3;IKKA, TCF16;None;IKBA MAD3 NFKBI;COT ESTF;None;None;BAP135 WBSCR6;LYT10;None;TXREB1;NFKB3;;IKBB TRIP9;ABIN2 FLIP1;CFR1 ESL1 MG160;FIP3, NEMO","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5233,"ComplexName":"TNF-alpha/NF-kappa B signaling complex 5","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14920;O15111;O15446;O95602;P19838;P23508;P42704;P46199;P52292;P52434;P62875;P63208;Q00653;Q04206;Q04864;Q13576;Q13616;Q15653;Q16342;Q9GZS1;Q9H9Y6;Q9UJF2;Q9UKB1;Q9Y2S0;Q9Y6K9","subunits.Entrez.IDs.":"3551;1147;10849;25885;4790;4163;10128;4528;3838;5437;5441;6500;4791;5970;5966;10788;8454;4793;5134;64425;84172;9462;23291;51082;8517","Protein.complex.purification.method":"MI:0676- tandem affinity purification","GO.ID":"GO:0007249;GO:0005125","GO.description":"I-kappaB kinase/NF-kappaB signaling;cytokine activity","FunCat.ID":"30.01.05.01.04;40.02.03.01","FunCat.description":"NIK-I-kappaB/NF-kappaB cascade;cytokines (interleukines, colony stimulating factors, etc.)","PubMed.ID":14743216,"subunits.Protein.name.":"Inhibitor of nuclear factor kappa-B kinase subunit beta;Inhibitor of nuclear factor kappa-B kinase subunit alpha;DNA-directed RNA polymerase I subunit RPA34 ;DNA-directed RNA polymerase I subunit RPA1 ;Nuclear factor NF-kappa-B p105 subunit;Colorectal mutant cancer protein ;Leucine-rich PPR motif-containing protein, mitochondrial ;Translation initiation factor IF-2, mitochondrial ;Importin subunit alpha-1;DNA-directed RNA polymerases I, II, and III subunit RPABC3 ;DNA-directed RNA polymerases I, II, and III subunit RPABC5 ;S-phase kinase-associated protein 1;Nuclear factor NF-kappa-B p100 subunit ;Transcription factor p65;Proto-oncogene c-Rel;Ras GTPase-activating-like protein IQGAP2;Cullin-1;NF-kappa-B inhibitor beta ;Programmed cell death protein 2 ;DNA-directed RNA polymerase I subunit RPA49 ;DNA-directed RNA polymerase I subunit RPA2 ;Ras GTPase-activating protein nGAP ;F-box/WD repeat-containing protein 11 ;DNA-directed RNA polymerases I and III subunit RPAC2 ;NF-kappa-B essential modulator","subunits.Gene.name.":"IKBKB;CHUK;CD3EAP;POLR1A;NFKB1;MCC;LRPPRC;MTIF2;KPNA2;POLR2H;POLR2L;SKP1;NFKB2;RELA;REL;IQGAP2;CUL1;NFKBIB;PDCD2;POLR1E;POLR1B;RASAL2;FBXW11;POLR1D;IKBKG","subunits.Gene.name.syn.":"IKKB;IKKA, TCF16;ASE1 CAST PAF49;;None;;LRP130;;RCH1, SRP1;;;EMC19, OCP2, SKP1A, TCEB1L;LYT10;NFKB3;;;None;IKBB TRIP9;RP8 ZMYND7;PAF53 PRAF1;;NGAP;BTRCP2 FBW1B FBXW1B KIAA0696;;FIP3, NEMO","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5234,"ComplexName":"IKBKB-CDC37-KIAA1967-HSP90AB1-HSP90AA1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14920;P07900;P08238;Q16543;Q8N163","subunits.Entrez.IDs.":"3551;3320;3326;11140;57805","Protein.complex.purification.method":"MI:0676- tandem affinity purification","GO.ID":"GO:0007249","GO.description":"I-kappaB kinase/NF-kappaB signaling","FunCat.ID":"30.01.05.01.04","FunCat.description":"NIK-I-kappaB/NF-kappaB cascade","PubMed.ID":14743216,"subunits.Protein.name.":"Inhibitor of nuclear factor kappa-B kinase subunit beta;Heat shock protein HSP 90-alpha;Heat shock protein HSP 90-beta;Hsp90 co-chaperone Cdc37;Cell cycle and apoptosis regulator protein 2","subunits.Gene.name.":"IKBKB;HSP90AA1;HSP90AB1;CDC37;CCAR2","subunits.Gene.name.syn.":"IKKB;HSP90A HSPC1 HSPCA;HSP90B HSPC2 HSPCB;CDC37A;DBC1 KIAA1967","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5235,"ComplexName":"WRN-Ku70-Ku80-PARP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"P09874;P12956;P13010;Q14191","subunits.Entrez.IDs.":"142;2547;7520;7486","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation; MI:0226- ion exchange chromatography; MI:0071- molecular sieving","GO.ID":"GO:0003677;GO:0006974;GO:0005634","GO.description":"DNA binding;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"16.03.01;32.01.09;70.10","FunCat.description":"DNA binding;DNA damage response;nucleus","PubMed.ID":14734561,"subunits.Protein.name.":"Poly [ADP-ribose] polymerase 1;X-ray repair cross-complementing protein 6 ;X-ray repair cross-complementing protein 5 ;Werner syndrome ATP-dependent helicase","subunits.Gene.name.":"PARP1;XRCC6;XRCC5;WRN","subunits.Gene.name.syn.":"ADPRT PPOL;G22P1;G22P2;RECQ3 RECQL2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"PARP1 regulates the exonucleolytic activity of WRN.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5237,"ComplexName":"c-Myc-Max-Arf complex","Organism":"Mouse","Synonyms":"None","Cell.line":"COS-7 cells","subunits.UniProt.IDs.":"P01108;P28574;Q64364","subunits.Entrez.IDs.":"17869;17187;12578","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;nucleus","FunCat.ID":"11.02.03.04;70.10","FunCat.description":"transcriptional control;nucleus","PubMed.ID":15361884,"subunits.Protein.name.":"Myc proto-oncogene protein ;Protein max ;Tumor suppressor ARF","subunits.Gene.name.":"Myc;Max;Cdkn2a","subunits.Gene.name.syn.":";Myn;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5239,"ComplexName":"CAP(C)-CAP(E) complex","Organism":"Human","Synonyms":"SMC2-SMC4 complex","Cell.line":"None","subunits.UniProt.IDs.":"O95347;Q9NTJ3","subunits.Entrez.IDs.":"10592;10051","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0000279;GO:0007067;GO:0030261;GO:0005634","GO.description":"M phase;mitotic nuclear division;chromosome condensation;nucleus","FunCat.ID":"10.03.01.01.11;10.03.04.03;70.10","FunCat.description":"M phase;chromosome condensation;nucleus","PubMed.ID":9789013,"subunits.Protein.name.":"Structural maintenance of chromosomes protein 2 ;Structural maintenance of chromosomes protein 4","subunits.Gene.name.":"SMC2;SMC4","subunits.Gene.name.syn.":"CAPE SMC2L1;CAPC SMC4L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"CAP(C)-CAP(E) complex is required for mitotic chromosome condensation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5241,"ComplexName":"SMC1-SMC3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q14683;Q9UQE7","subunits.Entrez.IDs.":"8243;9126","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0000279;GO:0007067;GO:0005634","GO.description":"M phase;mitotic nuclear division;nucleus","FunCat.ID":"10.03.01.01.11;70.10","FunCat.description":"M phase;nucleus","PubMed.ID":9789013,"subunits.Protein.name.":"Structural maintenance of chromosomes protein 1A ;Structural maintenance of chromosomes protein 3","subunits.Gene.name.":"SMC1A;SMC3","subunits.Gene.name.syn.":"DXS423E KIAA0178 SB1.8 SMC1 SMC1L1;BAM BMH CSPG6 SMC3L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SMC1-SMC3 complex is required for metaphase progression in mitotic cells.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5243,"ComplexName":"XRCC1-LIG3-PNK-TDP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P18887;P49916;Q96T60;Q9NUW8","subunits.Entrez.IDs.":"7515;3980;11284;55775","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006281","GO.description":"DNA repair","FunCat.ID":"10.01.05.01","FunCat.description":"DNA repair","PubMed.ID":15744309,"subunits.Protein.name.":"DNA repair protein XRCC1 ;DNA ligase 3 ;Bifunctional polynucleotide phosphatase/kinase ;Tyrosyl-DNA phosphodiesterase 1","subunits.Gene.name.":"XRCC1;LIG3;PNKP;TDP1","subunits.Gene.name.syn.":";;;","Disease.comment":"TDP1 is involved in Spinocerebellar ataxia with axonal neuropathy (SCAN1).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5244,"ComplexName":"Dolichol-phosphate mannose (DPM) synthase","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60762;O94777;Q9P2X0","subunits.Entrez.IDs.":"8813;8818;54344","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006486;GO:0042125;GO:0005783","GO.description":"protein glycosylation;protein galactosylation;endoplasmic reticulum","FunCat.ID":"14.07.02;70.07","FunCat.description":"modification with sugar residues (e.g. glycosylation, deglycosylation);endoplasmic reticulum","PubMed.ID":10835346,"subunits.Protein.name.":"Dolichol-phosphate mannosyltransferase subunit 1 ;Dolichol phosphate-mannose biosynthesis regulatory protein ;Dolichol-phosphate mannosyltransferase subunit 3","subunits.Gene.name.":"DPM1;DPM2;DPM3","subunits.Gene.name.syn.":";;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results indicate that DPM2 stabilizes DPM3 and DPM3 stabilizes DPM1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5248,"ComplexName":"Iqgap1-Cdc42-Ctnnb1-Cdh2 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q8CFN2;Q9JKF1;Q9WU82;Q9Z1Y3","subunits.Entrez.IDs.":"64465;29875;84353;83501","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0045216;GO:0007043;GO:0005911","GO.description":"cell-cell junction organization;cell-cell junction assembly;cell-cell junction","FunCat.ID":"42.06.04;70.06.04","FunCat.description":"intercellular junction (gap junction/adherens junction);intercellular junction (gap junction/adherens junction)","PubMed.ID":15389538,"subunits.Protein.name.":"Cell division control protein 42 homolog;Ras GTPase-activating-like protein IQGAP1;Catenin beta-1;Cadherin-2","subunits.Gene.name.":"Cdc42;Iqgap1;Ctnnb1;Cdh2","subunits.Gene.name.syn.":";;Catnb;None","Disease.comment":"None","Subunits.comment":"Since Iqgap1 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Mus musculus (Mouse);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5249,"ComplexName":"Iqgap1-Cdh1-Ctnnb1-Cdh2 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q9JKF1;Q9R0T4;Q9WU82;Q9Z1Y3","subunits.Entrez.IDs.":"29875;83502;84353;83501","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0045216;GO:0007043;GO:0005911","GO.description":"cell-cell junction organization;cell-cell junction assembly;cell-cell junction","FunCat.ID":"42.06.04;70.06.04","FunCat.description":"intercellular junction (gap junction/adherens junction);intercellular junction (gap junction/adherens junction)","PubMed.ID":15389538,"subunits.Protein.name.":"Ras GTPase-activating-like protein IQGAP1;Cadherin-1 ;Catenin beta-1;Cadherin-2","subunits.Gene.name.":"Iqgap1;Cdh1;Ctnnb1;Cdh2","subunits.Gene.name.syn.":";;Catnb;None","Disease.comment":"None","Subunits.comment":"Since Iqgap1 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5250,"ComplexName":"Iqgap1-Actb-Vim complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P31000;P60711;Q9JKF1","subunits.Entrez.IDs.":"81818;81822;29875","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0045216;GO:0007043;GO:0005911","GO.description":"cell-cell junction organization;cell-cell junction assembly;cell-cell junction","FunCat.ID":"42.06.04;70.06.04","FunCat.description":"intercellular junction (gap junction/adherens junction);intercellular junction (gap junction/adherens junction)","PubMed.ID":15389538,"subunits.Protein.name.":"Vimentin;Actin, cytoplasmic 1;Ras GTPase-activating-like protein IQGAP1","subunits.Gene.name.":"Vim;Actb;Iqgap1","subunits.Gene.name.syn.":";None;","Disease.comment":"None","Subunits.comment":"Since Iqgap1 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Mus musculus (Mouse)"}
{"ComplexID":5251,"ComplexName":"Ku-ORC complex","Organism":"Human","Synonyms":"None","Cell.line":"HCT116 cells","subunits.UniProt.IDs.":"O43929;P12956;P13010;Q13416;Q9UBD5;Q9Y5N6","subunits.Entrez.IDs.":"5000;2547;7520;4999;23595;23594","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0402- chromatin immunoprecipitation assays","GO.ID":"GO:0006267;GO:0003688;GO:0003677;GO:0005524;GO:0005694","GO.description":"pre-replicative complex assembly involved in nuclear cell cycle DNA replication;DNA replication origin binding;DNA binding;ATP binding;chromosome","FunCat.ID":"10.01.03.03;16.03.01;16.19.03;70.10.03","FunCat.description":"ori recognition and priming complex formation;DNA binding;ATP binding;chromosome","PubMed.ID":15910003,"subunits.Protein.name.":"Origin recognition complex subunit 4;X-ray repair cross-complementing protein 6 ;X-ray repair cross-complementing protein 5 ;Origin recognition complex subunit 2;Origin recognition complex subunit 3 ;Origin recognition complex subunit 6","subunits.Gene.name.":"ORC4;XRCC6;XRCC5;ORC2;ORC3;ORC6","subunits.Gene.name.syn.":"ORC4L;G22P1;G22P2;ORC2L;LATHEO ORC3L;ORC6L","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Ku associates specifically with DNA replication origins in vivo in a cell cycle dependent manner, its association being maximal in late G1 phase and decreasing as cells enter S phase (PMID:11694575).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5252,"ComplexName":"Htt-Dctn1-Hap1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O08788;O35668;P42859","subunits.Entrez.IDs.":"13191;15114;15194","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0016192;GO:0030705;GO:0015630","GO.description":"vesicle-mediated transport;cytoskeleton-dependent intracellular transport;microtubule cytoskeleton","FunCat.ID":"20.09.07;20.09.14;70.04.05","FunCat.description":"vesicular transport (Golgi network, etc.);cytoskeleton-dependent transport;microtubule cytoskeleton","PubMed.ID":15242649,"subunits.Protein.name.":"Dynactin subunit 1;Huntingtin-associated protein 1 ;Huntingtin","subunits.Gene.name.":"Dctn1;Hap1;Htt","subunits.Gene.name.syn.":"None;;Hd Hdh","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors demonstrate that htt is a processivity factor that increases the transport efficiency of BDNF-containing vesicles along MTs. The alteration of the huntingtin/HAP1/p150(Glued) complex correlates with reduced association of motor proteins with microtubules.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5253,"ComplexName":"MNK1-eIF4F complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"P06730;P60842;Q04637;Q9BUB5","subunits.Entrez.IDs.":"1977;1973;1981;8569","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0006413;GO:0003723","GO.description":"translational initiation;RNA binding","FunCat.ID":"12.04.01;16.03.03","FunCat.description":"translation initiation;RNA binding","PubMed.ID":9878069,"subunits.Protein.name.":"Eukaryotic translation initiation factor 4E;Eukaryotic initiation factor 4A-I;Eukaryotic translation initiation factor 4 gamma 1;MAP kinase-interacting serine/threonine-protein kinase 1","subunits.Gene.name.":"EIF4E;EIF4A1;EIF4G1;MKNK1","subunits.Gene.name.syn.":"EIF4EL1 EIF4F;DDX2A EIF4A;EIF4F EIF4G EIF4GI;MNK1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Mnk1 is associated with the eIF4F complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5260,"ComplexName":"TCF4-CTNNB1-SUMO1-EP300-HADAC6 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P15884;P35222;P63165;Q09472;Q9UBN7","subunits.Entrez.IDs.":"6925;1499;7341;2033;10013","Protein.complex.purification.method":"MI:0225- chromatin immunoprecipitation array","GO.ID":"GO:0006351","GO.description":"transcription, DNA-templated","FunCat.ID":"11","FunCat.description":"TRANSCRIPTION","PubMed.ID":15782138,"subunits.Protein.name.":"Transcription factor 4 ;Catenin beta-1;Small ubiquitin-related modifier 1 ;Histone acetyltransferase p300;Histone deacetylase 6","subunits.Gene.name.":"TCF4;CTNNB1;SUMO1;EP300;HDAC6","subunits.Gene.name.syn.":"BHLHB19 ITF2 SEF2;CTNNB;SMT3C SMT3H3 UBL1;P300;KIAA0901","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5261,"ComplexName":"TCF4-CTNNB1-EP300 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P15884;P35222;Q09472","subunits.Entrez.IDs.":"6925;1499;2033","Protein.complex.purification.method":"MI:0225- chromatin immunoprecipitation array","GO.ID":"GO:0006351","GO.description":"transcription, DNA-templated","FunCat.ID":"11","FunCat.description":"TRANSCRIPTION","PubMed.ID":15782138,"subunits.Protein.name.":"Transcription factor 4 ;Catenin beta-1;Histone acetyltransferase p300","subunits.Gene.name.":"TCF4;CTNNB1;EP300","subunits.Gene.name.syn.":"BHLHB19 ITF2 SEF2;CTNNB;P300","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5262,"ComplexName":"TCF4-CTNNB1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P15884;P35222","subunits.Entrez.IDs.":"6925;1499","Protein.complex.purification.method":"MI:0225- chromatin immunoprecipitation array","GO.ID":"GO:0006351","GO.description":"transcription, DNA-templated","FunCat.ID":"11","FunCat.description":"TRANSCRIPTION","PubMed.ID":15782138,"subunits.Protein.name.":"Transcription factor 4 ;Catenin beta-1","subunits.Gene.name.":"TCF4;CTNNB1","subunits.Gene.name.syn.":"BHLHB19 ITF2 SEF2;CTNNB","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5264,"ComplexName":"TCF4-CTNNB1-CREBBP complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P15884;P35222;Q92793","subunits.Entrez.IDs.":"6925;1499;1387","Protein.complex.purification.method":"MI:0225- chromatin immunoprecipitation array","GO.ID":"GO:0006351","GO.description":"transcription, DNA-templated","FunCat.ID":"11","FunCat.description":"TRANSCRIPTION","PubMed.ID":15782138,"subunits.Protein.name.":"Transcription factor 4 ;Catenin beta-1;CREB-binding protein","subunits.Gene.name.":"TCF4;CTNNB1;CREBBP","subunits.Gene.name.syn.":"BHLHB19 ITF2 SEF2;CTNNB;CBP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5266,"ComplexName":"TNF-alpha/NF-kappa B signaling complex 6","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14920;O15111;P07900;P08238;P22087;P36578;P62277;P62280;P62888;P62917;Q02878;Q16543;Q99558;Q9Y6K9","subunits.Entrez.IDs.":"3551;1147;3320;3326;2091;6124;6207;6205;6156;6132;6128;11140;9020;8517","Protein.complex.purification.method":"MI:0676- tandem affinity purification","GO.ID":"GO:0007249;GO:0005125","GO.description":"I-kappaB kinase/NF-kappaB signaling;cytokine activity","FunCat.ID":"30.01.05.01.04;40.02.03.01","FunCat.description":"NIK-I-kappaB/NF-kappaB cascade;cytokines (interleukines, colony stimulating factors, etc.)","PubMed.ID":14743216,"subunits.Protein.name.":"Inhibitor of nuclear factor kappa-B kinase subunit beta;Inhibitor of nuclear factor kappa-B kinase subunit alpha;Heat shock protein HSP 90-alpha;Heat shock protein HSP 90-beta;rRNA 2'-O-methyltransferase fibrillarin;60S ribosomal protein L4;40S ribosomal protein S13;40S ribosomal protein S11;60S ribosomal protein L30;60S ribosomal protein L8;60S ribosomal protein L6;Hsp90 co-chaperone Cdc37;Mitogen-activated protein kinase kinase kinase 14 ;NF-kappa-B essential modulator","subunits.Gene.name.":"IKBKB;CHUK;HSP90AA1;HSP90AB1;FBL;RPL4;RPS13;RPS11;RPL30;RPL8;RPL6;CDC37;MAP3K14;IKBKG","subunits.Gene.name.syn.":"IKKB;IKKA, TCF16;HSP90A HSPC1 HSPCA;HSP90B HSPC2 HSPCB;FIB1 FLRN;RPL1;None;None;None;None;TXREB1;CDC37A;NIK;FIP3, NEMO","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5267,"ComplexName":"VHL-VDU1-TCEB1-TCEB2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P40337;Q15369;Q15370;Q8TEY7","subunits.Entrez.IDs.":"7428;6921;6923;23032","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0043161;GO:0006511","GO.description":"proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process","FunCat.ID":"14.13.01.01","FunCat.description":"proteasomal degradation (ubiquitin/proteasomal pathway)","PubMed.ID":11739384,"subunits.Protein.name.":"Von Hippel-Lindau disease tumor suppressor;Transcription elongation factor B polypeptide 1;Transcription elongation factor B polypeptide 2;Ubiquitin carboxyl-terminal hydrolase 33","subunits.Gene.name.":"VHL;TCEB1;TCEB2;USP33","subunits.Gene.name.syn.":"None;elongin c;elongin b;KIAA1097 VDU1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Only in the presence of VHL, VDU1 could be precipitated along with VHL, Elongin B and Elongin C.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5268,"ComplexName":"TNF-alpha/NF-kappa B signaling complex 7","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43318;P07900;P08238;Q13451;Q15750;Q16543;Q8N5C8;Q9NYJ8","subunits.Entrez.IDs.":"6885;3320;3326;2289;10454;11140;257397;23118","Protein.complex.purification.method":"MI:0676- tandem affinity purification","GO.ID":"GO:0007249;GO:0005125","GO.description":"I-kappaB kinase/NF-kappaB signaling;cytokine activity","FunCat.ID":"30.01.05.01.04;40.02.03.01","FunCat.description":"NIK-I-kappaB/NF-kappaB cascade;cytokines (interleukines, colony stimulating factors, etc.)","PubMed.ID":14743216,"subunits.Protein.name.":"Mitogen-activated protein kinase kinase kinase 7;Heat shock protein HSP 90-alpha;Heat shock protein HSP 90-beta;Peptidyl-prolyl cis-trans isomerase FKBP5 ;TGF-beta-activated kinase 1 and MAP3K7-binding protein 1;Hsp90 co-chaperone Cdc37;TGF-beta-activated kinase 1 and MAP3K7-binding protein 3 ;TGF-beta-activated kinase 1 and MAP3K7-binding protein 2","subunits.Gene.name.":"MAP3K7;HSP90AA1;HSP90AB1;FKBP5;TAB1;CDC37;TAB3;TAB2","subunits.Gene.name.syn.":"TAK1;HSP90A HSPC1 HSPCA;HSP90B HSPC2 HSPCB;AIG6 FKBP51;MAP3K7IP1;CDC37A;MAP3K7IP3;KIAA0733, MAP3K7IP2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5269,"ComplexName":"TNF-alpha/NF-kappa B signaling complex 8","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P07900;P08238;Q13451;Q14164;Q16543;Q86UP2","subunits.Entrez.IDs.":"3320;3326;2289;9641;11140;3895","Protein.complex.purification.method":"MI:0676- tandem affinity purification","GO.ID":"GO:0007249;GO:0005125","GO.description":"I-kappaB kinase/NF-kappaB signaling;cytokine activity","FunCat.ID":"30.01.05.01.04;40.02.03.01","FunCat.description":"NIK-I-kappaB/NF-kappaB cascade;cytokines (interleukines, colony stimulating factors, etc.)","PubMed.ID":14743216,"subunits.Protein.name.":"Heat shock protein HSP 90-alpha;Heat shock protein HSP 90-beta;Peptidyl-prolyl cis-trans isomerase FKBP5 ;Inhibitor of nuclear factor kappa-B kinase subunit epsilon ;Hsp90 co-chaperone Cdc37;Kinectin","subunits.Gene.name.":"HSP90AA1;HSP90AB1;FKBP5;IKBKE;CDC37;KTN1","subunits.Gene.name.syn.":"HSP90A HSPC1 HSPCA;HSP90B HSPC2 HSPCB;AIG6 FKBP51;IKKE IKKI KIAA0151;CDC37A;CG1 KIAA0004","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5270,"ComplexName":"VHL-TCEB1-TCEB2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P40337;Q15369;Q15370","subunits.Entrez.IDs.":"7428;6921;6923","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0043161;GO:0006511","GO.description":"proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process","FunCat.ID":"14.13.01.01","FunCat.description":"proteasomal degradation (ubiquitin/proteasomal pathway)","PubMed.ID":11739384,"subunits.Protein.name.":"Von Hippel-Lindau disease tumor suppressor;Transcription elongation factor B polypeptide 1;Transcription elongation factor B polypeptide 2","subunits.Gene.name.":"VHL;TCEB1;TCEB2","subunits.Gene.name.syn.":"None;elongin c;elongin b","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5271,"ComplexName":"Kif3-cadherin-catenin complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P15116;P30999;P70188;Q02248;Q61771","subunits.Entrez.IDs.":"12558;12388;16579;12387;16569","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007420","GO.description":"brain development","FunCat.ID":"47.03.01.01.01","FunCat.description":"brain","PubMed.ID":15834408,"subunits.Protein.name.":"Cadherin-2;Catenin delta-1;Kinesin-associated protein 3;Catenin beta-1;Kinesin-like protein KIF3B","subunits.Gene.name.":"Cdh2;Ctnnd1;Kifap3;Ctnnb1;Kif3b","subunits.Gene.name.syn.":"None;Catns Kiaa0384;Kap3;Catnb;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5273,"ComplexName":"VHL-TBP1-HIF1A complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells, RCC4-VHL cells","subunits.UniProt.IDs.":"P17980;P40337;Q16665","subunits.Entrez.IDs.":"5702;7428;3091","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0043161;GO:0006511;GO:0000302;GO:0006979","GO.description":"proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;response to reactive oxygen species;response to oxidative stress","FunCat.ID":"14.13.01.01;32.01.01","FunCat.description":"proteasomal degradation (ubiquitin/proteasomal pathway);oxidative stress response","PubMed.ID":14556007,"subunits.Protein.name.":"26S protease regulatory subunit 6A ;Von Hippel-Lindau disease tumor suppressor;Hypoxia-inducible factor 1-alpha","subunits.Gene.name.":"PSMC3;VHL;HIF1A","subunits.Gene.name.syn.":"TBP1;None;BHLHE78 MOP1 PASD8","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TBP-1 associates with the beta-domain of VHL and complexes with VHL and Hif1-alpha in vivo. The ability of VHL to degrade Hif1-alpha depends in part on its interaction with TBP-1 and suggests a new mechanism for Hif1-alpha stabilization in some VHL-deficient tumors.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5274,"ComplexName":"Cell-cell junction complex (ARHGAP10-CTNNA1)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"A1A4S6;P35221","subunits.Entrez.IDs.":"79658;1495","Protein.complex.purification.method":"MI:0018- two hybrid","GO.ID":"GO:0007043","GO.description":"cell-cell junction assembly","FunCat.ID":"42.06.04","FunCat.description":"intercellular junction (gap junction/adherens junction)","PubMed.ID":16184169,"subunits.Protein.name.":"Rho GTPase-activating protein 10 ;Catenin alpha-1","subunits.Gene.name.":"ARHGAP10;CTNNA1","subunits.Gene.name.syn.":"GRAF2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"ARHGAP10 is a new component of cell-cell junctions that controls alpha-catenin recruitment and has a key role during L. monocytogenes uptake.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5276,"ComplexName":"HIF1A-OS9-EGLN1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"Q13438;Q16665;Q9GZT9","subunits.Entrez.IDs.":"10956;3091;54583","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0000302;GO:0006979","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;response to reactive oxygen species;response to oxidative stress","FunCat.ID":"11.02.03.04;32.01.01","FunCat.description":"transcriptional control;oxidative stress response","PubMed.ID":15721254,"subunits.Protein.name.":"Protein OS-9 ;Hypoxia-inducible factor 1-alpha;Egl nine homolog 1","subunits.Gene.name.":"OS9;HIF1A;EGLN1","subunits.Gene.name.syn.":";BHLHE78 MOP1 PASD8;C1orf12","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results indicate that OS-9 and PHD2 bind to different regions of HIF-1-alpha, and therefore may bind simultaneously. The results show enhanced binding of PHD2 to V5-OS-9  in the presence of HIF-1-alpha.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5277,"ComplexName":"HIF1A-OS9-EGLN3 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"Q13438;Q16665;Q9H6Z9","subunits.Entrez.IDs.":"10956;3091;112399","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:2001141;GO:0006355;GO:0000302;GO:0006979","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;response to reactive oxygen species;response to oxidative stress","FunCat.ID":"11.02.03.04;32.01.01","FunCat.description":"transcriptional control;oxidative stress response","PubMed.ID":15721254,"subunits.Protein.name.":"Protein OS-9 ;Hypoxia-inducible factor 1-alpha;Egl nine homolog 3","subunits.Gene.name.":"OS9;HIF1A;EGLN3","subunits.Gene.name.syn.":";BHLHE78 MOP1 PASD8;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Similar to its effect on PHD2, OS-9 stimulates the binding of PHD3 to HIF-1-alpha and cooperates with PHD3 to inhibit HIF-1 transcriptional activity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5280,"ComplexName":"RAB9-TIP47-MPRI complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60664;P11717;P51151","subunits.Entrez.IDs.":"10226;3482;9367","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0016192","GO.description":"intracellular protein transport;protein targeting;protein transport;vesicle-mediated transport","FunCat.ID":"14.04;20.01.10;20.09.07","FunCat.description":"protein targeting, sorting and translocation;protein transport;vesicular transport (Golgi network, etc.)","PubMed.ID":11359012,"subunits.Protein.name.":"Perilipin-3 ;Cation-independent mannose-6-phosphate receptor ;Ras-related protein Rab-9A","subunits.Gene.name.":"PLIN3;IGF2R;RAB9A","subunits.Gene.name.syn.":"M6PRBP1 TIP47;MPRI;RAB9","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Rab9 bound to immobilized CI-MPR only in the presence of TIP47 in a concentration-dependent manner. Thus TIP47 formed a ternary complex linking the CI-MPR and Rab9.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5281,"ComplexName":"Cell-cell junction complex (CDH1-CTNNB1)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12830;P35222","subunits.Entrez.IDs.":"999;1499","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0023052;GO:0007043","GO.description":"signaling;cell-cell junction assembly","FunCat.ID":"30.01;42.06.04","FunCat.description":"cellular signalling;intercellular junction (gap junction/adherens junction)","PubMed.ID":16184169,"subunits.Protein.name.":"Cadherin-1;Catenin beta-1","subunits.Gene.name.":"CDH1;CTNNB1","subunits.Gene.name.syn.":"CDHE UVO;CTNNB","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5282,"ComplexName":"CAS-SRC-FAK complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12931;P56945;Q05397","subunits.Entrez.IDs.":"6714;9564;5747","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007169","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway","FunCat.ID":"30.05.01.12","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways","PubMed.ID":9148935,"subunits.Protein.name.":"Proto-oncogene tyrosine-protein kinase Src;Breast cancer anti-estrogen resistance protein 1;Focal adhesion kinase 1","subunits.Gene.name.":"SRC;BCAR1;PTK2","subunits.Gene.name.syn.":"SRC1;CAS CASS1 CRKAS;FAK FAK1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5283,"ComplexName":"tRNA splicing endonuclease","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q7Z6J9;Q8NCE0;Q8WW01;Q92989;Q9BSV6","subunits.Entrez.IDs.":"283989;80746;116461;10978;79042","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0008033;GO:0000398;GO:0006397;GO:0005634","GO.description":"tRNA processing;mRNA splicing, via spliceosome;mRNA processing;nucleus","FunCat.ID":"11.04.02;11.04.03;70.10","FunCat.description":"tRNA processing;mRNA processing (splicing, 5'-, 3'-end processing);nucleus","PubMed.ID":15109492,"subunits.Protein.name.":"tRNA-splicing endonuclease subunit Sen54 ;tRNA-splicing endonuclease subunit Sen2 ;tRNA-splicing endonuclease subunit Sen15 ;Polyribonucleotide 5'-hydroxyl-kinase Clp1 ;tRNA-splicing endonuclease subunit Sen34","subunits.Gene.name.":"TSEN54;TSEN2;TSEN15;CLP1;TSEN34","subunits.Gene.name.syn.":"SEN54;SEN2;C1orf19 SEN15;HEAB;LENG5 SEN34","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5284,"ComplexName":"RNA endonuclease (SEN2deltaEx8, SEN54, CLP1)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q7Z6J9;Q8NCE0;Q92989","subunits.Entrez.IDs.":"283989;80746;10978","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006396","GO.description":"RNA processing","FunCat.ID":"11.04","FunCat.description":"RNA processing","PubMed.ID":15109492,"subunits.Protein.name.":"tRNA-splicing endonuclease subunit Sen54 ;tRNA-splicing endonuclease subunit Sen2 ;Polyribonucleotide 5'-hydroxyl-kinase Clp1","subunits.Gene.name.":"TSEN54;TSEN2;CLP1","subunits.Gene.name.syn.":"SEN54;SEN2;HEAB","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TSEN2 is an alternatively spliced gene. SEN2deltaEx8 is the variant lacking exon 8. The complex formed with variant SEN2deltaEx8 does not properly cleave pre-tRNAs, although it does retain endonucleolytic activity. It is likely that the SEN2deltaEx8-containing complex is not a tRNA splicing endonuclease but is responsible for processing as yet unknown RNA substrates.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5285,"ComplexName":"TNF-alpha/NF-kappa B signaling complex 9","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15111;P08238;Q13451;Q15653;Q16543","subunits.Entrez.IDs.":"1147;3326;2289;4793;11140","Protein.complex.purification.method":"MI:0676- tandem affinity purification","GO.ID":"GO:0007249;GO:0005125","GO.description":"I-kappaB kinase/NF-kappaB signaling;cytokine activity","FunCat.ID":"30.01.05.01.04;40.02.03.01","FunCat.description":"NIK-I-kappaB/NF-kappaB cascade;cytokines (interleukines, colony stimulating factors, etc.)","PubMed.ID":14743216,"subunits.Protein.name.":"Inhibitor of nuclear factor kappa-B kinase subunit alpha;Heat shock protein HSP 90-beta;Peptidyl-prolyl cis-trans isomerase FKBP5 ;NF-kappa-B inhibitor beta ;Hsp90 co-chaperone Cdc37","subunits.Gene.name.":"CHUK;HSP90AB1;FKBP5;NFKBIB;CDC37","subunits.Gene.name.syn.":"IKKA, TCF16;HSP90B HSPC2 HSPCB;AIG6 FKBP51;IKBB TRIP9;CDC37A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5286,"ComplexName":"TNF-alpha/NF-kappa B signaling complex 10","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15111;P07900;P08238;P40222;Q15653;Q16543;Q676U5;Q8IX12;Q9UHD2;Q9Y6K9","subunits.Entrez.IDs.":"1147;3320;3326;200081;4793;11140;55054;None;29110;8517","Protein.complex.purification.method":"MI:0676- tandem affinity purification","GO.ID":"GO:0007249;GO:0005125","GO.description":"I-kappaB kinase/NF-kappaB signaling;cytokine activity","FunCat.ID":"30.01.05.01.04;40.02.03.01","FunCat.description":"NIK-I-kappaB/NF-kappaB cascade;cytokines (interleukines, colony stimulating factors, etc.)","PubMed.ID":14743216,"subunits.Protein.name.":"Inhibitor of nuclear factor kappa-B kinase subunit alpha;Heat shock protein HSP 90-alpha;Heat shock protein HSP 90-beta;Alpha-taxilin;NF-kappa-B inhibitor beta ;Hsp90 co-chaperone Cdc37;Autophagy-related protein 16-1 ;Cell division cycle and apoptosis regulator protein 1 ;Serine/threonine-protein kinase TBK1 ;NF-kappa-B essential modulator","subunits.Gene.name.":"CHUK;HSP90AA1;HSP90AB1;TXLNA;NFKBIB;CDC37;ATG16L1;CCAR1;TBK1;IKBKG","subunits.Gene.name.syn.":"IKKA, TCF16;HSP90A HSPC1 HSPCA;HSP90B HSPC2 HSPCB;TXLN;IKBB TRIP9;CDC37A;APG16L;CARP1 DIS;NAK;FIP3, NEMO","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5287,"ComplexName":"CDK4-CCND1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P11802;P24385","subunits.Entrez.IDs.":"1019;595","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000082","GO.description":"G1/S transition of mitotic cell cycle","FunCat.ID":"10.03.01.01.03","FunCat.description":"G1/S transition of mitotic cell cycle","PubMed.ID":15735718,"subunits.Protein.name.":"Cyclin-dependent kinase 4 ;G1/S-specific cyclin-D1","subunits.Gene.name.":"CDK4;CCND1","subunits.Gene.name.syn.":";BCL1 PRAD1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5288,"ComplexName":"P53-BARD1-Ku70 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04637;P12956;Q99728","subunits.Entrez.IDs.":"7157;2547;580","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006915","GO.description":"apoptotic process","FunCat.ID":"40.10.02","FunCat.description":"apoptosis (type I programmed cell death)","PubMed.ID":15782130,"subunits.Protein.name.":"Cellular tumor antigen p53;X-ray repair cross-complementing protein 6 ;BRCA1-associated RING domain protein 1","subunits.Gene.name.":"TP53;XRCC6;BARD1","subunits.Gene.name.syn.":"P53;G22P1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5291,"ComplexName":"Cd3e-Nck1-Mink1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P22646;Q8BMV0;Q9JM52","subunits.Entrez.IDs.":"12501;17973;50932","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0035556","GO.description":"intracellular signal transduction","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":15608642,"subunits.Protein.name.":"T-cell surface glycoprotein CD3 epsilon chain ;Putative uncharacterized protein ;Misshapen-like kinase 1","subunits.Gene.name.":"Cd3e;Nck1;Mink1","subunits.Gene.name.syn.":";;Map4k6 Mink","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5292,"ComplexName":"Ets2-Ini1-Smarce1-Smarca4 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"NIH 3T3 cells","subunits.UniProt.IDs.":"O35845;O54941;P15037;Q9Z0H3","subunits.Entrez.IDs.":"20586;57376;23872;20587","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0045892","GO.description":"negative regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.03","FunCat.description":"transcription repression","PubMed.ID":12637547,"subunits.Protein.name.":"Brg1 protein ;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;Protein C-ets-2;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","subunits.Gene.name.":"Smarca4;Smarce1;Ets2;Smarcb1","subunits.Gene.name.syn.":"Brg1;Baf57;;Baf47 Ini1 Snf5l1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5293,"ComplexName":"ETS2-SMARCA4-INI1 complex","Organism":"Human","Synonyms":"None","Cell.line":"MCF-7 cells","subunits.UniProt.IDs.":"P15036;P51532;Q12824","subunits.Entrez.IDs.":"2114;6597;6598","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0045892;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;nucleus","FunCat.ID":"11.02.03.04.03;70.10","FunCat.description":"transcription repression;nucleus","PubMed.ID":12637547,"subunits.Protein.name.":"Protein C-ets-2;Transcription activator BRG1;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","subunits.Gene.name.":"ETS2;SMARCA4;SMARCB1","subunits.Gene.name.syn.":";BAF190A BRG1 SNF2B SNF2L4;BAF47, INI1, SNF5L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Brg-1 and Ini1 could be detected in complex with ets-2 after tetracycline removal, but not in cells maintained in tetracycline.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5295,"ComplexName":"Cd247 homodimer complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P24161","subunits.Entrez.IDs.":"12503","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0005886","GO.description":"intracellular protein transport;protein targeting;protein transport;plasma membrane","FunCat.ID":"14.04;20.01.10;70.02","FunCat.description":"protein targeting, sorting and translocation;protein transport;eukaryotic plasma membrane / membrane attached","PubMed.ID":9218590,"subunits.Protein.name.":"T-cell surface glycoprotein CD3 zeta chain","subunits.Gene.name.":"Cd247","subunits.Gene.name.syn.":"Cd3z Tcrz","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse)"}
{"ComplexID":5296,"ComplexName":"Cd3e homodimer complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P22646","subunits.Entrez.IDs.":"12501","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0005886","GO.description":"intracellular protein transport;protein targeting;protein transport;plasma membrane","FunCat.ID":"14.04;20.01.10;70.02","FunCat.description":"protein targeting, sorting and translocation;protein transport;eukaryotic plasma membrane / membrane attached","PubMed.ID":9218590,"subunits.Protein.name.":"T-cell surface glycoprotein CD3 epsilon chain","subunits.Gene.name.":"Cd3e","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse)"}
{"ComplexID":5301,"ComplexName":"Striatin-SG2NA-zinedin-caveolin1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P41350;P58404;P58405;P70483","subunits.Entrez.IDs.":"25404;97387;114520;29149","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation;MI:0096- pull down","GO.ID":"GO:0016192;GO:0019722;GO:0030182","GO.description":"vesicle-mediated transport;calcium-mediated signaling;neuron differentiation","FunCat.ID":"20.09.07;30.01.09.03;43.03.13","FunCat.description":"vesicular transport (Golgi network, etc.);Ca2+ mediated signal transduction;neuron","PubMed.ID":11707266,"subunits.Protein.name.":"Caveolin-1;Striatin-4 ;Striatin-3 ;Striatin","subunits.Gene.name.":"Cav1;Strn4;Strn3;Strn","subunits.Gene.name.syn.":"Cav;Zin;Gs2na Sg2na;","Disease.comment":"None","Subunits.comment":"Since Strn4 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"Caveolin-1 may directly regulate the function of the proteins of the striatin family, by concentrating them within caveolin-enriched domains.","SWISSPROT.organism":"Rattus norvegicus (Rat);Mus musculus (Mouse);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5302,"ComplexName":"Rab3a-Rims2-Rapgef4 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P63011;Q9EQZ6;Q9EQZ7","subunits.Entrez.IDs.":"19339;56508;116838","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006906;GO:0006887","GO.description":"vesicle fusion;exocytosis","FunCat.ID":"20.09.07.27;20.09.16.09.03","FunCat.description":"vesicle fusion;exocytosis","PubMed.ID":11056535,"subunits.Protein.name.":"Ras-related protein Rab-3A;Rap guanine nucleotide exchange factor 4 ;Regulating synaptic membrane exocytosis protein 2","subunits.Gene.name.":"Rab3a;Rapgef4;Rims2","subunits.Gene.name.syn.":";Cgef2 Epac2;Rab3ip2 Rim2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Rab3A-Rim2-cAMP-GEFII complex was formed in vitro when Rab3A was in the GTP-activated form. The authors showed that cAMP-GEFII is a direct target of cAMP in regulated exocytosis and is responsible for cAMP-dependent, PKA-independent exocytosis.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5308,"ComplexName":"Rb-NeuroD1-Ngfi-B complex","Organism":"Mouse","Synonyms":"None","Cell.line":"AtT-20 cells","subunits.UniProt.IDs.":"P12813;Q60867;Q64701","subunits.Entrez.IDs.":"15370;18012;19650","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0003677","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding","FunCat.ID":"11.02.03.04;16.03.01","FunCat.description":"transcriptional control;DNA binding","PubMed.ID":15701640,"subunits.Protein.name.":"Nuclear receptor subfamily 4 group A member 1 ;Neurogenic differentiation factor 1 ;Retinoblastoma-like protein 1","subunits.Gene.name.":"Nr4a1;Neurod1;Rbl1","subunits.Gene.name.syn.":"Gfrp Hmr N10 Nur77;Neurod;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Rb provides a bridge to bring together NGFI-B and NeuroD1 within a trimeric complex.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5309,"ComplexName":"Cd3g-Cd3e complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P11942;P22646","subunits.Entrez.IDs.":"12502;12501","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0005886","GO.description":"intracellular protein transport;protein targeting;protein transport;plasma membrane","FunCat.ID":"14.04;20.01.10;70.02","FunCat.description":"protein targeting, sorting and translocation;protein transport;eukaryotic plasma membrane / membrane attached","PubMed.ID":9218590,"subunits.Protein.name.":"T-cell surface glycoprotein CD3 gamma chain ;T-cell surface glycoprotein CD3 epsilon chain","subunits.Gene.name.":"Cd3g;Cd3e","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5310,"ComplexName":"Cd3d-Cd3g-Cd3e-Cd247 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04235;P11942;P22646;P24161","subunits.Entrez.IDs.":"12500;12502;12501;12503","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0023052;GO:0030217;GO:0005886","GO.description":"signaling;T cell differentiation;plasma membrane","FunCat.ID":"30.01;43.03.07.02.01.02;70.02","FunCat.description":"cellular signalling;T-cell;eukaryotic plasma membrane / membrane attached","PubMed.ID":9218590,"subunits.Protein.name.":"T-cell surface glycoprotein CD3 delta chain ;T-cell surface glycoprotein CD3 gamma chain ;T-cell surface glycoprotein CD3 epsilon chain ;T-cell surface glycoprotein CD3 zeta chain","subunits.Gene.name.":"Cd3d;Cd3g;Cd3e;Cd247","subunits.Gene.name.syn.":"T3d;;;Cd3z Tcrz","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5311,"ComplexName":"Cd3g-Cd3e-Cd247-Canx complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P11942;P22646;P24161;P35564","subunits.Entrez.IDs.":"12502;12501;12503;12330","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0023052;GO:0030217;GO:0005886","GO.description":"signaling;T cell differentiation;plasma membrane","FunCat.ID":"30.01;43.03.07.02.01.02;70.02","FunCat.description":"cellular signalling;T-cell;eukaryotic plasma membrane / membrane attached","PubMed.ID":9218590,"subunits.Protein.name.":"T-cell surface glycoprotein CD3 gamma chain ;T-cell surface glycoprotein CD3 epsilon chain ;T-cell surface glycoprotein CD3 zeta chain ;Calnexin","subunits.Gene.name.":"Cd3g;Cd3e;Cd247;Canx","subunits.Gene.name.syn.":";;Cd3z Tcrz;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5315,"ComplexName":"Munc13-1-Rim2-Rab3a complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P63012;Q62768;Q9JIS1","subunits.Entrez.IDs.":"25531;64829;116839","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0005326;GO:0006836;GO:0048489;GO:0016079","GO.description":"neurotransmitter transporter activity;neurotransmitter transport;synaptic vesicle transport;synaptic vesicle exocytosis","FunCat.ID":"20.01.26;20.09.16.09.05","FunCat.description":"neurotransmitter transport;synaptic vesicle exocytosis","PubMed.ID":16052212,"subunits.Protein.name.":"Ras-related protein Rab-3A;Protein unc-13 homolog A ;Regulating synaptic membrane exocytosis protein 2","subunits.Gene.name.":"Rab3a;Unc13a;Rims2","subunits.Gene.name.syn.":";Unc13h1;Rim2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results show that the N-terminal sequence of alpha-RIMs has a modular design that places Rab3A and Munc13-1 into close proximity, but not into competition.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5317,"ComplexName":"LATS1-HTRA2-BIRC4 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43464;O95835;P98170","subunits.Entrez.IDs.":"27429;9113;331","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008219","GO.description":"cell death","FunCat.ID":"40.1","FunCat.description":"cell death","PubMed.ID":16007220,"subunits.Protein.name.":"Serine protease HTRA2, mitochondrial ;Serine/threonine-protein kinase LATS1;E3 ubiquitin-protein ligase XIAP","subunits.Gene.name.":"HTRA2;LATS1;XIAP","subunits.Gene.name.syn.":"OMI PRSS25;WARTS;API3, BIRC4, IAP3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"WARTS forms a complex with XIAP while interacting with Omi and is potentially involved in the cell death through the inhibition of XIAP.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5318,"ComplexName":"DDEF1-CTTN-PXN complex","Organism":"Human","Synonyms":"None","Cell.line":"MDA-MB-231 cells, 4T1-Luc cells","subunits.UniProt.IDs.":"P49023;Q14247;Q9ULH1","subunits.Entrez.IDs.":"5829;2017;50807","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0007010","GO.description":"cytoskeleton organization","FunCat.ID":"42.04","FunCat.description":"cytoskeleton/structural proteins","PubMed.ID":15719014,"subunits.Protein.name.":"Paxillin;Src substrate cortactin;Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1","subunits.Gene.name.":"PXN;CTTN;ASAP1","subunits.Gene.name.syn.":";EMS1;DDEF1 KIAA1249","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This co-precipitation was only detected in highly invasive cells, such as MDA-MB-231 and 4T1/luc, but was undetectable in weak or noninvasive cells, such as MDA-MB-468 and MCF7, as well as in normal mammary epithelial cells. The authors describe that AMAP1 bridges cortactin and paxillin in highly invasive cells.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5319,"ComplexName":"CDH1-CKS1B complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12830;P61024","subunits.Entrez.IDs.":"999;1163","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000278","GO.description":"mitotic cell cycle","FunCat.ID":"10.03.01.01","FunCat.description":"mitotic cell cycle","PubMed.ID":15014502,"subunits.Protein.name.":"Cadherin-1;Cyclin-dependent kinases regulatory subunit 1","subunits.Gene.name.":"CDH1;CKS1B","subunits.Gene.name.syn.":"CDHE UVO;CKS1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5320,"ComplexName":"CDH1-SKP2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12830;Q13309","subunits.Entrez.IDs.":"999;6502","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000278","GO.description":"mitotic cell cycle","FunCat.ID":"10.03.01.01","FunCat.description":"mitotic cell cycle","PubMed.ID":15014502,"subunits.Protein.name.":"Cadherin-1;S-phase kinase-associated protein 2","subunits.Gene.name.":"CDH1;SKP2","subunits.Gene.name.syn.":"CDHE UVO;FBXL1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5321,"ComplexName":"Cebpa-Smarca2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"liver","subunits.UniProt.IDs.":"O35846;P53566","subunits.Entrez.IDs.":"67155;12606","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0000278;GO:0051726","GO.description":"mitotic cell cycle;regulation of cell cycle","FunCat.ID":"10.03.01.01;10.03.01","FunCat.description":"mitotic cell cycle;mitotic cell cycle and cell cycle control","PubMed.ID":15716955,"subunits.Protein.name.":"Brm protein;CCAAT/enhancer-binding protein alpha","subunits.Gene.name.":"Smarca2;Cebpa","subunits.Gene.name.syn.":"brm;Cebp","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The cEBP-alpha-Brm protein complex was detected in liver extracts from old isochronic parabionts but not from young isochronic parabionts.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5330,"ComplexName":"Lef1-Tle1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P27782;Q62440","subunits.Entrez.IDs.":"16842;21885","Protein.complex.purification.method":"MI:0067- light scattering","GO.ID":"GO:2001141;GO:0006355;GO:0003677","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding","FunCat.ID":"11.02.03.04;16.03.01","FunCat.description":"transcriptional control;DNA binding","PubMed.ID":15768032,"subunits.Protein.name.":"Lymphoid enhancer-binding factor 1 ;Transducin-like enhancer protein 1","subunits.Gene.name.":"Lef1;Tle1","subunits.Gene.name.syn.":"Lef-1;Grg1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In the absence of nuclear beta-catenin, Tcf/Lefs act as transcriptional repressors by binding to Groucho/TLE proteins.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5331,"ComplexName":"YY1-MDM2-p53 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04637;P25490;Q00987","subunits.Entrez.IDs.":"7157;7528;4193","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process","FunCat.ID":"14.07.05;14.13.01.01","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway)","PubMed.ID":15210108,"subunits.Protein.name.":"Cellular tumor antigen p53;Transcriptional repressor protein YY1;E3 ubiquitin-protein ligase Mdm2","subunits.Gene.name.":"TP53;YY1;MDM2","subunits.Gene.name.syn.":"P53;INO80S;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"YY1 is a potential cofactor for MDM2 in the regulation of p53 homeostasis. The physical interaction of YY1 with MDM2 appears to be important for efficient MDM2-p53 interaction in vivo, which in turn is necessary for p53 ubiquitination.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5333,"ComplexName":"Lef1-Tle1-Ctnnb1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P27782;Q02248;Q62440","subunits.Entrez.IDs.":"16842;12387;21885","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0027- cosedimentation","GO.ID":"GO:2001141;GO:0006355;GO:0003677","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding","FunCat.ID":"11.02.03.04;16.03.01","FunCat.description":"transcriptional control;DNA binding","PubMed.ID":15768032,"subunits.Protein.name.":"Lymphoid enhancer-binding factor 1 ;Catenin beta-1;Transducin-like enhancer protein 1","subunits.Gene.name.":"Lef1;Ctnnb1;Tle1","subunits.Gene.name.syn.":"Lef-1;Catnb;Grg1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In the absence of nuclear beta-catenin, Tcf/Lefs act as transcriptional repressors by binding to Groucho/TLE proteins.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5337,"ComplexName":"ELMO1-DOCK1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q14185;Q92556","subunits.Entrez.IDs.":"1793;9844","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0005515;GO:0007186;GO:0016477","GO.description":"protein binding;G-protein coupled receptor signaling pathway;cell migration","FunCat.ID":"16.01;30.05.02.24;34.05.01","FunCat.description":"protein binding;G-protein coupled receptor signalling pathway;cell migration","PubMed.ID":12134158,"subunits.Protein.name.":"Dedicator of cytokinesis protein 1 ;Engulfment and cell motility protein 1","subunits.Gene.name.":"DOCK1;ELMO1","subunits.Gene.name.syn.":";KIAA0281","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Dock-ELMO complex functions as an unconventional two-part exchange factor for Rac.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5341,"ComplexName":"ELMO1-DOCK2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q92556;Q92608","subunits.Entrez.IDs.":"9844;1794","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0005515;GO:0007186;GO:0016477","GO.description":"protein binding;G-protein coupled receptor signaling pathway;cell migration","FunCat.ID":"16.01;30.05.02.24;34.05.01","FunCat.description":"protein binding;G-protein coupled receptor signalling pathway;cell migration","PubMed.ID":12134158,"subunits.Protein.name.":"Engulfment and cell motility protein 1 ;Dedicator of cytokinesis protein 2","subunits.Gene.name.":"ELMO1;DOCK2","subunits.Gene.name.syn.":"KIAA0281;KIAA0209","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Dock-ELMO complex functions as an unconventional two-part exchange factor for Rac.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5342,"ComplexName":"ELMO1-DOCK1-RAC1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P63000;Q14185;Q92556","subunits.Entrez.IDs.":"5879;1793;9844","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0005515;GO:0007186;GO:0016477","GO.description":"protein binding;G-protein coupled receptor signaling pathway;cell migration","FunCat.ID":"16.01;30.05.02.24;34.05.01","FunCat.description":"protein binding;G-protein coupled receptor signalling pathway;cell migration","PubMed.ID":12134158,"subunits.Protein.name.":"Ras-related C3 botulinum toxin substrate 1 ;Dedicator of cytokinesis protein 1 ;Engulfment and cell motility protein 1","subunits.Gene.name.":"RAC1;DOCK1;ELMO1","subunits.Gene.name.syn.":"TC25;;KIAA0281","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Dock-ELMO complex functions as an unconventional two-part exchange factor for Rac.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5343,"ComplexName":"ELMO1-DOCK1-CRKII complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P46108;Q14185;Q92556","subunits.Entrez.IDs.":"1398;1793;9844","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0005515;GO:0007186;GO:0016477","GO.description":"protein binding;G-protein coupled receptor signaling pathway;cell migration","FunCat.ID":"16.01;30.05.02.24;34.05.01","FunCat.description":"protein binding;G-protein coupled receptor signalling pathway;cell migration","PubMed.ID":16025104,"subunits.Protein.name.":"Adapter molecule crk;Dedicator of cytokinesis protein 1 ;Engulfment and cell motility protein 1","subunits.Gene.name.":"CRK;DOCK1;ELMO1","subunits.Gene.name.syn.":"None;;KIAA0281","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5344,"ComplexName":"Endocytic coat complex (11 subunits)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O08838;O08839;O35179;O35964;P11442;P17426;P21575;P62944;Q05140;Q5JC29;Q62910","subunits.Entrez.IDs.":"60668;117028;116743;81922;54241;11771;140694;140670;65178;313474;85238","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006897","GO.description":"endocytosis","FunCat.ID":"20.09.18.09.01","FunCat.description":"endocytosis","PubMed.ID":9694653,"subunits.Protein.name.":"Amphiphysin;Myc box-dependent-interacting protein 1 ;Endophilin-A1 ;Endophilin-A2 ;Clathrin heavy chain 1;AP-2 complex subunit alpha-1;Dynamin-1 ;AP-2 complex subunit beta ;Clathrin coat assembly protein AP180 ;Epidermal growth factor receptor pathway substrate 15 isoform B;Synaptojanin-1","subunits.Gene.name.":"Amph;Bin1;Sh3gl2;Sh3gl1;Cltc;Ap2a1;Dnm1;Ap2b1;Snap91;Eps15;Synj1","subunits.Gene.name.syn.":"Amph1;Amph2 Amphl;Sh3d2a Sh3p4;Sh3p8;None;Adtaa Clapa1;Dnm;Clapb1;;;","Disease.comment":"None","Subunits.comment":"Since Ap2a1 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"Clathrin-mediated endocytosis involves cycles of assembly and disassembly of clathrin coat components and their accessory proteins. Dephosphorylation of rat brain extract was shown to promote the assembly of dynamin 1, synaptojanin 1, and amphiphysin into complexes that also included clathrin and AP-2.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Mus musculus (Mouse);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5345,"ComplexName":"Endocytic coat complex (7 subunits)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O08838;O08839;P11442;P17426;P21575;P62944;Q62910","subunits.Entrez.IDs.":"60668;117028;54241;11771;140694;140670;85238","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006897","GO.description":"endocytosis","FunCat.ID":"20.09.18.09.01","FunCat.description":"endocytosis","PubMed.ID":9694653,"subunits.Protein.name.":"Amphiphysin;Myc box-dependent-interacting protein 1 ;Clathrin heavy chain 1;AP-2 complex subunit alpha-1;Dynamin-1 ;AP-2 complex subunit beta ;Synaptojanin-1","subunits.Gene.name.":"Amph;Bin1;Cltc;Ap2a1;Dnm1;Ap2b1;Synj1","subunits.Gene.name.syn.":"Amph1;Amph2 Amphl;None;Adtaa Clapa1;Dnm;Clapb1;","Disease.comment":"None","Subunits.comment":"Since Ap2a1 from rat was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used.","Complex.comment":"Clathrin-mediated endocytosis involves cycles of assembly and disassembly of clathrin coat components and their accessory proteins. Dephosphorylation of rat brain extract was shown to promote the assembly of dynamin 1, synaptojanin 1, and amphiphysin into complexes that also included clathrin and AP-2.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Mus musculus (Mouse);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5348,"ComplexName":"Pik3r5-Pik3cg complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q5SW28;Q9JHG7","subunits.Entrez.IDs.":"320207;30955","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030234;GO:0050790","GO.description":"enzyme regulator activity;regulation of catalytic activity","FunCat.ID":"18.02.01","FunCat.description":"enzymatic activity regulation / enzyme regulator","PubMed.ID":15797027,"subunits.Protein.name.":"Phosphoinositide 3-kinase regulatory subunit 5 ;Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform","subunits.Gene.name.":"Pik3r5;Pik3cg","subunits.Gene.name.syn.":";Pi3kg1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5358,"ComplexName":"GTP-Rho-Rhpn1-Ropn1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q3TN61;Q61085;Q9ESG2","subunits.Entrez.IDs.":"11848;14787;76378","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006928","GO.description":"movement of cell or subcellular component","FunCat.ID":"34.05","FunCat.description":"cell motility","PubMed.ID":10591629,"subunits.Protein.name.":"Putative uncharacterized protein;Rhophilin-1 ;Ropporin-1","subunits.Gene.name.":"Rhoa;Rhpn1;Ropn1","subunits.Gene.name.syn.":";Grbp;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5360,"ComplexName":"AGO2-FXR1-TNF(alpha)ARE-RNP complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P51114;Q9UKV8","subunits.Entrez.IDs.":"8087;27161","Protein.complex.purification.method":"MI:0030- cross-linking studies; MI:0004- affinity chromatography technologies; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006417;GO:0003723;GO:0005737","GO.description":"regulation of translation;RNA binding;cytoplasm","FunCat.ID":"12.07;16.03.03;70.03","FunCat.description":"translational control;RNA binding;cytoplasm","PubMed.ID":17382880,"subunits.Protein.name.":"Fragile X mental retardation syndrome-related protein 1 ;Protein argonaute-2","subunits.Gene.name.":"FXR1;AGO2","subunits.Gene.name.syn.":";EIF2C2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"AGO2 functions as translational activator under serum-starved conditions.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5361,"ComplexName":"Cell division cycle complex (CDC27, CDC16, ANAPC7)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P30260;Q13042;Q9UJX3","subunits.Entrez.IDs.":"996;8881;51434","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000278","GO.description":"mitotic cell cycle","FunCat.ID":"10.03.01.01","FunCat.description":"mitotic cell cycle","PubMed.ID":15916961,"subunits.Protein.name.":"Cell division cycle protein 27 homolog ;Cell division cycle protein 16 homolog ;Anaphase-promoting complex subunit 7","subunits.Gene.name.":"CDC27;CDC16;ANAPC7","subunits.Gene.name.syn.":"ANAPC3 D0S1430E D17S978E;ANAPC6;APC7","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5363,"ComplexName":"Actin-ribonucleoprotein complex (POLR2A, GTF2F1, HNRNPU)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P24928;P35269;Q00839","subunits.Entrez.IDs.":"5430;2962;3192","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006351","GO.description":"transcription, DNA-templated","FunCat.ID":"11","FunCat.description":"TRANSCRIPTION","PubMed.ID":15711563,"subunits.Protein.name.":"DNA-directed RNA polymerase II subunit RPB1;General transcription factor IIF subunit 1;Heterogeneous nuclear ribonucleoprotein U","subunits.Gene.name.":"POLR2A;GTF2F1;HNRNPU","subunits.Gene.name.syn.":"POLR2;RAP74;HNRPU SAFA U21.1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5365,"ComplexName":"Ripk2-Nod2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P58801;Q8K3Z0","subunits.Entrez.IDs.":"192656;257632","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":15620648,"subunits.Protein.name.":"Receptor-interacting serine/threonine-protein kinase 2 ;Nucleotide-binding oligomerization domain-containing protein 2","subunits.Gene.name.":"Ripk2;Nod2","subunits.Gene.name.syn.":";Card15","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Nod2 binding to R2 and Rip2 expression are necessary for Nod2 to Induce ubiquitinylation of Nemo protein.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5366,"ComplexName":"Calm1-Ryr1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"F1LMY4;P62161","subunits.Entrez.IDs.":"114207;None","Protein.complex.purification.method":"MI:0040- electron microscopy","GO.ID":"GO:0006937","GO.description":"regulation of muscle contraction","FunCat.ID":"36.25.09.05","FunCat.description":"general muscle contraction regulation","PubMed.ID":11694536,"subunits.Protein.name.":"Ryanodine receptor 1 ;Calmodulin","subunits.Gene.name.":"Ryr1;Calm1; Cal","subunits.Gene.name.syn.":";Calm, Cam, Cam1, Cam2, Camb, Cam3, Camc","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5367,"ComplexName":"THRB-RXRB complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P10828;P28702","subunits.Entrez.IDs.":"7068;6257","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0009755","GO.description":"hormone-mediated signaling pathway","FunCat.ID":"30.01.09.08","FunCat.description":"hormone mediated signal transduction","PubMed.ID":9346901,"subunits.Protein.name.":"Thyroid hormone receptor beta ;Retinoic acid receptor RXR-beta","subunits.Gene.name.":"THRB;RXRB","subunits.Gene.name.syn.":"ERBA2 NR1A2 THR1;NR2B2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5368,"ComplexName":"Nfkb1-Rela complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P25799;Q04207","subunits.Entrez.IDs.":"18033;19697","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":9738011,"subunits.Protein.name.":"Nuclear factor NF-kappa-B p105 subunit ;Transcription factor p65","subunits.Gene.name.":"Nfkb1;Rela","subunits.Gene.name.syn.":";Nfkb3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5369,"ComplexName":"ATM homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q13315","subunits.Entrez.IDs.":"472","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0006281","GO.description":"DNA repair","FunCat.ID":"10.01.05.01","FunCat.description":"DNA repair","PubMed.ID":15790808,"subunits.Protein.name.":"Serine-protein kinase ATM","subunits.Gene.name.":"ATM","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":5370,"ComplexName":"ERAP1-ERAP2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q6P179;Q9NZ08","subunits.Entrez.IDs.":"64167;51752","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0019882","GO.description":"antigen processing and presentation","FunCat.ID":"36.25.16.03.05","FunCat.description":"antigen presentation / processing","PubMed.ID":15908954,"subunits.Protein.name.":"Endoplasmic reticulum aminopeptidase 2 ;Endoplasmic reticulum aminopeptidase 1","subunits.Gene.name.":"ERAP2;ERAP1","subunits.Gene.name.syn.":"LRAP;APPILS ARTS1 KIAA0525","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5371,"ComplexName":"Grancalcin-sorcin complex","Organism":"Human","Synonyms":"None","Cell.line":"human umbilical vein endothelial cells","subunits.UniProt.IDs.":"P28676;P30626","subunits.Entrez.IDs.":"25801;6717","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0096-pull down;MI:0018-two hybrid","GO.ID":"GO:0005509","GO.description":"calcium ion binding","FunCat.ID":"16.17.01","FunCat.description":"calcium binding","PubMed.ID":12804766,"subunits.Protein.name.":"Grancalcin;Sorcin","subunits.Gene.name.":"GCA;SRI","subunits.Gene.name.syn.":"GCL;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5372,"ComplexName":"Sorcin homodimer complex","Organism":"Human","Synonyms":"SRI homodimer complex","Cell.line":"None","subunits.UniProt.IDs.":"P30626","subunits.Entrez.IDs.":"6717","Protein.complex.purification.method":"MI:0018-two hybrid","GO.ID":"GO:0005515;GO:0005509","GO.description":"protein binding;calcium ion binding","FunCat.ID":"16.01;16.17.01","FunCat.description":"protein binding;calcium binding","PubMed.ID":12804766,"subunits.Protein.name.":"Sorcin","subunits.Gene.name.":"SRI","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The penta-EF hand (PEF) family of calcium binding proteins includes grancalcin, peflin, sorcin, calpain large and small subunits as well as ALG-2. Heterodimerization, in addition to differential interactions with target proteins, might be a way to regulate and fine tune processes mediated by calcium binding proteins of the penta-EF hand type. The interaction of grancalcin with sorcin is approximately 17 times stronger than sorcin homodimerization.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":5373,"ComplexName":"Chromatin remodeling complex (TACC2, TACC3, PCAF)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95359;Q92831;Q9Y6A5","subunits.Entrez.IDs.":"10579;8850;10460","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006265","GO.description":"DNA topological change","FunCat.ID":"10.01.09.05","FunCat.description":"DNA conformation modification (e.g. chromatin)","PubMed.ID":14767476,"subunits.Protein.name.":"Transforming acidic coiled-coil-containing protein 2 ;Histone acetyltransferase KAT2B;Transforming acidic coiled-coil-containing protein 3","subunits.Gene.name.":"TACC2;KAT2B;TACC3","subunits.Gene.name.syn.":";PCAF;ERIC1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5375,"ComplexName":"EGR-EP300 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P18146;Q09472","subunits.Entrez.IDs.":"1958;2033","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006351","GO.description":"transcription, DNA-templated","FunCat.ID":"11","FunCat.description":"TRANSCRIPTION","PubMed.ID":15225550,"subunits.Protein.name.":"Early growth response protein 1 ;Histone acetyltransferase p300","subunits.Gene.name.":"EGR1;EP300","subunits.Gene.name.syn.":"KROX24 ZNF225;P300","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results show that the interactions between p300/CBP and Egr1 can lead to complex feedback loops and to inhibition of Egr1 activities under specific conditions.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5376,"ComplexName":"Rock1-Pfn2 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q63644;Q9EPC6","subunits.Entrez.IDs.":"81762;81531","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006461","GO.description":"protein complex assembly","FunCat.ID":"14.1","FunCat.description":"assembly of protein complexes","PubMed.ID":15834419,"subunits.Protein.name.":"Rho-associated protein kinase 1 ;Profilin-2","subunits.Gene.name.":"Rock1;Pfn2","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5377,"ComplexName":"RNA-induced silencing complex, RISC","Organism":"Human","Synonyms":"TRBP containing complex (DICER, TRBP, AGO2)","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"Q15633;Q9UKV8;Q9UPY3","subunits.Entrez.IDs.":"6895;27161;23405","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0096- pull down","GO.ID":"GO:0032774;GO:0006396;GO:0003723","GO.description":"RNA biosynthetic process;RNA processing;RNA binding","FunCat.ID":"11.02;11.04;16.03.03","FunCat.description":"RNA synthesis;RNA processing;RNA binding","PubMed.ID":17507929,"subunits.Protein.name.":"RISC-loading complex subunit TARBP2 ;Protein argonaute-2 ;Endoribonuclease Dicer","subunits.Gene.name.":"TARBP2;AGO2;DICER1","subunits.Gene.name.syn.":"TRBP;EIF2C2;DICER HERNA KIAA0928","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors describe this complex as minimal Dicer-TRBP-AGO2 complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5378,"ComplexName":"TRBP containing complex (DICER, TRBP, AGO2, RPL7A, EIF6, MOV10)","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"P56537;P62424;Q15633;Q9HCE1;Q9UKV8;Q9UPY3","subunits.Entrez.IDs.":"3692;6130;6895;4343;27161;23405","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0096- pull down","GO.ID":"GO:0032774;GO:0006396;GO:0003723","GO.description":"RNA biosynthetic process;RNA processing;RNA binding","FunCat.ID":"11.02;11.04;16.03.03","FunCat.description":"RNA synthesis;RNA processing;RNA binding","PubMed.ID":17507929,"subunits.Protein.name.":"Eukaryotic translation initiation factor 6 ;60S ribosomal protein L7a;RISC-loading complex subunit TARBP2 ;Putative helicase MOV-10 ;Protein argonaute-2 ;Endoribonuclease Dicer","subunits.Gene.name.":"EIF6;RPL7A;TARBP2;MOV10;AGO2;DICER1","subunits.Gene.name.syn.":"EIF3A ITGB4BP;SURF-3 SURF3;TRBP;KIAA1631;EIF2C2;DICER HERNA KIAA0928","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors show that depletion of eIF6 in human cells specifically abrogates miRNA-mediated regulation of target protein and mRNA levels.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5379,"ComplexName":"Kcna2-Kcnab2 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62483;P63142","subunits.Entrez.IDs.":"29738;25468","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0027- cosedimentation","GO.ID":"GO:0008324;GO:0006812;GO:0015267","GO.description":"cation transmembrane transporter activity;cation transport;channel activity","FunCat.ID":"20.01.01.01;20.03.01","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);channel / pore class transport","PubMed.ID":8608002,"subunits.Protein.name.":"Voltage-gated potassium channel subunit beta-2 ;Potassium voltage-gated channel subfamily A member 2","subunits.Gene.name.":"Kcnab2;Kcna2","subunits.Gene.name.syn.":"Ckbeta2 Kcnb3;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5380,"ComplexName":"TRBP containing complex (DICER, RPL7A, EIF6, MOV10 and subunits of the 60S ribosomal particle)","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"P05386;P05387;P18077;P18124;P26373;P30050;P46778;P46779;P49207;P50914;P56537;P61313;P61353;P61513;P62424;P62888;P62906;P62910;P62913;P84098;Q02543;Q9HCE1;Q9UHA3;Q9UPY3;Q9Y3U8","subunits.Entrez.IDs.":"6176;6181;6165;6129;6137;6136;6144;6158;6164;9045;3692;6138;6155;6168;6130;6156;4736;6161;6135;6143;6142;4343;51187;23405;25873","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0096- pull down","GO.ID":"GO:0032774;GO:0006417;GO:0003723","GO.description":"RNA biosynthetic process;regulation of translation;RNA binding","FunCat.ID":"11.02;12.07;16.03.03","FunCat.description":"RNA synthesis;translational control;RNA binding","PubMed.ID":17507929,"subunits.Protein.name.":"60S acidic ribosomal protein P1;60S acidic ribosomal protein P2;60S ribosomal protein L35a;60S ribosomal protein L7;60S ribosomal protein L13;60S ribosomal protein L12;60S ribosomal protein L21;60S ribosomal protein L28;60S ribosomal protein L34;60S ribosomal protein L14;Eukaryotic translation initiation factor 6 ;60S ribosomal protein L15;60S ribosomal protein L27;60S ribosomal protein L37a;60S ribosomal protein L7a;60S ribosomal protein L30;60S ribosomal protein L10a;60S ribosomal protein L32;60S ribosomal protein L11;60S ribosomal protein L19;60S ribosomal protein L18a;Putative helicase MOV-10 ;Probable ribosome biogenesis protein RLP24 ;Endoribonuclease Dicer ;60S ribosomal protein L36","subunits.Gene.name.":"RPLP1;RPLP2;RPL35A;RPL7;RPL13;RPL12;RPL21;RPL28;RPL34;RPL14;EIF6;RPL15;RPL27;RPL37A;RPL7A;RPL30;RPL10A;RPL32;RPL11;RPL19;RPL18A;MOV10;RSL24D1;DICER1;RPL36","subunits.Gene.name.syn.":"RRP1;D11S2243E RPP2;None;None;BBC1;None;None;None;None;None;EIF3A ITGB4BP;EC45;None;None;SURF-3 SURF3;None;NEDD6;None;None;None;None;KIAA1631;C15orf15 RPL24L;DICER HERNA KIAA0928;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In mass spectrometric sequencing analyses the authors showed that in addition to RISC subunits they obtained protein sequences corresponding to nearly all subunits of the large (60S) ribosomal particle. The ability of eIF6 to inhibit joining of the 60S and 40S subunits of the ribosome and, thus, to prevent formation of a translationally competent complex, raises the possibility that eIF6 may repress translation by blocking initiation or ribosome recycling.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5381,"ComplexName":"RNA-induced silencing complex, RISC","Organism":"Human","Synonyms":"TRBP containing complex (DICER, TRBP, AGO2)","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"Q15633;Q9UKV8;Q9UPY3","subunits.Entrez.IDs.":"6895;27161;23405","Protein.complex.purification.method":"MI:0096- pull down; MI:0071- molecular sieving","GO.ID":"GO:0032774;GO:0006396;GO:0003723;GO:0005737","GO.description":"RNA biosynthetic process;RNA processing;RNA binding;cytoplasm","FunCat.ID":"11.02;11.04;16.03.03;70.03","FunCat.description":"RNA synthesis;RNA processing;RNA binding;cytoplasm","PubMed.ID":16271387,"subunits.Protein.name.":"RISC-loading complex subunit TARBP2 ;Protein argonaute-2 ;Endoribonuclease Dicer","subunits.Gene.name.":"TARBP2;AGO2;DICER1","subunits.Gene.name.syn.":"TRBP;EIF2C2;DICER HERNA KIAA0928","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors demonstrated that this complex can cleave target RNA using precursor microRNA (pre-miRNA) hairpin as the source of siRNA.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5382,"ComplexName":"ARNT-HIF1A complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P27540;Q16665","subunits.Entrez.IDs.":"405;3091","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0045893;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;nucleus","FunCat.ID":"11.02.03.04.01;70.10","FunCat.description":"transcription activation;nucleus","PubMed.ID":8663540,"subunits.Protein.name.":"Aryl hydrocarbon receptor nuclear translocator ;Hypoxia-inducible factor 1-alpha","subunits.Gene.name.":"ARNT;HIF1A","subunits.Gene.name.syn.":"BHLHE2;BHLHE78 MOP1 PASD8","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5383,"ComplexName":"TRIB3-DDIT3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P35638;Q96RU7","subunits.Entrez.IDs.":"1649;57761","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":15775988,"subunits.Protein.name.":"DNA damage-inducible transcript 3 protein ;Tribbles homolog 3","subunits.Gene.name.":"DDIT3;TRIB3","subunits.Gene.name.syn.":"CHOP CHOP10 GADD153;C20orf97 NIPK SKIP3 TRB3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5384,"ComplexName":"RAG1-RAG2 tetramer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P15918;P55895","subunits.Entrez.IDs.":"5896;5897","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006310","GO.description":"DNA recombination","FunCat.ID":"10.01.05.03","FunCat.description":"DNA recombination","PubMed.ID":10373515,"subunits.Protein.name.":"V;V","subunits.Gene.name.":"RAG1;RAG2","subunits.Gene.name.syn.":"RNF74;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5385,"ComplexName":"GAIT complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60506;P04406;P07814;P40429","subunits.Entrez.IDs.":"10492;2597;2058;23521","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006417","GO.description":"regulation of translation","FunCat.ID":"12.07","FunCat.description":"translational control","PubMed.ID":15479637,"subunits.Protein.name.":"Heterogeneous nuclear ribonucleoprotein Q;Glyceraldehyde-3-phosphate dehydrogenase;Bifunctional glutamate/proline--tRNA ligase ;60S ribosomal protein L13a","subunits.Gene.name.":"SYNCRIP;GAPDH;EPRS;RPL13A","subunits.Gene.name.syn.":"HNRPQ NSAP1;GAPD;GLNS PARS QARS QPRS;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5386,"ComplexName":"MLL1-WDR5 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00268;O43451;O75461;P21675;P34932;P49848;P51610;P61964;Q03164;Q15291;Q15545;Q16594;Q6PI98;Q7Z3B3;Q8IXM2;Q8IZL8;Q8WWY3;Q96EZ8;Q99496;Q9BVI0;Q9H4L4;Q9H7Z6;Q9HCK8;Q9NXF1;Q9UBL3;Q9Y265;Q9Y4W2","subunits.Entrez.IDs.":"6874;8972;1876;6872;3308;6878;3054;11091;4297;5929;6879;6880;125476;284058;124944;27043;26121;10445;6045;51230;26168;84148;57680;54881;9070;8607;81887","Protein.complex.purification.method":"MI:0226- ion exchange chromatography; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006265;GO:0045893;GO:0018126;GO:0006479;GO:0005634","GO.description":"DNA topological change;positive regulation of transcription, DNA-templated;protein hydroxylation;protein methylation;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04.01;14.07.09;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcription activation;posttranslational modification of amino acids (e.g. hydroxylation, methylation);nucleus","PubMed.ID":15960975,"subunits.Protein.name.":"Transcription initiation factor TFIID subunit 4;Maltase-glucoamylase, intestinal [Includes: Maltase ;Transcription factor E2F6 ;Transcription initiation factor TFIID subunit 1;Heat shock 70 kDa protein 4;Transcription initiation factor TFIID subunit 6;Host cell factor 1;WD repeat-containing protein 5;Histone-lysine N-methyltransferase 2A;Retinoblastoma-binding protein 5;Transcription initiation factor TFIID subunit 7;Transcription initiation factor TFIID subunit 9;INO80 complex subunit C ;KAT8 regulatory NSL complex subunit 1 ;Chromatin complexes subunit BAP18 ;Proline-, glutamic acid- and leucine-rich protein 1 ;U4/U6 small nuclear ribonucleoprotein Prp31 ;Microspherule protein 1 ;E3 ubiquitin-protein ligase RING2;PHD finger protein 20 ;Sentrin-specific protease 3 ;Histone acetyltransferase KAT8 ;Chromodomain-helicase-DNA-binding protein 8 ;Testis-expressed sequence 10 protein;Set1/Ash2 histone methyltransferase complex subunit ASH2;RuvB-like 1;Ribosomal biogenesis protein LAS1L","subunits.Gene.name.":"TAF4;MGAM;E2F6;TAF1;HSPA4;TAF6;HCFC1;WDR5;KMT2A;RBBP5;TAF7;TAF9;INO80C;KANSL1;BAP18;PELP1;PRPF31;MCRS1;RNF2;PHF20;SENP3;KAT8;CHD8;TEX10;ASH2L;RUVBL1;LAS1L","subunits.Gene.name.syn.":"TAF2C TAF2C1 TAF4A TAFII130 TAFII135;MGA MGAML;;BA2R CCG1 CCGS TAF2A;APG2;TAF2E TAFII70;HCF1, HFC1;BIG3;ALL1, CXXC7, HRX, HTRX, MLL, MLL1, TRX1;RBQ3;TAF2F TAFII55;TAF2G TAFII31;C18orf37;CENP-36 KIAA1267 MSL1V1 NSL1;C17orf49;HMX3 MNAR;PRP31;INO80Q MSP58;BAP1 DING HIPI3 RING1B;C20orf104 GLEA2 HCA58 NZF TZP;SSP3 SUSP3;MOF MYST1;HELSNF1 KIAA1564;;ASH2L1;INO80H NMP238 TIP49 TIP49A;","Disease.comment":"The MLL1 subunit is the product of a protooncogene that was first detected through chromosomal translocations directly associated with aggressive lymphoid and myeloid acute leukemias, especially among infants.","Subunits.comment":"The apparent size of the MOF-containing MLL1-WDR5 complex is around 1.5 MDa.","Complex.comment":"The MLL1-WDR5 complex has a robust MLL1-mediated histone methyltransferase activity that can effect mono-, di-, and trimethylation of H3 K4 and a MOF-mediated histone acetyltransferase activity that is specific for H4 K16. Both activities are required for optimal transcription activation on a chromatin template in vitro and on an endogenous MLL1 target gene, Hox a9, in vivo.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5388,"ComplexName":"SERPINA1-ELA2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P01009;P08246","subunits.Entrez.IDs.":"5265;1991","Protein.complex.purification.method":"MI:0107- surface plasmon resonance","GO.ID":"GO:0016485","GO.description":"protein processing","FunCat.ID":"14.07.11","FunCat.description":"protein processing (proteolytic)","PubMed.ID":15131125,"subunits.Protein.name.":"Alpha-1-antitrypsin ;Neutrophil elastase","subunits.Gene.name.":"SERPINA1;ELANE","subunits.Gene.name.syn.":"AAT PI;ELA2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5389,"ComplexName":"SERPINA3-CTSG complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P01011;P08311","subunits.Entrez.IDs.":"12;1511","Protein.complex.purification.method":"MI:0107- surface plasmon resonance","GO.ID":"GO:0016485","GO.description":"protein processing","FunCat.ID":"14.07.11","FunCat.description":"protein processing (proteolytic)","PubMed.ID":15131125,"subunits.Protein.name.":"Alpha-1-antichymotrypsin ;Cathepsin G","subunits.Gene.name.":"SERPINA3;CTSG","subunits.Gene.name.syn.":"AACT;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5391,"ComplexName":"SERPINA1-CTSG complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P01009;P08311","subunits.Entrez.IDs.":"5265;1511","Protein.complex.purification.method":"MI:0107- surface plasmon resonance","GO.ID":"GO:0016485","GO.description":"protein processing","FunCat.ID":"14.07.11","FunCat.description":"protein processing (proteolytic)","PubMed.ID":15131125,"subunits.Protein.name.":"Alpha-1-antitrypsin ;Cathepsin G","subunits.Gene.name.":"SERPINA1;CTSG","subunits.Gene.name.syn.":"AAT PI;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5400,"ComplexName":"BRCC complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P38398;P46736;P51587;Q06609;Q9NXR7","subunits.Entrez.IDs.":"672;79184;675;5888;9577","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006281;GO:0000075;GO:0016567;GO:0016579;GO:0006974;GO:0005634","GO.description":"DNA repair;cell cycle checkpoint;protein ubiquitination;protein deubiquitination;cellular response to DNA damage stimulus;nucleus","FunCat.ID":"10.01.05.01;10.03.01.03;14.07.05;32.01.09;70.10","FunCat.description":"DNA repair;cell cycle checkpoints (checkpoints of morphogenesis, DNA-damage,-replication, mitotic phase and spindle);modification by ubiquitination, deubiquitination;DNA damage response;nucleus","PubMed.ID":14636569,"subunits.Protein.name.":"Breast cancer type 1 susceptibility protein;Lys-63-specific deubiquitinase BRCC36 ;Breast cancer type 2 susceptibility protein ;DNA repair protein RAD51 homolog 1 ;BRCA1-A complex subunit BRE","subunits.Gene.name.":"BRCA1;BRCC3;BRCA2;RAD51;BRE","subunits.Gene.name.syn.":"RNF53;BRCC36 C6.1A CXorf53;FACD FANCD1;RAD51A RECA;BRCC45","Disease.comment":"BRCA1 or BRCA2 genes and their deleterious alleles are involved in breast cancer and ovarian cancer.","Subunits.comment":"None","Complex.comment":"BRCC may not play a direct role in DNA repair, but through its E3 ubiquitin ligase activity BRCC can regulate factors involved in DNA repair. BRE and BRCC36 are regulatory subunits modulating the ligase activity of the BRCC complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5401,"ComplexName":"PLEKHM2-KIF5B complex","Organism":"Human","Synonyms":"SKIP-kinesin complex","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"P33176;Q8IWE5","subunits.Entrez.IDs.":"3799;23207","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006928","GO.description":"movement of cell or subcellular component","FunCat.ID":"34.05","FunCat.description":"cell motility","PubMed.ID":15905402,"subunits.Protein.name.":"Kinesin-1 heavy chain;Pleckstrin homology domain-containing family M member 2","subunits.Gene.name.":"KIF5B;PLEKHM2","subunits.Gene.name.syn.":"KNS, KNS1;KIAA0842 SKIP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"During Salmonella typhimurium infection SKIP acts as an essential mediator of SifA (a S. thyphimurium protein, required for the formation of Salmonella-induced filaments). A dynamic process of kinesin recruitment in Salmonella-infected cells is mediated by the secretion of unidentified SPI-2 TTSS effectors and is down-regulated by the SifA-mediated recruitment of SKIP on membranes. The authors suggest that S. typhimurium is able to fine-tune the SCV-associated kinesin motor activity by regulating the secretion of its own effector proteins.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5402,"ComplexName":"Cdk5-Cdk5r1-Pctk1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P49615;P61809;Q04735","subunits.Entrez.IDs.":"12568;12569;18555","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0019209","GO.description":"kinase activator activity","FunCat.ID":"18.02.01.01.05","FunCat.description":"kinase activator","PubMed.ID":12084709,"subunits.Protein.name.":"Cyclin-dependent-like kinase 5 ;Cyclin-dependent kinase 5 activator 1 ;Cyclin-dependent kinase 16","subunits.Gene.name.":"Cdk5;Cdk5r1;Cdk16","subunits.Gene.name.syn.":"Cdkn5 Crk6;Cdk5r Nck5a;Crk5 Pctaire1 Pctk1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors show that Pctaire1 can be phosphorylated by the Cdk5/p25 complex, and serine 95 is the major phosphorylation site. In brain and muscle of Cdk5 None mice, Pctaire1 activity is significantly reduced.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5404,"ComplexName":"Myod1-Tcf3 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P10085;P15806","subunits.Entrez.IDs.":"17927;21423","Protein.complex.purification.method":"MI:0413- electrophoretic mobility shift assay","GO.ID":"GO:2001141;GO:0006355;GO:0003677;GO:0007519","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding;skeletal muscle tissue development","FunCat.ID":"11.02.03.04;16.03.01;41.05.15","FunCat.description":"transcriptional control;DNA binding;myogenesis","PubMed.ID":15719023,"subunits.Protein.name.":"Myoblast determination protein 1;Transcription factor E2-alpha","subunits.Gene.name.":"Myod1;Tcf3","subunits.Gene.name.syn.":"Myod;Alf2 Me2 Tcfe2a","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5405,"ComplexName":"Myod1 homodimer complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P10085","subunits.Entrez.IDs.":"17927","Protein.complex.purification.method":"MI:0053- fluorescence polarization spectroscopy","GO.ID":"GO:0045893;GO:0003677","GO.description":"positive regulation of transcription, DNA-templated;DNA binding","FunCat.ID":"11.02.03.04.01;16.03.01","FunCat.description":"transcription activation;DNA binding","PubMed.ID":9184158,"subunits.Protein.name.":"Myoblast determination protein 1","subunits.Gene.name.":"Myod1","subunits.Gene.name.syn.":"Myod","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse)"}
{"ComplexID":5406,"ComplexName":"Myod1-Tcf3 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P10085;P15806","subunits.Entrez.IDs.":"17927;21423","Protein.complex.purification.method":"MI:0053- fluorescence polarization spectroscopy","GO.ID":"GO:0003677;GO:0007519","GO.description":"DNA binding;skeletal muscle tissue development","FunCat.ID":"16.03.01;41.05.15","FunCat.description":"DNA binding;myogenesis","PubMed.ID":9184158,"subunits.Protein.name.":"Myoblast determination protein 1;Transcription factor E2-alpha","subunits.Gene.name.":"Myod1;Tcf3","subunits.Gene.name.syn.":"Myod;Alf2 Me2 Tcfe2a","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5407,"ComplexName":"NGF-TrkA complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P01138;P04629","subunits.Entrez.IDs.":"4803;4914","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0007169;GO:0022008;GO:0048699;GO:0007399","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway;neurogenesis;generation of neurons;nervous system development","FunCat.ID":"30.05.01.12;41.05.13;47.03.01","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways;neurogenesis;nervous system","PubMed.ID":10490030,"subunits.Protein.name.":"Beta-nerve growth factor ;High affinity nerve growth factor receptor","subunits.Gene.name.":"NGF;NTRK1","subunits.Gene.name.syn.":"NGFB;MTC TRK TRKA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5408,"ComplexName":"Neurotrophin-3-p75 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P08138;P20783","subunits.Entrez.IDs.":"4804;4908","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0007169;GO:0022008;GO:0048699;GO:0007399","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway;neurogenesis;generation of neurons;nervous system development","FunCat.ID":"30.05.01.12;41.05.13;47.03.01","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways;neurogenesis;nervous system","PubMed.ID":18596692,"subunits.Protein.name.":"Tumor necrosis factor receptor superfamily member 16 ;Neurotrophin-3","subunits.Gene.name.":"NGFR;NTF3","subunits.Gene.name.syn.":"TNFRSF16;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5409,"ComplexName":"TIAM1-GRIN1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q05586;Q13009","subunits.Entrez.IDs.":"2902;7074","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000902;GO:0016049;GO:0030182","GO.description":"cell morphogenesis;cell growth;neuron differentiation","FunCat.ID":"40.01;43.03.13","FunCat.description":"cell growth / morphogenesis;neuron","PubMed.ID":15721239,"subunits.Protein.name.":"Glutamate receptor ionotropic, NMDA 1 ;T-lymphoma invasion and metastasis-inducing protein 1","subunits.Gene.name.":"GRIN1;TIAM1","subunits.Gene.name.syn.":"NMDAR1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5411,"ComplexName":"HTR1D-S1PR1 complex","Organism":"Human","Synonyms":"HTR1D-EDG1 complex","Cell.line":"None","subunits.UniProt.IDs.":"P21453;P28221","subunits.Entrez.IDs.":"1901;3352","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007186","GO.description":"G-protein coupled receptor signaling pathway","FunCat.ID":"30.05.02.24","FunCat.description":"G-protein coupled receptor signalling pathway","PubMed.ID":11854302,"subunits.Protein.name.":"Sphingosine 1-phosphate receptor 1;5-hydroxytryptamine receptor 1D","subunits.Gene.name.":"S1PR1;HTR1D","subunits.Gene.name.syn.":"CHEDG1, EDG1, S1P1;HTR1DA HTRL","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5412,"ComplexName":"HTR1D  homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P28221","subunits.Entrez.IDs.":"3352","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515","GO.description":"protein binding","FunCat.ID":"16.01","FunCat.description":"protein binding","PubMed.ID":11854302,"subunits.Protein.name.":"5-hydroxytryptamine receptor 1D","subunits.Gene.name.":"HTR1D","subunits.Gene.name.syn.":"HTR1DA HTRL","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":5414,"ComplexName":"HTR1A-HTR1D complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P08908;P28221","subunits.Entrez.IDs.":"3350;3352","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515","GO.description":"protein binding","FunCat.ID":"16.01","FunCat.description":"protein binding","PubMed.ID":11854302,"subunits.Protein.name.":"5-hydroxytryptamine receptor 1A;5-hydroxytryptamine receptor 1D","subunits.Gene.name.":"HTR1A;HTR1D","subunits.Gene.name.syn.":"ADRB2RL1 ADRBRL1;HTR1DA HTRL","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5415,"ComplexName":"HTR1B homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P28222","subunits.Entrez.IDs.":"3351","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515","GO.description":"protein binding","FunCat.ID":"16.01","FunCat.description":"protein binding","PubMed.ID":11854302,"subunits.Protein.name.":"5-hydroxytryptamine receptor 1B","subunits.Gene.name.":"HTR1B","subunits.Gene.name.syn.":"HTR1DB","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":5416,"ComplexName":"HTR1A-HTR1B complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P08908;P28222","subunits.Entrez.IDs.":"3350;3351","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515","GO.description":"protein binding","FunCat.ID":"16.01","FunCat.description":"protein binding","PubMed.ID":11854302,"subunits.Protein.name.":"5-hydroxytryptamine receptor 1A;5-hydroxytryptamine receptor 1B","subunits.Gene.name.":"HTR1A;HTR1B","subunits.Gene.name.syn.":"ADRB2RL1 ADRBRL1;HTR1DB","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5417,"ComplexName":"HTR1D-HTR1B complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P28221;P28222","subunits.Entrez.IDs.":"3352;3351","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515","GO.description":"protein binding","FunCat.ID":"16.01","FunCat.description":"protein binding","PubMed.ID":11854302,"subunits.Protein.name.":"5-hydroxytryptamine receptor 1D;5-hydroxytryptamine receptor 1B","subunits.Gene.name.":"HTR1D;HTR1B","subunits.Gene.name.syn.":"HTR1DA HTRL;HTR1DB","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5418,"ComplexName":"GABBR2-HTR1A complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75899;P08908","subunits.Entrez.IDs.":"9568;3350","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515","GO.description":"protein binding","FunCat.ID":"16.01","FunCat.description":"protein binding","PubMed.ID":11854302,"subunits.Protein.name.":"Gamma-aminobutyric acid type B receptor subunit 2;5-hydroxytryptamine receptor 1A","subunits.Gene.name.":"GABBR2;HTR1A","subunits.Gene.name.syn.":"GPR51 GPRC3B;ADRB2RL1 ADRBRL1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5419,"ComplexName":"HTR1A-GPR26 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P08908;Q8NDV2","subunits.Entrez.IDs.":"3350;2849","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515","GO.description":"protein binding","FunCat.ID":"16.01","FunCat.description":"protein binding","PubMed.ID":11854302,"subunits.Protein.name.":"5-hydroxytryptamine receptor 1A;G-protein coupled receptor 26","subunits.Gene.name.":"HTR1A;GPR26","subunits.Gene.name.syn.":"ADRB2RL1 ADRBRL1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5420,"ComplexName":"HTR1A-EDG3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P08908;Q99500","subunits.Entrez.IDs.":"3350;1903","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515","GO.description":"protein binding","FunCat.ID":"16.01","FunCat.description":"protein binding","PubMed.ID":11854302,"subunits.Protein.name.":"5-hydroxytryptamine receptor 1A;Sphingosine 1-phosphate receptor 3","subunits.Gene.name.":"HTR1A;S1PR3","subunits.Gene.name.syn.":"ADRB2RL1 ADRBRL1;EDG3, S1P3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5421,"ComplexName":"HTR1A homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P08908","subunits.Entrez.IDs.":"3350","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005515","GO.description":"protein binding","FunCat.ID":"16.01","FunCat.description":"protein binding","PubMed.ID":11854302,"subunits.Protein.name.":"5-hydroxytryptamine receptor 1A","subunits.Gene.name.":"HTR1A","subunits.Gene.name.syn.":"ADRB2RL1 ADRBRL1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":5422,"ComplexName":"HTR1A-S1PR1 complex","Organism":"Human","Synonyms":"HTR1A-EDG1 complex","Cell.line":"None","subunits.UniProt.IDs.":"P08908;P21453","subunits.Entrez.IDs.":"3350;1901","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007186","GO.description":"G-protein coupled receptor signaling pathway","FunCat.ID":"30.05.02.24","FunCat.description":"G-protein coupled receptor signalling pathway","PubMed.ID":11854302,"subunits.Protein.name.":"5-hydroxytryptamine receptor 1A;Sphingosine 1-phosphate receptor 1","subunits.Gene.name.":"HTR1A;S1PR1","subunits.Gene.name.syn.":"ADRB2RL1 ADRBRL1;CHEDG1, EDG1, S1P1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5423,"ComplexName":"HSP70-BAG5-PARK2 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"O60260;P0DMV8;P34932;Q9UL15","subunits.Entrez.IDs.":"5071;3303;3308;9529","Protein.complex.purification.method":"MI:0096-pull down;MI:0019-coimmunoprecipitation","GO.ID":"GO:0050821;GO:0006457;GO:0030234;GO:0050790","GO.description":"protein stabilization;protein folding;enzyme regulator activity;regulation of catalytic activity","FunCat.ID":"14.01;18.02.01","FunCat.description":"protein folding and stabilization;enzymatic activity regulation / enzyme regulator","PubMed.ID":15603737,"subunits.Protein.name.":"E3 ubiquitin-protein ligase parkin;Heat shock 70 kDa protein 1A;Heat shock 70 kDa protein 4;BAG family molecular chaperone regulator 5","subunits.Gene.name.":"PARK2;HSPA1A;HSPA4;BAG5","subunits.Gene.name.syn.":"PRKN;HSPA1, HSX70, HSP70-1A;APG2;KIAA0873","Disease.comment":"None","Subunits.comment":"Since the authors did not specify HSP70, we used isoform HSPA1A (HSP70-1A).","Complex.comment":"The authors show that within this complex, BAG5 inhibits both parkin E3 ubiquitin ligase activity and Hsp70-mediated refolding of misfolded proteins.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5424,"ComplexName":"NGF-p75 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P01138;P08138","subunits.Entrez.IDs.":"4803;4804","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0007169;GO:0022008;GO:0048699;GO:0007399","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway;neurogenesis;generation of neurons;nervous system development","FunCat.ID":"30.05.01.12;41.05.13;47.03.01","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways;neurogenesis;nervous system","PubMed.ID":15131306,"subunits.Protein.name.":"Beta-nerve growth factor ;Tumor necrosis factor receptor superfamily member 16","subunits.Gene.name.":"NGF;NGFR","subunits.Gene.name.syn.":"NGFB;TNFRSF16","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The complex is composed of an NGF homodimer asymmetrically bound to a single p75.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5426,"ComplexName":"ANCO1-HDAC3  complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15379;Q6UB99","subunits.Entrez.IDs.":"8841;29123","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0096- pull down; MI:0018- two hybrid","GO.ID":"GO:0045892","GO.description":"negative regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.03","FunCat.description":"transcription repression","PubMed.ID":15184363,"subunits.Protein.name.":"Histone deacetylase 3;Ankyrin repeat domain-containing protein 11","subunits.Gene.name.":"HDAC3;ANKRD11","subunits.Gene.name.syn.":"None;ANCO1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5432,"ComplexName":"Sororin-cohesin complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60216;Q14683;Q29RF7;Q96FF9;Q9NTI5;Q9UQE7","subunits.Entrez.IDs.":"5885;8243;23244;113130;23047;9126","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0000278;GO:0007059;GO:0005634","GO.description":"mitotic cell cycle;chromosome segregation;nucleus","FunCat.ID":"10.03.01.01;10.03.04.05;70.10","FunCat.description":"mitotic cell cycle;chromosome segregation/division;nucleus","PubMed.ID":15837422,"subunits.Protein.name.":"Double-strand-break repair protein rad21 homolog ;Structural maintenance of chromosomes protein 1A ;Sister chromatid cohesion protein PDS5 homolog A ;Sororin ;Sister chromatid cohesion protein PDS5 homolog B ;Structural maintenance of chromosomes protein 3","subunits.Gene.name.":"RAD21;SMC1A;PDS5A;CDCA5;PDS5B;SMC3","subunits.Gene.name.syn.":"HR21 KIAA0078 NXP1;DXS423E KIAA0178 SB1.8 SMC1 SMC1L1;KIAA0648 PDS5;;APRIN AS3 KIAA0979;BAM BMH CSPG6 SMC3L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Sororin interacts with the cohesin complex. It regulates the ability of the cohesin complex to mediate sister chromatid cohesion.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5435,"ComplexName":"CycD1-Cdk4 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"NIH 3T3 cells","subunits.UniProt.IDs.":"P25322;P30285","subunits.Entrez.IDs.":"12443;12567","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0000278;GO:0051726","GO.description":"mitotic cell cycle;regulation of cell cycle","FunCat.ID":"10.03.01.01;10.03.01","FunCat.description":"mitotic cell cycle;mitotic cell cycle and cell cycle control","PubMed.ID":12588994,"subunits.Protein.name.":"G1/S-specific cyclin-D1;Cyclin-dependent kinase 4","subunits.Gene.name.":"Ccnd1;Cdk4","subunits.Gene.name.syn.":"Cyl-1;Crk3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5436,"ComplexName":"Cyclin D1-associated protein complex","Organism":"Mouse","Synonyms":"None","Cell.line":"NIH 3T3 cells","subunits.UniProt.IDs.":"P17879;P25322;P30285;P39689","subunits.Entrez.IDs.":"15511;12443;12567;12575","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0000080","GO.description":"mitotic G1 phase","FunCat.ID":"10.03.01.01.01","FunCat.description":"G1 phase of mitotic cell cycle","PubMed.ID":12588994,"subunits.Protein.name.":"Heat shock 70 kDa protein 1B ;G1/S-specific cyclin-D1;Cyclin-dependent kinase 4 ;Cyclin-dependent kinase inhibitor 1","subunits.Gene.name.":"Hspa1b;Ccnd1;Cdk4;Cdkn1a","subunits.Gene.name.syn.":"Hcp70.1 Hsp70-1 Hsp70a1 Hspa1;Cyl-1;Crk3;Cip1 Waf1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Hsc70 functions in the maturation of cyclin D1, thereby facilitating the assembly of an active CyclinD1-CDK4 holoenzyme.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5439,"ComplexName":"Eya1/3-Dach1/2-Six1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"C2C12 cells","subunits.UniProt.IDs.":"P97767;Q62231;Q9QYB2","subunits.Entrez.IDs.":"14048;20471;13134","Protein.complex.purification.method":"MI:0402-chromatin immunoprecipitation assays","GO.ID":"GO:0006355;GO:0003677;GO:0005634;GO:0048513","GO.description":"regulation of transcription, DNA-templated;DNA binding;nucleus;animal organ development","FunCat.ID":"11.02.03.04;16.03.01;70.10","FunCat.description":"transcriptional control;DNA binding;nucleus","PubMed.ID":14628042,"subunits.Protein.name.":"Eyes absent homolog 1;Homeobox protein SIX1;Dachshund homolog 1","subunits.Gene.name.":"Eya1;Six1;Dach1","subunits.Gene.name.syn.":"None;None;Dach","Disease.comment":"None","Subunits.comment":"Since the authors did not specify Dach as well as Eya, we used isoform Dach1 and isoform Eya1, respectively..","Complex.comment":"Two-step chip assay using either specific anti-Six1 IgG or anti-Eya1/3 IgG, indicating that Dach1/2 is co-recruited along with Six1 and Eya1/3, respectively, onto the c-Myc promoter.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5441,"ComplexName":"NRG1-IKZF4 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q02297;Q9H2S9","subunits.Entrez.IDs.":"3084;64375","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":15494726,"subunits.Protein.name.":"Pro-neuregulin-1, membrane-bound isoform ;Zinc finger protein Eos","subunits.Gene.name.":"NRG1;IKZF4","subunits.Gene.name.syn.":"GGF HGL HRGA NDF SMDF;KIAA1782 ZNFN1A4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The Nrg-ICD-Eos complex induces endogenous PSD-95 expression in vivo through a signaling pathway that is mostly independent of gamma-secretase regulation. This upregulation of PSD-95 expression by the Nrg-ICD-Eos complex provides a molecular basis for activity-dependent synaptic plasticity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5442,"ComplexName":"EPOR receptor complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P19235","subunits.Entrez.IDs.":"2057","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0005515","GO.description":"protein binding","FunCat.ID":"16.01","FunCat.description":"protein binding","PubMed.ID":8662530,"subunits.Protein.name.":"Erythropoietin receptor","subunits.Gene.name.":"EPOR","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":5444,"ComplexName":"CRKII-C3G complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P46108;Q13905","subunits.Entrez.IDs.":"1398;2889","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0007186","GO.description":"G-protein coupled receptor signaling pathway","FunCat.ID":"30.05.02.24","FunCat.description":"G-protein coupled receptor signalling pathway","PubMed.ID":9564038,"subunits.Protein.name.":"Adapter molecule crk;Rap guanine nucleotide exchange factor 1","subunits.Gene.name.":"CRK;RAPGEF1","subunits.Gene.name.syn.":"None;GRF2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5446,"ComplexName":"EPO-EPOR complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P01588;P19235","subunits.Entrez.IDs.":"2056;2057","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":9774108,"subunits.Protein.name.":"Erythropoietin ;Erythropoietin receptor","subunits.Gene.name.":"EPO;EPOR","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5447,"ComplexName":"Grin2a-Lrp8 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P35436;Q924X6","subunits.Entrez.IDs.":"14811;16975","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007268","GO.description":"synaptic transmission","FunCat.ID":"34.03.01","FunCat.description":"synaptic transmission","PubMed.ID":16102539,"subunits.Protein.name.":"Glutamate receptor ionotropic, NMDA 2A ;Low-density lipoprotein receptor-related protein 8","subunits.Gene.name.":"Grin2a;Lrp8","subunits.Gene.name.syn.":";Apoer2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5448,"ComplexName":"Grin2b-Lrp8 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q01097;Q924X6","subunits.Entrez.IDs.":"14812;16975","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007268","GO.description":"synaptic transmission","FunCat.ID":"34.03.01","FunCat.description":"synaptic transmission","PubMed.ID":16102539,"subunits.Protein.name.":"Glutamate receptor ionotropic, NMDA 2B;Low-density lipoprotein receptor-related protein 8","subunits.Gene.name.":"Grin2b;Lrp8","subunits.Gene.name.syn.":"NR2B;Apoer2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5449,"ComplexName":"Splicing-associated factors complex","Organism":"Human","Synonyms":"-20/24 complex","Cell.line":"None","subunits.UniProt.IDs.":"P35659;Q15287;Q86V81;Q8IYB3;Q9Y5S9","subunits.Entrez.IDs.":"7913;10921;10189;10250;9939","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008380;GO:0003723;GO:0005634","GO.description":"RNA splicing;RNA binding;nucleus","FunCat.ID":"11.04.03.01;16.03.03;70.10","FunCat.description":"splicing;RNA binding;nucleus","PubMed.ID":11118221,"subunits.Protein.name.":"Protein DEK;RNA-binding protein with serine-rich domain 1 ;THO complex subunit 4 ;Serine/arginine repetitive matrix protein 1 ;RNA-binding protein 8A","subunits.Gene.name.":"DEK;RNPS1;ALYREF;SRRM1;RBM8A","subunits.Gene.name.syn.":";LDC2;ALY BEF THOC4;SRM160;RBM8, Y14","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5450,"ComplexName":"Mediator complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"A0JLT2;O43513;O60244;O60313;O75448;O75586;O95402;Q13503;Q15528;Q15648;Q6P2C8;Q71F56;Q71SY5;Q96G25;Q96HR3;Q96RN5;Q9BTT4;Q9BUE0;Q9H944;Q9NPJ6;Q9NVC6;Q9NX70;Q9P086;Q9UHV7;Q9ULK4;Q9Y2X0;Q9Y3C7","subunits.Entrez.IDs.":"219541;9443;9282;4976;9862;10001;9441;9412;6837;5469;9442;23389;81857;112950;90390;51586;84246;54797;9477;29079;9440;55588;400569;9969;9439;10025;51003","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0045893;GO:0005515;GO:0051098;GO:0051090;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;protein binding;regulation of binding;regulation of sequence-specific DNA binding transcription factor activity;nucleus","FunCat.ID":"11.02.03.04.01;16.01;18.01.07;18.02.09;70.10","FunCat.description":"transcription activation;protein binding;regulation by binding / dissociation;regulator of transcription factor;nucleus","PubMed.ID":14576168,"subunits.Protein.name.":"Mediator of RNA polymerase II transcription subunit 19 ;Mediator of RNA polymerase II transcription subunit 7 ;Mediator of RNA polymerase II transcription subunit 14;Dynamin-like 120 kDa protein, mitochondrial ;Mediator of RNA polymerase II transcription subunit 24;Mediator of RNA polymerase II transcription subunit 6 ;Mediator of RNA polymerase II transcription subunit 26 ;Mediator of RNA polymerase II transcription subunit 21;Mediator of RNA polymerase II transcription subunit 22 ;Mediator of RNA polymerase II transcription subunit 1;Mediator of RNA polymerase II transcription subunit 27 ;Mediator of RNA polymerase II transcription subunit 13-like ;Mediator of RNA polymerase II transcription subunit 25 ;Mediator of RNA polymerase II transcription subunit 8 ;Mediator of RNA polymerase II transcription subunit 30 ;Mediator of RNA polymerase II transcription subunit 15;Mediator of RNA polymerase II transcription subunit 10 ;Mediator of RNA polymerase II transcription subunit 18 ;Mediator of RNA polymerase II transcription subunit 20 ;Mediator of RNA polymerase II transcription subunit 4 ;Mediator of RNA polymerase II transcription subunit 17;Mediator of RNA polymerase II transcription subunit 29 ;Mediator of RNA polymerase II transcription subunit 11 ;Mediator of RNA polymerase II transcription subunit 13 ;Mediator of RNA polymerase II transcription subunit 23 ;Mediator of RNA polymerase II transcription subunit 16;Mediator of RNA polymerase II transcription subunit 31","subunits.Gene.name.":"MED19;MED7;MED14;OPA1;MED24;MED6;MED26;MED21;MED22;MED1;MED27;MED13L;MED25;MED8;MED30;MED15;MED10;MED18;MED20;MED4;MED17;MED29;MED11;MED13;MED23;MED16;MED31","subunits.Gene.name.syn.":"LCMR1;ARC34 CRSP9;ARC150 CRSP2 CXorf4 DRIP150 EXLM1 RGR1 TRAP170;KIAA0567;ARC100 CRSP4 DRIP100 KIAA0130 THRAP4 TRAP100;ARC33;ARC70 CRSP7;SRB7 SURB7;SURF5;ARC205 CRSP1 CRSP200 DRIP205 DRIP230 PBP PPARBP PPARGBP RB18A TRAP220 TRIP2;CRSP34 CRSP8;KIAA1025 PROSIT240 THRAP2 TRAP240L;ACID1 ARC92 PTOV2;;THRAP6 TRAP25;ARC105 CTG7A PCQAP TIG1 TNRC7;;;TRFP;ARC36 DRIP36 VDRIP;ARC77 CRSP6 DRIP77 DRIP80 TRAP80;IXL;;ARC250 KIAA0593 THRAP1 TRAP240;ARC130 CRSP3 DRIP130 KIAA1216 SUR2;DRIP92 THRAP5;SOH1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5451,"ComplexName":"MED18-MED20-MED29 mediator subcomplex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q9BUE0;Q9H944;Q9NX70","subunits.Entrez.IDs.":"54797;9477;55588","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0045893;GO:0005515;GO:0051098;GO:0051090;GO:0005634","GO.description":"positive regulation of transcription, DNA-templated;protein binding;regulation of binding;regulation of sequence-specific DNA binding transcription factor activity;nucleus","FunCat.ID":"11.02.03.04.01;16.01;18.01.07;18.02.09;70.10","FunCat.description":"transcription activation;protein binding;regulation by binding / dissociation;regulator of transcription factor;nucleus","PubMed.ID":14576168,"subunits.Protein.name.":"Mediator of RNA polymerase II transcription subunit 18 ;Mediator of RNA polymerase II transcription subunit 20 ;Mediator of RNA polymerase II transcription subunit 29","subunits.Gene.name.":"MED18;MED20;MED29","subunits.Gene.name.syn.":";TRFP;IXL","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5452,"ComplexName":"Foxo4-Srf-Myocd complex","Organism":"Mouse","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"Q8VIM5;Q9JM73;Q9WVH3","subunits.Entrez.IDs.":"214384;20807;54601","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0048745","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;smooth muscle tissue development","FunCat.ID":"11.02.03.04;45.03.12.02","FunCat.description":"transcriptional control;smooth muscle","PubMed.ID":16054032,"subunits.Protein.name.":"Myocardin ;Serum response factor;Forkhead box protein O4","subunits.Gene.name.":"Myocd;Srf;Foxo4","subunits.Gene.name.syn.":"Bsac2 Mycd Srfcp;None;Afx Afx1 Fkhr3 Mllt7","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors conclude that signal-dependent interaction of Foxo4 with myocardin couples extracellular signals with the transcriptional program for SMC differentiation.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5459,"ComplexName":"Axin2-Ctnnb1-Apc complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O88566;Q02248;Q61315","subunits.Entrez.IDs.":"12006;12387;11789","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016055","GO.description":"Wnt signaling pathway","FunCat.ID":"30.05.02.20","FunCat.description":"Wnt signalling pathway","PubMed.ID":9554852,"subunits.Protein.name.":"Axin-2 ;Catenin beta-1;Adenomatous polyposis coli protein","subunits.Gene.name.":"Axin2;Ctnnb1;Apc","subunits.Gene.name.syn.":";Catnb;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors suggest that the assembly of a multiprotein complex by conductin controls the stability of b-catenin.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5460,"ComplexName":"p50-p65 NF(kappa)B complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P19838;Q04206","subunits.Entrez.IDs.":"4790;5970","Protein.complex.purification.method":"MI:0018- two hybrid","GO.ID":"GO:0045893;GO:0007249","GO.description":"positive regulation of transcription, DNA-templated;I-kappaB kinase/NF-kappaB signaling","FunCat.ID":"11.02.03.04.01;30.01.05.01.04","FunCat.description":"transcription activation;NIK-I-kappaB/NF-kappaB cascade","PubMed.ID":9556555,"subunits.Protein.name.":"Nuclear factor NF-kappa-B p105 subunit;Transcription factor p65","subunits.Gene.name.":"NFKB1;RELA","subunits.Gene.name.syn.":"None;NFKB3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5461,"ComplexName":"p50-p65 NF(kappa)B-SRC1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P19838;Q04206;Q15788","subunits.Entrez.IDs.":"4790;5970;8648","Protein.complex.purification.method":"MI:0018- two hybrid","GO.ID":"GO:0045893;GO:0007249","GO.description":"positive regulation of transcription, DNA-templated;I-kappaB kinase/NF-kappaB signaling","FunCat.ID":"11.02.03.04.01;30.01.05.01.04","FunCat.description":"transcription activation;NIK-I-kappaB/NF-kappaB cascade","PubMed.ID":9556555,"subunits.Protein.name.":"Nuclear factor NF-kappa-B p105 subunit;Transcription factor p65;Nuclear receptor coactivator 1","subunits.Gene.name.":"NFKB1;RELA;NCOA1","subunits.Gene.name.syn.":"None;NFKB3;BHLHE74, SRC1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SRC-1 potentiates NF(kappa)B transactivation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5464,"ComplexName":"I(kappa)B(alpha)-NF(kappa)Bp50-NF(kappa)Bp65 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P19838;P25963;Q04206","subunits.Entrez.IDs.":"4790;4792;5970","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007249;GO:0023052;GO:0005737","GO.description":"I-kappaB kinase/NF-kappaB signaling;signaling;cytoplasm","FunCat.ID":"30.01.05.01.04;30.01;70.03","FunCat.description":"NIK-I-kappaB/NF-kappaB cascade;cellular signalling;cytoplasm","PubMed.ID":9738011,"subunits.Protein.name.":"Nuclear factor NF-kappa-B p105 subunit;NF-kappa-B inhibitor alpha ;Transcription factor p65","subunits.Gene.name.":"NFKB1;NFKBIA;RELA","subunits.Gene.name.syn.":"None;IKBA MAD3 NFKBI;NFKB3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"I(kappa)B(alpha) inhibits DNA binding activity of NF(kappa)B heterodimer.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5465,"ComplexName":"IKB(epsilon)-RELA-cREL complex","Organism":"Human","Synonyms":"None","Cell.line":"Jurkat cells","subunits.UniProt.IDs.":"O00221;Q04206;Q04864","subunits.Entrez.IDs.":"4794;5970;5966","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0007249;GO:0005737","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;I-kappaB kinase/NF-kappaB signaling;cytoplasm","FunCat.ID":"11.02.03.04;30.01.05.01.04;70.03","FunCat.description":"transcriptional control;NIK-I-kappaB/NF-kappaB cascade;cytoplasm","PubMed.ID":9135156,"subunits.Protein.name.":"NF-kappa-B inhibitor epsilon ;Transcription factor p65;Proto-oncogene c-Rel","subunits.Gene.name.":"NFKBIE;RELA;REL","subunits.Gene.name.syn.":"IKBE;NFKB3;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"IKB(epsilon) is able to inhibit NF(kappa)B-directed transactivation via cytoplasmic retention of rel proteins.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5466,"ComplexName":"IKB(beta)-RELA-cREL complex","Organism":"Human","Synonyms":"None","Cell.line":"Jurkat cells","subunits.UniProt.IDs.":"Q04206;Q04864;Q15653","subunits.Entrez.IDs.":"5970;5966;4793","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0007249;GO:0005737","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;I-kappaB kinase/NF-kappaB signaling;cytoplasm","FunCat.ID":"11.02.03.04;30.01.05.01.04;70.03","FunCat.description":"transcriptional control;NIK-I-kappaB/NF-kappaB cascade;cytoplasm","PubMed.ID":9135156,"subunits.Protein.name.":"Transcription factor p65;Proto-oncogene c-Rel;NF-kappa-B inhibitor beta","subunits.Gene.name.":"RELA;REL;NFKBIB","subunits.Gene.name.syn.":"NFKB3;;IKBB TRIP9","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5467,"ComplexName":"IKB(alpha)-RELA-cREL complex","Organism":"Human","Synonyms":"None","Cell.line":"Jurkat cells","subunits.UniProt.IDs.":"P25963;Q04206;Q04864","subunits.Entrez.IDs.":"4792;5970;5966","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0007249;GO:0023052;GO:0005737","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;I-kappaB kinase/NF-kappaB signaling;signaling;cytoplasm","FunCat.ID":"11.02.03.04;30.01.05.01.04;30.01;70.03","FunCat.description":"transcriptional control;NIK-I-kappaB/NF-kappaB cascade;cellular signalling;cytoplasm","PubMed.ID":9135156,"subunits.Protein.name.":"NF-kappa-B inhibitor alpha ;Transcription factor p65;Proto-oncogene c-Rel","subunits.Gene.name.":"NFKBIA;RELA;REL","subunits.Gene.name.syn.":"IKBA MAD3 NFKBI;NFKB3;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5473,"ComplexName":"FAS-FADD-CASP8 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P25445;Q13158;Q14790","subunits.Entrez.IDs.":"355;8772;841","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006915","GO.description":"apoptotic process","FunCat.ID":"40.10.02","FunCat.description":"apoptosis (type I programmed cell death)","PubMed.ID":15383280,"subunits.Protein.name.":"Tumor necrosis factor receptor superfamily member 6 ;FAS-associated death domain protein;Caspase-8","subunits.Gene.name.":"FAS;FADD;CASP8","subunits.Gene.name.syn.":"APT1 FAS1 TNFRSF6;MORT1;MCH5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5475,"ComplexName":"MURR1-NF(kappa)Bp65-IKBA complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P25963;Q04206;Q8N668","subunits.Entrez.IDs.":"4792;5970;150684","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0007249","GO.description":"I-kappaB kinase/NF-kappaB signaling","FunCat.ID":"30.01.05.01.04","FunCat.description":"NIK-I-kappaB/NF-kappaB cascade","PubMed.ID":14685242,"subunits.Protein.name.":"NF-kappa-B inhibitor alpha ;Transcription factor p65;COMM domain-containing protein 1","subunits.Gene.name.":"NFKBIA;RELA;COMMD1","subunits.Gene.name.syn.":"IKBA MAD3 NFKBI;NFKB3;C2orf5, MURR1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Murr1, a gene product known previously for its involvement in copper regulation, inhibits HIV-1 growth in unstimulated CD4+ T cells. This inhibition was mediated in part through its ability to inhibit basal and cytokine-stimulated nuclear factor NF(kappa)B activity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5492,"ComplexName":"IKBA-NF(kappa)Bp65-NF(kappa)Bp50 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P19838;P25963;Q04206","subunits.Entrez.IDs.":"4790;4792;5970","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007249;GO:0023052;GO:0005737","GO.description":"I-kappaB kinase/NF-kappaB signaling;signaling;cytoplasm","FunCat.ID":"30.01.05.01.04;30.01;70.03","FunCat.description":"NIK-I-kappaB/NF-kappaB cascade;cellular signalling;cytoplasm","PubMed.ID":12972430,"subunits.Protein.name.":"Nuclear factor NF-kappa-B p105 subunit;NF-kappa-B inhibitor alpha ;Transcription factor p65","subunits.Gene.name.":"NFKB1;NFKBIA;RELA","subunits.Gene.name.syn.":"None;IKBA MAD3 NFKBI;NFKB3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5493,"ComplexName":"Tmsb4x-Lims1-Ilk complex","Organism":"Mouse","Synonyms":"None","Cell.line":"COS-1 cells, 10T1/2 cells, heart muscle","subunits.UniProt.IDs.":"O55222;P20065;Q99JW4","subunits.Entrez.IDs.":"16202;19241;110829","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0016477;GO:0050896","GO.description":"cell migration;response to stimulus","FunCat.ID":"34.05.01;36.25","FunCat.description":"cell migration;animal specific systemic sensing and response","PubMed.ID":15565145,"subunits.Protein.name.":"Integrin-linked protein kinase;Thymosin beta-4;LIM and senescent cell antigen-like-containing domain protein 1","subunits.Gene.name.":"Ilk;Tmsb4x;Lims1","subunits.Gene.name.syn.":"None;Ptmb4 Tmsb4;Pinch1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors showed that the LIM domain protein PINCH and ILK, both of which are necessary for cell migration and survival, formed a complex with thymosin beta4 that resulted in phosphorylation of the survival kinase Akt. Treatment of adult mice with thymosin beta4 after coronary ligation resulted in increased phosphorylation of Akt in the heart, enhanced early myocyte survival and improved cardiac function.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5495,"ComplexName":"TFIIH transcription factor complex (ERCC2, ERCC3, GTF2H1, CDK7, CCNH, GTF2H2)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P18074;P19447;P32780;P50613;P51946;Q13888","subunits.Entrez.IDs.":"2068;2071;2965;1022;902;2966","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006794;GO:0006796;GO:0006281;GO:0007049;GO:0006351;GO:2001141;GO:0006355;GO:0006464;GO:0030234;GO:0050790;GO:0005634","GO.description":"phosphorus utilization;phosphate-containing compound metabolic process;DNA repair;cell cycle;transcription, DNA-templated;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;cellular protein modification process;enzyme regulator activity;regulation of catalytic activity;nucleus","FunCat.ID":"01.04;10.01.05.01;10.03;11;11.02.03.04;14.07;18.02.01;70.10","FunCat.description":"phosphate metabolism;DNA repair;cell cycle;TRANSCRIPTION;transcriptional control;protein modification;enzymatic activity regulation / enzyme regulator;nucleus","PubMed.ID":12820975,"subunits.Protein.name.":"TFIIH basal transcription factor complex helicase XPD subunit ;TFIIH basal transcription factor complex helicase XPB subunit ;General transcription factor IIH subunit 1;Cyclin-dependent kinase 7 ;Cyclin-H ;General transcription factor IIH subunit 2","subunits.Gene.name.":"ERCC2;ERCC3;GTF2H1;CDK7;CCNH;GTF2H2","subunits.Gene.name.syn.":"XPD XPDC;XPB XPBC;BTF2;CAK CAK1 CDKN7 MO15 STK1;;BTF2P44","Disease.comment":"Xeroderma pigmentosum (XP); Trichothiodystrophy (TTD); Mutations in the XPD gene result in xeroderma pigmentosum (XP) and trichothiodystrophy (TTD), the phenotypes of which are often intricate.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5497,"ComplexName":"Thyroglobulin folding complex (Tg, Hspa5, Pdi, Erp29, Grp94)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06761;P06882;P20717;P52555;Q0R337","subunits.Entrez.IDs.":"25617;24826;29511;117030;362862","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0029- cosedimentation through density gradients; MI:0051- fluorescence technologies","GO.ID":"GO:0050821;GO:0006457","GO.description":"protein stabilization;protein folding","FunCat.ID":"14.01","FunCat.description":"protein folding and stabilization","PubMed.ID":11884402,"subunits.Protein.name.":"78 kDa glucose-regulated protein ;Thyroglobulin ;Protein-arginine deiminase type-2 ;Endoplasmic reticulum resident protein 29 ;Glucose-regulated protein 94","subunits.Gene.name.":"Hspa5;Tg;Padi2;Erp29;Grp94","subunits.Gene.name.syn.":"Grp78;;Pad2 Pdi Pdi2;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5498,"ComplexName":"ILK-PARVB-ARHGEF6 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"Q13418;Q15052;Q9HBI1","subunits.Entrez.IDs.":"3611;9459;29780","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0007264;GO:0030036","GO.description":"small GTPase mediated signal transduction;actin cytoskeleton organization","FunCat.ID":"30.01.05.05.01;42.04.03","FunCat.description":"small GTPase mediated signal transduction;actin cytoskeleton","PubMed.ID":15897874,"subunits.Protein.name.":"Integrin-linked protein kinase;Rho guanine nucleotide exchange factor 6 ;Beta-parvin","subunits.Gene.name.":"ILK;ARHGEF6;PARVB","subunits.Gene.name.syn.":"ILK1 ILK2;COOL2 KIAA0006 PIXA;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results suggest that activation of alpha-PIX is dependent on ILK binding to beta-parvin, an event that depends upon ILK activity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5499,"ComplexName":"PARVB-ARHGEF6 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"Q15052;Q9HBI1","subunits.Entrez.IDs.":"9459;29780","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0030036","GO.description":"actin cytoskeleton organization","FunCat.ID":"42.04.03","FunCat.description":"actin cytoskeleton","PubMed.ID":15897874,"subunits.Protein.name.":"Rho guanine nucleotide exchange factor 6 ;Beta-parvin","subunits.Gene.name.":"ARHGEF6;PARVB","subunits.Gene.name.syn.":"COOL2 KIAA0006 PIXA;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The complex between beta-parvin and alpha-PIX is constitutively formed and is not regulated by either the presence or absence of ILK or its kinase activity. This suggests that ILK may modulate the activity of alpha-PIX indirectly through its binding to and phosphorylation of beta-parvin.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5500,"ComplexName":"Thyroglobulin folding complex (Tg, Pdi, Erp29)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06882;P20717;P52555","subunits.Entrez.IDs.":"24826;29511;117030","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0050821;GO:0006457","GO.description":"protein stabilization;protein folding","FunCat.ID":"14.01","FunCat.description":"protein folding and stabilization","PubMed.ID":11884402,"subunits.Protein.name.":"Thyroglobulin ;Protein-arginine deiminase type-2 ;Endoplasmic reticulum resident protein 29","subunits.Gene.name.":"Tg;Padi2;Erp29","subunits.Gene.name.syn.":";Pad2 Pdi Pdi2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5501,"ComplexName":"Thyroglobulin folding complex (Tg, Hspa5, Erp29, Grp94)","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06761;P06882;P52555;Q0R337","subunits.Entrez.IDs.":"25617;24826;117030;362862","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0050821;GO:0006457","GO.description":"protein stabilization;protein folding","FunCat.ID":"14.01","FunCat.description":"protein folding and stabilization","PubMed.ID":11884402,"subunits.Protein.name.":"78 kDa glucose-regulated protein ;Thyroglobulin ;Endoplasmic reticulum resident protein 29 ;Glucose-regulated protein 94","subunits.Gene.name.":"Hspa5;Tg;Erp29;Grp94","subunits.Gene.name.syn.":"Grp78;;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5502,"ComplexName":"EED-EZH-YY1 polycomb complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75530;P25490;Q15910","subunits.Entrez.IDs.":"8726;7528;2146","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0045892;GO:0032774;GO:0003677;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;RNA biosynthetic process;DNA binding;nucleus","FunCat.ID":"11.02.03.04.03;11.02;16.03.01;70.10","FunCat.description":"transcription repression;RNA synthesis;DNA binding;nucleus","PubMed.ID":11158321,"subunits.Protein.name.":"Polycomb protein EED;Transcriptional repressor protein YY1;Histone-lysine N-methyltransferase EZH2","subunits.Gene.name.":"EED;YY1;EZH2","subunits.Gene.name.syn.":"None;INO80S;KMT6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5511,"ComplexName":"Tctex1-channel complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q02294;Q63100;Q9Z336","subunits.Entrez.IDs.":"257648;29564;83462","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0008324;GO:0006812;GO:0005216","GO.description":"cation transmembrane transporter activity;cation transport;ion channel activity","FunCat.ID":"20.01.01.01;20.03.01.01","FunCat.description":"cation transport (H+, Na+, K+, Ca2+ , NH4+, etc.);ion channels","PubMed.ID":15768038,"subunits.Protein.name.":"Voltage-dependent N-type calcium channel subunit alpha-1B;Cytoplasmic dynein 1 intermediate chain 1 ;Dynein light chain Tctex-type 1","subunits.Gene.name.":"Cacna1b;Dync1i1;Dynlt1","subunits.Gene.name.syn.":"Cach5 Cacnl1a5;Dnci1 Dncic1;Tctel1 Tctex-1 Tctex1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5513,"ComplexName":"Polycomb repressive complex","Organism":"Human","Synonyms":"hPc2-RING1-BMI1-HPH1 complex","Cell.line":"SW480 cells","subunits.UniProt.IDs.":"O00257;P35226;P78364;Q06587","subunits.Entrez.IDs.":"8535;648;1911;6015","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0045892;GO:0032774;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;RNA biosynthetic process;nucleus","FunCat.ID":"11.02.03.04.03;11.02;70.10","FunCat.description":"transcription repression;RNA synthesis;nucleus","PubMed.ID":9199346,"subunits.Protein.name.":"E3 SUMO-protein ligase CBX4;Polycomb complex protein BMI-1;Polyhomeotic-like protein 1;E3 ubiquitin-protein ligase RING1","subunits.Gene.name.":"CBX4;BMI1;PHC1;RING1","subunits.Gene.name.syn.":"None;PCGF4 RNF51;EDR1 PH1;RNF1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5518,"ComplexName":"BMI1-HPH1-HPH2 complex","Organism":"Human","Synonyms":"None","Cell.line":"U2OS cells","subunits.UniProt.IDs.":"P35226;P78364;Q8IXK0","subunits.Entrez.IDs.":"648;1911;1912","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0029- cosedimentation through density gradients","GO.ID":"GO:0045892;GO:0032774;GO:0003677;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;RNA biosynthetic process;DNA binding;nucleus","FunCat.ID":"11.02.03.04.03;11.02;16.03.01;70.10","FunCat.description":"transcription repression;RNA synthesis;DNA binding;nucleus","PubMed.ID":9121482,"subunits.Protein.name.":"Polycomb complex protein BMI-1;Polyhomeotic-like protein 1;Polyhomeotic-like protein 2","subunits.Gene.name.":"BMI1;PHC1;PHC2","subunits.Gene.name.syn.":"PCGF4 RNF51;EDR1 PH1;EDR2 PH2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5521,"ComplexName":"EED-EZH polycomb complex","Organism":"Human","Synonyms":"None","Cell.line":"U2OS cells","subunits.UniProt.IDs.":"O75530;Q15910","subunits.Entrez.IDs.":"8726;2146","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation; MI:0018- two hybrid","GO.ID":"GO:0045892;GO:0032774;GO:0003677;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;RNA biosynthetic process;DNA binding;nucleus","FunCat.ID":"11.02.03.04.03;11.02;16.03.01;70.10","FunCat.description":"transcription repression;RNA synthesis;DNA binding;nucleus","PubMed.ID":9584199,"subunits.Protein.name.":"Polycomb protein EED;Histone-lysine N-methyltransferase EZH2","subunits.Gene.name.":"EED;EZH2","subunits.Gene.name.syn.":"None;KMT6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5524,"ComplexName":"Bmi1-Mel18-Mph1-M33 polycomb repressor complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P23798;P25916;P30658;Q64028","subunits.Entrez.IDs.":"22658;12151;12416;13619","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045892;GO:0032774;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;RNA biosynthetic process;nucleus","FunCat.ID":"11.02.03.04.03;11.02;70.10","FunCat.description":"transcription repression;RNA synthesis;nucleus","PubMed.ID":9009205,"subunits.Protein.name.":"Polycomb group RING finger protein 2 ;Polycomb complex protein BMI-1 ;Chromobox protein homolog 2 ;Polyhomeotic-like protein 1","subunits.Gene.name.":"Pcgf2;Bmi1;Cbx2;Phc1","subunits.Gene.name.syn.":"Mel-18 Mel18 Rnf110 Zfp144 Znf144;Bmi-1 Pcgf4;M33;Edr Edr1 Rae28","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5526,"ComplexName":"CALM1-FKBP38-BCL2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P10415;P62158;Q14318","subunits.Entrez.IDs.":"596;None;23770","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005509;GO:0030234;GO:0050790;GO:0043067","GO.description":"calcium ion binding;enzyme regulator activity;regulation of catalytic activity;regulation of programmed cell death","FunCat.ID":"16.17.01;18.02.01;40.10.02.04","FunCat.description":"calcium binding;enzymatic activity regulation / enzyme regulator;regulation of apoptosis","PubMed.ID":15990872,"subunits.Protein.name.":"Apoptosis regulator Bcl-2;Calmodulin;Peptidyl-prolyl cis-trans isomerase FKBP8","subunits.Gene.name.":"BCL2;CALM1; CAL;FKBP8","subunits.Gene.name.syn.":"None;CALM, CAM, CAM1, CAM2, CAMB, CALML2, CAM3, CAMC, CAMIII;FKBP38","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5528,"ComplexName":"Homodimeric complex Adrb2","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P10608","subunits.Entrez.IDs.":"24176","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":15592462,"subunits.Protein.name.":"Beta-2 adrenergic receptor","subunits.Gene.name.":"Adrb2","subunits.Gene.name.syn.":"Adrb2r","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat)"}
{"ComplexID":5529,"ComplexName":"TRAF2-cIAP1/BIRC2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q12933;Q13490","subunits.Entrez.IDs.":"7186;329","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0006915","GO.description":"protein ubiquitination;protein deubiquitination;apoptotic process","FunCat.ID":"14.07.05;40.10.02","FunCat.description":"modification by ubiquitination, deubiquitination;apoptosis (type I programmed cell death)","PubMed.ID":15861135,"subunits.Protein.name.":"TNF receptor-associated factor 2;Baculoviral IAP repeat-containing protein 2","subunits.Gene.name.":"TRAF2;BIRC2","subunits.Gene.name.syn.":"TRAP3;API1 MIHB RNF48","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5530,"ComplexName":"Homodimeric complex LTBR","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P36941","subunits.Entrez.IDs.":"4055","Protein.complex.purification.method":"MI:0018- two hybrid","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":9371602,"subunits.Protein.name.":"Tumor necrosis factor receptor superfamily member 3","subunits.Gene.name.":"LTBR","subunits.Gene.name.syn.":"D12S370 TNFCR TNFR3 TNFRSF3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The viral HCV (hepatitis) core protein can associate with the dimeric oroligomeric form of LT-bR, and this protein-protein interaction has a modulatory effect on the signaling pathway of LT-bR in certain cell types.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":5531,"ComplexName":"Tumor necrosis factor receptor 1 signaling complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P19438;Q12933;Q13490;Q15628","subunits.Entrez.IDs.":"7132;7186;329;8717","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0023052;GO:0006915","GO.description":"signaling;apoptotic process","FunCat.ID":"30.01;40.10.02","FunCat.description":"cellular signalling;apoptosis (type I programmed cell death)","PubMed.ID":8943045,"subunits.Protein.name.":"Tumor necrosis factor receptor superfamily member 1A;TNF receptor-associated factor 2;Baculoviral IAP repeat-containing protein 2 ;Tumor necrosis factor receptor type 1-associated DEATH domain protein","subunits.Gene.name.":"TNFRSF1A;TRAF2;BIRC2;TRADD","subunits.Gene.name.syn.":"TNFAR, TNFR1;TRAP3;API1 MIHB RNF48;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5532,"ComplexName":"p35-Cdk5 complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P61810;Q03114","subunits.Entrez.IDs.":"116671;140908","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":8090221,"subunits.Protein.name.":"Cyclin-dependent kinase 5 activator 1 ;Cyclin-dependent-like kinase 5","subunits.Gene.name.":"Cdk5r1;Cdk5","subunits.Gene.name.syn.":"Cdk5r;Cdkn5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"p35 activates the Cdk5 kinase.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5533,"ComplexName":"p35-Cdk5 complex","Organism":"Bovine","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"Q02399;Q28199","subunits.Entrez.IDs.":"281066;282173","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":8090221,"subunits.Protein.name.":"Cyclin-dependent-like kinase 5 ;Cyclin-dependent kinase 5 activator 1","subunits.Gene.name.":"CDK5;CDK5R1","subunits.Gene.name.syn.":"CDKN5;CDK5R NCK5A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"p35 activates the Cdk5 kinase.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":5534,"ComplexName":"PLCB1-PARD3-PARD6A complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"Q8TEW0;Q9NPB6;Q9NQ66","subunits.Entrez.IDs.":"56288;50855;23236","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0023052;GO:0019932;GO:0051211;GO:0009798","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;signaling;second-messenger-mediated signaling;anisotropic cell growth;axis specification","FunCat.ID":"11.02.03.04;30.01;30.01.09;40.01.03;41.05.19","FunCat.description":"transcriptional control;cellular signalling;second messenger mediated signal transduction;directional cell growth (morphogenesis);asymmetries and axis determination","PubMed.ID":15782111,"subunits.Protein.name.":"Partitioning defective 3 homolog;Partitioning defective 6 homolog alpha;1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1","subunits.Gene.name.":"PARD3;PARD6A;PLCB1","subunits.Gene.name.syn.":"PAR3, PAR3A;PAR6A, PAR6;KIAA0581","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results suggest that the interaction of PLC-beta with cell polarity Par proteins may serve as a nexus to transduce extracellular signals to transcriptional regulation through G-protein-mediated signaling pathway in cell polarity and cell asymmetric division.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5535,"ComplexName":"PLCB3-PARD3-PARD6A complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"Q01970;Q8TEW0;Q9NPB6","subunits.Entrez.IDs.":"5331;56288;50855","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0023052;GO:0019932;GO:0051211;GO:0009798","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;signaling;second-messenger-mediated signaling;anisotropic cell growth;axis specification","FunCat.ID":"11.02.03.04;30.01;30.01.09;40.01.03;41.05.19","FunCat.description":"transcriptional control;cellular signalling;second messenger mediated signal transduction;directional cell growth (morphogenesis);asymmetries and axis determination","PubMed.ID":15782111,"subunits.Protein.name.":"1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3;Partitioning defective 3 homolog;Partitioning defective 6 homolog alpha","subunits.Gene.name.":"PLCB3;PARD3;PARD6A","subunits.Gene.name.syn.":"None;PAR3, PAR3A;PAR6A, PAR6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results suggest that the interaction of PLC-beta with cell polarity Par proteins may serve as a nexus to transduce extracellular signals to transcriptional regulation through G-protein-mediated signaling pathway in cell polarity and cell asymmetric division.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5540,"ComplexName":"TRAF2-TRADD complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q12933;Q15628","subunits.Entrez.IDs.":"7186;8717","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006915","GO.description":"apoptotic process","FunCat.ID":"40.10.02","FunCat.description":"apoptosis (type I programmed cell death)","PubMed.ID":12796506,"subunits.Protein.name.":"TNF receptor-associated factor 2;Tumor necrosis factor receptor type 1-associated DEATH domain protein","subunits.Gene.name.":"TRAF2;TRADD","subunits.Gene.name.syn.":"TRAP3;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TRADD and TRAF2 form a ternary complex  with the viral protein NS5A.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5541,"ComplexName":"Ternary complex (TRAF2, FADD, TRADD)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q12933;Q13158;Q15628","subunits.Entrez.IDs.":"7186;8772;8717","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006915","GO.description":"apoptotic process","FunCat.ID":"40.10.02","FunCat.description":"apoptosis (type I programmed cell death)","PubMed.ID":12796506,"subunits.Protein.name.":"TNF receptor-associated factor 2;FAS-associated death domain protein;Tumor necrosis factor receptor type 1-associated DEATH domain protein","subunits.Gene.name.":"TRAF2;FADD;TRADD","subunits.Gene.name.syn.":"TRAP3;MORT1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5542,"ComplexName":"CCNB2-CDC2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95067;P06493","subunits.Entrez.IDs.":"9133;983","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007049","GO.description":"cell cycle","FunCat.ID":"10.03","FunCat.description":"cell cycle","PubMed.ID":8070405,"subunits.Protein.name.":"G2/mitotic-specific cyclin-B2;Cyclin-dependent kinase 1","subunits.Gene.name.":"CCNB2;CDK1","subunits.Gene.name.syn.":";CDC2 CDC28A CDKN1 P34CDC2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5543,"ComplexName":"CCNB1-CDC2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06493;P14635","subunits.Entrez.IDs.":"983;891","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007049","GO.description":"cell cycle","FunCat.ID":"10.03","FunCat.description":"cell cycle","PubMed.ID":8070405,"subunits.Protein.name.":"Cyclin-dependent kinase 1 ;G2/mitotic-specific cyclin-B1","subunits.Gene.name.":"CDK1;CCNB1","subunits.Gene.name.syn.":"CDC2 CDC28A CDKN1 P34CDC2;CCNB","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5544,"ComplexName":"CDC2-PCNA-CCNB1-GADD45A complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06493;P12004;P14635;P24522","subunits.Entrez.IDs.":"983;5111;891;1647","Protein.complex.purification.method":"MI:0096- pull down; MI:0019- coimmunoprecipitation","GO.ID":"GO:0007049","GO.description":"cell cycle","FunCat.ID":"10.03","FunCat.description":"cell cycle","PubMed.ID":12124778,"subunits.Protein.name.":"Cyclin-dependent kinase 1 ;Proliferating cell nuclear antigen;G2/mitotic-specific cyclin-B1;Growth arrest and DNA damage-inducible protein GADD45 alpha","subunits.Gene.name.":"CDK1;PCNA;CCNB1;GADD45A","subunits.Gene.name.syn.":"CDC2 CDC28A CDKN1 P34CDC2;None;CCNB;DDIT1 GADD45","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5545,"ComplexName":"CDC2-PCNA-CCNB1-GADD45B complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75293;P06493;P12004;P14635","subunits.Entrez.IDs.":"4616;983;5111;891","Protein.complex.purification.method":"MI:0096- pull down; MI:0019- coimmunoprecipitation","GO.ID":"GO:0007049","GO.description":"cell cycle","FunCat.ID":"10.03","FunCat.description":"cell cycle","PubMed.ID":12124778,"subunits.Protein.name.":"Growth arrest and DNA damage-inducible protein GADD45 beta ;Cyclin-dependent kinase 1 ;Proliferating cell nuclear antigen;G2/mitotic-specific cyclin-B1","subunits.Gene.name.":"GADD45B;CDK1;PCNA;CCNB1","subunits.Gene.name.syn.":"MYD118;CDC2 CDC28A CDKN1 P34CDC2;None;CCNB","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5546,"ComplexName":"CDC2-PCNA-CCNB1-GADD45G complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95257;P06493;P12004;P14635","subunits.Entrez.IDs.":"10912;983;5111;891","Protein.complex.purification.method":"MI:0096- pull down; MI:0019- coimmunoprecipitation","GO.ID":"GO:0007049","GO.description":"cell cycle","FunCat.ID":"10.03","FunCat.description":"cell cycle","PubMed.ID":12124778,"subunits.Protein.name.":"Growth arrest and DNA damage-inducible protein GADD45 gamma ;Cyclin-dependent kinase 1 ;Proliferating cell nuclear antigen;G2/mitotic-specific cyclin-B1","subunits.Gene.name.":"GADD45G;CDK1;PCNA;CCNB1","subunits.Gene.name.syn.":"CR6 DDIT2;CDC2 CDC28A CDKN1 P34CDC2;None;CCNB","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5547,"ComplexName":"Cdc2-Ccnb1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P11440;P24860","subunits.Entrez.IDs.":"12534;268697","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0007049","GO.description":"cell cycle","FunCat.ID":"10.03","FunCat.description":"cell cycle","PubMed.ID":12124778,"subunits.Protein.name.":"Cyclin-dependent kinase 1 ;G2/mitotic-specific cyclin-B1","subunits.Gene.name.":"Cdk1;Ccnb1","subunits.Gene.name.syn.":"Cdc2 Cdc2a Cdkn1;Ccn-2 Ccnb1-rs13 Cycb Cycb1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5548,"ComplexName":"IL-12 heterodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"P29459;P29460","subunits.Entrez.IDs.":"3592;3593","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030217","GO.description":"T cell differentiation","FunCat.ID":"43.03.07.02.01.02","FunCat.description":"T-cell","PubMed.ID":7527811,"subunits.Protein.name.":"Interleukin-12 subunit alpha ;Interleukin-12 subunit beta","subunits.Gene.name.":"IL12A;IL12B","subunits.Gene.name.syn.":"NKSF1;NKSF2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors demonstrated that when p40 is associated with a p35 subunit, the heterodimer acts as an agonist mediating biologic activity, and when p40 associates with another p40, the homodimer behaves as an antagonist in vitro.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5549,"ComplexName":"IL-12 subunit p40 homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"P29460","subunits.Entrez.IDs.":"3593","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0071- molecular sieving","GO.ID":"GO:0030217","GO.description":"T cell differentiation","FunCat.ID":"43.03.07.02.01.02","FunCat.description":"T-cell","PubMed.ID":7527811,"subunits.Protein.name.":"Interleukin-12 subunit beta","subunits.Gene.name.":"IL12B","subunits.Gene.name.syn.":"NKSF2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors demonstrated that when p40 is associated with a p35 subunit, the heterodimer acts as an agonist mediating biologic activity, and when p40 associates with another p40, the homodimer behaves as an antagonist in vitro.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":5550,"ComplexName":"CDC2-CCNB1-CCNF complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06493;P14635;P41002","subunits.Entrez.IDs.":"983;891;899","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007049","GO.description":"cell cycle","FunCat.ID":"10.03","FunCat.description":"cell cycle","PubMed.ID":10716937,"subunits.Protein.name.":"Cyclin-dependent kinase 1 ;G2/mitotic-specific cyclin-B1;Cyclin-F","subunits.Gene.name.":"CDK1;CCNB1;CCNF","subunits.Gene.name.syn.":"CDC2 CDC28A CDKN1 P34CDC2;CCNB;FBX1 FBXO1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cdc2, cyclin B1 and cyclin F form  a complex that exhibits histone  H1 kinase activity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5551,"ComplexName":"CDC2-CCNB1-PTCH1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06493;P14635;Q13635","subunits.Entrez.IDs.":"983;891;5727","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007049","GO.description":"cell cycle","FunCat.ID":"10.03","FunCat.description":"cell cycle","PubMed.ID":11331587,"subunits.Protein.name.":"Cyclin-dependent kinase 1 ;G2/mitotic-specific cyclin-B1;Protein patched homolog 1","subunits.Gene.name.":"CDK1;CCNB1;PTCH1","subunits.Gene.name.syn.":"CDC2 CDC28A CDKN1 P34CDC2;CCNB;PTCH","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5556,"ComplexName":"CDK2-CCNA2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P20248;P24941","subunits.Entrez.IDs.":"890;1017","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007049","GO.description":"cell cycle","FunCat.ID":"10.03","FunCat.description":"cell cycle","PubMed.ID":8475101,"subunits.Protein.name.":"Cyclin-A2 ;Cyclin-dependent kinase 2","subunits.Gene.name.":"CCNA2;CDK2","subunits.Gene.name.syn.":"CCN1 CCNA;CDKN2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5557,"ComplexName":"CDC2-CCNA2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06493;P20248","subunits.Entrez.IDs.":"983;890","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007049","GO.description":"cell cycle","FunCat.ID":"10.03","FunCat.description":"cell cycle","PubMed.ID":8423786,"subunits.Protein.name.":"Cyclin-dependent kinase 1 ;Cyclin-A2","subunits.Gene.name.":"CDK1;CCNA2","subunits.Gene.name.syn.":"CDC2 CDC28A CDKN1 P34CDC2;CCN1 CCNA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5558,"ComplexName":"PAR6-CDC42 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P60953;Q9BYG5","subunits.Entrez.IDs.":"998;84612","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":12606577,"subunits.Protein.name.":"Cell division control protein 42 homolog;Partitioning defective 6 homolog beta","subunits.Gene.name.":"CDC42;PARD6B","subunits.Gene.name.syn.":"None;PAR6B","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5559,"ComplexName":"CDC2-CCNA2-CDK2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06493;P20248;P24941","subunits.Entrez.IDs.":"983;890;1017","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007049","GO.description":"cell cycle","FunCat.ID":"10.03","FunCat.description":"cell cycle","PubMed.ID":16009130,"subunits.Protein.name.":"Cyclin-dependent kinase 1 ;Cyclin-A2 ;Cyclin-dependent kinase 2","subunits.Gene.name.":"CDK1;CCNA2;CDK2","subunits.Gene.name.syn.":"CDC2 CDC28A CDKN1 P34CDC2;CCN1 CCNA;CDKN2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5560,"ComplexName":"CDK2-CCNE1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P24864;P24941","subunits.Entrez.IDs.":"898;1017","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007049","GO.description":"cell cycle","FunCat.ID":"10.03","FunCat.description":"cell cycle","PubMed.ID":8560263,"subunits.Protein.name.":"G1/S-specific cyclin-E1;Cyclin-dependent kinase 2","subunits.Gene.name.":"CCNE1;CDK2","subunits.Gene.name.syn.":"CCNE;CDKN2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5564,"ComplexName":"LMO4-gp130 complex","Organism":"Human","Synonyms":"None","Cell.line":"HepG2 cells","subunits.UniProt.IDs.":"O14543;P23458;P40189;P61968;Q06124","subunits.Entrez.IDs.":"9021;3716;3572;8543;5781","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045893;GO:0023052","GO.description":"positive regulation of transcription, DNA-templated;signaling","FunCat.ID":"11.02.03.04.01;30.01","FunCat.description":"transcription activation;cellular signalling","PubMed.ID":15677447,"subunits.Protein.name.":"Suppressor of cytokine signaling 3 ;Tyrosine-protein kinase JAK1 ;Interleukin-6 receptor subunit beta ;LIM domain transcription factor LMO4 ;Tyrosine-protein phosphatase non-receptor type 11","subunits.Gene.name.":"SOCS3;JAK1;IL6ST;LMO4;PTPN11","subunits.Gene.name.syn.":"CIS3 SSI3;JAK1A JAK1B;;;PTP2C SHPTP2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"LMO4 associates with the gp130 complex and IL-6 may enhance its association.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5566,"ComplexName":"Isl1-Jak1-Stat3 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"COS-1 cells","subunits.UniProt.IDs.":"P42227;P52332;P61372","subunits.Entrez.IDs.":"20848;16451;16392","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0007259;GO:0007399","GO.description":"JAK-STAT cascade;nervous system development","FunCat.ID":"30.01.05.01.01;47.03.01","FunCat.description":"JAK-STAT cascade;nervous system","PubMed.ID":15659653,"subunits.Protein.name.":"Signal transducer and activator of transcription 3 ;Tyrosine-protein kinase JAK1 ;Insulin gene enhancer protein ISL-1","subunits.Gene.name.":"Stat3;Jak1;Isl1","subunits.Gene.name.syn.":"Aprf;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Isl1 may function as an adaptor protein that brings Jak1 and Stat3 in proximity and thereby facilitates Stat3 phosphorylation by Jak1.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5573,"ComplexName":"Stat1-alpha-dimer-CBP DNA-protein complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P42224;Q92793","subunits.Entrez.IDs.":"6772;1387","Protein.complex.purification.method":"MI:0096- pull down; MI:0413- electrophoretic mobility shift assay","GO.ID":"GO:2001141;GO:0006355;GO:0005634","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;nucleus","FunCat.ID":"11.02.03.04;70.10","FunCat.description":"transcriptional control;nucleus","PubMed.ID":8986769,"subunits.Protein.name.":"Signal transducer and activator of transcription 1-alpha/beta ;CREB-binding protein","subunits.Gene.name.":"STAT1;CREBBP","subunits.Gene.name.syn.":";CBP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results demonstrate that both phosphorylated homodimeric and unphosphorylated monomeric Stat1-alpha can interact with CBP/p300, and their interactions occur at two different regions of both Stat1-alpha and CBP/p300.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5574,"ComplexName":"Vps29-Vps35-Vps26a complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P40336;Q9EQH3;Q9QZ88","subunits.Entrez.IDs.":"30930;65114;56433","Protein.complex.purification.method":"MI:0096- pull down; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0000301","GO.description":"intracellular protein transport;protein targeting;protein transport;retrograde transport, vesicle recycling within Golgi","FunCat.ID":"14.04;20.01.10;20.09.07.07","FunCat.description":"protein targeting, sorting and translocation;protein transport;retrograde transport","PubMed.ID":15965486,"subunits.Protein.name.":"Vacuolar protein sorting-associated protein 26A ;Vacuolar protein sorting-associated protein 35 ;Vacuolar protein sorting-associated protein 29","subunits.Gene.name.":"Vps26a;Vps35;Vps29","subunits.Gene.name.syn.":"Vps26;Mem3;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results show that this complex formation is essential for correct localization of mVps29 to endosomal compartments.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5575,"ComplexName":"SHP-NR5A2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00482;Q15466","subunits.Entrez.IDs.":"2494;8431","Protein.complex.purification.method":"MI:0096- pull down; MI:0018- two hybrid","GO.ID":"GO:0045892","GO.description":"negative regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.03","FunCat.description":"transcription repression","PubMed.ID":11030331,"subunits.Protein.name.":"Nuclear receptor subfamily 5 group A member 2 ;Nuclear receptor subfamily 0 group B member 2","subunits.Gene.name.":"NR5A2;NR0B2","subunits.Gene.name.syn.":"B1F CPF FTF;SHP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5576,"ComplexName":"Pigr-Vps35-Vps26a-Vps29 complex","Organism":"Rat","Synonyms":"None","Cell.line":"liver","subunits.UniProt.IDs.":"P15083;Q3TJ43;Q6AY86;Q9QZ88","subunits.Entrez.IDs.":"25046;65114;361846;56433","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0000301;GO:0005768","GO.description":"intracellular protein transport;protein targeting;protein transport;retrograde transport, vesicle recycling within Golgi;endosome","FunCat.ID":"14.04;20.01.10;20.09.07.07;70.22","FunCat.description":"protein targeting, sorting and translocation;protein transport;retrograde transport;endosome","PubMed.ID":15247922,"subunits.Protein.name.":"Polymeric immunoglobulin receptor;Putative uncharacterized protein;Vacuolar protein sorting-associated protein 26A;Vacuolar protein sorting-associated protein 29","subunits.Gene.name.":"Pigr;Vps35;Vps26a;Vps29","subunits.Gene.name.syn.":"None;None;Vps26;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors showed that the mammalian Vps35-Vps29-Vps26 retromer subcomplex is involved in pIgR-pIgA transcytosis.","SWISSPROT.organism":"Rattus norvegicus (Rat);Mus musculus (Mouse);Rattus norvegicus (Rat);Mus musculus (Mouse)"}
{"ComplexID":5577,"ComplexName":"Ephb1-Sdc2 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P09759;P34900","subunits.Entrez.IDs.":"24338;25615","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0030182","GO.description":"neuron differentiation","FunCat.ID":"43.03.13","FunCat.description":"neuron","PubMed.ID":11580899,"subunits.Protein.name.":"Ephrin type-B receptor 1 ;Syndecan-2","subunits.Gene.name.":"Ephb1;Sdc2","subunits.Gene.name.syn.":"Elk Epth2;Hspg1 Synd2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5578,"ComplexName":"Sdc2-Ephb2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P43407;P54763","subunits.Entrez.IDs.":"15529;13844","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0030182","GO.description":"neuron differentiation","FunCat.ID":"43.03.13","FunCat.description":"neuron","PubMed.ID":11580899,"subunits.Protein.name.":"Syndecan-2 ;Ephrin type-B receptor 2","subunits.Gene.name.":"Sdc2;Ephb2","subunits.Gene.name.syn.":"Hspg1 Synd2;Epth3 Nuk Sek3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5579,"ComplexName":"CNTF-CNTFR-gp130-LIFR complex","Organism":"Human","Synonyms":"None","Cell.line":"EW-1 cells","subunits.UniProt.IDs.":"P26441;P26992;P40189;P42702","subunits.Entrez.IDs.":"1270;1271;3572;3977","Protein.complex.purification.method":"MI:0030- cross-linking studies","GO.ID":"GO:0023052;GO:0007399","GO.description":"signaling;nervous system development","FunCat.ID":"30.01;47.03.01","FunCat.description":"cellular signalling;nervous system","PubMed.ID":8385113,"subunits.Protein.name.":"Ciliary neurotrophic factor ;Ciliary neurotrophic factor receptor subunit alpha ;Interleukin-6 receptor subunit beta ;Leukemia inhibitory factor receptor","subunits.Gene.name.":"CNTF;CNTFR;IL6ST;LIFR","subunits.Gene.name.syn.":";;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5582,"ComplexName":"LIFR-LIF-gp130 complex","Organism":"Human","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"P15018;P40189;P42702","subunits.Entrez.IDs.":"3976;3572;3977","Protein.complex.purification.method":"MI:0030- cross-linking studies","GO.ID":"GO:0023052;GO:0007399","GO.description":"signaling;nervous system development","FunCat.ID":"30.01;47.03.01","FunCat.description":"cellular signalling;nervous system","PubMed.ID":8385113,"subunits.Protein.name.":"Leukemia inhibitory factor ;Interleukin-6 receptor subunit beta ;Leukemia inhibitory factor receptor","subunits.Gene.name.":"LIF;IL6ST;LIFR","subunits.Gene.name.syn.":"HILDA;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5583,"ComplexName":"Per1-Cry1-Cry2-Nono-Wdr5 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q32Q86;Q498M4;Q5FVM4;Q8CHI5;Q923I8","subunits.Entrez.IDs.":"299691;362093;317259;287422;170917","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0045892;GO:0007624;GO:0048511","GO.description":"negative regulation of transcription, DNA-templated;ultradian rhythm;rhythmic process","FunCat.ID":"11.02.03.04.03;34.11.11","FunCat.description":"transcription repression;rhythm (e.g. circadian, ultradian)","PubMed.ID":15860628,"subunits.Protein.name.":"Cryptochrome-1;WD repeat-containing protein 5;Non-POU domain-containing octamer-binding protein ;Period circadian protein homolog 1 ;Cryptochrome-2","subunits.Gene.name.":"Cry1;Wdr5;Nono;Per1;Cry2","subunits.Gene.name.syn.":";;;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results suggest that NONO probably operates antagonistically to PER proteins in mammalian cells, and that it is essential to normal circadian rhythmicity in mammals and in Drosophila.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5584,"ComplexName":"Per1-Nono-Wdr5 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q498M4;Q5FVM4;Q8CHI5","subunits.Entrez.IDs.":"362093;317259;287422","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045892;GO:0007624;GO:0048511","GO.description":"negative regulation of transcription, DNA-templated;ultradian rhythm;rhythmic process","FunCat.ID":"11.02.03.04.03;34.11.11","FunCat.description":"transcription repression;rhythm (e.g. circadian, ultradian)","PubMed.ID":15860628,"subunits.Protein.name.":"WD repeat-containing protein 5;Non-POU domain-containing octamer-binding protein ;Period circadian protein homolog 1","subunits.Gene.name.":"Wdr5;Nono;Per1","subunits.Gene.name.syn.":";;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results suggest that NONO probably operates antagonistically to PER proteins in mammalian cells, and that it is essential to normal circadian rhythmicity in mammals and in Drosophila.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5585,"ComplexName":"Per2-Nono-Wdr5 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q498M4;Q5FVM4;Q9Z301","subunits.Entrez.IDs.":"362093;317259;63840","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045892;GO:0007624;GO:0048511","GO.description":"negative regulation of transcription, DNA-templated;ultradian rhythm;rhythmic process","FunCat.ID":"11.02.03.04.03;34.11.11","FunCat.description":"transcription repression;rhythm (e.g. circadian, ultradian)","PubMed.ID":15860628,"subunits.Protein.name.":"WD repeat-containing protein 5;Non-POU domain-containing octamer-binding protein ;Period circadian protein homolog 2","subunits.Gene.name.":"Wdr5;Nono;Per2","subunits.Gene.name.syn.":";;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results suggest that NONO probably operates antagonistically to PER proteins in mammalian cells, and that it is essential to normal circadian rhythmicity in mammals and in Drosophila.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5589,"ComplexName":"LINC complex, S-phase","Organism":"Human","Synonyms":"None","Cell.line":"T98G cells","subunits.UniProt.IDs.":"P10244;P28749;Q09028;Q52LA3;Q5TKA1;Q6MZP7;Q96GY3","subunits.Entrez.IDs.":"4605;5933;5928;91750;286826;132660;55957","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0000086;GO:0045893;GO:0005634","GO.description":"G2/M transition of mitotic cell cycle;positive regulation of transcription, DNA-templated;nucleus","FunCat.ID":"10.03.01.01.09;11.02.03.04.01;70.10","FunCat.description":"G2/M transition of mitotic cell cycle;transcription activation;nucleus","PubMed.ID":17671431,"subunits.Protein.name.":"Myb-related protein B ;Retinoblastoma-like protein 1;Histone-binding protein RBBP4;Protein lin-52 homolog;Protein lin-9 homolog ;Protein lin-54 homolog ;Protein lin-37 homolog","subunits.Gene.name.":"MYBL2;RBL1;RBBP4;LIN52;LIN9;LIN54;LIN37","subunits.Gene.name.syn.":"BMYB;PRB1, p107, CP107;RBAP48;C14orf46;BARA TGS;CXCDC1 KIAA2037;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"During S-phase B-MYB and p107 become incorporated into the LINC complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5590,"ComplexName":"Zip-Prkcz-Kcnab2 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O08623;P09217;P62483","subunits.Entrez.IDs.":"113894;25522;29738","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0050789;GO:0050896","GO.description":"regulation of biological process;response to stimulus","FunCat.ID":"18;36.25","FunCat.description":"REGULATION OF METABOLISM AND PROTEIN FUNCTION;animal specific systemic sensing and response","PubMed.ID":10477520,"subunits.Protein.name.":"Sequestosome-1 ;Protein kinase C zeta type;Voltage-gated potassium channel subunit beta-2","subunits.Gene.name.":"Sqstm1;Prkcz;Kcnab2","subunits.Gene.name.syn.":"Zip;Pkcz;Ckbeta2 Kcnb3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results suggest that ZIP acts as a link that targets the activity of PKC-zeta  to Kv-beta 2. ZIP1 and ZIP2, two alternatively spliced protein products, possess distinct activities in stimulating PKC-zeta  phosphorylation of Kv-beta 2. Their ability to interact with each other to form homo- and heteromultimeric complexes provides an explanation for the synergistic stimulatory activity seen only in the presence of both ZIP1 and ZIP2.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5593,"ComplexName":"LINC core complex","Organism":"Human","Synonyms":"None","Cell.line":"MOLT-4 cells","subunits.UniProt.IDs.":"Q09028;Q52LA3;Q5TKA1;Q6MZP7;Q96GY3","subunits.Entrez.IDs.":"5928;91750;286826;132660;55957","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0000086;GO:0045893;GO:0005634","GO.description":"G2/M transition of mitotic cell cycle;positive regulation of transcription, DNA-templated;nucleus","FunCat.ID":"10.03.01.01.09;11.02.03.04.01;70.10","FunCat.description":"G2/M transition of mitotic cell cycle;transcription activation;nucleus","PubMed.ID":17671431,"subunits.Protein.name.":"Histone-binding protein RBBP4;Protein lin-52 homolog;Protein lin-9 homolog ;Protein lin-54 homolog ;Protein lin-37 homolog","subunits.Gene.name.":"RBBP4;LIN52;LIN9;LIN54;LIN37","subunits.Gene.name.syn.":"RBAP48;C14orf46;BARA TGS;CXCDC1 KIAA2037;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"LINC selectively binds to the promoters of G2/M genes whose products are required for mitosis and plays an important role in their cell cycle dependent activation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5596,"ComplexName":"LINC complex, quiescent cells","Organism":"Human","Synonyms":"None","Cell.line":"T98G cells","subunits.UniProt.IDs.":"Q08999;Q09028;Q16254;Q52LA3;Q5TKA1;Q6MZP7;Q96GY3","subunits.Entrez.IDs.":"5934;5928;1874;91750;286826;132660;55957","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0000086;GO:0045893;GO:0005634","GO.description":"G2/M transition of mitotic cell cycle;positive regulation of transcription, DNA-templated;nucleus","FunCat.ID":"10.03.01.01.09;11.02.03.04.01;70.10","FunCat.description":"G2/M transition of mitotic cell cycle;transcription activation;nucleus","PubMed.ID":17671431,"subunits.Protein.name.":"Retinoblastoma-like protein 2;Histone-binding protein RBBP4;Transcription factor E2F4 ;Protein lin-52 homolog;Protein lin-9 homolog ;Protein lin-54 homolog ;Protein lin-37 homolog","subunits.Gene.name.":"RBL2;RBBP4;E2F4;LIN52;LIN9;LIN54;LIN37","subunits.Gene.name.syn.":"RB2, P130;RBAP48;;C14orf46;BARA TGS;CXCDC1 KIAA2037;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In quiescent cells LINC selectively interacts with p130 and E2F4. This association is lost during S-phase.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5597,"ComplexName":"Zip3-Prkcz-Gabrr3 complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"O08623;P09217;P50573","subunits.Entrez.IDs.":"113894;25522;192258","Protein.complex.purification.method":"MI:0096-pull down","GO.ID":"GO:0030545;GO:0050896","GO.description":"receptor regulator activity;response to stimulus","FunCat.ID":"18.02.07;36.25","FunCat.description":"regulator of receptor activity;animal specific systemic sensing and response","PubMed.ID":12431995,"subunits.Protein.name.":"Sequestosome-1 ;Protein kinase C zeta type;Gamma-aminobutyric acid receptor subunit rho-3","subunits.Gene.name.":"Sqstm1;Prkcz;Gabrr3","subunits.Gene.name.syn.":"Zip;Pkcz;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors analysed the splice variant Zip3. Zip3 was able to form homo- and heterodimers and bound to PKC-zeta  and Kv-beta 2. Furthermore, Zip3 interacted with GABAC receptor rho  subunits using a different binding site, allowing simultaneous binding of rho  subunits and PKC-zeta  in vitro. These results suggest a possible formation of a PKC-zeta /ZIP3/GABAC receptor containing macromolecular complex.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5604,"ComplexName":"Emerin complex 1","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P35579;P50402;P60709;Q12965;Q13813;Q15417;Q8WWI1;Q9BRV8","subunits.Entrez.IDs.":"4627;2010;60;4643;6709;1266;4008;80143","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0005634","GO.description":"nucleus","FunCat.ID":"70.1","FunCat.description":"nucleus","PubMed.ID":17620012,"subunits.Protein.name.":"Myosin-9 ;Emerin;Actin, cytoplasmic 1;Unconventional myosin-Ie ;Spectrin alpha chain, non-erythrocytic 1 ;Calponin-3 ;LIM domain only protein 7 ;Suppressor of IKBKE 1","subunits.Gene.name.":"MYH9;EMD;ACTB;MYO1E;SPTAN1;CNN3;LMO7;SIKE1","subunits.Gene.name.syn.":";EDMD STA;None;MYO1C;NEAS SPTA2;;FBX20 FBXO20 KIAA0858;SIKE","Disease.comment":"Emerin is involved in Emery-Dreifuss muscular dystrophy (EDMD).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5606,"ComplexName":"Emerin-actin-NMI-(alphaII)spectrin complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P50402;P60709;Q13287;Q13813","subunits.Entrez.IDs.":"2010;60;9111;6709","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0226- ion exchange chromatography; MI:0071- molecular sieving","GO.ID":"GO:0005634","GO.description":"nucleus","FunCat.ID":"70.1","FunCat.description":"nucleus","PubMed.ID":17620012,"subunits.Protein.name.":"Emerin;Actin, cytoplasmic 1;N-myc-interactor ;Spectrin alpha chain, non-erythrocytic 1","subunits.Gene.name.":"EMD;ACTB;NMI;SPTAN1","subunits.Gene.name.syn.":"EDMD STA;None;;NEAS SPTA2","Disease.comment":"Emerin is involved in Emery-Dreifuss muscular dystrophy (EDMD).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5607,"ComplexName":"Emerin-actin-NMI complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P50402;P60709;Q13287","subunits.Entrez.IDs.":"2010;60;9111","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0226- ion exchange chromatography; MI:0071- molecular sieving","GO.ID":"GO:0005634","GO.description":"nucleus","FunCat.ID":"70.1","FunCat.description":"nucleus","PubMed.ID":17620012,"subunits.Protein.name.":"Emerin;Actin, cytoplasmic 1;N-myc-interactor","subunits.Gene.name.":"EMD;ACTB;NMI","subunits.Gene.name.syn.":"EDMD STA;None;","Disease.comment":"Emerin is involved in Emery-Dreifuss muscular dystrophy (EDMD).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5608,"ComplexName":"Emerin architectural complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P02545;P20700;P50402;P60709;Q13287;Q13813","subunits.Entrez.IDs.":"4000;4001;2010;60;9111;6709","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0071- molecular sieving; MI:0226- ion exchange chromatography","GO.ID":"GO:0006997;GO:0005634","GO.description":"nucleus organization;nucleus","FunCat.ID":"42.10;70.10","FunCat.description":"nucleus;nucleus","PubMed.ID":17620012,"subunits.Protein.name.":"Prelamin-A/C [Cleaved into: Lamin-A/C ;Lamin-B1;Emerin;Actin, cytoplasmic 1;N-myc-interactor ;Spectrin alpha chain, non-erythrocytic 1","subunits.Gene.name.":"LMNA;LMNB1;EMD;ACTB;NMI;SPTAN1","subunits.Gene.name.syn.":"LMN1;LMN2 LMNB;EDMD STA;None;;NEAS SPTA2","Disease.comment":"Emerin is involved in Emery-Dreifuss muscular dystrophy (EDMD).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5609,"ComplexName":"Emerin regulatory complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15379;O75531;P28749;P50402;P60709;P68431;Q02539;Q13547;Q8WWI1","subunits.Entrez.IDs.":"8841;8815;5933;2010;60;None;3024;3065;4008","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0226- ion exchange chromatography; MI:0071- molecular sieving","GO.ID":"GO:0006265;GO:2001141;GO:0006355;GO:0051276;GO:0005634","GO.description":"DNA topological change;regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;11.02.03.04;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);transcriptional control;organization of chromosome structure;nucleus","PubMed.ID":17620012,"subunits.Protein.name.":"Histone deacetylase 3;Barrier-to-autointegration factor;Retinoblastoma-like protein 1;Emerin;Actin, cytoplasmic 1;Histone H3.1;Histone H1.1 ;Histone deacetylase 1;LIM domain only protein 7","subunits.Gene.name.":"HDAC3;BANF1;RBL1;EMD;ACTB;HIST1H3A;;HIST1H1A;HDAC1;LMO7","subunits.Gene.name.syn.":"None;BAF, BCRG1;PRB1, p107, CP107;EDMD STA;None;H3FA; H3FL; H3FC; H3FB; H3FD; H3FI; H3FH; H3FK; H3FF; H3FJ;H1F1;RPD3L1;FBX20 FBXO20 KIAA0858","Disease.comment":"Emerin is involved in Emery-Dreifuss muscular dystrophy (EDMD).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5610,"ComplexName":"Alpha-GDI-Hsp90 chaperone complex, ATP dependent","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P50398;P60905;P63018;P82995","subunits.Entrez.IDs.":"25183;79130;24468;299331","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0036465;GO:0000301;GO:0048489;GO:0016079;GO:0005886;GO:0030133","GO.description":"synaptic vesicle recycling;retrograde transport, vesicle recycling within Golgi;synaptic vesicle transport;synaptic vesicle exocytosis;plasma membrane;transport vesicle","FunCat.ID":"20.09.07.29;20.09.07.07;20.09.16.09.05;70.02;70.09","FunCat.description":"vesicle recycling;retrograde transport;synaptic vesicle exocytosis;eukaryotic plasma membrane / membrane attached;intracellular transport vesicles","PubMed.ID":12426384,"subunits.Protein.name.":"Rab GDP dissociation inhibitor alpha ;DnaJ homolog subfamily C member 5 ;Heat shock cognate 71 kDa protein ;Heat shock protein HSP 90-alpha","subunits.Gene.name.":"Gdi1;Dnajc5;Hspa8;Hsp90aa1","subunits.Gene.name.syn.":"Rabgdia;;Hsc70 Hsc73;Hsp86 Hspca","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"While the major pool comprising the cytosolic form of alpha-GDI in the brain is largely found in a complex with Rab3A (PMID:11152757), the authors found that a minor pool of membrane-associated alpha-GDI forms a complex with chaperones present on the synaptic vesicle membrane. The results suggest a novel role for Hsp90 in regulation of the client molecule alpha-GDI in Rab3A function leading to vesicle targeting and fusion at the synapse.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5611,"ComplexName":"Emerin complex 24","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P02545;P06400;P20700;P33991;P49736;P50402;P68431;Q00839;Q02539;Q07021;Q08999;Q13287;Q14566;Q9H0E3;Q9H503","subunits.Entrez.IDs.":"4000;5925;4001;4173;4171;2010;None;3192;3024;708;5934;9111;4175;79595;140836","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0226- ion exchange chromatography; MI:0071- molecular sieving","GO.ID":"GO:0006260;GO:0006396;GO:0005634","GO.description":"DNA replication;RNA processing;nucleus","FunCat.ID":"10.01.03;11.04;70.10","FunCat.description":"DNA synthesis and replication;RNA processing;nucleus","PubMed.ID":17620012,"subunits.Protein.name.":"Prelamin-A/C [Cleaved into: Lamin-A/C ;Retinoblastoma-associated protein ;Lamin-B1;DNA replication licensing factor MCM4 ;DNA replication licensing factor MCM2 ;Emerin;Histone H3.1;Heterogeneous nuclear ribonucleoprotein U ;Histone H1.1 ;Complement component 1 Q subcomponent-binding protein, mitochondrial;Retinoblastoma-like protein 2;N-myc-interactor ;DNA replication licensing factor MCM6 ;Histone deacetylase complex subunit SAP130;Barrier-to-autointegration factor-like protein","subunits.Gene.name.":"LMNA;RB1;LMNB1;MCM4;MCM2;EMD;HIST1H3A;;HNRNPU;HIST1H1A;C1QBP;RBL2;NMI;MCM6;SAP130;BANF2","subunits.Gene.name.syn.":"LMN1;;LMN2 LMNB;CDC21;BM28 CCNL1 CDCL1 KIAA0030;EDMD STA;H3FA; H3FL; H3FC; H3FB; H3FD; H3FI; H3FH; H3FK; H3FF; H3FJ;HNRPU SAFA U21.1;H1F1;GC1QBP HABP1 SF2P32;RB2, P130;;;None;BAFL, C20orf179","Disease.comment":"Emerin is involved in Emery-Dreifuss muscular dystrophy (EDMD).","Subunits.comment":"None","Complex.comment":"Complexes are named on the basis of their S300 elution fraction number. Subunits 9-15 were identified via LCMS/MS analysis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5612,"ComplexName":"Alpha-GDI-Rab3a complex, cytosolic","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P50398;P63012","subunits.Entrez.IDs.":"25183;25531","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006906;GO:0036465;GO:0000301;GO:0048489;GO:0016079;GO:0005737","GO.description":"vesicle fusion;synaptic vesicle recycling;retrograde transport, vesicle recycling within Golgi;synaptic vesicle transport;synaptic vesicle exocytosis;cytoplasm","FunCat.ID":"20.09.07.27;20.09.07.29;20.09.07.07;20.09.16.09.05;70.03","FunCat.description":"vesicle fusion;vesicle recycling;retrograde transport;synaptic vesicle exocytosis;cytoplasm","PubMed.ID":12426384,"subunits.Protein.name.":"Rab GDP dissociation inhibitor alpha ;Ras-related protein Rab-3A","subunits.Gene.name.":"Gdi1;Rab3a","subunits.Gene.name.syn.":"Rabgdia;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"While the major pool comprising the cytosolic form of alpha-GDI in the brain is largely found in a complex with Rab3A (PMID:11152757), the authors found that a minor pool of membrane-associated alpha-GDI forms a complex with chaperones present on the synaptic vesicle membrane.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5613,"ComplexName":"Emerin complex 25","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75531;O95218;O95777;P05455;P20700;P31946;P50402;P60709;P61978;P62258;P62314;Q13283;Q16543;Q9H0E3;Q9P287;Q9Y333","subunits.Entrez.IDs.":"8815;9406;51691;6741;4001;7529;2010;60;3190;7531;6632;10146;11140;79595;56647;57819","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0226- ion exchange chromatography; MI:0071- molecular sieving","GO.ID":"GO:0006396;GO:0035556;GO:0005634","GO.description":"RNA processing;intracellular signal transduction;nucleus","FunCat.ID":"11.04;30.01;70.10","FunCat.description":"RNA processing;cellular signalling;nucleus","PubMed.ID":17620012,"subunits.Protein.name.":"Barrier-to-autointegration factor;Zinc finger Ran-binding domain-containing protein 2 ;U6 snRNA-associated Sm-like protein LSm8;Lupus La protein ;Lamin-B1;14-3-3 protein beta/alpha ;Emerin;Actin, cytoplasmic 1;Heterogeneous nuclear ribonucleoprotein K ;14-3-3 protein epsilon ;Small nuclear ribonucleoprotein Sm D1 ;Ras GTPase-activating protein-binding protein 1 ;Hsp90 co-chaperone Cdc37;Histone deacetylase complex subunit SAP130;BRCA2 and CDKN1A-interacting protein ;U6 snRNA-associated Sm-like protein LSm2","subunits.Gene.name.":"BANF1;ZRANB2;LSM8;SSB;LMNB1;YWHAB;EMD;ACTB;HNRNPK;YWHAE;SNRPD1;G3BP1;CDC37;SAP130;BCCIP;LSM2","subunits.Gene.name.syn.":"BAF, BCRG1;ZIS ZNF265;;;LMN2 LMNB;;EDMD STA;None;HNRPK;;;G3BP;CDC37A;None;TOK1;C6orf28 G7B","Disease.comment":"Emerin is involved in Emery-Dreifuss muscular dystrophy (EDMD).","Subunits.comment":"None","Complex.comment":"Complexes are named on the basis of their S300 elution fraction number. Subunits 5-16 were identified via LCMS/MS analysis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5614,"ComplexName":"Emerin complex 32","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00422;O15379;P20700;P28749;P50402;P60709;P68431;Q08999;Q12824;Q13263;Q13287;Q13547;Q13813;Q14839;Q8TAQ2;Q92922;Q9BQ87;Q9BZK7;Q9C005;Q9H503;Q9NPJ6;Q9UKL0","subunits.Entrez.IDs.":"10284;8841;4001;5933;2010;60;None;5934;6598;10155;9111;3065;6709;1108;6601;6599;90665;79718;84661;140836;29079;23186","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0226- ion exchange chromatography; MI:0071- molecular sieving","GO.ID":"GO:0006265;GO:0051276;GO:0005634","GO.description":"DNA topological change;chromosome organization;nucleus","FunCat.ID":"10.01.09.05;42.10.03;70.10","FunCat.description":"DNA conformation modification (e.g. chromatin);organization of chromosome structure;nucleus","PubMed.ID":17620012,"subunits.Protein.name.":"Histone deacetylase complex subunit SAP18;Histone deacetylase 3;Lamin-B1;Retinoblastoma-like protein 1;Emerin;Actin, cytoplasmic 1;Histone H3.1;Retinoblastoma-like protein 2;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;Transcription intermediary factor 1-beta ;N-myc-interactor ;Histone deacetylase 1;Spectrin alpha chain, non-erythrocytic 1 ;Chromodomain-helicase-DNA-binding protein 4;SWI/SNF complex subunit SMARCC2;SWI/SNF complex subunit SMARCC1;F-box-like/WD repeat-containing protein TBL1Y ;F-box-like/WD repeat-containing protein TBL1XR1;Protein dpy-30 homolog;Barrier-to-autointegration factor-like protein;Mediator of RNA polymerase II transcription subunit 4 ;REST corepressor 1","subunits.Gene.name.":"SAP18;HDAC3;LMNB1;RBL1;EMD;ACTB;HIST1H3A;;RBL2;SMARCB1;TRIM28;NMI;HDAC1;SPTAN1;CHD4;SMARCC2;SMARCC1;TBL1Y;TBL1XR1;DPY30;BANF2;MED4;RCOR1","subunits.Gene.name.syn.":"None;None;LMN2 LMNB;PRB1, p107, CP107;EDMD STA;None;H3FA; H3FL; H3FC; H3FB; H3FD; H3FI; H3FH; H3FK; H3FF; H3FJ;RB2, P130;BAF47, INI1, SNF5L1;KAP1 RNF96 TIF1B;;RPD3L1;NEAS SPTA2;None;BAF170;BAF155;TBL1;IRA1 TBLR1;None;BAFL, C20orf179;ARC36 DRIP36 VDRIP;KIAA0071 RCOR","Disease.comment":"Emerin is involved in Emery-Dreifuss muscular dystrophy (EDMD).","Subunits.comment":"None","Complex.comment":"Complexes are named on the basis of their S300 elution fraction number. Subunits 9-22 were identified via LCMS/MS analysis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5615,"ComplexName":"Emerin complex 52","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00148;O95777;P10827;P12277;P14866;P20700;P27348;P46940;P50402;P51858;P60709;P61978;P62258;P62314;Q00839;Q02539;Q07021;Q08999;Q12906;Q13287;Q53EL6;Q9BZZ5;Q9Y2U8","subunits.Entrez.IDs.":"10212;51691;7067;1152;3191;4001;10971;8826;2010;3068;60;3190;7531;6632;3192;3024;708;5934;3609;9111;27250;8539;23592","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0226- ion exchange chromatography; MI:0071- molecular sieving","GO.ID":"GO:0006396;GO:0035556;GO:0005634","GO.description":"RNA processing;intracellular signal transduction;nucleus","FunCat.ID":"11.04;30.01;70.10","FunCat.description":"RNA processing;cellular signalling;nucleus","PubMed.ID":17620012,"subunits.Protein.name.":"ATP-dependent RNA helicase DDX39A ;U6 snRNA-associated Sm-like protein LSm8;Thyroid hormone receptor alpha;Creatine kinase B-type ;Heterogeneous nuclear ribonucleoprotein L ;Lamin-B1;14-3-3 protein theta;Ras GTPase-activating-like protein IQGAP1;Emerin;Hepatoma-derived growth factor ;Actin, cytoplasmic 1;Heterogeneous nuclear ribonucleoprotein K ;14-3-3 protein epsilon ;Small nuclear ribonucleoprotein Sm D1 ;Heterogeneous nuclear ribonucleoprotein U ;Histone H1.1 ;Complement component 1 Q subcomponent-binding protein, mitochondrial;Retinoblastoma-like protein 2;Interleukin enhancer-binding factor 3 ;N-myc-interactor ;Programmed cell death protein 4 ;Apoptosis inhibitor 5 ;Inner nuclear membrane protein Man1","subunits.Gene.name.":"DDX39A;LSM8;THRA;CKB;HNRNPL;LMNB1;YWHAQ;IQGAP1;EMD;HDGF;ACTB;HNRNPK;YWHAE;SNRPD1;HNRNPU;HIST1H1A;C1QBP;RBL2;ILF3;NMI;PDCD4;API5;LEMD3","subunits.Gene.name.syn.":"DDX39;;EAR7 ERBA1 NR1A1 THRA1 THRA2;CKBB;HNRPL;LMN2 LMNB;None;KIAA0051;EDMD STA;HMG1L2;None;HNRPK;;;HNRPU SAFA U21.1;H1F1;GC1QBP HABP1 SF2P32;RB2, P130;DRBF MPHOSPH4 NF90;;H731;;MAN1","Disease.comment":"Emerin is involved in Emery-Dreifuss muscular dystrophy (EDMD).","Subunits.comment":"None","Complex.comment":"Complexes are named on the basis of their S300 elution fraction number. Subunits 8-23 were identified via LCMS/MS analysis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5616,"ComplexName":"Hsp110-Hsc70-Hsp25 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"Colon-26 cells","subunits.UniProt.IDs.":"P14602;P63017;Q61699","subunits.Entrez.IDs.":"None;15481;15505","Protein.complex.purification.method":"MI:0091- chromatography technologies","GO.ID":"GO:0050821;GO:0006457","GO.description":"protein stabilization;protein folding","FunCat.ID":"14.01","FunCat.description":"protein folding and stabilization","PubMed.ID":10631312,"subunits.Protein.name.":"Heat shock protein beta-1 ;Heat shock cognate 71 kDa protein;Heat shock protein 105 kDa","subunits.Gene.name.":"Hspb1;Hspa8;Hsph1","subunits.Gene.name.syn.":"Hsp25 Hsp27;Hsc70 Hsc73;Hsp105 Hsp110 Kiaa0201","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Mutational analysis indicate that Hsp25 and Hsp70 can interact with Hsp110 at different sites and that the association of Hsp110 with Hsp25 requires the peptide-binding domain of Hsp110.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5622,"ComplexName":"HSP90-CIP1-FKBPL complex","Organism":"Human","Synonyms":"None","Cell.line":"U2OS cells","subunits.UniProt.IDs.":"P07900;P38936;Q9UIM3","subunits.Entrez.IDs.":"3320;1026;63943","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0006- anti bait coimmunoprecipitation; MI:0071- molecular sieving","GO.ID":"GO:0050821;GO:0006457;GO:0006974","GO.description":"protein stabilization;protein folding;cellular response to DNA damage stimulus","FunCat.ID":"14.01;32.01.09","FunCat.description":"protein folding and stabilization;DNA damage response","PubMed.ID":15664193,"subunits.Protein.name.":"Heat shock protein HSP 90-alpha;Cyclin-dependent kinase inhibitor 1 ;FK506-binding protein-like","subunits.Gene.name.":"HSP90AA1;CDKN1A;FKBPL","subunits.Gene.name.syn.":"HSP90A HSPC1 HSPCA;CAP20 CDKN1 CIP1 MDA6 PIC1 SDI1 WAF1;DIR1 NG7","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results show that the ability of WISp39 to stabilize p21 is dependent on its ability to bind and recruit Hsp90.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5623,"ComplexName":"Ask1-HSP90-AKT1 complex","Organism":"Bovine","Synonyms":"None","Cell.line":"BREC cells","subunits.UniProt.IDs.":"O35099;Q01314;Q76LV2","subunits.Entrez.IDs.":"26408;280991;281832","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006915","GO.description":"apoptotic process","FunCat.ID":"40.10.02","FunCat.description":"apoptosis (type I programmed cell death)","PubMed.ID":15782121,"subunits.Protein.name.":"Mitogen-activated protein kinase kinase kinase 5;RAC-alpha serine/threonine-protein kinase;Heat shock protein HSP 90-alpha","subunits.Gene.name.":"Map3k5;AKT1;HSP90AA1","subunits.Gene.name.syn.":"Ask1 Mekk5;PKB;HSP90A, HSPCA","Disease.comment":"None","Subunits.comment":"Since bovine Map3k5 was not available in the UniProt database at the time of annotation, the orthologous protein from mouse was used. Since the authors did not specify HSP 90, we used isoform HSP 90-alpha (HSP90AA1).","Complex.comment":"The data suggest that Hsp90 may serve as a scaffold to hold Akt-ASK1 in close proximity.","SWISSPROT.organism":"Mus musculus (Mouse);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":5624,"ComplexName":"Sema3E-PlexinD1 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS-7 cells","subunits.UniProt.IDs.":"P70275;Q3UH93","subunits.Entrez.IDs.":"20349;67784","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0023052;GO:0010183;GO:0030182;GO:0007420;GO:0001568;GO:0001944;GO:0005886","GO.description":"signaling;pollen tube guidance;neuron differentiation;brain development;blood vessel development;vasculature development;plasma membrane","FunCat.ID":"30.01;40.01.03.03;43.03.13;47.03.01.01.01;47.03.03.02;70.02","FunCat.description":"cellular signalling;guidance of longitudinal cell extension (e.g. pollen tube guidance, axonal pathfinding);neuron;brain;vessels;eukaryotic plasma membrane / membrane attached","PubMed.ID":18054858,"subunits.Protein.name.":"Semaphorin-3E;Plexin-D1","subunits.Gene.name.":"Sema3e;Plxnd1","subunits.Gene.name.syn.":"Semah Semh;None","Disease.comment":"None","Subunits.comment":"Mouse is used as reference organism.","Complex.comment":"Sema3E-PlexinD1 signaling plays an important role in initial development of descending axon tracts in the forebrain.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5626,"ComplexName":"Sema3E-PlexinD1-Nrp1 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS-7 cells","subunits.UniProt.IDs.":"P70275;P97333;Q3UH93","subunits.Entrez.IDs.":"20349;18186;67784","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0023052;GO:0010183;GO:0030182;GO:0007420;GO:0001568;GO:0001944;GO:0005886","GO.description":"signaling;pollen tube guidance;neuron differentiation;brain development;blood vessel development;vasculature development;plasma membrane","FunCat.ID":"30.01;40.01.03.03;43.03.13;47.03.01.01.01;47.03.03.02;70.02","FunCat.description":"cellular signalling;guidance of longitudinal cell extension (e.g. pollen tube guidance, axonal pathfinding);neuron;brain;vessels;eukaryotic plasma membrane / membrane attached","PubMed.ID":18054858,"subunits.Protein.name.":"Semaphorin-3E;Neuropilin-1;Plexin-D1","subunits.Gene.name.":"Sema3e;Nrp1;Plxnd1","subunits.Gene.name.syn.":"Semah Semh;Nrp;None","Disease.comment":"None","Subunits.comment":"Mouse is used as reference organism.","Complex.comment":"Sema3E-PlexinD1 signaling plays an important role in the initial development of descending axon tracts in the forebrain. Together with Npn1 the repulsive signaling of Sem3E-PlexinD1 is converted to attraction.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5627,"ComplexName":"Cdh23-Myo1c complex","Organism":"Mouse","Synonyms":"None","Cell.line":"ear","subunits.UniProt.IDs.":"Q99PF4;Q9WTI7","subunits.Entrez.IDs.":"22295;17913","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005216","GO.description":"ion channel activity","FunCat.ID":"20.03.01.01","FunCat.description":"ion channels","PubMed.ID":15057245,"subunits.Protein.name.":"Cadherin-23;Unconventional myosin-Ic","subunits.Gene.name.":"Cdh23;Myo1c","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"CDH23 and myosin-1c cooperate to regulate the activity of mechanically gated ion channels in hair cells.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5628,"ComplexName":"Ask1-Traf6 complex, LPS induced","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O35099;P70196","subunits.Entrez.IDs.":"26408;22034","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006955","GO.description":"immune response","FunCat.ID":"36.25.16","FunCat.description":"immune response","PubMed.ID":15864310,"subunits.Protein.name.":"Mitogen-activated protein kinase kinase kinase 5;TNF receptor-associated factor 6","subunits.Gene.name.":"Map3k5;Traf6","subunits.Gene.name.syn.":"Ask1 Mekk5;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"ASK1 formed a complex with TRAF6 in response to LPS (lipopolysaccharide), and this complex formation and subsequent ASK1 activation required LPS-induced production of reactive oxygen species (ROS).","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5629,"ComplexName":"Sema3E-PlexinD1 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS-1 cells","subunits.UniProt.IDs.":"P70275;Q3UH93","subunits.Entrez.IDs.":"20349;67784","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0023052;GO:0010183;GO:0030182;GO:0007420;GO:0001568;GO:0001944;GO:0005886","GO.description":"signaling;pollen tube guidance;neuron differentiation;brain development;blood vessel development;vasculature development;plasma membrane","FunCat.ID":"30.01;40.01.03.03;43.03.13;47.03.01.01.01;47.03.03.02;70.02","FunCat.description":"cellular signalling;guidance of longitudinal cell extension (e.g. pollen tube guidance, axonal pathfinding);neuron;brain;vessels;eukaryotic plasma membrane / membrane attached","PubMed.ID":15550623,"subunits.Protein.name.":"Semaphorin-3E;Plexin-D1","subunits.Gene.name.":"Sema3e;Plxnd1","subunits.Gene.name.syn.":"Semah Semh;None","Disease.comment":"None","Subunits.comment":"Mouse is used as reference organism.","Complex.comment":"Sema3E-PlexinD1 signaling does not require neuropilins, which were previously presumed to be obligate Sema3 coreceptors.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5641,"ComplexName":"PSD95-FYN-NR2A complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"P06241;P78352;Q12879","subunits.Entrez.IDs.":"2534;1742;2903","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0023052;GO:0005886","GO.description":"signaling;plasma membrane","FunCat.ID":"30.01;70.02","FunCat.description":"cellular signalling;eukaryotic plasma membrane / membrane attached","PubMed.ID":9892651,"subunits.Protein.name.":"Tyrosine-protein kinase Fyn;Disks large homolog 4 ;Glutamate receptor ionotropic, NMDA 2A","subunits.Gene.name.":"FYN;DLG4;GRIN2A","subunits.Gene.name.syn.":"None;PSD95;NMDAR2A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"NR2A was coimmunoprecipitated with Fyn only in the presence of PSD-95. So it was shown that PSD-95 induced formation of a ternary complex of NR2A, PSD-95, and Fyn.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5642,"ComplexName":"Securin-separase complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95997;Q14674","subunits.Entrez.IDs.":"9232;9700","Protein.complex.purification.method":"MI:0027- cosedimentation; MI:0071- molecular sieving","GO.ID":"GO:0000280;GO:0007059","GO.description":"nuclear division;chromosome segregation","FunCat.ID":"10.03.04.07;10.03.04.05","FunCat.description":"nuclear division;chromosome segregation/division","PubMed.ID":15880121,"subunits.Protein.name.":"Securin ;Separin","subunits.Gene.name.":"PTTG1;ESPL1","subunits.Gene.name.syn.":"EAP1 PTTG TUTR1;ESP1 KIAA0165","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5643,"ComplexName":"ESPL1-CDC2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06493;Q14674","subunits.Entrez.IDs.":"983;9700","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000280;GO:0007059","GO.description":"nuclear division;chromosome segregation","FunCat.ID":"10.03.04.07;10.03.04.05","FunCat.description":"nuclear division;chromosome segregation/division","PubMed.ID":15989971,"subunits.Protein.name.":"Cyclin-dependent kinase 1 ;Separin","subunits.Gene.name.":"CDK1;ESPL1","subunits.Gene.name.syn.":"CDC2 CDC28A CDKN1 P34CDC2;ESP1 KIAA0165","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5644,"ComplexName":"Sharpin homo-oligomer complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q9EQL9","subunits.Entrez.IDs.":"81859","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006461","GO.description":"protein complex assembly","FunCat.ID":"14.1","FunCat.description":"assembly of protein complexes","PubMed.ID":11178875,"subunits.Protein.name.":"Sharpin","subunits.Gene.name.":"Sharpin","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"Oligomer","Complex.comment":"The potential role of the multimerization of Sharpin is to provide a link between Shank and as yet undentified binding patner(s) of Sharpin.","SWISSPROT.organism":"Rattus norvegicus (Rat)"}
{"ComplexID":5645,"ComplexName":"Sharpin-Shank1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"Q9EQL9;Q9WV48","subunits.Entrez.IDs.":"81859;78957","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0035556","GO.description":"intracellular signal transduction","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":11178875,"subunits.Protein.name.":"Sharpin ;SH3 and multiple ankyrin repeat domains protein 1","subunits.Gene.name.":"Sharpin;Shank1","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5646,"ComplexName":"FARP2-NRP1-PlexinA1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"O14786;O94887;Q9UIW2","subunits.Entrez.IDs.":"8829;9855;5361","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0023052;GO:0007399","GO.description":"signaling;nervous system development","FunCat.ID":"30.01;47.03.01","FunCat.description":"cellular signalling;nervous system","PubMed.ID":16286926,"subunits.Protein.name.":"Neuropilin-1;FERM, RhoGEF and pleckstrin domain-containing protein 2 ;Plexin-A1","subunits.Gene.name.":"NRP1;FARP2;PLXNA1","subunits.Gene.name.syn.":"NRP VEGF165R;KIAA0793 PLEKHC3;NOV PLXN1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Interaction of FARP2 with PlexinA1 is substantially reduced in the absence of neuropilin1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5647,"ComplexName":"FARP2-NRP1-PlexinA2 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"O14786;O75051;O94887","subunits.Entrez.IDs.":"8829;5362;9855","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0023052;GO:0007399","GO.description":"signaling;nervous system development","FunCat.ID":"30.01;47.03.01","FunCat.description":"cellular signalling;nervous system","PubMed.ID":16286926,"subunits.Protein.name.":"Neuropilin-1;Plexin-A2 ;FERM, RhoGEF and pleckstrin domain-containing protein 2","subunits.Gene.name.":"NRP1;PLXNA2;FARP2","subunits.Gene.name.syn.":"NRP VEGF165R;KIAA0463 OCT PLXN2;KIAA0793 PLEKHC3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5648,"ComplexName":"FARP2-NRP1-PlexinA3 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"O14786;O94887;P51805","subunits.Entrez.IDs.":"8829;9855;55558","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0023052;GO:0007399","GO.description":"signaling;nervous system development","FunCat.ID":"30.01;47.03.01","FunCat.description":"cellular signalling;nervous system","PubMed.ID":16286926,"subunits.Protein.name.":"Neuropilin-1;FERM, RhoGEF and pleckstrin domain-containing protein 2 ;Plexin-A3","subunits.Gene.name.":"NRP1;FARP2;PLXNA3","subunits.Gene.name.syn.":"NRP VEGF165R;KIAA0793 PLEKHC3;PLXN4 SEX","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5649,"ComplexName":"FARP2-NRP1-PlexinA4 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"O14786;O94887;Q9HCM2","subunits.Entrez.IDs.":"8829;9855;91584","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0023052;GO:0007399","GO.description":"signaling;nervous system development","FunCat.ID":"30.01;47.03.01","FunCat.description":"cellular signalling;nervous system","PubMed.ID":16286926,"subunits.Protein.name.":"Neuropilin-1;FERM, RhoGEF and pleckstrin domain-containing protein 2 ;Plexin-A4","subunits.Gene.name.":"NRP1;FARP2;PLXNA4","subunits.Gene.name.syn.":"NRP VEGF165R;KIAA0793 PLEKHC3;KIAA1550 PLXNA4A PLXNA4B","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5654,"ComplexName":"SEMA4A-PlexinD1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q9H3S1;Q9Y4D7","subunits.Entrez.IDs.":"64218;23129","Protein.complex.purification.method":"MI:0030- cross-linking studies","GO.ID":"GO:0023052;GO:0010183;GO:0001525;GO:0001568;GO:0001944","GO.description":"signaling;pollen tube guidance;angiogenesis;blood vessel development;vasculature development","FunCat.ID":"30.01;40.01.03.03;41.05.16;47.03.03.02","FunCat.description":"cellular signalling;guidance of longitudinal cell extension (e.g. pollen tube guidance, axonal pathfinding);angiogenesis;vessels","PubMed.ID":17318185,"subunits.Protein.name.":"Semaphorin-4A ;Plexin-D1","subunits.Gene.name.":"SEMA4A;PLXND1","subunits.Gene.name.syn.":"SEMAB SEMB;KIAA0620","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SEMA4A-PlexinD1 signaling negatively regulates angiogenesis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5655,"ComplexName":"Ternary complex (LRRC7, CAMK2a, ACTN4)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43707;Q96NW7;Q9UQM7","subunits.Entrez.IDs.":"81;57554;815","Protein.complex.purification.method":"MI:0397- two hybrid array; MI:0019- coimmunoprecipitation","GO.ID":"GO:0007155","GO.description":"cell adhesion","FunCat.ID":"34.07","FunCat.description":"cell adhesion","PubMed.ID":11160423,"subunits.Protein.name.":"Alpha-actinin-4;Leucine-rich repeat-containing protein 7 ;Calcium/calmodulin-dependent protein kinase type II subunit alpha","subunits.Gene.name.":"ACTN4;LRRC7;CAMK2A","subunits.Gene.name.syn.":"None;KIAA1365 LAP1;CAMKA KIAA0968","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5656,"ComplexName":"CEBPE-E2F1-RB1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06400;Q01094;Q15744","subunits.Entrez.IDs.":"5925;1869;1053","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030851","GO.description":"granulocyte differentiation","FunCat.ID":"43.03.07.02.02","FunCat.description":"granulocyte","PubMed.ID":12947005,"subunits.Protein.name.":"Retinoblastoma-associated protein ;Transcription factor E2F1;CCAAT/enhancer-binding protein epsilon","subunits.Gene.name.":"RB1;E2F1;CEBPE","subunits.Gene.name.syn.":";RBBP3;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5658,"ComplexName":"Nrp1-PlexinD1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"O14786;Q9Y4D7","subunits.Entrez.IDs.":"8829;23129","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0023052;GO:0010183;GO:0001525;GO:0048738;GO:0007507;GO:0001568;GO:0001944","GO.description":"signaling;pollen tube guidance;angiogenesis;cardiac muscle tissue development;heart development;blood vessel development;vasculature development","FunCat.ID":"30.01;40.01.03.03;41.05.16;45.03.12.03;47.03.03.02","FunCat.description":"cellular signalling;guidance of longitudinal cell extension (e.g. pollen tube guidance, axonal pathfinding);angiogenesis;heart muscle;vessels","PubMed.ID":15239958,"subunits.Protein.name.":"Neuropilin-1;Plexin-D1","subunits.Gene.name.":"NRP1;PLXND1","subunits.Gene.name.syn.":"NRP VEGF165R;KIAA0620","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"PlexinD1-Npn1 form a functional receptor for Sema3C.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5659,"ComplexName":"SEMA3C-PlexinD1-Nrp1 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS-7 cells","subunits.UniProt.IDs.":"O14786;Q99985;Q9Y4D7","subunits.Entrez.IDs.":"8829;10512;23129","Protein.complex.purification.method":"MI:0428- imaging techniques","GO.ID":"GO:0023052;GO:0010183;GO:0001525;GO:0048738;GO:0007507;GO:0001568;GO:0001944","GO.description":"signaling;pollen tube guidance;angiogenesis;cardiac muscle tissue development;heart development;blood vessel development;vasculature development","FunCat.ID":"30.01;40.01.03.03;41.05.16;45.03.12.03;47.03.03.02","FunCat.description":"cellular signalling;guidance of longitudinal cell extension (e.g. pollen tube guidance, axonal pathfinding);angiogenesis;heart muscle;vessels","PubMed.ID":15239958,"subunits.Protein.name.":"Neuropilin-1;Semaphorin-3C ;Plexin-D1","subunits.Gene.name.":"NRP1;SEMA3C;PLXND1","subunits.Gene.name.syn.":"NRP VEGF165R;SEMAE;KIAA0620","Disease.comment":"None","Subunits.comment":"Human is used as reference organism.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5660,"ComplexName":"PlexinC1-SEMA7A complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"O60486;O75326","subunits.Entrez.IDs.":"10154;8482","Protein.complex.purification.method":"MI:0428- imaging techniques","GO.ID":"GO:0023052;GO:0010183","GO.description":"signaling;pollen tube guidance","FunCat.ID":"30.01;40.01.03.03","FunCat.description":"cellular signalling;guidance of longitudinal cell extension (e.g. pollen tube guidance, axonal pathfinding)","PubMed.ID":10520995,"subunits.Protein.name.":"Plexin-C1 ;Semaphorin-7A","subunits.Gene.name.":"PLXNC1;SEMA7A","subunits.Gene.name.syn.":"VESPR;CD108 SEMAL","Disease.comment":"None","Subunits.comment":"Human is used as reference organism.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5661,"ComplexName":"PlexinC1-SEMA7A complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"O43157;Q92854","subunits.Entrez.IDs.":"5364;10507","Protein.complex.purification.method":"MI:0428- imaging techniques","GO.ID":"GO:0023052;GO:0010183","GO.description":"signaling;pollen tube guidance","FunCat.ID":"30.01;40.01.03.03","FunCat.description":"cellular signalling;guidance of longitudinal cell extension (e.g. pollen tube guidance, axonal pathfinding)","PubMed.ID":10520995,"subunits.Protein.name.":"Plexin-B1 ;Semaphorin-4D","subunits.Gene.name.":"PLXNB1;SEMA4D","subunits.Gene.name.syn.":"KIAA0407 PLXN5 SEP;C9orf164 CD100 SEMAJ","Disease.comment":"None","Subunits.comment":"Human is used as reference organism.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5663,"ComplexName":"TRIM27-RB1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06400;P14373","subunits.Entrez.IDs.":"5925;5987","Protein.complex.purification.method":"MI:0096- pull down; MI:0019- coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":15837424,"subunits.Protein.name.":"Retinoblastoma-associated protein ;Zinc finger protein RFP","subunits.Gene.name.":"RB1;TRIM27","subunits.Gene.name.syn.":";RFP RNF76","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5668,"ComplexName":"PlexinA1-Nrp1 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"O14786;Q9UIW2","subunits.Entrez.IDs.":"8829;5361","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0023052;GO:0010183;GO:0007399","GO.description":"signaling;pollen tube guidance;nervous system development","FunCat.ID":"30.01;40.01.03.03;47.03.01","FunCat.description":"cellular signalling;guidance of longitudinal cell extension (e.g. pollen tube guidance, axonal pathfinding);nervous system","PubMed.ID":10520995,"subunits.Protein.name.":"Neuropilin-1;Plexin-A1","subunits.Gene.name.":"NRP1;PLXNA1","subunits.Gene.name.syn.":"NRP VEGF165R;NOV PLXN1","Disease.comment":"None","Subunits.comment":"The orthologous human proteins are used.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5669,"ComplexName":"PlexinA3-Nrp1 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"O14786;P51805","subunits.Entrez.IDs.":"8829;55558","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0023052;GO:0010183;GO:0007399","GO.description":"signaling;pollen tube guidance;nervous system development","FunCat.ID":"30.01;40.01.03.03;47.03.01","FunCat.description":"cellular signalling;guidance of longitudinal cell extension (e.g. pollen tube guidance, axonal pathfinding);nervous system","PubMed.ID":10520995,"subunits.Protein.name.":"Neuropilin-1;Plexin-A3","subunits.Gene.name.":"NRP1;PLXNA3","subunits.Gene.name.syn.":"NRP VEGF165R;PLXN4 SEX","Disease.comment":"None","Subunits.comment":"Human is used as reference organism","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5670,"ComplexName":"PlexinB1-Nrp1 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"O14786;O43157","subunits.Entrez.IDs.":"8829;5364","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0023052;GO:0010183;GO:0007399","GO.description":"signaling;pollen tube guidance;nervous system development","FunCat.ID":"30.01;40.01.03.03;47.03.01","FunCat.description":"cellular signalling;guidance of longitudinal cell extension (e.g. pollen tube guidance, axonal pathfinding);nervous system","PubMed.ID":10520995,"subunits.Protein.name.":"Neuropilin-1;Plexin-B1","subunits.Gene.name.":"NRP1;PLXNB1","subunits.Gene.name.syn.":"NRP VEGF165R;KIAA0407 PLXN5 SEP","Disease.comment":"None","Subunits.comment":"Human is used as reference organism.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5673,"ComplexName":"PlexinA1-Nrp2 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"O60462;Q9UIW2","subunits.Entrez.IDs.":"8828;5361","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0023052;GO:0010183;GO:0007399","GO.description":"signaling;pollen tube guidance;nervous system development","FunCat.ID":"30.01;40.01.03.03;47.03.01","FunCat.description":"cellular signalling;guidance of longitudinal cell extension (e.g. pollen tube guidance, axonal pathfinding);nervous system","PubMed.ID":10520995,"subunits.Protein.name.":"Neuropilin-2 ;Plexin-A1","subunits.Gene.name.":"NRP2;PLXNA1","subunits.Gene.name.syn.":"VEGF165R2;NOV PLXN1","Disease.comment":"None","Subunits.comment":"The orthologous human/mouse proteins are used.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5682,"ComplexName":"Retn homotrimer  complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q99P87","subunits.Entrez.IDs.":"57264","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0043609;GO:0043610;GO:0006109;GO:0042445","GO.description":"regulation of carbon utilization;regulation of carbohydrate utilization;regulation of carbohydrate metabolic process;hormone metabolic process","FunCat.ID":"01.05.25;01.08.02","FunCat.description":"regulation of C-compound and carbohydrate metabolism;metabolism of hormones","PubMed.ID":15155948,"subunits.Protein.name.":"Resistin","subunits.Gene.name.":"Retn","subunits.Gene.name.syn.":"Fizz3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse)"}
{"ComplexID":5683,"ComplexName":"hRAD51C-hXRCC3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43543;Q06609","subunits.Entrez.IDs.":"7516;5888","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006281","GO.description":"DNA repair","FunCat.ID":"10.01.05.01","FunCat.description":"DNA repair","PubMed.ID":15123651,"subunits.Protein.name.":"DNA repair protein XRCC2 ;DNA repair protein RAD51 homolog 1","subunits.Gene.name.":"XRCC2;RAD51","subunits.Gene.name.syn.":";RAD51A RECA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5684,"ComplexName":"Membrane protein complex (DERL1, SELS, VCP)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P55072;Q9BQE4;Q9BUN8","subunits.Entrez.IDs.":"7415;55829;79139","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0051- fluorescence technologies","GO.ID":"GO:0030970","GO.description":"retrograde protein transport, ER to cytosol","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":15215856,"subunits.Protein.name.":"Transitional endoplasmic reticulum ATPase;Selenoprotein S ;Derlin-1","subunits.Gene.name.":"VCP;VIMP;DERL1","subunits.Gene.name.syn.":"None;SELS;DER1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5685,"ComplexName":"Membrane protein complex (VCP, UFD1L, SEC61B)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P55072;P60468;Q92890","subunits.Entrez.IDs.":"7415;10952;7353","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030970","GO.description":"retrograde protein transport, ER to cytosol","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":15215856,"subunits.Protein.name.":"Transitional endoplasmic reticulum ATPase;Protein transport protein Sec61 subunit beta;Ubiquitin fusion degradation protein 1 homolog","subunits.Gene.name.":"VCP;SEC61B;UFD1L","subunits.Gene.name.syn.":"None;None;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5689,"ComplexName":"SEMA6D-PlexinA1-NRP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"O14786;Q8NFY4;Q9UIW2","subunits.Entrez.IDs.":"8829;80031;5361","Protein.complex.purification.method":"MI:0428-imaging techniques","GO.ID":"GO:0023052;GO:0010183;GO:0048738;GO:0007507;GO:0007399","GO.description":"signaling;pollen tube guidance;cardiac muscle tissue development;heart development;nervous system development","FunCat.ID":"30.01;40.01.03.03;45.03.12.03;47.03.01","FunCat.description":"cellular signalling;guidance of longitudinal cell extension (e.g. pollen tube guidance, axonal pathfinding);heart muscle;nervous system","PubMed.ID":14977921,"subunits.Protein.name.":"Neuropilin-1;Semaphorin-6D;Plexin-A1","subunits.Gene.name.":"NRP1;SEMA6D;PLXNA1","subunits.Gene.name.syn.":"NRP VEGF165R;KIAA1479;NOV PLXN1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5691,"ComplexName":"TALL1 homo-oligomer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q9Y275","subunits.Entrez.IDs.":"10673","Protein.complex.purification.method":"MI:0071- molecular sieving; MI:0114- x-ray crystallography","GO.ID":"GO:0030183","GO.description":"B cell differentiation","FunCat.ID":"43.03.07.02.01.01","FunCat.description":"B-cell","PubMed.ID":14749821,"subunits.Protein.name.":"Tumor necrosis factor ligand superfamily member 13B","subunits.Gene.name.":"TNFSF13B","subunits.Gene.name.syn.":"BAFF BLYS TALL1 TNFSF20 ZTNF4","Disease.comment":"None","Subunits.comment":"Oligomer","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":5693,"ComplexName":"Tip5-Dnmt-Hdac1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O09106;O88509;P13864;Q91YE5","subunits.Entrez.IDs.":"433759;13436;13433;116848","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:2001141;GO:0006355;GO:0006473;GO:0006476;GO:0003677","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;DNA binding","FunCat.ID":"11.02.03.04;14.07.04;16.03.01","FunCat.description":"transcriptional control;modification by acetylation, deacetylation;DNA binding","PubMed.ID":16085498,"subunits.Protein.name.":"Histone deacetylase 1;DNA ;DNA ;Bromodomain adjacent to zinc finger domain protein 2A","subunits.Gene.name.":"Hdac1;Dnmt3b;Dnmt1;Baz2a","subunits.Gene.name.syn.":"None;;Dnmt Met1 Uim;Kiaa0314 Tip5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5694,"ComplexName":"Nucleolar remodeling complex (NoRC complex)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60264;Q9UIF9","subunits.Entrez.IDs.":"8467;11176","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006265;GO:0009303;GO:0051276","GO.description":"DNA topological change;rRNA transcription;chromosome organization","FunCat.ID":"10.01.09.05;11.02.01;42.10.03","FunCat.description":"DNA conformation modification (e.g. chromatin);rRNA synthesis;organization of chromosome structure","PubMed.ID":16085498,"subunits.Protein.name.":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5;Bromodomain adjacent to zinc finger domain protein 2A","subunits.Gene.name.":"SMARCA5;BAZ2A","subunits.Gene.name.syn.":"SNF2H WCRF135;KIAA0314 TIP5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5695,"ComplexName":"TIP5-DNMT-HDAC1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P26358;Q13547;Q9UBC3;Q9UIF9","subunits.Entrez.IDs.":"1786;3065;1789;11176","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:2001141;GO:0006355;GO:0006473;GO:0006476;GO:0003677","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;protein acetylation;protein deacetylation;DNA binding","FunCat.ID":"11.02.03.04;14.07.04;16.03.01","FunCat.description":"transcriptional control;modification by acetylation, deacetylation;DNA binding","PubMed.ID":16085498,"subunits.Protein.name.":"DNA ;Histone deacetylase 1;DNA;Bromodomain adjacent to zinc finger domain protein 2A","subunits.Gene.name.":"DNMT1;HDAC1;DNMT3B;BAZ2A","subunits.Gene.name.syn.":"AIM CXXC9 DNMT;RPD3L1;None;KIAA0314 TIP5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5696,"ComplexName":"VEGFA(165)-KDR-NRP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14786;P15692;P35968","subunits.Entrez.IDs.":"8829;7422;3791","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0007169;GO:0001525;GO:0001568;GO:0001944","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway;angiogenesis;blood vessel development;vasculature development","FunCat.ID":"30.05.01.12;41.05.16;47.03.03.02","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways;angiogenesis;vessels","PubMed.ID":11948691,"subunits.Protein.name.":"Neuropilin-1;Vascular endothelial growth factor A ;Vascular endothelial growth factor receptor 2","subunits.Gene.name.":"NRP1;VEGFA;KDR","subunits.Gene.name.syn.":"NRP VEGF165R;VEGF;FLK1, VEGFR2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Binding of the isoform VEGF(165) to NRP1 is essential for the association of NRP1 and KDR. In contrast, isoform VEGF(121) does no support the complex formation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5697,"ComplexName":"VEGFA(165)-KDR-NRP1 complex","Organism":"Pig","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14786;P49151;Q9N0K7","subunits.Entrez.IDs.":"8829;397157;None","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0007167;GO:0001525;GO:0001568;GO:0001944","GO.description":"enzyme linked receptor protein signaling pathway;angiogenesis;blood vessel development;vasculature development","FunCat.ID":"30.05.01;41.05.16;47.03.03.02","FunCat.description":"receptor enzyme mediated signalling;angiogenesis;vessels","PubMed.ID":11948691,"subunits.Protein.name.":"Neuropilin-1;Vascular endothelial growth factor A ;Flk-1 type VEGF receptor","subunits.Gene.name.":"NRP1;VEGFA;flk-1","subunits.Gene.name.syn.":"NRP VEGF165R;VEGF;","Disease.comment":"None","Subunits.comment":"Since NRP1 from pig was not available in the UniProt database at the time of annotation, the orthologous human protein was used.","Complex.comment":"Binding of the isoform VEGF(165) to NRP1 is essential for the association of NRP1 and KDR. In contrast, isoform VEGF(121) does not support the complex formation.","SWISSPROT.organism":"Homo sapiens (Human);Sus scrofa (Pig);Sus scrofa (Pig)"}
{"ComplexID":5698,"ComplexName":"VEGFA(165)-VEGFR2-NRP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14786;P15692;P35968","subunits.Entrez.IDs.":"8829;7422;3791","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0007169;GO:0001525;GO:0001568;GO:0001944","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway;angiogenesis;blood vessel development;vasculature development","FunCat.ID":"30.05.01.12;41.05.16;47.03.03.02","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways;angiogenesis;vessels","PubMed.ID":18628209,"subunits.Protein.name.":"Neuropilin-1;Vascular endothelial growth factor A ;Vascular endothelial growth factor receptor 2","subunits.Gene.name.":"NRP1;VEGFA;KDR","subunits.Gene.name.syn.":"NRP VEGF165R;VEGF;FLK1, VEGFR2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"VEGFR2 and NRP1 associate upon stimulation with VEGF(165). Phosphorylation of VEGFR2 is required for this association.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5701,"ComplexName":"NRP1-VEGF(165/121) complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14786;P15692","subunits.Entrez.IDs.":"8829;7422","Protein.complex.purification.method":"MI:0107- surface plasmon resonance","GO.ID":"GO:0001525;GO:0001568;GO:0001944","GO.description":"angiogenesis;blood vessel development;vasculature development","FunCat.ID":"41.05.16;47.03.03.02","FunCat.description":"angiogenesis;vessels","PubMed.ID":17575273,"subunits.Protein.name.":"Neuropilin-1;Vascular endothelial growth factor A","subunits.Gene.name.":"NRP1;VEGFA","subunits.Gene.name.syn.":"NRP VEGF165R;VEGF","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In contrast to former publications (PMID:10991952), both isoforms of VEGFA, VEGF(165) and VEGF(121), bind to NRP1, but only VEGF165 is sufficient to promote complex formation between VEGFR2 and NRP1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5702,"ComplexName":"VEGF-KDR-NRP2 complex","Organism":"Pig","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P49151;Q5RLQ5;Q9N0K7","subunits.Entrez.IDs.":"397157;None;None","Protein.complex.purification.method":"MI:0031- protein cross-linking with a bifunctional re","GO.ID":"GO:0007167;GO:0001525;GO:0001568;GO:0001944","GO.description":"enzyme linked receptor protein signaling pathway;angiogenesis;blood vessel development;vasculature development","FunCat.ID":"30.05.01;41.05.16;47.03.03.02","FunCat.description":"receptor enzyme mediated signalling;angiogenesis;vessels","PubMed.ID":11278319,"subunits.Protein.name.":"Vascular endothelial growth factor A ;Neuropilin 2 ;Flk-1 type VEGF receptor","subunits.Gene.name.":"VEGFA;NRP2;flk-1","subunits.Gene.name.syn.":"VEGF;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Sus scrofa (Pig);Sus scrofa (Pig);Sus scrofa (Pig)"}
{"ComplexID":5703,"ComplexName":"Bash-Bnas2/Cmtm3-Btk-Erk2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P35991;P63085;Q99LJ5;Q9QUN3","subunits.Entrez.IDs.":"12229;26413;68119;17060","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007166","GO.description":"cell surface receptor signaling pathway","FunCat.ID":"30.05","FunCat.description":"transmembrane signal transduction","PubMed.ID":15087455,"subunits.Protein.name.":"Tyrosine-protein kinase BTK ;Mitogen-activated protein kinase 1;CKLF-like MARVEL transmembrane domain-containing protein 3 ;B-cell linker protein","subunits.Gene.name.":"Btk;Mapk1;Cmtm3;Blnk","subunits.Gene.name.syn.":"Bpk;Erk2, Mapk, Prkm1;Cklfsf3;Bash Ly57 Slp65","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5705,"ComplexName":"CyclinA2-Cdk2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P51943;P97377","subunits.Entrez.IDs.":"12428;12566","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007049;GO:0006974","GO.description":"cell cycle;cellular response to DNA damage stimulus","FunCat.ID":"10.03;32.01.09","FunCat.description":"cell cycle;DNA damage response","PubMed.ID":9371520,"subunits.Protein.name.":"Cyclin-A2 ;Cyclin-dependent kinase 2","subunits.Gene.name.":"Ccna2;Cdk2","subunits.Gene.name.syn.":"Ccna Cyca;Cdkn2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5706,"ComplexName":"CyclinB1-Cdc2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P11440;P24860","subunits.Entrez.IDs.":"12534;268697","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007049;GO:0006974","GO.description":"cell cycle;cellular response to DNA damage stimulus","FunCat.ID":"10.03;32.01.09","FunCat.description":"cell cycle;DNA damage response","PubMed.ID":9371520,"subunits.Protein.name.":"Cyclin-dependent kinase 1 ;G2/mitotic-specific cyclin-B1","subunits.Gene.name.":"Cdk1;Ccnb1","subunits.Gene.name.syn.":"Cdc2 Cdc2a Cdkn1;Ccn-2 Ccnb1-rs13 Cycb Cycb1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5707,"ComplexName":"Ternary complex (Abl1, Dok1, Nck1)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P00520;P97465;Q8BMV0","subunits.Entrez.IDs.":"11350;13448;17973","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030036;GO:0001649","GO.description":"actin cytoskeleton organization;osteoblast differentiation","FunCat.ID":"42.04.03;43.03.17","FunCat.description":"actin cytoskeleton;structural cell of tissue (fibroblast, osteoblast, etc.)","PubMed.ID":15148308,"subunits.Protein.name.":"Tyrosine-protein kinase ABL1 ;Docking protein 1 ;Putative uncharacterized protein","subunits.Gene.name.":"Abl1;Dok1;Nck1","subunits.Gene.name.syn.":"Abl;Dok;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Mouse fibroblasts lacking c-Abl, Dok1, or Nck had fewer filopodia than cells reexpressing the product of the disrupted gene. Dok1 and c-Abl were both detected in filopodia of spreading cells, and therefore may act locally to modulate actin. The data suggest a novel pathway by which c-Abl transduces signals to the actin cytoskeleton through phosphorylating Dok1 Y361 and recruiting Nck.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5708,"ComplexName":"Dok1-Map4k4-Nck1-Rasa1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P97465;P97820;Q8BMV0;Q91YX7","subunits.Entrez.IDs.":"13448;26921;17973;218397","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0007169","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;transmembrane receptor protein tyrosine kinase signaling pathway","FunCat.ID":"14.07.03;30.05.01.12","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;transmembrane receptor protein tyrosine kinase signalling pathways","PubMed.ID":10669731,"subunits.Protein.name.":"Docking protein 1 ;Mitogen-activated protein kinase kinase kinase kinase 4 ;Putative uncharacterized protein ;RAS p21 protein activator 1","subunits.Gene.name.":"Dok1;Map4k4;Nck1;Rasa1","subunits.Gene.name.syn.":"Dok;Nik;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5709,"ComplexName":"ArgBP2a-CBL-PTK2B complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O94875;P22681;Q14289","subunits.Entrez.IDs.":"8470;867;2185","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006886;GO:0006605;GO:0015031;GO:0030036;GO:0030182","GO.description":"intracellular protein transport;protein targeting;protein transport;actin cytoskeleton organization;neuron differentiation","FunCat.ID":"14.04;20.01.10;42.04.03;43.03.13","FunCat.description":"protein targeting, sorting and translocation;protein transport;actin cytoskeleton;neuron","PubMed.ID":15128873,"subunits.Protein.name.":"Sorbin and SH3 domain-containing protein 2 ;E3 ubiquitin-protein ligase CBL;Protein-tyrosine kinase 2-beta","subunits.Gene.name.":"SORBS2;CBL;PTK2B","subunits.Gene.name.syn.":"ARGBP2 KIAA0777;CBL2, RNF55;FAK2 PYK2 RAFTK","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5710,"ComplexName":"PRMT2 homo-oligomer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P55345","subunits.Entrez.IDs.":"3275","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0030545","GO.description":"receptor regulator activity","FunCat.ID":"18.02.07","FunCat.description":"regulator of receptor activity","PubMed.ID":12039952,"subunits.Protein.name.":"Protein arginine N-methyltransferase 2","subunits.Gene.name.":"PRMT2","subunits.Gene.name.syn.":"HMT1 HRMT1L1","Disease.comment":"None","Subunits.comment":"Oligomer","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":5712,"ComplexName":"FAK-beta5 integrin complex, VEGF induced","Organism":"Human","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P18084;Q05397","subunits.Entrez.IDs.":"3693;5747","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0007169;GO:0001525;GO:0007044","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway;angiogenesis;cell-substrate junction assembly","FunCat.ID":"30.05.01.12;41.05.16;42.06.03","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways;angiogenesis;cell-substrate adherens junction","PubMed.ID":12844492,"subunits.Protein.name.":"Integrin beta-5;Focal adhesion kinase 1","subunits.Gene.name.":"ITGB5;PTK2","subunits.Gene.name.syn.":";FAK FAK1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"VEGF induces the formation of FAK-beta5 integrin complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5713,"ComplexName":"SH3P2/OSTF1-CBL-SRC complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12931;P22681;Q92882","subunits.Entrez.IDs.":"6714;867;26578","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0047- far western blotting","GO.ID":"GO:0007155;GO:0015629","GO.description":"cell adhesion;actin cytoskeleton","FunCat.ID":"34.07;70.04.03","FunCat.description":"cell adhesion;actin cytoskeleton","PubMed.ID":15135048,"subunits.Protein.name.":"Proto-oncogene tyrosine-protein kinase Src;E3 ubiquitin-protein ligase CBL;Osteoclast-stimulating factor 1","subunits.Gene.name.":"SRC;CBL;OSTF1","subunits.Gene.name.syn.":"SRC1;CBL2, RNF55;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5714,"ComplexName":"eNOS-CAV1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P29474;Q03135","subunits.Entrez.IDs.":"4846;857","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0006808;GO:0051171;GO:0007263","GO.description":"regulation of nitrogen utilization;regulation of nitrogen compound metabolic process;nitric oxide mediated signal transduction","FunCat.ID":"01.02.07.01;30.01.09.01","FunCat.description":"regulation of nitrogen metabolism;NO mediated signal transduction","PubMed.ID":11425855,"subunits.Protein.name.":"Nitric oxide synthase, endothelial;Caveolin-1","subunits.Gene.name.":"NOS3;CAV1","subunits.Gene.name.syn.":"None;CAV","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5716,"ComplexName":"eNOS-HSP90 complex, VEGF induced","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P07900;P29474","subunits.Entrez.IDs.":"3320;4846","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0006809;GO:0006808;GO:0051171;GO:0007263;GO:0007169;GO:0001525","GO.description":"nitric oxide biosynthetic process;regulation of nitrogen utilization;regulation of nitrogen compound metabolic process;nitric oxide mediated signal transduction;transmembrane receptor protein tyrosine kinase signaling pathway;angiogenesis","FunCat.ID":"01.02.02.07;01.02.07.01;30.01.09.01;30.05.01.12;41.05.16","FunCat.description":"nitric oxide biosynthesis;regulation of nitrogen metabolism;NO mediated signal transduction;transmembrane receptor protein tyrosine kinase signalling pathways;angiogenesis","PubMed.ID":11425855,"subunits.Protein.name.":"Heat shock protein HSP 90-alpha;Nitric oxide synthase, endothelial","subunits.Gene.name.":"HSP90AA1;NOS3","subunits.Gene.name.syn.":"HSP90A HSPC1 HSPCA;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"VEGF stimulation promotes dissociation of eNOS and Caveolin and association of eNOS with HSP90.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5718,"ComplexName":"eNOS-HSP90-AKT complex, VEGF induced","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P07900;P29474;P31749","subunits.Entrez.IDs.":"3320;4846;207","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0006809;GO:0006808;GO:0051171;GO:0007263;GO:0007169;GO:0001525","GO.description":"nitric oxide biosynthetic process;regulation of nitrogen utilization;regulation of nitrogen compound metabolic process;nitric oxide mediated signal transduction;transmembrane receptor protein tyrosine kinase signaling pathway;angiogenesis","FunCat.ID":"01.02.02.07;01.02.07.01;30.01.09.01;30.05.01.12;41.05.16","FunCat.description":"nitric oxide biosynthesis;regulation of nitrogen metabolism;NO mediated signal transduction;transmembrane receptor protein tyrosine kinase signalling pathways;angiogenesis","PubMed.ID":11425855,"subunits.Protein.name.":"Heat shock protein HSP 90-alpha;Nitric oxide synthase, endothelial;RAC-alpha serine/threonine-protein kinase","subunits.Gene.name.":"HSP90AA1;NOS3;AKT1","subunits.Gene.name.syn.":"HSP90A HSPC1 HSPCA;None;PKB, RAC","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"VEGF stimulation promotes association of eNOS with HSP90 and AKT.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5719,"ComplexName":"eNos3-Calmodulin complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62161;Q62600","subunits.Entrez.IDs.":"None;24600","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0006808;GO:0051171;GO:0007263;GO:0019722","GO.description":"regulation of nitrogen utilization;regulation of nitrogen compound metabolic process;nitric oxide mediated signal transduction;calcium-mediated signaling","FunCat.ID":"01.02.07.01;30.01.09.01;30.01.09.03","FunCat.description":"regulation of nitrogen metabolism;NO mediated signal transduction;Ca2+ mediated signal transduction","PubMed.ID":9856995,"subunits.Protein.name.":"Calmodulin;Nitric oxide synthase, endothelial","subunits.Gene.name.":"Calm1; Cal;Nos3","subunits.Gene.name.syn.":"Calm, Cam, Cam1, Cam2, Camb, Cam3, Camc;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5720,"ComplexName":"CIN85-CBL complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"P22681;Q96B97","subunits.Entrez.IDs.":"867;30011","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0006900;GO:0016050;GO:0006897","GO.description":"membrane budding;vesicle organization;endocytosis","FunCat.ID":"20.09.07.25;20.09.18.09.01","FunCat.description":"vesicle formation;endocytosis","PubMed.ID":11894095,"subunits.Protein.name.":"E3 ubiquitin-protein ligase CBL;SH3 domain-containing kinase-binding protein 1","subunits.Gene.name.":"CBL;SH3KBP1","subunits.Gene.name.syn.":"CBL2, RNF55;CIN85","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5721,"ComplexName":"CIN85-CBL-SH3GL2 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"P22681;Q96B97;Q99962","subunits.Entrez.IDs.":"867;30011;6456","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006900;GO:0016050;GO:0006897","GO.description":"membrane budding;vesicle organization;endocytosis","FunCat.ID":"20.09.07.25;20.09.18.09.01","FunCat.description":"vesicle formation;endocytosis","PubMed.ID":11894095,"subunits.Protein.name.":"E3 ubiquitin-protein ligase CBL;SH3 domain-containing kinase-binding protein 1;Endophilin-A1","subunits.Gene.name.":"CBL;SH3KBP1;SH3GL2","subunits.Gene.name.syn.":"CBL2, RNF55;CIN85;CNSA2 SH3D2A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Endogenous or overexpressed Cbl co-precipitated with endophilin A1 only in the presence of CIN85, indicating that CIN85 acts as a linker between Cbl and endophilins.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5722,"ComplexName":"Cbl-Cd2ap complex","Organism":"Mouse","Synonyms":"None","Cell.line":"NIH 3T3 cells","subunits.UniProt.IDs.":"P22682;Q9JLQ0","subunits.Entrez.IDs.":"12402;12488","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0005515;GO:0006897;GO:0030133","GO.description":"protein binding;endocytosis;transport vesicle","FunCat.ID":"16.01;20.09.18.09.01;70.09","FunCat.description":"protein binding;endocytosis;intracellular transport vesicles","PubMed.ID":15001553,"subunits.Protein.name.":"E3 ubiquitin-protein ligase CBL;CD2-associated protein","subunits.Gene.name.":"Cbl;Cd2ap","subunits.Gene.name.syn.":"None;Mets1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5723,"ComplexName":"Cbl-Cd2ap-Flt1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"NIH 3T3 cells","subunits.UniProt.IDs.":"P22682;P35969;Q9JLQ0","subunits.Entrez.IDs.":"12402;14254;12488","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0006897;GO:0007169;GO:0001525;GO:0030133","GO.description":"protein ubiquitination;protein deubiquitination;endocytosis;transmembrane receptor protein tyrosine kinase signaling pathway;angiogenesis;transport vesicle","FunCat.ID":"14.07.05;20.09.18.09.01;30.05.01.12;41.05.16;70.09","FunCat.description":"modification by ubiquitination, deubiquitination;endocytosis;transmembrane receptor protein tyrosine kinase signalling pathways;angiogenesis;intracellular transport vesicles","PubMed.ID":15001553,"subunits.Protein.name.":"E3 ubiquitin-protein ligase CBL;Vascular endothelial growth factor receptor 1;CD2-associated protein","subunits.Gene.name.":"Cbl;Flt1;Cd2ap","subunits.Gene.name.syn.":"None;Emrk2 Flt Vegfr1;Mets1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"After VEGF stimulation the Cbl-Cda2p complex binds to activated Flt-1 and plays a crucial role in endocytosis and subsequent ubiquitination of Flt-1.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5724,"ComplexName":"CIN85-SH3GL3-CBL complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"P22681;Q96B97;Q99963","subunits.Entrez.IDs.":"867;30011;6457","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006900;GO:0016050;GO:0006897;GO:0007169","GO.description":"membrane budding;vesicle organization;endocytosis;transmembrane receptor protein tyrosine kinase signaling pathway","FunCat.ID":"20.09.07.25;20.09.18.09.01;30.05.01.12","FunCat.description":"vesicle formation;endocytosis;transmembrane receptor protein tyrosine kinase signalling pathways","PubMed.ID":11894096,"subunits.Protein.name.":"E3 ubiquitin-protein ligase CBL;SH3 domain-containing kinase-binding protein 1;Endophilin-A3","subunits.Gene.name.":"CBL;SH3KBP1;SH3GL3","subunits.Gene.name.syn.":"CBL2, RNF55;CIN85;CNSA3 SH3D2C","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5725,"ComplexName":"Mdm2-P53 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P02340;P23804;P51480;Q9CXW4","subunits.Entrez.IDs.":"22059;17246;12578;67025","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007049;GO:0000902;GO:0016049;GO:0008219","GO.description":"cell cycle;cell morphogenesis;cell growth;cell death","FunCat.ID":"10.03;40.01;40.10","FunCat.description":"cell cycle;cell growth / morphogenesis;cell death","PubMed.ID":15989966,"subunits.Protein.name.":"Cellular tumor antigen p53 ;E3 ubiquitin-protein ligase Mdm2 ;Cyclin-dependent kinase inhibitor 2A ;60S ribosomal protein L11","subunits.Gene.name.":"Tp53;Mdm2;Cdkn2a;Rpl11","subunits.Gene.name.syn.":"P53 Trp53;;P16ink4a;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5727,"ComplexName":"TBP-TAF complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P20226;Q15572;Q15573;Q53T94","subunits.Entrez.IDs.":"6908;9013;9015;9014","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006351;GO:0003677","GO.description":"transcription, DNA-templated;DNA binding","FunCat.ID":"11;16.03.01","FunCat.description":"TRANSCRIPTION;DNA binding","PubMed.ID":7801123,"subunits.Protein.name.":"TATA-box-binding protein;TATA box-binding protein-associated factor RNA polymerase I subunit C ;TATA box-binding protein-associated factor RNA polymerase I subunit A ;TATA box-binding protein-associated factor RNA polymerase I subunit B","subunits.Gene.name.":"TBP;TAF1C;TAF1A;TAF1B","subunits.Gene.name.syn.":"GTF2D1 TF2D TFIID;;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5728,"ComplexName":"VEGFR2-STAT3 complex, VEGF induced","Organism":"Bovine","Synonyms":"None","Cell.line":"BREC cells","subunits.UniProt.IDs.":"P61635;Q28197","subunits.Entrez.IDs.":"508541;407170","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0045893;GO:0007169;GO:0001525","GO.description":"positive regulation of transcription, DNA-templated;transmembrane receptor protein tyrosine kinase signaling pathway;angiogenesis","FunCat.ID":"11.02.03.04.01;30.05.01.12;41.05.16","FunCat.description":"transcription activation;transmembrane receptor protein tyrosine kinase signalling pathways;angiogenesis","PubMed.ID":12824281,"subunits.Protein.name.":"Signal transducer and activator of transcription 3;Tyrosine kinase receptor","subunits.Gene.name.":"STAT3;flk-1","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"VEGF promotes STAT3-VEGFR2 complex formation in BREC cells, but not in BAEC cells.","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":5729,"ComplexName":"VEGF-VEGFR2 complex","Organism":"Bovine","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P15691;Q28197","subunits.Entrez.IDs.":"281572;407170","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0007169;GO:0001525","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway;angiogenesis","FunCat.ID":"30.05.01.12;41.05.16","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways;angiogenesis","PubMed.ID":12824281,"subunits.Protein.name.":"Vascular endothelial growth factor A ;Tyrosine kinase receptor","subunits.Gene.name.":"VEGFA;flk-1","subunits.Gene.name.syn.":"VEGF;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":5730,"ComplexName":"IKBKG homotrimer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q9Y6K9","subunits.Entrez.IDs.":"8517","Protein.complex.purification.method":"MI:0018- two hybrid; MI:0030- cross-linking studies","GO.ID":"GO:0030234;GO:0050790","GO.description":"enzyme regulator activity;regulation of catalytic activity","FunCat.ID":"18.02.01","FunCat.description":"enzymatic activity regulation / enzyme regulator","PubMed.ID":12435599,"subunits.Protein.name.":"NF-kappa-B essential modulator","subunits.Gene.name.":"IKBKG","subunits.Gene.name.syn.":"FIP3, NEMO","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":5731,"ComplexName":"NRP1-VEGFC complex, heparin dependent","Organism":"Human","Synonyms":"None","Cell.line":"HDMVEC cells","subunits.UniProt.IDs.":"O14786;P49767","subunits.Entrez.IDs.":"8829;7424","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006898;GO:0007169;GO:0001525;GO:0030133","GO.description":"receptor-mediated endocytosis;transmembrane receptor protein tyrosine kinase signaling pathway;angiogenesis;transport vesicle","FunCat.ID":"20.09.18.09.01.01;30.05.01.12;41.05.16;70.09","FunCat.description":"receptor-mediated endocytosis;transmembrane receptor protein tyrosine kinase signalling pathways;angiogenesis;intracellular transport vesicles","PubMed.ID":16816121,"subunits.Protein.name.":"Neuropilin-1;Vascular endothelial growth factor C","subunits.Gene.name.":"NRP1;VEGFC","subunits.Gene.name.syn.":"NRP VEGF165R;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5732,"ComplexName":"NRP2-VEGFC complex","Organism":"Human","Synonyms":"None","Cell.line":"HDMVEC cells","subunits.UniProt.IDs.":"O60462;P49767","subunits.Entrez.IDs.":"8828;7424","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0428- imaging techniques","GO.ID":"GO:0006898;GO:0007169;GO:0001525;GO:0030133","GO.description":"receptor-mediated endocytosis;transmembrane receptor protein tyrosine kinase signaling pathway;angiogenesis;transport vesicle","FunCat.ID":"20.09.18.09.01.01;30.05.01.12;41.05.16;70.09","FunCat.description":"receptor-mediated endocytosis;transmembrane receptor protein tyrosine kinase signalling pathways;angiogenesis;intracellular transport vesicles","PubMed.ID":16816121,"subunits.Protein.name.":"Neuropilin-2 ;Vascular endothelial growth factor C","subunits.Gene.name.":"NRP2;VEGFC","subunits.Gene.name.syn.":"VEGF165R2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"VEGFC colocalizes with NRP2 in endocytotic vesicles.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5733,"ComplexName":"NRP2-VEGFD complex, heparin dependent","Organism":"Human","Synonyms":"None","Cell.line":"HDMVEC cells","subunits.UniProt.IDs.":"O43915;O60462","subunits.Entrez.IDs.":"2277;8828","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies; MI:0428- imaging techniques","GO.ID":"GO:0006898;GO:0007169;GO:0001525;GO:0030133","GO.description":"receptor-mediated endocytosis;transmembrane receptor protein tyrosine kinase signaling pathway;angiogenesis;transport vesicle","FunCat.ID":"20.09.18.09.01.01;30.05.01.12;41.05.16;70.09","FunCat.description":"receptor-mediated endocytosis;transmembrane receptor protein tyrosine kinase signalling pathways;angiogenesis;intracellular transport vesicles","PubMed.ID":16816121,"subunits.Protein.name.":"Vascular endothelial growth factor D ;Neuropilin-2","subunits.Gene.name.":"VEGFD;NRP2","subunits.Gene.name.syn.":"FIGF;VEGF165R2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"VEGFD colocalizes with NRP2 in endocytotic vesicles.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5734,"ComplexName":"NRP1-VEGFD complex, heparin dependent","Organism":"Human","Synonyms":"None","Cell.line":"HDMVEC cells","subunits.UniProt.IDs.":"O14786;O43915","subunits.Entrez.IDs.":"8829;2277","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006898;GO:0007169;GO:0001525;GO:0030133","GO.description":"receptor-mediated endocytosis;transmembrane receptor protein tyrosine kinase signaling pathway;angiogenesis;transport vesicle","FunCat.ID":"20.09.18.09.01.01;30.05.01.12;41.05.16;70.09","FunCat.description":"receptor-mediated endocytosis;transmembrane receptor protein tyrosine kinase signalling pathways;angiogenesis;intracellular transport vesicles","PubMed.ID":16816121,"subunits.Protein.name.":"Neuropilin-1;Vascular endothelial growth factor D","subunits.Gene.name.":"NRP1;VEGFD","subunits.Gene.name.syn.":"NRP VEGF165R;FIGF","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5735,"ComplexName":"TGF-beta receptor-SMAD3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P36897;P37173;P84022","subunits.Entrez.IDs.":"7046;7048;4088","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007179;GO:0008083","GO.description":"transforming growth factor beta receptor signaling pathway;growth factor activity","FunCat.ID":"30.05.01.18.01;40.02.03.05","FunCat.description":"TGF-beta-receptor signalling pathway;growth factors","PubMed.ID":8774881,"subunits.Protein.name.":"TGF-beta receptor type-1;TGF-beta receptor type-2;Mothers against decapentaplegic homolog 3","subunits.Gene.name.":"TGFBR1;TGFBR2;SMAD3","subunits.Gene.name.syn.":"ALK5 SKR4;None;MADH3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5736,"ComplexName":"Pre-initiation complex (PIC)","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P20226;P24928;P60709","subunits.Entrez.IDs.":"6908;5430;60","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0047- far western blotting","GO.ID":"GO:0006352;GO:0003676","GO.description":"DNA-templated transcription, initiation;nucleic acid binding","FunCat.ID":"11.02.03.01.01;16.03","FunCat.description":"transcription initiation;nucleic acid binding","PubMed.ID":15502823,"subunits.Protein.name.":"TATA-box-binding protein;DNA-directed RNA polymerase II subunit RPB1;Actin, cytoplasmic 1","subunits.Gene.name.":"TBP;POLR2A;ACTB","subunits.Gene.name.syn.":"GTF2D1 TF2D TFIID;POLR2;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Actin is required for the initiation of transcription (for the formation of pre-initiation complexes).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5737,"ComplexName":"Multicomponent signaling complex, anti-CD40 stimulated (Birc2, Birc3, Cd40, Ikbkg, Map2k4, Map2k7, Map3k1, Traf2, Ube2n)","Organism":"Mouse","Synonyms":"None","Cell.line":"Splenic B cells","subunits.UniProt.IDs.":"O08863;O88522;P27512;P39429;P47809;P53349;P61089;Q62210;Q8CE90","subunits.Entrez.IDs.":"11796;16151;21939;22030;26398;26401;93765;11797;26400","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0000165;GO:0019724;GO:0030183","GO.description":"MAPK cascade;B cell mediated immunity;B cell differentiation","FunCat.ID":"30.01.05.01.03;36.25.16.03.01;43.03.07.02.01.01","FunCat.description":"MAPKKK cascade;humoral response (B-cells);B-cell","PubMed.ID":18635759,"subunits.Protein.name.":"Baculoviral IAP repeat-containing protein 3;NF-kappa-B essential modulator;Tumor necrosis factor receptor superfamily member 5;TNF receptor-associated factor 2;Dual specificity mitogen-activated protein kinase kinase 4;Mitogen-activated protein kinase kinase kinase 1;Ubiquitin-conjugating enzyme E2 N;Baculoviral IAP repeat-containing protein 2;Dual specificity mitogen-activated protein kinase kinase 7","subunits.Gene.name.":"Birc3;Ikbkg;Cd40;Traf2;Map2k4;Map3k1;Ube2n;Birc2;Map2k7","subunits.Gene.name.syn.":"None;Nemo;Tnfrsf5;None;Jnkk1 Mek4 Mkk4 Prkmk4 Sek1 Serk1 Skk1;Mekk Mekk1;Blu;None;Mkk7","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"With anti-CD40 as the immunoprecipitating antibody the complex included trace amounts of the MEKK1 substrates MKK4 and MKK7, furthermore it was shown that the amounts of most complex components declined between 10 and 30 min after stimulation. The results indicate that MAPK signaling, at least by CD40 and other TNFRs, follows a two-stage mechanism based on assembly of a multiprotein complex at the receptor that primes MAP3Ks for activation, but in which kinase activation is delayed until the complex is released to the cytoplasm.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5740,"ComplexName":"NRP2-VEGFR3 complex","Organism":"Human","Synonyms":"None","Cell.line":"HDMVEC cells","subunits.UniProt.IDs.":"O60462;P35916","subunits.Entrez.IDs.":"8828;2324","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0006898;GO:0007169;GO:0001525;GO:0030133","GO.description":"receptor-mediated endocytosis;transmembrane receptor protein tyrosine kinase signaling pathway;angiogenesis;transport vesicle","FunCat.ID":"20.09.18.09.01.01;30.05.01.12;41.05.16;70.09","FunCat.description":"receptor-mediated endocytosis;transmembrane receptor protein tyrosine kinase signalling pathways;angiogenesis;intracellular transport vesicles","PubMed.ID":16816121,"subunits.Protein.name.":"Neuropilin-2 ;Vascular endothelial growth factor receptor 3","subunits.Gene.name.":"NRP2;FLT4","subunits.Gene.name.syn.":"VEGF165R2;VEGFR3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5742,"ComplexName":"Multicomponent signaling complex, anti-CD40 stimulated,(Birc2, Birc3, Cd40, Ikbkg, Map3k1, Traf2, Ube2n)","Organism":"Mouse","Synonyms":"None","Cell.line":"Splenic B cells","subunits.UniProt.IDs.":"O08863;O88522;P27512;P39429;P53349;P61089;Q62210","subunits.Entrez.IDs.":"11796;16151;21939;22030;26401;93765;11797","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0000165;GO:0019724;GO:0030183","GO.description":"MAPK cascade;B cell mediated immunity;B cell differentiation","FunCat.ID":"30.01.05.01.03;36.25.16.03.01;43.03.07.02.01.01","FunCat.description":"MAPKKK cascade;humoral response (B-cells);B-cell","PubMed.ID":18635759,"subunits.Protein.name.":"Baculoviral IAP repeat-containing protein 3;NF-kappa-B essential modulator;Tumor necrosis factor receptor superfamily member 5;TNF receptor-associated factor 2;Mitogen-activated protein kinase kinase kinase 1;Ubiquitin-conjugating enzyme E2 N;Baculoviral IAP repeat-containing protein 2","subunits.Gene.name.":"Birc3;Ikbkg;Cd40;Traf2;Map3k1;Ube2n;Birc2","subunits.Gene.name.syn.":"None;Nemo;Tnfrsf5;None;Mekk Mekk1;Blu;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"With anti-MEKK1 as the immunoprecipitating antibody  it was shown that the apparent dissociation of the complex was not seen like in the anti-CD40 immunoprecipitated complexes,  where the amounts of most complex components declined between 10 and 30 min after stimulation. The results indicate that MAPK signaling, at least by CD40 and other TNFRs, follows a two-stage mechanism based on assembly of a multiprotein complex at the receptor that primes MAP3Ks for activation, but in which kinase activation is delayed until the complex is released to the cytoplasm.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5743,"ComplexName":"Membrane-associated multicomponent signaling complex, anti-CD40 stimulated (Cd40, Ikbkg, Map3k1, Traf2, Ube2n)","Organism":"Mouse","Synonyms":"None","Cell.line":"Splenic B cells","subunits.UniProt.IDs.":"O88522;P27512;P39429;P53349;P61089","subunits.Entrez.IDs.":"16151;21939;22030;26401;93765","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0000165;GO:0019724;GO:0030183;GO:0005886","GO.description":"MAPK cascade;B cell mediated immunity;B cell differentiation;plasma membrane","FunCat.ID":"30.01.05.01.03;36.25.16.03.01;43.03.07.02.01.01;70.02","FunCat.description":"MAPKKK cascade;humoral response (B-cells);B-cell;eukaryotic plasma membrane / membrane attached","PubMed.ID":18635759,"subunits.Protein.name.":"NF-kappa-B essential modulator;Tumor necrosis factor receptor superfamily member 5;TNF receptor-associated factor 2;Mitogen-activated protein kinase kinase kinase 1;Ubiquitin-conjugating enzyme E2 N","subunits.Gene.name.":"Ikbkg;Cd40;Traf2;Map3k1;Ube2n","subunits.Gene.name.syn.":"Nemo;Tnfrsf5;None;Mekk Mekk1;Blu","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The complex isolated with either CD40, IKK-gamma, or MEKK1-specific antibodies was present in the membrane-containing fraction at 10 min after stimulation but was barely detected after 30 min.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5744,"ComplexName":"Cytosolic multicomponent signaling complex, anti-CD40 stimulated, (Ikbkg, Map3k1, Traf2, Ube2n)","Organism":"Mouse","Synonyms":"None","Cell.line":"Splenic B cells","subunits.UniProt.IDs.":"O88522;P39429;P53349;P61089","subunits.Entrez.IDs.":"16151;22030;26401;93765","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0000165;GO:0019724;GO:0030183;GO:0005737","GO.description":"MAPK cascade;B cell mediated immunity;B cell differentiation;cytoplasm","FunCat.ID":"30.01.05.01.03;36.25.16.03.01;43.03.07.02.01.01;70.03","FunCat.description":"MAPKKK cascade;humoral response (B-cells);B-cell;cytoplasm","PubMed.ID":18635759,"subunits.Protein.name.":"NF-kappa-B essential modulator;TNF receptor-associated factor 2;Mitogen-activated protein kinase kinase kinase 1;Ubiquitin-conjugating enzyme E2 N","subunits.Gene.name.":"Ikbkg;Traf2;Map3k1;Ube2n","subunits.Gene.name.syn.":"Nemo;None;Mekk Mekk1;Blu","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex containing TRAF2, MEKK1, IKK-gamma, and Ubc13, but not CD40, was detected in the soluble cytosol fraction within 10 min, and most of its components were relatively stably associated for up to 60 min after CD40 engagement.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5745,"ComplexName":"PlexinA1-NRP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"O14786;Q9UIW2","subunits.Entrez.IDs.":"8829;5361","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0023052;GO:0010183;GO:0007399","GO.description":"signaling;pollen tube guidance;nervous system development","FunCat.ID":"30.01;40.01.03.03;47.03.01","FunCat.description":"cellular signalling;guidance of longitudinal cell extension (e.g. pollen tube guidance, axonal pathfinding);nervous system","PubMed.ID":10520994,"subunits.Protein.name.":"Neuropilin-1;Plexin-A1","subunits.Gene.name.":"NRP1;PLXNA1","subunits.Gene.name.syn.":"NRP VEGF165R;NOV PLXN1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5746,"ComplexName":"PlexinA1-NRP1-SEMA3A complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"O14786;Q14563;Q9UIW2","subunits.Entrez.IDs.":"8829;10371;5361","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0023052;GO:0010183;GO:0007399","GO.description":"signaling;pollen tube guidance;nervous system development","FunCat.ID":"30.01;40.01.03.03;47.03.01","FunCat.description":"cellular signalling;guidance of longitudinal cell extension (e.g. pollen tube guidance, axonal pathfinding);nervous system","PubMed.ID":10520994,"subunits.Protein.name.":"Neuropilin-1;Semaphorin-3A ;Plexin-A1","subunits.Gene.name.":"NRP1;SEMA3A;PLXNA1","subunits.Gene.name.syn.":"NRP VEGF165R;SEMAD;NOV PLXN1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Plexin A increases Neuropilin 1 affinity for SEMA3A.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5747,"ComplexName":"2AR-mGluR2 complex","Organism":"Human","Synonyms":"None","Cell.line":"brain cortex","subunits.UniProt.IDs.":"P08913;P42262","subunits.Entrez.IDs.":"150;2891","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0007186;GO:0097332","GO.description":"G-protein coupled receptor signaling pathway;response to antipsychotic drug","FunCat.ID":"30.05.02.24","FunCat.description":"G-protein coupled receptor signalling pathway","PubMed.ID":18297054,"subunits.Protein.name.":"Alpha-2A adrenergic receptor ;Glutamate receptor 2","subunits.Gene.name.":"ADRA2A;GRIA2","subunits.Gene.name.syn.":"ADRA2R ADRAR;GLUR2","Disease.comment":"2AR-mGluR2 complex is involved in psychosis.","Subunits.comment":"None","Complex.comment":"The results are consistent with the hypothesis that the 2AR-mGluR2 complex integrates serotonin and glutamate signaling to regulate the sensory gating functions of the cortex, a process that is disrupted in psychosis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5748,"ComplexName":"2AR-mGluR2 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"P08913;P42262","subunits.Entrez.IDs.":"150;2891","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation; MI:0012- bioluminescence resonance energy transfer; MI:0055- fluorescent resonance energy transfer","GO.ID":"GO:0007186","GO.description":"G-protein coupled receptor signaling pathway","FunCat.ID":"30.05.02.24","FunCat.description":"G-protein coupled receptor signalling pathway","PubMed.ID":18297054,"subunits.Protein.name.":"Alpha-2A adrenergic receptor ;Glutamate receptor 2","subunits.Gene.name.":"ADRA2A;GRIA2","subunits.Gene.name.syn.":"ADRA2R ADRAR;GLUR2","Disease.comment":"2AR-mGluR2 complex is involved in psychosis.","Subunits.comment":"None","Complex.comment":"The results are consistent with the hypothesis that the 2AR-mGluR2 complex integrates serotonin and glutamate signalling to regulate the sensory gating functions of the cortex, a process that is disrupted in psychosis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5749,"ComplexName":"MRIT complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15519;Q07817;Q14790","subunits.Entrez.IDs.":"8837;598;841","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0047- far western blotting; MI:0018- two hybrid","GO.ID":"GO:0006919","GO.description":"activation of cysteine-type endopeptidase activity involved in apoptotic process","FunCat.ID":"40.10.02.02.02","FunCat.description":"caspase activation","PubMed.ID":9326610,"subunits.Protein.name.":"CASP8 and FADD-like apoptosis regulator ;Bcl-2-like protein 1 ;Caspase-8","subunits.Gene.name.":"CFLAR;BCL2L1;CASP8","subunits.Gene.name.syn.":"CASH CASP8AP1 CLARP MRIT;BCL2L BCLX;MCH5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5755,"ComplexName":"SUMO1-SUA1-UBA2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P63165;Q9UBE0;Q9UBT2","subunits.Entrez.IDs.":"7341;10055;10054","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0016567;GO:0016579;GO:0000338;GO:0016925;GO:0016926;GO:0045116;GO:0019951","GO.description":"protein ubiquitination;protein deubiquitination;protein deneddylation;protein sumoylation;protein desumoylation;protein neddylation;Smt3-protein conjugation","FunCat.ID":"14.07.05;14.07.07","FunCat.description":"modification by ubiquitination, deubiquitination;modification by ubiquitin-related proteins","PubMed.ID":9920803,"subunits.Protein.name.":"Small ubiquitin-related modifier 1 ;SUMO-activating enzyme subunit 1 ;SUMO-activating enzyme subunit 2","subunits.Gene.name.":"SUMO1;SAE1;UBA2","subunits.Gene.name.syn.":"SMT3C SMT3H3 UBL1;AOS1 SUA1 UBLE1A;SAE2 UBLE1B","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Sua1p and hUba2p form a complex, and the complexed hUba2p binds SUMO-1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5756,"ComplexName":"SUA1-UBA2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q9UBE0;Q9UBT2","subunits.Entrez.IDs.":"10055;10054","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0050789","GO.description":"regulation of biological process","FunCat.ID":"18","FunCat.description":"REGULATION OF METABOLISM AND PROTEIN FUNCTION","PubMed.ID":9920803,"subunits.Protein.name.":"SUMO-activating enzyme subunit 1 ;SUMO-activating enzyme subunit 2","subunits.Gene.name.":"SAE1;UBA2","subunits.Gene.name.syn.":"AOS1 SUA1 UBLE1A;SAE2 UBLE1B","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5757,"ComplexName":"PLXNA1-RANBPM complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"Q96S59;Q9UIW2","subunits.Entrez.IDs.":"10048;5361","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0000301;GO:0023052;GO:0010183","GO.description":"retrograde transport, vesicle recycling within Golgi;signaling;pollen tube guidance","FunCat.ID":"20.09.07.07;30.01;40.01.03.03","FunCat.description":"retrograde transport;cellular signalling;guidance of longitudinal cell extension (e.g. pollen tube guidance, axonal pathfinding)","PubMed.ID":16672672,"subunits.Protein.name.":"Ran-binding protein 9 ;Plexin-A1","subunits.Gene.name.":"RANBP9;PLXNA1","subunits.Gene.name.syn.":"RANBPM;NOV PLXN1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"RanBPM has the potential to link Plexin-A receptors to retrograde transport and microtubule function in axonal guidance.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5758,"ComplexName":"PLXNA2-RANBPM complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"O75051;Q96S59","subunits.Entrez.IDs.":"5362;10048","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0000301;GO:0023052;GO:0010183","GO.description":"retrograde transport, vesicle recycling within Golgi;signaling;pollen tube guidance","FunCat.ID":"20.09.07.07;30.01;40.01.03.03","FunCat.description":"retrograde transport;cellular signalling;guidance of longitudinal cell extension (e.g. pollen tube guidance, axonal pathfinding)","PubMed.ID":16672672,"subunits.Protein.name.":"Plexin-A2 ;Ran-binding protein 9","subunits.Gene.name.":"PLXNA2;RANBP9","subunits.Gene.name.syn.":"KIAA0463 OCT PLXN2;RANBPM","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"RanBPM has the potential to link Plexin-A receptors to retrograde transport and microtubule function in axonal guidance.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5759,"ComplexName":"PLXNA3-RANBPM complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"P51805;Q96S59","subunits.Entrez.IDs.":"55558;10048","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0000301;GO:0023052;GO:0010183","GO.description":"retrograde transport, vesicle recycling within Golgi;signaling;pollen tube guidance","FunCat.ID":"20.09.07.07;30.01;40.01.03.03","FunCat.description":"retrograde transport;cellular signalling;guidance of longitudinal cell extension (e.g. pollen tube guidance, axonal pathfinding)","PubMed.ID":16672672,"subunits.Protein.name.":"Plexin-A3 ;Ran-binding protein 9","subunits.Gene.name.":"PLXNA3;RANBP9","subunits.Gene.name.syn.":"PLXN4 SEX;RANBPM","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"RanBPM has the potential to link Plexin-A receptors to retrograde transport and microtubule function in axonal guidance.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5760,"ComplexName":"PLXNA4-RANBPM complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"Q96S59;Q9HCM2","subunits.Entrez.IDs.":"10048;91584","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0000301;GO:0023052;GO:0010183","GO.description":"retrograde transport, vesicle recycling within Golgi;signaling;pollen tube guidance","FunCat.ID":"20.09.07.07;30.01;40.01.03.03","FunCat.description":"retrograde transport;cellular signalling;guidance of longitudinal cell extension (e.g. pollen tube guidance, axonal pathfinding)","PubMed.ID":16672672,"subunits.Protein.name.":"Ran-binding protein 9 ;Plexin-A4","subunits.Gene.name.":"RANBP9;PLXNA4","subunits.Gene.name.syn.":"RANBPM;KIAA1550 PLXNA4A PLXNA4B","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"RanBPM has the potential to link Plexin-A receptors to retrograde transport and microtubule function in axonal guidance.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5762,"ComplexName":"CRMP-MICAL-PlexinA1 complex, induced by SEMA3A","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"Q14194;Q8TDZ2;Q9UIW2","subunits.Entrez.IDs.":"1400;64780;5361","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0023052;GO:0010183;GO:0007399","GO.description":"signaling;pollen tube guidance;nervous system development","FunCat.ID":"30.01;40.01.03.03;47.03.01","FunCat.description":"cellular signalling;guidance of longitudinal cell extension (e.g. pollen tube guidance, axonal pathfinding);nervous system","PubMed.ID":18305261,"subunits.Protein.name.":"Dihydropyrimidinase-related protein 1 ;Protein-methionine sulfoxide oxidase MICAL1 ;Plexin-A1","subunits.Gene.name.":"CRMP1;MICAL1;PLXNA1","subunits.Gene.name.syn.":"DPYSL1 ULIP3;MICAL NICAL;NOV PLXN1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"MIDCAL1 forms a SEMA3A-modulated complex with CRMP and PlexA proteins.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5770,"ComplexName":"RUNX1-CBF-beta-DNA complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q01196;Q13951","subunits.Entrez.IDs.":"861;865","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:2001141;GO:0006355;GO:0003677","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;DNA binding","FunCat.ID":"11.02.03.04;16.03.01","FunCat.description":"transcriptional control;DNA binding","PubMed.ID":11276260,"subunits.Protein.name.":"Runt-related transcription factor 1 ;Core-binding factor subunit beta","subunits.Gene.name.":"RUNX1;CBFB","subunits.Gene.name.syn.":"AML1 CBFA2;","Disease.comment":"The complex is involved in acute leukemias.","Subunits.comment":"None","Complex.comment":"The heterodimeric complex between AML1 and CBF beta has an essential role in the ontogeny of definitive hematopoiesis and is the most frequent target for chromosomal rearrangements in human acute leukemias.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5772,"ComplexName":"ZO1-(beta)cadherin-(VE)cadherin-VEGFR2 complex","Organism":"Human","Synonyms":"None","Cell.line":"HUVEC cells","subunits.UniProt.IDs.":"P33151;P35222;P35968;Q07157","subunits.Entrez.IDs.":"1003;1499;3791;7082","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0007169;GO:0001525;GO:0007043;GO:0001568;GO:0001944","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway;angiogenesis;cell-cell junction assembly;blood vessel development;vasculature development","FunCat.ID":"30.05.01.12;41.05.16;42.06.04;47.03.03.02","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways;angiogenesis;intercellular junction (gap junction/adherens junction);vessels","PubMed.ID":18662404,"subunits.Protein.name.":"Cadherin-5;Catenin beta-1;Vascular endothelial growth factor receptor 2;Tight junction protein ZO-1","subunits.Gene.name.":"CDH5;CTNNB1;KDR;TJP1","subunits.Gene.name.syn.":"None;CTNNB;FLK1, VEGFR2;ZO1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5791,"ComplexName":"PlexinA1-PlexinB1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P70206;Q8CJH3","subunits.Entrez.IDs.":"18844;235611","Protein.complex.purification.method":"MI:0018- two hybrid; MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0007169;GO:0001525","GO.description":"transmembrane receptor protein tyrosine kinase signaling pathway;angiogenesis","FunCat.ID":"30.05.01.12;41.05.16","FunCat.description":"transmembrane receptor protein tyrosine kinase signalling pathways;angiogenesis","PubMed.ID":12559962,"subunits.Protein.name.":"Plexin-A1 ;Plexin-B1","subunits.Gene.name.":"Plxna1;Plxnb1","subunits.Gene.name.syn.":"Kiaa4053;Kiaa0407","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5798,"ComplexName":"Death induced signaling complex II (FADD, CASP8, CFLAR), cytosolic, CD95L induced","Organism":"Human","Synonyms":"None","Cell.line":"SKW 6.4 cells","subunits.UniProt.IDs.":"O15519;Q13158;Q14790","subunits.Entrez.IDs.":"8837;8772;841","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0097190","GO.description":"apoptotic signaling pathway","FunCat.ID":"40.10.02.03.01","FunCat.description":"induction of apoptosis by extracellular signals","PubMed.ID":18635548,"subunits.Protein.name.":"CASP8 and FADD-like apoptosis regulator ;FAS-associated death domain protein;Caspase-8","subunits.Gene.name.":"CFLAR;FADD;CASP8","subunits.Gene.name.syn.":"CASH CASP8AP1 CLARP MRIT;MORT1;MCH5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In contrast to the caspase activation at the CD95 DISC reported to occur within seconds after stimulation, caspase activation in the cytosol took place hours after stimulation. This complex was found in all investigated cell lines:  SKW6.4, BJAB, Raji, HUT78 and J16.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5799,"ComplexName":"Death induced signaling complex DISC (FAS, FADD, CASP8, CFLAR), membrane-associated, CD95L induced","Organism":"Human","Synonyms":"None","Cell.line":"SKW 6.4 cells","subunits.UniProt.IDs.":"O15519;P25445;Q13158;Q14790","subunits.Entrez.IDs.":"8837;355;8772;841","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0097190","GO.description":"apoptotic signaling pathway","FunCat.ID":"40.10.02.03.01","FunCat.description":"induction of apoptosis by extracellular signals","PubMed.ID":18635548,"subunits.Protein.name.":"CASP8 and FADD-like apoptosis regulator ;Tumor necrosis factor receptor superfamily member 6 ;FAS-associated death domain protein;Caspase-8","subunits.Gene.name.":"CFLAR;FAS;FADD;CASP8","subunits.Gene.name.syn.":"CASH CASP8AP1 CLARP MRIT;APT1 FAS1 TNFRSF6;MORT1;MCH5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The CD95 DISC is formed within seconds after CD95 stimulation, followed by caspase-8 activation at the DISC complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5800,"ComplexName":"Death-inducing signaling complex DISC (type I cells associated), stimulated","Organism":"Human","Synonyms":"None","Cell.line":"SKW 6.4 cells, H9 cells","subunits.UniProt.IDs.":"P25445;Q13158;Q14790","subunits.Entrez.IDs.":"355;8772;841","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006915;GO:0005886","GO.description":"apoptotic process;plasma membrane","FunCat.ID":"40.10.02;70.02","FunCat.description":"apoptosis (type I programmed cell death);eukaryotic plasma membrane / membrane attached","PubMed.ID":9501089,"subunits.Protein.name.":"Tumor necrosis factor receptor superfamily member 6 ;FAS-associated death domain protein;Caspase-8","subunits.Gene.name.":"FAS;FADD;CASP8","subunits.Gene.name.syn.":"APT1 FAS1 TNFRSF6;MORT1;MCH5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors compared the formation of the DISC between typeI (SKW6.5, H9) and type II  (JUrkat, CEM) cells. In type I cells, induction of apoptosis was accompanied by activation of large amounts of caspase-8 by the death-inducing signaling complex (DISC), whereas in type II cells DISC formation was strongly reduced and activation of caspase-8 and caspase-3 occurred following the loss of mitochondrial transmembrane potential.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5805,"ComplexName":"PGAM5-KEAP1-NRF2 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells, COS-1 cells","subunits.UniProt.IDs.":"Q14145;Q16236;Q96HS1","subunits.Entrez.IDs.":"9817;4780;192111","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:2001141;GO:0006355;GO:0000302;GO:0006979;GO:0005741","GO.description":"regulation of RNA biosynthetic process;regulation of transcription, DNA-templated;response to reactive oxygen species;response to oxidative stress;mitochondrial outer membrane","FunCat.ID":"11.02.03.04;32.01.01;70.16.01","FunCat.description":"transcriptional control;oxidative stress response;mitochondrial outer membrane","PubMed.ID":18387606,"subunits.Protein.name.":"Kelch-like ECH-associated protein 1 ;Nuclear factor erythroid 2-related factor 2 ;Serine/threonine-protein phosphatase PGAM5, mitochondrial","subunits.Gene.name.":"KEAP1;NFE2L2;PGAM5","subunits.Gene.name.syn.":"INRF2 KIAA0132 KLHL19;NRF2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors describe that PGAM5, by anchoring the Keap1-Nrf2 complex to outer membrane of mitochondria, may facilitate coordination between mitochondrial function and regulation of Nrf2-dependent anti-oxidant gene expression.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5806,"ComplexName":"Keap1-Nrf2-Cul3 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"liver","subunits.UniProt.IDs.":"Q60795;Q9JLV5;Q9Z2X8","subunits.Entrez.IDs.":"18024;26554;50868","Protein.complex.purification.method":"MI:0029-cosedimentation through density gradients","GO.ID":"GO:0043161;GO:0006511;GO:0000302;GO:0006979;GO:0005737","GO.description":"proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;response to reactive oxygen species;response to oxidative stress;cytoplasm","FunCat.ID":"14.13.01.01;32.01.01;70.03","FunCat.description":"proteasomal degradation (ubiquitin/proteasomal pathway);oxidative stress response;cytoplasm","PubMed.ID":17903176,"subunits.Protein.name.":"Nuclear factor erythroid 2-related factor 2;Cullin-3;Kelch-like ECH-associated protein 1","subunits.Gene.name.":"Nfe2l2;Cul3;Keap1","subunits.Gene.name.syn.":"Nrf-2 Nrf2;None;Inrf2 Kiaa0132","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors propose that Cul3 regulates the Nrf2 turnover through forming the Keap1-Nrf2-Cul3 complex.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5807,"ComplexName":"Keap1-Nrf2 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"Q60795;Q9Z2X8","subunits.Entrez.IDs.":"18024;50868","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0043161;GO:0006511;GO:0000302;GO:0006979;GO:0005737","GO.description":"proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;response to reactive oxygen species;response to oxidative stress;cytoplasm","FunCat.ID":"14.13.01.01;32.01.01;70.03","FunCat.description":"proteasomal degradation (ubiquitin/proteasomal pathway);oxidative stress response;cytoplasm","PubMed.ID":17903176,"subunits.Protein.name.":"Nuclear factor erythroid 2-related factor 2;Kelch-like ECH-associated protein 1","subunits.Gene.name.":"Nfe2l2;Keap1","subunits.Gene.name.syn.":"Nrf-2 Nrf2;Inrf2 Kiaa0132","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors described that the electrophilic stress does not disrupt the association of Keap1 and Nrf2, but rather it represses Keap1-mediated ubiquitination of Nrf2.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5808,"ComplexName":"DISC complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"HCT116 cells","subunits.UniProt.IDs.":"Q13158;Q14790;Q8IUB6","subunits.Entrez.IDs.":"8772;841;355","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0097190","GO.description":"apoptotic signaling pathway","FunCat.ID":"40.10.02.03.01","FunCat.description":"induction of apoptosis by extracellular signals","PubMed.ID":19347032,"subunits.Protein.name.":"FAS-associated death domain protein;Caspase-8;CD95 antigen","subunits.Gene.name.":"FADD;CASP8;CD95","subunits.Gene.name.syn.":"MORT1;MCH5;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex formation was induced by 5-FU.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5809,"ComplexName":"GABAA receptor","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P14867;P18507;P47870","subunits.Entrez.IDs.":"2554;2566;2561","Protein.complex.purification.method":"MI:0401- biochemical","GO.ID":"GO:0006821;GO:0005216","GO.description":"chloride transport;ion channel activity","FunCat.ID":"20.01.01.07.09;20.03.01.01","FunCat.description":"chloride transport;ion channels","PubMed.ID":11992121,"subunits.Protein.name.":"Gamma-aminobutyric acid receptor subunit alpha-1 ;Gamma-aminobutyric acid receptor subunit gamma-2 ;Gamma-aminobutyric acid receptor subunit beta-2","subunits.Gene.name.":"GABRA1;GABRG2;GABRB2","subunits.Gene.name.syn.":";;","Disease.comment":"Epilepsy, juvenile mioclonic.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5811,"ComplexName":"p53-BCL2 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04637;P10415","subunits.Entrez.IDs.":"7157;596","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006915;GO:0005739","GO.description":"apoptotic process;mitochondrion","FunCat.ID":"40.10.02;70.16","FunCat.description":"apoptosis (type I programmed cell death);mitochondrion","PubMed.ID":12667443,"subunits.Protein.name.":"Cellular tumor antigen p53;Apoptosis regulator Bcl-2","subunits.Gene.name.":"TP53;BCL2","subunits.Gene.name.syn.":"P53;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5812,"ComplexName":"p53-BCL2 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04637;Q07817","subunits.Entrez.IDs.":"7157;598","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006915;GO:0005739","GO.description":"apoptotic process;mitochondrion","FunCat.ID":"40.10.02;70.16","FunCat.description":"apoptosis (type I programmed cell death);mitochondrion","PubMed.ID":12667443,"subunits.Protein.name.":"Cellular tumor antigen p53;Bcl-2-like protein 1","subunits.Gene.name.":"TP53;BCL2L1","subunits.Gene.name.syn.":"P53;BCL2L BCLX","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5813,"ComplexName":"tBID-BAK1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O08734;P70444","subunits.Entrez.IDs.":"12018;12122","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006915;GO:0005739","GO.description":"apoptotic process;mitochondrion","FunCat.ID":"40.10.02;70.16","FunCat.description":"apoptosis (type I programmed cell death);mitochondrion","PubMed.ID":12667443,"subunits.Protein.name.":"Bcl-2 homologous antagonist/killer ;BH3-interacting domain death agonist","subunits.Gene.name.":"Bak1;Bid","subunits.Gene.name.syn.":"Bak;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5814,"ComplexName":"Tp53-BAK1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O08734;P02340","subunits.Entrez.IDs.":"12018;22059","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006915;GO:0005739","GO.description":"apoptotic process;mitochondrion","FunCat.ID":"40.10.02;70.16","FunCat.description":"apoptosis (type I programmed cell death);mitochondrion","PubMed.ID":12667443,"subunits.Protein.name.":"Bcl-2 homologous antagonist/killer ;Cellular tumor antigen p53","subunits.Gene.name.":"Bak1;Tp53","subunits.Gene.name.syn.":"Bak;P53 Trp53","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5815,"ComplexName":"Quaternary complex (Dvl, Gsk3b, Frat1, Axin1)","Organism":"Mouse","Synonyms":"None","Cell.line":"NIH 3T3 cells","subunits.UniProt.IDs.":"O35625;P51141;P70339;Q9WV60","subunits.Entrez.IDs.":"12005;13542;14296;56637","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0096- pull down","GO.ID":"GO:0016055","GO.description":"Wnt signaling pathway","FunCat.ID":"30.05.02.20","FunCat.description":"Wnt signalling pathway","PubMed.ID":10428961,"subunits.Protein.name.":"Axin-1 ;Segment polarity protein dishevelled homolog DVL-1;Proto-oncogene FRAT1 ;Glycogen synthase kinase-3 beta","subunits.Gene.name.":"Axin1;Dvl1;Frat1;Gsk3b","subunits.Gene.name.syn.":"Axin Fu;Dvl;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Dvl and GSK bind to different portions of Frat1.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5816,"ComplexName":"Apoptosome-procaspase 9 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O14727;P55211;P99999","subunits.Entrez.IDs.":"317;842;54205","Protein.complex.purification.method":"MI:0226- ion exchange chromatography","GO.ID":"GO:0006915;GO:0005737","GO.description":"apoptotic process;cytoplasm","FunCat.ID":"40.10.02;70.03","FunCat.description":"apoptosis (type I programmed cell death);cytoplasm","PubMed.ID":10692394,"subunits.Protein.name.":"Apoptotic protease-activating factor 1 ;Caspase-9 ;Cytochrome c","subunits.Gene.name.":"APAF1;CASP9;CYCS","subunits.Gene.name.syn.":"KIAA0413;MCH6;CYC","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5817,"ComplexName":"tBID-BCL2 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P10415;P55957","subunits.Entrez.IDs.":"596;637","Protein.complex.purification.method":"MI:0030- cross-linking studies; MI:0019- coimmunoprecipitation","GO.ID":"GO:0043067;GO:0005741","GO.description":"regulation of programmed cell death;mitochondrial outer membrane","FunCat.ID":"40.10.02.04;70.16.01","FunCat.description":"regulation of apoptosis;mitochondrial outer membrane","PubMed.ID":11583631,"subunits.Protein.name.":"Apoptosis regulator Bcl-2;BH3-interacting domain death agonist","subunits.Gene.name.":"BCL2;BID","subunits.Gene.name.syn.":"None;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5818,"ComplexName":"BIM-BCL2 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43521;P10415","subunits.Entrez.IDs.":"10018;596","Protein.complex.purification.method":"MI:0030- cross-linking studies; MI:0019- coimmunoprecipitation","GO.ID":"GO:0043067;GO:0005741","GO.description":"regulation of programmed cell death;mitochondrial outer membrane","FunCat.ID":"40.10.02.04;70.16.01","FunCat.description":"regulation of apoptosis;mitochondrial outer membrane","PubMed.ID":11583631,"subunits.Protein.name.":"Bcl-2-like protein 11 ;Apoptosis regulator Bcl-2","subunits.Gene.name.":"BCL2L11;BCL2","subunits.Gene.name.syn.":"BIM;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5819,"ComplexName":"BIM-BCL2xL complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43521;Q07817","subunits.Entrez.IDs.":"10018;598","Protein.complex.purification.method":"MI:0030- cross-linking studies; MI:0019- coimmunoprecipitation","GO.ID":"GO:0043067;GO:0005741","GO.description":"regulation of programmed cell death;mitochondrial outer membrane","FunCat.ID":"40.10.02.04;70.16.01","FunCat.description":"regulation of apoptosis;mitochondrial outer membrane","PubMed.ID":11583631,"subunits.Protein.name.":"Bcl-2-like protein 11 ;Bcl-2-like protein 1","subunits.Gene.name.":"BCL2L11;BCL2L1","subunits.Gene.name.syn.":"BIM;BCL2L BCLX","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5820,"ComplexName":"tBID-BCL2xL complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P55957;Q07817","subunits.Entrez.IDs.":"637;598","Protein.complex.purification.method":"MI:0030- cross-linking studies; MI:0019- coimmunoprecipitation","GO.ID":"GO:0043067;GO:0005741","GO.description":"regulation of programmed cell death;mitochondrial outer membrane","FunCat.ID":"40.10.02.04;70.16.01","FunCat.description":"regulation of apoptosis;mitochondrial outer membrane","PubMed.ID":11583631,"subunits.Protein.name.":"BH3-interacting domain death agonist ;Bcl-2-like protein 1","subunits.Gene.name.":"BID;BCL2L1","subunits.Gene.name.syn.":";BCL2L BCLX","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5821,"ComplexName":"BAD-BCL2xL complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q61337;Q64373","subunits.Entrez.IDs.":"12015;12048","Protein.complex.purification.method":"MI:0030- cross-linking studies","GO.ID":"GO:0043067;GO:0005741","GO.description":"regulation of programmed cell death;mitochondrial outer membrane","FunCat.ID":"40.10.02.04;70.16.01","FunCat.description":"regulation of apoptosis;mitochondrial outer membrane","PubMed.ID":12242151,"subunits.Protein.name.":"Bcl2-associated agonist of cell death ;Bcl-2-like protein 1","subunits.Gene.name.":"Bad;Bcl2l1","subunits.Gene.name.syn.":"Bbc6;Bcl2l Bclx","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5822,"ComplexName":"MCL1-NOXA complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q07820;Q13794","subunits.Entrez.IDs.":"4170;5366","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0043067;GO:0005741","GO.description":"regulation of programmed cell death;mitochondrial outer membrane","FunCat.ID":"40.10.02.04;70.16.01","FunCat.description":"regulation of apoptosis;mitochondrial outer membrane","PubMed.ID":16697956,"subunits.Protein.name.":"Induced myeloid leukemia cell differentiation protein Mcl-1 ;Phorbol-12-myristate-13-acetate-induced protein 1","subunits.Gene.name.":"MCL1;PMAIP1","subunits.Gene.name.syn.":"BCL2L3;NOXA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5823,"ComplexName":"MCL1-BAK1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q07820;Q16611","subunits.Entrez.IDs.":"4170;578","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0043067;GO:0005741","GO.description":"regulation of programmed cell death;mitochondrial outer membrane","FunCat.ID":"40.10.02.04;70.16.01","FunCat.description":"regulation of apoptosis;mitochondrial outer membrane","PubMed.ID":15077116,"subunits.Protein.name.":"Induced myeloid leukemia cell differentiation protein Mcl-1 ;Bcl-2 homologous antagonist/killer","subunits.Gene.name.":"MCL1;BAK1","subunits.Gene.name.syn.":"BCL2L3;BAK BCL2L7 CDN1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5827,"ComplexName":"IKBKG tetramer complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"Q9Y6K9","subunits.Entrez.IDs.":"8517","Protein.complex.purification.method":"MI:0030- cross-linking studies","GO.ID":"GO:0007249","GO.description":"I-kappaB kinase/NF-kappaB signaling","FunCat.ID":"30.01.05.01.04","FunCat.description":"NIK-I-kappaB/NF-kappaB cascade","PubMed.ID":12612076,"subunits.Protein.name.":"NF-kappa-B essential modulator","subunits.Gene.name.":"IKBKG","subunits.Gene.name.syn.":"FIP3, NEMO","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cross link agent EGS appears to cross-link preferentially the IKK-gamma subunits in the IKK-alpha-IKK-beta-IKK-gamma holocomplex.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":5828,"ComplexName":"IKBKG-IKBKB  complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O14920;Q9Y6K9","subunits.Entrez.IDs.":"3551;8517","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0007249","GO.description":"I-kappaB kinase/NF-kappaB signaling","FunCat.ID":"30.01.05.01.04","FunCat.description":"NIK-I-kappaB/NF-kappaB cascade","PubMed.ID":12612076,"subunits.Protein.name.":"Inhibitor of nuclear factor kappa-B kinase subunit beta;NF-kappa-B essential modulator","subunits.Gene.name.":"IKBKB;IKBKG","subunits.Gene.name.syn.":"IKKB;FIP3, NEMO","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The tetrameric oligomerization is not required for binding of IKK-gamma to IKK-alpha or IKK-beta.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5829,"ComplexName":"IKBKG-CHUK complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O15111;Q9Y6K9","subunits.Entrez.IDs.":"1147;8517","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0007249","GO.description":"I-kappaB kinase/NF-kappaB signaling","FunCat.ID":"30.01.05.01.04","FunCat.description":"NIK-I-kappaB/NF-kappaB cascade","PubMed.ID":12612076,"subunits.Protein.name.":"Inhibitor of nuclear factor kappa-B kinase subunit alpha;NF-kappa-B essential modulator","subunits.Gene.name.":"CHUK;IKBKG","subunits.Gene.name.syn.":"IKKA, TCF16;FIP3, NEMO","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The tetrameric oligomerization is not required for binding of IKK-gamma to IKK-alpha or IKK-beta.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5830,"ComplexName":"DJ-1-SNCA complex, high molecular weight complex","Organism":"Human","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P37840;Q99497","subunits.Entrez.IDs.":"6622;11315","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation;MI:0071-molecular sieving","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":15935068,"subunits.Protein.name.":"Alpha-synuclein ;Protein deglycase DJ-1","subunits.Gene.name.":"SNCA;PARK7","subunits.Gene.name.syn.":"NACP PARK1;DJ1, DJ-1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5832,"ComplexName":"PINK1-MIRO2-Milton complex","Organism":"Human","Synonyms":"None","Cell.line":"COS7","subunits.UniProt.IDs.":"Q8IXI1;Q9BXM7;Q9UPV9","subunits.Entrez.IDs.":"89941;65018;22906","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016192;GO:0005741","GO.description":"vesicle-mediated transport;mitochondrial outer membrane","FunCat.ID":"20.09.07;70.16.01","FunCat.description":"vesicular transport (Golgi network, etc.);mitochondrial outer membrane","PubMed.ID":19152501,"subunits.Protein.name.":"Mitochondrial Rho GTPase 2 ;Serine/threonine-protein kinase PINK1, mitochondrial ;Trafficking kinesin-binding protein 1","subunits.Gene.name.":"RHOT2;PINK1;TRAK1","subunits.Gene.name.syn.":"ARHT2 C16orf39;;KIAA1042 OIP106","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex is involved in anterograde axonal transport of mitochondria.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5836,"ComplexName":"MIRO2-Milton complex","Organism":"Human","Synonyms":"None","Cell.line":"COS7","subunits.UniProt.IDs.":"Q8IXI1;Q9UPV9","subunits.Entrez.IDs.":"89941;22906","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0016192;GO:0005741","GO.description":"vesicle-mediated transport;mitochondrial outer membrane","FunCat.ID":"20.09.07;70.16.01","FunCat.description":"vesicular transport (Golgi network, etc.);mitochondrial outer membrane","PubMed.ID":19152501,"subunits.Protein.name.":"Mitochondrial Rho GTPase 2 ;Trafficking kinesin-binding protein 1","subunits.Gene.name.":"RHOT2;TRAK1","subunits.Gene.name.syn.":"ARHT2 C16orf39;KIAA1042 OIP106","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex is involved in anterograde axonal transport of mitochondria.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5837,"ComplexName":"PPD complex","Organism":"Human","Synonyms":"Parkin-PINK1-DJ1 complex","Cell.line":"brain","subunits.UniProt.IDs.":"O60260;Q99497;Q9BXM7","subunits.Entrez.IDs.":"5071;11315;65018","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0071-molecular sieving","GO.ID":"GO:0043161;GO:0006511;GO:0005737","GO.description":"proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process;cytoplasm","FunCat.ID":"14.13.01.01;70.03","FunCat.description":"proteasomal degradation (ubiquitin/proteasomal pathway);cytoplasm","PubMed.ID":19229105,"subunits.Protein.name.":"E3 ubiquitin-protein ligase parkin;Protein deglycase DJ-1;Serine/threonine-protein kinase PINK1, mitochondrial","subunits.Gene.name.":"PARK2;PARK7;PINK1","subunits.Gene.name.syn.":"PRKN;DJ1, DJ-1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"PPD complex plays an important role in degradation of un- or misfolded Parkin substrates, like Parkin itself or Synphilin-1. Usually the PPD complex is found in the cytoplasm, but a small ammount was also detected in the mitochondrial fraction.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5838,"ComplexName":"Heterotrimeric complex (Rnd1, Rras, Plxnb1)","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P10833;Q8BLR7;Q8CJH3","subunits.Entrez.IDs.":"20130;223881;235611","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005096;GO:0043547;GO:0007166;GO:0007155","GO.description":"GTPase activator activity;positive regulation of GTPase activity;cell surface receptor signaling pathway;cell adhesion","FunCat.ID":"18.02.01.01.01;30.05;34.07","FunCat.description":"GTPase activator (GAP);transmembrane signal transduction;cell adhesion","PubMed.ID":15297673,"subunits.Protein.name.":"Ras-related protein R-Ras ;Rho-related GTP-binding protein Rho6 ;Plexin-B1","subunits.Gene.name.":"Rras;Rnd1;Plxnb1","subunits.Gene.name.syn.":";Rho6;Kiaa0407","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5843,"ComplexName":"AIF-CYPA-DNA complex","Organism":"Human","Synonyms":"None","Cell.line":"Jurkat cells","subunits.UniProt.IDs.":"O95831;P62937","subunits.Entrez.IDs.":"9131;5478","Protein.complex.purification.method":"MI:0096- pull down; MI:0019- coimmunoprecipitation","GO.ID":"GO:0006915;GO:0005634","GO.description":"apoptotic process;nucleus","FunCat.ID":"40.10.02;70.10","FunCat.description":"apoptosis (type I programmed cell death);nucleus","PubMed.ID":14716299,"subunits.Protein.name.":"Apoptosis-inducing factor 1, mitochondrial ;Peptidyl-prolyl cis-trans isomerase A","subunits.Gene.name.":"AIFM1;PPIA","subunits.Gene.name.syn.":"AIF PDCD8;CYPA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"After apoptotic stimulus, AIF translocates to the nucleus, interacts with DNA and tethers CypA to chromatin.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5844,"ComplexName":"I-kappa-B kinase complex","Organism":"Human","Synonyms":"IKK complex","Cell.line":"None","subunits.UniProt.IDs.":"O14920;O15111;Q9Y6K9","subunits.Entrez.IDs.":"3551;1147;8517","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":10893415,"subunits.Protein.name.":"Inhibitor of nuclear factor kappa-B kinase subunit beta;Inhibitor of nuclear factor kappa-B kinase subunit alpha;NF-kappa-B essential modulator","subunits.Gene.name.":"IKBKB;CHUK;IKBKG","subunits.Gene.name.syn.":"IKKB;IKKA, TCF16;FIP3, NEMO","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors conclude that while IKK gamma is a stoichiometric component of the IKK complex, obligatory for NF-kappa B signaling, IKAP is not associated with IKKs and plays no specific role in cytokine-induced NF-kappa B activation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5849,"ComplexName":"HSP90-CDC37-LRRK2 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"P08238;Q16543;Q5S007","subunits.Entrez.IDs.":"3326;11140;120892","Protein.complex.purification.method":"MI:0676- tandem affinity purification","GO.ID":"GO:0035556","GO.description":"intracellular signal transduction","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":16321986,"subunits.Protein.name.":"Heat shock protein HSP 90-beta;Hsp90 co-chaperone Cdc37;Leucine-rich repeat serine/threonine-protein kinase 2","subunits.Gene.name.":"HSP90AB1;CDC37;LRRK2","subunits.Gene.name.syn.":"HSP90B HSPC2 HSPCB;CDC37A;PARK8","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"HSP90 and CDC37 do not serve as substrate for LRRK2 kinase but associates as chaperones participating in maintenance of proper folding of the kinase.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5850,"ComplexName":"p65-p65 Nf(kappa)B complex, Il-1-beta induced","Organism":"Rat","Synonyms":"None","Cell.line":"INS-1E cells","subunits.UniProt.IDs.":"Q7TQN4","subunits.Entrez.IDs.":"309165","Protein.complex.purification.method":"MI:0412- electrophoretic mobility supershift assay","GO.ID":"GO:0045893;GO:0003677;GO:0007249","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;I-kappaB kinase/NF-kappaB signaling","FunCat.ID":"11.02.03.04.01;16.03.01;30.01.05.01.04","FunCat.description":"transcription activation;DNA binding;NIK-I-kappaB/NF-kappaB cascade","PubMed.ID":16556731,"subunits.Protein.name.":"Protein Rela","subunits.Gene.name.":"Rela","subunits.Gene.name.syn.":"RelA","Disease.comment":"In pancreatic beta cells the cytokine induced p65-p65 Nf(kappa)B complex is involved in Diabetes mellitus, type I.","Subunits.comment":"None","Complex.comment":"The results suggest that in INS-1E (beta cell line) cells the cytokines IL-1-beta or TNF-alpha induce a complex preferentially constituted by p65 homodimers, with a minor contribution by the p65/p50 heterodimer. The results further show that cytokine induced NF(kappa)B activation in insulin-producing cells is more intense and sustained than in fibroblasts.","SWISSPROT.organism":"Rattus norvegicus (Rat)"}
{"ComplexID":5851,"ComplexName":"p65-p50 Nf(kappa)B complex, Il-1-beta induced","Organism":"Rat","Synonyms":"None","Cell.line":"INS-1E cells","subunits.UniProt.IDs.":"Q63369;Q7TQN4","subunits.Entrez.IDs.":"81736;309165","Protein.complex.purification.method":"MI:0412- electrophoretic mobility supershift assay","GO.ID":"GO:0045893;GO:0003677;GO:0007249","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;I-kappaB kinase/NF-kappaB signaling","FunCat.ID":"11.02.03.04.01;16.03.01;30.01.05.01.04","FunCat.description":"transcription activation;DNA binding;NIK-I-kappaB/NF-kappaB cascade","PubMed.ID":16556731,"subunits.Protein.name.":"Nuclear factor NF-kappa-B p105 subunit ;Protein Rela","subunits.Gene.name.":"Nfkb1;Rela","subunits.Gene.name.syn.":";RelA","Disease.comment":"In pancreatic beta cells the cytokine induced p65-p50 Nf(kappa)B complex is involved in Diabetes mellitus, type I.","Subunits.comment":"None","Complex.comment":"The results suggest that in INS-1E (beta cell line) cells the cytokines IL-1-beta or TNF-alpha induce a complex preferentially constituted by p65 homodimers, with a minor contribution by the p65/p50 heterodimer. The results further show that cytokine induced NF(kappa)B activation in insulin-producing cells is more intense and sustained than in fibroblasts.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5852,"ComplexName":"p65-p50 Nf(kappa)B complex, Il-1-beta induced","Organism":"Rat","Synonyms":"None","Cell.line":"208F cells","subunits.UniProt.IDs.":"Q63369;Q7TQN4","subunits.Entrez.IDs.":"81736;309165","Protein.complex.purification.method":"MI:0412- electrophoretic mobility supershift assay","GO.ID":"GO:0045893;GO:0003677;GO:0007249","GO.description":"positive regulation of transcription, DNA-templated;DNA binding;I-kappaB kinase/NF-kappaB signaling","FunCat.ID":"11.02.03.04.01;16.03.01;30.01.05.01.04","FunCat.description":"transcription activation;DNA binding;NIK-I-kappaB/NF-kappaB cascade","PubMed.ID":16556731,"subunits.Protein.name.":"Nuclear factor NF-kappa-B p105 subunit ;Protein Rela","subunits.Gene.name.":"Nfkb1;Rela","subunits.Gene.name.syn.":";RelA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results suggest that 208F cells (fibroblast cell line) exposed to cytokine IL-1-beta have a different pattern of NF(kappa)B activation, with p65/p50 as the predominant NF-(kappa)B dimer. The results further show that cytokine induced NF(kappa)B activation in insulin-producing cells is more intense and sustained than in fibroblasts.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5856,"ComplexName":"AK2-FADD-caspase-10 (AFAC10) complex","Organism":"Human","Synonyms":"None","Cell.line":"Hela cells","subunits.UniProt.IDs.":"P54819;Q13158;Q92851","subunits.Entrez.IDs.":"204;8772;843","Protein.complex.purification.method":"MI:0096- pull down; MI:0071- molecular sieving","GO.ID":"GO:0097193","GO.description":"intrinsic apoptotic signaling pathway","FunCat.ID":"40.10.02.03.02","FunCat.description":"induction of apoptosis by intracellular signals","PubMed.ID":17952061,"subunits.Protein.name.":"Adenylate kinase 2, mitochondrial ;FAS-associated death domain protein;Caspase-10","subunits.Gene.name.":"AK2;FADD;CASP10","subunits.Gene.name.syn.":"ADK2;MORT1;MCH4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"AFAC10 complexes are detected in cells undergoing intrinsic cell death and AK2 promotes the association of caspase-10 with FADD. AK2 mediates a novel intrinsic apoptotic pathway that may be involved in tumorigenesis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5859,"ComplexName":"FAS-FADD-CASP8-CASP10 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P25445;Q13158;Q14790;Q92851","subunits.Entrez.IDs.":"355;8772;841;843","Protein.complex.purification.method":"MI:0055- fluorescent resonance energy transfer; MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006915","GO.description":"apoptotic process","FunCat.ID":"40.10.02","FunCat.description":"apoptosis (type I programmed cell death)","PubMed.ID":11717445,"subunits.Protein.name.":"Tumor necrosis factor receptor superfamily member 6 ;FAS-associated death domain protein;Caspase-8;Caspase-10","subunits.Gene.name.":"FAS;FADD;CASP8;CASP10","subunits.Gene.name.syn.":"APT1 FAS1 TNFRSF6;MORT1;MCH5;MCH4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Stimulation of Fas was induced by anti-Fas or by FasL. The FRET-results suggest that caspase-8 and -10 can be recruited likely within 50 \\u00c5, which would constitute the same Fas signaling complex. Caspase-10 is recruited into the Fas signaling complex and becomes activated like caspase-8 with slightly faster kinetics under these conditions. FRET signals showed pairs of of caspase-8 and -10 DEDs (death effector domains) with themselves and with each other, indicating a natural propensity of these domains to cause homotypic and heterotypic complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5860,"ComplexName":"FAS-FADD-CASP8 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P25445;Q13158;Q14790","subunits.Entrez.IDs.":"355;8772;841","Protein.complex.purification.method":"MI:0055- fluorescent resonance energy transfer","GO.ID":"GO:0006915","GO.description":"apoptotic process","FunCat.ID":"40.10.02","FunCat.description":"apoptosis (type I programmed cell death)","PubMed.ID":11717445,"subunits.Protein.name.":"Tumor necrosis factor receptor superfamily member 6 ;FAS-associated death domain protein;Caspase-8","subunits.Gene.name.":"FAS;FADD;CASP8","subunits.Gene.name.syn.":"APT1 FAS1 TNFRSF6;MORT1;MCH5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Stimulation of Fas was induced by anti-Fas or by FasL.  FRET signals showed pairs of of caspase-8 and -10 DEDs (death effector domains) with themselves and with each other, indicating a natural propensity of these domains to cause homotypic and heterotypic complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5861,"ComplexName":"FAS-FADD-CASP10 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P25445;Q13158;Q92851","subunits.Entrez.IDs.":"355;8772;843","Protein.complex.purification.method":"MI:0055- fluorescent resonance energy transfer","GO.ID":"GO:0006915","GO.description":"apoptotic process","FunCat.ID":"40.10.02","FunCat.description":"apoptosis (type I programmed cell death)","PubMed.ID":11717445,"subunits.Protein.name.":"Tumor necrosis factor receptor superfamily member 6 ;FAS-associated death domain protein;Caspase-10","subunits.Gene.name.":"FAS;FADD;CASP10","subunits.Gene.name.syn.":"APT1 FAS1 TNFRSF6;MORT1;MCH4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Stimulation of Fas was induced by anti-Fas or by FasL.  FRET signals showed pairs of of caspase-8 and -10 DEDs (death effector domains) with themselves and with each other, indicating a natural propensity of these domains to cause homotypic and heterotypic complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5862,"ComplexName":"CAV1-VDAC1-ESR1 complex","Organism":"Human","Synonyms":"None","Cell.line":"cortical and hippocampal areas","subunits.UniProt.IDs.":"P03372;P21796;Q03135","subunits.Entrez.IDs.":"2099;7416;857","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation;MI:0663-confocal microscopy","GO.ID":"GO:0005216;GO:0005886","GO.description":"ion channel activity;plasma membrane","FunCat.ID":"20.03.01.01;70.02","FunCat.description":"ion channels;eukaryotic plasma membrane / membrane attached","PubMed.ID":19595769,"subunits.Protein.name.":"Estrogen receptor;Voltage-dependent anion-selective channel protein 1;Caveolin-1","subunits.Gene.name.":"ESR1;VDAC1;CAV1","subunits.Gene.name.syn.":"ESR, NR3A1;VDAC;CAV","Disease.comment":"Disease: CAV1-VDAC1-ESR1 complex is involved in Alzheimer's disease.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5870,"ComplexName":"FE65-TSHZ3-HDAC1 complex","Organism":"Human","Synonyms":"None","Cell.line":"human H4 neuroglioma cells","subunits.UniProt.IDs.":"O00213;Q13547;Q63HK5","subunits.Entrez.IDs.":"322;3065;57616","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0045892;GO:0005634","GO.description":"negative regulation of transcription, DNA-templated;nucleus","FunCat.ID":"11.02.03.04.03;70.10","FunCat.description":"transcription repression;nucleus","PubMed.ID":19343227,"subunits.Protein.name.":"Amyloid beta A4 precursor protein-binding family B member 1 ;Histone deacetylase 1;Teashirt homolog 3","subunits.Gene.name.":"APBB1;HDAC1;TSHZ3","subunits.Gene.name.syn.":"FE65 RIR;RPD3L1;KIAA1474 TSH3 ZNF537","Disease.comment":"Disease: TSHZ3 is involved in Alzheimer disease.","Subunits.comment":"None","Complex.comment":"CASP4 appears to be one target for the repressor complex centering on FE65.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5871,"ComplexName":"Gamma-secretase complex (Aph1a, Psen1, Psenen, Ncstn)","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P49769;P57716;Q8BVF7;Q9CQR7","subunits.Entrez.IDs.":"19164;59287;226548;66340","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016485;GO:0023052;GO:0007219;GO:0005886","GO.description":"protein processing;signaling;Notch signaling pathway;plasma membrane","FunCat.ID":"14.07.11;30.01;30.05.02.14;70.02","FunCat.description":"protein processing (proteolytic);cellular signalling;Notch-receptor signalling pathway;eukaryotic plasma membrane / membrane attached","PubMed.ID":17911105,"subunits.Protein.name.":"Presenilin-1 ;Nicastrin;Gamma-secretase subunit APH-1A ;Gamma-secretase subunit PEN-2","subunits.Gene.name.":"Psen1;Ncstn;Aph1a;Psenen","subunits.Gene.name.syn.":"Ad3h Psnl1;;;Pen2","Disease.comment":"Gamma-secretase complex is involved in Alzheimer disease.","Subunits.comment":"None","Complex.comment":"The results demonstrated that having one of each of the four subunits is sufficient for gamma-secretase complexes to bind and cleave substrates.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5872,"ComplexName":"BRAF-MAP2K1-MAP2K2-YWHAE complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293","subunits.UniProt.IDs.":"P15056;P36507;P62258;Q02750","subunits.Entrez.IDs.":"673;5605;7531;5604","Protein.complex.purification.method":"MI:0676- tandem affinity purification","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":17979178,"subunits.Protein.name.":"Serine/threonine-protein kinase B-raf;Dual specificity mitogen-activated protein kinase kinase 2 ;14-3-3 protein epsilon ;Dual specificity mitogen-activated protein kinase kinase 1","subunits.Gene.name.":"BRAF;MAP2K2;YWHAE;MAP2K1","subunits.Gene.name.syn.":"BRAF1, RAFB1;MEK2 MKK2 PRKMK2;;MEK1, PRKMK1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5873,"ComplexName":"RAF1-MAP2K1-YWHAE complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293","subunits.UniProt.IDs.":"P04049;P62258;Q02750","subunits.Entrez.IDs.":"5894;7531;5604","Protein.complex.purification.method":"MI:0676- tandem affinity purification","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":17979178,"subunits.Protein.name.":"RAF proto-oncogene serine/threonine-protein kinase;14-3-3 protein epsilon ;Dual specificity mitogen-activated protein kinase kinase 1","subunits.Gene.name.":"RAF1;YWHAE;MAP2K1","subunits.Gene.name.syn.":"RAF;;MEK1, PRKMK1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5876,"ComplexName":"PPP2R1A-PPP2R1B-PPP2CA-PPME1-EIF4A1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HT-1080","subunits.UniProt.IDs.":"P30153;P30154;P60842;P67775;Q9Y570","subunits.Entrez.IDs.":"5518;5519;1973;5515;51400","Protein.complex.purification.method":"MI:0676- tandem affinity purification","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0006469;GO:0019210","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;negative regulation of protein kinase activity;kinase inhibitor activity","FunCat.ID":"14.07.03;18.02.01.02.05","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;kinase inhibitior","PubMed.ID":15761952,"subunits.Protein.name.":"Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform;Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform;Eukaryotic initiation factor 4A-I;Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform;Protein phosphatase methylesterase 1","subunits.Gene.name.":"PPP2R1A;PPP2R1B;EIF4A1;PPP2CA;PPME1","subunits.Gene.name.syn.":"None;None;DDX2A EIF4A;None;PME1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5877,"ComplexName":"MAP2K1-BRAF-RAF1-YWHAE-KSR1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"P04049;P15056;P62258;Q02750;Q8IVT5","subunits.Entrez.IDs.":"5894;673;7531;5604;8844","Protein.complex.purification.method":"MI:0676- tandem affinity purification","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":17979178,"subunits.Protein.name.":"RAF proto-oncogene serine/threonine-protein kinase;Serine/threonine-protein kinase B-raf;14-3-3 protein epsilon ;Dual specificity mitogen-activated protein kinase kinase 1;Kinase suppressor of Ras 1","subunits.Gene.name.":"RAF1;BRAF;YWHAE;MAP2K1;KSR1","subunits.Gene.name.syn.":"RAF;BRAF1, RAFB1;;MEK1, PRKMK1;KSR","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5879,"ComplexName":"Ksr1-PP2A holoenzyme complex (Ppp2r1a, Ppp2r2b, Ppp2ca), PDGF stimulated","Organism":"Mouse","Synonyms":"None","Cell.line":"NIH3T3 cells","subunits.UniProt.IDs.":"P63330;Q61097;Q6ZWR4;Q76MZ3","subunits.Entrez.IDs.":"19052;16706;72930;51792","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0000165;GO:0005886","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;MAPK cascade;plasma membrane","FunCat.ID":"14.07.03;30.01.05.01.03;70.02","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;MAPKKK cascade;eukaryotic plasma membrane / membrane attached","PubMed.ID":12932319,"subunits.Protein.name.":"Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform;Kinase suppressor of Ras 1;Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform ;Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform","subunits.Gene.name.":"Ppp2ca;Ksr1;Ppp2r2b;Ppp2r1a","subunits.Gene.name.syn.":"None;Ksr;;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors showed that the protein phosphatase PP2A is a component of the KSR1 scaffolding complex and demonstrated that PP2A activity is required for the stimulus-induced dephosphorylation of S392.  The binding of the regulatory B subunit (Ppp2r2b) was dramatically increased by PDGF treatment. The data indicate that the PP2A core enzyme is a constitutive component of the KSR1 complex, whereas the regulatory B subunit interaction is induced by Ras pathway activation.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5880,"ComplexName":"Ksr1-PP2A core enzyme complex (Ppp2r1a, Ppp2ca), untreated","Organism":"Mouse","Synonyms":"None","Cell.line":"NIH3T3 cells","subunits.UniProt.IDs.":"P63330;Q61097;Q76MZ3","subunits.Entrez.IDs.":"19052;16706;51792","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0000165","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;MAPK cascade","FunCat.ID":"14.07.03;30.01.05.01.03","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;MAPKKK cascade","PubMed.ID":12932319,"subunits.Protein.name.":"Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform;Kinase suppressor of Ras 1;Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform","subunits.Gene.name.":"Ppp2ca;Ksr1;Ppp2r1a","subunits.Gene.name.syn.":"None;Ksr;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The data indicate that the PP2A core enzyme is a constitutive component of the KSR1 complex, whereas the regulatory B (Ppp2r2b) subunit interaction is induced by Ras pathway activation.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5881,"ComplexName":"Ksr1-PP2A core enzyme complex (Ppp2r1a, Ppp2ca), untreated","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P63330;Q61097;Q76MZ3","subunits.Entrez.IDs.":"19052;16706;51792","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0000165;GO:0005737","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;MAPK cascade;cytoplasm","FunCat.ID":"14.07.03;30.01.05.01.03;70.03","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;MAPKKK cascade;cytoplasm","PubMed.ID":12932319,"subunits.Protein.name.":"Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform;Kinase suppressor of Ras 1;Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform","subunits.Gene.name.":"Ppp2ca;Ksr1;Ppp2r1a","subunits.Gene.name.syn.":"None;Ksr;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The A and C core subunits were readily detected in the KSR1 immunoprecipitates from brain lysates, but much lower levels of the B subunit were observed.The data indicate that the PP2A core enzyme is a constitutive component of the KSR1 complex, whereas the regulatory B (Ppp2r2b) subunit interaction is induced by Ras pathway activation.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5882,"ComplexName":"Raf1-PP2A holoenzyme complex (Ppp2r1a, Ppp2r2b, Ppp2ca), PDGF stimulated","Organism":"Mouse","Synonyms":"None","Cell.line":"NIH3T3 cells","subunits.UniProt.IDs.":"P63330;Q6ZWR4;Q76MZ3;Q99N57","subunits.Entrez.IDs.":"19052;72930;51792;110157","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0000165;GO:0005886","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;MAPK cascade;plasma membrane","FunCat.ID":"14.07.03;30.01.05.01.03;70.02","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;MAPKKK cascade;eukaryotic plasma membrane / membrane attached","PubMed.ID":12932319,"subunits.Protein.name.":"Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform;Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform ;Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform;RAF proto-oncogene serine/threonine-protein kinase","subunits.Gene.name.":"Ppp2ca;Ppp2r2b;Ppp2r1a;Raf1","subunits.Gene.name.syn.":"None;;None;Craf","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Studies indicate that PP2A contributes to Raf-1 activation by dephosphorylating S259 (PMID: 11782426) The examination of the PP2A/Raf-1 interaction by immunoblot analysis revealed that, like KSR1, the association of the dimeric core subunits (A and C) was constitutive, whereas binding of the regulatory B subunit was significantly induced by growth factor treatment.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5883,"ComplexName":"Raf1-PP2A core enzyme complex (Ppp2r1a, Ppp2ca), untreated","Organism":"Mouse","Synonyms":"None","Cell.line":"NIH3T3 cells","subunits.UniProt.IDs.":"P63330;Q76MZ3;Q99N57","subunits.Entrez.IDs.":"19052;51792;110157","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0000165;GO:0005737","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;MAPK cascade;cytoplasm","FunCat.ID":"14.07.03;30.01.05.01.03;70.03","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;MAPKKK cascade;cytoplasm","PubMed.ID":12932319,"subunits.Protein.name.":"Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform;Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform;RAF proto-oncogene serine/threonine-protein kinase","subunits.Gene.name.":"Ppp2ca;Ppp2r1a;Raf1","subunits.Gene.name.syn.":"None;None;Craf","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The examination of the PP2A/Raf-1 interaction by immunoblot analysis revealed that, like KSR1, the association of the dimeric core subunits (A and C) was constitutive, whereas binding of the regulatory B subunit was significantly induced by growth factor treatment.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5886,"ComplexName":"Ksr1 complex (Ksr1, Mek, 14-3-3), unstimulated","Organism":"Mouse","Synonyms":"None","Cell.line":"Cos cells","subunits.UniProt.IDs.":"P31938;P63101;Q61097","subunits.Entrez.IDs.":"26395;22631;16706","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0000165;GO:0005737","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;MAPK cascade;cytoplasm","FunCat.ID":"14.07.03;30.01.05.01.03;70.03","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;MAPKKK cascade;cytoplasm","PubMed.ID":11741534,"subunits.Protein.name.":"Dual specificity mitogen-activated protein kinase kinase 1;14-3-3 protein zeta/delta;Kinase suppressor of Ras 1","subunits.Gene.name.":"Map2k1;Ywhaz;Ksr1","subunits.Gene.name.syn.":"Mek1, Prkmk1;None;Ksr","Disease.comment":"None","Subunits.comment":"Since the authors did not specify Mek, we used isoform Mek1.","Complex.comment":"The amount of 14-3-3 bound to WT KSR1 did not change in response to EGF treatment, consistent with previous findings that the interaction with both Ser-297 and Ser-392 must be disrupted to reduce 14-3-3 dimer binding to KSR1.Even though MAPK was not observed in KSR1 immunoprecipitates from untreated cells, low levels of MAPK were detected in S392A and S297A/S392A mutant samples. The constitutive interaction between KSR1 and MEK is not affected by mutation of the serine sites.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5899,"ComplexName":"Lebercilin complex (Lca5, Ncl, Npm1, Ywhae, HSPA1A/B, Dctn1, Dctn2)","Organism":"Pig","Synonyms":"None","Cell.line":"eye","subunits.UniProt.IDs.":"O08788;P09405;P34930;P62259;Q61937;Q80ST9;Q99KJ8","subunits.Entrez.IDs.":"13191;17975;None;22627;18148;75782;69654","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0015630","GO.description":"microtubule cytoskeleton","FunCat.ID":"70.04.05","FunCat.description":"microtubule cytoskeleton","PubMed.ID":17546029,"subunits.Protein.name.":"Dynactin subunit 1;Nucleolin;Heat shock 70 kDa protein 1A;14-3-3 protein epsilon;Nucleophosmin;Lebercilin;Dynactin subunit 2","subunits.Gene.name.":"Dctn1;Ncl;HSPA1A;Ywhae;Npm1;Lca5;Dctn2","subunits.Gene.name.syn.":"None;Nuc;HSPA1;None;None;None;None","Disease.comment":"Lca5 is involved in Leber congenital amaurosis.","Subunits.comment":"Since Lca5, Ncl, Npm1, Ywhae, Dctn2 and Dctn1 from pig were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used. Since the authors did not specify HSP70, we used isoform HSPA1A.","Complex.comment":"The results showed that lebercilin is a ciliary and microtubule-associated protein.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Sus scrofa (Pig);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5909,"ComplexName":"Ksr1 complex (Ksr1, Mek, 14-3-3, Mapk), EGF stimulated","Organism":"Mouse","Synonyms":"None","Cell.line":"Cos cells","subunits.UniProt.IDs.":"P31938;P63085;P63101;Q61097","subunits.Entrez.IDs.":"26395;26413;22631;16706","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0000165;GO:0005886","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;MAPK cascade;plasma membrane","FunCat.ID":"14.07.03;30.01.05.01.03;70.02","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;MAPKKK cascade;eukaryotic plasma membrane / membrane attached","PubMed.ID":11741534,"subunits.Protein.name.":"Dual specificity mitogen-activated protein kinase kinase 1;Mitogen-activated protein kinase 1;14-3-3 protein zeta/delta;Kinase suppressor of Ras 1","subunits.Gene.name.":"Map2k1;Mapk1;Ywhaz;Ksr1","subunits.Gene.name.syn.":"Mek1, Prkmk1;Erk2, Mapk, Prkm1;None;Ksr","Disease.comment":"None","Subunits.comment":"Since the authors did not specify Mek, we used isoform Mek1..","Complex.comment":"The amount of 14-3-3 bound to WT KSR1 did not change in response to EGF treatment, consistent with previous findings that the interaction with both Ser-297 and Ser-392 must be disrupted to reduce 14-3-3 dimer binding to KSR1.Even though MAPK was not observed in KSR1 immunoprecipitates from untreated cells, low levels of MAPK were detected in S392A and S297A/S392A mutant samples. The constitutive interaction between KSR1 and MEK is not affected by mutation of the serine sites.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5910,"ComplexName":"Ksr1-CK2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"O54833;P67871;Q60737;Q61097","subunits.Entrez.IDs.":"13000;13001;12995;16706","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0000165;GO:0005886","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;MAPK cascade;plasma membrane","FunCat.ID":"14.07.03;30.01.05.01.03;70.02","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;MAPKKK cascade;eukaryotic plasma membrane / membrane attached","PubMed.ID":17174095,"subunits.Protein.name.":"Casein kinase II subunit alpha';Casein kinase II subunit beta;Casein kinase II subunit alpha;Kinase suppressor of Ras 1","subunits.Gene.name.":"Csnk2a2;Csnk2b;Csnk2a1;Ksr1","subunits.Gene.name.syn.":"None;Ck2n;Ckiia;Ksr","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors showed that binding of the CK2 subunits to Ksr1 was found to be constitutive and did not change with growth-factor treatment.The results identify CK2 as a novel component of the KSR1 scaffolding complex that facilitates ERK cascade signaling by functioning as a Raf family N-Region kinase.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5915,"ComplexName":"Ksr1-Brap (IMP) complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q61097;Q99MP8","subunits.Entrez.IDs.":"16706;72399","Protein.complex.purification.method":"MI:0006- anti bait coimmunoprecipitation","GO.ID":"GO:0000165","GO.description":"MAPK cascade","FunCat.ID":"30.01.05.01.03","FunCat.description":"MAPKKK cascade","PubMed.ID":14724641,"subunits.Protein.name.":"Kinase suppressor of Ras 1;BRCA1-associated protein","subunits.Gene.name.":"Ksr1;Brap","subunits.Gene.name.syn.":"Ksr;","Disease.comment":"None","Subunits.comment":"Since Ksr1 and Brap from rat were not available in the UniProt database at the time of annotation, the orthologous proteins from mouse were used.","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5918,"ComplexName":"KSR1 homooligomer complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"Q8IVT5","subunits.Entrez.IDs.":"8844","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0000165","GO.description":"MAPK cascade","FunCat.ID":"30.01.05.01.03","FunCat.description":"MAPKKK cascade","PubMed.ID":18332145,"subunits.Protein.name.":"Kinase suppressor of Ras 1","subunits.Gene.name.":"KSR1","subunits.Gene.name.syn.":"KSR","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors found that KSR1 homo-oligomerization is required to couple distinct KSR\\u00b7MEK and KSR\\u00b7B-Raf complexes to allow MEK activation. IMP (the Ras effector and ubiquitin-protein isopeptide ligase family member) association blocks KSR1 homo-oligomerization.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":5919,"ComplexName":"BRAF-RAF1-14-3-3 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"P04049;P15056;P63104","subunits.Entrez.IDs.":"5894;673;7534","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0000165","GO.description":"MAPK cascade","FunCat.ID":"30.01.05.01.03","FunCat.description":"MAPKKK cascade","PubMed.ID":18332145,"subunits.Protein.name.":"RAF proto-oncogene serine/threonine-protein kinase;Serine/threonine-protein kinase B-raf;14-3-3 protein zeta/delta","subunits.Gene.name.":"RAF1;BRAF;YWHAZ","subunits.Gene.name.syn.":"RAF;BRAF1, RAFB1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Expression of IMP (Ras effector and ubiquitin-protein isopeptide ligase family member)  blocked BRAF-RAF1 complex formation.Although 14-3-3 association has been implicated as a prerequisite for B-Raf\\u00b7c-Raf complex formation, IMP impaired Raf hetero-oligomerization without affecting the relative amounts of 14-3-3 coprecipitating with B-Raf.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5920,"ComplexName":"KSR1-RAF1-MEK complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"P04049;Q02750;Q8IVT5","subunits.Entrez.IDs.":"5894;5604;8844","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0000165","GO.description":"MAPK cascade","FunCat.ID":"30.01.05.01.03","FunCat.description":"MAPKKK cascade","PubMed.ID":18332145,"subunits.Protein.name.":"RAF proto-oncogene serine/threonine-protein kinase;Dual specificity mitogen-activated protein kinase kinase 1;Kinase suppressor of Ras 1","subunits.Gene.name.":"RAF1;MAP2K1;KSR1","subunits.Gene.name.syn.":"RAF;MEK1, PRKMK1;KSR","Disease.comment":"None","Subunits.comment":"Since the authors did not specify Mek, we used isoform Mek1.","Complex.comment":"IMP (Ras effector and ubiquitin-protein isopeptide ligase family member)  significantly inhibited the association of c-Raf with KSR1. This is in stark contrast to the insensitivity of KSR1\\u00b7B-Raf complexes to IMP expression.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5921,"ComplexName":"KSR1-BRAF-MEK complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"P15056;Q02750;Q8IVT5","subunits.Entrez.IDs.":"673;5604;8844","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0000165","GO.description":"MAPK cascade","FunCat.ID":"30.01.05.01.03","FunCat.description":"MAPKKK cascade","PubMed.ID":18332145,"subunits.Protein.name.":"Serine/threonine-protein kinase B-raf;Dual specificity mitogen-activated protein kinase kinase 1;Kinase suppressor of Ras 1","subunits.Gene.name.":"BRAF;MAP2K1;KSR1","subunits.Gene.name.syn.":"BRAF1, RAFB1;MEK1, PRKMK1;KSR","Disease.comment":"None","Subunits.comment":"Since the authors did not specify Mek, we used isoform Mek1.","Complex.comment":"IMP (Ras effector and ubiquitin-protein isopeptide ligase family member)  significantly inhibited the association of c-Raf with KSR1. This is in stark contrast to the insensitivity of KSR1\\u00b7B-Raf complexes to IMP expression.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5922,"ComplexName":"RAF1-RAS complex, EGF induced","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P01112;P04049","subunits.Entrez.IDs.":"3265;5894","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0023052;GO:0005886","GO.description":"signaling;plasma membrane","FunCat.ID":"30.01;70.02","FunCat.description":"cellular signalling;eukaryotic plasma membrane / membrane attached","PubMed.ID":16364920,"subunits.Protein.name.":"GTPase HRas;RAF proto-oncogene serine/threonine-protein kinase","subunits.Gene.name.":"HRAS;RAF1","subunits.Gene.name.syn.":"HRAS1;RAF","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors showed that whereas EGF induces complex formation between RAS and C-RAF, and (G12V)RAS binds directly to C-RAF, a RAS:C-RAF complex is not induced by the impaired activity mutants of B-RAF or by (V600E)B-RAF.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5923,"ComplexName":"RAF1-BRAF complex, RAS stimulated","Organism":"Human","Synonyms":"None","Cell.line":"Cos cells","subunits.UniProt.IDs.":"P04049;P15056","subunits.Entrez.IDs.":"5894;673","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":16364920,"subunits.Protein.name.":"RAF proto-oncogene serine/threonine-protein kinase;Serine/threonine-protein kinase B-raf","subunits.Gene.name.":"RAF1;BRAF","subunits.Gene.name.syn.":"RAF;BRAF1, RAFB1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors found that C-RAF binds to B-RAF only under activating conditions, whereas mutant B-RAF binds to C-RAF constitutively. Additionally they showed that wild-type B-RAF can also activate C-RAF, but that C-RAF does not activate B-RAF.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5924,"ComplexName":"RAF1-CNK1 complex, RAS stimulated","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"P04049;Q969H4","subunits.Entrez.IDs.":"5894;10256","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":15845549,"subunits.Protein.name.":"RAF proto-oncogene serine/threonine-protein kinase;Connector enhancer of kinase suppressor of ras 1","subunits.Gene.name.":"RAF1;CNKSR1","subunits.Gene.name.syn.":"RAF;CNK1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors described that the interaction between the wild-type proteins of Raf and CNK was detectable but weak. Further they showed that coexpression of activated RasV12 enhanced the association between the two proteins, indicating that Raf-1 preactivated by RasV12 undergoes a conformational change that improves its binding to CNK1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5925,"ComplexName":"BRAF-CNK1 complex, not RAS stimulated","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"P15056;Q969H4","subunits.Entrez.IDs.":"673;10256","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":15845549,"subunits.Protein.name.":"Serine/threonine-protein kinase B-raf;Connector enhancer of kinase suppressor of ras 1","subunits.Gene.name.":"BRAF;CNKSR1","subunits.Gene.name.syn.":"BRAF1, RAFB1;CNK1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors showed that in contrast to Raf-1, B-Raf bound to CNK1 without the coexpression of activated Ras.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5926,"ComplexName":"CNK1 homodimer complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"Q969H4","subunits.Entrez.IDs.":"10256","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":15845549,"subunits.Protein.name.":"Connector enhancer of kinase suppressor of ras 1","subunits.Gene.name.":"CNKSR1","subunits.Gene.name.syn.":"CNK1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors showed that coexpression of activators of the MAP kinase pathway such as RasV12 or the constitutively active MEK mutant MEK-Glu-217/Glu-221  strongly induced dimerization of the CNK proteins.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":5928,"ComplexName":"CNK1-SRC-RAF1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"P04049;P12931;Q969H4","subunits.Entrez.IDs.":"5894;6714;10256","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":15845549,"subunits.Protein.name.":"RAF proto-oncogene serine/threonine-protein kinase;Proto-oncogene tyrosine-protein kinase Src;Connector enhancer of kinase suppressor of ras 1","subunits.Gene.name.":"RAF1;SRC;CNKSR1","subunits.Gene.name.syn.":"RAF;SRC1;CNK1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results indicated that CNK1 regulates the Src-dependent activation of Raf-1 only under optimized conditions. Too low or too high amounts of CNK1 prevented the formation of the trimeric complex and promoted dimerization between CNK1 and Src or Raf-1, thereby preventing activation of Raf-1 by Src. The authors describe that CNK1 acts as a scaffold protein that assembles and coordinates two kinases of a single signaling pathway.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5936,"ComplexName":"Ksr1-CK2-MEK-14-3-3 complex, PDGF treated","Organism":"Mouse","Synonyms":"None","Cell.line":"NIH3T3 cells, brain","subunits.UniProt.IDs.":"O54833;P31938;P63101;P67871;Q60737;Q61097","subunits.Entrez.IDs.":"13000;26395;22631;13001;12995;16706","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0000165;GO:0005886","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;MAPK cascade;plasma membrane","FunCat.ID":"14.07.03;30.01.05.01.03;70.02","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;MAPKKK cascade;eukaryotic plasma membrane / membrane attached","PubMed.ID":17174095,"subunits.Protein.name.":"Casein kinase II subunit alpha';Dual specificity mitogen-activated protein kinase kinase 1;14-3-3 protein zeta/delta;Casein kinase II subunit beta;Casein kinase II subunit alpha;Kinase suppressor of Ras 1","subunits.Gene.name.":"Csnk2a2;Map2k1;Ywhaz;Csnk2b;Csnk2a1;Ksr1","subunits.Gene.name.syn.":"None;Mek1, Prkmk1;None;Ck2n;Ckiia;Ksr","Disease.comment":"None","Subunits.comment":"Since the authors did not specify Mek, we used Mek1.","Complex.comment":"The authors showed that mutation of lysine 360 and arginine 363 to either alanine residues (KR/AA) or to glutamine and glycine residues KR/QG (as found in the C-Raf C1 domain) abolished CK2 binding but had no effect on the association of MEK and 14-3-3, proteins that bind to sites outside the C1 domain.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5937,"ComplexName":"B-Ksr1-MEK-MAPK-14-3-3 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"adult forebrain neurons","subunits.UniProt.IDs.":"P31938;P63085;P63101;Q61097","subunits.Entrez.IDs.":"26395;26413;22631;16706","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0000165;GO:0022008;GO:0048699","GO.description":"MAPK cascade;neurogenesis;generation of neurons","FunCat.ID":"30.01.05.01.03;41.05.13","FunCat.description":"MAPKKK cascade;neurogenesis","PubMed.ID":10891492,"subunits.Protein.name.":"Dual specificity mitogen-activated protein kinase kinase 1;Mitogen-activated protein kinase 1;14-3-3 protein zeta/delta;Kinase suppressor of Ras 1","subunits.Gene.name.":"Map2k1;Mapk1;Ywhaz;Ksr1","subunits.Gene.name.syn.":"Mek1, Prkmk1;Erk2, Mapk, Prkm1;None;Ksr","Disease.comment":"None","Subunits.comment":"B-Ksr1, (corresponding to isoform 2 in Swiss-Prot: Q61097) is a splice variant that is highly expressed in brain-derived tissues. Since the authors did not specify Mek, we used isoform Mek1.","Complex.comment":"Experiments done in RASV12 activated 293 cells and in lysates of mouse brain.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5946,"ComplexName":"Ksr1-Mek-Braf complex, EGF induced","Organism":"Mouse","Synonyms":"None","Cell.line":"MEF cells","subunits.UniProt.IDs.":"P28028;P31938;Q61097","subunits.Entrez.IDs.":"109880;26395;16706","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0000165","GO.description":"MAPK cascade","FunCat.ID":"30.01.05.01.03","FunCat.description":"MAPKKK cascade","PubMed.ID":19541618,"subunits.Protein.name.":"Serine/threonine-protein kinase B-raf;Dual specificity mitogen-activated protein kinase kinase 1;Kinase suppressor of Ras 1","subunits.Gene.name.":"Braf;Map2k1;Ksr1","subunits.Gene.name.syn.":"B-raf;Mek1, Prkmk1;Ksr","Disease.comment":"None","Subunits.comment":"Since the authors did not specify Mek, we used isoform Mek1.","Complex.comment":"The authors conclude that ternary interactions between KSR1, MEK, and B-Raf facilitate signal transmission from B-Raf to MEK.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5947,"ComplexName":"Ksr1-Mek-Braf-Erk complex, EGF induced","Organism":"Mouse","Synonyms":"None","Cell.line":"MEF cells","subunits.UniProt.IDs.":"P28028;P31938;Q61097;Q63844","subunits.Entrez.IDs.":"109880;26395;16706;26417","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0000165","GO.description":"MAPK cascade","FunCat.ID":"30.01.05.01.03","FunCat.description":"MAPKKK cascade","PubMed.ID":19541618,"subunits.Protein.name.":"Serine/threonine-protein kinase B-raf;Dual specificity mitogen-activated protein kinase kinase 1;Kinase suppressor of Ras 1;Mitogen-activated protein kinase 3","subunits.Gene.name.":"Braf;Map2k1;Ksr1;Mapk3","subunits.Gene.name.syn.":"B-raf;Mek1, Prkmk1;Ksr;Erk1, Prkm3","Disease.comment":"None","Subunits.comment":"Since the authors did not specify Mek as well as Erk, we used isoform Mek1 and isoform ERK1, respectively","Complex.comment":"The authors found that the docking of activated ERK to the KSR1 complex accelerates the phosphorylation of these sites in response to growth factor treatment. As a functional consequence, phosphorylation of B-Raf and KSR1 on the S/TP sites disrupts the B-Raf/KSR1 interaction and promotes the release of KSR1 from the plasma membrane. Thus, the docking of activated ERK downregulates KSR1's scaffold activity and its ability to potentiate signal transmission from B-Raf to MEK.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5948,"ComplexName":"p18-p14-Mp1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O88653;Q9CQ22;Q9JHS3","subunits.Entrez.IDs.":"56692;66508;83409","Protein.complex.purification.method":"MI:0676- tandem affinity purification","GO.ID":"GO:0007034;GO:0000165;GO:0007032;GO:0005768","GO.description":"vacuolar transport;MAPK cascade;endosome organization;endosome","FunCat.ID":"20.09.13;30.01.05.01.03;42.22;70.22","FunCat.description":"vacuolar/lysosomal transport;MAPKKK cascade;endosome;endosome","PubMed.ID":19177150,"subunits.Protein.name.":"Ragulator complex protein LAMTOR3;Ragulator complex protein LAMTOR1 ;Ragulator complex protein LAMTOR2","subunits.Gene.name.":"Lamtor3;Lamtor1;Lamtor2","subunits.Gene.name.syn.":"Map2k1ip1, Mapbp, Mapksp1;;Mapbpip, Robld3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Experiments were done in mouse embryonic fibroblasts (MEFs). The authors showed that p18 specifically binds to the p14-MP1 complex, a scaffold for MEK1. Further results indicated that p18 serves as a functional component of the MEK-ERK pathway by anchoring the p14-MP1-MEK complex to late endosomes.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5951,"ComplexName":"Mp1-p14 scaffolding complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q9JHS3;Q9UHA4","subunits.Entrez.IDs.":"83409;8649","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0000165;GO:0005768","GO.description":"MAPK cascade;endosome","FunCat.ID":"30.01.05.01.03;70.22","FunCat.description":"MAPKKK cascade;endosome","PubMed.ID":15016825,"subunits.Protein.name.":"Ragulator complex protein LAMTOR2;Ragulator complex protein LAMTOR3","subunits.Gene.name.":"Lamtor2;LAMTOR3","subunits.Gene.name.syn.":"Mapbpip, Robld3;MAP2K1IP1 MAPKSP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors describe that an intact and correctly localized MP1-p14 complex is required for MAPK signaling.","SWISSPROT.organism":"Mus musculus (Mouse);Homo sapiens (Human)"}
{"ComplexID":5952,"ComplexName":"Mp1-p14 scaffolding complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O88653;Q9JHS3","subunits.Entrez.IDs.":"56692;83409","Protein.complex.purification.method":"MI:0114- x-ray crystallography; MI:0004- affinity chromatography technologies; MI:0071- molecular sieving","GO.ID":"GO:0000165;GO:0005768","GO.description":"MAPK cascade;endosome","FunCat.ID":"30.01.05.01.03;70.22","FunCat.description":"MAPKKK cascade;endosome","PubMed.ID":15263099,"subunits.Protein.name.":"Ragulator complex protein LAMTOR3;Ragulator complex protein LAMTOR2","subunits.Gene.name.":"Lamtor3;Lamtor2","subunits.Gene.name.syn.":"Map2k1ip1, Mapbp, Mapksp1;Mapbpip, Robld3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors describe that p14/MP1 acts as a MAPK-scaffolding complex anchored to late endosomes.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5960,"ComplexName":"p65-p50 Nf(kappa)B complex, Il-1-beta induced","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P25799;Q04207","subunits.Entrez.IDs.":"18033;19697","Protein.complex.purification.method":"MI:0412- electrophoretic mobility supershift assay","GO.ID":"GO:0007249","GO.description":"I-kappaB kinase/NF-kappaB signaling","FunCat.ID":"30.01.05.01.04","FunCat.description":"NIK-I-kappaB/NF-kappaB cascade","PubMed.ID":16551748,"subunits.Protein.name.":"Nuclear factor NF-kappa-B p105 subunit ;Transcription factor p65","subunits.Gene.name.":"Nfkb1;Rela","subunits.Gene.name.syn.":";Nfkb3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":5963,"ComplexName":"ALB-TGFbetaRII complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P02770;P38438","subunits.Entrez.IDs.":"24186;81810","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007179","GO.description":"transforming growth factor beta receptor signaling pathway","FunCat.ID":"30.05.01.18.01","FunCat.description":"TGF-beta-receptor signalling pathway","PubMed.ID":19605630,"subunits.Protein.name.":"Serum albumin;TGF-beta receptor type-2","subunits.Gene.name.":"Alb;Tgfbr2","subunits.Gene.name.syn.":";","Disease.comment":"OMIM:600669 Epilepsy, idopathic generalized, susceptibility to","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":5975,"ComplexName":"Gamma-secretase complex (APH1A, PSENEN, PSEN1, NCSTN, TMP21)","Organism":"Human","Synonyms":"None","Cell.line":"HEK-293 cells; SHSY-5Y cells","subunits.UniProt.IDs.":"P49755;P49768;Q92542;Q96BI3;Q9NZ42","subunits.Entrez.IDs.":"10972;5663;23385;51107;55851","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0016485;GO:0051090;GO:0023052;GO:0007219;GO:0005886;GO:0005794","GO.description":"protein processing;regulation of sequence-specific DNA binding transcription factor activity;signaling;Notch signaling pathway;plasma membrane;Golgi apparatus","FunCat.ID":"14.07.11;18.02.09;30.01;30.05.02.14;70.02;70.08","FunCat.description":"protein processing (proteolytic);regulator of transcription factor;cellular signalling;Notch-receptor signalling pathway;eukaryotic plasma membrane / membrane attached;Golgi","PubMed.ID":16641999,"subunits.Protein.name.":"Transmembrane emp24 domain-containing protein 10;Presenilin-1;Nicastrin;Gamma-secretase subunit APH-1A;Gamma-secretase subunit PEN-2","subunits.Gene.name.":"TMED10;PSEN1;NCSTN;APH1A;PSENEN","subunits.Gene.name.syn.":"TMP21;AD3 PS1 PSNL1;KIAA0253;PSF;PEN2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5980,"ComplexName":"LRRK2-CHIP-HSP90 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P08238;Q5S007;Q9UNE7","subunits.Entrez.IDs.":"3326;120892;10273","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0043161;GO:0006511","GO.description":"proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process","FunCat.ID":"14.13.01.01","FunCat.description":"proteasomal degradation (ubiquitin/proteasomal pathway)","PubMed.ID":19196961,"subunits.Protein.name.":"Heat shock protein HSP 90-beta;Leucine-rich repeat serine/threonine-protein kinase 2 ;E3 ubiquitin-protein ligase CHIP","subunits.Gene.name.":"HSP90AB1;LRRK2;STUB1","subunits.Gene.name.syn.":"HSP90B HSPC2 HSPCB;PARK8;CHIP","Disease.comment":"LRRK2 is involved in Parkinson disease.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":5991,"ComplexName":"LRRK2-FADD-CASP8","Organism":"Human","Synonyms":"None","Cell.line":"HEK-293 cell","subunits.UniProt.IDs.":"Q13158;Q14790;Q5S007","subunits.Entrez.IDs.":"8772;841;120892","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006915","GO.description":"apoptotic process","FunCat.ID":"40.10.02","FunCat.description":"apoptosis (type I programmed cell death)","PubMed.ID":19176810,"subunits.Protein.name.":"FAS-associated death domain protein;Caspase-8;Leucine-rich repeat serine/threonine-protein kinase 2","subunits.Gene.name.":"FADD;CASP8;LRRK2","subunits.Gene.name.syn.":"MORT1;MCH5;PARK8","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6023,"ComplexName":"Calcineurin","Organism":"Human","Synonyms":"CaN","Cell.line":"None","subunits.UniProt.IDs.":"P63098;Q08209","subunits.Entrez.IDs.":"5534;5530","Protein.complex.purification.method":"MI:0114-x-ray crystallography","GO.ID":"GO:0019722;GO:0005955;GO:0005516;GO:0016791","GO.description":"calcium-mediated signaling;calcineurin complex;calmodulin binding;phosphatase activity","FunCat.ID":"30.01.09.03","FunCat.description":"Ca2+ mediated signal transduction","PubMed.ID":8524402,"subunits.Protein.name.":"Calcineurin subunit B type 1;Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform","subunits.Gene.name.":"PPP3R1;PPP3CA","subunits.Gene.name.syn.":"CNA2 CNB;CALNA CNA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Calcineurin (CaN) is a calcium- and calmodulin-dependent protein serine/threonine phosphatase which is critical for several important cellular processes, including T-cell activation. CaN is the target of the immunosuppressive drugs cyclosporin A and FK506, which inhibit CaN after forming complexes with cytoplasmic binding proteins (cyclophilin and FKBP12, respectively). CaN is a heterodimer composed of a catalytic A unit and a regulatory B unit.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6025,"ComplexName":"Ubiquitin-conjugating enzyme E2 (UBC13-UEV1A)","Organism":"Human","Synonyms":"UBC13-UEV1A complex; TRIKA1 complex; TRAF6-regulated IKK activator 1","Cell.line":"HeLa cell","subunits.UniProt.IDs.":"P61088;Q13404","subunits.Entrez.IDs.":"7334;7335","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0016567;GO:0070534;GO:0007249","GO.description":"protein ubiquitination;protein K63-linked ubiquitination;I-kappaB kinase/NF-kappaB signaling","FunCat.ID":"14.07.05;30.01.05.01.04","FunCat.description":"modification by ubiquitination, deubiquitination;NIK-I-kappaB/NF-kappaB cascade","PubMed.ID":11057907,"subunits.Protein.name.":"Ubiquitin-conjugating enzyme E2 N;Ubiquitin-conjugating enzyme E2 variant 1","subunits.Gene.name.":"UBE2N;UBE2V1","subunits.Gene.name.syn.":"BLU;CROC1 UBE2V UEV1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex supports the activation of the I-kappa-B kinase complex by TRAF6. It catalyzes the formation of a Lys 63 (K63)-linked polyubiquitin chain.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6036,"ComplexName":"PARK2-EPS15-EGFR","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60260;P00533;P42566","subunits.Entrez.IDs.":"None;None;None","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0007034;GO:0007173","GO.description":"vacuolar transport;epidermal growth factor receptor signaling pathway","FunCat.ID":"20.09.13;30.05.01.12.01","FunCat.description":"vacuolar/lysosomal transport;EGF-receptor signalling pathway","PubMed.ID":16862145,"subunits.Protein.name.":"E3 ubiquitin-protein ligase parkin;Epidermal growth factor receptor;Epidermal growth factor receptor substrate 15","subunits.Gene.name.":"PARK2;EGFR;EPS15","subunits.Gene.name.syn.":"PRKN;ERBB, ERBB1, HER1;AF1P","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6037,"ComplexName":"CHIP-HSC70 complex","Organism":"Human","Synonyms":"None","Cell.line":"COS-1 cells","subunits.UniProt.IDs.":"P11142;Q9UNE7","subunits.Entrez.IDs.":"3312;10273","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0016567;GO:0016579;GO:0043161;GO:0006511","GO.description":"protein ubiquitination;protein deubiquitination;proteasome-mediated ubiquitin-dependent protein catabolic process;ubiquitin-dependent protein catabolic process","FunCat.ID":"14.07.05;14.13.01.01","FunCat.description":"modification by ubiquitination, deubiquitination;proteasomal degradation (ubiquitin/proteasomal pathway)","PubMed.ID":14612456,"subunits.Protein.name.":"Heat shock cognate 71 kDa protein;E3 ubiquitin-protein ligase CHIP","subunits.Gene.name.":"HSPA8;STUB1","subunits.Gene.name.syn.":"HSC70, HSP73, HSPA10;CHIP","Disease.comment":"CHIP-Hsc70 complex ubiquitinates phosphorylated Tau and enhances cell survival by decreasing the toxicity of hyperphosphorylated tau, a important factor in the neurofibrillary pathology of Alzheimer disease, via proteasomal degradation.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6038,"ComplexName":"dynein complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"O14576;P63167;Q14204;Q9Y6G9","subunits.Entrez.IDs.":"None;None;None;None","Protein.complex.purification.method":"MI:0096-pull down","GO.ID":"GO:0030705","GO.description":"cytoskeleton-dependent intracellular transport","FunCat.ID":"20.09.14","FunCat.description":"cytoskeleton-dependent transport","PubMed.ID":17403682,"subunits.Protein.name.":"Cytoplasmic dynein 1 intermediate chain 1;Dynein light chain 1, cytoplasmic;Cytoplasmic dynein 1 heavy chain 1;Cytoplasmic dynein 1 light intermediate chain 1","subunits.Gene.name.":"DYNC1I1;DYNLL1;DYNC1H1;DYNC1LI1","subunits.Gene.name.syn.":"DNCI1, DNCIC1;DLC1 DNCL1 DNCLC1 HDLC1;DHC1, DNCH1, DNCL, DNECL DYHC, KIAA0325;DNCLI1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6039,"ComplexName":"dynein-dynactin complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"O14576;P63167;Q14203;Q14204;Q9Y6G9","subunits.Entrez.IDs.":"None;None;None;None;None","Protein.complex.purification.method":"MI:0096-pull down","GO.ID":"GO:0030705","GO.description":"cytoskeleton-dependent intracellular transport","FunCat.ID":"20.09.14","FunCat.description":"cytoskeleton-dependent transport","PubMed.ID":17403682,"subunits.Protein.name.":"Cytoplasmic dynein 1 intermediate chain 1;Dynein light chain 1, cytoplasmic;Dynactin subunit 1;Cytoplasmic dynein 1 heavy chain 1;Cytoplasmic dynein 1 light intermediate chain 1","subunits.Gene.name.":"DYNC1I1;DYNLL1;DCTN1;DYNC1H1;DYNC1LI1","subunits.Gene.name.syn.":"DNCI1, DNCIC1;DLC1 DNCL1 DNCLC1 HDLC1;None;DHC1, DNCH1, DNCL, DNECL DYHC, KIAA0325;DNCLI1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6041,"ComplexName":"DISC-FEZ1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q99689;Q9NRI5","subunits.Entrez.IDs.":"None;27185","Protein.complex.purification.method":"MI:0018- two hybrid","GO.ID":"GO:0000902;GO:0016049","GO.description":"cell morphogenesis;cell growth","FunCat.ID":"40.01","FunCat.description":"cell growth / morphogenesis","PubMed.ID":12874605,"subunits.Protein.name.":"Fasciculation and elongation protein zeta-1 ;Disrupted in schizophrenia 1 protein","subunits.Gene.name.":"FEZ1;DISC1","subunits.Gene.name.syn.":";KIAA0457","Disease.comment":"OMIM: 181500 Schizophrenia","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6043,"ComplexName":"DISC-FEZ1-F-actin complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q6PJ43;Q99689;Q9NRI5","subunits.Entrez.IDs.":"None;None;27185","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0000902;GO:0016049","GO.description":"cell morphogenesis;cell growth","FunCat.ID":"40.01","FunCat.description":"cell growth / morphogenesis","PubMed.ID":12874605,"subunits.Protein.name.":"ACTG1 protein ;Fasciculation and elongation protein zeta-1 ;Disrupted in schizophrenia 1 protein","subunits.Gene.name.":"ACTG1;FEZ1;DISC1","subunits.Gene.name.syn.":";;KIAA0457","Disease.comment":"OMIM: 181500 Schizophrenia","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6046,"ComplexName":"PDE4B-DISC1 complex","Organism":"Human","Synonyms":"None","Cell.line":"SH-SY5Y cells","subunits.UniProt.IDs.":"Q07343;Q9NRI5","subunits.Entrez.IDs.":"5142;27185","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0030820","GO.description":"regulation of cAMP catabolic process","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":16293762,"subunits.Protein.name.":"cAMP-specific 3',5'-cyclic phosphodiesterase 4B ;Disrupted in schizophrenia 1 protein","subunits.Gene.name.":"PDE4B;DISC1","subunits.Gene.name.syn.":"DPDE4;KIAA0457","Disease.comment":"OMIM:181500 Schizophrenia, OMIM:608516.Major depression disorder (PMID:17823207).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6048,"ComplexName":"dynein-dynactin complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O08788;O88485;Q99KJ8","subunits.Entrez.IDs.":"None;None;None","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0030705","GO.description":"cytoskeleton-dependent intracellular transport","FunCat.ID":"20.09.14","FunCat.description":"cytoskeleton-dependent transport","PubMed.ID":18094236,"subunits.Protein.name.":"Dynactin subunit 1;Cytoplasmic dynein 1 intermediate chain 1 ;Dynactin subunit 2","subunits.Gene.name.":"Dctn1;Dync1i1;Dctn2","subunits.Gene.name.syn.":"None;Dnci1 Dncic1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6049,"ComplexName":"Ncstn-Psen1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"embryonic stem cells","subunits.UniProt.IDs.":"P49769;P57716","subunits.Entrez.IDs.":"None;None","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation; MI:0047- far western blotting","GO.ID":"GO:0016485;GO:0016504;GO:0023052;GO:0005886;GO:0005794","GO.description":"protein processing;peptidase activator activity;signaling;plasma membrane;Golgi apparatus","FunCat.ID":"14.07.11;18.02.01.01.03;30.01;70.02;70.08","FunCat.description":"protein processing (proteolytic);protease activator;cellular signalling;eukaryotic plasma membrane / membrane attached;Golgi","PubMed.ID":12603837,"subunits.Protein.name.":"Presenilin-1 ;Nicastrin","subunits.Gene.name.":"Psen1;Ncstn","subunits.Gene.name.syn.":"Ad3h Psnl1;","Disease.comment":"Presenilins are catalytic components of gamma-secretase, the protease responsible for generating the Alzheimer's amyloid beta peptides.","Subunits.comment":"None","Complex.comment":"The nicastrin-presenilin1 complex affects activity of gamma-secretase and is localized to the trans-Golgi network.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6052,"ComplexName":"BAG3-HSC70-HSPB8-CHIP complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O95817;P11142;Q9UJY1;Q9UNE7","subunits.Entrez.IDs.":"9531;3312;26353;10273","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0050821;GO:0006457;GO:0006950","GO.description":"protein stabilization;protein folding;response to stress","FunCat.ID":"14.01;32.01","FunCat.description":"protein folding and stabilization;stress response","PubMed.ID":20060297,"subunits.Protein.name.":"BAG family molecular chaperone regulator 3 ;Heat shock cognate 71 kDa protein;Heat shock protein beta-8 ;E3 ubiquitin-protein ligase CHIP","subunits.Gene.name.":"BAG3;HSPA8;HSPB8;STUB1","subunits.Gene.name.syn.":"BIS;HSC70, HSP73, HSPA10;CRYAC E2IG1 HSP22;CHIP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The BAG3-HSC70-HSPB8-CHIP complex facilitates the degradation of damaged components, such as filamin, through chaperone-assisted selective autophagy (CASA).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6053,"ComplexName":"LKB1-STRAD-MO25 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK-293 cells","subunits.UniProt.IDs.":"Q15831;Q7RTN6;Q9Y376","subunits.Entrez.IDs.":"6794;92335;51719","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0006468;GO:0006470;GO:0046777;GO:0006464","GO.description":"protein phosphorylation;protein dephosphorylation;protein autophosphorylation;cellular protein modification process","FunCat.ID":"14.07.03;14.07","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;protein modification","PubMed.ID":19892943,"subunits.Protein.name.":"Serine/threonine-protein kinase STK11 ;STE20-related kinase adapter protein alpha ;Calcium-binding protein 39","subunits.Gene.name.":"STK11;STRADA;CAB39","subunits.Gene.name.syn.":"LKB1 PJS;LYK5 STRAD;MO25","Disease.comment":"Loss-of-function mutations in the tumor suppressor LKB1 cause the rare inherited disease Peutz-Jeghers syndrome (PJS) in humans and are associated with various sporadic cancers, in particular non\\u2013small cell lung cancer.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6056,"ComplexName":"APP-DR6 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75509;P05067","subunits.Entrez.IDs.":"27242;351","Protein.complex.purification.method":"MI:0096- pull down;MI:0019- coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":19225519,"subunits.Protein.name.":"Tumor necrosis factor receptor superfamily member 21 ;Amyloid beta A4 protein","subunits.Gene.name.":"TNFRSF21;APP","subunits.Gene.name.syn.":"DR6;A4 AD1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"APP binds DR6 to trigger axon pruning and neuron death via distinct caspases.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6060,"ComplexName":"DISC1-ZNF365","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"None","subunits.Entrez.IDs.":"None","Protein.complex.purification.method":"MI:0018- two hybrid","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":19191256,"subunits.Protein.name.":"None","subunits.Gene.name.":"None","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"None"}
{"ComplexID":6061,"ComplexName":"DISC1-ZNF365 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q70YC5;Q9NRI5","subunits.Entrez.IDs.":"22891;27185","Protein.complex.purification.method":"MI:0018- two hybrid","GO.ID":"GO:0022008;GO:0048699","GO.description":"neurogenesis;generation of neurons","FunCat.ID":"41.05.13","FunCat.description":"neurogenesis","PubMed.ID":19191256,"subunits.Protein.name.":"Protein ZNF365 ;Disrupted in schizophrenia 1 protein","subunits.Gene.name.":"ZNF365;DISC1","subunits.Gene.name.syn.":"KIAA0844;KIAA0457","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6062,"ComplexName":"DISC1-IMMT complex","Organism":"Mouse","Synonyms":"None","Cell.line":"CAD cells","subunits.UniProt.IDs.":"Q811T9;Q8CAQ8","subunits.Entrez.IDs.":"244667;76614","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20880836,"subunits.Protein.name.":"Disrupted in schizophrenia 1 homolog;MICOS complex subunit Mic60","subunits.Gene.name.":"Disc1;Immt","subunits.Gene.name.syn.":";Mic60","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6066,"ComplexName":"Xanthine oxidase","Organism":"Human","Synonyms":"Xanthine oxidase/dehydrogenase (EC 1.17.3.2); Xanthine oxidase type D/ type O","Cell.line":"human milk","subunits.UniProt.IDs.":"P47989","subunits.Entrez.IDs.":"7498","Protein.complex.purification.method":"MI:0071-molecular sieving","GO.ID":"GO:0006195;GO:0030151;GO:0006150;GO:0006151;GO:0070403","GO.description":"purine nucleotide catabolic process;molybdenum ion binding;hypoxanthine oxidation;xanthine oxidation;NAD+ binding","FunCat.ID":"01.03.01.01","FunCat.description":"purine nucleotide /nucleoside/nucleobase catabolism","PubMed.ID":1627588,"subunits.Protein.name.":"Xanthine dehydrogenase/oxidase [Includes: Xanthine dehydrogenase","subunits.Gene.name.":"XDH","subunits.Gene.name.syn.":"XDHA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Xanthine oxidase is a molybdoenzyme that catalyses the oxidation of hypoxanthine to xanthine and of xanthine to uric acid. In mammalian systems, it occurs as partially interconvertible Type D (dehydrogenase) and Type O (oxidase) forms, reducing, respectively, NAD+ or oxygen. In such systems, the term 'xanthine oxidase' commonly refers to both Type D and Type O forms.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":6067,"ComplexName":"ESR1-SP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"MCF-7 MDA-MB-231 HeLa","subunits.UniProt.IDs.":"P03372;P08047","subunits.Entrez.IDs.":"2099;6667","Protein.complex.purification.method":"MI:0045- experimental","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":10681512,"subunits.Protein.name.":"Estrogen receptor;Transcription factor Sp1","subunits.Gene.name.":"ESR1;SP1","subunits.Gene.name.syn.":"ESR, NR3A1;TSFP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6068,"ComplexName":"ESR1-CEBPB complex","Organism":"Human","Synonyms":"None","Cell.line":"MCF-7  Hep-G2","subunits.UniProt.IDs.":"P03372;P17676","subunits.Entrez.IDs.":"2099;1051","Protein.complex.purification.method":"MI:0045- experimental","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":18852215,"subunits.Protein.name.":"Estrogen receptor;CCAAT/enhancer-binding protein beta","subunits.Gene.name.":"ESR1;CEBPB","subunits.Gene.name.syn.":"ESR, NR3A1;TCF5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6069,"ComplexName":"ESR1-GRIP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"U-937","subunits.UniProt.IDs.":"P03372;Q9Y3R0","subunits.Entrez.IDs.":"2099;23426","Protein.complex.purification.method":"MI:0045- experimental","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":10611355,"subunits.Protein.name.":"Estrogen receptor;Glutamate receptor-interacting protein 1","subunits.Gene.name.":"ESR1;GRIP1","subunits.Gene.name.syn.":"ESR, NR3A1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6072,"ComplexName":"TRA2B1-SRp30c-SRp55 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P62995;Q13242;Q13247","subunits.Entrez.IDs.":"None;None;None","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0043484;GO:0048024","GO.description":"regulation of RNA splicing;regulation of mRNA splicing, via spliceosome","FunCat.ID":"11.04.03.01.10","FunCat.description":"regulation of splicing","PubMed.ID":15695522,"subunits.Protein.name.":"Transformer-2 protein homolog beta;Serine/arginine-rich splicing factor 9;Serine/arginine-rich splicing factor 6","subunits.Gene.name.":"TRA2B;SRSF9;SRSF6","subunits.Gene.name.syn.":"SFRS10;SFRS9 SRP30C;SFRS6 SRP55","Disease.comment":"None","Subunits.comment":"TRA2B1 variant was used.","Complex.comment":"SRp30c is also known as SRSF9, and SRp55 as SRSF6. To confirm that the three factors can act as a complex, co-immunoprecipitations of the three proteins were done. It could be shown that htra2beta1 (a variant of TRA2B) interacts with SRp55 and that SRp30c interacts with both SRp55 and htra2beta1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6073,"ComplexName":"SRp30c-SRp55 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q13242;Q13247","subunits.Entrez.IDs.":"None;None","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0043484;GO:0048024","GO.description":"regulation of RNA splicing;regulation of mRNA splicing, via spliceosome","FunCat.ID":"11.04.03.01.10","FunCat.description":"regulation of splicing","PubMed.ID":15695522,"subunits.Protein.name.":"Serine/arginine-rich splicing factor 9;Serine/arginine-rich splicing factor 6","subunits.Gene.name.":"SRSF9;SRSF6","subunits.Gene.name.syn.":"SFRS9 SRP30C;SFRS6 SRP55","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Tau exons 2 and 10, which are misregulated in neurodegenerative diseases, are partly regulated by silencers which bind a SRp30c-SRp55 complex that either recruits or antagonizes htra2beta1 (a variant of TRA2B).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6074,"ComplexName":"PAS (PIKfyve-ArPIKfyve-Sac3) complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS7 cells","subunits.UniProt.IDs.":"Q08AM6;Q92562;Q9Z1T6","subunits.Entrez.IDs.":"55697;9896;18711","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006661;GO:0006897;GO:0048015","GO.description":"phosphatidylinositol biosynthetic process;endocytosis;phosphatidylinositol-mediated signaling","FunCat.ID":"20.09.18.09.01","FunCat.description":"endocytosis","PubMed.ID":18950639,"subunits.Protein.name.":"Protein VAC14 homolog;Polyphosphoinositide phosphatase;1-phosphatidylinositol 3-phosphate 5-kinase","subunits.Gene.name.":"VAC14;FIG4;Pikfyve","subunits.Gene.name.syn.":"TAX1BP2, TRX;KIAA0274, SAC3;Kiaa0981, Pip5k3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"ArPIKfyve is the principal organizer interacting with both Sac3 and PIKfyve, whereas Sac3 is permissive for maximal PIKfyve-ArPIKfyve association in the PAS complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Mus musculus (Mouse)"}
{"ComplexID":6075,"ComplexName":"CST complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q2NKJ3;Q86WV5;Q9H668","subunits.Entrez.IDs.":"80169;100134934;79991","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0018- two hybrid","GO.ID":"GO:0003697;GO:0000723","GO.description":"single-stranded DNA binding;telomere maintenance","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":19854130,"subunits.Protein.name.":"CST complex subunit CTC1 ;CST complex subunit TEN1 ;CST complex subunit STN1","subunits.Gene.name.":"CTC1;TEN1;OBFC1","subunits.Gene.name.syn.":"C17orf68;C17orf106;STN1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6076,"ComplexName":"c-Abl-cortactin-nmMLCK complex","Organism":"Human","Synonyms":"None","Cell.line":"Human pulmonary artery endothelial cells (HPAEC)","subunits.UniProt.IDs.":"P00519;Q14247;Q15746","subunits.Entrez.IDs.":"25;2017;4638","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007010;GO:0061028","GO.description":"cytoskeleton organization;establishment of endothelial barrier","FunCat.ID":"42.04","FunCat.description":"cytoskeleton/structural proteins","PubMed.ID":20861316,"subunits.Protein.name.":"Tyrosine-protein kinase ABL1;Src substrate cortactin;Myosin light chain kinase, smooth muscle","subunits.Gene.name.":"ABL1;CTTN;MYLK","subunits.Gene.name.syn.":"ABL, JTK7;EMS1;MLCK, MLCK1, MYLK1","Disease.comment":"nmMLCK plays a role in inflammatory processes, several polymorphisms in the nmMLCK gene (MYLK) are highly associated with susceptibility to acute inflammatory states such as acute lung injury/acute respiratory distress syndrome (ALI/ARDS) and asthma.","Subunits.comment":"MYLK has been defined as non-muscle isoform, nmMYLK.","Complex.comment":"The association of c-Abl, nmMLCK, and cortactin is increased in ECs (endothelial cells) during S1P (sphingosine 1-phosphate) ,induced barrier enhancement.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6077,"ComplexName":"Mcl1-1-Her2 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"MEF cells","subunits.UniProt.IDs.":"P04626;P97287","subunits.Entrez.IDs.":"2064;17210","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0001666","GO.description":"response to hypoxia","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26921175,"subunits.Protein.name.":"Receptor tyrosine-protein kinase erbB-2;Induced myeloid leukemia cell differentiation protein Mcl-1 homolog","subunits.Gene.name.":"ERBB2;Mcl1","subunits.Gene.name.syn.":"HER2, MLN19, NEU, NGL;","Disease.comment":"OMIM:114480 Breast cancer","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Mus musculus (Mouse)"}
{"ComplexID":6078,"ComplexName":"HSPA2-ACR-PDIA6 complex","Organism":"Human","Synonyms":"None","Cell.line":"testis","subunits.UniProt.IDs.":"P12821;P54652;Q15084","subunits.Entrez.IDs.":"1636;3306;10130","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0060046","GO.description":"regulation of acrosome reaction","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26676989,"subunits.Protein.name.":"Angiotensin-converting enzyme ;Heat shock-related 70 kDa protein 2 ;Protein disulfide-isomerase A6","subunits.Gene.name.":"ACE;HSPA2;PDIA6","subunits.Gene.name.syn.":"DCP DCP1;;ERP5 P5 TXNDC7","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6079,"ComplexName":"BAG6-HSPA2 complex","Organism":"Human","Synonyms":"None","Cell.line":"spermatozoa","subunits.UniProt.IDs.":"P46379;P54652","subunits.Entrez.IDs.":"7917;3306","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007283;GO:1903332","GO.description":"spermatogenesis;regulation of protein folding","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26153132,"subunits.Protein.name.":"Large proline-rich protein BAG6 ;Heat shock-related 70 kDa protein 2","subunits.Gene.name.":"BAG6;HSPA2","subunits.Gene.name.syn.":"BAT3 G3;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6080,"ComplexName":"ACAP1-CHC-Glut4 complex","Organism":"Human","Synonyms":"None","Cell.line":"differentiated 3T3-L1 cells","subunits.UniProt.IDs.":"P14672;Q00610;Q15027","subunits.Entrez.IDs.":"6517;1213;9744","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0032456","GO.description":"endocytic recycling","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":17664335,"subunits.Protein.name.":"Solute carrier family 2, facilitated glucose transporter member 4;Clathrin heavy chain 1;Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1","subunits.Gene.name.":"SLC2A4;CLTC;ACAP1","subunits.Gene.name.syn.":"GLUT4;CLH17, CLTCL2, KIAA0034, CHC;CENTB1, KIAA0050","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results suggested that ACAP1 acted like AP adaptors in bridging an interaction between cargo tails and clathrin triskelion.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6083,"ComplexName":"CART complex","Organism":"Human","Synonyms":"Cytoskeleton-associated recycling or transport complex","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O14964;O43707;O75382;Q9ULV0","subunits.Entrez.IDs.":"9146;81;10612;4645","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0004998;GO:0001881;GO:0032456","GO.description":"transferrin receptor activity;receptor recycling;endocytic recycling","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":15772161,"subunits.Protein.name.":"Hepatocyte growth factor-regulated tyrosine kinase substrate;Alpha-actinin-4;Tripartite motif-containing protein 3;Unconventional myosin-Vb","subunits.Gene.name.":"HGS;ACTN4;TRIM3;MYO5B","subunits.Gene.name.syn.":"HRS;None;BERP, RNF22, RNF97;KIAA1119","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The CART complex is necessary for efficient recycling of the transferrin (Tf) receptor to the plasma membrane, but not movement to lysosomes and degradation of the EGFR.The CART complex, composed of hrs, actinin-4, BERP, and myosin V, seemed to require BERP to link myosin V to hrs-actinin-4.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6084,"ComplexName":"AFF4 super elongation complex (SEC)","Organism":"Human","Synonyms":"None","Cell.line":"293 Flp-in-TRex cells","subunits.UniProt.IDs.":"O00472;O60563;O60583;P42568;P50750;P51825;P55199;Q03111;Q96JC9;Q9HB65;Q9UHB7","subunits.Entrez.IDs.":"22936;904;905;4300;1025;4299;8178;4298;85403;80237;27125","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies;MI:0019-coimmunoprecipitation;MI:0071-molecular sieving","GO.ID":"GO:0006354","GO.description":"DNA-templated transcription, elongation","FunCat.ID":"11.02.03.01.04","FunCat.description":"transcription elongation","PubMed.ID":20159561,"subunits.Protein.name.":"RNA polymerase II elongation factor ELL2;Cyclin-T1;Cyclin-T2;Protein AF-9;Cyclin-dependent kinase 9;AF4/FMR2 family member 1;RNA polymerase II elongation factor ELL;Protein ENL;ELL-associated factor 1;RNA polymerase II elongation factor ELL3;AF4/FMR2 family member 4","subunits.Gene.name.":"ELL2;CCNT1;CCNT2;MLLT3;CDK9;AFF1;ELL;MLLT1;EAF1;ELL3;AFF4","subunits.Gene.name.syn.":"None;None;None;AF9, YEATS3;CDC2L4, TAK;AF4, FEL, MLLT2, PBM1;C19orf17;ENL, LTG19, YEATS1;None;None;AF5Q31, MCEF","Disease.comment":"The authors propose that the AFF4 super elongation complex (SEC) could be a key regulator in the pathogenesis of leukemia through many of the MLL (Mixed Lineage Leukemia) partners are found in hematological malignancies.","Subunits.comment":"Complex subunit Cyclin-T2  is described as isoform Cyclin-T2a or Cyclin-T2b.","Complex.comment":"AFF4 is a central factor required for the assembly and integrity of the ELL/P-TEFb (consisting of Cdk9 with cyclin T1, T2a orT2b)/MLL partner elongation complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6085,"ComplexName":"MCPIP1-MCPIP4 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK-293 cells","subunits.UniProt.IDs.":"A2A288;Q5D1E8","subunits.Entrez.IDs.":"340152;80149","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0018- two hybrid;MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0006954","GO.description":"inflammatory response","FunCat.ID":"36.25.16.07","FunCat.description":"inflammatory response","PubMed.ID":26134560,"subunits.Protein.name.":"Probable ribonuclease ZC3H12D ;Endoribonuclease ZC3H12A","subunits.Gene.name.":"ZC3H12D;ZC3H12A","subunits.Gene.name.syn.":"C6orf95 MCPIP4 TFL;MCPIP MCPIP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6086,"ComplexName":"Atp7a-PAM complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"AtT-20 cells","subunits.UniProt.IDs.":"P19021;Q64430","subunits.Entrez.IDs.":"5066;11977","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006825;GO:0055070","GO.description":"copper ion transport;copper ion homeostasis","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26170456,"subunits.Protein.name.":"Peptidyl-glycine alpha-amidating monooxygenase ;Copper-transporting ATPase 1","subunits.Gene.name.":"PAM;Atp7a","subunits.Gene.name.syn.":";Mnk","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Mus musculus (Mouse)"}
{"ComplexID":6087,"ComplexName":"ERbeta-AR complex","Organism":"Human","Synonyms":"None","Cell.line":"Prostate cancer cells","subunits.UniProt.IDs.":"P10275;Q92731","subunits.Entrez.IDs.":"367;2100","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006355","GO.description":"regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":26015225,"subunits.Protein.name.":"Androgen receptor;Estrogen receptor beta","subunits.Gene.name.":"AR;ESR2","subunits.Gene.name.syn.":"DHTR, NR3C4;ESTRB NR3A2","Disease.comment":"OMIM:176807 Prostate cancer","Subunits.comment":"None","Complex.comment":"17beta-estradiol (E2) up-regulates SOX4 expression in the absence of androgen through the formation of a protein complex between ERbeta (estrogen beta receptor) and AR (androgen receptor). Knockdown of AR or ERbeta blocks the E2-induced SOX4 expression. ChIP assays confirmed that both ERbeta and AR bind to the SOX4 promoter in response to E2. E2 could promote proliferation of PCa cells through the up-regulation of SOX4 under androgen-depleted environment (PMID:26015225).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6088,"ComplexName":"Seipin-AGPAT2 complex","Organism":"Human","Synonyms":"BSCL2--AGPAT2 complex","Cell.line":"HEK-293 cells","subunits.UniProt.IDs.":"O15120;Q96G97","subunits.Entrez.IDs.":"10555;26580","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:1904177;GO:0008610","GO.description":"regulation of adipose tissue development;lipid biosynthetic process","FunCat.ID":"1.06","FunCat.description":"lipid, fatty acid and isoprenoid metabolism","PubMed.ID":25737955,"subunits.Protein.name.":"1-acyl-sn-glycerol-3-phosphate acyltransferase beta ;Seipin","subunits.Gene.name.":"AGPAT2;BSCL2","subunits.Gene.name.syn.":";","Disease.comment":"OMIM:608594 Lipodystrophy, congenital generalized, type 1","Subunits.comment":"None","Complex.comment":"The seipin can bind AGPAT2 during adipogenesis and this interaction during adipogenesis can increase the nuclear accumulation of PPARgamma (PMID:25737955).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6089,"ComplexName":"Seipin-AGPAT2-lipin1 complex","Organism":"Human","Synonyms":"BSCL2-AGPAT2-LPIN1 complex","Cell.line":"HEK-293 cells","subunits.UniProt.IDs.":"O15120;Q14693;Q96G97","subunits.Entrez.IDs.":"10555;23175;26580","Protein.complex.purification.method":"MI:0428- imaging techniques","GO.ID":"GO:1904177;GO:0008610","GO.description":"regulation of adipose tissue development;lipid biosynthetic process","FunCat.ID":"1.06","FunCat.description":"lipid, fatty acid and isoprenoid metabolism","PubMed.ID":25737955,"subunits.Protein.name.":"1-acyl-sn-glycerol-3-phosphate acyltransferase beta ;Phosphatidate phosphatase LPIN1 ;Seipin","subunits.Gene.name.":"AGPAT2;LPIN1;BSCL2","subunits.Gene.name.syn.":";KIAA0188;","Disease.comment":"OMIM:269700 LipoLdystrophy, congenital generalized, type 2OMIM:608594  LipoLdystrophy, congenital generalized, type 1","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6090,"ComplexName":"Seipin-lipin1 complex","Organism":"Human","Synonyms":"BSCL2-LPIN1 complex","Cell.line":"HEK-293 cells","subunits.UniProt.IDs.":"Q14693;Q96G97","subunits.Entrez.IDs.":"23175;26580","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25737955,"subunits.Protein.name.":"Phosphatidate phosphatase LPIN1 ;Seipin","subunits.Gene.name.":"LPIN1;BSCL2","subunits.Gene.name.syn.":"KIAA0188;","Disease.comment":"OMIM:269700 Lipodystrophy, congenital generalized, type 2","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6091,"ComplexName":"NF-YA-LaminA complex","Organism":"Human","Synonyms":"NFYA-LMNA complex","Cell.line":"SKBR3 cells","subunits.UniProt.IDs.":"P02545;P23511","subunits.Entrez.IDs.":"4000;4800","Protein.complex.purification.method":"MI:0069- mass spectrometry studies of complexes","GO.ID":"GO:0007049;GO:0008283","GO.description":"cell cycle;cell proliferation","FunCat.ID":"10.03","FunCat.description":"cell cycle","PubMed.ID":27793050,"subunits.Protein.name.":"Prelamin-A/C [Cleaved into: Lamin-A/C ;Nuclear transcription factor Y subunit alpha","subunits.Gene.name.":"LMNA;NFYA","subunits.Gene.name.syn.":"LMN1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6092,"ComplexName":"c-Jun-ATF3 complex","Organism":"Human","Synonyms":"JUN-ATF3 complex","Cell.line":"MDA-MB-231 cells","subunits.UniProt.IDs.":"P05412;P18847","subunits.Entrez.IDs.":"3725;467","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006355","GO.description":"regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":27751807,"subunits.Protein.name.":"Transcription factor AP-1 ;Cyclic AMP-dependent transcription factor ATF-3","subunits.Gene.name.":"JUN;ATF3","subunits.Gene.name.syn.":";","Disease.comment":"OMIM:114480 Breast cancer","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6093,"ComplexName":"Trim27-Slx2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"testis","subunits.UniProt.IDs.":"Q62158;Q9DAC5","subunits.Entrez.IDs.":"19720;75514","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0018- two hybrid","GO.ID":"GO:0007286;GO:0060631","GO.description":"spermatid development;regulation of meiosis I","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":27612028,"subunits.Protein.name.":"Zinc finger protein RFP ;MCG8351","subunits.Gene.name.":"Trim27;1700013H16","subunits.Gene.name.syn.":"Rfp;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6094,"ComplexName":"SIRT1-HERC2-LKB1 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O95714;Q96EB6;Q9WTK7","subunits.Entrez.IDs.":"8924;23411;20869","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0060312","GO.description":"regulation of blood vessel remodeling","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":27259994,"subunits.Protein.name.":"E3 ubiquitin-protein ligase HERC2 ;NAD-dependent protein deacetylase sirtuin-1 ;Serine/threonine-protein kinase STK11","subunits.Gene.name.":"HERC2;SIRT1;Stk11","subunits.Gene.name.syn.":";SIR2L1;Lkb1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Mus musculus (Mouse)"}
{"ComplexID":6095,"ComplexName":"PLEKHA7-PDZD11 complex","Organism":"Human","Synonyms":"MDCK cells","Cell.line":"None","subunits.UniProt.IDs.":"Q5EBL8;Q6IQ23","subunits.Entrez.IDs.":"51248;144100","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0096- pull down;MI:0018- two hybrid","GO.ID":"GO:0005912","GO.description":"adherens junction","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":27044745,"subunits.Protein.name.":"PDZ domain-containing protein 11;Pleckstrin homology domain-containing family A member 7","subunits.Gene.name.":"PDZD11;PLEKHA7","subunits.Gene.name.syn.":"AIPP1 PDZK11 PISP;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6096,"ComplexName":"alphaB-crystallin-Nav1.5 complex","Organism":"Human","Synonyms":"CRYAB-SCN5A complex","Cell.line":"HEK-293 cells","subunits.UniProt.IDs.":"P02511;Q14524","subunits.Entrez.IDs.":"1410;6331","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0096- pull down","GO.ID":"GO:1905150;GO:0031396","GO.description":"regulation of voltage-gated sodium channel activity;regulation of protein ubiquitination","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26961874,"subunits.Protein.name.":"Alpha-crystallin B chain ;Sodium channel protein type 5 subunit alpha","subunits.Gene.name.":"CRYAB;SCN5A","subunits.Gene.name.syn.":"CRYA2 HSPB5;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6097,"ComplexName":"MEF2-NR2F2 complex","Organism":"Human","Synonyms":"None","Cell.line":"testis","subunits.UniProt.IDs.":"P24468;Q02078","subunits.Entrez.IDs.":"7026;4205","Protein.complex.purification.method":"None","GO.ID":"GO:0019218","GO.description":"regulation of steroid metabolic process","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26748576,"subunits.Protein.name.":"COUP transcription factor 2 ;Myocyte-specific enhancer factor 2A","subunits.Gene.name.":"NR2F2;MEF2A","subunits.Gene.name.syn.":"ARP1 TFCOUP2;MEF2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6098,"ComplexName":"ZP3-ACR complex","Organism":"Bovine","Synonyms":"None","Cell.line":"epididymis, semen","subunits.UniProt.IDs.":"P48830;P79343","subunits.Entrez.IDs.":"None;None","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0004- affinity chromatography technologies","GO.ID":"GO:0007340;GO:0051336;GO:0043159","GO.description":"acrosome reaction;regulation of hydrolase activity;acrosomal matrix","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26897631,"subunits.Protein.name.":"Zona pellucida sperm-binding protein 3 ;Acrosin","subunits.Gene.name.":"ZP3;bovine pro","subunits.Gene.name.syn.":"ZPC;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":6099,"ComplexName":"ZP3-MFGE8 protein","Organism":"Human","Synonyms":"OMC32-lactadherin protein","Cell.line":"epidydimis, semen","subunits.UniProt.IDs.":"P48830;Q95114","subunits.Entrez.IDs.":"280964;281913","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0004- affinity chromatography technologies","GO.ID":"GO:0007340;GO:0051336;GO:0043159","GO.description":"acrosome reaction;regulation of hydrolase activity;acrosomal matrix","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26897631,"subunits.Protein.name.":"Zona pellucida sperm-binding protein 3 ;Lactadherin","subunits.Gene.name.":"ZP3;MFGE8","subunits.Gene.name.syn.":"ZPC;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":6100,"ComplexName":"ZP3-SPACA3 complex","Organism":"Human","Synonyms":"None","Cell.line":"epididymis, semen","subunits.UniProt.IDs.":"A6QQ77;P48830","subunits.Entrez.IDs.":"617955;280964","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0004- affinity chromatography technologies","GO.ID":"GO:0007340;GO:0051336;GO:0043159","GO.description":"acrosome reaction;regulation of hydrolase activity;acrosomal matrix","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26897631,"subunits.Protein.name.":"Sperm acrosome membrane-associated protein 3;Zona pellucida sperm-binding protein 3","subunits.Gene.name.":"SPACA3;ZP3","subunits.Gene.name.syn.":";ZPC","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":6102,"ComplexName":"ZP3-IZUMO1 complex","Organism":"Human","Synonyms":"OMC32-IZUMO1 complex","Cell.line":"epididymis, semen","subunits.UniProt.IDs.":"P21754;Q8IYV9","subunits.Entrez.IDs.":"7784;284359","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0004- affinity chromatography technologies","GO.ID":"GO:0060046","GO.description":"regulation of acrosome reaction","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26897631,"subunits.Protein.name.":"Zona pellucida sperm-binding protein 3 ;Izumo sperm-egg fusion protein 1","subunits.Gene.name.":"ZP3;IZUMO1","subunits.Gene.name.syn.":"ZP3A ZP3B ZPC;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6103,"ComplexName":"proMBP-angiotensinogen complex","Organism":"Human","Synonyms":"None","Cell.line":"pregnancy serum and plasma","subunits.UniProt.IDs.":"P01019;P13727","subunits.Entrez.IDs.":"183;5553","Protein.complex.purification.method":"MI:0226-ion exchange chromatography;MI:0071-molecular sieving","GO.ID":"GO:0008217;GO:0007565","GO.description":"regulation of blood pressure;female pregnancy","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":7539791,"subunits.Protein.name.":"Angiotensinogen;Bone marrow proteoglycan","subunits.Gene.name.":"AGT;PRG2","subunits.Gene.name.syn.":"SERPINA8;MBP","Disease.comment":"The authors suggest that this complex may be involved in the pathophysiology of pregnancies associated with hypertension.","Subunits.comment":"proMBP (MBP) is derived from a preproprotein of 222 amino acids.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6104,"ComplexName":"PAPP-A-proMBP complex","Organism":"Human","Synonyms":"None","Cell.line":"pregnancy serum","subunits.UniProt.IDs.":"P13727;Q13219","subunits.Entrez.IDs.":"5553;5069","Protein.complex.purification.method":"MI:0226- ion exchange chromatography","GO.ID":"GO:0007565","GO.description":"female pregnancy","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":7539791,"subunits.Protein.name.":"Bone marrow proteoglycan;Pappalysin-1","subunits.Gene.name.":"PRG2;PAPPA","subunits.Gene.name.syn.":"MBP;","Disease.comment":"None","Subunits.comment":"proMBP (MBP) is derived from a preproprotein of 222 amino acids.","Complex.comment":"The serum levels of proMBP exceeds that of PAPP-A by several fold on a molar basis, and consequently, only a fraction of circulating proMBP is bound to PAPP-A.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6105,"ComplexName":"CCT-gelsolin complex","Organism":"Mouse","Synonyms":"Tcp1-Gsn complex","Cell.line":"None","subunits.UniProt.IDs.":"P11983;P13020","subunits.Entrez.IDs.":"21454;227753","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0048870","GO.description":"cell motility","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26364302,"subunits.Protein.name.":"T-complex protein 1 subunit alpha;Gelsolin","subunits.Gene.name.":"Tcp1;Gsn","subunits.Gene.name.syn.":"Cct1 Ccta;Gsb","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6106,"ComplexName":"KGF-KITLG complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"ovary","subunits.UniProt.IDs.":"A0A0F7CV11;A0A0F7GJB8","subunits.Entrez.IDs.":"None;102401528","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0001541","GO.description":"ovarian follicle development","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26083339,"subunits.Protein.name.":"Fibroblast growth factor ;Kit ligand","subunits.Gene.name.":"KGF;KITLG","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Bubalus bubalis (Domestic water buffalo);Bubalus bubalis (Domestic water buffalo)"}
{"ComplexID":6107,"ComplexName":"proMBP-angiotensinogen-c3dg complex","Organism":"Human","Synonyms":"None","Cell.line":"pregnancy serum and plasma","subunits.UniProt.IDs.":"P01019;P01024;P13727","subunits.Entrez.IDs.":"183;718;5553","Protein.complex.purification.method":"None","GO.ID":"GO:0008217;GO:0007565","GO.description":"regulation of blood pressure;female pregnancy","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":7539791,"subunits.Protein.name.":"Angiotensinogen;Complement C3;Bone marrow proteoglycan","subunits.Gene.name.":"AGT;C3;PRG2","subunits.Gene.name.syn.":"SERPINA8;CPAMD1;MBP","Disease.comment":"The authors suggest that this complex may be involved in the pathophysiology of pregnancies associated with hypertension.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6108,"ComplexName":"STIM1-TRPV4 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK-293 cells","subunits.UniProt.IDs.":"Q13586;Q9HBA0","subunits.Entrez.IDs.":"6786;59341","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0096- pull down","GO.ID":"GO:0051924","GO.description":"regulation of calcium ion transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25972993,"subunits.Protein.name.":"Stromal interaction molecule 1;Transient receptor potential cation channel subfamily V member 4","subunits.Gene.name.":"STIM1;TRPV4","subunits.Gene.name.syn.":"GOK;VRL2 VROAC","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6109,"ComplexName":"FHF complex","Organism":"Human","Synonyms":"None","Cell.line":"human embryonic kidney 293T cells","subunits.UniProt.IDs.":"Q86VS8;Q8N612;Q96ED9;Q9H8T0;Q9UJC3","subunits.Entrez.IDs.":"84376;84067;29911;64400;51361","Protein.complex.purification.method":"MI:0071-molecular sieving","GO.ID":"GO:0016192;GO:0006906;GO:0016197","GO.description":"vesicle-mediated transport;vesicle fusion;endosomal transport","FunCat.ID":"20.09.07;20.09.07.27","FunCat.description":"vesicular transport (Golgi network, etc.);vesicle fusion","PubMed.ID":18799622,"subunits.Protein.name.":"Protein Hook homolog 3;FTS and Hook-interacting protein;Protein Hook homolog 2;AKT-interacting protein;Protein Hook homolog 1","subunits.Gene.name.":"HOOK3;FAM160A2;HOOK2;AKTIP;HOOK1","subunits.Gene.name.syn.":"None;C11orf56, KIAA1759;None;FTS;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Hook proteins as well as FTS interact with members of both the class B and class C components of the homotypic vesicular protein sorting (HOPS) complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6110,"ComplexName":"Drd3-Slc6a complex","Organism":"Mouse","Synonyms":"D3R-DAT complex","Cell.line":"None","subunits.UniProt.IDs.":"P30728;Q61327","subunits.Entrez.IDs.":"13490;13162","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0051584","GO.description":"regulation of dopamine uptake involved in synaptic transmission","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25511804,"subunits.Protein.name.":"D;Sodium-dependent dopamine transporter","subunits.Gene.name.":"Drd3;Slc6a3","subunits.Gene.name.syn.":";Dat Dat1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6111,"ComplexName":"protein phosphatase 2A C-subunit-synapsin complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P17600;P67775","subunits.Entrez.IDs.":"6853;5515","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0050804","GO.description":"modulation of synaptic transmission","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25522393,"subunits.Protein.name.":"Synapsin-1 ;Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform","subunits.Gene.name.":"SYN1;PPP2CA","subunits.Gene.name.syn.":";None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6112,"ComplexName":"DGAT2-MGAT2 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK-293 cells","subunits.UniProt.IDs.":"Q10469;Q96PD7","subunits.Entrez.IDs.":"4247;84649","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0030- cross-linking studies","GO.ID":"GO:0019432","GO.description":"triglyceride biosynthetic process","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25164810,"subunits.Protein.name.":"Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase;Diacylglycerol O-acyltransferase 2","subunits.Gene.name.":"MGAT2;DGAT2","subunits.Gene.name.syn.":"None;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6114,"ComplexName":"BAG1-HSC70 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P11142;Q99933","subunits.Entrez.IDs.":"3312;573","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0006457","GO.description":"protein folding","FunCat.ID":"14.01","FunCat.description":"protein folding and stabilization","PubMed.ID":9305631,"subunits.Protein.name.":"Heat shock cognate 71 kDa protein;BAG family molecular chaperone regulator 1","subunits.Gene.name.":"HSPA8;BAG1","subunits.Gene.name.syn.":"HSC70, HSP73, HSPA10;HAP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6115,"ComplexName":"BAG1-HSP70 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P0DMV8;Q99933","subunits.Entrez.IDs.":"3303;573","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0006457","GO.description":"protein folding","FunCat.ID":"14.01","FunCat.description":"protein folding and stabilization","PubMed.ID":9305631,"subunits.Protein.name.":"Heat shock 70 kDa protein 1A;BAG family molecular chaperone regulator 1","subunits.Gene.name.":"HSPA1A;BAG1","subunits.Gene.name.syn.":"HSPA1, HSX70, HSP70-1A;HAP","Disease.comment":"None","Subunits.comment":"Since the authors did not specify HSP70, we used isoform HSPA1A.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6116,"ComplexName":"Hook1-Vps16 complex","Organism":"Human","Synonyms":"None","Cell.line":"human embryonic kidney 293T cells","subunits.UniProt.IDs.":"Q9H269;Q9UJC3","subunits.Entrez.IDs.":"64601;51361","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0016197","GO.description":"endosomal transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":18799622,"subunits.Protein.name.":"Vacuolar protein sorting-associated protein 16 homolog;Protein Hook homolog 1","subunits.Gene.name.":"VPS16;HOOK1","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"FTS and Hook proteins associate with class B and class C components of the HOPS complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6117,"ComplexName":"Hook1-Vps18 complex","Organism":"Human","Synonyms":"None","Cell.line":"human embryonic kidney 293T cells","subunits.UniProt.IDs.":"Q9P253;Q9UJC3","subunits.Entrez.IDs.":"57617;51361","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0016197","GO.description":"endosomal transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":18799622,"subunits.Protein.name.":"Vacuolar protein sorting-associated protein 18 homolog;Protein Hook homolog 1","subunits.Gene.name.":"VPS18;HOOK1","subunits.Gene.name.syn.":"KIAA1475;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"FTS and Hook proteins associate with class B and class C components of the HOPS complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6118,"ComplexName":"Hook1-Vps39 complex","Organism":"Human","Synonyms":"None","Cell.line":"human embryonic kidney 293T cells","subunits.UniProt.IDs.":"Q96JC1;Q9UJC3","subunits.Entrez.IDs.":"23339;51361","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0016197","GO.description":"endosomal transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":18799622,"subunits.Protein.name.":"Vam6/Vps39-like protein;Protein Hook homolog 1","subunits.Gene.name.":"VPS39;HOOK1","subunits.Gene.name.syn.":"KIAA0770, TLP, VAM6;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"FTS and Hook proteins associate with class B and class C components of the HOPS complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6119,"ComplexName":"Hook1-Vps41 complex","Organism":"Human","Synonyms":"None","Cell.line":"human embryonic kidney 293T cells","subunits.UniProt.IDs.":"P49754;Q9UJC3","subunits.Entrez.IDs.":"27072;51361","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0016197","GO.description":"endosomal transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":18799622,"subunits.Protein.name.":"Vacuolar protein sorting-associated protein 41 homolog;Protein Hook homolog 1","subunits.Gene.name.":"VPS41;HOOK1","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"FTS and Hook proteins associate with class B and class C components of the HOPS complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6120,"ComplexName":"Hook2-Vps16 complex","Organism":"Human","Synonyms":"None","Cell.line":"human embryonic kidney 293T cells","subunits.UniProt.IDs.":"Q96ED9;Q9H269","subunits.Entrez.IDs.":"29911;64601","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0016197","GO.description":"endosomal transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":18799622,"subunits.Protein.name.":"Protein Hook homolog 2;Vacuolar protein sorting-associated protein 16 homolog","subunits.Gene.name.":"HOOK2;VPS16","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"FTS and Hook proteins associate with class B and class C components of the HOPS complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6121,"ComplexName":"Hook2-Vps41 complex","Organism":"Human","Synonyms":"None","Cell.line":"human embryonic kidney 293T cells","subunits.UniProt.IDs.":"P49754;Q96ED9","subunits.Entrez.IDs.":"27072;29911","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0016197","GO.description":"endosomal transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":18799622,"subunits.Protein.name.":"Vacuolar protein sorting-associated protein 41 homolog;Protein Hook homolog 2","subunits.Gene.name.":"VPS41;HOOK2","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"FTS and Hook proteins associate with class B and class C components of the HOPS complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6122,"ComplexName":"Hook3-Vps16 complex","Organism":"Human","Synonyms":"None","Cell.line":"human embryonic kidney 293T cells","subunits.UniProt.IDs.":"Q86VS8;Q9H269","subunits.Entrez.IDs.":"84376;64601","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0016197","GO.description":"endosomal transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":18799622,"subunits.Protein.name.":"Protein Hook homolog 3;Vacuolar protein sorting-associated protein 16 homolog","subunits.Gene.name.":"HOOK3;VPS16","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"FTS and Hook proteins associate with class B and class C components of the HOPS complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6123,"ComplexName":"Hook3-Vps41 complex","Organism":"Human","Synonyms":"None","Cell.line":"human embryonic kidney 293T cells","subunits.UniProt.IDs.":"P49754;Q86VS8","subunits.Entrez.IDs.":"27072;84376","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0016197","GO.description":"endosomal transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":18799622,"subunits.Protein.name.":"Vacuolar protein sorting-associated protein 41 homolog;Protein Hook homolog 3","subunits.Gene.name.":"VPS41;HOOK3","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"FTS and Hook proteins associate with class B and class C components of the HOPS complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6124,"ComplexName":"FTS-Vps16 complex","Organism":"Human","Synonyms":"None","Cell.line":"human embryonic kidney 293T cells","subunits.UniProt.IDs.":"Q9H269;Q9H8T0","subunits.Entrez.IDs.":"64601;64400","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0016197","GO.description":"endosomal transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":18799622,"subunits.Protein.name.":"Vacuolar protein sorting-associated protein 16 homolog;AKT-interacting protein","subunits.Gene.name.":"VPS16;AKTIP","subunits.Gene.name.syn.":"None;FTS","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"FTS and Hook proteins associate with class B and class C components of the HOPS complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6125,"ComplexName":"FTS-Vps18 complex","Organism":"Human","Synonyms":"None","Cell.line":"human embryonic kidney 293T cells","subunits.UniProt.IDs.":"Q9H8T0;Q9P253","subunits.Entrez.IDs.":"64400;57617","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0016197","GO.description":"endosomal transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":18799622,"subunits.Protein.name.":"AKT-interacting protein;Vacuolar protein sorting-associated protein 18 homolog","subunits.Gene.name.":"AKTIP;VPS18","subunits.Gene.name.syn.":"FTS;KIAA1475","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"FTS and Hook proteins associate with class B and class C components of the HOPS complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6126,"ComplexName":"FTS-Vps41 complex","Organism":"Human","Synonyms":"None","Cell.line":"human embryonic kidney 293T cells","subunits.UniProt.IDs.":"P49754;Q9H8T0","subunits.Entrez.IDs.":"27072;64400","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0016197","GO.description":"endosomal transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":18799622,"subunits.Protein.name.":"Vacuolar protein sorting-associated protein 41 homolog;AKT-interacting protein","subunits.Gene.name.":"VPS41;AKTIP","subunits.Gene.name.syn.":"None;FTS","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"FTS and Hook proteins associate with class B and class C components of the HOPS complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6127,"ComplexName":"DAXX-MDM2-USP7 complex","Organism":"Human","Synonyms":"None","Cell.line":"HCT116 cells","subunits.UniProt.IDs.":"Q00987;Q93009;Q9UER7","subunits.Entrez.IDs.":"4193;7874;1616","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0042769;GO:0061136;GO:0005654","GO.description":"DNA damage response, detection of DNA damage;regulation of proteasomal protein catabolic process;nucleoplasm","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":16845383,"subunits.Protein.name.":"E3 ubiquitin-protein ligase Mdm2 ;Ubiquitin carboxyl-terminal hydrolase 7 ;Death domain-associated protein 6","subunits.Gene.name.":"MDM2;USP7;DAXX","subunits.Gene.name.syn.":";HAUSP;BING2 DAP6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6128,"ComplexName":"DCN-MFAP2-ELN complex","Organism":"Bovine","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04985;P21793;P27424","subunits.Entrez.IDs.":"None;280760;281912","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0048251","GO.description":"elastic fiber assembly","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":11723132,"subunits.Protein.name.":"Elastin ;Decorin ;Microfibrillar-associated protein 2","subunits.Gene.name.":"ELN;DCN;MFAP2","subunits.Gene.name.syn.":";;MAGP MAGP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":6129,"ComplexName":"CBP80/20- dependent translation complex","Organism":"Human","Synonyms":"CT initiation complex","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O43310;P38919;P52298;P55884;Q09161;Q9BZI7","subunits.Entrez.IDs.":"9811;9775;22916;8662;4686;65109","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":19648179,"subunits.Protein.name.":"CBP80/20-dependent translation initiation factor;Eukaryotic initiation factor 4A-III;Nuclear cap-binding protein subunit 2;Eukaryotic translation initiation factor 3 subunit B;Nuclear cap-binding protein subunit 1;Regulator of nonsense transcripts 3B","subunits.Gene.name.":"CTIF;EIF4A3;NCBP2;EIF3B;NCBP1;UPF3B","subunits.Gene.name.syn.":"KIAA0427;DDX48, KIAA0111;CBP20;EIF3S9;CBP80 NCBP;RENT3B, UPF3X","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"CTIF interacts directly via its MIF4G domain with CBP80, is part of the CBP80/20-dependent translation initiation complex, and is complexed with eIF3 and eIF4AIII. Endogenous CBP80, eIF3b, and NMD factor Upf3X copurified with endogenous CTIF. Depletion of endogenous CTIF from an in vitro translation system selectively blocks the translation of CBP80-bound mRNAs, while addition of purified CTIF restores it.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6130,"ComplexName":"Dynactin","Organism":"Bovine","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"A4FUA8;A4IFE3;A5PKJ3;E1BBI8;P60712;P79136;Q0P5A1;Q148G7;Q3MHY9;Q3ZBD2;Q3ZC02;Q3ZCF0;Q5E997","subunits.Entrez.IDs.":"534656;100125305;511045;613489;280979;338052;514327;513751;None;511083;506441;527201;493728","Protein.complex.purification.method":"MI:0226- ion exchange chromatography;MI:0027- cosedimentation","GO.ID":"GO:0045502;GO:0051329;GO:0051640;GO:0070631","GO.description":"dynein binding;mitotic interphase;organelle localization;spindle pole body localization","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23455152,"subunits.Protein.name.":"F-actin-capping protein subunit alpha-1 ;Beta-centractin ;DCTN1 protein;Uncharacterized protein;Actin, cytoplasmic 1 ;F-actin-capping protein subunit beta ;Dynactin subunit 3;Dynactin subunit 6;ACTR1A protein ;Actin-related protein 10;DCTN5 protein;Dynactin subunit 2;F-actin-capping protein subunit alpha-2","subunits.Gene.name.":"CAPZA1;ACTR1B;DCTN1;DCTN4;ACTB;CAPZB;DCTN3;DCTN6;ACTR1A;ACTR10;DCTN5;DCTN2;CAPZA2","subunits.Gene.name.syn.":";;;;;;;;;;;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":6131,"ComplexName":"SELK multiprotein complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK-293 cells","subunits.UniProt.IDs.":"P04843;P04844;P27824;P39656;P46977;P55072;Q9BQE4;Q9BUN8;Q9GZP9;Q9Y6D0","subunits.Entrez.IDs.":"6184;6185;821;1650;3703;7415;55829;79139;51009;58515","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0030968;GO:0036503","GO.description":"endoplasmic reticulum unfolded protein response;ERAD pathway","FunCat.ID":"32.01.07","FunCat.description":"unfolded protein response (e.g. ER quality control)","PubMed.ID":22016385,"subunits.Protein.name.":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 ;Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2 ;Calnexin ;Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit ;Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A ;Transitional endoplasmic reticulum ATPase;Selenoprotein S ;Derlin-1 ;Derlin-2 ;Selenoprotein K","subunits.Gene.name.":"RPN1;RPN2;CANX;DDOST;STT3A;VCP;VIMP;DERL1;DERL2;SELK","subunits.Gene.name.syn.":";;;KIAA0115 OST48;ITM1 TMC;None;SELS;DER1;DER2 FLANA;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6132,"ComplexName":"MINOS complex","Organism":"Human","Synonyms":"IMMT-MINOS1-CHCHD3  complex","Cell.line":"primary fibroblast cells","subunits.UniProt.IDs.":"Q16891;Q5TGZ0;Q9NX63","subunits.Entrez.IDs.":"10989;440574;54927","Protein.complex.purification.method":"MI:0416- fluorescence microscopy;MI:0040- electron microscopy","GO.ID":"GO:0007007","GO.description":"inner mitochondrial membrane organization","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23676277,"subunits.Protein.name.":"MICOS complex subunit MIC60 ;MICOS complex subunit MIC10 ;MICOS complex subunit MIC19","subunits.Gene.name.":"IMMT;MINOS1;CHCHD3","subunits.Gene.name.syn.":"HMP MIC60 MINOS2;C1orf151 MIC10;MIC19 MINOS3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6133,"ComplexName":"RFX5-RFXANK-RFXAP complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00287;O14593;P48382","subunits.Entrez.IDs.":"5994;8625;5993","Protein.complex.purification.method":"MI:0114- x-ray crystallography;MI:0030- cross-linking studies","GO.ID":"GO:0003700","GO.description":"transcription factor activity, sequence-specific DNA binding","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20637319,"subunits.Protein.name.":"Regulatory factor X-associated protein ;DNA-binding protein RFXANK ;DNA-binding protein RFX5","subunits.Gene.name.":"RFXAP;RFXANK;RFX5","subunits.Gene.name.syn.":";ANKRA1 RFXB;","Disease.comment":"OMIM:209920 Bare lymphocyte syndrome, type II (PMID:10417269)","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6134,"ComplexName":"Rs1 homooctamer complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK-293 cells","subunits.UniProt.IDs.":"O15537","subunits.Entrez.IDs.":"6247","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0007601;GO:0010842;GO:0016062;GO:0007155","GO.description":"visual perception;retina layer formation;adaptation of rhodopsin mediated signaling;cell adhesion","FunCat.ID":"34.11.01.03;34.07","FunCat.description":"visual transduction;cell adhesion","PubMed.ID":15644328,"subunits.Protein.name.":"Retinoschisin","subunits.Gene.name.":"RS1","subunits.Gene.name.syn.":"XLRS1","Disease.comment":"OMIM:312700 Retinoschisis (PMID:15644328).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":6135,"ComplexName":"Ferritin complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P02792;P02794","subunits.Entrez.IDs.":"2512;2495","Protein.complex.purification.method":"MI:0428- imaging techniques","GO.ID":"GO:0006879;GO:0006955;GO:0006826","GO.description":"cellular iron ion homeostasis;immune response;iron ion transport","FunCat.ID":"36.25.16","FunCat.description":"immune response","PubMed.ID":8695634,"subunits.Protein.name.":"Ferritin light chain ;Ferritin heavy chain","subunits.Gene.name.":"FTL;FTH1","subunits.Gene.name.syn.":";FTH FTHL6","Disease.comment":"None","Subunits.comment":"OMIM:615604  L-ferritin deficiency, OMIM:615517 Hemochromatosis, type 5 (PMID:8695634),","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6136,"ComplexName":"USP7-MAGEL2-TRIM27 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P14373;Q93009;Q9UJ55","subunits.Entrez.IDs.":"5987;7874;54551","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0016197","GO.description":"endosomal transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26365382,"subunits.Protein.name.":"Zinc finger protein RFP ;Ubiquitin carboxyl-terminal hydrolase 7 ;MAGE-like protein 2","subunits.Gene.name.":"TRIM27;USP7;MAGEL2","subunits.Gene.name.syn.":"RFP RNF76;HAUSP;NDNL1","Disease.comment":"None","Subunits.comment":"OMIM:209850 Autism (PMID:26365382).","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6137,"ComplexName":"GM-CSF receptor complex","Organism":"Human","Synonyms":"None","Cell.line":"erythroleukemic TF-1 cell line","subunits.UniProt.IDs.":"P04141;P15509;P32927","subunits.Entrez.IDs.":"1437;1438;1439","Protein.complex.purification.method":"MI:0114-x-ray crystallography","GO.ID":"GO:0038158;GO:0004896","GO.description":"granulocyte colony-stimulating factor signaling pathway;cytokine receptor activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":18692472,"subunits.Protein.name.":"Granulocyte-macrophage colony-stimulating factor;Granulocyte-macrophage colony-stimulating factor receptor subunit alpha;Cytokine receptor common subunit beta","subunits.Gene.name.":"CSF2;CSF2RA;CSF2RB","subunits.Gene.name.syn.":"GMCSF;CSF2R, CSF2RY;IL3RB, IL5RB","Disease.comment":"Abnormalities in GM-CSF production or receptor function have been implicated in multiple pathologies such as rheumatoid arthritis (Cook et al., 2001), juvenile myelomonocytic leukemia (Birnbaum et al., 2000), chronic myelomonocytic leukemia (Ramshaw et al., 2002), and alveolar proteinosis (Dirksen et al., 1998). Furthermore, the GM-CSF receptor may also be important in the pathogenesis of chronic myeloid leukemia and myeloproliferative diseases by propagating survival and proliferation signalspromoted by the abnormal expression of Bcr-Abl and JAK2 mutations, respectively (PMID:18692472).","Subunits.comment":"None","Complex.comment":"Granulocyte-macrophage colony-stimulating factor (GM-CSF) is a pleiotropic cytokine that controls the production and function of blood cells. It is deregulated in clinical conditions such as rheumatoid arthritis and leukemia. Its receptors are heterodimers consisting of a ligand-specific alpha subunit and a beta subunit that is shared with the interleukin (IL)-3 and IL-5 receptors. JAK2 activation is a feature of GM-CSF receptor activation and plays a critical  role in GM-CSF signaling. The structure of the GM-CSF receptor complex reveals a hexameric 2:2:2 assembly, consisting of two beta chains, two GMR alpha chains, and two GM-CSF molecules. The crystal lattice generates an unexpected dodecamer complex, an assembly consisting of two hexameric complexes related by a crystallographic two-fold axis. The dodecamer assembles in a head-to-head orientation. Functional studies reveal that dodecamer formation is required for receptor activation and signaling. This differs from the 2:1:1 stoichiometry  (2 betac,1 GMRalpha,1 GM-CSF) (McClure et al., 2003). This is likely to be a result of differences in the total protein concentration at which the complex is formed as we observe a protein concentration-dependent shift in molecular  weight and hence stoichiometry of GM-CSF receptor complex. The 2:1:1 complex probably represents a relatively stable intermediate in the assembly of higher-order 2:2:2 GM-CSFreceptor complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6138,"ComplexName":"STEAP1-STEAP2 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"B6A7P8;Q8NFT2","subunits.Entrez.IDs.":"100328630;261729","Protein.complex.purification.method":"MI:0400- affinity technologies;MI:0027- cosedimentation","GO.ID":"GO:0006897;GO:0055072","GO.description":"endocytosis;iron ion homeostasis","FunCat.ID":"20.09.18.09.01","FunCat.description":"endocytosis","PubMed.ID":27792302,"subunits.Protein.name.":"Six transmembrane epithelial antigen of the prostate 1 ;Metalloreductase STEAP2","subunits.Gene.name.":"STEAP1;STEAP2","subunits.Gene.name.syn.":";PCANAP1 STAMP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Oryctolagus cuniculus (Rabbit);Homo sapiens (Human)"}
{"ComplexID":6139,"ComplexName":"STEAP1 homotrimer complex","Organism":"Rabbit","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"B6A7P8","subunits.Entrez.IDs.":"100328630","Protein.complex.purification.method":"MI:0027- cosedimentation;MI:0091- chromatography technologies","GO.ID":"GO:0055072;GO:0006897","GO.description":"iron ion homeostasis;endocytosis","FunCat.ID":"20.09.18.09.01","FunCat.description":"endocytosis","PubMed.ID":27792302,"subunits.Protein.name.":"Six transmembrane epithelial antigen of the prostate 1","subunits.Gene.name.":"STEAP1","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"OMIM:601518 Prostate cancer (PMID:27792302).","Complex.comment":"None","SWISSPROT.organism":"Oryctolagus cuniculus (Rabbit)"}
{"ComplexID":6140,"ComplexName":"Cdt1-Geminin complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75496;Q9H211","subunits.Entrez.IDs.":"51053;81620","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0006275","GO.description":"regulation of DNA replication","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":19906994,"subunits.Protein.name.":"Geminin;DNA replication factor Cdt1","subunits.Gene.name.":"GMNN;CDT1","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6141,"ComplexName":"Importin alpha-CAS-RanGTP complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P52292;P55060;P62826","subunits.Entrez.IDs.":"3838;1434;5901","Protein.complex.purification.method":"MI:0051-fluorescence technologies;MI:0413-electrophoretic mobility shift assay","GO.ID":"GO:0006913;GO:0005634;GO:0015031;GO:0005737;GO:0006611;GO:0055085","GO.description":"nucleocytoplasmic transport;nucleus;protein transport;cytoplasm;protein export from nucleus;transmembrane transport","FunCat.ID":"70.10;20.01.10;70.03","FunCat.description":"nucleus;protein transport;cytoplasm","PubMed.ID":9323134,"subunits.Protein.name.":"Importin subunit alpha-1;Exportin-2;GTP-binding nuclear protein Ran","subunits.Gene.name.":"KPNA2;CSE1L;RAN","subunits.Gene.name.syn.":"RCH1, SRP1;CAS XPO2;ARA24","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"NLS proteins are transported into the nucleus by the importin alpha/beta heterodimer. Importin alpha binds the NLS, while importin beta mediates translocation through the nuclear pore complex. After translocation, RanGTP, whose predicted concentration is high in the nucleus and low in the cytoplasm, binds importin beta and displaces importin alpha. Importin alpha must then be returned to the cytoplasm, leaving the NLS protein behind. CAS protein mediates importin alpha re-export. CAS binds strongly to importin alpha only in the presence of RanGTP, forming an importin alpha/CAS/RanGTP complex. Importin alpha is released from this complex in the cytoplasm by the combined action of RanBP1 and RanGAP1. CAS binds preferentially to NLS-free importin alpha, hereby leaving import substrates back in the nucleus. CAS binding to importin alpha depends on RanGTP. It was shown that without further addition or with addition of wild-type RanGDP, importin beta bound efficiently to importin alpha, but CAS only weakly. The opposite pattern was observed when the permanently GTP-bound Ran mutants were added: importin beta binding was completely abolished, whereas the CAS binding to importin alpha was greatly enhanced. This suggested that the CAS/RanGTP complex is the high affinity form for importin alpha binding.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6142,"ComplexName":"KPNA2-KPNB1 complex","Organism":"Human","Synonyms":"Importin alpha/beta complex","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"P52292;Q14974","subunits.Entrez.IDs.":"3838;3837","Protein.complex.purification.method":"MI:0051-fluorescence technologies;MI:0413-electrophoretic mobility shift assay","GO.ID":"GO:0006913;GO:0005634;GO:0005737;GO:0015031;GO:0000060;GO:0055085","GO.description":"nucleocytoplasmic transport;nucleus;cytoplasm;protein transport;protein import into nucleus, translocation;transmembrane transport","FunCat.ID":"70.10;70.03;20.01.10","FunCat.description":"nucleus;cytoplasm;protein transport","PubMed.ID":9323134,"subunits.Protein.name.":"Importin subunit alpha-1;Importin subunit beta-1","subunits.Gene.name.":"KPNA2;KPNB1","subunits.Gene.name.syn.":"RCH1, SRP1;NTF97","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"NLS proteins are transported into the nucleus by the importin alpha/beta heterodimer. Importin alpha binds the NLS, while importin beta mediates translocation through the nuclear pore complex. It was shown that without further addition or with addition of wild-type RanGDP, importin beta bound efficiently to importin alpha.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6143,"ComplexName":"KPNB1-RAN complex","Organism":"Human","Synonyms":"Importin beta-RanGTP complex","Cell.line":"None","subunits.UniProt.IDs.":"P62826;Q14974","subunits.Entrez.IDs.":"5901;3837","Protein.complex.purification.method":"MI:0051-fluorescence technologies;MI:0413-electrophoretic mobility shift assay","GO.ID":"GO:0006913;GO:0006611;GO:0005634;GO:0005737;GO:0055085","GO.description":"nucleocytoplasmic transport;protein export from nucleus;nucleus;cytoplasm;transmembrane transport","FunCat.ID":"70.10;70.03","FunCat.description":"nucleus;cytoplasm","PubMed.ID":9323134,"subunits.Protein.name.":"GTP-binding nuclear protein Ran;Importin subunit beta-1","subunits.Gene.name.":"RAN;KPNB1","subunits.Gene.name.syn.":"ARA24;NTF97","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"NLS proteins are transported into the nucleus by the importin alpha/beta heterodimer. Importin alpha binds the NLS, while importin beta mediates translocation through the nuclear pore complex. After translocation, RanGTP, whose predicted concentration is high in the nucleus and low in the cytoplasm, binds importin beta disassembling the importin alpha/beta heterodimer.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6144,"ComplexName":"CENP-T-W complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q5EE01;Q96BT3","subunits.Entrez.IDs.":"387103;80152","Protein.complex.purification.method":"MI:0071-molecular sieving","GO.ID":"GO:0007059;GO:0003677;GO:0051382","GO.description":"chromosome segregation;DNA binding;kinetochore assembly","FunCat.ID":"10.03.04.05;16.03.01;10.03.04.01","FunCat.description":"chromosome segregation/division;DNA binding;centromere/kinetochore complex maturation","PubMed.ID":22304917,"subunits.Protein.name.":"Centromere protein W;Centromere protein T","subunits.Gene.name.":"CENPW;CENPT","subunits.Gene.name.syn.":"C6orf173, CUG2;C16orf56, ICEN22","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6145,"ComplexName":"CENP-S-X complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"A8MT69;Q8N2Z9","subunits.Entrez.IDs.":"201254;378708","Protein.complex.purification.method":"MI:0071-molecular sieving","GO.ID":"GO:0007059;GO:0003677;GO:0051382","GO.description":"chromosome segregation;DNA binding;kinetochore assembly","FunCat.ID":"10.03.04.05;16.03.01;10.03.04.01","FunCat.description":"chromosome segregation/division;DNA binding;centromere/kinetochore complex maturation","PubMed.ID":22304917,"subunits.Protein.name.":"Centromere protein X;Centromere protein S","subunits.Gene.name.":"STRA13;APITD1","subunits.Gene.name.syn.":"CENPX, FAAP10, MHF2;CENPS, FAAP16, MHF1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6146,"ComplexName":"CENP-T-W-S-X heterotetramer complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"A8MT69;Q5EE01;Q8N2Z9;Q96BT3","subunits.Entrez.IDs.":"201254;387103;378708;80152","Protein.complex.purification.method":"MI:0071-molecular sieving","GO.ID":"GO:0051382;GO:0003677;GO:0007059","GO.description":"kinetochore assembly;DNA binding;chromosome segregation","FunCat.ID":"10.03.04.01;16.03.01;10.03.04.05","FunCat.description":"centromere/kinetochore complex maturation;DNA binding;chromosome segregation/division","PubMed.ID":22304917,"subunits.Protein.name.":"Centromere protein X;Centromere protein W;Centromere protein S;Centromere protein T","subunits.Gene.name.":"STRA13;CENPW;APITD1;CENPT","subunits.Gene.name.syn.":"CENPX, FAAP10, MHF2;C6orf173, CUG2;CENPS, FAAP16, MHF1;C16orf56, ICEN22","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6147,"ComplexName":"BAFL-BAF-LAP2beta complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75531;P42167;Q9H503","subunits.Entrez.IDs.":"8815;7112;140836","Protein.complex.purification.method":"MI:0096-pull down;MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":16337940,"subunits.Protein.name.":"Barrier-to-autointegration factor;Lamina-associated polypeptide 2, isoforms beta/gamma;Barrier-to-autointegration factor-like protein","subunits.Gene.name.":"BANF1;TMPO;BANF2","subunits.Gene.name.syn.":"BAF, BCRG1;LAP2;BAFL, C20orf179","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"BAF-L forms ternary complexes in vitro with BAF and LAP2beta through heterodimerization with BAF.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6148,"ComplexName":"BAFL-BAF complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75531;Q9H503","subunits.Entrez.IDs.":"8815;140836","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":16337940,"subunits.Protein.name.":"Barrier-to-autointegration factor;Barrier-to-autointegration factor-like protein","subunits.Gene.name.":"BANF1;BANF2","subunits.Gene.name.syn.":"BAF, BCRG1;BAFL, C20orf179","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"BAF-L regulates BAF function via heterodimerization and might thereby influence tissue-specific roles of BAF.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6149,"ComplexName":"Codanin-1-Asf1\\u2013histone H3.1-histone H4\\u2013importin-4 complex,  cytosolic","Organism":"Human","Synonyms":"None","Cell.line":"HeLa S3 cells","subunits.UniProt.IDs.":"P62805;P68431;Q8IWY9;Q8TEX9;Q9Y294","subunits.Entrez.IDs.":"None;None;146059;79711;25842","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0071-molecular sieving","GO.ID":"GO:0031497;GO:0006260","GO.description":"chromatin assembly;DNA replication","FunCat.ID":"10.01.03","FunCat.description":"DNA synthesis and replication","PubMed.ID":22407294,"subunits.Protein.name.":"Histone H4;Histone H3.1;Codanin-1;Importin-4;Histone chaperone ASF1A","subunits.Gene.name.":"HIST1H4A;;HIST1H3A;;CDAN1;IPO4;ASF1A","subunits.Gene.name.syn.":"H4/A H4FA; H4/I H4FI; H4/G H4FG; H4/B H4FB; H4/J H4FJ; H4/C H4FC; H4/H H4FH; H4/M H4FM; H4/E H4FE; H;H3FA; H3FL; H3FC; H3FB; H3FD; H3FI; H3FH; H3FK; H3FF; H3FJ;None;IMP4B, RANBP4;None","Disease.comment":"Mutations in Codanin-1 can cause congenital dyserythropoietic anaemia type I (CDAI), characterized by chromatin abnormalities in bone marrow erythroblasts.","Subunits.comment":"Codanin-1 seems to guard a limiting step in chromatin replication.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6152,"ComplexName":"I-kappa-B kinase complex","Organism":"Human","Synonyms":"IKK complex","Cell.line":"HeLa cell","subunits.UniProt.IDs.":"O15111;Q9Y6K9","subunits.Entrez.IDs.":"1147;8517","Protein.complex.purification.method":"MI:0096-pull down","GO.ID":"GO:0007249","GO.description":"I-kappaB kinase/NF-kappaB signaling","FunCat.ID":"30.01.05.01.04","FunCat.description":"NIK-I-kappaB/NF-kappaB cascade","PubMed.ID":11057907,"subunits.Protein.name.":"Inhibitor of nuclear factor kappa-B kinase subunit alpha;NF-kappa-B essential modulator","subunits.Gene.name.":"CHUK;IKBKG","subunits.Gene.name.syn.":"IKKA, TCF16;FIP3, NEMO","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The complex can be activated directly by MEKK1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6153,"ComplexName":"PRKAA2-PRKAB2-PRKAG3 complex","Organism":"Human","Synonyms":"AMPK alpha2-beta2-gamma3 complex","Cell.line":"skeletal muscle cells","subunits.UniProt.IDs.":"O43741;P54646;Q9UGI9","subunits.Entrez.IDs.":"5565;5563;53632","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0004679;GO:0043501","GO.description":"AMP-activated protein kinase activity;skeletal muscle adaptation","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":17038425,"subunits.Protein.name.":"5'-AMP-activated protein kinase subunit beta-2 ;5'-AMP-activated protein kinase catalytic subunit alpha-2 ;5'-AMP-activated protein kinase subunit gamma-3","subunits.Gene.name.":"PRKAB2;PRKAA2;PRKAG3","subunits.Gene.name.syn.":";AMPK AMPK2;AMPKG3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6154,"ComplexName":"PRKAA1-PRKAB2-PRKAG1 complex","Organism":"Human","Synonyms":"AMPK alpha1-beta2-gamma1 complex, skeletal muscle","Cell.line":"skeletal muscle cells","subunits.UniProt.IDs.":"O43741;P54619;Q13131","subunits.Entrez.IDs.":"5565;5571;5562","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0004679","GO.description":"AMP-activated protein kinase activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":17038425,"subunits.Protein.name.":"5'-AMP-activated protein kinase subunit beta-2 ;5'-AMP-activated protein kinase subunit gamma-1 ;5'-AMP-activated protein kinase catalytic subunit alpha-1","subunits.Gene.name.":"PRKAB2;PRKAG1;PRKAA1","subunits.Gene.name.syn.":";;AMPK1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6155,"ComplexName":"PRKAA2-PRKAB2-PRKAG1 complex","Organism":"Human","Synonyms":"AMPK alpha2-beta2-gamma1 complex, skeletal muscle","Cell.line":"skeletal muscle cells","subunits.UniProt.IDs.":"O43741;P54619;P54646","subunits.Entrez.IDs.":"5565;5571;5563","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0004679;GO:0043501","GO.description":"AMP-activated protein kinase activity;skeletal muscle adaptation","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":17038425,"subunits.Protein.name.":"5'-AMP-activated protein kinase subunit beta-2 ;5'-AMP-activated protein kinase subunit gamma-1 ;5'-AMP-activated protein kinase catalytic subunit alpha-2","subunits.Gene.name.":"PRKAB2;PRKAG1;PRKAA2","subunits.Gene.name.syn.":";;AMPK AMPK2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6157,"ComplexName":"GNAI1-Gnb1-Gng2 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P54311;P63096;P63212","subunits.Entrez.IDs.":"24400;2770;281203","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0114- x-ray crystallography","GO.ID":"GO:0007186","GO.description":"G-protein coupled receptor signaling pathway","FunCat.ID":"30.05.02.24","FunCat.description":"G-protein coupled receptor signalling pathway","PubMed.ID":27498775,"subunits.Protein.name.":"Guanine nucleotide-binding protein G;Guanine nucleotide-binding protein G;Guanine nucleotide-binding protein G","subunits.Gene.name.":"Gnb1;GNAI1;GNG2","subunits.Gene.name.syn.":";;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Homo sapiens (Human);Bos taurus (Bovine)"}
{"ComplexID":6158,"ComplexName":"TRIAL-DR5 complex","Organism":"Human","Synonyms":"TNFSF10-TNFRSF10B complex","Cell.line":"MCF-10A cells","subunits.UniProt.IDs.":"O14763;P50591","subunits.Entrez.IDs.":"8795;8743","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006915","GO.description":"apoptotic process","FunCat.ID":"40.10.02","FunCat.description":"apoptosis (type I programmed cell death)","PubMed.ID":27542249,"subunits.Protein.name.":"Tumor necrosis factor receptor superfamily member 10B ;Tumor necrosis factor ligand superfamily member 10","subunits.Gene.name.":"TNFRSF10B;TNFSF10","subunits.Gene.name.syn.":"DR5 KILLER TRAILR2 TRICK2 ZTNFR9;APO2L TRAIL","Disease.comment":"OMIM: 114480 Breast cancer","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6159,"ComplexName":"LPP-PPP2CA-PPP2R3A complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P67775;Q93052;Q9Z176","subunits.Entrez.IDs.":"5515;4026;None","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0018- two hybrid","GO.ID":"GO:0005925","GO.description":"focal adhesion","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26945059,"subunits.Protein.name.":"Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform;Lipoma-preferred partner ;Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit delta","subunits.Gene.name.":"PPP2CA;LPP;Ppp2r3d","subunits.Gene.name.syn.":"None;;Ppp2r3a Ppp2r6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Mus musculus (Mouse)"}
{"ComplexID":6160,"ComplexName":"hTREX84 complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cell line","subunits.UniProt.IDs.":"Q13769;Q6I9Y2;Q86W42;Q8NI27;Q96FV9;Q96J01","subunits.Entrez.IDs.":"8563;80145;79228;57187;9984;84321","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0006406","GO.description":"mRNA export from nucleus","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":15833825,"subunits.Protein.name.":"THO complex subunit 5 homolog;THO complex subunit 7 homolog;THO complex subunit 6 homolog;THO complex subunit 2;THO complex subunit 1;THO complex subunit 3","subunits.Gene.name.":"THOC5;THOC7;THOC6;THOC2;THOC1;THOC3","subunits.Gene.name.syn.":"C22orf19, KIAA0983;NIF3L1BP1;WDR58;CXorf3;HPR1;None","Disease.comment":"hTREX84 is highly expressed in aggressive forms of breast cancer.","Subunits.comment":"The 40K protein has been described as hTREX40. hTREX40 is described as isoform 2 of THOC6 (Q86W42).","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6163,"ComplexName":"BBSome","Organism":"Human","Synonyms":"None","Cell.line":"HEK-293T cells","subunits.UniProt.IDs.":"A8MTZ0;Q3SYG4;Q8IWZ6;Q8N3I7;Q8NFJ9;Q8TAM2;Q96RK4;Q9BXC9","subunits.Entrez.IDs.":"92482;27241;55212;129880;582;123016;585;583","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0416- fluorescence microscopy","GO.ID":"GO:0044782;GO:0042073;GO:0005929","GO.description":"cilium organization;intraciliary transport;cilium","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25964651,"subunits.Protein.name.":"BBSome-interacting protein 1;Protein PTHB1;Bardet-Biedl syndrome 7 protein;Bardet-Biedl syndrome 5 protein;Bardet-Biedl syndrome 1 protein;Tetratricopeptide repeat protein 8;Bardet-Biedl syndrome 4 protein;Bardet-Biedl syndrome 2 protein","subunits.Gene.name.":"BBIP1;BBS9;BBS7;BBS5;BBS1;TTC8;BBS4;BBS2","subunits.Gene.name.syn.":"BBIP10, NCRNA00081;PTHB1;BBS2L1;None;BBS2L2;BBS8;None;None","Disease.comment":"All the BBS proteins were identified by mutations of their respective genes in patients with Bardet\\u2013Biedl syndrome (BBS), a genetically heterogeneous disease (ciliopathy) characterized by a wide spectrum of clinical features, including rod\\u2013cone dystrophy, morbid obesity, polydactyly, genital anomalies, learning difficulties, and renal anomalies.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6164,"ComplexName":"ACK1 signaling complex","Organism":"Human","Synonyms":"CDC42-ACK1-p130Cas-CRK collagen-regulated signaling complex","Cell.line":"T47D cells","subunits.UniProt.IDs.":"P46108;P56945;P60953;Q07912","subunits.Entrez.IDs.":"1398;9564;998;10188","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0023052","GO.description":"signaling","FunCat.ID":"30.01","FunCat.description":"cellular signalling","PubMed.ID":17038317,"subunits.Protein.name.":"Adapter molecule crk;Breast cancer anti-estrogen resistance protein 1;Cell division control protein 42 homolog;Activated CDC42 kinase 1","subunits.Gene.name.":"CRK;BCAR1;CDC42;TNK2","subunits.Gene.name.syn.":"None;CAS CASS1 CRKAS;None;ACK1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"CDC42, ACK1, p130Cas, and CRK form a collagen-regulated signaling complex. The interaction of Ack1 and p130Cas relies on SH3 and Proline-rich domains. ACK1 not only associated with p130Casbut also induced its phosphorylation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6165,"ComplexName":"BBSome core complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK-293T cells","subunits.UniProt.IDs.":"Q3SYG4;Q8IWZ6;Q8NFJ9;Q9BXC9","subunits.Entrez.IDs.":"27241;55212;582;583","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0416-fluorescence microscopy","GO.ID":"GO:0005929","GO.description":"cilium","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25964651,"subunits.Protein.name.":"Protein PTHB1;Bardet-Biedl syndrome 7 protein;Bardet-Biedl syndrome 1 protein;Bardet-Biedl syndrome 2 protein","subunits.Gene.name.":"BBS9;BBS7;BBS1;BBS2","subunits.Gene.name.syn.":"PTHB1;BBS2L1;BBS2L2;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6166,"ComplexName":"BBSome linker complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK-293T cells","subunits.UniProt.IDs.":"A8MTZ0;Q8TAM2;Q96RK4","subunits.Entrez.IDs.":"92482;123016;585","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0416-fluorescence microscopy","GO.ID":"GO:0005929","GO.description":"cilium","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25964651,"subunits.Protein.name.":"BBSome-interacting protein 1;Tetratricopeptide repeat protein 8;Bardet-Biedl syndrome 4 protein","subunits.Gene.name.":"BBIP1;TTC8;BBS4","subunits.Gene.name.syn.":"BBIP10, NCRNA00081;BBS8;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6167,"ComplexName":"Exocyst complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK-293T cells","subunits.UniProt.IDs.":"O00471;O60645;Q8IYI6;Q8TAG9;Q96A65;Q96KP1;Q9NV70;Q9UPT5","subunits.Entrez.IDs.":"10640;11336;149371;54536;60412;55770;55763;23265","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0416-fluorescence microscopy","GO.ID":"GO:0099022;GO:0006887","GO.description":"vesicle tethering;exocytosis","FunCat.ID":"20.09.16.09.03","FunCat.description":"exocytosis","PubMed.ID":25964651,"subunits.Protein.name.":"Exocyst complex component 5;Exocyst complex component 3;Exocyst complex component 8;Exocyst complex component 6;Exocyst complex component 4;Exocyst complex component 2;Exocyst complex component 1;Exocyst complex component 7","subunits.Gene.name.":"EXOC5;EXOC3;EXOC8;EXOC6;EXOC4;EXOC2;EXOC1;EXOC7","subunits.Gene.name.syn.":"SEC10 SEC10L1;SEC6 SEC6L1;None;SEC15A SEC15L SEC15L1;KIAA1699 SEC8 SEC8L1;SEC5 SEC5L1;SEC3 SEC3L1;EXO70 KIAA1067","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The exocyst complex regulates tethering of transferrin-receptor-containing recycling vesicles to the plasma membrane, downstream of the Rab11 small GTPase.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6168,"ComplexName":"Exocyst EXOC5-EXOC6 subcomplex","Organism":"Human","Synonyms":"Exocyst sec10-sec15 subcomplex","Cell.line":"HEK-293T cells","subunits.UniProt.IDs.":"O00471;Q8TAG9","subunits.Entrez.IDs.":"10640;54536","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0416-fluorescence microscopy","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25964651,"subunits.Protein.name.":"Exocyst complex component 5;Exocyst complex component 6","subunits.Gene.name.":"EXOC5;EXOC6","subunits.Gene.name.syn.":"SEC10 SEC10L1;SEC15A SEC15L SEC15L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6169,"ComplexName":"Exocyst EXOC5-EXOC6-EXOC7 subcomplex","Organism":"Human","Synonyms":"Exocyst sec10-sec15-exo70  subcomplex","Cell.line":"HEK-293T cells","subunits.UniProt.IDs.":"O00471;Q8TAG9;Q9UPT5","subunits.Entrez.IDs.":"10640;54536;23265","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0416-fluorescence microscopy","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25964651,"subunits.Protein.name.":"Exocyst complex component 5;Exocyst complex component 6;Exocyst complex component 7","subunits.Gene.name.":"EXOC5;EXOC6;EXOC7","subunits.Gene.name.syn.":"SEC10 SEC10L1;SEC15A SEC15L SEC15L1;EXO70 KIAA1067","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6170,"ComplexName":"Angiogenin-PRI complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P03950;P13489","subunits.Entrez.IDs.":"283;6050","Protein.complex.purification.method":"MI:0226-ion exchange chromatography","GO.ID":"GO:0045765","GO.description":"regulation of angiogenesis","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":3470787,"subunits.Protein.name.":"Angiogenin;Ribonuclease inhibitor","subunits.Gene.name.":"ANG;RNH1","subunits.Gene.name.syn.":"RNASE5;PRI, RNH","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6171,"ComplexName":"STRIPAK complex","Organism":"Human","Synonyms":"Striatin-interacting phosphatase and kinase complex; PP2A-\\u0002striatin-\\u0002Mob3-\\u0002STRIP complex","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O43815;P30153;P67775;Q8C079;Q9Y3A3","subunits.Entrez.IDs.":"6801;5518;5515;229707;25843","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":18782753,"subunits.Protein.name.":"Striatin;Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform;Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform;Striatin-interacting protein 1;MOB-like protein phocein","subunits.Gene.name.":"STRN;PPP2R1A;PPP2CA;Strip1;MOB4","subunits.Gene.name.syn.":"None;None;None;Fam40a, Kiaa1761;MOB3, MOBKL3, PHOCN, PREI3","Disease.comment":"None","Subunits.comment":"Since the authors did not specify serine/threonine-protein phosphatase 2A catalytic subunit  we used the alpha isoform. Since the authors did not specify the striatin-interacting protein, we used the isoform Strip1","Complex.comment":"The data highlight a stable, core complex containing PP2A catalytic and scaffolding subunits, striatin(s), Mob3, and STRIP.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Mus musculus (Mouse);Homo sapiens (Human)"}
{"ComplexID":6172,"ComplexName":"Intraflagellar transport complex B","Organism":"Human","Synonyms":"IFT-B","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"A0AVF1;Q13099;Q8IY31;Q8N4P2;Q8R3P7;Q8TDR0;Q8WYA0;Q96LB3;Q9BW83;Q9H7X7;Q9NQC8;Q9NWB7;Q9P2H3;Q9UG01;Q9Y366;Q9Y547","subunits.Entrez.IDs.":"79989;8100;90410;150737;76779;26146;28981;80173;11020;64792;56912;55081;57560;26160;51098;51668","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0416-fluorescence microscopy","GO.ID":"GO:0042073;GO:0005929","GO.description":"intraciliary transport;cilium","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26980730,"subunits.Protein.name.":"Intraflagellar transport protein 56;Intraflagellar transport protein 88 homolog;Intraflagellar transport protein 20 homolog;Tetratricopeptide repeat protein 30B;Clusterin-associated protein 1;TRAF3-interacting protein 1;Intraflagellar transport protein 81 homolog;Intraflagellar transport protein 74 homolog;Intraflagellar transport protein 27 homolog;Intraflagellar transport protein 22 homolog;Intraflagellar transport protein 46 homolog;Intraflagellar transport protein 57 homolog;Intraflagellar transport protein 80 homolog;Intraflagellar transport protein 172 homolog;Intraflagellar transport protein 52 homolog;Intraflagellar transport protein 25 homolog","subunits.Gene.name.":"TTC26;IFT88;IFT20;TTC30B;Cluap1;TRAF3IP1;IFT81;IFT74;IFT27;IFT22;IFT46;IFT57;IFT80;IFT172;IFT52;HSPB11","subunits.Gene.name.syn.":"IFT56;TG737 TTC10;None;None;None;IFT54, MIPT3;CDV1;CCDC2 CMG1;RABL4 RAYL;RABL5;C11orf2 C11orf60;DERP8 ESRRBL1 HIPPI;KIAA1374 WDR56;KIAA1179;C20orf9 NGD5;C1orf41 IFT25","Disease.comment":"None","Subunits.comment":"All but one of the subunits we examined were of human origin, except mouse Cluap1.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Mus musculus (Mouse);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6173,"ComplexName":"Intraflagellar transport complex B core complex","Organism":"Human","Synonyms":"IFT-B core complex","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"A0AVF1;Q13099;Q8N4P2;Q8WYA0;Q96LB3;Q9BW83;Q9H7X7;Q9NQC8;Q9Y366;Q9Y547","subunits.Entrez.IDs.":"79989;8100;150737;28981;80173;11020;64792;56912;51098;51668","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0416-fluorescence microscopy","GO.ID":"GO:0005929;GO:0042073","GO.description":"cilium;intraciliary transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26980730,"subunits.Protein.name.":"Intraflagellar transport protein 56;Intraflagellar transport protein 88 homolog;Tetratricopeptide repeat protein 30B;Intraflagellar transport protein 81 homolog;Intraflagellar transport protein 74 homolog;Intraflagellar transport protein 27 homolog;Intraflagellar transport protein 22 homolog;Intraflagellar transport protein 46 homolog;Intraflagellar transport protein 52 homolog;Intraflagellar transport protein 25 homolog","subunits.Gene.name.":"TTC26;IFT88;TTC30B;IFT81;IFT74;IFT27;IFT22;IFT46;IFT52;HSPB11","subunits.Gene.name.syn.":"IFT56;TG737 TTC10;None;CDV1;CCDC2 CMG1;RABL4 RAYL;RABL5;C11orf2 C11orf60;C20orf9 NGD5;C1orf41 IFT25","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6174,"ComplexName":"Intraflagellar transport complex B peripheral subcomplex","Organism":"Human","Synonyms":"IFT-B peripheral subcomplex","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"Q8IY31;Q8R3P7;Q8TDR0;Q9NWB7;Q9P2H3;Q9UG01","subunits.Entrez.IDs.":"90410;76779;26146;55081;57560;26160","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0416-fluorescence microscopy","GO.ID":"GO:0005929","GO.description":"cilium","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26980730,"subunits.Protein.name.":"Intraflagellar transport protein 20 homolog;Clusterin-associated protein 1;TRAF3-interacting protein 1;Intraflagellar transport protein 57 homolog;Intraflagellar transport protein 80 homolog;Intraflagellar transport protein 172 homolog","subunits.Gene.name.":"IFT20;Cluap1;TRAF3IP1;IFT57;IFT80;IFT172","subunits.Gene.name.syn.":"None;None;IFT54, MIPT3;DERP8 ESRRBL1 HIPPI;KIAA1374 WDR56;KIAA1179","Disease.comment":"None","Subunits.comment":"All but one of the subunits we examined were of human origin, except mouse Cluap1.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Mus musculus (Mouse);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6175,"ComplexName":"Caspase-10-SUMO-FADD/Drp1 complex","Organism":"Human","Synonyms":"CASP10-FADD-DNM1L complex","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O00429;Q13158;Q92851","subunits.Entrez.IDs.":"10059;8772;843","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0070266;GO:0005739","GO.description":"necroptotic process;mitochondrion","FunCat.ID":"70.16","FunCat.description":"mitochondrion","PubMed.ID":27799292,"subunits.Protein.name.":"Dynamin-1-like protein ;FAS-associated death domain protein;Caspase-10","subunits.Gene.name.":"DNM1L;FADD;CASP10","subunits.Gene.name.syn.":"DLP1 DRP1;MORT1;MCH4","Disease.comment":"Disease: ischemic injury","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6176,"ComplexName":"CDCP1-Src-EGFR complex","Organism":"Human","Synonyms":"None","Cell.line":"MDA-MB-468 cells","subunits.UniProt.IDs.":"P00533;P12931;Q9H5V8","subunits.Entrez.IDs.":"1956;6714;64866","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0004- affinity chromatography technologies","GO.ID":"GO:0007173","GO.description":"epidermal growth factor receptor signaling pathway","FunCat.ID":"30.05.01.12.01","FunCat.description":"EGF-receptor signalling pathway","PubMed.ID":27495374,"subunits.Protein.name.":"Epidermal growth factor receptor;Proto-oncogene tyrosine-protein kinase Src;CUB domain-containing protein 1","subunits.Gene.name.":"EGFR;SRC;CDCP1","subunits.Gene.name.syn.":"ERBB, ERBB1, HER1;SRC1;TRASK","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6177,"ComplexName":"PPARgamma-pERK complex","Organism":"Mouse","Synonyms":"Pparg-Mapk1 complex","Cell.line":"hippocampal cells","subunits.UniProt.IDs.":"P37238;P63085","subunits.Entrez.IDs.":"19016;26413","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0035357;GO:0070372","GO.description":"peroxisome proliferator activated receptor signaling pathway;regulation of ERK1 and ERK2 cascade","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":24623782,"subunits.Protein.name.":"Peroxisome proliferator-activated receptor gamma ;Mitogen-activated protein kinase 1","subunits.Gene.name.":"Pparg;Mapk1","subunits.Gene.name.syn.":"Nr1c3;Erk2, Mapk, Prkm1","Disease.comment":"PPARgamma recruitment to active ERK during memory consolidation is required for Alzheimer disease-related cognitive enhancement.","Subunits.comment":"None","Complex.comment":"Coimmunoprecipitation of hippocampal extracts revealed that PPARgamma and activated, phosphorylated ERK (pERK) associated in Tg2576 in vivo, and that PPARgamma agonism facilitated recruitment of PPARgamma to pERK during memory consolidation. The amount of PPARgamma recruited to pERK correlated with the cognitive reserve in humans with AD and in Tg2576. The finding that PPARgamma association with pERK in vivo was increased in RSG-treated Tg2576 mice only during memory consolidation suggests a dynamic ligand-dependent (RSG) mechanism for recruitment of pERK and other signaling partners (e.g. MEK and p90RSK).","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6178,"ComplexName":"LUBAC complex","Organism":"Human","Synonyms":"SHARPIN-HOIL1L-HOIP complex;  Linear ubiquitin chain assembly complex; Ubiquitin ligase E3 LUBAC","Cell.line":"HEK293T, Jurkat","subunits.UniProt.IDs.":"Q96EP0;Q9BYM8;Q9H0F6","subunits.Entrez.IDs.":"55072;10616;81858","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0071-molecular sieving","GO.ID":"GO:0070534;GO:0007249;GO:0045087","GO.description":"protein K63-linked ubiquitination;I-kappaB kinase/NF-kappaB signaling;innate immune response","FunCat.ID":"30.01.05.01.04;36.25.16.01","FunCat.description":"NIK-I-kappaB/NF-kappaB cascade;innate immune response (invertebrates and vertebrates)","PubMed.ID":21455180,"subunits.Protein.name.":"E3 ubiquitin-protein ligase RNF31;RanBP-type and C3HC4-type zinc finger-containing protein 1;Sharpin","subunits.Gene.name.":"RNF31;RBCK1;SHARPIN","subunits.Gene.name.syn.":"ZIBRA;C20orf18, RNF54, UBCE7IP3, XAP3, XAP4;SIPL1","Disease.comment":"Null mutations in the Sharpin gene are responsible for chronic proliferative dermatitis in mice.","Subunits.comment":"None","Complex.comment":"LUBAC complex binds to NEMO (IKBKG ) in the IKK complex, and assembles linear polyubiquitin chains on NEMO. The activated IKK complex subsequently induces the degradation of NFKBIA resulting in activation of NF-kappaB complex.LUBAC catalyzes the formation of M1-linked ubiquitin chains (PMID:26670046).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6179,"ComplexName":"mGluR5-PP2A complex","Organism":"Rat","Synonyms":"None","Cell.line":"hippocampal brain cells","subunits.UniProt.IDs.":"P31424;P63331","subunits.Entrez.IDs.":"24418;24672","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":24395787,"subunits.Protein.name.":"Metabotropic glutamate receptor 5 ;Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform","subunits.Gene.name.":"Grm5;Ppp2ca","subunits.Gene.name.syn.":"Gprc1e Mglur5;None","Disease.comment":"Experimental findings suggest that the mGluR5\\u2013PP2A axis has a centralrole in neurofibrillary degeneration in Guam PD and thus may be a therapeutic target for the treatment of this disease and related tauopathies like Alzheimer.","Subunits.comment":"None","Complex.comment":"Coimmunoprecipitation experiments showed that BMAA treatment dissociated PP2Ac from mGluR5, making it available for phosphorylation at Tyr(307). These findings suggest a scenario in which BMAA can lead to tau pathology by inhibiting PP2A through the activation of mGluR5, the consequent release of PP2Ac from the mGluR5-PP2A complex, and its phosphorylation at Tyr(307) by Src.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6180,"ComplexName":"PPP2R1A-PPP2R3B complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P30153;Q9Y5P8","subunits.Entrez.IDs.":"5518;28227","Protein.complex.purification.method":"MI:0114-x-ray crystallography;MI:0071-molecular sieving","GO.ID":"GO:0006470","GO.description":"protein dephosphorylation","FunCat.ID":"14.07.03","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation","PubMed.ID":25007185,"subunits.Protein.name.":"Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform;Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta","subunits.Gene.name.":"PPP2R1A;PPP2R3B","subunits.Gene.name.syn.":"None;PPP2R3L","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6181,"ComplexName":"LRP-PS1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain cells","subunits.UniProt.IDs.":"P97887;Q9QYP1","subunits.Entrez.IDs.":"29192;83469","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0051-fluorescence technologies;MI:0096-pull down","GO.ID":"GO:0070765","GO.description":"gamma-secretase complex","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":15917251,"subunits.Protein.name.":"Presenilin-1;Low-density lipoprotein receptor-related protein 4","subunits.Gene.name.":"Psen1;Lrp4","subunits.Gene.name.syn.":"Psnl1;Megf7","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Low density lipoprotein receptor-related protein (LRP) colocalizes and interacts with endogenous PS1 using coimmunoprecipitation, a pull-down assay, and fluorescence lifetime imaging microscopy. LRP is a competitive substrate of the amyloid precursor protein (APP) for gamma-secretase. No exact LRP gene is given in paper. As LRP4 is expressed in different regions of the brain, mainly in the olfactory bulb, at lower level in the cerebral cortex and hippocampus, this subunit is used for annotation.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6182,"ComplexName":"PP2A A/C-striatin complex","Organism":"Human","Synonyms":"None","Cell.line":"transfected NIH 3T3 cells","subunits.UniProt.IDs.":"O43815;P30153;P67775","subunits.Entrez.IDs.":"6801;5518;5515","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006470;GO:0019722","GO.description":"protein dephosphorylation;calcium-mediated signaling","FunCat.ID":"14.07.03;30.01.09.03","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;Ca2+ mediated signal transduction","PubMed.ID":10681496,"subunits.Protein.name.":"Striatin;Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform;Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform","subunits.Gene.name.":"STRN;PPP2R1A;PPP2CA","subunits.Gene.name.syn.":"None;None;None","Disease.comment":"None","Subunits.comment":"Since the authors did not specify serine/threonine-protein phosphatase 2A catalytic subunit we used the alpha isoform. Since the authors did not specify serine/threonine-protein phosphatase 2A regulartory subunit we used the alpha isoform.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6183,"ComplexName":"PP2A A/C-SG2NA complex","Organism":"Human","Synonyms":"None","Cell.line":"transfected NIH 3T3 cells","subunits.UniProt.IDs.":"P30153;P67775;Q13033","subunits.Entrez.IDs.":"5518;5515;29966","Protein.complex.purification.method":"None","GO.ID":"GO:0006470;GO:0019722","GO.description":"protein dephosphorylation;calcium-mediated signaling","FunCat.ID":"14.07.03;30.01.09.03","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation;Ca2+ mediated signal transduction","PubMed.ID":10681496,"subunits.Protein.name.":"Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform;Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform;Striatin-3","subunits.Gene.name.":"PPP2R1A;PPP2CA;STRN3","subunits.Gene.name.syn.":"None;None;GS2NA, SG2NA","Disease.comment":"None","Subunits.comment":"Since the authors did not specify serine/threonine-protein phosphatase 2A catalytic subunit we used the alpha isoform. Since the authors did not specify serine/threonine-protein phosphatase 2A regulartory subunit we used the alpha isoform.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6184,"ComplexName":"AuroraB-AuroraC-INCENP complex","Organism":"Human","Synonyms":"None","Cell.line":"PC3 cells","subunits.UniProt.IDs.":"O14965;Q96GD4;Q9NQS7","subunits.Entrez.IDs.":"6790;9212;3619","Protein.complex.purification.method":"MI:0027- cosedimentation;MI:0019- coimmunoprecipitation;MI:0416- fluorescence microscopy","GO.ID":"GO:0050821","GO.description":"protein stabilization","FunCat.ID":"14.01","FunCat.description":"protein folding and stabilization","PubMed.ID":27332895,"subunits.Protein.name.":"Aurora kinase A;Aurora kinase B;Inner centromere protein","subunits.Gene.name.":"AURKA;AURKB;INCENP","subunits.Gene.name.syn.":"AIK, AIRK1, ARK1, AURA, AYK1, BTAK, IAK1, STK15, STK6;AIK2, AIM1, AIRK2, ARK2 STK1, STK12, STK5;","Disease.comment":"Prostate cancer","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6185,"ComplexName":"SAPCD2-Galphai-LGN complex","Organism":"Human","Synonyms":"SAPCD2-GNAI1-GPSM2 complex","Cell.line":"HEK-293T cells","subunits.UniProt.IDs.":"P63096;P81274;Q86UD0","subunits.Entrez.IDs.":"2770;29899;89958","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0096- pull down","GO.ID":"GO:0000132;GO:0008356","GO.description":"establishment of mitotic spindle orientation;asymmetric cell division","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26766442,"subunits.Protein.name.":"Guanine nucleotide-binding protein G;G-protein-signaling modulator 2 ;Suppressor APC domain-containing protein 2","subunits.Gene.name.":"GNAI1;GPSM2;SAPCD2","subunits.Gene.name.syn.":";LGN;C9orf140","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6186,"ComplexName":"ArPIKfyve-Sac3-Sph1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK-293 cells","subunits.UniProt.IDs.":"Q92562;Q9Y2I7;Q9Y6H5","subunits.Entrez.IDs.":"9896;200576;9627","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0416- fluorescence microscopy","GO.ID":"GO:0050821","GO.description":"protein stabilization","FunCat.ID":"14.01","FunCat.description":"protein folding and stabilization","PubMed.ID":26405034,"subunits.Protein.name.":"Polyphosphoinositide phosphatase;1-phosphatidylinositol 3-phosphate 5-kinase ;Synphilin-1","subunits.Gene.name.":"FIG4;PIKFYVE;SNCAIP","subunits.Gene.name.syn.":"KIAA0274, SAC3;KIAA0981 PIP5K3;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6187,"ComplexName":"STIP-USP7-Mdm2 complex","Organism":"Human","Synonyms":"TFIP11-USP7-MDM2 complex","Cell.line":"O2-OS cells","subunits.UniProt.IDs.":"Q00987;Q93009;Q9UBB9","subunits.Entrez.IDs.":"4193;7874;None","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0050821","GO.description":"protein stabilization","FunCat.ID":"14.01","FunCat.description":"protein folding and stabilization","PubMed.ID":26460617,"subunits.Protein.name.":"E3 ubiquitin-protein ligase Mdm2 ;Ubiquitin carboxyl-terminal hydrolase 7 ;Tuftelin-interacting protein 11","subunits.Gene.name.":"MDM2;USP7;TFIP11","subunits.Gene.name.syn.":";HAUSP;STIP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6188,"ComplexName":"STIP-USP7-p53 complex","Organism":"Human","Synonyms":"TFIP11-USP7-TP53 complex","Cell.line":"U2-OS cells","subunits.UniProt.IDs.":"P04637;Q93009;Q9UBB9","subunits.Entrez.IDs.":"7157;7874;None","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0050821;GO:0005654","GO.description":"protein stabilization;nucleoplasm","FunCat.ID":"14.01","FunCat.description":"protein folding and stabilization","PubMed.ID":26460617,"subunits.Protein.name.":"Cellular tumor antigen p53;Ubiquitin carboxyl-terminal hydrolase 7 ;Tuftelin-interacting protein 11","subunits.Gene.name.":"TP53;USP7;TFIP11","subunits.Gene.name.syn.":"P53;HAUSP;STIP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6189,"ComplexName":"ArgRS-GlnRS-AIMP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P47897;P54136;Q12904","subunits.Entrez.IDs.":"5859;5917;9255","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0006418;GO:0017101","GO.description":"tRNA aminoacylation for protein translation;aminoacyl-tRNA synthetase multienzyme complex","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25288775,"subunits.Protein.name.":"Glutamine--tRNA ligase ;Arginine--tRNA ligase, cytoplasmic ;Aminoacyl tRNA synthase complex-interacting multifunctional protein 1","subunits.Gene.name.":"QARS;RARS;AIMP1","subunits.Gene.name.syn.":";;EMAP2 SCYE1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6190,"ComplexName":"p38gamma-Hsp90-K-Ras complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK-293T","subunits.UniProt.IDs.":"P01116;P08238;P53778","subunits.Entrez.IDs.":"3845;3326;6300","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0001558","GO.description":"regulation of cell growth","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":24962213,"subunits.Protein.name.":"GTPase KRas ;Heat shock protein HSP 90-beta;Mitogen-activated protein kinase 12","subunits.Gene.name.":"KRAS;HSP90AB1;MAPK12","subunits.Gene.name.syn.":"KRAS2 RASK2;HSP90B HSPC2 HSPCB;ERK6 SAPK3","Disease.comment":"K-Ras-dependent colon cancer","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6191,"ComplexName":"IGF2-IGFBP2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P01344;P18065","subunits.Entrez.IDs.":"3481;3485","Protein.complex.purification.method":"MI:0004- affinity chromatography technologies","GO.ID":"GO:0045667;GO:0008201","GO.description":"regulation of osteoblast differentiation;heparin binding","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":24604839,"subunits.Protein.name.":"Insulin-like growth factor II ;Insulin-like growth factor-binding protein 2","subunits.Gene.name.":"IGF2;IGFBP2","subunits.Gene.name.syn.":";BP2 IBP2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6192,"ComplexName":"CHDH-SQSTM1-MAP1LC3 complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"Q13501;Q8NE62;Q9H492","subunits.Entrez.IDs.":"8878;55349;84557","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:1904925","GO.description":"positive regulation of mitophagy in response to mitochondrial depolarization","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25483962,"subunits.Protein.name.":"Sequestosome-1 ;Choline dehydrogenase, mitochondrial ;Microtubule-associated proteins 1A/1B light chain 3A","subunits.Gene.name.":"SQSTM1;CHDH;MAP1LC3A","subunits.Gene.name.syn.":"ORCA OSIL;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6193,"ComplexName":"ADAM12-alphaVbeta3-integrin-MMP-14 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK-293 cells","subunits.UniProt.IDs.":"O43184;P05106;P06756;P50281","subunits.Entrez.IDs.":"8038;3690;3685;4323","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0042981","GO.description":"regulation of apoptotic process","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":24006261,"subunits.Protein.name.":"Disintegrin and metalloproteinase domain-containing protein 12 ;Integrin beta-3;Integrin alpha-V;Matrix metalloproteinase-14","subunits.Gene.name.":"ADAM12;ITGB3;ITGAV;MMP14","subunits.Gene.name.syn.":"MLTN;GP3A;MSK8 VNRA;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6194,"ComplexName":"B-WICH complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O00159;O60264;O75533;P35659;Q03468;Q9BQG0;Q9NR30;Q9UIG0","subunits.Entrez.IDs.":"4641;8467;23451;7913;2074;10514;9188;9031","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0226- ion exchange chromatography","GO.ID":"GO:0003682;GO:0001035;GO:0005634","GO.description":"chromatin binding;transcription from RNA polymerase III type 3 promoter;nucleus","FunCat.ID":"70.1","FunCat.description":"nucleus","PubMed.ID":25883140,"subunits.Protein.name.":"Unconventional myosin-Ic ;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5;Splicing factor 3B subunit 1 ;Protein DEK;DNA excision repair protein ERCC-6 ;Myb-binding protein 1A;Nucleolar RNA helicase 2 ;Tyrosine-protein kinase BAZ1B","subunits.Gene.name.":"MYO1C;SMARCA5;SF3B1;DEK;ERCC6;MYBBP1A;DDX21;BAZ1B","subunits.Gene.name.syn.":";SNF2H WCRF135;SAP155;;CSB;P160;;WBSC10 WBSCR10 WBSCR9 WSTF","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The 45 S rRNA, the 5 S rRNA, and the 7SL RNA are parts of the B-WICH complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6195,"ComplexName":"Stargazin-AP-2-AP-3a complex","Organism":"Human","Synonyms":"CACNG2-AP2A1-AP3D1 complex","Cell.line":"None","subunits.UniProt.IDs.":"O14617;O95782;Q9Y698","subunits.Entrez.IDs.":"8943;160;10369","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2000311","GO.description":"regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":24217640,"subunits.Protein.name.":"AP-3 complex subunit delta-1;AP-2 complex subunit alpha-1;Voltage-dependent calcium channel gamma-2 subunit","subunits.Gene.name.":"AP3D1;AP2A1;CACNG2","subunits.Gene.name.syn.":"None;ADTAA CLAPA1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6196,"ComplexName":"Stargazin-Glu1-mu2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P42261;Q96CW1;Q9Y698","subunits.Entrez.IDs.":"2890;1173;10369","Protein.complex.purification.method":"None","GO.ID":"GO:2000311","GO.description":"regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":24217640,"subunits.Protein.name.":"Glutamate receptor 1 ;AP-2 complex subunit mu ;Voltage-dependent calcium channel gamma-2 subunit","subunits.Gene.name.":"GRIA1;AP2M1;CACNG2","subunits.Gene.name.syn.":"GLUH1 GLUR1;CLAPM1 KIAA0109;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6197,"ComplexName":"Stargazin-Glu1-mu3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P42261;P53677;Q9Y698","subunits.Entrez.IDs.":"2890;10947;10369","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2000311","GO.description":"regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":24217640,"subunits.Protein.name.":"Glutamate receptor 1 ;AP-3 complex subunit mu-2;Voltage-dependent calcium channel gamma-2 subunit","subunits.Gene.name.":"GRIA1;AP3M2;CACNG2","subunits.Gene.name.syn.":"GLUH1 GLUR1;None;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6198,"ComplexName":"Stargazin-Glu2A-mu2 complex","Organism":"Human","Synonyms":"CACNG2-GRIA2-AP2M1 complex","Cell.line":"None","subunits.UniProt.IDs.":"P42262;Q96CW1;Q9Y698","subunits.Entrez.IDs.":"2891;1173;10369","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2000311","GO.description":"regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":24217640,"subunits.Protein.name.":"Glutamate receptor 2 ;AP-2 complex subunit mu ;Voltage-dependent calcium channel gamma-2 subunit","subunits.Gene.name.":"GRIA2;AP2M1;CACNG2","subunits.Gene.name.syn.":"GLUR2;CLAPM1 KIAA0109;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6199,"ComplexName":"Stargazin-Glu2A-mu3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P42262;P53677;Q9Y698","subunits.Entrez.IDs.":"2891;10947;10369","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:2000311","GO.description":"regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":24217640,"subunits.Protein.name.":"Glutamate receptor 2 ;AP-3 complex subunit mu-2;Voltage-dependent calcium channel gamma-2 subunit","subunits.Gene.name.":"GRIA2;AP3M2;CACNG2","subunits.Gene.name.syn.":"GLUR2;None;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6200,"ComplexName":"Axin-TNKS2-KIF3A complex","Organism":"Mouse","Synonyms":"None","Cell.line":"3T3-L1 adipocytes","subunits.UniProt.IDs.":"O35625;P28741;Q3UES3","subunits.Entrez.IDs.":"12005;16568;74493","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0096- pull down","GO.ID":"GO:0010827","GO.description":"regulation of glucose transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":22473005,"subunits.Protein.name.":"Axin-1 ;Kinesin-like protein KIF3A;Tankyrase-2","subunits.Gene.name.":"Axin1;Kif3a;Tnks2","subunits.Gene.name.syn.":"Axin Fu;Kif3;Tank2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6201,"ComplexName":"Dock3-Elmo-RhoG complex","Organism":"Mouse","Synonyms":"None","Cell.line":"PC12 cells","subunits.UniProt.IDs.":"P84096;Q8BPU7;Q8CIQ7","subunits.Entrez.IDs.":"56212;140580;56212","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0031548;GO:0051386","GO.description":"regulation of brain-derived neurotrophic factor receptor signaling pathway;regulation of neurotrophin TRK receptor signaling pathway","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":22734669,"subunits.Protein.name.":"Rho-related GTP-binding protein RhoG ;Engulfment and cell motility protein 1 ;Dedicator of cytokinesis protein 3","subunits.Gene.name.":"Rhog;Elmo1;Dock3","subunits.Gene.name.syn.":"Arhg Sid10750;;Moca","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6202,"ComplexName":"S100A10-annexin A2-AHNAK","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P07355;Q09666;Q6SQH4","subunits.Entrez.IDs.":"302;79026;100008922","Protein.complex.purification.method":"MI:0077- nuclear magnetic resonance","GO.ID":"GO:0001778","GO.description":"plasma membrane repair","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":22940583,"subunits.Protein.name.":"Annexin A2 ;Neuroblast differentiation-associated protein AHNAK ;Protein S100-A10","subunits.Gene.name.":"ANXA2;AHNAK;S100a10","subunits.Gene.name.syn.":"ANX2 ANX2L4 CAL1H LPC2D;PM227;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Oryctolagus cuniculus (Rabbit)"}
{"ComplexID":6203,"ComplexName":"TFAP2C-Myc-KDM5B complex","Organism":"Human","Synonyms":"None","Cell.line":"MCF-7 cells","subunits.UniProt.IDs.":"P01106;Q92754;Q9UGL1","subunits.Entrez.IDs.":"4609;7022;10765","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0010564","GO.description":"regulation of cell cycle process","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":22371483,"subunits.Protein.name.":"Myc proto-oncogene protein ;Transcription factor AP-2 gamma ;Lysine-specific demethylase 5B","subunits.Gene.name.":"MYC;TFAP2C;KDM5B","subunits.Gene.name.syn.":"BHLHE39;;JARID1B PLU1 RBBP2H1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6204,"ComplexName":"Kremen1-AP-2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P34056;Q99N43","subunits.Entrez.IDs.":"21418;84035","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0030111","GO.description":"regulation of Wnt signaling pathway","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23251700,"subunits.Protein.name.":"Transcription factor AP-2-alpha ;Kremen protein 1","subunits.Gene.name.":"Tfap2a;Kremen1","subunits.Gene.name.syn.":"Ap2tf Tcfap2a;Kremen","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6205,"ComplexName":"Dkk1-Lrp6-Kremen2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O54908;O88572;Q8K1S7","subunits.Entrez.IDs.":"13380;16974;73016","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030111","GO.description":"regulation of Wnt signaling pathway","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":12050670,"subunits.Protein.name.":"Dickkopf-related protein 1 ;Low-density lipoprotein receptor-related protein 6 ;Kremen protein 2","subunits.Gene.name.":"Dkk1;Lrp6;Kremen2","subunits.Gene.name.syn.":";;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6206,"ComplexName":"ICAT-AR-beta-catenin complex","Organism":"Human","Synonyms":"None","Cell.line":"Prostate cancer cells","subunits.UniProt.IDs.":"P10275;P35222;Q9NSA3","subunits.Entrez.IDs.":"367;1499;56998","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0096- pull down","GO.ID":"GO:0030111;GO:2000823","GO.description":"regulation of Wnt signaling pathway;regulation of androgen receptor activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":21885566,"subunits.Protein.name.":"Androgen receptor;Catenin beta-1;Beta-catenin-interacting protein 1","subunits.Gene.name.":"AR;CTNNB1;CTNNBIP1","subunits.Gene.name.syn.":"DHTR, NR3C4;CTNNB;ICAT","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6207,"ComplexName":"beta2AR-Gs complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04896;P07550","subunits.Entrez.IDs.":"281793;154","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0008277","GO.description":"regulation of G-protein coupled receptor protein signaling pathway","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":21772288,"subunits.Protein.name.":"Guanine nucleotide-binding protein G;Beta-2 adrenergic receptor","subunits.Gene.name.":"GNAS;ADRB2","subunits.Gene.name.syn.":"GNAS1;ADRB2R B2AR","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Bos taurus (Bovine);Homo sapiens (Human)"}
{"ComplexID":6208,"ComplexName":"PNP homotrimer","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P00491","subunits.Entrez.IDs.":"4860","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0042278;GO:0004731","GO.description":"purine nucleoside metabolic process;purine-nucleoside phosphorylase activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":2104852,"subunits.Protein.name.":"Purine nucleoside phosphorylase","subunits.Gene.name.":"PNP","subunits.Gene.name.syn.":"NP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":6209,"ComplexName":"MT1-G(i)-RGS20 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O76081;P48039;P63096","subunits.Entrez.IDs.":"8601;4543;2770","Protein.complex.purification.method":"MI:0012- bioluminescence resonance energy transfer","GO.ID":"GO:0007187","GO.description":"G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20859254,"subunits.Protein.name.":"Regulator of G-protein signaling 20 ;Melatonin receptor type 1A ;Guanine nucleotide-binding protein G","subunits.Gene.name.":"RGS20;MTNR1A;GNAI1","subunits.Gene.name.syn.":"RGSZ1 ZGAP1;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6210,"ComplexName":"MT1-MT2 complex","Organism":"Human","Synonyms":"MTNR1A-MTNR1B complex","Cell.line":"HEK-234T cells","subunits.UniProt.IDs.":"P48039;P49286","subunits.Entrez.IDs.":"4543;4544","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007187","GO.description":"G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20859254,"subunits.Protein.name.":"Melatonin receptor type 1A ;Melatonin receptor type 1B","subunits.Gene.name.":"MTNR1A;MTNR1B","subunits.Gene.name.syn.":";","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6211,"ComplexName":"RSG20-MT1-MT2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O76081;P48039;P49286","subunits.Entrez.IDs.":"8601;4543;4544","Protein.complex.purification.method":"MI:0012- bioluminescence resonance energy transfer","GO.ID":"GO:1901979","GO.description":"regulation of inward rectifier potassium channel activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20859254,"subunits.Protein.name.":"Regulator of G-protein signaling 20 ;Melatonin receptor type 1A ;Melatonin receptor type 1B","subunits.Gene.name.":"RGS20;MTNR1A;MTNR1B","subunits.Gene.name.syn.":"RGSZ1 ZGAP1;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6212,"ComplexName":"GM130-GRASP65 complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"Q08379;Q9BQQ3","subunits.Entrez.IDs.":"2801;64689","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0006888;GO:0099041","GO.description":"ER to Golgi vesicle-mediated transport;vesicle tethering to Golgi","FunCat.ID":"20.09.07.03","FunCat.description":"ER to Golgi transport","PubMed.ID":26363069,"subunits.Protein.name.":"Golgin subfamily A member 2 ;Golgi reassembly-stacking protein 1","subunits.Gene.name.":"GOLGA2;GORASP1","subunits.Gene.name.syn.":";GOLPH5 GRASP65","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6213,"ComplexName":"DOCK8-WIP-WASp complex","Organism":"Human","Synonyms":"DOCK8-WIPF1-WAS complex","Cell.line":"peripheral blood T cells;  DND41 T cell line","subunits.UniProt.IDs.":"O43516;P42768;Q8NF50","subunits.Entrez.IDs.":"7456;7454;81704","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0428-imaging techniques","GO.ID":"GO:0015629;GO:0042608;GO:0000910;GO:0001771;GO:0072678","GO.description":"actin cytoskeleton;T cell receptor binding;cytokinesis;immunological synapse formation;T cell migration","FunCat.ID":"70.04.03;10.03.03","FunCat.description":"actin cytoskeleton;cytokinesis (cell division) /septum formation and hydrolysis","PubMed.ID":27599296,"subunits.Protein.name.":"WAS/WASL-interacting protein family member 1;Wiskott-Aldrich syndrome protein;Dedicator of cytokinesis protein 8","subunits.Gene.name.":"WIPF1;WAS;DOCK8","subunits.Gene.name.syn.":"WASPIP WIP;IMD2;None","Disease.comment":"Wiskott-Aldrich syndrome (WAS) is associated with mutations in the WAS protein (WASp), which plays a critical role in the initiation of T cell receptor-driven (TCR-driven) actin polymerization. The clinical phenotype of WAS includes susceptibility to infection, allergy, autoimmunity, and malignancy and overlaps with the symptoms of dedicator of cytokinesis 8 (DOCK8) deficiency, suggesting that the 2 syndromes share common pathogenic mechanisms.","Subunits.comment":"None","Complex.comment":"DOCK8-WIP-WASp complex links T cell receptors to the actin cytoskeleton. The WASp-interacting protein (WIP) bridges DOCK8 to WASp and actin in T cells. The guanine nucleotide exchange factor activity of DOCK8 is essential for the integrity of the subcortical actin cytoskeleton as well as for TCR-driven WASp activation, F-actin assembly, immune synapse formation, actin foci formation, mechanotransduction, T cell transendothelial migration, and homing to lymph nodes, all of which also depend on WASp. The results indicate that DOCK8 and WASp are in the same signaling pathway that links TCRs to the actin cytoskeleton in TCR-driven actin assembly. DOCK8 binds to and colocalizes constitutively with WIP and WASp in T cells. WIP bridges DOCK8 to actin. DOCK8 GEF activity mediates TCR-driven WASp activation. DOCK8 is essential for TCR-driven actin foci formation and mechanotransduction.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6214,"ComplexName":"Dock8-Wipf1-Was complex","Organism":"Mouse","Synonyms":"Dock8-Wip-Wasp complex","Cell.line":"None","subunits.UniProt.IDs.":"P70315;Q8C147;Q8K1I7","subunits.Entrez.IDs.":"22376;76088;215280","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0015629;GO:0042608;GO:0000910;GO:0001771;GO:0072678","GO.description":"actin cytoskeleton;T cell receptor binding;cytokinesis;immunological synapse formation;T cell migration","FunCat.ID":"70.04.03;10.03.03","FunCat.description":"actin cytoskeleton;cytokinesis (cell division) /septum formation and hydrolysis","PubMed.ID":27599296,"subunits.Protein.name.":"Wiskott-Aldrich syndrome protein homolog;Dedicator of cytokinesis protein 8;WAS/WASL-interacting protein family member 1","subunits.Gene.name.":"Was;Dock8;Wipf1","subunits.Gene.name.syn.":"Wasp;None;Waspip Wip","Disease.comment":"Wiskott-Aldrich syndrome (WAS) is associated with mutations in the WAS protein (WASp), which plays a critical role in the initiation of T cell receptor-driven (TCR-driven) actin polymerization. The clinical phenotype of WAS includes susceptibility to infection, allergy, autoimmunity, and malignancy and overlaps with the symptoms of dedicator of cytokinesis 8 (DOCK8) deficiency, suggesting that the 2 syndromes share common pathogenic mechanisms.","Subunits.comment":"None","Complex.comment":"DOCK8-WIP-WASp complex links T cell receptors to the actin cytoskeleton. The WASp-interacting protein (WIP) bridges DOCK8 to WASp and actin in T cells. The guanine nucleotide exchange factor activity of DOCK8 is essential for the integrity of the subcortical actin cytoskeleton as well as for TCR-driven WASp activation, F-actin assembly, immune synapse formation, actin foci formation, mechanotransduction, T cell transendothelial migration, and homing to lymph nodes, all of which also depend on WASp. The results indicate that DOCK8 and WASp are in the same signaling pathway that links TCRs to the actin cytoskeleton in TCR-driven actin assembly. DOCK8 binds to and colocalizes constitutively with WIP and WASp in T cells. WIP bridges DOCK8 to actin. DOCK8 GEF activity mediates TCR-driven WASp activation. DOCK8 is essential for TCR-driven actin foci formation and mechanotransduction.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6215,"ComplexName":"GATOR1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK-293T cells","subunits.UniProt.IDs.":"O75140;Q12980;Q8WTW4","subunits.Entrez.IDs.":"9681;8131;10641","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:1903832;GO:1904262;GO:0005096","GO.description":"regulation of cellular response to amino acid starvation;negative regulation of TORC1 signaling;GTPase activator activity","FunCat.ID":"18.02.01.01.01","FunCat.description":"GTPase activator (GAP)","PubMed.ID":23723238,"subunits.Protein.name.":"DEP domain-containing protein 5;Nitrogen permease regulator 3-like protein;Nitrogen permease regulator 2-like protein","subunits.Gene.name.":"DEPDC5;NPRL3;NPRL2","subunits.Gene.name.syn.":"KIAA0645;C16orf35 CGTHBA MARE;TUSC4","Disease.comment":"GATOR1 components are present in low single-digit percentages of glioblastomas and ovarian cancers,","Subunits.comment":"None","Complex.comment":"The loss of GATOR1 proteins prevented the inactivation of mTORC1 and dTORC1 normally caused by amino acid deprivation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6216,"ComplexName":"GATOR2 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK-293T cells","subunits.UniProt.IDs.":"P55735;Q6PJI9;Q96EE3;Q96S15;Q9NXC5","subunits.Entrez.IDs.":"6396;79726;81929;84219;54468","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:1903432","GO.description":"regulation of TORC1 signaling","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23723238,"subunits.Protein.name.":"Protein SEC13 homolog;WD repeat-containing protein 59;Nucleoporin SEH1;WD repeat-containing protein 24;WD repeat-containing protein mio","subunits.Gene.name.":"SEC13;WDR59;SEH1L;WDR24;MIOS","subunits.Gene.name.syn.":"D3S1231E SEC13L1 SEC13R;KIAA1923;SEC13L SEH1;C16orf21;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Inhibition of GATOR2 subunits suppresses mTORC1 signaling. GATOR2 is an inhibitor of an inhibitor (GATOR1) of the amino acid\\u2013sensing branch of the TORC1 pathway.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6217,"ComplexName":"GATOR complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK-293T cells","subunits.UniProt.IDs.":"O75140;P55735;Q12980;Q6PJI9;Q8WTW4;Q96EE3;Q96S15;Q9NXC5","subunits.Entrez.IDs.":"9681;6396;8131;79726;10641;81929;84219;54468","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:1903432;GO:1903832","GO.description":"regulation of TORC1 signaling;regulation of cellular response to amino acid starvation","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23723238,"subunits.Protein.name.":"DEP domain-containing protein 5;Protein SEC13 homolog;Nitrogen permease regulator 3-like protein;WD repeat-containing protein 59;Nitrogen permease regulator 2-like protein;Nucleoporin SEH1;WD repeat-containing protein 24;WD repeat-containing protein mio","subunits.Gene.name.":"DEPDC5;SEC13;NPRL3;WDR59;NPRL2;SEH1L;WDR24;MIOS","subunits.Gene.name.syn.":"KIAA0645;D3S1231E SEC13L1 SEC13R;C16orf35 CGTHBA MARE;KIAA1923;TUSC4;SEC13L SEH1;C16orf21;None","Disease.comment":"Inactivating mutations in GATOR1 components were found in glioblastomas and ovarian cancers.","Subunits.comment":"None","Complex.comment":"GATOR as a complex that is composed of the two subcomplexes GATOR1 complexand GATOR2 complex. GATOR as a complex that interacts with and negatively regulates the Rag guanosine triphosphatases (GTPases) which promote mTORC1 translocation to the lysosomal surface.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6218,"ComplexName":"POL2R-SYMPK-SSU72 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P24928;Q92797;Q9NP77","subunits.Entrez.IDs.":"5430;8189;29101","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:1900363","GO.description":"regulation of mRNA polyadenylation","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20861839,"subunits.Protein.name.":"DNA-directed RNA polymerase II subunit RPB1;Symplekin;RNA polymerase II subunit A C-terminal domain phosphatase SSU72","subunits.Gene.name.":"POLR2A;SYMPK;SSU72","subunits.Gene.name.syn.":"POLR2;SPK;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6219,"ComplexName":"DGKZ-RASGRP1-HRAS complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"O95267;P01112;Q13574","subunits.Entrez.IDs.":"10125;3265;8525","Protein.complex.purification.method":"None","GO.ID":"GO:0007265","GO.description":"Ras protein signal transduction","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":11257115,"subunits.Protein.name.":"RAS guanyl-releasing protein 1 ;GTPase HRas;Diacylglycerol kinase zeta","subunits.Gene.name.":"RASGRP1;HRAS;DGKZ","subunits.Gene.name.syn.":"RASGRP;HRAS1;DAGK6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6220,"ComplexName":"HDAC10-PAX3-KAP1 complex","Organism":"Human","Synonyms":"HDAC10-PAX3-TRIM28 complex","Cell.line":"HEK-293 cells","subunits.UniProt.IDs.":"P23760;Q13263;Q969S8","subunits.Entrez.IDs.":"5077;10155;83933","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0416- fluorescence microscopy","GO.ID":"GO:0048021;GO:0003700","GO.description":"regulation of melanin biosynthetic process;transcription factor activity, sequence-specific DNA binding","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20032463,"subunits.Protein.name.":"Paired box protein Pax-3 ;Transcription intermediary factor 1-beta ;Histone deacetylase 10","subunits.Gene.name.":"PAX3;TRIM28;HDAC10","subunits.Gene.name.syn.":"HUP2;KAP1 RNF96 TIF1B;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6221,"ComplexName":"Ccm2-Krit1-Ccm3 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q6S5J6;Q8K2Y9;Q8VE70","subunits.Entrez.IDs.":"79264;216527;56426","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0001525;GO:0090049;GO:1903587","GO.description":"angiogenesis;regulation of cell migration involved in sprouting angiogenesis;regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis","FunCat.ID":"41.05.16","FunCat.description":"angiogenesis","PubMed.ID":17900104,"subunits.Protein.name.":"Krev interaction trapped protein 1 ;Cerebral cavernous malformations protein 2 homolog ;Programmed cell death protein 10","subunits.Gene.name.":"Krit1;Ccm2;Pdcd10","subunits.Gene.name.syn.":"Ccm1;Osm;Tfar15","Disease.comment":"OMIM:116860 Cerebral cavernous malformations 1OMIM:603284 Cerebral cavernous malformations 2OMIM:603285 Cerebral cavernous malformations 3","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6222,"ComplexName":"CCM1-CCM2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"MEF cells","subunits.UniProt.IDs.":"Q6S5J6;Q8K2Y9","subunits.Entrez.IDs.":"79264;216527","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0001525;GO:0090049;GO:1903587","GO.description":"angiogenesis;regulation of cell migration involved in sprouting angiogenesis;regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis","FunCat.ID":"41.05.16","FunCat.description":"angiogenesis","PubMed.ID":16037064,"subunits.Protein.name.":"Krev interaction trapped protein 1 ;Cerebral cavernous malformations protein 2 homolog","subunits.Gene.name.":"Krit1;Ccm2","subunits.Gene.name.syn.":"Ccm1;Osm","Disease.comment":"OMIM:116860 Cerebral cavernous malformations 1OMIM:603284 Cerebral cavernous malformations 2","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6223,"ComplexName":"KRIT1-CCM2-ICAP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK-293T cells","subunits.UniProt.IDs.":"O00522;O14713;Q9BSQ5","subunits.Entrez.IDs.":"889;9270;83605","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007155","GO.description":"cell adhesion","FunCat.ID":"34.07","FunCat.description":"cell adhesion","PubMed.ID":16037064,"subunits.Protein.name.":"Krev interaction trapped protein 1;Integrin beta-1-binding protein 1;Cerebral cavernous malformations 2 protein","subunits.Gene.name.":"KRIT1;ITGB1BP1;CCM2","subunits.Gene.name.syn.":"CCM1;ICAP1;C7orf22","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6224,"ComplexName":"KRIT1-CCM2-MEKK3 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK-293T cells","subunits.UniProt.IDs.":"O00522;Q99759;Q9BSQ5","subunits.Entrez.IDs.":"889;4215;83605","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:1900744","GO.description":"regulation of p38MAPK cascade","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":16037064,"subunits.Protein.name.":"Krev interaction trapped protein 1;Mitogen-activated protein kinase kinase kinase 3 ;Cerebral cavernous malformations 2 protein","subunits.Gene.name.":"KRIT1;MAP3K3;CCM2","subunits.Gene.name.syn.":"CCM1;MAPKKK3 MEKK3;C7orf22","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6225,"ComplexName":"Heg1-Krit1-Ccm2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"E9Q7X6;Q6S5J6;Q8K2Y9","subunits.Entrez.IDs.":"None;79264;216527","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0060914;GO:0001944","GO.description":"heart formation;vasculature development","FunCat.ID":"47.03.03.02","FunCat.description":"vessels","PubMed.ID":19151727,"subunits.Protein.name.":"Protein HEG homolog 1;Krev interaction trapped protein 1 ;Cerebral cavernous malformations protein 2 homolog","subunits.Gene.name.":"Heg1;Krit1;Ccm2","subunits.Gene.name.syn.":";Ccm1;Osm","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6226,"ComplexName":"Rab11a-FIP3-DLIC-1 complex","Organism":"Human","Synonyms":"None","Cell.line":"A-431 cells","subunits.UniProt.IDs.":"P62491;Q9Y6G9;Q9Y6K9","subunits.Entrez.IDs.":"8766;51143;8517","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0016197","GO.description":"endosomal transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20026645,"subunits.Protein.name.":"Ras-related protein Rab-11A;Cytoplasmic dynein 1 light intermediate chain 1;NF-kappa-B essential modulator","subunits.Gene.name.":"RAB11A;DYNC1LI1;IKBKG","subunits.Gene.name.syn.":"RAB11;DNCLI1;FIP3, NEMO","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6227,"ComplexName":"S4-synectin-RhoGDI1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P84096;Q3U5S6;Q9Z0G0","subunits.Entrez.IDs.":"56212;20971;67903","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0096- pull down","GO.ID":"GO:0043087;GO:0010594","GO.description":"regulation of GTPase activity;regulation of endothelial cell migration","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":19581409,"subunits.Protein.name.":"Rho-related GTP-binding protein RhoG ;Syndecan;PDZ domain-containing protein GIPC1","subunits.Gene.name.":"Rhog;Sdc4;Gipc1","subunits.Gene.name.syn.":"Arhg Sid10750;;Gipc Rgs19ip1 Semcap1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6228,"ComplexName":"Ubiquitin E3 ligase (CUL3, KLHL3)","Organism":"Mammalia","Synonyms":"CUL3-KLHL3 complex","Cell.line":"COS-7 cells","subunits.UniProt.IDs.":"A0A0D9RLK8;F6R900","subunits.Entrez.IDs.":"103244596;707550","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0069- mass spectrometry studies of complexes","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23576762,"subunits.Protein.name.":"Uncharacterized protein;Cullin-3","subunits.Gene.name.":"KLHL3;CUL3","subunits.Gene.name.syn.":"None;None","Disease.comment":"Pseudohypoaldosteronism type II (PHAII) is a rare Mendelian syndrome featuring hypertension and hyperkalemia resulting from constitutive renal salt reabsorption and impaired K+ secretion. Mutations in Kelch-like 3 (KLHL3) and Cullin 3 (CUL3), components of an E3 ubiquitin ligase complex, were found to cause PHAII.","Subunits.comment":"None","Complex.comment":"Kelch-like 3 and Cullin 3 regulate electrolyte homeostasis via ubiquitination and degradation of WNK4.","SWISSPROT.organism":"Chlorocebus sabaeus (Green monkey) (Cercopithecus;Macaca mulatta (Rhesus macaque)"}
{"ComplexID":6229,"ComplexName":"ULK1-ATG13-RB1CC1  complex","Organism":"Human","Synonyms":"ULK1-ATG13-FIP200 complex","Cell.line":"None","subunits.UniProt.IDs.":"O75143;O75385;Q8TDY2","subunits.Entrez.IDs.":"9776;8408;9821","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:1905037;GO:0006914","GO.description":"autophagosome organization;autophagy","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26921696,"subunits.Protein.name.":"Autophagy-related protein 13;Serine/threonine-protein kinase ULK1;RB1-inducible coiled-coil protein 1","subunits.Gene.name.":"ATG13;ULK1;RB1CC1","subunits.Gene.name.syn.":"KIAA0652;KIAA0722;KIAA0203 RBICC","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6230,"ComplexName":"ULK2-ATG13-RB1CC1 complex","Organism":"Human","Synonyms":"ULK2-ATG13-FIP200 complex","Cell.line":"None","subunits.UniProt.IDs.":"O75143;Q8IYT8;Q8TDY2","subunits.Entrez.IDs.":"9776;9706;9821","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006914;GO:1905037","GO.description":"autophagy;autophagosome organization","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26921696,"subunits.Protein.name.":"Autophagy-related protein 13;Serine/threonine-protein kinase ULK2;RB1-inducible coiled-coil protein 1","subunits.Gene.name.":"ATG13;ULK2;RB1CC1","subunits.Gene.name.syn.":"KIAA0652;KIAA0623;KIAA0203 RBICC","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6231,"ComplexName":"Ubiquitin E3 ligase (CUL3, KLHL3, WNK1)","Organism":"Mammalia","Synonyms":"KLHL3-CUL3-WNK1 complex","Cell.line":"COS-7 cells","subunits.UniProt.IDs.":"A0A0D9RLK8;F6R900;F6RGS5","subunits.Entrez.IDs.":"103244596;707550;706493","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0069-mass spectrometry studies of complexes","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23576762,"subunits.Protein.name.":"Uncharacterized protein;Cullin-3;Uncharacterized protein","subunits.Gene.name.":"KLHL3;CUL3;WNK1","subunits.Gene.name.syn.":"None;None;None","Disease.comment":"Pseudohypoaldosteronism type II (PHAII) is a rare Mendelian syndrome featuring hypertension and hyperkalemia resulting from constitutive renal salt reabsorption and impaired K(+) secretion. Mutations in Kelch-like 3 (KLHL3) and Cullin 3 (CUL3), components of an E3 ubiquitin ligase complex, were found to cause PHAII.","Subunits.comment":"None","Complex.comment":"KLHL3 normally binds to WNK1 and WNK4, members of WNK (with no lysine) kinase family that have been found mutated in Pseudohypoaldosteronism type II (PHAII). CUL3 is a scaffold protein that assembles a complex that targets specific proteins for ubiquitination.","SWISSPROT.organism":"Chlorocebus sabaeus (Green monkey) (Cercopithecus;Macaca mulatta (Rhesus macaque);Macaca mulatta (Rhesus macaque)"}
{"ComplexID":6232,"ComplexName":"ULK1-ATG13-RB1CC1-ATG101 complex","Organism":"Human","Synonyms":"ULK1-ATG13-FIP200-ATG101 complex; Autophagy initiation complex","Cell.line":"None","subunits.UniProt.IDs.":"O75143;O75385;Q8TDY2;Q9BSB4","subunits.Entrez.IDs.":"9776;8408;9821;60673","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006914","GO.description":"autophagy","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":19597335,"subunits.Protein.name.":"Autophagy-related protein 13;Serine/threonine-protein kinase ULK1;RB1-inducible coiled-coil protein 1;Autophagy-related protein 101","subunits.Gene.name.":"ATG13;ULK1;RB1CC1;ATG101","subunits.Gene.name.syn.":"KIAA0652;KIAA0722;KIAA0203 RBICC;C12orf44","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6233,"ComplexName":"Ubiquitin E3 ligase (CUL3, KLHL3, WNK1)","Organism":"Human","Synonyms":"CUL3-KLHL3-WNK1 E3 ligase complex","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"Q13618;Q9H4A3;Q9UH77","subunits.Entrez.IDs.":"8452;65125;26249","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23387299,"subunits.Protein.name.":"Cullin-3;Serine/threonine-protein kinase WNK1;Kelch-like protein 3","subunits.Gene.name.":"CUL3;WNK1;KLHL3","subunits.Gene.name.syn.":"KIAA0617;HSN2 KDP KIAA0344 PRKWNK1;KIAA1129","Disease.comment":"The CUL3-KLHL3 E3 ligase complex is mutated in Gordon hypertension syndrome (= Pseudohypoaldosteronismtype II = PHAII).","Subunits.comment":"None","Complex.comment":"CUL3 assembles with BTB proteins (e.g. KLHL3) to form Cullin-RING E3 ubiquitin ligase complexes. The CUL3-KLHL3 E3 ligase complex regulates blood pressure via its ability to interact with and ubiquitylate WNK isoforms. The recombinant wild-type CUL3-KLHL3 E3 ligase complex, but not a disease-causing CUL3-KLHL3[R528H] mutant complex, ubiquitylated WNK1 in vitro. siRNA (small interfering RNA)-mediated knockdown of CUL3 increased WNK1 protein levels and kinase activity in HeLa cells. The KLHL3 interaction site in WNK1 could be mapped to a non-catalytic region (residues 479-667).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6234,"ComplexName":"TGF-betaR2-TGF-beta3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P10600;P37173","subunits.Entrez.IDs.":"7043;7048","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0007178","GO.description":"transmembrane receptor protein serine/threonine kinase signaling pathway","FunCat.ID":"30.05.01.18","FunCat.description":"transmembrane receptor protein serine/threonine kinase signalling pathways","PubMed.ID":11850637,"subunits.Protein.name.":"Transforming growth factor beta-3 ;TGF-beta receptor type-2","subunits.Gene.name.":"TGFB3;TGFBR2","subunits.Gene.name.syn.":";None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6235,"ComplexName":"c-Fos-c-Jun-SAF-1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HTB-94 cells","subunits.UniProt.IDs.":"P01100;P05412;P56270","subunits.Entrez.IDs.":"2353;3725;4150","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006355;GO:0003677","GO.description":"regulation of transcription, DNA-templated;DNA binding","FunCat.ID":"11.02.03.04;16.03.01","FunCat.description":"transcriptional control;DNA binding","PubMed.ID":19028685,"subunits.Protein.name.":"Proto-oncogene c-Fos ;Transcription factor AP-1 ;Myc-associated zinc finger protein","subunits.Gene.name.":"FOS;JUN;MAZ","subunits.Gene.name.syn.":"G0S7;;ZNF801","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6236,"ComplexName":"Dynein-2 complex, cytoplasmic","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P51808;P63167;P63172;Q8IVD9;Q8NCM8;Q8TCX1;Q8TF09;Q8WVS4;Q8WW35;Q96EX3;Q96FJ2;Q9NP97","subunits.Entrez.IDs.":"6990;8655;6993;23386;79659;51626;83657;55112;255758;89891;140735;83658","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0035721;GO:0005929;GO:0007224","GO.description":"intraciliary retrograde transport;cilium;smoothened signaling pathway","FunCat.ID":"30.05.02.16","FunCat.description":"hedgehog-dependent signalling pathway","PubMed.ID":25205765,"subunits.Protein.name.":"Dynein light chain Tctex-type 3 ;Dynein light chain 1, cytoplasmic;Dynein light chain Tctex-type 1 ;NudC domain-containing protein 3;Cytoplasmic dynein 2 heavy chain 1 ;Cytoplasmic dynein 2 light intermediate chain 1 ;Dynein light chain roadblock-type 2 ;WD repeat-containing protein 60;Tctex1 domain-containing protein 2;WD repeat-containing protein 34;Dynein light chain 2, cytoplasmic ;Dynein light chain roadblock-type 1","subunits.Gene.name.":"DYNLT3;DYNLL1;DYNLT1;NUDCD3;DYNC2H1;DYNC2LI1;DYNLRB2;WDR60;TCTEX1D2;WDR34;DYNLL2;DYNLRB1","subunits.Gene.name.syn.":"TCTE1L TCTE1XL;DLC1 DNCL1 DNCLC1 HDLC1;TCTEL1 TCTEX-1 TCTEX1;KIAA1068;DHC1B DHC2 DNCH2 DYH1B KIAA1997;D2LIC LIC3;DNCL2B DNLC2B ROBLD2;;;;DLC2;BITH DNCL2A DNLC2A ROBLD1","Disease.comment":"Defects in the function of primary cilia lead to a cohort of human diseases known as the ciliopathies; among these, mutations in components of the dynein-2 complex cause Jeune syndrome, short rib polydactyly type III and asphyxiating thoracic dystrophy.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6237,"ComplexName":"AJUBA-GFI1-HDAC1 complex","Organism":"Human","Synonyms":"None","Cell.line":"Jurkat T cell nuclear extracts","subunits.UniProt.IDs.":"Q13547;Q96IF1;Q99684","subunits.Entrez.IDs.":"3065;84962;2672","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0071-molecular sieving","GO.ID":"GO:0045892","GO.description":"negative regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.03","FunCat.description":"transcription repression","PubMed.ID":18805794,"subunits.Protein.name.":"Histone deacetylase 1;LIM domain-containing protein ajuba;Zinc finger protein Gfi-1","subunits.Gene.name.":"HDAC1;AJUBA;GFI1","subunits.Gene.name.syn.":"RPD3L1;JUB;ZNF163","Disease.comment":"It has been demonstrated that SCN (severe congenital neutropenia)-associated mutations in GFI1 generate dominant-negative-acting proteins (GFI1N382S), which selectively deprepress GFI1 target genes such as CSF1. A SNAG domain mutant protein (Gfi1P2A) also functioned in a dominant negative manner;however, a protein with both mutations (Gfi1P2A\\u0002N382S) lacked dominant negative activity.","Subunits.comment":"None","Complex.comment":"The majority of Gfi1 repression activity is dependent upon HDAC function. However, a residual repression activity is present in inhibitor-treated samples suggesting Gfi1 and Ajuba utilize as yet unidentified non-HDAC-dependent repression mechanism(s).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6238,"ComplexName":"DHDDS-NUS1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"Q86SQ9;Q96E22","subunits.Entrez.IDs.":"79947;116150","Protein.complex.purification.method":"None","GO.ID":"GO:0043048;GO:0006486;GO:0005783;GO:0042632","GO.description":"dolichyl monophosphate biosynthetic process;protein glycosylation;endoplasmic reticulum;cholesterol homeostasis","FunCat.ID":"14.07.02;70.07;34.01.07","FunCat.description":"modification with sugar residues (e.g. glycosylation, deglycosylation);endoplasmic reticulum;cholesterol homeostasis","PubMed.ID":21572394,"subunits.Protein.name.":"Dehydrodolichyl diphosphate synthase complex subunit DHDDS ;Dehydrodolichyl diphosphate synthase complex subunit NUS1","subunits.Gene.name.":"DHDDS;NUS1","subunits.Gene.name.syn.":"HDS;C6orf68 NGBR","Disease.comment":"A Mutation on NgBR Causes Congenital Scoliosis, Severe Neurological Impairment, Refractory Epilepsy, Hearing Deficit, and Visual Impairment.","Subunits.comment":"None","Complex.comment":"Dolichol monophosphate (Dol-P) functions as an obligate glycosyl carrier lipid in protein glycosylation reactions. Nogo-B receptor (NUS1)as an essential component of the Dol-P biosynthetic machinery.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6239,"ComplexName":"Fras1-Frem1-Frem2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"HEK-293F cells","subunits.UniProt.IDs.":"Q5H8C1;Q5SZK8;Q80T14","subunits.Entrez.IDs.":"158326;341640;231470","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0007160","GO.description":"cell-matrix adhesion","FunCat.ID":"34.07.02","FunCat.description":"cell-matrix adhesion","PubMed.ID":16880404,"subunits.Protein.name.":"FRAS1-related extracellular matrix protein 1 ;FRAS1-related extracellular matrix protein 2 ;Extracellular matrix protein FRAS1","subunits.Gene.name.":"FREM1;FREM2;Fras1","subunits.Gene.name.syn.":"C9orf143 C9orf145 C9orf154;;Kiaa1500","Disease.comment":"None","Subunits.comment":"Disease:Fraser syndrome-like phenotype","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Mus musculus (Mouse)"}
{"ComplexID":6240,"ComplexName":"PMCA1-alpha-1-syntrophin-NOS-1 complex","Organism":"Mouse","Synonyms":"Atp2b1-Snta1-Nos1 complex","Cell.line":"cardiac muscle cells","subunits.UniProt.IDs.":"G5E829;Q61234;Q9Z0J4","subunits.Entrez.IDs.":"67972;20648;18125","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0050999","GO.description":"regulation of nitric-oxide synthase activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":16735509,"subunits.Protein.name.":"Plasma membrane calcium-transporting ATPase 1 ;Alpha-1-syntrophin;Nitric oxide synthase, brain","subunits.Gene.name.":"Atp2b1;Snta1;Nos1","subunits.Gene.name.syn.":";Snt1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6241,"ComplexName":"PMCA4-alpha-1-syntrophin-NOS-1 complex","Organism":"Human","Synonyms":"Atp2b4-Snta1-Nos1 complex","Cell.line":"cardiac muscle","subunits.UniProt.IDs.":"Q61234;Q6Q477;Q9Z0J4","subunits.Entrez.IDs.":"20648;381290;18125","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0050999","GO.description":"regulation of nitric-oxide synthase activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":16735509,"subunits.Protein.name.":"Alpha-1-syntrophin;Plasma membrane calcium-transporting ATPase 4 ;Nitric oxide synthase, brain","subunits.Gene.name.":"Snta1;Atp2b4;Nos1","subunits.Gene.name.syn.":"Snt1;;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6242,"ComplexName":"14-3-3q-SGK1-tau complex","Organism":"Human","Synonyms":"YWHAQ-SGK1-MAPT complex","Cell.line":"None","subunits.UniProt.IDs.":"O00141;P10636;P27348","subunits.Entrez.IDs.":"6446;4137;10971","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0001932","GO.description":"regulation of protein phosphorylation","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":15650334,"subunits.Protein.name.":"Serine/threonine-protein kinase Sgk1 ;Microtubule-associated protein tau ;14-3-3 protein theta","subunits.Gene.name.":"SGK1;MAPT;YWHAQ","subunits.Gene.name.syn.":"SGK;MAPTL MTBT1 TAU;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6243,"ComplexName":"AJUBA-GFI1-HDAC2 complex","Organism":"Human","Synonyms":"None","Cell.line":"Jurkat T cell nuclear extracts","subunits.UniProt.IDs.":"Q92769;Q96IF1;Q99684","subunits.Entrez.IDs.":"3066;84962;2672","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0071-molecular sieving","GO.ID":"GO:0045892","GO.description":"negative regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.03","FunCat.description":"transcription repression","PubMed.ID":18805794,"subunits.Protein.name.":"Histone deacetylase 2;LIM domain-containing protein ajuba;Zinc finger protein Gfi-1","subunits.Gene.name.":"HDAC2;AJUBA;GFI1","subunits.Gene.name.syn.":"None;JUB;ZNF163","Disease.comment":"It has been demonstrated that SCN (severe congenital neutropenia)-associated mutations in GFI1 generate dominant-negative-acting proteins (GFI1N382S), which selectively deprepress GFI1 target genes such as CSF1. A SNAG domain mutant protein (Gfi1P2A) also functioned in a dominant negative manner;however, a protein with both mutations (Gfi1P2A\\u0002N382S) lacked dominant negative activity.","Subunits.comment":"None","Complex.comment":"The majority of Gfi1 repression activity is dependent upon HDAC function. However, a residual repression activity is present in inhibitor-treated samples suggesting Gfi1 and Ajuba utilize as yet unidentified non-HDAC-dependent repression mechanism(s).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6244,"ComplexName":"AJUBA-GFI1-HDAC3 complex","Organism":"Human","Synonyms":"None","Cell.line":"Jurkat T cell nuclear extracts","subunits.UniProt.IDs.":"O15379;Q96IF1;Q99684","subunits.Entrez.IDs.":"8841;84962;2672","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0071-molecular sieving","GO.ID":"GO:0045892","GO.description":"negative regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.03","FunCat.description":"transcription repression","PubMed.ID":18805794,"subunits.Protein.name.":"Histone deacetylase 3;LIM domain-containing protein ajuba;Zinc finger protein Gfi-1","subunits.Gene.name.":"HDAC3;AJUBA;GFI1","subunits.Gene.name.syn.":"None;JUB;ZNF163","Disease.comment":"It has been demonstrated that SCN (severe congenital neutropenia)-associated mutations in GFI1 generate dominant-negative-acting proteins (GFI1N382S), which selectively deprepress GFI1 target genes such as CSF1. A SNAG domain mutant protein (Gfi1P2A) also functioned in a dominant negative manner;however, a protein with both mutations (Gfi1P2A\\u0002N382S) lacked dominant negative activity.","Subunits.comment":"None","Complex.comment":"The majority of Gfi1 repression activity is dependent upon HDAC function. However, a residual repression activity is present in inhibitor-treated samples suggesting Gfi1 and Ajuba utilize as yet unidentified non-HDAC-dependent repression mechanism(s).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6245,"ComplexName":"Telomerase holoenzyme","Organism":"Human","Synonyms":"None","Cell.line":"HeLa S3 cells","subunits.UniProt.IDs.":"O14746;O60832;Q86US8;Q9BUR4;Q9NPE3;Q9NX24;Q9NY12","subunits.Entrez.IDs.":"7015;1736;23293;55135;55505;55651;54433","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0003720;GO:0005697","GO.description":"telomerase activity;telomerase holoenzyme complex","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":19179534,"subunits.Protein.name.":"Telomerase reverse transcriptase ;H/ACA ribonucleoprotein complex subunit 4 ;Telomerase-binding protein EST1A ;Telomerase Cajal body protein 1 ;H/ACA ribonucleoprotein complex subunit 3 ;H/ACA ribonucleoprotein complex subunit 2 ;H/ACA ribonucleoprotein complex subunit 1","subunits.Gene.name.":"TERT;DKC1;SMG6;WRAP53;NOP10;NHP2;GAR1","subunits.Gene.name.syn.":"EST2 TCS1 TRT;NOLA4;C17orf31 EST1A KIAA0732;TCAB1 WDR79;NOLA3;NOLA2;NOLA1","Disease.comment":"Telomerase is associated with various diseases such as cancer, dyskeratosis congenita, bone marrow failure and idiopathic pulmonary fibrosis","Subunits.comment":"None","Complex.comment":".","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6246,"ComplexName":"BBS4 centriolar satellite complex","Organism":"Human","Synonyms":"BBS4-PCM1-CEP131 complex; BBS4-PCM1-AZI1 complex","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"Q15154;Q96RK4;Q9UPN4","subunits.Entrez.IDs.":"5108;585;22994","Protein.complex.purification.method":"MI:0029- cosedimentation through density gradients","GO.ID":"GO:0005929;GO:0042073","GO.description":"cilium;intraciliary transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":24550735,"subunits.Protein.name.":"Pericentriolar material 1 protein ;Bardet-Biedl syndrome 4 protein;Centrosomal protein of 131 kDa","subunits.Gene.name.":"PCM1;BBS4;CEP131","subunits.Gene.name.syn.":";None;AZI1 KIAA1118","Disease.comment":"Bardet-Biedl syndrome (BBS) is a well-known ciliopathy with mutations reported in 18 different genes. Most of the proteinproducts of the BBS genes localize at or near the primary cilium and the centrosome. Near the centrosome, BBS proteinsinteract with centriolar satellite proteins, and the BBSome (a complex of seven BBS proteins) is believed to play a role intransporting ciliary membrane proteins.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6247,"ComplexName":"BBS-chaperonin complex","Organism":"Human","Synonyms":"BBS/CCT complex","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"P17987;P48643;P49368;P50990;P50991;P78371;Q6ZW61;Q8IWZ6;Q8TAM1;Q9NPJ1","subunits.Entrez.IDs.":"6950;22948;7203;10694;10575;10576;166379;55212;79738;8195","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005929;GO:0051131;GO:0042073","GO.description":"cilium;chaperone-mediated protein complex assembly;intraciliary transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20080638,"subunits.Protein.name.":"T-complex protein 1 subunit alpha;T-complex protein 1 subunit epsilon;T-complex protein 1 subunit gamma;T-complex protein 1 subunit theta;T-complex protein 1 subunit delta;T-complex protein 1 subunit beta;Bardet-Biedl syndrome 12 protein;Bardet-Biedl syndrome 7 protein;Bardet-Biedl syndrome 10 protein;McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin","subunits.Gene.name.":"TCP1;CCT5;CCT3;CCT8;CCT4;CCT2;BBS12;BBS7;BBS10;MKKS","subunits.Gene.name.syn.":"CCT1 CCTA;CCTE KIAA0098;CCTG TRIC5;C21orf112 CCTQ KIAA0002;CCTD SRB;99D8.1 CCTB;C4orf24;BBS2L1;C12orf58;BBS6","Disease.comment":"Bardet-Biedl syndrome (BBS) is a human genetic disorder resultingin obesity, retinal degeneration, polydactyly, and nephropathy.Recent studies indicate that trafficking defects to the ciliary membraneare involved in this syndrome.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6248,"ComplexName":"CSF3R-FBXW7-GSK3B complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"P49841;Q969H0;Q99062","subunits.Entrez.IDs.":"2932;55294;1441","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0031146;GO:0030851;GO:0038158","GO.description":"SCF-dependent proteasomal ubiquitin-dependent protein catabolic process;granulocyte differentiation;granulocyte colony-stimulating factor signaling pathway","FunCat.ID":"43.03.07.02.02","FunCat.description":"granulocyte","PubMed.ID":23820376,"subunits.Protein.name.":"Glycogen synthase kinase-3 beta;F-box/WD repeat-containing protein 7;Granulocyte colony-stimulating factor receptor","subunits.Gene.name.":"GSK3B;FBXW7;CSF3R","subunits.Gene.name.syn.":"None;FBW7, FBX30, SEL10;GCSFR","Disease.comment":"Fbw7 also interacts with and degrades G-CSFR-T718 (a truncated mutant of G-CSFR found in severe congenital neutropenia/acute myeloid leukemia (SCN/AML patients)) though at a quite slower rate compared to G-CSFR.","Subunits.comment":"None","Complex.comment":"Fbw7 in cooperation with GSK3B negatively modulates G-CSFR protein steady state levels by promoting its degradation and thus regulates granulocytic differentiation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6249,"ComplexName":"MIB complex","Organism":"Human","Synonyms":"Mitochondrial intermembrane space bridging complex","Cell.line":"Human osteosarcoma 143B cells","subunits.UniProt.IDs.":"O75431;Q13505;Q16891;Q5TGZ0;Q5XKP0;Q6UXV4;Q9BRQ6;Q9BUR5;Q9NVH1;Q9NX63;Q9Y512","subunits.Entrez.IDs.":"10651;4580;10989;440574;125988;139322;84303;79135;55735;54927;25813","Protein.complex.purification.method":"MI:0276- blue native page","GO.ID":"GO:0044284;GO:0042407","GO.description":"mitochondrial crista junction;cristae formation","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26477565,"subunits.Protein.name.":"Metaxin-2 ;Metaxin-1 ;MICOS complex subunit MIC60 ;MICOS complex subunit MIC10 ;MICOS complex subunit MIC13 ;MICOS complex subunit MIC27 ;MICOS complex subunit MIC25 ;MICOS complex subunit MIC26 ;DnaJ homolog subfamily C member 11;MICOS complex subunit MIC19 ;Sorting and assembly machinery component 50 homolog","subunits.Gene.name.":"MTX2;MTX1;IMMT;MINOS1;MIC13;APOOL;CHCHD6;APOO;DNAJC11;CHCHD3;SAMM50","subunits.Gene.name.syn.":";MTX MTXN;HMP MIC60 MINOS2;C1orf151 MIC10;C19orf70 QIL1;CXorf33 FAM121A MIC27;CHCM1 MIC25;FAM121B MIC23 MIC26;;MIC19 MINOS3;SAM50","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6250,"ComplexName":"LPA(2)-NHERF2-PLC-beta3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q01970;Q15599;Q9HBW0","subunits.Entrez.IDs.":"5331;9351;9170","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0096-pull down","GO.ID":"GO:0019216","GO.description":"regulation of lipid metabolic process","FunCat.ID":"01.06.10","FunCat.description":"regulation of lipid, fatty acid and isoprenoid metabolism","PubMed.ID":15143197,"subunits.Protein.name.":"1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3;Na(+)/H(+) exchange regulatory cofactor NHE-RF2;Lysophosphatidic acid receptor 2","subunits.Gene.name.":"PLCB3;SLC9A3R2;LPAR2","subunits.Gene.name.syn.":"None;NHERF2;EDG4, LPA2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6251,"ComplexName":"Shc-ERalpha-IGF-1R complex","Organism":"Human","Synonyms":"SHC1-ESR1-","Cell.line":"MCF-7 cells","subunits.UniProt.IDs.":"P03372;P08069;P29353","subunits.Entrez.IDs.":"2099;3480;6464","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0043405","GO.description":"regulation of MAP kinase activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":14764897,"subunits.Protein.name.":"Estrogen receptor;Insulin-like growth factor 1 receptor;SHC-transforming protein 1","subunits.Gene.name.":"ESR1;IGF1R;SHC1","subunits.Gene.name.syn.":"ESR, NR3A1;None;SHC SHCA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6252,"ComplexName":"Rabep1-Ap1g1-Ap1s1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"Fibroblast cells","subunits.UniProt.IDs.":"O35551;P22892;P61967","subunits.Entrez.IDs.":"54189;11765;11769","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0096- pull down","GO.ID":"GO:0055038","GO.description":"recycling endosome membrane","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":12773381,"subunits.Protein.name.":"Rab GTPase-binding effector protein 1 ;AP-1 complex subunit gamma-1;AP-1 complex subunit sigma-1A","subunits.Gene.name.":"Rabep1;Ap1g1;Ap1s1","subunits.Gene.name.syn.":"Rab5ep Rabpt5 Rabpt5a;Adtg Clapg1;Ap19","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6253,"ComplexName":"myosin-Vb-Rab11-FIP2-Rab11a complex","Organism":"Human","Synonyms":"HeLa cells","Cell.line":"None","subunits.UniProt.IDs.":"P62491;Q7L804;Q9ULV0","subunits.Entrez.IDs.":"8766;22841;4645","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:0016192","GO.description":"vesicle-mediated transport","FunCat.ID":"20.09.07","FunCat.description":"vesicular transport (Golgi network, etc.)","PubMed.ID":12393859,"subunits.Protein.name.":"Ras-related protein Rab-11A;Rab11 family-interacting protein 2 ;Unconventional myosin-Vb","subunits.Gene.name.":"RAB11A;RAB11FIP2;MYO5B","subunits.Gene.name.syn.":"RAB11;KIAA0941;KIAA1119","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6254,"ComplexName":"GPC-4.1R-p55 complex","Organism":"Human","Synonyms":"None","Cell.line":"erythrocyte cells","subunits.UniProt.IDs.":"P04921;P11171;Q00013","subunits.Entrez.IDs.":"2995;2035;4354","Protein.complex.purification.method":"MI:0107- surface plasmon resonance","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":10831591,"subunits.Protein.name.":"Glycophorin-C ;Protein 4.1 ;55 kDa erythrocyte membrane protein","subunits.Gene.name.":"GYPC;EPB41;MPP1","subunits.Gene.name.syn.":"GLPC GPC;E41P;DXS552E EMP55","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6255,"ComplexName":"MICOS complex","Organism":"Human","Synonyms":"Mitochondrial contact site and cristae junction organizing system","Cell.line":"Human osteosarcoma 143B cells","subunits.UniProt.IDs.":"Q16891;Q5TGZ0;Q5XKP0;Q6UXV4;Q9BRQ6;Q9BUR5;Q9NX63","subunits.Entrez.IDs.":"10989;440574;125988;139322;84303;79135;54927","Protein.complex.purification.method":"MI:0276- blue native page","GO.ID":"GO:0061617;GO:0042407","GO.description":"MICOS complex;cristae formation","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26477565,"subunits.Protein.name.":"MICOS complex subunit MIC60 ;MICOS complex subunit MIC10 ;MICOS complex subunit MIC13 ;MICOS complex subunit MIC27 ;MICOS complex subunit MIC25 ;MICOS complex subunit MIC26 ;MICOS complex subunit MIC19","subunits.Gene.name.":"IMMT;MINOS1;MIC13;APOOL;CHCHD6;APOO;CHCHD3","subunits.Gene.name.syn.":"HMP MIC60 MINOS2;C1orf151 MIC10;C19orf70 QIL1;CXorf33 FAM121A MIC27;CHCM1 MIC25;FAM121B MIC23 MIC26;MIC19 MINOS3","Disease.comment":"Several mitochondrial disorders in humans areoften accompanied by alterations of mitochondrial ultrastructure including MERRF syndrome (Myoclonic epilepsy with ragged red fibers), BTHS (Barth syndrome), fatal neonatal lactic acidosis, mtDNA defects and hypertrophic cardiomyopathy and loss of CJs with the formation of concentric stacks of cristae membrane are some of the hallmarks observed in mitochondria from such patients.","Subunits.comment":"None","Complex.comment":"The mitochondrial contact site and cristae junction (CJ) organizing system (MICOS) dynamically regulate mitochondrial membrane architecture.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6256,"ComplexName":"GM-CSF-receptor complex","Organism":"Human","Synonyms":"GM-CSF-CSF2RA-CSF2RB complex","Cell.line":"transfection of soluble receptor components in Sf21 cells","subunits.UniProt.IDs.":"P04141;P15509;P32927","subunits.Entrez.IDs.":"1437;1438;1439","Protein.complex.purification.method":"MI:0071-molecular sieving","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":12393492,"subunits.Protein.name.":"Granulocyte-macrophage colony-stimulating factor;Granulocyte-macrophage colony-stimulating factor receptor subunit alpha;Cytokine receptor common subunit beta","subunits.Gene.name.":"CSF2;CSF2RA;CSF2RB","subunits.Gene.name.syn.":"GMCSF;CSF2R, CSF2RY;IL3RB, IL5RB","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The used recombinant proteins display the soluble part of the GM-CSF receptor subunits CSF2RA (1-320),CSF2RB (1-438).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6257,"ComplexName":"ANKS6-NEK8-INVS-NPHP3 complex","Organism":"Human","Synonyms":"NPHP16-NPHP9-NPHP2-NPHP3 complex","Cell.line":"HEK-293T cells","subunits.UniProt.IDs.":"Q68DC2;Q7Z494;Q86SG6;Q9Y283","subunits.Entrez.IDs.":"203286;27031;284086;27130","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005929;GO:0001822","GO.description":"cilium;kidney development","FunCat.ID":"47.03.07.01","FunCat.description":"kidney","PubMed.ID":23793029,"subunits.Protein.name.":"Ankyrin repeat and SAM domain-containing protein 6;Nephrocystin-3;Serine/threonine-protein kinase Nek8;Inversin","subunits.Gene.name.":"ANKS6;NPHP3;NEK8;INVS","subunits.Gene.name.syn.":"ANKRD14 PKDR1 SAMD6;KIAA2000;JCK, NEK12A, NPHP9;INV NPHP2","Disease.comment":"Nephronophthisis is the most frequent genetic cause of renal failure in children, presenting  with cystic kidney disease combined with extrarenal manifestations, such as retinitis pigmentosa (Senior-L\\u00f8ken syndrome), liver fibrosis, cerebellar vermis hypoplasia (Joubert syndrome), situs inversus or cardiac malformations. Because most NPHP gene products  localize to the cilium or its associated structures, nephronophthisis and related syndromes, such as Joubert syndrome and Meckel-Gruber syndrome (MKS), have been termed ciliopathies.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6258,"ComplexName":"FXN-ISCU-NFS1-ISD11 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"Q16595;Q8K215;Q9D7P6;Q9Z1J3","subunits.Entrez.IDs.":"2395;380840;66383;18041","Protein.complex.purification.method":"MI:0096- pull down;MI:0019- coimmunoprecipitation","GO.ID":"GO:1903329;GO:0005739","GO.description":"regulation of iron-sulfur cluster assembly;mitochondrion","FunCat.ID":"70.16","FunCat.description":"mitochondrion","PubMed.ID":21298097,"subunits.Protein.name.":"Frataxin, mitochondrial ;LYR motif-containing protein 4;Iron-sulfur cluster assembly enzyme ISCU, mitochondrial ;Cysteine desulfurase, mitochondrial","subunits.Gene.name.":"FXN;Lyrm4;Iscu;Nfs1","subunits.Gene.name.syn.":"FRDA X25;Isd11;Nifun;Nifs","Disease.comment":"OMIM:229300 Friedreich ataxia","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6259,"ComplexName":"USH2 complex","Organism":"Human","Synonyms":"WHRN-USH2A-PDZD7-GPR98 complex; Usher Syndrome Type 2 complex","Cell.line":"None","subunits.UniProt.IDs.":"O75445;Q8WXG9;Q9H5P4;Q9P202","subunits.Entrez.IDs.":"7399;84059;79955;25861","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25406310,"subunits.Protein.name.":"Usherin ;G-protein coupled receptor 98 ;PDZ domain-containing protein 7;Whirlin","subunits.Gene.name.":"USH2A;GPR98;PDZD7;WHRN","subunits.Gene.name.syn.":";KIAA0686 KIAA1943 MASS1 VLGR1;PDZK7;DFNB31 KIAA1526","Disease.comment":"OMIM:276901 Usher syndrome, type 2A, (PMID:25406310).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6260,"ComplexName":"MPP7-DLG1-LIN7A complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"O14910;Q12959;Q5T2T1","subunits.Entrez.IDs.":"8825;1739;143098","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0097025","GO.description":"MPP7-DLG1-LIN7 complex","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":17237226,"subunits.Protein.name.":"Protein lin-7 homolog A;Disks large homolog 1 ;MAGUK p55 subfamily member 7","subunits.Gene.name.":"LIN7A;DLG1;MPP7","subunits.Gene.name.syn.":"MALS1 VELI1;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6261,"ComplexName":"Histone-2-Histone-4-ASF1-MCM2 complex","Organism":"Human","Synonyms":"HIST1H3A-HIST1H4A-ASF1-MCM2 complex","Cell.line":"None","subunits.UniProt.IDs.":"P49736;P62805;P68431;Q07955","subunits.Entrez.IDs.":"4171;None;None;6426","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0031497","GO.description":"chromatin assembly","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26186914,"subunits.Protein.name.":"DNA replication licensing factor MCM2 ;Histone H4;Histone H3.1;Serine/arginine-rich splicing factor 1","subunits.Gene.name.":"MCM2;HIST1H4A;;HIST1H3A;;SRSF1","subunits.Gene.name.syn.":"BM28 CCNL1 CDCL1 KIAA0030;H4/A H4FA; H4/I H4FI; H4/G H4FG; H4/B H4FB; H4/J H4FJ; H4/C H4FC; H4/H H4FH; H4/M H4FM; H4/E H4FE; H;H3FA; H3FL; H3FC; H3FB; H3FD; H3FI; H3FH; H3FK; H3FF; H3FJ;ASF SF2 SF2P33 SFRS1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6262,"ComplexName":"L11-HDM2-p53-ARF complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P02340;P23804;Q64364;Q9CXW4","subunits.Entrez.IDs.":"22059;17246;12578;67025","Protein.complex.purification.method":"MI:0402- chromatin immunoprecipitation assays","GO.ID":"GO:0090071;GO:0030308;GO:0008284","GO.description":"negative regulation of ribosome biogenesis;negative regulation of cell growth;positive regulation of cell proliferation","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":14612427,"subunits.Protein.name.":"Cellular tumor antigen p53 ;E3 ubiquitin-protein ligase Mdm2 ;Tumor suppressor ARF ;60S ribosomal protein L11","subunits.Gene.name.":"Tp53;Mdm2;Cdkn2a;Rpl11","subunits.Gene.name.syn.":"P53 Trp53;;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6263,"ComplexName":"MPP7-DLG1-LIN7C complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"Q12959;Q5T2T1;Q9NUP9","subunits.Entrez.IDs.":"1739;143098;55327","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0097025","GO.description":"MPP7-DLG1-LIN7 complex","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":17237226,"subunits.Protein.name.":"Disks large homolog 1 ;MAGUK p55 subfamily member 7;Protein lin-7 homolog C","subunits.Gene.name.":"DLG1;MPP7;LIN7C","subunits.Gene.name.syn.":";;MALS3 VELI3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6264,"ComplexName":"DLG5-SORBS3-CTNNB1 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS-7 cells","subunits.UniProt.IDs.":"O60504;P35222;Q8TDM6","subunits.Entrez.IDs.":"10174;1499;9231","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005911","GO.description":"cell-cell junction","FunCat.ID":"70.06.04","FunCat.description":"intercellular junction (gap junction/adherens junction)","PubMed.ID":12657639,"subunits.Protein.name.":"Vinexin ;Catenin beta-1;Disks large homolog 5","subunits.Gene.name.":"SORBS3;CTNNB1;DLG5","subunits.Gene.name.syn.":"SCAM1;CTNNB;KIAA0583 PDLG","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6265,"ComplexName":"Dlgap1-Dlg4-Begain complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O88881;P31016;P97836","subunits.Entrez.IDs.":"79146;29495;65040","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0097060;GO:0014069","GO.description":"synaptic membrane;postsynaptic density","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":9756850,"subunits.Protein.name.":"Brain-enriched guanylate kinase-associated protein;Disks large homolog 4;Disks large-associated protein 1","subunits.Gene.name.":"Begain;Dlg4;Dlgap1","subunits.Gene.name.syn.":";Dlgh4, Psd95;Gkap","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6266,"ComplexName":"Ubiquitin E3 ligase (CUL3, KLHL3, WNK4)","Organism":"Human","Synonyms":"CUL3-KLHL3-WNK4 E3 ligase complex","Cell.line":"HEK-293 cells","subunits.UniProt.IDs.":"Q13618;Q96J92;Q9UH77","subunits.Entrez.IDs.":"8452;65266;26249","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0016874;GO:0016567;GO:0050801;GO:0000151","GO.description":"ligase activity;protein ubiquitination;ion homeostasis;ubiquitin ligase complex","FunCat.ID":"14.07.05;34.01","FunCat.description":"modification by ubiquitination, deubiquitination;homeostasis","PubMed.ID":23387299,"subunits.Protein.name.":"Cullin-3;Serine/threonine-protein kinase WNK4;Kelch-like protein 3","subunits.Gene.name.":"CUL3;WNK4;KLHL3","subunits.Gene.name.syn.":"KIAA0617;PRKWNK4;KIAA1129","Disease.comment":"The CUL3-KLHL3 E3 ligase complex is mutated in Gordon hypertension syndrome (= Pseudohypoaldosteronismtype II = PHAII).","Subunits.comment":"None","Complex.comment":"CUL3 assembles with BTB proteins (e.g. KLHL3) to form Cullin-RING E3 ubiquitin ligase complexes. The CUL3-KLHL3 E3 ligase complex regulates blood pressure via its ability to interact with and ubiquitylate WNK isoforms. Immunoprecipitation studies confirmed that the wild-type WNK4 robustly bound to KLHL3, but interaction with either disease-causing WNK4 mutant tested was strikingly impaired.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6267,"ComplexName":"Ubiquitin E3 ligase (CUL3, KLHL3)","Organism":"Human","Synonyms":"CUL3\\u2013KLHL3 complex","Cell.line":"HEK-293 cells","subunits.UniProt.IDs.":"Q13618;Q9UH77","subunits.Entrez.IDs.":"8452;26249","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0016874;GO:0016567;GO:0050801;GO:0000151","GO.description":"ligase activity;protein ubiquitination;ion homeostasis;ubiquitin ligase complex","FunCat.ID":"14.07.05;34.01","FunCat.description":"modification by ubiquitination, deubiquitination;homeostasis","PubMed.ID":23387299,"subunits.Protein.name.":"Cullin-3;Kelch-like protein 3","subunits.Gene.name.":"CUL3;KLHL3","subunits.Gene.name.syn.":"KIAA0617;KIAA1129","Disease.comment":"The CUL3-KLHL3 E3 ligase complex is mutated in Gordon hypertension syndrome (= Pseudohypoaldosteronismtype II = PHAII).","Subunits.comment":"None","Complex.comment":"CUL3 assembles with BTB proteins (e.g. KLHL3) to form Cullin-RING E3 ubiquitin ligase complexes. The CUL3-KLHL3 E3 ligase complex regulates blood pressure via its ability to interact with and ubiquitylate WNK isoforms.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6268,"ComplexName":"Cullin-RING E3 ubiquitin ligase complex","Organism":"Human","Synonyms":"ASB9-ELOBC-CUL5 quaternary complex; CRL","Cell.line":"None","subunits.UniProt.IDs.":"Q15369;Q15370;Q93034;Q96DX5","subunits.Entrez.IDs.":"6921;6923;8065;140462","Protein.complex.purification.method":"MI:0069-mass spectrometry studies of complexes;MI:0013-biophysical","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23837592,"subunits.Protein.name.":"Transcription elongation factor B polypeptide 1;Transcription elongation factor B polypeptide 2;Cullin-5;Ankyrin repeat and SOCS box protein 9","subunits.Gene.name.":"TCEB1;TCEB2;CUL5;ASB9","subunits.Gene.name.syn.":"elongin c;elongin b;VACM1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cullin RING E3 ubiquitin ligase (CRL) complexes catalyze the specific polyubiquitination of cellular proteins to target them for degradation by the proteasome. ASB9 is unstable alone but forms a stable ternary complex with EloBC that binds with high affinity to the Cullin 5 N-terminal domain (Cul5NTD) but not to Cul2NTD. The application of several biophysical techniques are described including differential scanning fluorimetry, isothermal titration calorimetry (ITC), nanoelectrospray ionization, and ion-mobility mass spectrometry (IM-MS) to provide structural and thermodynamic information for the quaternary ASB CRL complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6269,"ComplexName":"DLL1-CTNNB1-CDH2 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293E cells","subunits.UniProt.IDs.":"O00548;P19022;P35222","subunits.Entrez.IDs.":"28514;1000;1499","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0005912;GO:0071896","GO.description":"adherens junction;protein localization to adherens junction","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":15908431,"subunits.Protein.name.":"Delta-like protein 1;Cadherin-2 ;Catenin beta-1","subunits.Gene.name.":"DLL1;CDH2;CTNNB1","subunits.Gene.name.syn.":"None;CDHN NCAD;CTNNB","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Experimental results suggest that Dll1 is presented on the surface of adherens junctions formed at the apical termini of processes through interaction with MAGI1 to activate Notch on neighboring cells in the developing central nervous system.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6270,"ComplexName":"DMTN-SYNE1- complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q08495;Q8NF91","subunits.Entrez.IDs.":"2039;23345","Protein.complex.purification.method":"None","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":22927433,"subunits.Protein.name.":"Dematin ;Nesprin-1","subunits.Gene.name.":"DMTN;SYNE1","subunits.Gene.name.syn.":"DMT EPB49;C6orf98 KIAA0796 KIAA1262 KIAA1756 MYNE1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6271,"ComplexName":"CASQ2-RYR1-ASPH-TRDN complex","Organism":"Human","Synonyms":"None","Cell.line":"cardiac muscle cells","subunits.UniProt.IDs.":"F1PIS0;P12637;P82179;Q28264","subunits.Entrez.IDs.":"None;483134;403776;403846","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0004- affinity chromatography technologies","GO.ID":"GO:0010880;GO:0016529","GO.description":"regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum;sarcoplasmic reticulum","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":9287354,"subunits.Protein.name.":"Uncharacterized protein;Calsequestrin-2 ;Triadin;Junctional sarcoplasmic reticulum protein","subunits.Gene.name.":"RYR1;CASQ2;TRDN;ASPH","subunits.Gene.name.syn.":";;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Canis lupus familiaris (Dog) (Canis familiaris);Canis lupus familiaris (Dog) (Canis familiaris);Canis lupus familiaris (Dog) (Canis familiaris);Canis lupus familiaris (Dog) (Canis familiaris)"}
{"ComplexID":6272,"ComplexName":"CASQ2-RYR1-ASPH-TRDN complex","Organism":"Human","Synonyms":"None","Cell.line":"cardiac muscle cells","subunits.UniProt.IDs.":"F1PIS0;P12637;P82179;Q28264","subunits.Entrez.IDs.":"None;483134;403776;403846","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation;MI:0004- affinity chromatography technologies","GO.ID":"GO:0010880;GO:0016529","GO.description":"regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum;sarcoplasmic reticulum","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":9287354,"subunits.Protein.name.":"Uncharacterized protein;Calsequestrin-2 ;Triadin;Junctional sarcoplasmic reticulum protein","subunits.Gene.name.":"RYR1;CASQ2;TRDN;ASPH","subunits.Gene.name.syn.":";;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Canis lupus familiaris (Dog) (Canis familiaris);Canis lupus familiaris (Dog) (Canis familiaris);Canis lupus familiaris (Dog) (Canis familiaris);Canis lupus familiaris (Dog) (Canis familiaris)"}
{"ComplexID":6273,"ComplexName":"Lep-Lepr quaternary protein","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P41160;P48356","subunits.Entrez.IDs.":"16846;16847","Protein.complex.purification.method":"MI:0065- isothermal titration calorimetry;MI:0040- electron microscopy","GO.ID":"GO:0033210","GO.description":"leptin-mediated signaling pathway","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23063524,"subunits.Protein.name.":"Leptin ;Leptin receptor","subunits.Gene.name.":"Lep;Lepr","subunits.Gene.name.syn.":"Ob;Db Obr","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6274,"ComplexName":"HEXA-HEXB complex","Organism":"Human","Synonyms":"beta-hexosaminidase A complex","Cell.line":"placenta cells","subunits.UniProt.IDs.":"P06865;P07686","subunits.Entrez.IDs.":"3073;3074","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0004563;GO:0005975;GO:0006687;GO:0030203;GO:0004553","GO.description":"beta-N-acetylhexosaminidase activity;carbohydrate metabolic process;glycosphingolipid metabolic process;glycosaminoglycan metabolic process;hydrolase activity, hydrolyzing O-glycosyl compounds","FunCat.ID":"1.05","FunCat.description":"C-compound and carbohydrate metabolism","PubMed.ID":16698036,"subunits.Protein.name.":"Beta-hexosaminidase subunit alpha ;Beta-hexosaminidase subunit beta","subunits.Gene.name.":"HEXA;HEXB","subunits.Gene.name.syn.":";","Disease.comment":"OMIM:272800 Tay-Sachs disease (PMID::2141777).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6275,"ComplexName":"HEXB homodimer","Organism":"Human","Synonyms":"beta-Hexosaminidase B complex","Cell.line":"placenta cells","subunits.UniProt.IDs.":"P07686","subunits.Entrez.IDs.":"3074","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0004563;GO:0005975;GO:0006687;GO:0030203;GO:0004553","GO.description":"beta-N-acetylhexosaminidase activity;carbohydrate metabolic process;glycosphingolipid metabolic process;glycosaminoglycan metabolic process;hydrolase activity, hydrolyzing O-glycosyl compounds","FunCat.ID":"1.05","FunCat.description":"C-compound and carbohydrate metabolism","PubMed.ID":12662933,"subunits.Protein.name.":"Beta-hexosaminidase subunit beta","subunits.Gene.name.":"HEXB","subunits.Gene.name.syn.":"None","Disease.comment":"OMIM:268800 Sandhoff disease (PMID: 2147027).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":6276,"ComplexName":"Factor-Xa-TFPI-factor-VIIa-tissue factor complex","Organism":"Human","Synonyms":"F10-TFPI-F7-F3 complex","Cell.line":"None","subunits.UniProt.IDs.":"P00742;P08709;P10646;P13726","subunits.Entrez.IDs.":"2159;2155;7035;2152","Protein.complex.purification.method":"MI:0401- biochemical","GO.ID":"GO:0030193","GO.description":"regulation of blood coagulation","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":7662667,"subunits.Protein.name.":"Coagulation factor X ;Coagulation factor VII ;Tissue factor pathway inhibitor ;Tissue factor","subunits.Gene.name.":"F10;F7;TFPI;F3","subunits.Gene.name.syn.":";;LACI TFPI1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6277,"ComplexName":"Rev1-Rev3-Rev7-Polkappa complex","Organism":"Human","Synonyms":"REV1-REV3L-MAD2L2-POLK complex","Cell.line":"None","subunits.UniProt.IDs.":"O60673;Q9UBT6;Q9UBZ9;Q9UI95","subunits.Entrez.IDs.":"5980;51426;51455;10459","Protein.complex.purification.method":"MI:0055- fluorescent resonance energy transfer","GO.ID":"GO:1904331","GO.description":"regulation of error-prone translesion synthesis","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23143872,"subunits.Protein.name.":"DNA polymerase zeta catalytic subunit ;DNA polymerase kappa ;DNA repair protein REV1 ;Mitotic spindle assembly checkpoint protein MAD2B","subunits.Gene.name.":"REV3L;POLK;REV1;MAD2L2","subunits.Gene.name.syn.":"POLZ REV3;DINB1;REV1L;MAD2B REV7","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6278,"ComplexName":"Cd22-Ship-Grb2-Shc complex","Organism":"Mouse","Synonyms":"None","Cell.line":"B-lymphocytes; spleen","subunits.UniProt.IDs.":"P35329;P98083;Q60631;Q9ES52","subunits.Entrez.IDs.":"12483;20416;14784;16331","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0090279","GO.description":"regulation of calcium ion import","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":10748054,"subunits.Protein.name.":"B-cell receptor CD22 ;SHC-transforming protein 1 ;Growth factor receptor-bound protein 2;Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1","subunits.Gene.name.":"Cd22;Shc1;Grb2;Inpp5d","subunits.Gene.name.syn.":"Lyb-8 Siglec2;Shc ShcA;None;7a33 Ship Ship1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6279,"ComplexName":"p65-IkappaBalpha-beta-arrestin-iNOS complex","Organism":"Mouse","Synonyms":"Rela-Nfkbia-Arrb2-Nos2 complex","Cell.line":"HEK-293 cells","subunits.UniProt.IDs.":"Q04207;Q06518;Q91YI4;Q9Z1E3","subunits.Entrez.IDs.":"19697;24599;216869;18035","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007263","GO.description":"nitric oxide mediated signal transduction","FunCat.ID":"30.01.09.01","FunCat.description":"NO mediated signal transduction","PubMed.ID":21464294,"subunits.Protein.name.":"Transcription factor p65;Nitric oxide synthase, inducible;Beta-arrestin-2;NF-kappa-B inhibitor alpha","subunits.Gene.name.":"Rela;Nos2;Arrb2;Nfkbia","subunits.Gene.name.syn.":"Nfkb3;None;None;Ikba","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Rattus norvegicus (Rat);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6280,"ComplexName":"NUB1L-UFD1-NPL4-NEDD8 complex","Organism":"Human","Synonyms":"NUB1-UFD1L-NPLOC4-NEDD8 complex","Cell.line":"HEK-293T cells","subunits.UniProt.IDs.":"Q15843;Q8TAT6;Q92890;Q9Y5A7","subunits.Entrez.IDs.":"4738;55666;7353;51667","Protein.complex.purification.method":"MI:0096- pull down","GO.ID":"GO:2000434","GO.description":"regulation of protein neddylation","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":24019527,"subunits.Protein.name.":"NEDD8 ;Nuclear protein localization protein 4 homolog ;Ubiquitin fusion degradation protein 1 homolog ;NEDD8 ultimate buster 1","subunits.Gene.name.":"NEDD8;NPLOC4;UFD1L;NUB1","subunits.Gene.name.syn.":";KIAA1499 NPL4;;NYREN18","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6281,"ComplexName":"PAI-1-uPA-uPAR-LRP complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P06869;P22777;P35456;Q91ZX7","subunits.Entrez.IDs.":"18792;None;18793;16971","Protein.complex.purification.method":"MI:0047- far western blotting","GO.ID":"GO:0030336","GO.description":"negative regulation of cell migration","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":9497365,"subunits.Protein.name.":"Urokinase-type plasminogen activator ;Plasminogen activator inhibitor 1 ;Urokinase plasminogen activator surface receptor ;Prolow-density lipoprotein receptor-related protein 1","subunits.Gene.name.":"Plau;Serpine1;Plaur;Lrp1","subunits.Gene.name.syn.":";Mr1 Pai1 Planh1;;A2mr","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6282,"ComplexName":"G alpha-13-Hax-1-cortactin-Rac complex","Organism":"Human","Synonyms":"None","Cell.line":"COS-7 cells","subunits.UniProt.IDs.":"O00165;P31749;Q14247;Q14344","subunits.Entrez.IDs.":"10456;207;2017;10672","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0016477","GO.description":"cell migration","FunCat.ID":"34.05.01","FunCat.description":"cell migration","PubMed.ID":15339924,"subunits.Protein.name.":"HCLS1-associated protein X-1;RAC-alpha serine/threonine-protein kinase;Src substrate cortactin;Guanine nucleotide-binding protein subunit alpha-13","subunits.Gene.name.":"HAX1;AKT1;CTTN;GNA13","subunits.Gene.name.syn.":"HS1BP1;PKB, RAC;EMS1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"By tethering G alpha-\\u000113 to cortactin in a complex containing Rac, Hax-1 provides a signaling nexus that facilitates the dynamic and uninterrupted transmission of signals from G alpha-\\u000113 to cortactin through Rac to promote cell protrusion and migration.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6283,"ComplexName":"SIVA1-XIAP-TAK1 complex","Organism":"Human","Synonyms":"None","Cell.line":"Jurkat T cells","subunits.UniProt.IDs.":"O15304;O43318;P98170","subunits.Entrez.IDs.":"10572;6885;331","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007249","GO.description":"I-kappaB kinase/NF-kappaB signaling","FunCat.ID":"30.01.05.01.04","FunCat.description":"NIK-I-kappaB/NF-kappaB cascade","PubMed.ID":19584092,"subunits.Protein.name.":"Apoptosis regulatory protein Siva;Mitogen-activated protein kinase kinase kinase 7;E3 ubiquitin-protein ligase XIAP","subunits.Gene.name.":"SIVA1;MAP3K7;XIAP","subunits.Gene.name.syn.":"SIVA;TAK1;API3, BIRC4, IAP3","Disease.comment":"None","Subunits.comment":"SIVA1 is a proapoptotic protein involved in T-cell apoptosis through a caspase-dependent mitochondrial pathway.XIAP functions as ubiquitin-E3-ligase and belongs to a family of apoptosis inhibitors. (PMID:19584092)TAK1 is a subunit of the TAK1 complex (Corum-ID 2758) known to regulate NF-kappaB activity.","Complex.comment":"XIAP, SIVA1 and TAK1 form a ternary complex in Jurkat T cells. Complex formation increases after PMA/Iono stimulation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6284,"ComplexName":"PKA RIbeta holoenzyme","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P05132;P12849","subunits.Entrez.IDs.":"18747;19085","Protein.complex.purification.method":"MI:0114- x-ray crystallography","GO.ID":"GO:0004691;GO:0004672","GO.description":"cAMP-dependent protein kinase activity;protein kinase activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":22797896,"subunits.Protein.name.":"cAMP-dependent protein kinase catalytic subunit alpha ;cAMP-dependent protein kinase type I-beta regulatory subunit","subunits.Gene.name.":"Prkaca;Prkar1b","subunits.Gene.name.syn.":"Pkaca;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6285,"ComplexName":"Ucp3-Hax-1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"O35387;P56501","subunits.Entrez.IDs.":"23897;22229","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0005743;GO:0051592;GO:0055074","GO.description":"mitochondrial inner membrane;response to calcium ion;calcium ion homeostasis","FunCat.ID":"70.16.05","FunCat.description":"mitochondrial inner membrane","PubMed.ID":26915802,"subunits.Protein.name.":"HCLS1-associated protein X-1;Mitochondrial uncoupling protein 3","subunits.Gene.name.":"Hax1;Ucp3","subunits.Gene.name.syn.":"Hs1bp1;Slc25a9","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Hax-1 binding to UCP3 localized at the mitochondrial inner membrane. Interaction of these proteins occurred in a calcium-dependent manner.The results suggested that the UCP3-Hax-1 complex may regulate mitochondrial functional changes caused by mitochondrial Ca(2+).","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6287,"ComplexName":"SLC2A1-DMTN-ADD2 complex","Organism":"Human","Synonyms":"None","Cell.line":"human erythrocyte ghosts","subunits.UniProt.IDs.":"P11166;P35612;Q08495","subunits.Entrez.IDs.":"6513;119;2039","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0003779;GO:0044425;GO:0030507","GO.description":"actin binding;membrane part;spectrin binding","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":18347014,"subunits.Protein.name.":"Solute carrier family 2, facilitated glucose transporter member 1 ;Beta-adducin ;Dematin","subunits.Gene.name.":"SLC2A1;ADD2;DMTN","subunits.Gene.name.syn.":"GLUT1;ADDB;DMT EPB49","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors proposed model predicts a major role of GLUT1 interactions with dematin and adducin in stabilizing the vertical linkage of the junctional complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6288,"ComplexName":"RPGR-PDEdelta-Arl3 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O55057;Q92834;Q9WUL7","subunits.Entrez.IDs.":"18582;6103;56350","Protein.complex.purification.method":"MI:0096-pull down","GO.ID":"GO:0007601;GO:0060271","GO.description":"visual perception;cilium assembly","FunCat.ID":"34.11.01.03","FunCat.description":"visual transduction","PubMed.ID":23559067,"subunits.Protein.name.":"Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta ;X-linked retinitis pigmentosa GTPase regulator;ADP-ribosylation factor-like protein 3","subunits.Gene.name.":"Pde6d;RPGR;Arl3","subunits.Gene.name.syn.":";RP3, XLRP3;","Disease.comment":"OMIM:300029 Retinitis pigmentosa 3 (PMID:8673101).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Homo sapiens (Human);Mus musculus (Mouse)"}
{"ComplexID":6289,"ComplexName":"prohibitin 2 complex, mitochondrial","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O00165;P05141;P35232;P45880;Q99623","subunits.Entrez.IDs.":"10456;292;5245;7417;11331","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0006915;GO:0008637","GO.description":"apoptotic process;apoptotic mitochondrial changes","FunCat.ID":"40.10.02;40.10.02.02.01","FunCat.description":"apoptosis (type I programmed cell death);apoptotic mitochondrial changes","PubMed.ID":17008324,"subunits.Protein.name.":"HCLS1-associated protein X-1;ADP/ATP translocase 2;Prohibitin;Voltage-dependent anion-selective channel protein 2;Prohibitin-2","subunits.Gene.name.":"HAX1;SLC25A5;PHB;VDAC2;PHB2","subunits.Gene.name.syn.":"HS1BP1;ANT2;None;None;BAP, REA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Human PHB2 has pleiotropic functions in the mitochondria, including inhibition of apoptosis via the PHB2-\\u0001Hax-1 complex and regulation of the mitochondrial morphology.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6290,"ComplexName":"Ubiquitin E3 ligase (DDB1, DYRK2, EDD, VPRBP)","Organism":"Human","Synonyms":"EDVP\\u2013DYRK2 complex","Cell.line":"293T cells","subunits.UniProt.IDs.":"O95071;Q16531;Q92630;Q9Y4B6","subunits.Entrez.IDs.":"51366;1642;8445;9730","Protein.complex.purification.method":"MI:0676- tandem affinity purification","GO.ID":"GO:0044772;GO:1902002","GO.description":"mitotic cell cycle phase transition;protein phosphorylation involved in cellular protein catabolic process","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":19287380,"subunits.Protein.name.":"E3 ubiquitin-protein ligase UBR5 ;DNA damage-binding protein 1;Dual specificity tyrosine-phosphorylation-regulated kinase 2 ;Protein VPRBP","subunits.Gene.name.":"UBR5;DDB1;DYRK2;VPRBP","subunits.Gene.name.syn.":"EDD EDD1 HYD KIAA0896;XAP1;;DCAF1 KIAA0800 RIP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"EDVP\\u2013DYRK2 complex regulates katanin p60 ubiquitylation. EDVP\\u2013DYRK2 complex controls mitotic transition through the modulation of katanin protein levels.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6291,"ComplexName":"Ubiquitin E3 ligase (DDIT4, DDB1, BTRC, CUL4A)","Organism":"Human","Synonyms":"None","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"Q13619;Q16531;Q9NX09;Q9Y297","subunits.Entrez.IDs.":"8451;1642;54541;8945","Protein.complex.purification.method":"MI:0007- anti tag coimmunoprecipitation","GO.ID":"GO:0032006;GO:0000151;GO:0006511;GO:0006468;GO:0001666","GO.description":"regulation of TOR signaling;ubiquitin ligase complex;ubiquitin-dependent protein catabolic process;protein phosphorylation;response to hypoxia","FunCat.ID":"14.13.01.01;14.07.03","FunCat.description":"proteasomal degradation (ubiquitin/proteasomal pathway);modification by phosphorylation, dephosphorylation, autophosphorylation","PubMed.ID":19557001,"subunits.Protein.name.":"Cullin-4A;DNA damage-binding protein 1;DNA damage-inducible transcript 4 protein ;F-box/WD repeat-containing protein 1A","subunits.Gene.name.":"CUL4A;DDB1;DDIT4;BTRC","subunits.Gene.name.syn.":"None;XAP1;REDD1 RTP801;BTRCP FBW1A FBXW1A","Disease.comment":"Decreased REDD1 mRNA expression hasbeen observed in primary breast tumours.","Subunits.comment":"None","Complex.comment":"The CUL4A\\u2013DDB1\\u2013ROC1\\u2013b-TRCP ubiquitin ligase complex acts to regulate mTOR signalling by modulating the stability of REDD1. REDD1 is a recently described component of the stress response. REDD1 was first identified as a gene induced by hypoxia and DNA damage.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6292,"ComplexName":"HAX-1\\u2013XIAP complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells and Bosc 23 cells","subunits.UniProt.IDs.":"O00165;P98170","subunits.Entrez.IDs.":"10456;331","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0006915;GO:1902915","GO.description":"apoptotic process;negative regulation of protein polyubiquitination","FunCat.ID":"40.10.02","FunCat.description":"apoptosis (type I programmed cell death)","PubMed.ID":20171186,"subunits.Protein.name.":"HCLS1-associated protein X-1;E3 ubiquitin-protein ligase XIAP","subunits.Gene.name.":"HAX1;XIAP","subunits.Gene.name.syn.":"HS1BP1;API3, BIRC4, IAP3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The formation of the HAX-1\\u2013XIAP complex inhibits apoptosis by enhancing the stability of XIAP against proteosomal degradation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6293,"ComplexName":"DDN-MAGI2-SH3KBP1 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS-7 cells","subunits.UniProt.IDs.":"O94850;Q86UL8;Q96B97","subunits.Entrez.IDs.":"23109;9863;30011","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0043197","GO.description":"dendritic spine","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":16751601,"subunits.Protein.name.":"Dendrin;Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2 ;SH3 domain-containing kinase-binding protein 1","subunits.Gene.name.":"DDN;MAGI2;SH3KBP1","subunits.Gene.name.syn.":"KIAA0749;ACVRINP1 AIP1 KIAA0705;CIN85","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6294,"ComplexName":"DDR1-PRKCZ-WWC1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK-293 cells","subunits.UniProt.IDs.":"Q05513;Q08345;Q8IX03","subunits.Entrez.IDs.":"5590;780;23286","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":18190796,"subunits.Protein.name.":"Protein kinase C zeta type;Epithelial discoidin domain-containing receptor 1 ;Protein KIBRA","subunits.Gene.name.":"PRKCZ;DDR1;WWC1","subunits.Gene.name.syn.":"PKC2;CAK EDDR1 NEP NTRK4 PTK3A RTK6 TRKE;KIAA0869","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"DDR1, PRKCZ and WWC1 interact in atripartite complex, but predominantly in the absence of collagen.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6295,"ComplexName":"CR2-CD19 complex","Organism":"Human","Synonyms":"CD21-CD19 complex","Cell.line":"Raji B lymphoblastoid cells","subunits.UniProt.IDs.":"P15391;P20023","subunits.Entrez.IDs.":"930;1380","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0006955","GO.description":"immune response","FunCat.ID":"36.25.16","FunCat.description":"immune response","PubMed.ID":1702139,"subunits.Protein.name.":"B-lymphocyte antigen CD19;Complement receptor type 2","subunits.Gene.name.":"CD19;CR2","subunits.Gene.name.syn.":"None;C3DR","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6296,"ComplexName":"SPATA2-CYLD complex","Organism":"Human","Synonyms":"None","Cell.line":"U2OS cells","subunits.UniProt.IDs.":"Q9NQC7;Q9UM82","subunits.Entrez.IDs.":"1540;9825","Protein.complex.purification.method":"MI:0071-molecular sieving","GO.ID":"GO:0070536;GO:0045087;GO:0007249","GO.description":"protein K63-linked deubiquitination;innate immune response;I-kappaB kinase/NF-kappaB signaling","FunCat.ID":"36.25.16.01;30.01.05.01.04","FunCat.description":"innate immune response (invertebrates and vertebrates);NIK-I-kappaB/NF-kappaB cascade","PubMed.ID":27591049,"subunits.Protein.name.":"Ubiquitin carboxyl-terminal hydrolase CYLD;Spermatogenesis-associated protein 2","subunits.Gene.name.":"CYLD;SPATA2","subunits.Gene.name.syn.":"CYLD1, KIAA0849;KIAA0757, PD1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The SPATA2 PUB domain (aa 1\\u2013241) formes a 2:2 complex with dimeric CYLD USP domain of 136 kDa in SEC-MALS.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6297,"ComplexName":"vWF-GPIb complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04275;P07359","subunits.Entrez.IDs.":"7450;2811","Protein.complex.purification.method":"MI:0019- coimmunoprecipitation","GO.ID":"GO:0030193","GO.description":"regulation of blood coagulation","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":7887899,"subunits.Protein.name.":"von Willebrand factor ;Platelet glycoprotein Ib alpha chain","subunits.Gene.name.":"VWF;GP1BA","subunits.Gene.name.syn.":"F8VWF;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6298,"ComplexName":"ELK1-SAP1a-SRF complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"G1SZG6;P11831;P28324","subunits.Entrez.IDs.":"None;6722;2005","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0003700;GO:0006355","GO.description":"transcription factor activity, sequence-specific DNA binding;regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":9010223,"subunits.Protein.name.":"Uncharacterized protein;Serum response factor ;ETS domain-containing protein Elk-4","subunits.Gene.name.":"ELK1;SRF;ELK4","subunits.Gene.name.syn.":";;SAP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Oryctolagus cuniculus (Rabbit);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6299,"ComplexName":"ELK1-SAP1a-EWS-FLI-FLI complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P19419;P28324;Q01543;Q16198","subunits.Entrez.IDs.":"2002;2005;2313;None","Protein.complex.purification.method":"MI:0071- molecular sieving","GO.ID":"GO:0006355","GO.description":"regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":9010223,"subunits.Protein.name.":"ETS domain-containing protein Elk-1;ETS domain-containing protein Elk-4 ;Friend leukemia integration 1 transcription factor ;EWS-Fli1 protein","subunits.Gene.name.":"ELK1;ELK4;FLI1;EWS-Fli1","subunits.Gene.name.syn.":";SAP1;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6300,"ComplexName":"CDKN1A-TP53-CDK1-PCNA complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P04637;P06493;P38936","subunits.Entrez.IDs.":"7157;983;1026","Protein.complex.purification.method":"MI:0045- experimental","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":7624128,"subunits.Protein.name.":"Cellular tumor antigen p53;Cyclin-dependent kinase 1 ;Cyclin-dependent kinase inhibitor 1","subunits.Gene.name.":"TP53;CDK1;CDKN1A","subunits.Gene.name.syn.":"P53;CDC2 CDC28A CDKN1 P34CDC2;CAP20 CDKN1 CIP1 MDA6 PIC1 SDI1 WAF1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6301,"ComplexName":"tRNA Splicing Ligase Complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"Q52LJ0;Q92499;Q9BVC5;Q9Y224;Q9Y3I0","subunits.Entrez.IDs.":"283742;1653;79074;51637;51493","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0071-molecular sieving","GO.ID":"GO:0072669;GO:0000394","GO.description":"tRNA-splicing ligase complex;RNA splicing, via endonucleolytic cleavage and ligation","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":21311021,"subunits.Protein.name.":"Protein FAM98B;ATP-dependent RNA helicase DDX1 ;Ashwin;UPF0568 protein C14orf166 ;tRNA-splicing ligase RtcB homolog","subunits.Gene.name.":"FAM98B;DDX1;C2orf49;C14orf166;RTCB","subunits.Gene.name.syn.":";;;;C22orf28","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6302,"ComplexName":"B-WICH complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O00159;O60264;O75533;P35659;Q03468;Q9BQG0;Q9C093;Q9NR30;Q9UIG0","subunits.Entrez.IDs.":"4641;8467;23451;7913;2074;10514;79925;9188;9031","Protein.complex.purification.method":"MI:0071-molecular sieving;MI:0226-ion exchange chromatography;MI:0019-coimmunoprecipitation","GO.ID":"GO:0006351;GO:0043044;GO:0005634","GO.description":"transcription, DNA-templated;ATP-dependent chromatin remodeling;nucleus","FunCat.ID":"11;70.10","FunCat.description":"TRANSCRIPTION;nucleus","PubMed.ID":16603771,"subunits.Protein.name.":"Unconventional myosin-Ic ;SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5;Splicing factor 3B subunit 1 ;Protein DEK;DNA excision repair protein ERCC-6 ;Myb-binding protein 1A;Sperm flagellar protein 2 ;Nucleolar RNA helicase 2 ;Tyrosine-protein kinase BAZ1B","subunits.Gene.name.":"MYO1C;SMARCA5;SF3B1;DEK;ERCC6;MYBBP1A;SPEF2;DDX21;BAZ1B","subunits.Gene.name.syn.":";SNF2H WCRF135;SAP155;;CSB;P160;KIAA1770 KPL2;;WBSC10 WBSCR10 WBSCR9 WSTF","Disease.comment":"None","Subunits.comment":"Interactions in the B-WICH Depend on RNA and active transcription. U1 small nuclear ribonucleoprotein 1SNRP homolog protein was nor available at the time of annotation","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6303,"ComplexName":"DDX11-RAD21-SMC1A-SMC3 complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O60216;Q14683;Q96FC9;Q9UQE7","subunits.Entrez.IDs.":"5885;8243;1663;9126","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007062","GO.description":"sister chromatid cohesion","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":17105772,"subunits.Protein.name.":"Double-strand-break repair protein rad21 homolog ;Structural maintenance of chromosomes protein 1A ;ATP-dependent DNA helicase DDX11 ;Structural maintenance of chromosomes protein 3","subunits.Gene.name.":"RAD21;SMC1A;DDX11;SMC3","subunits.Gene.name.syn.":"HR21 KIAA0078 NXP1;DXS423E KIAA0178 SB1.8 SMC1 SMC1L1;CHL1 CHLR1 KRG2;BAM BMH CSPG6 SMC3L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6304,"ComplexName":"DDX11-Ctf18-RFC complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"O75717;P12004;Q5FWF5;Q8WVB6;Q96FC9;Q9BVC3","subunits.Entrez.IDs.":"11169;5111;114799;63922;1663;79075","Protein.complex.purification.method":"None","GO.ID":"GO:0004386;GO:0007062","GO.description":"helicase activity;sister chromatid cohesion","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":18499658,"subunits.Protein.name.":"WD repeat and HMG-box DNA-binding protein 1 ;Proliferating cell nuclear antigen;N-acetyltransferase ESCO1 ;Chromosome transmission fidelity protein 18 homolog;ATP-dependent DNA helicase DDX11 ;Sister chromatid cohesion protein DCC1","subunits.Gene.name.":"WDHD1;PCNA;ESCO1;CHTF18;DDX11;DSCC1","subunits.Gene.name.syn.":"AND1;None;EFO1 KIAA1911;C16orf41 CTF18;CHL1 CHLR1 KRG2;DCC1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6305,"ComplexName":"Hoxa9-Meis1-Pbx3 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O35317;P09631;Q60954","subunits.Entrez.IDs.":"18516;15405;17268","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006355;GO:0003700;GO:0003677","GO.description":"regulation of transcription, DNA-templated;transcription factor activity, sequence-specific DNA binding;DNA binding","FunCat.ID":"11.02.03.04;16.03.01","FunCat.description":"transcriptional control;DNA binding","PubMed.ID":25911551,"subunits.Protein.name.":"Pre-B-cell leukemia transcription factor 3 ;Homeobox protein Hox-A9 ;Homeobox protein Meis1","subunits.Gene.name.":"Pbx3;Hoxa9;Meis1","subunits.Gene.name.syn.":";Hox-1.7 Hoxa-9;","Disease.comment":"Hox-induced murine leukemia (PMID:25911551).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6306,"ComplexName":"DDX27-PeBoW complex","Organism":"Human","Synonyms":"None","Cell.line":"RajiB-cells; U2OS cells","subunits.UniProt.IDs.":"O00541;Q14137;Q96GQ7;Q9GZL7","subunits.Entrez.IDs.":"23481;23246;55661;55759","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006364;GO:0005730","GO.description":"rRNA processing;nucleolus","FunCat.ID":"11.04.01;70.10.07","FunCat.description":"rRNA processing;nucleolus","PubMed.ID":25825154,"subunits.Protein.name.":"Pescadillo homolog;Ribosome biogenesis protein BOP1 ;Probable ATP-dependent RNA helicase DDX27 ;Ribosome biogenesis protein WDR12","subunits.Gene.name.":"PES1;BOP1;DDX27;WDR12","subunits.Gene.name.syn.":";KIAA0124;cPERP-F RHLP;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Knockdown of DDX27 impairs processing of 47S rRNA.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6307,"ComplexName":"RAB27A-SLP3-KLC1 transport complex","Organism":"Human","Synonyms":"None","Cell.line":"293T cells","subunits.UniProt.IDs.":"P51159;Q07866;Q4VX76","subunits.Entrez.IDs.":"5873;3831;94120","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0043316","GO.description":"cytotoxic T cell degranulation","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":22308290,"subunits.Protein.name.":"Ras-related protein Rab-27A;Kinesin light chain 1;Synaptotagmin-like protein 3","subunits.Gene.name.":"RAB27A;KLC1;SYTL3","subunits.Gene.name.syn.":"RAB27;KLC, KNS2;SLP3","Disease.comment":"Rab27a deficiency is associated with impaired cytotoxic activity, unbalanced expansion, and activation of CD8 T lymphocytes and the uncontrolled macrophage activation that characterizes Griscelli syndrome type 2.","Subunits.comment":"None","Complex.comment":"Inhibition of the Rab27a/Slp3/kinesin-1 transport compleximpairs lytic granule secretion. This multiprotein complex enables lytic granules to reach the plasma membrane and is thus essential for their release into the IS (immune synapse).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6308,"ComplexName":"protein complex (DDX28; DHX30; GRSF1; FASTKD2; FASTKD5)","Organism":"Human","Synonyms":"None","Cell.line":"143B cells","subunits.UniProt.IDs.":"Q12849;Q7L2E3;Q7L8L6;Q9NUL7;Q9NYY8","subunits.Entrez.IDs.":"2926;22907;60493;55794;22868","Protein.complex.purification.method":"None","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25683715,"subunits.Protein.name.":"G-rich sequence factor 1 ;Putative ATP-dependent RNA helicase DHX30 ;FAST kinase domain-containing protein 5, mitochondrial;Probable ATP-dependent RNA helicase DDX28 ;FAST kinase domain-containing protein 2, mitochondrial","subunits.Gene.name.":"GRSF1;DHX30;FASTKD5;DDX28;FASTKD2","subunits.Gene.name.syn.":";DDX30 KIAA0890;KIAA1792;MDDX28;KIAA0971","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6310,"ComplexName":"DEAF1- complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T/17 cells; CV1 cells","subunits.UniProt.IDs.":"O75398;P12956;P13010","subunits.Entrez.IDs.":"10522;2547;7520","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0005634","GO.description":"nucleus","FunCat.ID":"70.1","FunCat.description":"nucleus","PubMed.ID":22442688,"subunits.Protein.name.":"Deformed epidermal autoregulatory factor 1 homolog ;X-ray repair cross-complementing protein 6 ;X-ray repair cross-complementing protein 5","subunits.Gene.name.":"DEAF1;XRCC6;XRCC5","subunits.Gene.name.syn.":"SPN ZMYND5;G22P1;G22P2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6311,"ComplexName":"CABP1-CACNA1C complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"O88751;P22002","subunits.Entrez.IDs.":"171051;24239","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:1901385;GO:0014069","GO.description":"regulation of voltage-gated calcium channel activity;postsynaptic density","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":15140941,"subunits.Protein.name.":"Calcium-binding protein 1 ;Voltage-dependent L-type calcium channel subunit alpha-1C","subunits.Gene.name.":"Cabp1;Cacna1c","subunits.Gene.name.syn.":";Cach2 Cacn2 Cacnl1a1 Cchl1a1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6312,"ComplexName":"P300\\u2013Clock\\u2013Bmal1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"liver","subunits.UniProt.IDs.":"B2RWS6;O08785;Q9WTL8","subunits.Entrez.IDs.":"328572;12753;11865","Protein.complex.purification.method":"None","GO.ID":"GO:0042752;GO:0005634","GO.description":"regulation of circadian rhythm;nucleus","FunCat.ID":"70.1","FunCat.description":"nucleus","PubMed.ID":12483227,"subunits.Protein.name.":"Histone acetyltransferase p300 ;Circadian locomoter output cycles protein kaput ;Aryl hydrocarbon receptor nuclear translocator-like protein 1","subunits.Gene.name.":"Ep300;Clock;Arntl","subunits.Gene.name.syn.":"P300;;Bmal1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6313,"ComplexName":"AATF-NGDN-NOL10 complex","Organism":"Human","Synonyms":"ANN complex","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"Q8NEJ9;Q9BSC4;Q9NY61","subunits.Entrez.IDs.":"25983;79954;26574","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0096-pull down","GO.ID":"GO:0090069","GO.description":"regulation of ribosome biogenesis","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":27599843,"subunits.Protein.name.":"Neuroguidin ;Nucleolar protein 10;Protein AATF","subunits.Gene.name.":"NGDN;NOL10;AATF","subunits.Gene.name.syn.":"C14orf120;;CHE1 DED","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6314,"ComplexName":"MSP58-RINT1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q6NUQ1;Q96EZ8","subunits.Entrez.IDs.":"60561;10445","Protein.complex.purification.method":"MI:0018-two hybrid","GO.ID":"GO:0090069","GO.description":"regulation of ribosome biogenesis","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":27530925,"subunits.Protein.name.":"RAD50-interacting protein 1 ;Microspherule protein 1","subunits.Gene.name.":"RINT1;MCRS1","subunits.Gene.name.syn.":";INO80Q MSP58","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6315,"ComplexName":"mGluR1-mGluR5 complex","Organism":"Mouse","Synonyms":"GRM1-GRM5","Cell.line":"hippocampus","subunits.UniProt.IDs.":"P97772;Q3UVX5","subunits.Entrez.IDs.":"14816;108071","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007216","GO.description":"G-protein coupled glutamate receptor signaling pathway","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":27392515,"subunits.Protein.name.":"Metabotropic glutamate receptor 1 ;Metabotropic glutamate receptor 5","subunits.Gene.name.":"Grm1;Grm5","subunits.Gene.name.syn.":"Gprc1a Mglur1;Gprc1e Mglur5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6316,"ComplexName":"Slp1-Rab27b-Crmp2 complex","Organism":"Rat","Synonyms":"Sytl1-Rab27b-Dpysl2 complex","Cell.line":"COS 7 cells","subunits.UniProt.IDs.":"P47942;Q4KMA1;Q99P74","subunits.Entrez.IDs.":"25416;297872;84590","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0007411","GO.description":"axon guidance","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":19460344,"subunits.Protein.name.":"Dihydropyrimidinase-related protein 2;Protein Sytl1;Ras-related protein Rab-27B","subunits.Gene.name.":"Dpysl2;Sytl1;Rab27b","subunits.Gene.name.syn.":"Crmp2;Slp-1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"GTP-gamma-S-bound MBP-Rab27B consistently formed a complex with His-Slp1 and CRMP-2-GST with \\u00020.2:0.3:1 stoichiometry, whereas GDP-bound Rab27B did not form a complex.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6317,"ComplexName":"NLRP1 inflammasome","Organism":"Human","Synonyms":"NALP1 inflammasome","Cell.line":"THP-1 cell","subunits.UniProt.IDs.":"P29466;P51878;Q9C000;Q9ULZ3","subunits.Entrez.IDs.":"834;838;22861;29108","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0070498","GO.description":"interleukin-1-mediated signaling pathway","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":12191486,"subunits.Protein.name.":"Caspase-1;Caspase-5;NACHT, LRR and PYD domains-containing protein 1;Apoptosis-associated speck-like protein containing a CARD","subunits.Gene.name.":"CASP1;CASP5;NLRP1;PYCARD","subunits.Gene.name.syn.":"IL1BC, IL1BCE;ICH3;CARD7, DEFCAP, KIAA0926, NAC, NALP1;ASC, CARD5, TMS1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"PYCARD recruits CASP1 and the C-terminal CARD domain of NALP1 recruits, and activates CASP5. (PMID:15030775)","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6318,"ComplexName":"Dlg4-Dlgap1-Shank1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P31016;P97836;Q9WV48","subunits.Entrez.IDs.":"29495;65040;78957","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0097107","GO.description":"postsynaptic density assembly","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":10433269,"subunits.Protein.name.":"Disks large homolog 4;Disks large-associated protein 1 ;SH3 and multiple ankyrin repeat domains protein 1","subunits.Gene.name.":"Dlg4;Dlgap1;Shank1","subunits.Gene.name.syn.":"Dlgh4, Psd95;Gkap;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6319,"ComplexName":"MEKK2-MEK5alpha complex","Organism":"Mouse","Synonyms":"None","Cell.line":"MEF cells","subunits.UniProt.IDs.":"Q9WVS7;Q9Y2U5","subunits.Entrez.IDs.":"23938;10746","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0070376","GO.description":"regulation of ERK5 cascade","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":16260599,"subunits.Protein.name.":"Dual specificity mitogen-activated protein kinase kinase 5 ;Mitogen-activated protein kinase kinase kinase 2","subunits.Gene.name.":"Map2k5;MAP3K2","subunits.Gene.name.syn.":"Mek5 Mkk5 Prkmk5;MAPKKK2 MEKK2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Homo sapiens (Human)"}
{"ComplexID":6320,"ComplexName":"ERK5-MEK5 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"MEF cells","subunits.UniProt.IDs.":"Q9WVS7;Q9WVS8","subunits.Entrez.IDs.":"23938;23939","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0070376","GO.description":"regulation of ERK5 cascade","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":16260599,"subunits.Protein.name.":"Dual specificity mitogen-activated protein kinase kinase 5 ;Mitogen-activated protein kinase 7","subunits.Gene.name.":"Map2k5;Mapk7","subunits.Gene.name.syn.":"Mek5 Mkk5 Prkmk5;Bmk1 Erk5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6321,"ComplexName":"DLG4-DLGAP1-SHANK3 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK cells","subunits.UniProt.IDs.":"O14490;P78352;Q9BYB0","subunits.Entrez.IDs.":"9229;1742;85358","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":10527873,"subunits.Protein.name.":"Disks large-associated protein 1 ;Disks large homolog 4 ;SH3 and multiple ankyrin repeat domains protein 3","subunits.Gene.name.":"DLGAP1;DLG4;SHANK3","subunits.Gene.name.syn.":"DAP1 GKAP;PSD95;KIAA1650 PROSAP2 PSAP2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6322,"ComplexName":"DLG4-DLGAP1-SHANK2 complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain","subunits.UniProt.IDs.":"P31016;P97836;Q9QX74","subunits.Entrez.IDs.":"29495;65040;171093","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":10527873,"subunits.Protein.name.":"Disks large homolog 4;Disks large-associated protein 1 ;SH3 and multiple ankyrin repeat domains protein 2","subunits.Gene.name.":"Dlg4;Dlgap1;Shank2","subunits.Gene.name.syn.":"Dlgh4, Psd95;Gkap;Cortbp1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6323,"ComplexName":"NLRP3 inflammasome","Organism":"Human","Synonyms":"NALP3 inflammasome","Cell.line":"THP-1 cell","subunits.UniProt.IDs.":"P29466;Q96P20;Q9ULZ3;Q9Y2G2","subunits.Entrez.IDs.":"834;114548;29108;22900","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0070498","GO.description":"interleukin-1-mediated signaling pathway","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":15030775,"subunits.Protein.name.":"Caspase-1;NACHT, LRR and PYD domains-containing protein 3;Apoptosis-associated speck-like protein containing a CARD;Caspase recruitment domain-containing protein 8","subunits.Gene.name.":"CASP1;NLRP3;PYCARD;CARD8","subunits.Gene.name.syn.":"IL1BC, IL1BCE;C1orf7, CIAS1, NALP3, PYPAF1;ASC, CARD5, TMS1;KIAA0955, NDPP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6324,"ComplexName":"NLRP2 inflammasome","Organism":"Human","Synonyms":"NALP2 inflammasome","Cell.line":"THP-1 cell","subunits.UniProt.IDs.":"P29466;Q9NX02;Q9ULZ3;Q9Y2G2","subunits.Entrez.IDs.":"834;55655;29108;22900","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0070498","GO.description":"interleukin-1-mediated signaling pathway","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":15030775,"subunits.Protein.name.":"Caspase-1;NACHT, LRR and PYD domains-containing protein 2;Apoptosis-associated speck-like protein containing a CARD;Caspase recruitment domain-containing protein 8","subunits.Gene.name.":"CASP1;NLRP2;PYCARD;CARD8","subunits.Gene.name.syn.":"IL1BC, IL1BCE;NALP2, NBS1, PAN1, PYPAF2;ASC, CARD5, TMS1;KIAA0955, NDPP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6325,"ComplexName":"PDC-GNGT1-GNB1 complex","Organism":"Bovine","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P19632;P62871;P63211","subunits.Entrez.IDs.":"287007;281201;2792","Protein.complex.purification.method":"MI:0114-x-ray crystallography","GO.ID":"GO:0007601","GO.description":"visual perception","FunCat.ID":"34.11.01.03","FunCat.description":"visual transduction","PubMed.ID":9739091,"subunits.Protein.name.":"Phosducin ;Guanine nucleotide-binding protein G;Guanine nucleotide-binding protein G","subunits.Gene.name.":"PDC;GNB1;GNGT1","subunits.Gene.name.syn.":";;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine);Homo sapiens (Human)"}
{"ComplexID":6326,"ComplexName":"Dystrophin complex (Dmd; Snta1)","Organism":"Mouse","Synonyms":"None","Cell.line":"skeletal muscle","subunits.UniProt.IDs.":"P11531;Q61234","subunits.Entrez.IDs.":"13405;20648","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":9214383,"subunits.Protein.name.":"Dystrophin;Alpha-1-syntrophin","subunits.Gene.name.":"Dmd;Snta1","subunits.Gene.name.syn.":"None;Snt1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6327,"ComplexName":"Dystrophin complex (Dmd; Stnb1)","Organism":"Mouse","Synonyms":"None","Cell.line":"skeletal muscle","subunits.UniProt.IDs.":"P11531;Q99L88","subunits.Entrez.IDs.":"13405;20649","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":9214383,"subunits.Protein.name.":"Dystrophin;Beta-1-syntrophin","subunits.Gene.name.":"Dmd;Sntb1","subunits.Gene.name.syn.":"None;Snt2b1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6328,"ComplexName":"Utrophin complex (Utrn, Stnb1)","Organism":"Mouse","Synonyms":"None","Cell.line":"skeletal muscle","subunits.UniProt.IDs.":"P46939;Q99L88","subunits.Entrez.IDs.":"7402;20649","Protein.complex.purification.method":"None","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":9214383,"subunits.Protein.name.":"Utrophin ;Beta-1-syntrophin","subunits.Gene.name.":"UTRN;Sntb1","subunits.Gene.name.syn.":"DMDL DRP1;Snt2b1","Disease.comment":"None","Subunits.comment":"As Utrn from mouse was not available at the time of annotation, the human ortholog was annotated.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Mus musculus (Mouse)"}
{"ComplexID":6329,"ComplexName":"BAX-DNAJA1-HSPA1B complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS-7 cells","subunits.UniProt.IDs.":"A0A0D9S330;P0DMV9;Q95JF4","subunits.Entrez.IDs.":"None;3303;None","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0043066","GO.description":"negative regulation of apoptotic process","FunCat.ID":"40.10.02.01","FunCat.description":"anti-apoptosis","PubMed.ID":14752510,"subunits.Protein.name.":"Uncharacterized protein;Heat shock 70 kDa protein 1B;DnaJ homolog subfamily A member 1","subunits.Gene.name.":"BAX;HSPA1B;DNAJA1","subunits.Gene.name.syn.":";None;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Experiments indicate that CHOP-induced apoptosis is mediated by translocation of Bax from the cytosol to the mitochondria, and HSP70/DNAJA1 or DNAJA2 chaperone pair prevents apoptosis by interacting with Bax and preventing translocation to the mitochondria.","SWISSPROT.organism":"Chlorocebus sabaeus (Green monkey) (Cercopithecus ;Homo sapiens (Human);Chlorocebus aethiops (Green monkey) (Cercopithecus"}
{"ComplexID":6330,"ComplexName":"BAX-DNAJA2-HSPA1B complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS-7 cells","subunits.UniProt.IDs.":"A0A0D9S330;O60884;P0DMV9","subunits.Entrez.IDs.":"None;10294;3303","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0043066","GO.description":"negative regulation of apoptotic process","FunCat.ID":"40.10.02.01","FunCat.description":"anti-apoptosis","PubMed.ID":14752510,"subunits.Protein.name.":"Uncharacterized protein;DnaJ homolog subfamily A member 2 ;Heat shock 70 kDa protein 1B","subunits.Gene.name.":"BAX;DNAJA2;HSPA1B","subunits.Gene.name.syn.":";CPR3 HIRIP4;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Experiments indicate that CHOP-induced apoptosis is mediated by translocation of Bax from the cytosol to the mitochondria, and HSP70/DNAJA1 or DNAJA2 chaperone pair prevents apoptosis by interacting with Bax and preventing translocation to the mitochondria.","SWISSPROT.organism":"Chlorocebus sabaeus (Green monkey) (Cercopithecus ;Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6331,"ComplexName":"Ribosome-associated complex (RAC)","Organism":"Rat","Synonyms":"MPP11-Hsp70L1 complex","Cell.line":"rat liver","subunits.UniProt.IDs.":"Q6AYB4;Q7TQ20","subunits.Entrez.IDs.":"307133;116456","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0276-blue native page","GO.ID":"GO:0043022","GO.description":"ribosome binding","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":16002468,"subunits.Protein.name.":"Heat shock 70 kDa protein 14;DnaJ homolog subfamily C member 2","subunits.Gene.name.":"Hspa14;Dnajc2","subunits.Gene.name.syn.":";Mida1 Zrf1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"MPP11\\u0002 forms a stable complex with Hsp70L1, and the mammalian complex rescuesgrowth defects in yeast strains lacking functional Ribosome-associated complex.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6332,"ComplexName":"Elongator complex (ELP1, ELP2, ELP3, ELP4, ELP5, ELP6)","Organism":"Human","Synonyms":"ELP1-ELP2-ELP3-ELP4-ELP5-ELP6 complex","Cell.line":"HEK-293 cells","subunits.UniProt.IDs.":"O95163;Q0PNE2;Q6IA86;Q8TE02;Q96EB1;Q9H9T3","subunits.Entrez.IDs.":"8518;54859;55250;23587;26610;55140","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006357","GO.description":"regulation of transcription from RNA polymerase II promoter","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":22854966,"subunits.Protein.name.":"Elongator complex protein 1 ;Elongator complex protein 6 ;Elongator complex protein 2 ;Elongator complex protein 5 ;Elongator complex protein 4 ;Elongator complex protein 3","subunits.Gene.name.":"IKBKAP;ELP6;ELP2;ELP5;ELP4;ELP3","subunits.Gene.name.syn.":"ELP1 IKAP;ATP1 C3orf75 TMEM103;STATIP1;C17orf81 DERP6;C11orf19 PAXNEB;","Disease.comment":"OMIM:117100  Centrotemporal epilepsy (PMID:19172991).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6333,"ComplexName":"Nav1.2-beta2 complex","Organism":"Human","Synonyms":"SCN2A-SCN2B complex","Cell.line":"None","subunits.UniProt.IDs.":"O60939;Q99250","subunits.Entrez.IDs.":"6327;6326","Protein.complex.purification.method":"MI:0114-x-ray crystallography","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26894959,"subunits.Protein.name.":"Sodium channel subunit beta-2;Sodium channel protein type 2 subunit alpha","subunits.Gene.name.":"SCN2B;SCN2A","subunits.Gene.name.syn.":";NAC2 SCN2A1 SCN2A2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6334,"ComplexName":"Afadin-beta-catenin complex","Organism":"Human","Synonyms":"AFDN-CTNNB1 complex","Cell.line":"Mesaglial cells","subunits.UniProt.IDs.":"P35222;P55196","subunits.Entrez.IDs.":"1499;4301","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0098609;GO:0034332","GO.description":"cell-cell adhesion;adherens junction organization","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26568295,"subunits.Protein.name.":"Catenin beta-1;Afadin","subunits.Gene.name.":"CTNNB1;AFDN","subunits.Gene.name.syn.":"CTNNB;AF6 MLLT4","Disease.comment":"Mesangial proliferative nephritis, glomerulonephritis (PMID:26568295).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6335,"ComplexName":"PKA-RII-AKAP18gamma complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43687;P05132;P12367;P68181","subunits.Entrez.IDs.":"9465;18747;19087;18749","Protein.complex.purification.method":"MI:0040-electron microscopy","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":24192038,"subunits.Protein.name.":"A-kinase anchor protein 7 isoforms alpha and beta ;cAMP-dependent protein kinase catalytic subunit alpha ;cAMP-dependent protein kinase type II-alpha regulatory subunit;cAMP-dependent protein kinase catalytic subunit beta","subunits.Gene.name.":"AKAP7;Prkaca;Prkar2a;Prkacb","subunits.Gene.name.syn.":"AKAP15 AKAP18;Pkaca;;Pkacb","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6336,"ComplexName":"CTNNB1-DNMT1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HC-116 cells","subunits.UniProt.IDs.":"P26358;P35222","subunits.Entrez.IDs.":"1786;1499","Protein.complex.purification.method":"MI:0069-mass spectrometry studies of complexes","GO.ID":"GO:0030111;GO:0006306","GO.description":"regulation of Wnt signaling pathway;DNA methylation","FunCat.ID":"10.01.09.01","FunCat.description":"DNA methylation","PubMed.ID":25753001,"subunits.Protein.name.":"DNA ;Catenin beta-1","subunits.Gene.name.":"DNMT1;CTNNB1","subunits.Gene.name.syn.":"AIM CXXC9 DNMT;CTNNB","Disease.comment":"Colorectal cancer (PMID:25753001).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6337,"ComplexName":"Amot-cadherin-11-beta-catenin-p120 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK-293T cells","subunits.UniProt.IDs.":"O60716;P35222;P55287;Q4VCS5","subunits.Entrez.IDs.":"1500;1499;1009;154796","Protein.complex.purification.method":"MI:0096-pull down","GO.ID":"GO:0030334","GO.description":"regulation of cell migration","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25466890,"subunits.Protein.name.":"Catenin delta-1;Catenin beta-1;Cadherin-11;Angiomotin","subunits.Gene.name.":"CTNND1;CTNNB1;CDH11;AMOT","subunits.Gene.name.syn.":"KIAA0384;CTNNB;None;KIAA1071","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6338,"ComplexName":"NRF2- Axin1-GSK-3beta-TrCP  complex","Organism":"Mouse","Synonyms":"Hepatocyte","Cell.line":"None","subunits.UniProt.IDs.":"O35625;Q3ULA2;Q60795;Q9WV60","subunits.Entrez.IDs.":"12005;12234;18024;56637","Protein.complex.purification.method":"MI:0096-pull down","GO.ID":"GO:0045454","GO.description":"cell redox homeostasis","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25336178,"subunits.Protein.name.":"Axin-1 ;F-box/WD repeat-containing protein 1A ;Nuclear factor erythroid 2-related factor 2;Glycogen synthase kinase-3 beta","subunits.Gene.name.":"Axin1;Btrc;Nfe2l2;Gsk3b","subunits.Gene.name.syn.":"Axin Fu;Fbw1 Fbxw1 Fwd1 Kiaa4123;Nrf-2 Nrf2;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6339,"ComplexName":"beta-catenin-B-cell lymphoma 9 protein  complex","Organism":"Human","Synonyms":"CTNNB1-BCL9 complex","Cell.line":"None","subunits.UniProt.IDs.":"O00512;P35222","subunits.Entrez.IDs.":"607;1499","Protein.complex.purification.method":"MI:0051-fluorescence technologies","GO.ID":"GO:0030111","GO.description":"regulation of Wnt signaling pathway","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25312469,"subunits.Protein.name.":"B-cell CLL/lymphoma 9 protein ;Catenin beta-1","subunits.Gene.name.":"BCL9;CTNNB1","subunits.Gene.name.syn.":";CTNNB","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6340,"ComplexName":"PITX2-MLL4-ASH2L-RBBP5-PTIP complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"O14686;Q15291;Q6ZW49;Q99697;Q9UBL3","subunits.Entrez.IDs.":"8085;5929;22976;5308;9070","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0045595","GO.description":"regulation of cell differentiation","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":24486544,"subunits.Protein.name.":"Histone-lysine N-methyltransferase 2D;Retinoblastoma-binding protein 5;PAX-interacting protein 1;Pituitary homeobox 2 ;Set1/Ash2 histone methyltransferase complex subunit ASH2","subunits.Gene.name.":"KMT2D;RBBP5;PAXIP1;PITX2;ASH2L","subunits.Gene.name.syn.":"ALR, MLL2, MLL4;RBQ3;PAXIP1L, PTIP;ARP1 RGS RIEG RIEG1;ASH2L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6341,"ComplexName":"PAK1-betaPIX-GIT1-paxillin complex","Organism":"Human","Synonyms":"PAK1-ARHGEF7-GIT1-PXN complex","Cell.line":"None","subunits.UniProt.IDs.":"P49023;Q13153;Q14155;Q9Y2X7","subunits.Entrez.IDs.":"5829;5058;8874;28964","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":16944954,"subunits.Protein.name.":"Paxillin;Serine/threonine-protein kinase PAK 1;Rho guanine nucleotide exchange factor 7;ARF GTPase-activating protein GIT1","subunits.Gene.name.":"PXN;PAK1;ARHGEF7;GIT1","subunits.Gene.name.syn.":";None;COOL1, KIAA0142, P85SPR, PAK3BP, PIXB;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6342,"ComplexName":"Jade-1-NPHP4 complex","Organism":"Human","Synonyms":"JADE1-NPHP4 complex","Cell.line":"H-293T cells","subunits.UniProt.IDs.":"O75161;Q6IE81","subunits.Entrez.IDs.":"261734;79960","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0030178","GO.description":"negative regulation of Wnt signaling pathway","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":22654112,"subunits.Protein.name.":"Nephrocystin-4;Protein Jade-1","subunits.Gene.name.":"NPHP4;JADE1","subunits.Gene.name.syn.":"KIAA0673;KIAA1807 PHF17","Disease.comment":"OMIM:606966 Nephronophthisis 4 (PMID:11920287).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6343,"ComplexName":"SETD7-YAP-AXIN1-beta-catenin complex","Organism":"Human","Synonyms":"SETD7-YAP1-AXIN1-CTNNB1 complex","Cell.line":"HEK-293T cells","subunits.UniProt.IDs.":"O15169;P35222;P46937;Q8WTS6","subunits.Entrez.IDs.":"8312;1499;10413;80854","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0030111;GO:0035330","GO.description":"regulation of Wnt signaling pathway;regulation of hippo signaling","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":27046831,"subunits.Protein.name.":"Axin-1 ;Catenin beta-1;Transcriptional coactivator YAP1;Histone-lysine N-methyltransferase SETD7","subunits.Gene.name.":"AXIN1;CTNNB1;YAP1;SETD7","subunits.Gene.name.syn.":"AXIN;CTNNB;YAP65;KIAA1717 KMT7 SET7 SET9","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6344,"ComplexName":"TNF-R1-associated signaling complex","Organism":"Human","Synonyms":"native TNF-RSC; native TNF-R1 signaling complex; TNFR1-associated signaling complex","Cell.line":"U937 cell line","subunits.UniProt.IDs.":"O14920;O15111;O43318;P01375;P19438;Q12933;Q13489;Q13546;Q15025;Q15628;Q15750;Q96EP0;Q9BYM8;Q9NYJ8;Q9Y6K9","subunits.Entrez.IDs.":"3551;1147;6885;7124;7132;7186;330;8737;10318;8717;10454;55072;10616;23118;8517","Protein.complex.purification.method":"MI:0676-tandem affinity purification","GO.ID":"GO:0007249","GO.description":"I-kappaB kinase/NF-kappaB signaling","FunCat.ID":"30.01.05.01.04","FunCat.description":"NIK-I-kappaB/NF-kappaB cascade","PubMed.ID":20005846,"subunits.Protein.name.":"Inhibitor of nuclear factor kappa-B kinase subunit beta;Inhibitor of nuclear factor kappa-B kinase subunit alpha;Mitogen-activated protein kinase kinase kinase 7;Tumor necrosis factor;Tumor necrosis factor receptor superfamily member 1A;TNF receptor-associated factor 2;Baculoviral IAP repeat-containing protein 3;Receptor-interacting serine/threonine-protein kinase 1;TNFAIP3-interacting protein 1;Tumor necrosis factor receptor type 1-associated DEATH domain protein;TGF-beta-activated kinase 1 and MAP3K7-binding protein 1;E3 ubiquitin-protein ligase RNF31;RanBP-type and C3HC4-type zinc finger-containing protein 1;TGF-beta-activated kinase 1 and MAP3K7-binding protein 2;NF-kappa-B essential modulator","subunits.Gene.name.":"IKBKB;CHUK;MAP3K7;TNF;TNFRSF1A;TRAF2;BIRC3;RIPK1;TNIP1;TRADD;TAB1;RNF31;RBCK1;TAB2;IKBKG","subunits.Gene.name.syn.":"IKKB;IKKA, TCF16;TAK1;TNFA, TNFSF2;TNFAR, TNFR1;TRAP3;API2 MIHC RNF49;RIP, RIP1;KIAA0113, NAF1;None;MAP3K7IP1;ZIBRA;C20orf18, RNF54, UBCE7IP3, XAP3, XAP4;KIAA0733, MAP3K7IP2;FIP3, NEMO","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"After binding of TNF to its receptor TNFR1 BIRC3 (cIAP) is recruited to the TNF-R1 complex via TRADD and TRAF2. BIRC3 together with BIRC2, ubiquitylates RIPK1 allowing the recruitment of LUBAC complex. LUBAC adds linear polyUb chains to NEMO (IKKBKG) and possibly other substrates in the complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6345,"ComplexName":"ZNF304-corepressor complex","Organism":"Human","Synonyms":"None","Cell.line":"DLD-1 cells","subunits.UniProt.IDs.":"P26358;Q13263;Q15047;Q9HCX3","subunits.Entrez.IDs.":"1786;10155;9869;57343","Protein.complex.purification.method":"MI:0402-chromatin immunoprecipitation assays","GO.ID":"GO:0006306;GO:0003677;GO:0005634;GO:0090309","GO.description":"DNA methylation;DNA binding;nucleus;positive regulation of methylation-dependent chromatin silencing","FunCat.ID":"10.01.09.01;16.03.01;70.10","FunCat.description":"DNA methylation;DNA binding;nucleus","PubMed.ID":24623306,"subunits.Protein.name.":"DNA ;Transcription intermediary factor 1-beta ;Histone-lysine N-methyltransferase SETDB1;Zinc finger protein 304","subunits.Gene.name.":"DNMT1;TRIM28;SETDB1;ZNF304","subunits.Gene.name.syn.":"AIM CXXC9 DNMT;KAP1 RNF96 TIF1B;KIAA0067 KMT1E;","Disease.comment":"The ZNF304-corepressor complex is involved in colorectal cancer. ZNF304 is a protein that binds to stretches of DNA, including regions of DNA at the start of several tumor suppressor genes, and it recruits the enzymes that add the chemical marks that switch off these genes.","Subunits.comment":"None","Complex.comment":"Promoter-bound ZNF304 recruits a corepressor complex that includes the DNA methyltransferase DNMT1, resulting in DNAhypermethylation and transcriptional silencing.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6346,"ComplexName":"TrkB-Slp1-Rab27b-Crmp2-Kinesin-1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"embryonic rat brains, growth cone vesicle fractions","subunits.UniProt.IDs.":"P37285;P47942;Q2PQA9;Q4KMA1;Q63604;Q6QLM7;Q99P74","subunits.Entrez.IDs.":"171041;25416;117550;297872;25054;314906;84590","Protein.complex.purification.method":"MI:0029-cosedimentation through density gradients;MI:0019-coimmunoprecipitation","GO.ID":"GO:0008089;GO:0031547","GO.description":"anterograde axonal transport;brain-derived neurotrophic factor receptor signaling pathway","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":19460344,"subunits.Protein.name.":"Kinesin light chain 1;Dihydropyrimidinase-related protein 2;Kinesin-1 heavy chain ;Protein Sytl1;BDNF/NT-3 growth factors receptor ;Kinesin heavy chain isoform 5A;Ras-related protein Rab-27B","subunits.Gene.name.":"Klc1;Dpysl2;Kif5b;Sytl1;Ntrk2;Kif5a;Rab27b","subunits.Gene.name.syn.":"Klc, Kns2;Crmp2;Khc;Slp-1;Trkb;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"A subset of total cellular TrkB forms a complex with Slp1/Rab27/CRMP-2/Kinesin-1under physiological conditions.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6347,"ComplexName":"TNF-R1 signaling complex","Organism":"Human","Synonyms":"TNFR1 complex","Cell.line":"HEK293 cell line","subunits.UniProt.IDs.":"P01375;P19438;Q12933;Q13546;Q15628","subunits.Entrez.IDs.":"7124;7132;7186;8737;8717","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007249","GO.description":"I-kappaB kinase/NF-kappaB signaling","FunCat.ID":"30.01.05.01.04","FunCat.description":"NIK-I-kappaB/NF-kappaB cascade","PubMed.ID":8612133,"subunits.Protein.name.":"Tumor necrosis factor;Tumor necrosis factor receptor superfamily member 1A;TNF receptor-associated factor 2;Receptor-interacting serine/threonine-protein kinase 1;Tumor necrosis factor receptor type 1-associated DEATH domain protein","subunits.Gene.name.":"TNF;TNFRSF1A;TRAF2;RIPK1;TRADD","subunits.Gene.name.syn.":"TNFA, TNFSF2;TNFAR, TNFR1;TRAP3;RIP, RIP1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TNF binds to its receptor TNFR1. TRADD recruits TRAF2 and RIPK1 simultaneously to TNFR1 via its N-terminal TRAF-interacting domain and C-terminal death domain, respectively.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6348,"ComplexName":"G-protein-coupled receptor (GABBR1; GABBR2)","Organism":"Hamster","Synonyms":"None","Cell.line":"CHO cells","subunits.UniProt.IDs.":"O75899;Q9UBS5","subunits.Entrez.IDs.":"9568;2550","Protein.complex.purification.method":"MI:0021-colocalization by fluorescent probes cloning","GO.ID":"GO:1902710;GO:0016917","GO.description":"GABA receptor complex;GABA receptor activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23267088,"subunits.Protein.name.":"Gamma-aminobutyric acid type B receptor subunit 2;Gamma-aminobutyric acid type B receptor subunit 1","subunits.Gene.name.":"GABBR2;GABBR1","subunits.Gene.name.syn.":"GPR51 GPRC3B;GPRC3A","Disease.comment":"None","Subunits.comment":"As protein sequences from hamster were not available at the time of annotation, homologs from homo sapiens were used.","Complex.comment":"Depending on cellular conditions the protein complexes also appear as tetramers (dimers of dimers) and octamers (tetramers of dimers).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6349,"ComplexName":"Tubulin-Crmp2-Klc1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P37285;P47942;P68370;Q6P9V9","subunits.Entrez.IDs.":"171041;25416;64158;500929","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007409;GO:0003401","GO.description":"axonogenesis;axis elongation","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":15935053,"subunits.Protein.name.":"Kinesin light chain 1;Dihydropyrimidinase-related protein 2;Tubulin alpha-1A chain;Tubulin alpha-1B chain","subunits.Gene.name.":"Klc1;Dpysl2;Tuba1a;Tuba1b","subunits.Gene.name.syn.":"Klc, Kns2;Crmp2;Tuba1;Tuba2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Soluble tubulin binds to the middle of CRMP-2 and forms a trimeric complex with CRMP-2-KLC1.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6350,"ComplexName":"LGR5\\u2013Rspo2\\u2013Znrf3 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O75473;Q5SSZ7;Q8BFU0","subunits.Entrez.IDs.":"8549;407821;239405","Protein.complex.purification.method":"MI:0114-x-ray crystallography","GO.ID":"GO:0030111","GO.description":"regulation of Wnt signaling pathway","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26123262,"subunits.Protein.name.":"Leucine-rich repeat-containing G-protein coupled receptor 5 ;E3 ubiquitin-protein ligase ZNRF3 ;R-spondin-2","subunits.Gene.name.":"LGR5;Znrf3;Rspo2","subunits.Gene.name.syn.":"GPR49 GPR67;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6351,"ComplexName":"PKP1-ZO-1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"Cervical-loop derived dental epithelium cells","subunits.UniProt.IDs.":"Q07157;Q13835","subunits.Entrez.IDs.":"7082;5317","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007155;GO:0042481;GO:0036305","GO.description":"cell adhesion;regulation of odontogenesis;ameloblast differentiation","FunCat.ID":"34.07","FunCat.description":"cell adhesion","PubMed.ID":27015268,"subunits.Protein.name.":"Tight junction protein ZO-1;Plakophilin-1","subunits.Gene.name.":"TJP1;PKP1","subunits.Gene.name.syn.":"ZO1;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6352,"ComplexName":"FoxM1-Axin-GSK3beta complex","Organism":"Human","Synonyms":"FOXM1-AXIN1-GSK3B complex","Cell.line":"LN-229 cells","subunits.UniProt.IDs.":"O15169;P49841;Q08050","subunits.Entrez.IDs.":"8312;2932;2305","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26912724,"subunits.Protein.name.":"Axin-1 ;Glycogen synthase kinase-3 beta;Forkhead box protein M1","subunits.Gene.name.":"AXIN1;GSK3B;FOXM1","subunits.Gene.name.syn.":"AXIN;None;FKHL16 HFH11 MPP2 WIN","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6353,"ComplexName":"beta-Catenin destruction complex","Organism":"Human","Synonyms":"CTNNB1-APC-AXIN-GSK3B complex","Cell.line":"MCF-7 cells","subunits.UniProt.IDs.":"O15169;P25054;P35222;P49841","subunits.Entrez.IDs.":"8312;324;1499;2932","Protein.complex.purification.method":"MI:0027-cosedimentation","GO.ID":"GO:0030877","GO.description":"beta-catenin destruction complex","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":11157977,"subunits.Protein.name.":"Axin-1 ;Adenomatous polyposis coli protein;Catenin beta-1;Glycogen synthase kinase-3 beta","subunits.Gene.name.":"AXIN1;APC;CTNNB1;GSK3B","subunits.Gene.name.syn.":"AXIN;DP2.5;CTNNB;None","Disease.comment":"OMIM:114500 Colorectal cancer, OMIM:175100 Adenomatous polyposis of the colon (PMID:27462886).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6354,"ComplexName":"Sox4-beta-catenin-p300 complex","Organism":"Human","Synonyms":"SOX4-CTNNB1-EP300 complex","Cell.line":"Ishikawa cells, Hec-251 cells, Hec6 cells","subunits.UniProt.IDs.":"P35222;Q06945;Q09472","subunits.Entrez.IDs.":"1499;6659;2033","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0051091","GO.description":"positive regulation of sequence-specific DNA binding transcription factor activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26841870,"subunits.Protein.name.":"Catenin beta-1;Transcription factor SOX-4;Histone acetyltransferase p300","subunits.Gene.name.":"CTNNB1;SOX4;EP300","subunits.Gene.name.syn.":"CTNNB;;P300","Disease.comment":"Uterine carcinosarcoma (PMID:26841870).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6355,"ComplexName":"Metabotropic glutamate receptor 1 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS-7 cells","subunits.UniProt.IDs.":"Q13255","subunits.Entrez.IDs.":"2911","Protein.complex.purification.method":"MI:0055-fluorescent resonance energy transfer","GO.ID":"GO:0008066","GO.description":"glutamate receptor activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20826542,"subunits.Protein.name.":"Metabotropic glutamate receptor 1","subunits.Gene.name.":"GRM1","subunits.Gene.name.syn.":"GPRC1A MGLUR1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":6356,"ComplexName":"Metabotropic glutamate receptor 2 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS-7 cells","subunits.UniProt.IDs.":"Q14416","subunits.Entrez.IDs.":"2912","Protein.complex.purification.method":"MI:0055-fluorescent resonance energy transfer","GO.ID":"GO:0008066","GO.description":"glutamate receptor activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20826542,"subunits.Protein.name.":"Metabotropic glutamate receptor 2","subunits.Gene.name.":"GRM2","subunits.Gene.name.syn.":"GPRC1B MGLUR2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":6357,"ComplexName":"Metabotropic glutamate receptor 4 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS-7 cells","subunits.UniProt.IDs.":"Q14833","subunits.Entrez.IDs.":"2914","Protein.complex.purification.method":"MI:0055-fluorescent resonance energy transfer","GO.ID":"GO:0008066","GO.description":"glutamate receptor activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20826542,"subunits.Protein.name.":"Metabotropic glutamate receptor 4","subunits.Gene.name.":"GRM4","subunits.Gene.name.syn.":"GPRC1D MGLUR4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":6358,"ComplexName":"Metabotropic glutamate receptor 7 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS-7 cells","subunits.UniProt.IDs.":"Q14831","subunits.Entrez.IDs.":"2917","Protein.complex.purification.method":"MI:0055-fluorescent resonance energy transfer","GO.ID":"GO:0008066","GO.description":"glutamate receptor activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20826542,"subunits.Protein.name.":"Metabotropic glutamate receptor 7","subunits.Gene.name.":"GRM7","subunits.Gene.name.syn.":"GPRC1G MGLUR7","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":6359,"ComplexName":"RHAMM-beta-catenin complex","Organism":"Human","Synonyms":"None","Cell.line":"HT-1080 cell","subunits.UniProt.IDs.":"O75330;P35222","subunits.Entrez.IDs.":"3161;1499","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0042127","GO.description":"regulation of cell proliferation","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26825774,"subunits.Protein.name.":"Hyaluronan mediated motility receptor ;Catenin beta-1","subunits.Gene.name.":"HMMR;CTNNB1","subunits.Gene.name.syn.":"IHABP RHAMM;CTNNB","Disease.comment":"Fibrosarcoma (PMID:26825774).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6360,"ComplexName":"Metabotropic glutamate receptor 8 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS-7 cells","subunits.UniProt.IDs.":"O00222","subunits.Entrez.IDs.":"2918","Protein.complex.purification.method":"MI:0055-fluorescent resonance energy transfer","GO.ID":"GO:0008066","GO.description":"glutamate receptor activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20826542,"subunits.Protein.name.":"Metabotropic glutamate receptor 8","subunits.Gene.name.":"GRM8","subunits.Gene.name.syn.":"GPRC1H MGLUR8","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":6361,"ComplexName":"PDK1-beta-catenin complex","Organism":"Rat","Synonyms":"Pdpk1-Ctnnb1 complex","Cell.line":"IEC-18 cells","subunits.UniProt.IDs.":"O55173;Q9WU82","subunits.Entrez.IDs.":"81745;84353","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26739494,"subunits.Protein.name.":"3-phosphoinositide-dependent protein kinase 1 ;Catenin beta-1","subunits.Gene.name.":"Pdpk1;Ctnnb1","subunits.Gene.name.syn.":"Pdk1;Catnb","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6362,"ComplexName":"PDLIM1-E-cadherin-beta-catenin complex","Organism":"Human","Synonyms":"PDLIM1-CDH1-CTNNB1 complex","Cell.line":"None","subunits.UniProt.IDs.":"O00151;P12830;P35222","subunits.Entrez.IDs.":"9124;999;1499","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0061635","GO.description":"regulation of protein complex stability","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26701804,"subunits.Protein.name.":"PDZ and LIM domain protein 1 ;Cadherin-1;Catenin beta-1","subunits.Gene.name.":"PDLIM1;CDH1;CTNNB1","subunits.Gene.name.syn.":"CLIM1 CLP36;CDHE UVO;CTNNB","Disease.comment":"Colorectal cancer (PMID:26701804).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6363,"ComplexName":"mGluR2-mGluR4 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK cells","subunits.UniProt.IDs.":"Q14416;Q14833","subunits.Entrez.IDs.":"2912;2914","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0008066","GO.description":"glutamate receptor activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":24381270,"subunits.Protein.name.":"Metabotropic glutamate receptor 2 ;Metabotropic glutamate receptor 4","subunits.Gene.name.":"GRM2;GRM4","subunits.Gene.name.syn.":"GPRC1B MGLUR2;GPRC1D MGLUR4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6364,"ComplexName":"OVOL2-beta-catenin-TCF4 complex","Organism":"Human","Synonyms":"None","Cell.line":"LS174T cells","subunits.UniProt.IDs.":"P15884;P35222;Q9BRP0","subunits.Entrez.IDs.":"6925;1499;58495","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0060828","GO.description":"regulation of canonical Wnt signaling pathway","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26619963,"subunits.Protein.name.":"Transcription factor 4 ;Catenin beta-1;Transcription factor Ovo-like 2","subunits.Gene.name.":"TCF4;CTNNB1;OVOL2","subunits.Gene.name.syn.":"BHLHB19 ITF2 SEF2;CTNNB;ZNF339","Disease.comment":"Colorectal cancer (PMID:26619963).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6365,"ComplexName":"Synexin-sorcin complex","Organism":"Human","Synonyms":"ANX7-SRI complex","Cell.line":"None","subunits.UniProt.IDs.":"P20073;P30626","subunits.Entrez.IDs.":"310;6717","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0042583;GO:0042584","GO.description":"chromaffin granule;chromaffin granule membrane","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":9268363,"subunits.Protein.name.":"Annexin A7;Sorcin","subunits.Gene.name.":"ANXA7;SRI","subunits.Gene.name.syn.":"ANX7 SNX;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Synexin (annexin VII) forms a complex with sorcin and recruits this protein to chromaffin granule membranes in a Ca2+-dependent manner. Sorcin is able to inhibit synexin-mediated chromaffin granule aggregation in a manner saturable with increasing sorcin concentrations, but does not influence the Ca2+ sensitivity of synexin-mediated granule aggregation. Therefore, the interaction between sorcin and synexin may serve to regulate the functions of these proteins on membrane surfaces in a Ca2+-dependent manner. Overlay assays using deletion constructs of the synexin N-terminal domain mapped the sorcin binding site to the N-terminal 31 amino acids of the synexin protein. Affinity chromatography identified sorcin as a Ca2+-dependent synexin-binding protein.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6366,"ComplexName":"MCC complex (p85alpha, p110alpha, Akt,14-3-3theta, beta-catenin)","Organism":"Mouse","Synonyms":"Multiprotein cytosolic complex, Pik3r1-Pik3ca-Akt1-Ywhaz-","Cell.line":"Intestinal epithelial cells","subunits.UniProt.IDs.":"P26450;P31750;P42337;P63101;Q02248","subunits.Entrez.IDs.":"18708;11651;18706;22631;12387","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0050727","GO.description":"regulation of inflammatory response","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26565021,"subunits.Protein.name.":"Phosphatidylinositol 3-kinase regulatory subunit alpha ;RAC-alpha serine/threonine-protein kinase;Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform ;14-3-3 protein zeta/delta;Catenin beta-1","subunits.Gene.name.":"Pik3r1;Akt1;Pik3ca;Ywhaz;Ctnnb1","subunits.Gene.name.syn.":";Akt, Rac;;None;Catnb","Disease.comment":"Colitis and colitis-associated cancer (PMID:26565021).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6367,"ComplexName":"mGluR2-mGluR7 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS-7 cells","subunits.UniProt.IDs.":"Q14416;Q14831","subunits.Entrez.IDs.":"2912;2917","Protein.complex.purification.method":"MI:0055-fluorescent resonance energy transfer","GO.ID":"GO:0008066","GO.description":"glutamate receptor activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20826542,"subunits.Protein.name.":"Metabotropic glutamate receptor 2 ;Metabotropic glutamate receptor 7","subunits.Gene.name.":"GRM2;GRM7","subunits.Gene.name.syn.":"GPRC1B MGLUR2;GPRC1G MGLUR7","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6368,"ComplexName":"mGluR2-mGluR8 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS-7 cells","subunits.UniProt.IDs.":"O00222;Q14416","subunits.Entrez.IDs.":"2918;2912","Protein.complex.purification.method":"MI:0055-fluorescent resonance energy transfer","GO.ID":"GO:0008066","GO.description":"glutamate receptor activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20826542,"subunits.Protein.name.":"Metabotropic glutamate receptor 8 ;Metabotropic glutamate receptor 2","subunits.Gene.name.":"GRM8;GRM2","subunits.Gene.name.syn.":"GPRC1H MGLUR8;GPRC1B MGLUR2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6369,"ComplexName":"mGluR3-mGluR4 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS-7 cells","subunits.UniProt.IDs.":"Q14832;Q14833","subunits.Entrez.IDs.":"2913;2914","Protein.complex.purification.method":"MI:0055-fluorescent resonance energy transfer","GO.ID":"GO:0008066","GO.description":"glutamate receptor activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20826542,"subunits.Protein.name.":"Metabotropic glutamate receptor 3 ;Metabotropic glutamate receptor 4","subunits.Gene.name.":"GRM3;GRM4","subunits.Gene.name.syn.":"GPRC1C MGLUR3;GPRC1D MGLUR4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6370,"ComplexName":"mGluR3-mGluR7 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS-7 cells","subunits.UniProt.IDs.":"Q14831;Q14832","subunits.Entrez.IDs.":"2917;2913","Protein.complex.purification.method":"MI:0055-fluorescent resonance energy transfer","GO.ID":"GO:0008066","GO.description":"glutamate receptor activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20826542,"subunits.Protein.name.":"Metabotropic glutamate receptor 7 ;Metabotropic glutamate receptor 3","subunits.Gene.name.":"GRM7;GRM3","subunits.Gene.name.syn.":"GPRC1G MGLUR7;GPRC1C MGLUR3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6371,"ComplexName":"mGluR3-mGluR8 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS-7 cells","subunits.UniProt.IDs.":"O00222;Q14832","subunits.Entrez.IDs.":"2918;2913","Protein.complex.purification.method":"MI:0055-fluorescent resonance energy transfer","GO.ID":"GO:0008066","GO.description":"glutamate receptor activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20826542,"subunits.Protein.name.":"Metabotropic glutamate receptor 8 ;Metabotropic glutamate receptor 3","subunits.Gene.name.":"GRM8;GRM3","subunits.Gene.name.syn.":"GPRC1H MGLUR8;GPRC1C MGLUR3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6372,"ComplexName":"GABAB core receptor","Organism":"Rat","Synonyms":"None","Cell.line":"brain membranes","subunits.UniProt.IDs.":"O88871;Q50H33;Q5DTY9;Q6WVG3;Q8C7J6;Q9Z0U4","subunits.Entrez.IDs.":"83633;243043;383348;239217;207474;81657","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007214;GO:1902712","GO.description":"gamma-aminobutyric acid signaling pathway;G-protein coupled GABA receptor complex","FunCat.ID":"30.05.02.24.04","FunCat.description":"gamma-aminobutyric acid signalling pathway","PubMed.ID":26691831,"subunits.Protein.name.":"Gamma-aminobutyric acid type B receptor subunit 2 ;BTB/POZ domain-containing protein KCTD8;BTB/POZ domain-containing protein KCTD16;BTB/POZ domain-containing protein KCTD12 ;Potassium channel tetramerisation domain containing 12b ;Gamma-aminobutyric acid type B receptor subunit 1","subunits.Gene.name.":"Gabbr2;Kctd8;Kctd16;Kctd12;Kctd12b;Gabbr1","subunits.Gene.name.syn.":"Gpr51;;Gm1267 Kiaa1317;Pfet1;;","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Rattus norvegicus (Rat)"}
{"ComplexID":6373,"ComplexName":"MiDAC complex","Organism":"Human","Synonyms":"None","Cell.line":"K562 cells","subunits.UniProt.IDs.":"Q13547;Q6PJG2;Q92769;Q9H147","subunits.Entrez.IDs.":"3065;91748;3066;116092","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":21258344,"subunits.Protein.name.":"Histone deacetylase 1;ELM2 and SANT domain-containing protein 1 ;Histone deacetylase 2;Deoxynucleotidyltransferase terminal-interacting protein 1","subunits.Gene.name.":"HDAC1;ELMSAN1;HDAC2;DNTTIP1","subunits.Gene.name.syn.":"RPD3L1;C14orf117 C14orf43;None;C20orf167 TDIF1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6374,"ComplexName":"Calcineurin-FKBP12 complex","Organism":"Human","Synonyms":"CaN-FKBP12 complex","Cell.line":"None","subunits.UniProt.IDs.":"P62942;P63098;Q08209","subunits.Entrez.IDs.":"2280;5534;5530","Protein.complex.purification.method":"MI:0114-x-ray crystallography","GO.ID":"GO:0019722;GO:0005955;GO:0005516;GO:0016791","GO.description":"calcium-mediated signaling;calcineurin complex;calmodulin binding;phosphatase activity","FunCat.ID":"30.01.09.03","FunCat.description":"Ca2+ mediated signal transduction","PubMed.ID":8524402,"subunits.Protein.name.":"Peptidyl-prolyl cis-trans isomerase FKBP1A;Calcineurin subunit B type 1;Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform","subunits.Gene.name.":"FKBP1A;PPP3R1;PPP3CA","subunits.Gene.name.syn.":"FKBP1 FKBP12;CNA2 CNB;CALNA CNA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Calcineurin (CaN) is a calcium- and calmodulin-dependent protein serine/threonine phosphatase which is critical for several important cellular processes, including T-cell activation. CaN is the target of the immunosuppressive drugs cyclosporin A and FK506, which inhibit CaN after forming complexes with cytoplasmic binding proteins (cyclophilin and FKBP12, respectively). In the native CaN structure, an auto-inhibitory element binds at the Zn/Fe-containing active site. The metal-site geometry and active-site water structure suggest a catalytic mechanism involving nucleophilic attack on the substrate phosphate by a metal-activated water molecule. In the FKBP12-FK506-CaN complex, the auto-inhibitory element is displaced from the active site. The site of binding of FKBP12-FK506 appears to be shared by other non-competitive inhibitors of calcineurin, including a natural anchoring protein. CaN is a heterodimer composed of a catalytic A unit and a regulatory B unit.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6375,"ComplexName":"PEF1-ALG2 complex","Organism":"Human","Synonyms":"PEF1-PDCD6 complex","Cell.line":"Jurkat cells","subunits.UniProt.IDs.":"O75340;Q9UBV8","subunits.Entrez.IDs.":"10016;553115","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0091-chromatography technologies","GO.ID":"GO:0051592;GO:0005737","GO.description":"response to calcium ion;cytoplasm","FunCat.ID":"70.03","FunCat.description":"cytoplasm","PubMed.ID":11278427,"subunits.Protein.name.":"Programmed cell death protein 6;Peflin","subunits.Gene.name.":"PDCD6;PEF1","subunits.Gene.name.syn.":"ALG2;ABP32","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Peflin dissociated from ALG-2 in the presence of Ca(2+). Peflin and ALG-2 co-localized in the cytoplasm, but ALG-2 was also detected in the nuclei as revealed by immunofluorescent staining and subcellular fractionation. Peflin was recovered in the cytosolic fraction in the absence of Ca(2+) but in the membrane/cytoskeletal fraction in the presence of Ca(2+). These results suggest that peflin has features common to those of other PEF proteins (dimerization and translocation to membranes) and may modulate the function of ALG-2 in Ca(2+) signaling. Peflin, a Ca(2+)-binding protein, belongs to the penta-EF-hand (PEF) protein family, which includes the calpain small subunit, sorcin, grancalcin, and ALG-2 (apoptosis-linked gene 2).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6376,"ComplexName":"Calcineurin (subunit CnA) -Cacng8 complex","Organism":"Mammalia","Synonyms":"Calcineurin (subunit CnA) -TARP gamma-8 complex","Cell.line":"primary hippocampal neurons from embryonic day 18 Wistar rats;","subunits.UniProt.IDs.":"Q08209;Q8VHW5","subunits.Entrez.IDs.":"5530;140729","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation;MI:0096-pull down","GO.ID":"GO:0004872;GO:0005102;GO:0055085;GO:0005262","GO.description":"receptor activity;receptor binding;transmembrane transport;calcium channel activity","FunCat.ID":"16.01.01","FunCat.description":"receptor binding","PubMed.ID":24418105,"subunits.Protein.name.":"Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform;Voltage-dependent calcium channel gamma-8 subunit","subunits.Gene.name.":"PPP3CA;Cacng8","subunits.Gene.name.syn.":"CALNA CNA;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Transmembrane alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA) receptor regulatory proteins (TARPs) are auxiliary subunits that regulate AMPA receptor trafficking to the plasma membrane and localization to postsynaptic sites. The classical TARP family consists of four members: stargazin/gamma-2, gamma-3, gamma-4 and gamma-8. The TARP gamma-8 isoform, which is highly expressed in the hippocampus, has a unique, long C-terminal domain with five distinct regions: two glycine-rich regions, a serine/arginine-rich region, a proline/alanine (P/A) rich region, and a PSD-95/Dlg/ZO-1 (PDZ) binding motif. Calcineurin/PP2B interacts with TARP gamma-8 in a Ca2+-dependent manner and co-localizes with TARP gamma-8 in rat primary hippocampal neurons. The long C-terminal tail of TARP gamma-8 is essential for association with calcineurin/PP2B.","SWISSPROT.organism":"Homo sapiens (Human);Rattus norvegicus (Rat)"}
{"ComplexID":6377,"ComplexName":"Dlg4-Cacng8 complex","Organism":"Rat","Synonyms":"Psd95-TARP gamma-8 complex","Cell.line":"None","subunits.UniProt.IDs.":"P31016;Q8VHW5","subunits.Entrez.IDs.":"29495;140729","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0005262;GO:0004872;GO:0055085","GO.description":"calcium channel activity;receptor activity;transmembrane transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":24418105,"subunits.Protein.name.":"Disks large homolog 4;Voltage-dependent calcium channel gamma-8 subunit","subunits.Gene.name.":"Dlg4;Cacng8","subunits.Gene.name.syn.":"Dlgh4, Psd95;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Transmembrane alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA) receptor regulatory proteins (TARPs) are auxiliary subunits that regulate AMPA receptor trafficking to the plasma membrane and localization to postsynaptic sites. The classical TARP family consists of four members: stargazin/gamma-2, gamma-3, gamma-4 and gamma-8. The TARP gamma-8 isoform, which is highly expressed in the hippocampus, has a unique, long C-terminal domain with five distinct regions: two glycine-rich regions, a serine/arginine-rich region, a proline/alanine (P/A) rich region, and a PSD-95/Dlg/ZO-1 (PDZ) binding motif.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6378,"ComplexName":"Cacng8-Gria1-Gria2 complex","Organism":"Rat","Synonyms":"None","Cell.line":"hippocampal neurons","subunits.UniProt.IDs.":"P19490;P19491;Q8VHW5","subunits.Entrez.IDs.":"50592;29627;140729","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0004872;GO:0055085;GO:0008066;GO:0005262","GO.description":"receptor activity;transmembrane transport;glutamate receptor activity;calcium channel activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":24418105,"subunits.Protein.name.":"Glutamate receptor 1;Glutamate receptor 2;Voltage-dependent calcium channel gamma-8 subunit","subunits.Gene.name.":"Gria1;Gria2;Cacng8","subunits.Gene.name.syn.":"Glur1;Glur2;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Transmembrane a-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA) receptor regulatory proteins (TARPs) are auxiliary subunits that regulate AMPA receptor trafficking to the plasma membrane and localization to postsynaptic sites. The classical TARP family consists of four members: stargazin/gamma-2, gamma-3, gamma-4 and gamma-8. The TARP gamma-8 isoform, which is highly expressed in the hippocampus, has a unique, long C-terminal domain with five distinct regions: two glycine-rich regions, a serine/arginine-rich region, a proline/alanine (P/A) rich region, and a PSD-95/Dlg/ZO-1 (PDZ) binding motif.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6379,"ComplexName":"Calcineurin (subunit CnA) -Cacng8 complex","Organism":"Rat","Synonyms":"Calcineurin (subunit CnA) -TARP gamma-8 complex","Cell.line":"hippocampal neurons","subunits.UniProt.IDs.":"P63329;Q8VHW5","subunits.Entrez.IDs.":"24674;140729","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0004872;GO:0005102;GO:0055085;GO:0005262","GO.description":"receptor activity;receptor binding;transmembrane transport;calcium channel activity","FunCat.ID":"16.01.01","FunCat.description":"receptor binding","PubMed.ID":24418105,"subunits.Protein.name.":"Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform;Voltage-dependent calcium channel gamma-8 subunit","subunits.Gene.name.":"Ppp3ca;Cacng8","subunits.Gene.name.syn.":"Calna;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Transmembrane alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA) receptor regulatory proteins (TARPs) are auxiliary subunits that regulate AMPA receptor trafficking to the plasma membrane and localization to postsynaptic sites. The classical TARP family consists of four members: stargazin/gamma-2, gamma-3, gamma-4 and gamma-8. The TARP gamma-8 isoform, which is highly expressed in the hippocampus, has a unique, long C-terminal domain with five distinct regions: two glycine-rich regions, a serine/arginine-rich region, a proline/alanine (P/A) rich region, and a PSD-95/Dlg/ZO-1 (PDZ) binding motif. Calcineurin interacts with TARP gamma-8 in a Ca2+-dependent manner and co-localizes with TARP gamma-8 in rat primary hippocampal neurons. The long C-terminal tail of TARP gamma-8 is essential for association with calcineurin.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6380,"ComplexName":"Cacng2-Gria1-Gria2 complex","Organism":"Rat","Synonyms":"None","Cell.line":"hippocampal neurons","subunits.UniProt.IDs.":"P19490;P19491;Q71RJ2","subunits.Entrez.IDs.":"50592;29627;None","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0004872;GO:0055085;GO:0008066;GO:0005262","GO.description":"receptor activity;transmembrane transport;glutamate receptor activity;calcium channel activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":24418105,"subunits.Protein.name.":"Glutamate receptor 1;Glutamate receptor 2;Voltage-dependent calcium channel gamma-2 subunit","subunits.Gene.name.":"Gria1;Gria2;Cacng2","subunits.Gene.name.syn.":"Glur1;Glur2;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Transmembrane a-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA) receptor regulatory proteins (TARPs) are auxiliary subunits that regulate AMPA receptor trafficking to the plasma membrane and localization to postsynaptic sites. The classical TARP family consists of four members: stargazin/gamma-2, gamma-3, gamma-4 and gamma-8.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6381,"ComplexName":"NPHP1-NPHP4-BCAR1 complex","Organism":"Human","Synonyms":"NPHP1-NPHP4-p130Cas complex","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"O15259;O75161;P56945","subunits.Entrez.IDs.":"4867;261734;9564","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0098609;GO:0007160;GO:0051301","GO.description":"cell-cell adhesion;cell-matrix adhesion;cell division","FunCat.ID":"34.07.02","FunCat.description":"cell-matrix adhesion","PubMed.ID":15661758,"subunits.Protein.name.":"Nephrocystin-1;Nephrocystin-4;Breast cancer anti-estrogen resistance protein 1","subunits.Gene.name.":"NPHP1;NPHP4;BCAR1","subunits.Gene.name.syn.":"NPH1;KIAA0673;CAS CASS1 CRKAS","Disease.comment":"Nephrocystin and nephrocystin-4 are proteins involved in familial juvenile nephronophthisis, an autosomal recessive nephropathy characterized by cyst formation and renal fibrosis (PMID:15661758).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6382,"ComplexName":"Dlg4-Cacng2 complex","Organism":"Rat","Synonyms":"Psd95-TARP gamma-2 complex","Cell.line":"hippocampal neurons","subunits.UniProt.IDs.":"P31016;Q71RJ2","subunits.Entrez.IDs.":"29495;None","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0004872;GO:0055085;GO:0005262","GO.description":"receptor activity;transmembrane transport;calcium channel activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":24418105,"subunits.Protein.name.":"Disks large homolog 4;Voltage-dependent calcium channel gamma-2 subunit","subunits.Gene.name.":"Dlg4;Cacng2","subunits.Gene.name.syn.":"Dlgh4, Psd95;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Transmembrane alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA) receptor regulatory proteins (TARPs) are auxiliary subunits that regulate AMPA receptor trafficking to the plasma membrane and localization to postsynaptic sites. The classical TARP family consists of four members: stargazin/gamma-2, gamma-3, gamma-4 and gamma-8.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6383,"ComplexName":"Nphp1-Ptk2b-Bcar1-tensin complex","Organism":"Mouse","Synonyms":"Nphp1-Pyk2-p130cas-tensin complex","Cell.line":"embryonic kidneys and testes","subunits.UniProt.IDs.":"Q61140;Q8CGB6;Q9QVP9;Q9QY53","subunits.Entrez.IDs.":"12927;209039;19229;53885","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0016310;GO:0007160","GO.description":"phosphorylation;cell-matrix adhesion","FunCat.ID":"34.07.02","FunCat.description":"cell-matrix adhesion","PubMed.ID":11493697,"subunits.Protein.name.":"Breast cancer anti-estrogen resistance protein 1;Tensin-2;Protein-tyrosine kinase 2-beta;Nephrocystin-1","subunits.Gene.name.":"Bcar1;Tns2;Ptk2b;Nphp1","subunits.Gene.name.syn.":"Cas, Crkas, p130cas;Tenc1;Fak2, Pyk2, Raftk;Nph1","Disease.comment":"None","Subunits.comment":"Since the authors did not specify tensin, we used isoform Tns2.","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6384,"ComplexName":"Calcineurin (subunit CnA)-Cacng8-Tuba1a complex","Organism":"Rat","Synonyms":"None","Cell.line":"hippocampal neurons","subunits.UniProt.IDs.":"P63329;P68370;Q8VHW5","subunits.Entrez.IDs.":"24674;64158;140729","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0004872;GO:0005102;GO:0055085;GO:0005262","GO.description":"receptor activity;receptor binding;transmembrane transport;calcium channel activity","FunCat.ID":"16.01.01","FunCat.description":"receptor binding","PubMed.ID":24418105,"subunits.Protein.name.":"Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform;Tubulin alpha-1A chain;Voltage-dependent calcium channel gamma-8 subunit","subunits.Gene.name.":"Ppp3ca;Tuba1a;Cacng8","subunits.Gene.name.syn.":"Calna;Tuba1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The TARP gamma-8 isoform, which is highly expressed in the hippocampus, has a unique, long C-terminal domain with five distinct regions: two glycine-rich regions, a serine/arginine-rich region, a proline/alanine (P/A) rich region, and a PSD-95/Dlg/ZO-1 (PDZ) binding motif.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6385,"ComplexName":"Calcineurin complex (Calna, Cna2, Gria1, Gria2, Cacng8)","Organism":"Rat","Synonyms":"None","Cell.line":"hippocampal neurons","subunits.UniProt.IDs.":"P19490;P19491;P63100;P63329;Q8VHW5","subunits.Entrez.IDs.":"50592;29627;29748;24674;140729","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0004872;GO:0055085;GO:0005262;GO:0008066","GO.description":"receptor activity;transmembrane transport;calcium channel activity;glutamate receptor activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":24418105,"subunits.Protein.name.":"Glutamate receptor 1;Glutamate receptor 2;Calcineurin subunit B type 1;Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform;Voltage-dependent calcium channel gamma-8 subunit","subunits.Gene.name.":"Gria1;Gria2;Ppp3r1;Ppp3ca;Cacng8","subunits.Gene.name.syn.":"Glur1;Glur2;Cna2,Cnb;Calna;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The TARP gamma-8 isoform, which is highly expressed in the hippocampus, has a unique, long C-terminal domain with five distinct regions: two glycine-rich regions, a serine/arginine-rich region, a proline/alanine (P/A) rich region, and a PSD-95/Dlg/ZO-1 (PDZ) binding motif.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6386,"ComplexName":"Dlg4-Cacng8-Calna complex","Organism":"Rat","Synonyms":"None","Cell.line":"hippocampal neurons","subunits.UniProt.IDs.":"P31016;P63329;Q8VHW5","subunits.Entrez.IDs.":"29495;24674;140729","Protein.complex.purification.method":"MI:0051-fluorescence technologies","GO.ID":"GO:0005262;GO:0055085","GO.description":"calcium channel activity;transmembrane transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":24418105,"subunits.Protein.name.":"Disks large homolog 4;Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform;Voltage-dependent calcium channel gamma-8 subunit","subunits.Gene.name.":"Dlg4;Ppp3ca;Cacng8","subunits.Gene.name.syn.":"Dlgh4, Psd95;Calna;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Transmembrane alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA) receptor regulatory proteins (TARPs) are auxiliary subunits that regulate AMPA receptor trafficking to the plasma membrane and localization to postsynaptic sites. The classical TARP family consists of four members: stargazin/gamma-2, gamma-3, gamma-4 and gamma-8. The TARP gamma-8 isoform, which is highly expressed in the hippocampus, has a unique, long C-terminal domain with five distinct regions: two glycine-rich regions, a serine/arginine-rich region, a proline/alanine (P/A) rich region, and a PSD-95/Dlg/ZO-1 (PDZ) binding motif.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6387,"ComplexName":"Ship1-Hdac1-Hspa2-Kctd19 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"testis","subunits.UniProt.IDs.":"O09106;P17156;Q562E2;Q9ES52","subunits.Entrez.IDs.":"433759;15512;279499;16331","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005634;GO:0007283;GO:0006338","GO.description":"nucleus;spermatogenesis;chromatin remodeling","FunCat.ID":"70.1","FunCat.description":"nucleus","PubMed.ID":18849567,"subunits.Protein.name.":"Histone deacetylase 1;Heat shock-related 70 kDa protein 2;BTB/POZ domain-containing protein KCTD19;Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1","subunits.Gene.name.":"Hdac1;Hspa2;Kctd19;Inpp5d","subunits.Gene.name.syn.":"None;None;None;7a33 Ship Ship1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6388,"ComplexName":"CORVET complex","Organism":"Human","Synonyms":"Class C core vacuole/endosome tethering complex; Endosomal tethering complex CORVET","Cell.line":"MelJuSo cell","subunits.UniProt.IDs.":"Q8N3P4;Q8WUH2;Q96AX1;Q9H269;Q9H270;Q9P253","subunits.Entrez.IDs.":"23355;9392;65082;64601;55823;57617","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0033263;GO:0099022;GO:0034058","GO.description":"CORVET complex;vesicle tethering;endosomal vesicle fusion","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26463206,"subunits.Protein.name.":"Vacuolar protein sorting-associated protein 8 homolog;Transforming growth factor-beta receptor-associated protein 1;Vacuolar protein sorting-associated protein 33A;Vacuolar protein sorting-associated protein 16 homolog;Vacuolar protein sorting-associated protein 11 homolog;Vacuolar protein sorting-associated protein 18 homolog","subunits.Gene.name.":"VPS8;TGFBRAP1;VPS33A;VPS16;VPS11;VPS18","subunits.Gene.name.syn.":"KIAA0804;None;None;None;RNF108;KIAA1475","Disease.comment":"Missense mutations in the gene VPS11 are associated with  hypomyelination and developmental delay (PMID:26307567).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6389,"ComplexName":"HOPS complex","Organism":"Human","Synonyms":"Homotypic fusion and vacuole protein sorting complex; Endosomal tethering complex HOPS","Cell.line":"MelJuSo cell","subunits.UniProt.IDs.":"P49754;Q96AX1;Q96JC1;Q9H269;Q9H270;Q9P253","subunits.Entrez.IDs.":"27072;65082;23339;64601;55823;57617","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0030897;GO:0099022;GO:0034058","GO.description":"HOPS complex;vesicle tethering;endosomal vesicle fusion","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26463206,"subunits.Protein.name.":"Vacuolar protein sorting-associated protein 41 homolog;Vacuolar protein sorting-associated protein 33A;Vam6/Vps39-like protein;Vacuolar protein sorting-associated protein 16 homolog;Vacuolar protein sorting-associated protein 11 homolog;Vacuolar protein sorting-associated protein 18 homolog","subunits.Gene.name.":"VPS41;VPS33A;VPS39;VPS16;VPS11;VPS18","subunits.Gene.name.syn.":"None;None;KIAA0770, TLP, VAM6;None;RNF108;KIAA1475","Disease.comment":"Missense mutations in the gene VPS11 are associated with hypomyelination and developmental delay (PMID:26307567).","Subunits.comment":"None","Complex.comment":"The mammalian HOPS complex is recruited to membranes by binding to the RAB7 effector RILP.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6390,"ComplexName":"Endosomal targeting complex (VIPAS39-VPS33B)","Organism":"Human","Synonyms":"VPS33B-VIPAS39 complex","Cell.line":"MelJuSo cell","subunits.UniProt.IDs.":"Q9H267;Q9H9C1","subunits.Entrez.IDs.":"26276;63894","Protein.complex.purification.method":"None","GO.ID":"GO:0034058;GO:0099022","GO.description":"endosomal vesicle fusion;vesicle tethering","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26463206,"subunits.Protein.name.":"Vacuolar protein sorting-associated protein 33B;Spermatogenesis-defective protein 39 homolog","subunits.Gene.name.":"VPS33B;VIPAS39","subunits.Gene.name.syn.":"None;C14orf133,SPE39,VIPAR","Disease.comment":"Autosomal recessive mutations in VPS33B or VIPAS39 cause arthrogryposis-renal dysfunction-cholestasis (ARC) syndrome.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6391,"ComplexName":"KCTD12-GNB1-GNG2 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"P59768;P62873;Q96CX2","subunits.Entrez.IDs.":"54331;2782;115207","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0002029","GO.description":"desensitization of G-protein coupled receptor protein signaling pathway","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":24836506,"subunits.Protein.name.":"Guanine nucleotide-binding protein G;Guanine nucleotide-binding protein G;BTB/POZ domain-containing protein KCTD12","subunits.Gene.name.":"GNG2;GNB1;KCTD12","subunits.Gene.name.syn.":"None;None;C13orf2,KIAA1778,PFET1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6392,"ComplexName":"KCTD8-GNB1-GNG2 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"P59768;P62873;Q6ZWB6","subunits.Entrez.IDs.":"54331;2782;386617","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007186","GO.description":"G-protein coupled receptor signaling pathway","FunCat.ID":"30.05.02.24","FunCat.description":"G-protein coupled receptor signalling pathway","PubMed.ID":24836506,"subunits.Protein.name.":"Guanine nucleotide-binding protein G;Guanine nucleotide-binding protein G;BTB/POZ domain-containing protein KCTD8","subunits.Gene.name.":"GNG2;GNB1;KCTD8","subunits.Gene.name.syn.":"None;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6393,"ComplexName":"KCTD16-GNB1-GNG2 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"P59768;P62873;Q68DU8","subunits.Entrez.IDs.":"54331;2782;57528","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007186","GO.description":"G-protein coupled receptor signaling pathway","FunCat.ID":"30.05.02.24","FunCat.description":"G-protein coupled receptor signalling pathway","PubMed.ID":24836506,"subunits.Protein.name.":"Guanine nucleotide-binding protein G;Guanine nucleotide-binding protein G;BTB/POZ domain-containing protein KCTD16","subunits.Gene.name.":"GNG2;GNB1;KCTD16","subunits.Gene.name.syn.":"None;None;KIAA1317","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6394,"ComplexName":"CNOT1-CNOT2-CNOT3 complex","Organism":"Human","Synonyms":"CCR4-NOT complex","Cell.line":"None","subunits.UniProt.IDs.":"A5YKK6;O75175;Q9NZN8","subunits.Entrez.IDs.":"23019;4849;4848","Protein.complex.purification.method":"MI:0114-x-ray crystallography","GO.ID":"GO:0006355;GO:0035195;GO:1901873","GO.description":"regulation of transcription, DNA-templated;gene silencing by miRNA;regulation of post-translational protein modification","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":24121232,"subunits.Protein.name.":"CCR4-NOT transcription complex subunit 1;CCR4-NOT transcription complex subunit 3;CCR4-NOT transcription complex subunit 2","subunits.Gene.name.":"CNOT1;CNOT3;CNOT2","subunits.Gene.name.syn.":"CDC39 KIAA1007 NOT1;KIAA0691 LENG2 NOT3;CDC36 NOT2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6395,"ComplexName":"4E-T-DDX6-CNOT1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"A5YKK6;P26196;Q9NRA8","subunits.Entrez.IDs.":"23019;1656;56478","Protein.complex.purification.method":"MI:0114-x-ray crystallography","GO.ID":"GO:0017148;GO:1901834","GO.description":"negative regulation of translation;regulation of deadenylation-independent decapping of nuclear-transcribed mRNA","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26489469,"subunits.Protein.name.":"CCR4-NOT transcription complex subunit 1;Probable ATP-dependent RNA helicase DDX6;Eukaryotic translation initiation factor 4E transporter","subunits.Gene.name.":"CNOT1;DDX6;EIF4ENIF1","subunits.Gene.name.syn.":"CDC39 KIAA1007 NOT1;HLR2 RCK;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6396,"ComplexName":"DNJC3-DNAJB1-HSPA8 complex","Organism":"Human","Synonyms":"P58IPK-HSP40-HSC70 complex","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"P11142;P25685;Q13217","subunits.Entrez.IDs.":"3312;3337;5611","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0039585","GO.description":"PKR signal transduction","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":9920933,"subunits.Protein.name.":"Heat shock cognate 71 kDa protein;DnaJ homolog subfamily B member 1;DnaJ homolog subfamily C member 3","subunits.Gene.name.":"HSPA8;DNAJB1;DNAJC3","subunits.Gene.name.syn.":"HSC70, HSP73, HSPA10;DNAJ1 HDJ1 HSPF1;P58IPK PRKRI","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6397,"ComplexName":"Dnajc5-Sgta complex","Organism":"Mouse","Synonyms":"None","Cell.line":"MIN6 cells","subunits.UniProt.IDs.":"P60904;P63017;Q8BJU0","subunits.Entrez.IDs.":"13002;15481;52551","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0016020;GO:0005802","GO.description":"membrane;trans-Golgi network","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":17034881,"subunits.Protein.name.":"DnaJ homolog subfamily C member 5;Heat shock cognate 71 kDa protein;Small glutamine-rich tetratricopeptide repeat-containing protein alpha","subunits.Gene.name.":"Dnajc5;Hspa8;Sgta","subunits.Gene.name.syn.":"None;Hsc70 Hsc73;Sgt","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6398,"ComplexName":"Dnajc5b-Sgta-Hsc70 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"MIN6 cells","subunits.UniProt.IDs.":"P63017;Q8BJU0;Q9CQ94","subunits.Entrez.IDs.":"15481;52551;66326","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0031982;GO:0016020;GO:0007268","GO.description":"vesicle;membrane;synaptic transmission","FunCat.ID":"34.03.01","FunCat.description":"synaptic transmission","PubMed.ID":17034881,"subunits.Protein.name.":"Heat shock cognate 71 kDa protein;Small glutamine-rich tetratricopeptide repeat-containing protein alpha;DnaJ homolog subfamily C member 5B","subunits.Gene.name.":"Hspa8;Sgta;Dnajc5b","subunits.Gene.name.syn.":"Hsc70 Hsc73;Sgt;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6399,"ComplexName":"DNAJC7-HSPA8-HSP90AA1 complex","Organism":"Mammalia","Synonyms":"TRP2-HSP70-HSP90 complex","Cell.line":"rabbit reticulocyte lysate\\u000b\\u0010\\u000f\\u0003 \\u0004\\u0010\\u000e\\u0006\\u000f\\u0003","subunits.UniProt.IDs.":"P07900;P11142;Q99615","subunits.Entrez.IDs.":"3320;3312;7266","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:1990507;GO:0009408","GO.description":"ATP-independent chaperone mediated protein folding;response to heat","FunCat.ID":"32.01.05","FunCat.description":"heat shock response","PubMed.ID":12853476,"subunits.Protein.name.":"Heat shock protein HSP 90-alpha;Heat shock cognate 71 kDa protein;DnaJ homolog subfamily C member 7","subunits.Gene.name.":"HSP90AA1;HSPA8;DNAJC7","subunits.Gene.name.syn.":"HSP90A HSPC1 HSPCA;HSC70, HSP73, HSPA10;TPR2,TTC2","Disease.comment":"None","Subunits.comment":"Since HSP70 and HSP90 from rabbit were not available in the UniProt database at the time of annotation, the orthologous proteins from homo sapiens were used.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6400,"ComplexName":"AnkG-PKP2-Cx43 complex","Organism":"Rat","Synonyms":"Ank3-Pkp2-Gja1 complex","Cell.line":"Adult heart cells","subunits.UniProt.IDs.":"F1M7L9;O70511;P08050","subunits.Entrez.IDs.":"287925;361833;24392","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0014704","GO.description":"intercalated disc","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":21617128,"subunits.Protein.name.":"Protein Pkp2;Ankyrin-3;Gap junction alpha-1 protein","subunits.Gene.name.":"Pkp2;Ank3;Gja1","subunits.Gene.name.syn.":"None;None;Cxn-43, Cx43","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6401,"ComplexName":"Cr16-N-WASP complex","Organism":"Mammalia","Synonyms":"Cr16-WASL complex","Cell.line":"brain extracts, infected Sf9 cells","subunits.UniProt.IDs.":"Q95107;Q9Z0G8","subunits.Entrez.IDs.":"281577;259242","Protein.complex.purification.method":"MI:0071-molecular sieving;MI:0029-cosedimentation through density gradients;MI:0019-coimmunoprecipitation","GO.ID":"GO:0030426","GO.description":"growth cone","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":11553796,"subunits.Protein.name.":"Neural Wiskott-Aldrich syndrome protein;WAS/WASL-interacting protein family member 3","subunits.Gene.name.":"WASL;Wipf3","subunits.Gene.name.syn.":"None;Cr16","Disease.comment":"None","Subunits.comment":"Since Cr16 from rat was used in additional experiments, in vitro by pull-down assay, coexpression in insect cells, and in vivo by double-staining immunof luorescence microscopy in primary hippocampal neurons, the corresponding protein was used..","Complex.comment":"CR16 and N-WASP colocalize significantly in the cell body, axons, and growth cones, including many of the filopodial tips as shownn in rat embryonic hippocampal neurons.  Only CR16+Ex7 and notCR16-Ex7 has the ability to bind N-WASP.","SWISSPROT.organism":"Bos taurus (Bovine);Rattus norvegicus (Rat)"}
{"ComplexID":6402,"ComplexName":"NMNAT2-HSP90 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293-tau cells","subunits.UniProt.IDs.":"P07900;Q9BZQ4","subunits.Entrez.IDs.":"3320;23057","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0061077;GO:0042026","GO.description":"chaperone-mediated protein folding;protein refolding","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":27254664,"subunits.Protein.name.":"Heat shock protein HSP 90-alpha;Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2","subunits.Gene.name.":"HSP90AA1;NMNAT2","subunits.Gene.name.syn.":"HSP90A HSPC1 HSPCA;C1orf15,KIAA0479","Disease.comment":"Brain NMNAT2 mRNA levels correlate positively with global cognitive function and negatively with Alzheimer disease pathology. In Alzheimer disease brains, NMNAT2 mRNA and protein levels are reduced.","Subunits.comment":"None","Complex.comment":"Elevating NMNAT2 levels in rTg4510 mice (aFrontotemporal Dementia and Parkinsonism-17 (FTDP-17) tauopathy model) ameliorates their neurodegenerative phenotype. These finding suggest a role for NMNAT2 in neuronal maintenance in the brain, but the mechanism underlying neuroprotection remains to be elucidated.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6403,"ComplexName":"MST1-SAV1 complex","Organism":"Human","Synonyms":"None","Cell.line":"293T cells","subunits.UniProt.IDs.":"Q13043;Q9H4B6","subunits.Entrez.IDs.":"6789;60485","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0060271","GO.description":"cilium assembly","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":16930133,"subunits.Protein.name.":"Serine/threonine-protein kinase 4;Protein salvador homolog 1","subunits.Gene.name.":"STK4;SAV1","subunits.Gene.name.syn.":"KRS2, MST1;WW45","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The effect of Mst2 on Sav phosphorylation and stability was almost always greater than that of Mst1, suggesting that Sav is a preferred partner-substrate of Mst2 compared to Mst1. Sav is phosphorylated by Mst and the phosphorylation is likely to be direct.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6404,"ComplexName":"MST2-SAV1 complex","Organism":"Human","Synonyms":"None","Cell.line":"293T cells","subunits.UniProt.IDs.":"Q13188;Q9H4B6","subunits.Entrez.IDs.":"6788;60485","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0060271","GO.description":"cilium assembly","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":16930133,"subunits.Protein.name.":"Serine/threonine-protein kinase 3;Protein salvador homolog 1","subunits.Gene.name.":"STK3;SAV1","subunits.Gene.name.syn.":"KRS1, MST2;WW45","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The effect of Mst2 on Sav phosphorylation and stability was almost always greater than that of Mst1, suggesting that Sav is a preferred partner-substrate of Mst2 compared to Mst1. Sav is phosphorylated by Mst and the phosphorylation is likely to be direct.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6405,"ComplexName":"MITRAC12-SURF1-COX1 complex","Organism":"Human","Synonyms":"COA3-SURF1-MT-CO1 complex","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"P00395;Q15526;Q9Y2R0","subunits.Entrez.IDs.":"4512;6834;28958","Protein.complex.purification.method":"MI:0047-far western blotting;MI:0276-blue native page;MI:0019-coimmunoprecipitation","GO.ID":"GO:0005739;GO:0005743;GO:0006412","GO.description":"mitochondrion;mitochondrial inner membrane;translation","FunCat.ID":"70.16;70.16.05;12.04","FunCat.description":"mitochondrion;mitochondrial inner membrane;translation","PubMed.ID":23260140,"subunits.Protein.name.":"Cytochrome c oxidase subunit 1;Surfeit locus protein 1;Cytochrome c oxidase assembly factor 3 homolog, mitochondrial","subunits.Gene.name.":"MT-CO1;SURF1;COA3","subunits.Gene.name.syn.":"COI, COXI, MTCO1;None;CCDC56,MITRAC12,HSPC009","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Copurification of MITRAC12 with COX1 and SURF1 suggested a role in early steps of cytochrome c oxidase biogenesis. MITRAC12 is a cytochrome c oxidase assembly factor and required for efficient COX1 translation. Mitochondria from MITRAC12-depleted cells displayed reduced cytochrome c oxidase activity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6406,"ComplexName":"Rgs4-Mor complex","Organism":"Rat","Synonyms":"None","Cell.line":"Brain","subunits.UniProt.IDs.":"P33535;P49799","subunits.Entrez.IDs.":"25601;29480","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0038003","GO.description":"opioid receptor signaling pathway","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26119705,"subunits.Protein.name.":"Mu-type opioid receptor;Regulator of G-protein signaling 4","subunits.Gene.name.":"Oprm1;Rgs4","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6407,"ComplexName":"Vangl1-Vangl2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"Cochlea cells","subunits.UniProt.IDs.":"Q80Z96;Q91ZD4","subunits.Entrez.IDs.":"229658;93840","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0090102","GO.description":"cochlea development","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23029439,"subunits.Protein.name.":"Vang-like protein 1;Vang-like protein 2","subunits.Gene.name.":"Vangl1;Vangl2","subunits.Gene.name.syn.":"Lpp2;Lpp1, Ltap","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6408,"ComplexName":"p85alpha-SHP2-Gab2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"32D cells","subunits.UniProt.IDs.":"P35235;P70305;Q9Z1S8","subunits.Entrez.IDs.":"19247;18708;14389","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0014066","GO.description":"regulation of phosphatidylinositol 3-kinase signaling","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":22806893,"subunits.Protein.name.":"Tyrosine-protein phosphatase non-receptor type 11;Phosphatidylinositol 3-kinase regulatory subunit alpha;GRB2-associated-binding protein 2","subunits.Gene.name.":"Ptpn11;Pik3r1;Gab2","subunits.Gene.name.syn.":"None;None;None","Disease.comment":"OMIM:601626 Leukemia, acute myeloid and systemic mastocytosis (PMID:22806893).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6409,"ComplexName":"BACE1-UBB complex","Organism":"Rat","Synonyms":"Brain, ischemic striatum","Cell.line":"None","subunits.UniProt.IDs.":"P0CG51;P56819","subunits.Entrez.IDs.":"192255;29392","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:1902003","GO.description":"regulation of beta-amyloid formation","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":19844237,"subunits.Protein.name.":"Polyubiquitin-B;Beta-secretase 1","subunits.Gene.name.":"Ubb;Bace1","subunits.Gene.name.syn.":"None;Bace","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6410,"ComplexName":"MITRAC7-COX1 complex","Organism":"Human","Synonyms":"SMIM20-MT-CO1 complex","Cell.line":"None","subunits.UniProt.IDs.":"P00395;Q8N5G0","subunits.Entrez.IDs.":"4512;389203","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005739;GO:1903607","GO.description":"mitochondrion;cytochrome c biosynthetic process","FunCat.ID":"70.16","FunCat.description":"mitochondrion","PubMed.ID":26321642,"subunits.Protein.name.":"Cytochrome c oxidase subunit 1;Small integral membrane protein 20","subunits.Gene.name.":"MT-CO1;SMIM20","subunits.Gene.name.syn.":"COI, COXI, MTCO1;C4orf52,MITRAC7","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cytochrome c oxidase, the terminal enzyme of the respiratory chain, is assembled from mitochondria- and nuclear-encoded subunits. The MITRAC complex represents the central assembly intermediate during this process as it receives imported subunits and regulates mitochondrial translation of COX1 mRNA. MITRAC7 is a COX1-specific chaperone that binds newly synthesized COX1 to stabilize the molecule during assembly. Although a lack of MITRAC7 causes turnover of newly synthesized COX1, overabundance of MITRAC7 traps COX1 in the MITRAC assembly intermediate. Hence, MITRAC7 reveals a checkpoint of the cytochrome c oxidase assembly process.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6411,"ComplexName":"TRIM31-MAGEA1-NSE4 complex","Organism":"Human","Synonyms":"TRIM31-MAGEA1-NSMCE4A complex","Cell.line":"None","subunits.UniProt.IDs.":"P43355;Q9BZY9;Q9NXX6","subunits.Entrez.IDs.":"4100;11074;54780","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006355","GO.description":"regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":25590999,"subunits.Protein.name.":"Melanoma-associated antigen 1;E3 ubiquitin-protein ligase TRIM31;Non-structural maintenance of chromosomes element 4 homolog A","subunits.Gene.name.":"MAGEA1;TRIM31;NSMCE4A","subunits.Gene.name.syn.":"MAGE1,MAGE1A;C6orf13,RNF;C10orf86,PP4762","Disease.comment":"Melanoma (PMID:25590999).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6412,"ComplexName":"AURKA-HDAC6 cilia-disassembly complex","Organism":"Human","Synonyms":"None","Cell.line":"293T cells","subunits.UniProt.IDs.":"O14965;Q9UBN7","subunits.Entrez.IDs.":"6790;10013","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0061523","GO.description":"cilium disassembly","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25367221,"subunits.Protein.name.":"Aurora kinase A;Histone deacetylase 6","subunits.Gene.name.":"AURKA;HDAC6","subunits.Gene.name.syn.":"AIK, AIRK1, ARK1, AURA, AYK1, BTAK, IAK1, STK15, STK6;KIAA0901","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Upon receiving a cell-cycle re-entry cue, Aurora kinase A (AURKA) is activated and in turn enhances the activity of HDAC6, an enzyme that deacetylates ciliary tubulin, promoting cilia disassembly.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6413,"ComplexName":"PDGFB-PDGFRB complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P01127;P09619","subunits.Entrez.IDs.":"5155;5159","Protein.complex.purification.method":"MI:0047-far western blotting","GO.ID":"GO:0035791","GO.description":"platelet-derived growth factor receptor-beta signaling pathway","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":7679113,"subunits.Protein.name.":"Platelet-derived growth factor subunit B;Platelet-derived growth factor receptor beta","subunits.Gene.name.":"PDGFB;PDGFRB","subunits.Gene.name.syn.":"PDGF2,SIS;PDGFR,PDGFR1","Disease.comment":"OMIM:606190 Meningioma, radiation-induced (PMID:8057146).OMIM:607907 Dermatofibrosarcoma protuberans (PMID:12202658).OMIM:615007 Basal ganglia calcification (PMID: 23255827).OMIM:228550 Myofibromatosis (PMID: 23731537).OMIM:616592 Kosaki overgrowth syndrome (PMID:25454926).OMIM:601812 Premature aging syndrome(PMID:9056558).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6414,"ComplexName":"RIPK1-FADD-caspase-8 complex","Organism":"Human","Synonyms":"RIPK1-FADD-CASP8 complex","Cell.line":"None","subunits.UniProt.IDs.":"Q13158;Q13546;Q14790","subunits.Entrez.IDs.":"8772;8737;841","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0097342;GO:2001236;GO:0060544","GO.description":"ripoptosome;regulation of extrinsic apoptotic signaling pathway;regulation of necroptotic process","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20038679,"subunits.Protein.name.":"FAS-associated death domain protein;Receptor-interacting serine/threonine-protein kinase 1;Caspase-8","subunits.Gene.name.":"FADD;RIPK1;CASP8","subunits.Gene.name.syn.":"MORT1;RIP, RIP1;MCH5","Disease.comment":"Cancer (PMID:20038679).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6415,"ComplexName":"pallidin-Cappuccino-BLOS1 complex","Organism":"Human","Synonyms":"BLOC1S6-BLOC1S4-BLOC1S1 subcomplex","Cell.line":"None","subunits.UniProt.IDs.":"P78537;Q9NUP1;Q9UL45","subunits.Entrez.IDs.":"2647;55330;26258","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":22203680,"subunits.Protein.name.":"Biogenesis of lysosome-related organelles complex 1 subunit 1;Biogenesis of lysosome-related organelles complex 1 subunit 4;Biogenesis of lysosome-related organelles complex 1 subunit 6","subunits.Gene.name.":"BLOC1S1;BLOC1S4;BLOC1S6","subunits.Gene.name.syn.":"BLOS1 GCN5L1 RT14;CNO;PA, PLDN","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6416,"ComplexName":"dysbindin-Snapin-BLOS2 complex","Organism":"Human","Synonyms":"DTNBP1-SNAPIN-BLOC1S2 subcomplex","Cell.line":"None","subunits.UniProt.IDs.":"O95295;Q6QNY1;Q96EV8","subunits.Entrez.IDs.":"23557;282991;84062","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":22203680,"subunits.Protein.name.":"SNARE-associated protein Snapin;Biogenesis of lysosome-related organelles complex 1 subunit 2;Dysbindin","subunits.Gene.name.":"SNAPIN;BLOC1S2;DTNBP1","subunits.Gene.name.syn.":"BLOC1S7 SNAP25BP SNAPAP;BLOS2 CEAP;BLOC1S8","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6417,"ComplexName":"Fibrinogen complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P02671;P02675;P02679","subunits.Entrez.IDs.":"2243;2244;2266","Protein.complex.purification.method":"MI:0071-molecular sieving;MI:0114-x-ray crystallography","GO.ID":"GO:0030168","GO.description":"platelet activation","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":19296670,"subunits.Protein.name.":"Fibrinogen alpha chain;Fibrinogen beta chain;Fibrinogen gamma chain","subunits.Gene.name.":"FGA;FGB;FGG","subunits.Gene.name.syn.":"None;None;PRO2061","Disease.comment":"Congenital fibrinogen disorders (PMID:).27492693","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6418,"ComplexName":"C1q complex","Organism":"Human","Synonyms":"C1QA-C1QB-C1QC complex","Cell.line":"None","subunits.UniProt.IDs.":"P02745;P02746;P02747","subunits.Entrez.IDs.":"712;713;714","Protein.complex.purification.method":"MI:0071-molecular sieving","GO.ID":"GO:0002376;GO:0006955;GO:0006956;GO:0006958;GO:0045087","GO.description":"immune system process;immune response;complement activation;complement activation, classical pathway;innate immune response","FunCat.ID":"36.25.16;36.25.16.01.01;36.25.16.01","FunCat.description":"immune response;complement response;innate immune response (invertebrates and vertebrates)","PubMed.ID":938474,"subunits.Protein.name.":"Complement C1q subcomponent subunit A;Complement C1q subcomponent subunit B;Complement C1q subcomponent subunit C","subunits.Gene.name.":"C1QA;C1QB;C1QC","subunits.Gene.name.syn.":"None;None;C1QG","Disease.comment":"OMIM:613652 C1q deficiency (PMID:884029, PMID:2894352, PMID:8630118).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6419,"ComplexName":"Bcl2l1-Dnm1l complex","Organism":"Rat","Synonyms":"Bclx-Drp1 complex","Cell.line":"brain","subunits.UniProt.IDs.":"O35303;P53563","subunits.Entrez.IDs.":"114114;24888","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0048488;GO:0030672;GO:0048167","GO.description":"synaptic vesicle endocytosis;synaptic vesicle membrane;regulation of synaptic plasticity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23792689,"subunits.Protein.name.":"Dynamin-1-like protein;Bcl-2-like protein 1","subunits.Gene.name.":"Dnm1l;Bcl2l1","subunits.Gene.name.syn.":"Dlp1;Bclx,Blc2l","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Formation of the Bclx-Drp1 complex is necessary for the enhanced rate of vesicle endocytosis produced by Bclx, providing a mechanism for presynaptic plasticity.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6420,"ComplexName":"Bcl2l1-Dnm1l-Mff-Clta complex","Organism":"Rat","Synonyms":"Bclx-Drp1-Mff-clathrin complex","Cell.line":"brain","subunits.UniProt.IDs.":"O35303;P08081;P53563;Q4KM98","subunits.Entrez.IDs.":"114114;83800;24888;102556337","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005905;GO:0008021","GO.description":"clathrin-coated pit;synaptic vesicle","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23792689,"subunits.Protein.name.":"Dynamin-1-like protein;Clathrin light chain A;Bcl-2-like protein 1;Mitochondrial fission factor","subunits.Gene.name.":"Dnm1l;Clta;Bcl2l1;Mff","subunits.Gene.name.syn.":"Dlp1;None;Bclx,Blc2l;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6421,"ComplexName":"DNTTIP1-ZNF541-HDAC1-HDAC2 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293","subunits.UniProt.IDs.":"Q13547;Q92769;Q9H0D2;Q9H147","subunits.Entrez.IDs.":"3065;3066;84215;116092","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0000118;GO:0004407","GO.description":"histone deacetylase complex;histone deacetylase activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":21573134,"subunits.Protein.name.":"Histone deacetylase 1;Histone deacetylase 2;Zinc finger protein 541;Deoxynucleotidyltransferase terminal-interacting protein 1","subunits.Gene.name.":"HDAC1;HDAC2;ZNF541;DNTTIP1","subunits.Gene.name.syn.":"RPD3L1;None;None;C20orf167 TDIF1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6422,"ComplexName":"SETDB1-DNMT3A complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS-7cells","subunits.UniProt.IDs.":"Q15047;Q9Y6K1","subunits.Entrez.IDs.":"9869;1788","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0017053;GO:0006355","GO.description":"transcriptional repressor complex;regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":16682412,"subunits.Protein.name.":"Histone-lysine N-methyltransferase SETDB1;DNA","subunits.Gene.name.":"SETDB1;DNMT3A","subunits.Gene.name.syn.":"KIAA0067 KMT1E;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6423,"ComplexName":"SETDB1-DNMT3B complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS-7","subunits.UniProt.IDs.":"Q15047;Q9UBC3","subunits.Entrez.IDs.":"9869;1789","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":16682412,"subunits.Protein.name.":"Histone-lysine N-methyltransferase SETDB1;DNA","subunits.Gene.name.":"SETDB1;DNMT3B","subunits.Gene.name.syn.":"KIAA0067 KMT1E;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6424,"ComplexName":"FOXO1-CREB1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"Osteoblasts","subunits.UniProt.IDs.":"Q01147;Q9R1E0","subunits.Entrez.IDs.":"12912;56458","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006355","GO.description":"regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":22945629,"subunits.Protein.name.":"Cyclic AMP-responsive element-binding protein 1;Forkhead box protein O1","subunits.Gene.name.":"Creb1;Foxo1","subunits.Gene.name.syn.":"None;Fkhr,Foxo1a","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6425,"ComplexName":"FOXO1-ATF4 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"Osteoblast","subunits.UniProt.IDs.":"Q06507;Q9R1E0","subunits.Entrez.IDs.":"11911;56458","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006355","GO.description":"regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":22945629,"subunits.Protein.name.":"Cyclic AMP-dependent transcription factor ATF-4;Forkhead box protein O1","subunits.Gene.name.":"Atf4;Foxo1","subunits.Gene.name.syn.":"None;Fkhr,Foxo1a","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6426,"ComplexName":"ATF4-CREB1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"P16220;P18848","subunits.Entrez.IDs.":"1385;468","Protein.complex.purification.method":"MI:0071-molecular sieving","GO.ID":"GO:0006355","GO.description":"regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":12871976,"subunits.Protein.name.":"Cyclic AMP-responsive element-binding protein 1;Cyclic AMP-dependent transcription factor ATF-4","subunits.Gene.name.":"CREB1;ATF4","subunits.Gene.name.syn.":"None;CREB2 TXREB","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6427,"ComplexName":"Sufu-Mycbp-Gli1 complex","Organism":"Human","Synonyms":"None","Cell.line":"MEF cells","subunits.UniProt.IDs.":"Q0VGT2;Q9EQS3;Q9Z0P7","subunits.Entrez.IDs.":"14633;56309;24069","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25403183,"subunits.Protein.name.":"Zinc finger protein GLI2;C-Myc-binding protein;Suppressor of fused homolog","subunits.Gene.name.":"Gli2;Mycbp;Sufu","subunits.Gene.name.syn.":"Thp;Amy1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6428,"ComplexName":"SPG3A oligomer complex","Organism":"Human","Synonyms":"Atlastin-1 oligomer complex; ATL1 oligomer complex","Cell.line":"None","subunits.UniProt.IDs.":"Q8WXF7","subunits.Entrez.IDs.":"51062","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0397-two hybrid array;MI:0091-chromatography technologies;MI:0030-cross-linking studies","GO.ID":"GO:0098796","GO.description":"membrane protein complex","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":14506257,"subunits.Protein.name.":"Atlastin-1","subunits.Gene.name.":"ATL1","subunits.Gene.name.syn.":"GBP3,SPG3A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Yeast two-hybrid analyses and co-immunoprecipitation studies demonstrated that atlastin-1 can self-associate, and gel-exclusion chromatography and chemical cross-linking studies indicated that atlastin-1 exists as an oligomer in vivo, most likely a tetramer. Membrane fractionation and protease protection assays revealed that atlastin-1 is an integral membrane protein with two predicted transmembrane domains; both the N-terminal GTP-binding and C-terminal domains are exposed to the cytoplasm. Together, these findings indicate that the SPG3A protein atlastin-1 is a multimeric integral membrane GTPase that may be involved in Golgi membrane dynamics or vesicle trafficking.","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":6429,"ComplexName":"SPG3A-SPG4-SPG31 complex","Organism":"Human","Synonyms":"REEP1-ATL1-SPAST complex","Cell.line":"None","subunits.UniProt.IDs.":"Q8WXF7;Q9H902;Q9UBP0","subunits.Entrez.IDs.":"51062;65055;6683","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0008017;GO:0007029","GO.description":"microtubule binding;endoplasmic reticulum organization","FunCat.ID":"42.07","FunCat.description":"endoplasmic reticulum","PubMed.ID":20200447,"subunits.Protein.name.":"Atlastin-1;Receptor expression-enhancing protein 1;Spastin","subunits.Gene.name.":"ATL1;REEP1;SPAST","subunits.Gene.name.syn.":"GBP3,SPG3A;C2orf23,SPG31;ADPSP,FSP2,KIAA1083,SPG4","Disease.comment":"Hereditary spastic paraplegias (HSPs; SPG1\\u201345) are inherited neurological disorders characterized by lower extremity spastic weakness. More than half of HSP cases result from autosomal dominant mutations in atlastin-1 (also known as SPG3A), receptor expression enhancing protein 1 (REEP1; SPG31), or spastin (SPG4). The atlastin-1 GTPase interacts with spastin, a microtubule-severing ATPase, as well as with the DP1/Yop1p and reticulon families of ER-shaping proteins, and SPG3A caused by atlastin-1 mutations has been linked pathogenically to abnormal ER morphology. Defects in tubular ER shaping and network interactions with the microtubule cytoskeleton seem to be the predominant pathogenic mechanism of HSP.","Subunits.comment":"None","Complex.comment":"REEP1 interacts with the HSP proteins atlastin-1 and spastin through intramembrane hairpin domains. REEP proteins were required for ER network formation in vitro, and REEP1 also bound microtubules and promoted ER alignment along the microtubule cytoskeleton (PMID:20200447).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6430,"ComplexName":"ATL2-SPG31 complex","Organism":"Human","Synonyms":"REEP1-ATL2 complex","Cell.line":"None","subunits.UniProt.IDs.":"Q8NHH9;Q9H902","subunits.Entrez.IDs.":"64225;65055","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007029;GO:0008017","GO.description":"endoplasmic reticulum organization;microtubule binding","FunCat.ID":"42.07","FunCat.description":"endoplasmic reticulum","PubMed.ID":20200447,"subunits.Protein.name.":"Atlastin-2;Receptor expression-enhancing protein 1","subunits.Gene.name.":"ATL2;REEP1","subunits.Gene.name.syn.":"ARL6IP2;C2orf23,SPG31","Disease.comment":"Mutations in the receptor expression enhancing protein 1 (REEP1) gene have been reported to be associated with an autosomal dominant HSP phenotype (SPG31) (PMID:19034539). REEP proteins were required for ER network formation, and REEP1 also bound microtubules and promoted ER alignment along the microtubule cytoskeleton (PMID:20200447).","Subunits.comment":"None","Complex.comment":"REEP1 coimmunoprecipitated with the human atlastin family members, atlastin-1, atlastin-2 and atlastin-3. ATL2 and ATL3 are highly similar to ATL1 in the membrane-spanning regions but divergent in the cytoplasmic C terminus.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6431,"ComplexName":"ATL3-SPG31 complex","Organism":"Human","Synonyms":"ATL3-REEP1 complex","Cell.line":"None","subunits.UniProt.IDs.":"Q6DD88;Q9H902","subunits.Entrez.IDs.":"25923;65055","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007029;GO:0008017","GO.description":"endoplasmic reticulum organization;microtubule binding","FunCat.ID":"42.07","FunCat.description":"endoplasmic reticulum","PubMed.ID":20200447,"subunits.Protein.name.":"Atlastin-3;Receptor expression-enhancing protein 1","subunits.Gene.name.":"ATL3;REEP1","subunits.Gene.name.syn.":"None;C2orf23,SPG31","Disease.comment":"REEP proteins were required for ER network formation, and REEP1 also bound microtubules and promoted ER alignment along the microtubule cytoskeleton (PMID:20200447).","Subunits.comment":"None","Complex.comment":"REEP1 coimmunoprecipitated with the human atlastin family members, atlastin-1, atlastin-2 and atlastin-3. ATL2 and ATL3 are highly similar to ATL1 in the membrane-spanning regions but divergent in the cytoplasmic C terminus.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6432,"ComplexName":"TTN-TCAP complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15273;Q8WZ42","subunits.Entrez.IDs.":"8557;7273","Protein.complex.purification.method":"MI:0428-imaging techniques","GO.ID":"GO:0045214;GO:0048739;GO:0055003;GO:0030049","GO.description":"sarcomere organization;cardiac muscle fiber development;cardiac myofibril assembly;muscle filament sliding","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":19622741,"subunits.Protein.name.":"Telethonin;Titin","subunits.Gene.name.":"TCAP;TTN","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6433,"ComplexName":"TTN-TCAP complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15273;Q8WZ42","subunits.Entrez.IDs.":"8557;7273","Protein.complex.purification.method":"MI:0428-imaging techniques","GO.ID":"GO:0045214;GO:0048739;GO:0055003;GO:0030049","GO.description":"sarcomere organization;cardiac muscle fiber development;cardiac myofibril assembly;muscle filament sliding","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":19622741,"subunits.Protein.name.":"Telethonin;Titin","subunits.Gene.name.":"TCAP;TTN","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6434,"ComplexName":"MIS18 complex","Organism":"Human","Synonyms":"MIS18A-OIP5-MIS18BP1 complex","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O43482;Q6P0N0;Q9NYP9","subunits.Entrez.IDs.":"11339;55320;54069","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0034508;GO:1903097","GO.description":"centromere complex assembly;regulation of CENP-A containing nucleosome assembly","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":17199038,"subunits.Protein.name.":"Protein Mis18-beta;Mis18-binding protein 1;Protein Mis18-alpha","subunits.Gene.name.":"OIP5;MIS18BP1;MIS18A","subunits.Gene.name.syn.":"MIS18B;C14orf106,KIAA1903,KNL2,M18BP1;C21orf45,C21orf46,FASP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6435,"ComplexName":"HAUS augmin-like complex","Organism":"Human","Synonyms":"HAUS1-HAUS2-HAUS3-HAUS4-HAUS5-HAUS6-HAUS7-HAUS8 complex","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O94927;Q68CZ6;Q7Z4H7;Q8BFT2;Q96CS2;Q99871;Q9BT25;Q9NVX0","subunits.Entrez.IDs.":"23354;79441;54801;219072;115106;55559;93323;55142","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0004-affinity chromatography technologies;MI:0069-mass spectrometry studies of complexes","GO.ID":"GO:0007067;GO:0051225;GO:0051297;GO:0000086","GO.description":"mitotic nuclear division;spindle assembly;centrosome organization;G2/M transition of mitotic cell cycle","FunCat.ID":"10.03.01.01.11;10.03.05.01;42.05;10.03.01.01.09","FunCat.description":"M phase;spindle pole body/centrosome and microtubule cycle;centrosome;G2/M transition of mitotic cell cycle","PubMed.ID":19427217,"subunits.Protein.name.":"HAUS augmin-like complex subunit 5;HAUS augmin-like complex subunit 3;HAUS augmin-like complex subunit 6;HAUS augmin-like complex subunit 4;HAUS augmin-like complex subunit 1;HAUS augmin-like complex subunit 7;HAUS augmin-like complex subunit 8;HAUS augmin-like complex subunit 2","subunits.Gene.name.":"HAUS5;HAUS3;HAUS6;Haus4;HAUS1;HAUS7;HAUS8;HAUS2","subunits.Gene.name.syn.":"KIAA0841;C4orf15;DGT6,FAM29A,KIAA1574;D14Ertd500e;CCDC5 HEIC;UCHL5IP,UIP1;HICE1;C15orf25,CEP27","Disease.comment":"OMIM:601626 Acute myeloid leukemia (PMID:27036161). Congenital glioblastoma multiforme (PMID:27121553).Clear cell renal cell carcinoma (PMID:26061684).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Mus musculus (Mouse);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6436,"ComplexName":"ATP4A-ATP4B complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P20648;P51164","subunits.Entrez.IDs.":"495;496","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies;MI:0069-mass spectrometry studies of complexes","GO.ID":"GO:0071805","GO.description":"potassium ion transmembrane transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":17255364,"subunits.Protein.name.":"Potassium-transporting ATPase alpha chain 1;Potassium-transporting ATPase subunit beta","subunits.Gene.name.":"ATP4A;ATP4B","subunits.Gene.name.syn.":"None;None","Disease.comment":"Familial gastric neuroendocrine tumors (PMID:27491072).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6437,"ComplexName":"GABBR1-GABBR2 complex","Organism":"Human","Synonyms":"GAB(B) complex","Cell.line":"None","subunits.UniProt.IDs.":"O75899;Q9UBS5","subunits.Entrez.IDs.":"9568;2550","Protein.complex.purification.method":"MI:0018-two hybrid","GO.ID":"GO:0007214;GO:0051932","GO.description":"gamma-aminobutyric acid signaling pathway;synaptic transmission, GABAergic","FunCat.ID":"30.05.02.24.04","FunCat.description":"gamma-aminobutyric acid signalling pathway","PubMed.ID":9872316,"subunits.Protein.name.":"Gamma-aminobutyric acid type B receptor subunit 2;Gamma-aminobutyric acid type B receptor subunit 1","subunits.Gene.name.":"GABBR2;GABBR1","subunits.Gene.name.syn.":"GPR51 GPRC3B;GPRC3A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6438,"ComplexName":"SCNN1A-SCNN1B-SCNN1G complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P37088;P51168;P51170","subunits.Entrez.IDs.":"6337;6338;6340","Protein.complex.purification.method":"MI:0013-biophysical","GO.ID":"GO:0006814","GO.description":"sodium ion transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":7499195,"subunits.Protein.name.":"Amiloride-sensitive sodium channel subunit alpha;Amiloride-sensitive sodium channel subunit beta;Amiloride-sensitive sodium channel subunit gamma","subunits.Gene.name.":"SCNN1A;SCNN1B;SCNN1G","subunits.Gene.name.syn.":"SCNN1;None;None","Disease.comment":"OMIM:264350 Pseudohypoaldosteronism, type I (PMID:10404817). OMIM:177200 Liddle syndrome (PMID:7550319, PMID:7954808). OMIM:219700 Cystic fibrosis (PMID:19060118).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6439,"ComplexName":"SCNN1B-SCNN1G-SCNN1D complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P51168;P51170;P51172","subunits.Entrez.IDs.":"6338;6340;6339","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006814","GO.description":"sodium ion transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":16423824,"subunits.Protein.name.":"Amiloride-sensitive sodium channel subunit beta;Amiloride-sensitive sodium channel subunit gamma;Amiloride-sensitive sodium channel subunit delta","subunits.Gene.name.":"SCNN1B;SCNN1G;SCNN1D","subunits.Gene.name.syn.":"None;None;DNACH","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6440,"ComplexName":"CHRNA2-CHRNB4 complex","Organism":"Human","Synonyms":"nAChR complex (alpha2, beta4)","Cell.line":"Thalamus,","subunits.UniProt.IDs.":"P30926;Q15822;Q9UBK2-2","subunits.Entrez.IDs.":"1143;1135;10891","Protein.complex.purification.method":"MI:0001-interaction detection method","GO.ID":"GO:0007271;GO:0035094;GO:0007274","GO.description":"synaptic transmission, cholinergic;response to nicotine;neuromuscular synaptic transmission","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":8906617,"subunits.Protein.name.":"Neuronal acetylcholine receptor subunit beta-4;Neuronal acetylcholine receptor subunit alpha-2;Peroxisome proliferator-activated receptor gamma coactivator 1-alpha (splice)","subunits.Gene.name.":"CHRNB4;CHRNA2;PPARGC1A","subunits.Gene.name.syn.":"None;None;LEM6,PGC1,PGC1A,PPARGC1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6441,"ComplexName":"KIAA0753-FOR20-OFD1 complex","Organism":"Human","Synonyms":"OFIP-FOR20-OFD1 complex","Cell.line":"HeLa Kyoto cells; RPE1 cells (immortalized human retinal pigment epithelial cells htert-RPE1); Cos1","subunits.UniProt.IDs.":"O75665;Q2KHM9;Q96NB1","subunits.Entrez.IDs.":"8481;9851;123811","Protein.complex.purification.method":"MI:0416-fluorescence microscopy;MI:0019-coimmunoprecipitation","GO.ID":"GO:0060271;GO:0034451;GO:0032053","GO.description":"cilium assembly;centriolar satellite;ciliary basal body organization","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26643951,"subunits.Protein.name.":"Oral-facial-digital syndrome 1 protein;Protein moonraker;LisH domain-containing protein FOPNL","subunits.Gene.name.":"OFD1;KIAA0753;FOPNL","subunits.Gene.name.syn.":"CXorf5;MNR, OFIP, OFD15;C16orf63, FOR20, PHSECRG2","Disease.comment":"The OFIP-OFD1-FOR20 complex is defective in a patient with oral-facial-digital (OFD) syndromes. Heterozygous mutations of KIAA0753/OFIP in a patientwith an OFD VI syndrome have been analyzed.. The patient cells showed a strong reduction of FOR20 and OFD1 at the centrosome and PSs (pericentriolar satellites).","Subunits.comment":"The central region of KIAA0753 (OFIP) stabilizes MTs.","Complex.comment":"Depletion of individual proteins of the complex affectscentrosomes, PSs (pericentriolar satellites) and ciliogenesis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6442,"ComplexName":"Cytochrome c oxidase, mitochondrial","Organism":"Human","Synonyms":"Complex IV; COX; Cytochrome c oxidase (EC 1.9.3.1), mitochondrial","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"P00395;P00403;P00414;P09669;P13073;P20674;Q15526;Q7KZN9;Q7Z7K0;Q96I36;Q9BVV7;Q9GZY4;Q9P0S2;Q9Y2R0","subunits.Entrez.IDs.":"4512;4513;4514;1345;1327;9377;6834;1355;152100;84987;29090;55744;51241;28958","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0069-mass spectrometry studies of complexes;MI:0047-far western blotting","GO.ID":"GO:0022904;GO:0005515;GO:0005743;GO:0009060;GO:0006818;GO:0006091;GO:0004129","GO.description":"respiratory electron transport chain;protein binding;mitochondrial inner membrane;aerobic respiration;hydrogen transport;generation of precursor metabolites and energy;cytochrome-c oxidase activity","FunCat.ID":"02.11.07;20.01.15;16.01;70.16.05;02.13.03;01","FunCat.description":"regulation of electron transport and membrane-associated energy conservation;electron transport;protein binding;mitochondrial inner membrane;aerobic respiration;METABOLISM","PubMed.ID":23260140,"subunits.Protein.name.":"Cytochrome c oxidase subunit 1;Cytochrome c oxidase subunit 2;Cytochrome c oxidase subunit 3;Cytochrome c oxidase subunit 6C;Cytochrome c oxidase subunit 4 isoform 1, mitochondrial;Cytochrome c oxidase subunit 5A, mitochondrial;Surfeit locus protein 1;Cytochrome c oxidase assembly protein COX15 homolog;COX assembly mitochondrial protein homolog;Cytochrome c oxidase assembly protein COX14;Mitochondrial import inner membrane translocase subunit Tim21;Cytochrome c oxidase assembly factor 1 homolog;Cytochrome c oxidase assembly protein COX16 homolog, mitochondrial;Cytochrome c oxidase assembly factor 3 homolog, mitochondrial","subunits.Gene.name.":"MT-CO1;MT-CO2;MT-CO3;COX6C;COX4I1;COX5A;SURF1;COX15;CMC1;COX14;TIMM21;COA1;COX16;COA3","subunits.Gene.name.syn.":"COI, COXI, MTCO1;COII COXII MTCO2;COIII,COXIII,MTCO3;None;COX4;None;None;None;C3orf68;C12orf62;C18orf55,TIM21,HSPC154;C7orf44,MITRAC15;C14orf112,HSPC203,PTD019;CCDC56,MITRAC12,HSPC009","Disease.comment":"Mutations in SURF1 are the most frequent cause of Leigh Syndrome with cytochrome c oxidase deficiency. Mutations in C12orf62, a factor that couples COX I synthesis with cytochrome c oxidase assembly, cause fatal neonatal lactic acidosis.","Subunits.comment":"None","Complex.comment":"During complex IV (= cytochrome C oxidase) assembly, imported subunits engage with mitochondria-encoded COX1 in assembly intermediates. The majority of imported complex IV subunits present N-terminal presequences and are transported by the presequence translocase. Progression of complex IV assembly requires nuclear-encoded subunits to utilize this import pathway: human TIM21 associates with the presequence translocase as well as MITRAC complexes in a dynamic manner. MITRAC12 associates with SURF1 and COX1 assembly intermediates and is required for efficient COX1 translation. Assembly of the early cytochrome c oxidase subunit COX4-1 requires TIM21, whereas it is dispensable forlate-assembling subunits. The finding that TIM21 also interacts with complex I intermediates points to a more general role of TIM21 in respiratory-chain assembly. Furthermore, TIM21 appears to be tightly connected to MITRAC15, which, in contrast to TIM23 and MITRAC12, coimmunoprecipitates with TIM21 under all tested conditions. MITRAC15 associates with MITRAC and is required for complex IV but also complex I assembly.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6443,"ComplexName":"SMAR1-HDAC1-SIN3A-SIN3B repressor complex","Organism":"Human","Synonyms":"BANP-HDAC1-SIN3A-SIN3B repressor complex","Cell.line":"293 cell lysate","subunits.UniProt.IDs.":"O75182;Q13547;Q8N9N5;Q96ST3","subunits.Entrez.IDs.":"23309;3065;54971;25942","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0006355;GO:0005634","GO.description":"regulation of transcription, DNA-templated;nucleus","FunCat.ID":"11.02.03.04;70.10","FunCat.description":"transcriptional control;nucleus","PubMed.ID":16166625,"subunits.Protein.name.":"Paired amphipathic helix protein Sin3b;Histone deacetylase 1;Protein BANP;Paired amphipathic helix protein Sin3a","subunits.Gene.name.":"SIN3B;HDAC1;BANP;SIN3A","subunits.Gene.name.syn.":"KIAA0700;RPD3L1;BEND1, SMAR1;None","Disease.comment":"Amplification and dysregulation of cyclin D1 is predominantly observed in breast carcinomas. In the majority of the breast cancer cell lines used, elevated levels of cyclin D1 were correlated with drastically reduced levels of SMAR1.","Subunits.comment":"None","Complex.comment":"The authors demonstrate that SMAR1 represses cyclin D1gene expression by acting as a transcriptional repressor.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6444,"ComplexName":"SMAR1-HDAC1-SIN3A-SIN3B-p107-p130 repressor complex","Organism":"Human","Synonyms":"BANP-HDAC1-SIN3A-SIN3B-RBL1-RBL2 repressor complex","Cell.line":"293 cell lysate","subunits.UniProt.IDs.":"O75182;P28749;Q08999;Q13547;Q8N9N5;Q96ST3","subunits.Entrez.IDs.":"23309;5933;5934;3065;54971;25942","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0006355;GO:0005634","GO.description":"regulation of transcription, DNA-templated;nucleus","FunCat.ID":"11.02.03.04;70.10","FunCat.description":"transcriptional control;nucleus","PubMed.ID":16166625,"subunits.Protein.name.":"Paired amphipathic helix protein Sin3b;Retinoblastoma-like protein 1;Retinoblastoma-like protein 2;Histone deacetylase 1;Protein BANP;Paired amphipathic helix protein Sin3a","subunits.Gene.name.":"SIN3B;RBL1;RBL2;HDAC1;BANP;SIN3A","subunits.Gene.name.syn.":"KIAA0700;PRB1, p107, CP107;RB2, P130;RPD3L1;BEND1, SMAR1;None","Disease.comment":"Amplification and dysregulation of cyclin D1 is predominantly observed in breast carcinomas. In the majority of the breast cancer cell lines used, elevated levels of cyclin D1 were correlated with drastically reduced levels of SMAR1.","Subunits.comment":"Although the authors observed the interaction of pocket Rb proteins (RBL1, RBL2) in the SMAR1-associated complex, Western analysis data from an Rb-None cell line (MDA-MB-468) and Rb-inactive cell lines (293 and HBL-100) suggest that the Rb is dispensable for SMAR1-mediated cyclin D1 repression.","Complex.comment":"The authors demonstrate that SMAR1 represses cyclin D1 gene expression by acting as a transcriptional repressor.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6445,"ComplexName":"TIM50-TIM23 complex, mitochondrial","Organism":"Human","Synonyms":"TIM (TIMM23, TIMM50) complex, mitochondrial","Cell.line":"HeLa and 293T cells","subunits.UniProt.IDs.":"O14925;Q3ZCQ8","subunits.Entrez.IDs.":"100287932;92609","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":15044455,"subunits.Protein.name.":"Mitochondrial import inner membrane translocase subunit Tim23;Mitochondrial import inner membrane translocase subunit TIM50","subunits.Gene.name.":"TIMM23;TIMM50","subunits.Gene.name.syn.":"TIM23;TIM50","Disease.comment":"TIM50 is an essential component of TIM23 complex and involved in protein translocating into the inner mitochondrial membrane. It was found that the loss of TIM50 suppresses proliferation and induces apoptosis in breast cancer (PMID:26289846).Injection of Tim50-specific morpholino antisense oligonucleotides during early zebrafish embryonic development causes neurodegeneration, dysmorphic hearts, and reduced motility as a result of increased cell death (PMID:15044455).","Subunits.comment":"None","Complex.comment":"Translocation of nuclear-encoded mitochondrial preproteins is mediated by translocases in the outer (TOM) and inner (TIM) membranes.Tim50, a component of the mitochondrial translocator, regulates mitochondrial integrity and cell death. It is demonstrated that human Tim50 possesses phosphatase activity and is present in a complex with human Tim23. Down-regulation of human Tim50 expression by RNA interference increases the sensitivity of human cell lines to death stimuli by accelerating the release of cytochrome c from the mitochondria. The loss of Tim50 in vertebrates causes mitochondrial membrane permeabilization and dysfunction followed by cytoplasmic release of cytochrome c along with other mitochondrial inducers of cell death. Thus Tim50 is important for both mitochondrial function and early neuronal development.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6446,"ComplexName":"Set/TAF-I beta-TAF-I alpha-PP32 complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa nuclear extracts","subunits.UniProt.IDs.":"P39687;Q01105-1;Q01105-2","subunits.Entrez.IDs.":"8125;6418;6418","Protein.complex.purification.method":"MI:0226-ion exchange chromatography;MI:0071-molecular sieving;MI:0019-coimmunoprecipitation","GO.ID":"GO:0035067;GO:0006338;GO:0048387;GO:0006355","GO.description":"negative regulation of histone acetylation;chromatin remodeling;negative regulation of retinoic acid receptor signaling pathway;regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":11163245,"subunits.Protein.name.":"Acidic leucine-rich nuclear phosphoprotein 32 family member A;Protein SET;Protein SET","subunits.Gene.name.":"ANP32A;SET;SET","subunits.Gene.name.syn.":"C15orf1, LANP, MAPM, PHAP1;TAF-I alpha;TAF-I beta","Disease.comment":"None","Subunits.comment":"Except for the subtype-specific N-terminus, Set/TAF-Ib and TAF-Ia are identical. UniProtKB - Q01105 shows isoform 1 as TAF-I alpha and isoform 2 as TAF-I beta.","Complex.comment":"Set/TAF-Ib, TAF-Ia, and pp32 are subunits of the INHAT (inhibitor of acetyltransferases) complex. INHAT functions by masking the accessibility of lysines of histones to the acetylases.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6447,"ComplexName":"TIM23-TOM22-TIM50-HSD3B2 complex","Organism":"Human","Synonyms":"TIMM23-TOMM22-TIMM50-3betaHSD2 complex","Cell.line":"adrenal NCI H295 cells","subunits.UniProt.IDs.":"O14925;P26439;Q3ZCQ8;Q9NS69","subunits.Entrez.IDs.":"100287932;3284;92609;56993","Protein.complex.purification.method":"MI:0069-mass spectrometry studies of complexes;MI:0047-far western blotting;MI:0029-cosedimentation through density gradients;MI:0019-coimmunoprecipitation","GO.ID":"GO:0050810;GO:0005743","GO.description":"regulation of steroid biosynthetic process;mitochondrial inner membrane","FunCat.ID":"70.16.05","FunCat.description":"mitochondrial inner membrane","PubMed.ID":21930695,"subunits.Protein.name.":"Mitochondrial import inner membrane translocase subunit Tim23;3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2;Mitochondrial import inner membrane translocase subunit TIM50;Mitochondrial import receptor subunit TOM22 homolog","subunits.Gene.name.":"TIMM23;HSD3B2;TIMM50;TOMM22","subunits.Gene.name.syn.":"TIM23;HSDB3B;TIM50;TOM22","Disease.comment":"In the adrenals, testes, and ovaries, 3beta-hydroxysteroid dehydrogenase type 2 (3betaHSD2) catalyzes the conversion of pregnenolone to progesterone and dehydroepiandrostenedione to androstenedione. Alterations in this pathway can have deleterious effects, including sexual development impairment, spontaneous abortion, and breast cancer.","Subunits.comment":"None","Complex.comment":"Inner mitochondrial translocase Tim50 interacts with 3beta-hydroxysteroid dehydrogenase type 2 to regulate adrenal and gonadal steroidogenesis. Through mass spectrometry and Western blotting of mitochondrial complexes and density gradient ultracentrifugation, it was shown that that 3betaHSD2 formed a transient association with the translocases Tim50 and Tom22 and with Tim23. This association occurred primarily through the interaction of Tim50 with the N terminus of 3betaHSD2 and contributed to enzymatic activity. Tim50 knockdown inhibited catalysis of dehydroepiandrostenedione to androstenedione and pregnenolone to progesterone.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6448,"ComplexName":"APC-Asef complex","Organism":"Rat","Synonyms":"APC-Arhgef4 complex","Cell.line":"embryonic rat brain","subunits.UniProt.IDs.":"D3ZKB4;P70478","subunits.Entrez.IDs.":"301334;24205","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:1905097","GO.description":"regulation of guanyl-nucleotide exchange factor activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":10947987,"subunits.Protein.name.":"Protein Arhgef4;Adenomatous polyposis coli protein","subunits.Gene.name.":"Arhgef4;Apc","subunits.Gene.name.syn.":"LOC301334, rCG_22222;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The results show that the armadillo repeat domain of APC interacts with a Rac-specific GEF (guanine nucleotide exchange factor), Asef, and activates its activity.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6449,"ComplexName":"APC-Asef-beta-catenin complex","Organism":"Rat","Synonyms":"APC-Arhgef4-beta-catenin complex","Cell.line":"embryonic rat brain","subunits.UniProt.IDs.":"D3ZKB4;P70478;Q9WU82","subunits.Entrez.IDs.":"301334;24205;84353","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":10947987,"subunits.Protein.name.":"Protein Arhgef4;Adenomatous polyposis coli protein;Catenin beta-1","subunits.Gene.name.":"Arhgef4;Apc;Ctnnb1","subunits.Gene.name.syn.":"LOC301334, rCG_22222;None;Catnb","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6450,"ComplexName":"DJ-1-DJBP-AR complex","Organism":"Human","Synonyms":"None","Cell.line":"293T cells, treated with testosterone","subunits.UniProt.IDs.":"P10275;Q5THR3;Q99497","subunits.Entrez.IDs.":"367;64800;11315","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0060765;GO:0006355","GO.description":"regulation of androgen receptor signaling pathway;regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":12612053,"subunits.Protein.name.":"Androgen receptor;EF-hand calcium-binding domain-containing protein 6;Protein deglycase DJ-1","subunits.Gene.name.":"AR;EFCAB6;PARK7","subunits.Gene.name.syn.":"DHTR, NR3C4;DJBP, KIAA1672;DJ1, DJ-1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"DJBP directly binds to both DJ-1 and AR in a testosterone-dependent manner and  DJ-1 associates with AR via DJBP in a ternary complex. DJBP was found to inhibit AR transcription activity by recruiting histone-deacetylase complexes, including HDAC1 and mSin3, and DJ-1 was found to restore the repressed activity of the AR.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6451,"ComplexName":"MAK-ACTR-AR complex","Organism":"Human","Synonyms":"MAK-NCOA3-AR complex","Cell.line":"293T cells","subunits.UniProt.IDs.":"P10275;P20794;Q9Y6Q9","subunits.Entrez.IDs.":"367;4117;8202","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0060765;GO:0006355","GO.description":"regulation of androgen receptor signaling pathway;regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":16951154,"subunits.Protein.name.":"Androgen receptor;Serine/threonine-protein kinase MAK;Nuclear receptor coactivator 3","subunits.Gene.name.":"AR;MAK;NCOA3","subunits.Gene.name.syn.":"DHTR, NR3C4;None;AIB1, BHLHE42, RAC3, TRAM1, ACTR","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"MAK and ACTR seem to be in proximity and synergize with each other in the transactivation of AR.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6452,"ComplexName":"DDP1-TIM13 complex, mitochondrial","Organism":"Human","Synonyms":"hTim13 complex; TIMM8A-TIMM13 70K mitochondrial intermembrane space complex","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O60220;Q9Y5L4","subunits.Entrez.IDs.":"1678;26517","Protein.complex.purification.method":"MI:0047-far western blotting;MI:0413-electrophoretic mobility shift assay;MI:0019-coimmunoprecipitation;MI:0071-molecular sieving","GO.ID":"GO:0005758;GO:0015031","GO.description":"mitochondrial intermembrane space;protein transport","FunCat.ID":"70.16.03;20.01.10","FunCat.description":"mitochondrial intermembrane space;protein transport","PubMed.ID":11489896,"subunits.Protein.name.":"Mitochondrial import inner membrane translocase subunit Tim8 A;Mitochondrial import inner membrane translocase subunit Tim13","subunits.Gene.name.":"TIMM8A;TIMM13","subunits.Gene.name.syn.":"DDP,DDP1,TIM8A;TIM13B,TIMM13A,TIMM13B","Disease.comment":"Mutations in the DDP1 cause the Mohr-Tranebjaerg syndrome, a progressive neurodegenerative disorder characterized by sensorineural hearing loss, dystonia, mental retardation, and blindness.","Subunits.comment":"The 70-kDa complex appears to be composed of threemolecules of DDP1 and three molecules of hTim13. However, itcannot be decided whether this stoichiometry is fixed or determined by the relative expression levels of the components.","Complex.comment":"The DDP1\\u0001-Tim13 complex acts in the intermembrane space and specifically assists the import of the Tim23 precursors into the mitochondrial inner membrane thereby forming a hetero-oligomeric complex of 70 kDa. It is suggested that an impaired mitochondrial preprotein import is the pathogenetic basis of the Mohr-Tranebjaerg syndrome.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6454,"ComplexName":"Zipzap/p200-Srf-p49/STRAP-Nkx2.5 complex","Organism":"Mouse","Synonyms":"Arid2-Srf-Srfbp1-Nkx-2-5 complex","Cell.line":"NIH3T3 cells","subunits.UniProt.IDs.":"E9Q7E2;P42582;Q9CZ91;Q9JM73","subunits.Entrez.IDs.":"77044;18091;67222;20807","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0006355","GO.description":"regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04","FunCat.description":"transcriptional control","PubMed.ID":16782067,"subunits.Protein.name.":"Protein Arid2;Homeobox protein Nkx-2.5;Serum response factor-binding protein 1;Serum response factor","subunits.Gene.name.":"Arid2;Nkx2-5;Srfbp1;Srf","subunits.Gene.name.syn.":"zipzap/p200;Csx, Nkx-2.5, Nkx2e;p49/STRAP;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Zipzap may serve as a transcription co-activator for the regulation of cardiac gene expression.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6455,"ComplexName":"ARL2-TBCD complex","Organism":"Human","Synonyms":"ARL2-Tubulin-folding cofactor D complex","Cell.line":"293T cells","subunits.UniProt.IDs.":"P36404;Q9BTW9","subunits.Entrez.IDs.":"402;6904","Protein.complex.purification.method":"MI:0030-cross-linking studies","GO.ID":"GO:0000226","GO.description":"microtubule cytoskeleton organization","FunCat.ID":"42.04.05","FunCat.description":"microtubule cytoskeleton","PubMed.ID":10831612,"subunits.Protein.name.":"ADP-ribosylation factor-like protein 2;Tubulin-specific chaperone D","subunits.Gene.name.":"ARL2;TBCD","subunits.Gene.name.syn.":"None;KIAA0988, SSD1, TFCD","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Arl2 has a role in modulating the interaction of tubulin-folding cofactors with native tubulin in vivo.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6456,"ComplexName":"TIM17A-TIM23 complex, mitochondrial","Organism":"Human","Synonyms":"TIMM17A-TIMM23 complex","Cell.line":"HEK293T, HeLa, and Huh7 cells","subunits.UniProt.IDs.":"O14925;Q99595","subunits.Entrez.IDs.":"100287932;10440","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005739;GO:0098800;GO:0045039;GO:0006950","GO.description":"mitochondrion;inner mitochondrial membrane protein complex;protein import into mitochondrial inner membrane;response to stress","FunCat.ID":"70.16;32.01","FunCat.description":"mitochondrion;stress response","PubMed.ID":24315374,"subunits.Protein.name.":"Mitochondrial import inner membrane translocase subunit Tim23;Mitochondrial import inner membrane translocase subunit Tim17-A","subunits.Gene.name.":"TIMM23;TIMM17A","subunits.Gene.name.syn.":"TIM23;MIMT17, TIM17, TIM17A TIMM17","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TIM17A and TIM17B are expressed ubiquitously in mammals, however they demonstrate tissue-specific expression profiles with TIM17A enriched in the brain and TIM17B enriched in skeletal muscle. No functional differences between Tim17A and Tim17B are currently known, TIM17A is a transcriptional target of the mammalian UPRmt, suggesting that these two Tim17 homologs are differentially regulated during stress. Tim17A and Tim17B co-immunopurify with Tim23 in mitochondria. Tim17A is a stress-regulated subunit of the translocase of the inner membrane 23 (TIM23) mitochondrial protein import complex. It is indicated that Tim17A degradation is a stress-responsive mechanism by which cells adapt mitochondrial protein import efficiency and promote mitochondrial proteostasis in response to the numerous pathologic insults that induce stress-regulated translation attenuation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6457,"ComplexName":"MLL1 core complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"P61964;Q03164;Q15291;Q9UBL3","subunits.Entrez.IDs.":"11091;4297;5929;9070","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0051568","GO.description":"histone H3-K4 methylation","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":22665483,"subunits.Protein.name.":"WD repeat-containing protein 5;Histone-lysine N-methyltransferase 2A;Retinoblastoma-binding protein 5;Set1/Ash2 histone methyltransferase complex subunit ASH2","subunits.Gene.name.":"WDR5;KMT2A;RBBP5;ASH2L","subunits.Gene.name.syn.":"BIG3;ALL1, CXXC7, HRX, HTRX, MLL, MLL1, TRX1;RBQ3;ASH2L1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Whereas wild-type MLL1 co-immunoprecipitates theWDR5, RbBP5, and Ash2L subcomplex, co-immunoprecipitation is abolished when Arg-3765 of MLL1 is replaced with alanine.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6458,"ComplexName":"TIM17B-TIM23 complex, mitochondrial","Organism":"Human","Synonyms":"TIM17B-TIMM23 complex, mitochondrial","Cell.line":"HEK293T, HeLa, and Huh7 cells","subunits.UniProt.IDs.":"O14925;O60830","subunits.Entrez.IDs.":"100287932;10245","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0098800;GO:0005739;GO:0045039;GO:0006950","GO.description":"inner mitochondrial membrane protein complex;mitochondrion;protein import into mitochondrial inner membrane;response to stress","FunCat.ID":"70.16;32.01","FunCat.description":"mitochondrion;stress response","PubMed.ID":24315374,"subunits.Protein.name.":"Mitochondrial import inner membrane translocase subunit Tim23;Mitochondrial import inner membrane translocase subunit Tim17-B","subunits.Gene.name.":"TIMM23;TIMM17B","subunits.Gene.name.syn.":"TIM23;TIM17B","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TIM17A and TIM17B are expressed ubiquitously in mammals, however they demonstrate tissue-specific expression profiles with TIM17A enriched in the brain and TIM17B enriched in skeletal muscle. No functional differences between Tim17A and Tim17B are currently known. Tim17A and Tim17B co-immunopurify with Tim23 in mitochondria.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6459,"ComplexName":"EARP complex","Organism":"Human","Synonyms":"Endosome-associated recycling protein complex","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"Q5VIR6;Q8N1B4;Q96JG6;Q9UID3","subunits.Entrez.IDs.":"55275;6293;55610;738","Protein.complex.purification.method":"MI:0071-molecular sieving;MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25799061,"subunits.Protein.name.":"Vacuolar protein sorting-associated protein 53 homolog;Vacuolar protein sorting-associated protein 52 homolog;Syndetin;Vacuolar protein sorting-associated protein 51 homolog","subunits.Gene.name.":"VPS53;VPS52;VPS50;VPS51","subunits.Gene.name.syn.":"PP13624;SACM2L;CCDC132,KIAA1861;ANG2,C11orf2,C11orf3,FFR,PP5382","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6460,"ComplexName":"MLL2 complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa nuclear extracts","subunits.UniProt.IDs.":"O00255;O14686;O15294;O75475;P51610;P61964;Q15291;Q9C005;Q9UBL3;Q9Y5Z7","subunits.Entrez.IDs.":"4221;8085;8473;11168;3054;11091;5929;84661;9070;29915","Protein.complex.purification.method":"MI:0096-pull down;MI:0069-mass spectrometry studies of complexes","GO.ID":"GO:0051568;GO:0006355;GO:0005634;GO:0006325","GO.description":"histone H3-K4 methylation;regulation of transcription, DNA-templated;nucleus;chromatin organization","FunCat.ID":"11.02.03.04;70.10","FunCat.description":"transcriptional control;nucleus","PubMed.ID":23508102,"subunits.Protein.name.":"Menin;Histone-lysine N-methyltransferase 2D;UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit;PC4 and SFRS1-interacting protein;Host cell factor 1;WD repeat-containing protein 5;Retinoblastoma-binding protein 5;Protein dpy-30 homolog;Set1/Ash2 histone methyltransferase complex subunit ASH2;Host cell factor 2","subunits.Gene.name.":"MEN1;KMT2D;OGT;PSIP1;HCFC1;WDR5;RBBP5;DPY30;ASH2L;HCFC2","subunits.Gene.name.syn.":"SCG2;ALR, MLL2, MLL4;None;DFS70, LEDGF, PSIP2;HCF1, HFC1;BIG3;RBQ3;None;ASH2L1;None","Disease.comment":"None","Subunits.comment":"Corresponding to protein Menin, the authors refer to isoform 2 of Uniprot: O00255 (O00255-2).The authors did not specify the proteins HCFC1 and HCFC2. Both proteins are shown alternatively.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6461,"ComplexName":"MLL3 complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa nuclear extracts","subunits.UniProt.IDs.":"O15550;P61964;Q14686;Q15291;Q6ZW49;Q8NEZ4;Q9BTK6;Q9C005;Q9UBL3","subunits.Entrez.IDs.":"7403;11091;23054;5929;22976;58508;79447;84661;9070","Protein.complex.purification.method":"MI:0069-mass spectrometry studies of complexes;MI:0096-pull down","GO.ID":"GO:0051568;GO:0005634;GO:0006355;GO:0006325","GO.description":"histone H3-K4 methylation;nucleus;regulation of transcription, DNA-templated;chromatin organization","FunCat.ID":"70.10;11.02.03.04","FunCat.description":"nucleus;transcriptional control","PubMed.ID":23508102,"subunits.Protein.name.":"Lysine-specific demethylase 6A;WD repeat-containing protein 5;Nuclear receptor coactivator 6;Retinoblastoma-binding protein 5;PAX-interacting protein 1;Histone-lysine N-methyltransferase 2C;PAXIP1-associated glutamate-rich protein 1;Protein dpy-30 homolog;Set1/Ash2 histone methyltransferase complex subunit ASH2","subunits.Gene.name.":"KDM6A;WDR5;NCOA6;RBBP5;PAXIP1;KMT2C;PAGR1;DPY30;ASH2L","subunits.Gene.name.syn.":"UTX;BIG3;AIB3, KIAA0181, RAP250, TRBP;RBQ3;PAXIP1L, PTIP;HALR, KIAA1506, MLL3;C16orf53, PA1;None;ASH2L1","Disease.comment":"None","Subunits.comment":"Corresponding to protein MLL3, the authors refer to isoform 3 of Uniprot: Q8NEZ4 (Q8NEZ4-3).","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6462,"ComplexName":"MLL1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa nuclear extracts","subunits.UniProt.IDs.":"O00255;O15294;P51610;P61964;Q03164;Q15291;Q9C005;Q9UBL3","subunits.Entrez.IDs.":"4221;8473;3054;11091;4297;5929;84661;9070","Protein.complex.purification.method":"MI:0096-pull down;MI:0069-mass spectrometry studies of complexes","GO.ID":"GO:0051568;GO:0006355;GO:0005634;GO:0006325","GO.description":"histone H3-K4 methylation;regulation of transcription, DNA-templated;nucleus;chromatin organization","FunCat.ID":"11.02.03.04;70.10","FunCat.description":"transcriptional control;nucleus","PubMed.ID":23508102,"subunits.Protein.name.":"Menin;UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit;Host cell factor 1;WD repeat-containing protein 5;Histone-lysine N-methyltransferase 2A;Retinoblastoma-binding protein 5;Protein dpy-30 homolog;Set1/Ash2 histone methyltransferase complex subunit ASH2","subunits.Gene.name.":"MEN1;OGT;HCFC1;WDR5;KMT2A;RBBP5;DPY30;ASH2L","subunits.Gene.name.syn.":"SCG2;None;HCF1, HFC1;BIG3;ALL1, CXXC7, HRX, HTRX, MLL, MLL1, TRX1;RBQ3;None;ASH2L1","Disease.comment":"None","Subunits.comment":"Corresponding to protein Menin, the authors refer to isoform 2 of Uniprot: O00255 (O00255-2). Since the authors did not specify host cell factor, we used HCFC1","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6463,"ComplexName":"GARP complex","Organism":"Human","Synonyms":"Golgi-associated retrograde protein complex; Vps fifty-three complex; VFT complex","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"Q5VIR6;Q8N1B4;Q9P1Q0;Q9UID3","subunits.Entrez.IDs.":"55275;6293;51542;738","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0042147;GO:0005802;GO:0000938","GO.description":"retrograde transport, endosome to Golgi;trans-Golgi network;GARP complex","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20685960,"subunits.Protein.name.":"Vacuolar protein sorting-associated protein 53 homolog;Vacuolar protein sorting-associated protein 52 homolog;Vacuolar protein sorting-associated protein 54;Vacuolar protein sorting-associated protein 51 homolog","subunits.Gene.name.":"VPS53;VPS52;VPS54;VPS51","subunits.Gene.name.syn.":"PP13624;SACM2L;HCC8;ANG2,C11orf2,C11orf3,FFR,PP5382","Disease.comment":"People with mutations in VPS53, a subunit of the GARP complex, suffer from a severe neurodegenerative disease known as \\u2018progressive cerebello-cerebral atrophy type 2\\u2019 (PCCA2).","Subunits.comment":"None","Complex.comment":"GARP deficiency results in accumulation of sphingolipid synthesis intermediates and lysosomal dysfunction, indicating that GARP is necessary for sphingolipid homeostasis (PMID:26357016).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6464,"ComplexName":"Hsp70-Tim44 complex","Organism":"Rat","Synonyms":"mHsp70-Timm44 complex","Cell.line":"liver mitochondria","subunits.UniProt.IDs.":"O35094;P0DMW0","subunits.Entrez.IDs.":"29635;108348108","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0031072;GO:0005743;GO:0005739","GO.description":"heat shock protein binding;mitochondrial inner membrane;mitochondrion","FunCat.ID":"70.16.05;70.16","FunCat.description":"mitochondrial inner membrane;mitochondrion","PubMed.ID":9538267,"subunits.Protein.name.":"Mitochondrial import inner membrane translocase subunit TIM44;Heat shock 70 kDa protein 1A","subunits.Gene.name.":"Timm44;Hspa1a","subunits.Gene.name.syn.":"Mimt44, Tim44;Hspa1, Hsp70-1","Disease.comment":"None","Subunits.comment":"Since the authors did not specify Hsp70, we used isoform Hsp70-1.","Complex.comment":"The Tim17-Tim23 and the Tim44-mHsp70 complexes in rat liver mitochondria were detected by immunoprecipitation.The formation of the mHsp70-rTim44 complex was observed when the lysate prepared from apyrase/oligomycin-treated mitochondriawas used, indicating that the lysate contained a low concentration of ATP or ADP, which induced dissociation of the mHsp70-rTim44 complex.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6465,"ComplexName":"Tim17a-Tim23 complex","Organism":"Rat","Synonyms":"Timm17-Timm23 complex","Cell.line":"liver mitochondria","subunits.UniProt.IDs.":"O35092;O35093","subunits.Entrez.IDs.":"54311;54312","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005739;GO:0005743;GO:0015031;GO:0006886","GO.description":"mitochondrion;mitochondrial inner membrane;protein transport;intracellular protein transport","FunCat.ID":"70.16;70.16.05;20.01.10;14.04","FunCat.description":"mitochondrion;mitochondrial inner membrane;protein transport;protein targeting, sorting and translocation","PubMed.ID":9538267,"subunits.Protein.name.":"Mitochondrial import inner membrane translocase subunit Tim17-A;Mitochondrial import inner membrane translocase subunit Tim23","subunits.Gene.name.":"Timm17a;Timm23","subunits.Gene.name.syn.":"Mimt17, Tim17, Tim17a, Timm17;Tim23","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The Tim17-Tim23 and the Tim44-mHsp70 complexesin rat liver mitochondria were detected by immunoprecipitation.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6466,"ComplexName":"Ninjurin1 homooligomer","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q92982","subunits.Entrez.IDs.":"4814","Protein.complex.purification.method":"MI:0055-fluorescent resonance energy transfer","GO.ID":"GO:0007155","GO.description":"cell adhesion","FunCat.ID":"34.07","FunCat.description":"cell adhesion","PubMed.ID":28067406,"subunits.Protein.name.":"Ninjurin-1","subunits.Gene.name.":"NINJ1","subunits.Gene.name.syn.":"None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":6467,"ComplexName":"MLL4 complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa nuclear extracts","subunits.UniProt.IDs.":"O14686;O15550;P61964;Q14686;Q15291;Q6ZW49;Q9BTK6;Q9C005;Q9UBL3","subunits.Entrez.IDs.":"8085;7403;11091;23054;5929;22976;79447;84661;9070","Protein.complex.purification.method":"MI:0096-pull down;MI:0069-mass spectrometry studies of complexes","GO.ID":"GO:0051568;GO:0005634;GO:0006355;GO:0006325","GO.description":"histone H3-K4 methylation;nucleus;regulation of transcription, DNA-templated;chromatin organization","FunCat.ID":"70.10;11.02.03.04","FunCat.description":"nucleus;transcriptional control","PubMed.ID":23508102,"subunits.Protein.name.":"Histone-lysine N-methyltransferase 2D;Lysine-specific demethylase 6A;WD repeat-containing protein 5;Nuclear receptor coactivator 6;Retinoblastoma-binding protein 5;PAX-interacting protein 1;PAXIP1-associated glutamate-rich protein 1;Protein dpy-30 homolog;Set1/Ash2 histone methyltransferase complex subunit ASH2","subunits.Gene.name.":"KMT2D;KDM6A;WDR5;NCOA6;RBBP5;PAXIP1;PAGR1;DPY30;ASH2L","subunits.Gene.name.syn.":"ALR, MLL2, MLL4;UTX;BIG3;AIB3, KIAA0181, RAP250, TRBP;RBQ3;PAXIP1L, PTIP;C16orf53, PA1;None;ASH2L1","Disease.comment":"None","Subunits.comment":"Corresponding to protein MLL4, the authors refer to isoform 3 of Uniprot: O14686 (O14686-3).","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6468,"ComplexName":"TRAPP complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"O43617;O75865;P0DI81;P48553;Q5T215;Q7Z392;Q86SZ2;Q8IUR0;Q8WVT3;Q96Q05;Q9UL33;Q9Y296;Q9Y2L5;Q9Y5R8","subunits.Entrez.IDs.":"27095;79090;6399;7109;100128327;60684;122553;126003;51112;83696;51693;51399;22878;58485","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0676-tandem affinity purification;MI:0071-molecular sieving","GO.ID":"GO:0006888;GO:0016192;GO:0030137","GO.description":"ER to Golgi vesicle-mediated transport;vesicle-mediated transport;COPI-coated vesicle","FunCat.ID":"20.09.07.03;20.09.07","FunCat.description":"ER to Golgi transport;vesicular transport (Golgi network, etc.)","PubMed.ID":21525244,"subunits.Protein.name.":"Trafficking protein particle complex subunit 3;Trafficking protein particle complex subunit 6A;Trafficking protein particle complex subunit 2;Trafficking protein particle complex subunit 10;Trafficking protein particle complex subunit 3-like protein;Trafficking protein particle complex subunit 11;Trafficking protein particle complex subunit 6B;Trafficking protein particle complex subunit 5;Trafficking protein particle complex subunit 12;Trafficking protein particle complex subunit 9;Trafficking protein particle complex subunit 2-like protein;Trafficking protein particle complex subunit 4;Trafficking protein particle complex subunit 8;Trafficking protein particle complex subunit 1","subunits.Gene.name.":"TRAPPC3;TRAPPC6A;TRAPPC2;TRAPPC10;TRAPPC3L;TRAPPC11;TRAPPC6B;TRAPPC5;TRAPPC12;TRAPPC9;TRAPPC2L;TRAPPC4;TRAPPC8;TRAPPC1","subunits.Gene.name.syn.":"BET3,CDABP0066;HSPC289;SEDL;EHOC1,TMEM1;BET3L;C4orf41;None;None;TRAMM,TTC15;KIAA1882 NIBP;HSPC126;SBDN,HSPC172,PTD009;KIAA1012;BET5,MUM2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6469,"ComplexName":"Set1A complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa nuclear extracts","subunits.UniProt.IDs.":"O15047;O15294;P51610;P61964;Q15291;Q6UXN9;Q9C005;Q9P0U4;Q9UBL3;Q9Y5Z7","subunits.Entrez.IDs.":"9739;8473;3054;11091;5929;80335;84661;30827;9070;29915","Protein.complex.purification.method":"MI:0096-pull down;MI:0069-mass spectrometry studies of complexes","GO.ID":"GO:0051568;GO:0005634;GO:0006355;GO:0006325","GO.description":"histone H3-K4 methylation;nucleus;regulation of transcription, DNA-templated;chromatin organization","FunCat.ID":"70.10;11.02.03.04","FunCat.description":"nucleus;transcriptional control","PubMed.ID":23508102,"subunits.Protein.name.":"Histone-lysine N-methyltransferase SETD1A;UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit;Host cell factor 1;WD repeat-containing protein 5;Retinoblastoma-binding protein 5;WD repeat-containing protein 82;Protein dpy-30 homolog;CXXC-type zinc finger protein 1;Set1/Ash2 histone methyltransferase complex subunit ASH2;Host cell factor 2","subunits.Gene.name.":"SETD1A;OGT;HCFC1;WDR5;RBBP5;WDR82;DPY30;CXXC1;ASH2L;HCFC2","subunits.Gene.name.syn.":"KIAA0339, KMT2F, SET1, SET1A;None;HCF1, HFC1;BIG3;RBQ3;TMEM113, WDR82A;None;CFP1, CGBP, PCCX1, PHF18;ASH2L1;None","Disease.comment":"None","Subunits.comment":"Corresponding to protein CXXC1 (CFP1) , the authors refer to isoform 2 of Uniprot: Q9P0U4 (Q9P0U4-2).The authors did not specify the proteins HCFC1 and HCFC2. Both proteins are shown alternatively.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6470,"ComplexName":"Set1B complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa nuclear extracts","subunits.UniProt.IDs.":"O15294;P51610;P61964;Q15291;Q6UXN9;Q8NFC6;Q96IK1;Q9C005;Q9P0U4;Q9UBL3;Q9UPS6;Q9Y5Z7","subunits.Entrez.IDs.":"8473;3054;11091;5929;80335;259282;91272;84661;30827;9070;23067;29915","Protein.complex.purification.method":"MI:0096-pull down;MI:0069-mass spectrometry studies of complexes","GO.ID":"GO:0051568;GO:0005634;GO:0006355;GO:0006325","GO.description":"histone H3-K4 methylation;nucleus;regulation of transcription, DNA-templated;chromatin organization","FunCat.ID":"70.10;11.02.03.04","FunCat.description":"nucleus;transcriptional control","PubMed.ID":23508102,"subunits.Protein.name.":"UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit;Host cell factor 1;WD repeat-containing protein 5;Retinoblastoma-binding protein 5;WD repeat-containing protein 82;Biorientation of chromosomes in cell division protein 1-like 1;Biorientation of chromosomes in cell division protein 1;Protein dpy-30 homolog;CXXC-type zinc finger protein 1;Set1/Ash2 histone methyltransferase complex subunit ASH2;Histone-lysine N-methyltransferase SETD1B;Host cell factor 2","subunits.Gene.name.":"OGT;HCFC1;WDR5;RBBP5;WDR82;BOD1L1;BOD1;DPY30;CXXC1;ASH2L;SETD1B;HCFC2","subunits.Gene.name.syn.":"None;HCF1, HFC1;BIG3;RBQ3;TMEM113, WDR82A;BOD1L, FAM44A, KIAA1327;FAM44B;None;CFP1, CGBP, PCCX1, PHF18;ASH2L1;KIAA1076, KMT2G, SET1B;None","Disease.comment":"None","Subunits.comment":"Corresponding to protein CXXC1 (CFP1) , the authors refer to isoform 2 of Uniprot: Q9P0U4 (Q9P0U4-2).The authors did not specify the proteins HCFC1 and HCFC2. Both proteins are shown alternatively.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6471,"ComplexName":"Cx43-Trim21 complex","Organism":"Rat","Synonyms":"Gja1-Trim21 complex","Cell.line":"C6 rat glioma (C6) cells","subunits.UniProt.IDs.":"D4ACF2;P08050","subunits.Entrez.IDs.":"308901;24392","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0071-molecular sieving","GO.ID":"GO:1903596;GO:0016567;GO:0005921","GO.description":"regulation of gap junction assembly;protein ubiquitination;gap junction","FunCat.ID":"14.07.05","FunCat.description":"modification by ubiquitination, deubiquitination","PubMed.ID":23106098,"subunits.Protein.name.":"Protein Trim21;Gap junction alpha-1 protein","subunits.Gene.name.":"Trim21;Gja1","subunits.Gene.name.syn.":"Trim21_predicted, rCG_40392;Cxn-43, Cx43","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Through the examinations of Cx43 assemblies under nondenaturing conditions, the results suggests that the Cx43/Trim21 complex is an active participant of GJ ubiquitylation and turnover. Cx43 phosphorylation, not association with TRIM21 alone, regulates GJ ubiquitylation.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6472,"ComplexName":"Bcl-2-Beclin1-UVRAG-PI(3)KC3 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"P10415;Q14457;Q8NEB9;Q99570;Q9P2Y5","subunits.Entrez.IDs.":"596;8678;5289;30849;7405","Protein.complex.purification.method":"MI:0096-pull down","GO.ID":"GO:0000045","GO.description":"autophagosome assembly","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":16799551,"subunits.Protein.name.":"Apoptosis regulator Bcl-2;Beclin-1;Phosphatidylinositol 3-kinase catalytic subunit type 3;Phosphoinositide 3-kinase regulatory subunit 4;UV radiation resistance-associated gene protein","subunits.Gene.name.":"BCL2;BECN1;PIK3C3;PIK3R4;UVRAG","subunits.Gene.name.syn.":"None;GT197;VPS34;VPS15;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Beclin1 functions as a platform to form a Bcl-2\\u2013UVRAG\\u2013PI(3)KC3 multiprotein complex in which binding of each constituent requires a different region of Beclin1. Bcl-2\\u2013Beclin1 interaction declines during starvation, whereas the UVRAG\\u2013Beclin1 interaction remains intact. This indicates that UVRAG and Bcl-2 function as activator and repressor, respectively. Under stressed conditions, Bcl-2 only weakly associates with the Beclin\\u2013PI(3)KC3 complex, whereas UVRAG remains in the complex, resulting in continuously activating signal transduction and thus unbalanced, amplified autophagy. (PMID:16799551)","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6473,"ComplexName":"mitochondrial calcium uniporter complex","Organism":"Human","Synonyms":"mitochondrial calcium uniplex","Cell.line":"HEK-293T cells","subunits.UniProt.IDs.":"Q8IYU8;Q8NE86;Q9BPX6;Q9H4I9;Q9NWR8","subunits.Entrez.IDs.":"221154;90550;10367;91689;55013","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0006851;GO:0005739;GO:0051560","GO.description":"mitochondrial calcium ion transport;mitochondrion;mitochondrial calcium ion homeostasis","FunCat.ID":"70.16","FunCat.description":"mitochondrion","PubMed.ID":24231807,"subunits.Protein.name.":"Calcium uptake protein 2, mitochondrial;Calcium uniporter protein, mitochondrial;Calcium uptake protein 1, mitochondrial;Essential MCU regulator, mitochondrial;Calcium uniporter regulatory subunit MCUb, mitochondrial","subunits.Gene.name.":"MICU2;MCU;MICU1;SMDT1;MCUB","subunits.Gene.name.syn.":"EFHA1;C10orf42, CCDC109A;CALC, CBARA1;C22orf32, EMRE;CCDC109B","Disease.comment":"Loss-of-function mutations in MICU1 cause a brain and muscle disorder linked to primary alterations in mitochondrial calcium signaling (OMIM:615673, PMID:24336167).","Subunits.comment":"None","Complex.comment":"Subunit EMRE (SMDT1) is essential for in vivo uniporter current and additionally bridges the calcium-sensing role of MICU1 and MICU2 with the calcium conducting role of MCU.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6474,"ComplexName":"Cubam complex","Organism":"Human","Synonyms":"Cubiln-AMN complex; Cubilin-amnionless complex","Cell.line":"renal cortex membranes","subunits.UniProt.IDs.":"O60494;Q9BXJ7","subunits.Entrez.IDs.":"8029;81693","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies;MI:0071-molecular sieving","GO.ID":"GO:0006897;GO:0015889","GO.description":"endocytosis;cobalamin transport","FunCat.ID":"20.09.18.09.01","FunCat.description":"endocytosis","PubMed.ID":14576052,"subunits.Protein.name.":"Cubilin;Protein amnionless","subunits.Gene.name.":"CUBN;AMN","subunits.Gene.name.syn.":"IFCR;None","Disease.comment":"Imerslund-Gr\\u00e4sbeck syndrome (I-GS; megaloblastic anemia 1, OMIM:261100), is caused by genetic defects in either the cubilin or AMN genes. IG-S is characterized by selective malabsorption of cobalamin (vitamin B(12)) despite normal production and function of intrinsic factor GIF.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6475,"ComplexName":"Dnm1l-Mff complex","Organism":"Mouse","Synonyms":"Drp1-Mff complex","Cell.line":"None","subunits.UniProt.IDs.":"Q6PCP5;Q8K1M6","subunits.Entrez.IDs.":"75734;74006","Protein.complex.purification.method":"MI:0027-cosedimentation","GO.ID":"GO:0000266","GO.description":"mitochondrial fission","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26446846,"subunits.Protein.name.":"Mitochondrial fission factor;Dynamin-1-like protein","subunits.Gene.name.":"Mff;Dnm1l","subunits.Gene.name.syn.":"None;Drp1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Residing in the cytosol as dimers and tetramers, Drp1 is recruited by receptors (Mff; Fis1; MiD51 and MiD49) on the mitochondrial outer membrane, where it further assembles into a helical ring that drives division via GTP-dependent constriction.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6476,"ComplexName":"erlin1/2-RNF170 complex","Organism":"Human","Synonyms":"None","Cell.line":"alpha T3-1 cell line; HeLa cells","subunits.UniProt.IDs.":"O75477;O94905;Q96K19","subunits.Entrez.IDs.":"10613;11160;81790","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005789;GO:0001881","GO.description":"endoplasmic reticulum membrane;receptor recycling","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":21610068,"subunits.Protein.name.":"Erlin-1;Erlin-2;E3 ubiquitin-protein ligase RNF170","subunits.Gene.name.":"ERLIN1;ERLIN2;RNF170","subunits.Gene.name.syn.":"C10orf69, KE04, KEO4, SPFH1;C8orf2, SPFH2;None","Disease.comment":"A  point mutation Arg-to-Cys in human RNF170 is the cause of autosomaldominant sensory ataxia, a rare, progressive ataxia caused bydegeneration of the posterior columns of the spinal cord (OMIM:608984)","Subunits.comment":"None","Complex.comment":"RNF170 interacts constitutively with the erlin1/2 complex and depletion of the erlin1/2 complex inhibits RNF170 association with activated IP3 receptors but not vice-versa. It appears that RNF170 is recruited to activated IP3 receptors by the erlin1/2 complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6477,"ComplexName":"ZEB2-KDM1A complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O60315;O60341","subunits.Entrez.IDs.":"9839;23028","Protein.complex.purification.method":"MI:0096-pull down","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":28069602,"subunits.Protein.name.":"Zinc finger E-box-binding homeobox 2;Lysine-specific histone demethylase 1A","subunits.Gene.name.":"ZEB2;KDM1A","subunits.Gene.name.syn.":"KIAA0569 SIP1 ZFHX1B ZFX1B;AOF2 KDM1 KIAA0601 LSD1","Disease.comment":"OMIM:613065 Leukemia, acute lymphoblastic; ALL","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6478,"ComplexName":"Dnm1l-Mief1 complex","Organism":"Mouse","Synonyms":"Drp1-MiD51 complex","Cell.line":"None","subunits.UniProt.IDs.":"Q8BGV8;Q8K1M6","subunits.Entrez.IDs.":"239555;74006","Protein.complex.purification.method":"MI:0027-cosedimentation","GO.ID":"GO:0000266","GO.description":"mitochondrial fission","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26446846,"subunits.Protein.name.":"Mitochondrial dynamics protein MID51;Dynamin-1-like protein","subunits.Gene.name.":"Mief1;Dnm1l","subunits.Gene.name.syn.":"Mid51,Smcr7l;Drp1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Residing in the cytosol as dimers and tetramers, Drp1 is recruited by receptors (Mff; Fis1; MiD51 and MiD49) on the mitochondrial outer membrane, where it further assembles into a helical ring that drives division via GTP-dependent constriction.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6479,"ComplexName":"Cubilin-intrinsic factor-cobalamin complex","Organism":"Human","Synonyms":"Cubilin-IF-B12 receptor complex","Cell.line":"renal cortex membranes","subunits.UniProt.IDs.":"O60494;P27352","subunits.Entrez.IDs.":"8029;2694","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0015889","GO.description":"cobalamin transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":14576052,"subunits.Protein.name.":"Cubilin;Gastric intrinsic factor","subunits.Gene.name.":"CUBN;GIF","subunits.Gene.name.syn.":"IFCR;IFMH","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cobalamin (vitamin B12 is bound to the intrinsic factor GIF.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6480,"ComplexName":"Ncam-Fgfr4 signaling complex","Organism":"Mouse","Synonyms":"Ncam-fibroblast-growth-factor receptor-4 signalling complex","Cell.line":"Rip1Tag2 NCAM+/+ mice (model of pancreatic beta-cell carcinogenesis)","subunits.UniProt.IDs.":"P05480;P06837;P13595;P15116;Q03142;Q60598;Q62077;Q8C180","subunits.Entrez.IDs.":"20779;14432;17967;12558;14186;13043;18803;327826","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0031175;GO:0007160","GO.description":"neuron projection development;cell-matrix adhesion","FunCat.ID":"34.07.02","FunCat.description":"cell-matrix adhesion","PubMed.ID":20798051,"subunits.Protein.name.":"Neuronal proto-oncogene tyrosine-protein kinase Src;Neuromodulin;Neural cell adhesion molecule 1;Cadherin-2;Fibroblast growth factor receptor 4;Src substrate cortactin;1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1;Fibroblast growth factor receptor substrate 2","subunits.Gene.name.":"Src;Gap43;Ncam1;Cdh2;Fgfr4;Cttn;Plcg1;Frs2","subunits.Gene.name.syn.":"pp60c-src;Basp2;Ncam;None;None;Ems1;Plcg-1;Frs2a","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"N-CAM stimulates beta1-integrin-mediated cell-matrix adhesion by activating FGFR signalling.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6481,"ComplexName":"WASH complex","Organism":"Human","Synonyms":"WASH regulatory complex (SHRC)","Cell.line":"HeLa cells; Jurkat T cell lysates","subunits.UniProt.IDs.":"A8K0Z3;Q12768;Q2M389;Q9Y3C0;Q9Y4E1","subunits.Entrez.IDs.":"100287171;9897;23325;51019;253725","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20498093,"subunits.Protein.name.":"WAS protein family homolog 1;WASH complex subunit strumpellin;WASH complex subunit SWIP;WASH complex subunit CCDC53;WASH complex subunit FAM21C","subunits.Gene.name.":"WASH1;KIAA0196;KIAA1033;CCDC53;FAM21C","subunits.Gene.name.syn.":"FAM39E;SPG8, RTSC, RTSC1, WASHC5;MRT43, SWIP, WASHC4;x0009; AD-016; CGI-116;KIAA0592","Disease.comment":"Strumpellin is mutated in the human disease hereditary spastic paraplegia (OMIM:603563). WASH is a member of the Wiskott-Aldrich syndrome protein family (WASP).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6482,"ComplexName":"CUL4B-DDB1-DTL-CSN complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"P61201;Q13098;Q13620;Q16531;Q9NZJ0","subunits.Entrez.IDs.":"9318;2873;8450;1642;51514","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":16861906,"subunits.Protein.name.":"COP9 signalosome complex subunit 2;COP9 signalosome complex subunit 1;Cullin-4B;DNA damage-binding protein 1;Denticleless protein homolog","subunits.Gene.name.":"COPS2;GPS1;CUL4B;DDB1;DTL","subunits.Gene.name.syn.":"CSN2, TRIP15;COPS1, CSN1;KIAA0695;XAP1;CDT2,CDW1,DCAF2,L2DTL,RAMP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"CUL4/DDB1 E3 ligase complex plays a critical role in regulating the cell cycle progression, replication and DNA damage.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6483,"ComplexName":"CAPZalpha-CAPZbeta complex","Organism":"Human","Synonyms":"CAPZalpha-CAPZbeta heterodimer complex","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"P47756;P52907","subunits.Entrez.IDs.":"832;829","Protein.complex.purification.method":"None","GO.ID":"GO:0051693","GO.description":"actin filament capping","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20498093,"subunits.Protein.name.":"F-actin-capping protein subunit beta;F-actin-capping protein subunit alpha-1","subunits.Gene.name.":"CAPZB;CAPZA1","subunits.Gene.name.syn.":"CAPB, CAPPB, CAPZ;CAPPA1, CAPZ, CAZ1","Disease.comment":"None","Subunits.comment":"Since the authors did not specify F-actin-capping protein, we used isoform CAPZA1.","Complex.comment":"CAPZalpha-CAPZbeta complex is weakly associated with the WASH complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6484,"ComplexName":"WASH-CAPZalpa/beta complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"A8K0Z3;P47756;P52907;Q12768;Q2M389;Q9Y3C0;Q9Y4E1","subunits.Entrez.IDs.":"100287171;832;829;9897;23325;51019;253725","Protein.complex.purification.method":"None","GO.ID":"GO:0051693;GO:0005769;GO:0034314;GO:0016197","GO.description":"actin filament capping;early endosome;Arp2/3 complex-mediated actin nucleation;endosomal transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20498093,"subunits.Protein.name.":"WAS protein family homolog 1;F-actin-capping protein subunit beta;F-actin-capping protein subunit alpha-1;WASH complex subunit strumpellin;WASH complex subunit SWIP;WASH complex subunit CCDC53;WASH complex subunit FAM21C","subunits.Gene.name.":"WASH1;CAPZB;CAPZA1;KIAA0196;KIAA1033;CCDC53;FAM21C","subunits.Gene.name.syn.":"FAM39E;CAPB, CAPPB, CAPZ;CAPPA1, CAPZ, CAZ1;SPG8, RTSC, RTSC1, WASHC5;MRT43, SWIP, WASHC4;x0009; AD-016; CGI-116;KIAA0592","Disease.comment":"Strumpellin is mutated in the human disease hereditary spastic paraplegia (OMIM:603563). WASH is a member of the Wiskott-Aldrich syndrome protein family (WASP).","Subunits.comment":"Since the authors did not specify F-actin-capping protein, we used isoform CAPZA1.","Complex.comment":"CAPZalpha/beta heterodimer complex also copurified with WASH complex, but only weakly, suggesting that CAPZ is a peripheral component. FAM21 interacts directly with CAPZ and inhibits its actin-capping activity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6485,"ComplexName":"HIF1alpha-VHL-ElonginB-ElonginC complex","Organism":"Mammalia","Synonyms":"HIF1alpha-VBC complex","Cell.line":"None","subunits.UniProt.IDs.":"P40337;Q15369;Q15370;Q16665","subunits.Entrez.IDs.":"7428;6921;6923;3091","Protein.complex.purification.method":"MI:0114-x-ray crystallography","GO.ID":"GO:0032364","GO.description":"oxygen homeostasis","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":12004076,"subunits.Protein.name.":"Von Hippel-Lindau disease tumor suppressor;Transcription elongation factor B polypeptide 1;Transcription elongation factor B polypeptide 2;Hypoxia-inducible factor 1-alpha","subunits.Gene.name.":"VHL;TCEB1;TCEB2;HIF1A","subunits.Gene.name.syn.":"None;elongin c;elongin b;BHLHE78 MOP1 PASD8","Disease.comment":"Mutations in the VHL protein are associated with von Hippel\\u2013Lindau cancer predisposition syndrome (OMIM:193300).","Subunits.comment":"Since the cell line was not specified in the publication, the orthologous human proteins were used.","Complex.comment":"VHL is responsible for the ubiquitination of  HIF1alpha.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6486,"ComplexName":"CUL4A-DDB1-DTL complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"Q13619;Q16531;Q9NZJ0","subunits.Entrez.IDs.":"8451;1642;51514","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0044257;GO:0006974","GO.description":"cellular protein catabolic process;cellular response to DNA damage stimulus","FunCat.ID":"14.13.01;32.01.09","FunCat.description":"cytoplasmic and nuclear protein degradation;DNA damage response","PubMed.ID":16861906,"subunits.Protein.name.":"Cullin-4A;DNA damage-binding protein 1;Denticleless protein homolog","subunits.Gene.name.":"CUL4A;DDB1;DTL","subunits.Gene.name.syn.":"None;XAP1;CDT2,CDW1,DCAF2,L2DTL,RAMP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"CUL4/DDB1 E3 ligase complex plays a critical role in regulating the cell cycle progression, replication and DNA damage.DTL is a protein that associates with CUL4 and DDB1 and is required for CDT1 degradation in response to DNA damage in both Drosophila and human cells.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6487,"ComplexName":"CUL4B-DDB1-TLE2 complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"Q04725;Q13620;Q16531","subunits.Entrez.IDs.":"7089;8450;1642","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0010498","GO.description":"proteasomal protein catabolic process","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":17041588,"subunits.Protein.name.":"Transducin-like enhancer protein 2;Cullin-4B;DNA damage-binding protein 1","subunits.Gene.name.":"TLE2;CUL4B;DDB1","subunits.Gene.name.syn.":"None;KIAA0695;XAP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6488,"ComplexName":"CUL4A-DDB1-EED complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O75530;Q13619;Q16531","subunits.Entrez.IDs.":"8726;8451;1642","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0010498;GO:0031060","GO.description":"proteasomal protein catabolic process;regulation of histone methylation","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":17041588,"subunits.Protein.name.":"Polycomb protein EED;Cullin-4A;DNA damage-binding protein 1","subunits.Gene.name.":"EED;CUL4A;DDB1","subunits.Gene.name.syn.":"None;None;XAP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6489,"ComplexName":"CUL4A-DDB1-WDR5 complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"P61964;Q13619;Q16531","subunits.Entrez.IDs.":"11091;8451;1642","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0031060;GO:0010498","GO.description":"regulation of histone methylation;proteasomal protein catabolic process","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":17041588,"subunits.Protein.name.":"WD repeat-containing protein 5;Cullin-4A;DNA damage-binding protein 1","subunits.Gene.name.":"WDR5;CUL4A;DDB1","subunits.Gene.name.syn.":"BIG3;None;XAP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"WDR5, DDB1 and CUL4A can interact with the H3 N-terminal peptide containing methylated K4, but not its unmodified form in cell lysates, suggesting that these interactions are specific for methylated histone H3.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6490,"ComplexName":"CUL4B-DDB1-WDR26 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"Q13620;Q16531;Q9H7D7","subunits.Entrez.IDs.":"8450;1642;80232","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":17041588,"subunits.Protein.name.":"Cullin-4B;DNA damage-binding protein 1;WD repeat-containing protein 26","subunits.Gene.name.":"CUL4B;DDB1;WDR26","subunits.Gene.name.syn.":"KIAA0695;XAP1;CDW2,MIP2,PRO0852","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6491,"ComplexName":"CUL4A-DDB1-RBBP5 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"Q13619;Q15291;Q16531","subunits.Entrez.IDs.":"8451;5929;1642","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":17041588,"subunits.Protein.name.":"Cullin-4A;Retinoblastoma-binding protein 5;DNA damage-binding protein 1","subunits.Gene.name.":"CUL4A;RBBP5;DDB1","subunits.Gene.name.syn.":"None;RBQ3;XAP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6492,"ComplexName":"CUL4A-DDB1-WDR5B complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"Q13619;Q16531;Q86VZ2","subunits.Entrez.IDs.":"8451;1642;54554","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":17041588,"subunits.Protein.name.":"Cullin-4A;DNA damage-binding protein 1;WD repeat-containing protein 5B","subunits.Gene.name.":"CUL4A;DDB1;WDR5B","subunits.Gene.name.syn.":"None;XAP1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6493,"ComplexName":"CUL4A-DDB1-WDR57 complex","Organism":"Human","Synonyms":"CUL4A-DDB1-SNRNP40 complex","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"Q13619;Q16531;Q96DI7","subunits.Entrez.IDs.":"8451;1642;9410","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":17041588,"subunits.Protein.name.":"Cullin-4A;DNA damage-binding protein 1;U5 small nuclear ribonucleoprotein 40 kDa protein","subunits.Gene.name.":"CUL4A;DDB1;SNRNP40","subunits.Gene.name.syn.":"None;XAP1;PRP8BP SFP38 WDR57","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6494,"ComplexName":"CUL4A-DDB1-WDR61 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"Q13619;Q16531;Q9GZS3","subunits.Entrez.IDs.":"8451;1642;80349","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":17041588,"subunits.Protein.name.":"Cullin-4A;DNA damage-binding protein 1;WD repeat-containing protein 61","subunits.Gene.name.":"CUL4A;DDB1;WDR61","subunits.Gene.name.syn.":"None;XAP1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6495,"ComplexName":"CUL4B-DDB1-GRWD1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"Q13620;Q16531;Q9BQ67","subunits.Entrez.IDs.":"8450;1642;83743","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":17041588,"subunits.Protein.name.":"Cullin-4B;DNA damage-binding protein 1;Glutamate-rich WD repeat-containing protein 1","subunits.Gene.name.":"CUL4B;DDB1;GRWD1","subunits.Gene.name.syn.":"KIAA0695;XAP1;GRWD,KIAA1942,WDR28","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6496,"ComplexName":"TOM20-TOM22-pOTC complex","Organism":"Human","Synonyms":"TOMM20-TOMM22-pOTC complex","Cell.line":"None","subunits.UniProt.IDs.":"P00480;Q15388;Q9NS69","subunits.Entrez.IDs.":"5009;9804;56993","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005742;GO:0005739;GO:0006839","GO.description":"mitochondrial outer membrane translocase complex;mitochondrion;mitochondrial transport","FunCat.ID":"70.16;20.09.04","FunCat.description":"mitochondrion;mitochondrial transport","PubMed.ID":10982837,"subunits.Protein.name.":"Ornithine carbamoyltransferase, mitochondrial;Mitochondrial import receptor subunit TOM20 homolog;Mitochondrial import receptor subunit TOM22 homolog","subunits.Gene.name.":"OTC;TOMM20;TOMM22","subunits.Gene.name.syn.":"None;KIAA0016;TOM22","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Tom22 functions as an import receptor for preproteins. It forms a receptor complex with human Tom20. The internal segment of the human Tom22 cytosolic domain is important for the complex formation. The N-terminal domain of Tom22 is important for binding to the mature portion of pre-ornithine transcarbamylase (pOTC).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6497,"ComplexName":"TOM complex (TOM5, TOM6, TOM7, TOM20, TOM22, TOM40, TOM70), mitochondrial","Organism":"Human","Synonyms":"TOM (TOMM5, TOMM6, TOMM7, TOMM20, TOMM22, TOMM40, TOMM70) complex; preprotein translocase complex","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O94826;O96008;Q15388;Q8N4H5;Q96B49;Q9NS69;Q9P0U1","subunits.Entrez.IDs.":"9868;10452;9804;401505;100188893;56993;54543","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0051-fluorescence technologies;MI:0276-blue native page;MI:0047-far western blotting","GO.ID":"GO:0045040;GO:0005739;GO:0005741;GO:0005742;GO:0070096","GO.description":"protein import into mitochondrial outer membrane;mitochondrion;mitochondrial outer membrane;mitochondrial outer membrane translocase complex;mitochondrial outer membrane translocase complex assembly","FunCat.ID":"70.16;70.16.01","FunCat.description":"mitochondrion;mitochondrial outer membrane","PubMed.ID":18331822,"subunits.Protein.name.":"Mitochondrial import receptor subunit TOM70;Mitochondrial import receptor subunit TOM40 homolog;Mitochondrial import receptor subunit TOM20 homolog;Mitochondrial import receptor subunit TOM5 homolog;Mitochondrial import receptor subunit TOM6 homolog;Mitochondrial import receptor subunit TOM22 homolog;Mitochondrial import receptor subunit TOM7 homolog","subunits.Gene.name.":"TOMM70;TOMM40;TOMM20;TOMM5;TOMM6;TOMM22;TOMM7","subunits.Gene.name.syn.":"KIAA0719 TOM70 TOMM70A;C19orf1 PEREC1 TOM40;KIAA0016;C9orf105,TOM5;OBTP,TOM6;TOM22;TOM7,TOMM07","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In the present study, the TOM complex was immuno-isolated from HeLa cells and hTom5 and hTom6 were newly identified as components of the complex together with hTom70, hTom20, hTom22, hTom40, and hTom7. Knockdown of Tom7, but not Tom5 and Tom6, strongly compromised stability of the TOM complex. Conversely, knockdown of hTom40 decreased the level of all small Tom proteins. Matrix import of preprotein was affected by double knockdown of any combinationof small Tom proteins. These results indicate that human small Tom proteins maintain the structural integrity of the TOM complex.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6498,"ComplexName":"TOM7 120K intermediate assembly complex (TOM7, TOM22, TOM40), mitochondrial","Organism":"Human","Synonyms":"120-kDa complex (TOMM7, TOMM22, TOMM40); preprotein translocase assembly intermediate complex","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O96008;Q9NS69;Q9P0U1","subunits.Entrez.IDs.":"10452;56993;54543","Protein.complex.purification.method":"MI:0413-electrophoretic mobility shift assay;MI:0276-blue native page","GO.ID":"GO:0005741;GO:0098799;GO:0005742;GO:0005739;GO:0045040;GO:0098799","GO.description":"mitochondrial outer membrane;outer mitochondrial membrane protein complex;mitochondrial outer membrane translocase complex;mitochondrion;protein import into mitochondrial outer membrane;outer mitochondrial membrane protein complex","FunCat.ID":"70.16.01;70.16","FunCat.description":"mitochondrial outer membrane;mitochondrion","PubMed.ID":12198123,"subunits.Protein.name.":"Mitochondrial import receptor subunit TOM40 homolog;Mitochondrial import receptor subunit TOM22 homolog;Mitochondrial import receptor subunit TOM7 homolog","subunits.Gene.name.":"TOMM40;TOMM22;TOMM7","subunits.Gene.name.syn.":"C19orf1 PEREC1 TOM40;TOM22;TOM7,TOMM07","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Tom7 is a component of the translocase of the outermitochondrial membrane (TOM) and assembles into ageneral import pore complex that translocates preproteinsinto mitochondria. Tom7 does not require ATP for its import and assembly.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6499,"ComplexName":"SOS1-ABI1-EPS8 complex","Organism":"Human","Synonyms":"None","Cell.line":"293T cells","subunits.UniProt.IDs.":"Q07889;Q12929;Q8IZP0","subunits.Entrez.IDs.":"6654;2059;10006","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0007264;GO:0007169;GO:0031532","GO.description":"small GTPase mediated signal transduction;transmembrane receptor protein tyrosine kinase signaling pathway;actin cytoskeleton reorganization","FunCat.ID":"30.01.05.05.01;30.05.01.12","FunCat.description":"small GTPase mediated signal transduction;transmembrane receptor protein tyrosine kinase signalling pathways","PubMed.ID":14565974,"subunits.Protein.name.":"Son of sevenless homolog 1;Epidermal growth factor receptor kinase substrate 8;Abl interactor 1","subunits.Gene.name.":"SOS1;EPS8;ABI1","subunits.Gene.name.syn.":"None;None;SSH3BP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Similarly to eps8, eps8Ls interact with Abi1 and Sos-1; however, only eps8L1 and eps8L2 activate the Rac-GEF activity of Sos-1, and bind to actin in vivo.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6500,"ComplexName":"TOM complex (Tom7, Tom22, Hsp60), mitochondrial","Organism":"Rat","Synonyms":"TOM complex (Tomm7, Tomm22, Hspd1)","Cell.line":"rat kidney mitochondria","subunits.UniProt.IDs.":"D3ZMR1;P63039;Q75Q41","subunits.Entrez.IDs.":"685620;63868;300075","Protein.complex.purification.method":"MI:0276-blue native page","GO.ID":"GO:0005741;GO:0005739;GO:0045040;GO:0005742;GO:0070096","GO.description":"mitochondrial outer membrane;mitochondrion;protein import into mitochondrial outer membrane;mitochondrial outer membrane translocase complex;mitochondrial outer membrane translocase complex assembly","FunCat.ID":"70.16.01;70.16","FunCat.description":"mitochondrial outer membrane;mitochondrion","PubMed.ID":12198123,"subunits.Protein.name.":"Protein Tomm7;60 kDa heat shock protein, mitochondrial;Mitochondrial import receptor subunit TOM22 homolog","subunits.Gene.name.":"Tomm7;Hspd1;Tomm22","subunits.Gene.name.syn.":"None;Hsp60;Tom22","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Tom7 is a component of the translocase of the outermitochondrial membrane (TOM) and assembles into ageneral import pore complex that translocates preproteinsinto mitochondria.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6501,"ComplexName":"SOS1-ABI1-EPS8L1 complex","Organism":"Human","Synonyms":"None","Cell.line":"293T cells","subunits.UniProt.IDs.":"Q07889;Q8IZP0;Q8TE68","subunits.Entrez.IDs.":"6654;10006;54869","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0031532;GO:0007264;GO:0007169","GO.description":"actin cytoskeleton reorganization;small GTPase mediated signal transduction;transmembrane receptor protein tyrosine kinase signaling pathway","FunCat.ID":"30.01.05.05.01;30.05.01.12","FunCat.description":"small GTPase mediated signal transduction;transmembrane receptor protein tyrosine kinase signalling pathways","PubMed.ID":14565974,"subunits.Protein.name.":"Son of sevenless homolog 1;Abl interactor 1;Epidermal growth factor receptor kinase substrate 8-like protein 1","subunits.Gene.name.":"SOS1;ABI1;EPS8L1","subunits.Gene.name.syn.":"None;SSH3BP1;DRC3, EPS8R1, PP10566","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Similarly to eps8, eps8Ls interact with Abi1 and Sos-1; however, only eps8L1 and eps8L2 activate the Rac-GEF activity of Sos-1, and bind to actin in vivo.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6502,"ComplexName":"Estrogen receptor complex (ESR1, EP300, NCOA1)","Organism":"Human","Synonyms":"None","Cell.line":"MCF-7 breast cancer cells; HEK-293 cell","subunits.UniProt.IDs.":"P03372;Q09472;Q15788","subunits.Entrez.IDs.":"2099;2033;8648","Protein.complex.purification.method":"MI:0096-pull down;MI:0019-coimmunoprecipitation;MI:0047-far western blotting","GO.ID":"GO:0071898","GO.description":"regulation of estrogen receptor binding","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":8876171,"subunits.Protein.name.":"Estrogen receptor;Histone acetyltransferase p300;Nuclear receptor coactivator 1","subunits.Gene.name.":"ESR1;EP300;NCOA1","subunits.Gene.name.syn.":"ESR, NR3A1;P300;BHLHE74, SRC1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"ERAP160 directly interacts with ER and associates with p300 in vivo in rabbit reticulocyte lysates.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6503,"ComplexName":"SOS1-ABI1-EPS8L2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q07889;Q8IZP0;Q9H6S3","subunits.Entrez.IDs.":"6654;10006;64787","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0031532;GO:0007264;GO:0007169","GO.description":"actin cytoskeleton reorganization;small GTPase mediated signal transduction;transmembrane receptor protein tyrosine kinase signaling pathway","FunCat.ID":"30.01.05.05.01;30.05.01.12","FunCat.description":"small GTPase mediated signal transduction;transmembrane receptor protein tyrosine kinase signalling pathways","PubMed.ID":14565974,"subunits.Protein.name.":"Son of sevenless homolog 1;Abl interactor 1;Epidermal growth factor receptor kinase substrate 8-like protein 2","subunits.Gene.name.":"SOS1;ABI1;EPS8L2","subunits.Gene.name.syn.":"None;SSH3BP1;EPS8R2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Similarly to eps8, eps8Ls interact with Abi1 and Sos-1; however, only eps8L1 and eps8L2 activate the Rac-GEF activity of Sos-1, and bind to actin in vivo.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6504,"ComplexName":"SOS1-ABI1-EPS8L3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q07889;Q8IZP0;Q8TE67","subunits.Entrez.IDs.":"6654;10006;79574","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":14565974,"subunits.Protein.name.":"Son of sevenless homolog 1;Abl interactor 1;Epidermal growth factor receptor kinase substrate 8-like protein 3","subunits.Gene.name.":"SOS1;ABI1;EPS8L3","subunits.Gene.name.syn.":"None;SSH3BP1;EPS8R3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The lack of Rac-GEF activity in eps8L3-containing complexes indicated that some additional molecular characteristics, shared by eps8, eps8L1, and eps8L2, are not present in eps8L3. Eps8, eps8L1, and L2, but not eps8L3 could directly associate to F-actin.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6505,"ComplexName":"ERBB3-SPG1 complex","Organism":"Human","Synonyms":"HER3-L1CAM complex","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"P21860;P32004","subunits.Entrez.IDs.":"2065;3897","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0043125;GO:0038129;GO:1901184;GO:0038131","GO.description":"ErbB-3 class receptor binding;ERBB3 signaling pathway;regulation of ERBB signaling pathway;neuregulin receptor activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":22815787,"subunits.Protein.name.":"Receptor tyrosine-protein kinase erbB-3;Neural cell adhesion molecule L1","subunits.Gene.name.":"ERBB3;L1CAM","subunits.Gene.name.syn.":"HER3;CAML1,MIC5,SPG1","Disease.comment":"Mutations in the human L1-CAM gene are responsible for a complex neurodevelopmental condition, generally referred to as L1 syndrome. Several pathogenic L1-CAM mutations have been identified in humans that cause L1 syndrome in affected individuals without affecting the level of L1-CAM-mediated homophilic cell adhesion when tested in vitro (PMID:19617634).","Subunits.comment":"None","Complex.comment":"During nervous system development different cell-to-cell communication mechanisms operate in parallel guiding migrating neurons and growing axons to generate complex arrays of neural circuits. Cross-regulatory interactions between different signalling pathways and redundancy between them can increase precision and fidelity of guidance systems. Immunoglobulin superfamily proteins of the NCAM and L1 families couple specific substrate recognition and cell adhesion with the activation of receptor tyrosine kinases. It has been shown that L1CAM binds physically erbB receptors. Different Ig-like domains located in the extracellular part of L1CAM can support this interaction. Binding of L1CAM to erbB enhances its response to neuregulins. L1CAM was able to physically interact with erbB3 in HEK293 cells.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6506,"ComplexName":"ERBB2-SPG1 complex","Organism":"Human","Synonyms":"ERBB2-L1CAM complex","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"P04626;P32004","subunits.Entrez.IDs.":"2064;3897","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0038131;GO:1901184;GO:0038128;GO:0005176","GO.description":"neuregulin receptor activity;regulation of ERBB signaling pathway;ERBB2 signaling pathway;ErbB-2 class receptor binding","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":22815787,"subunits.Protein.name.":"Receptor tyrosine-protein kinase erbB-2;Neural cell adhesion molecule L1","subunits.Gene.name.":"ERBB2;L1CAM","subunits.Gene.name.syn.":"HER2, MLN19, NEU, NGL;CAML1,MIC5,SPG1","Disease.comment":"Mutations in the human L1-CAM gene are responsible for a complex neurodevelopmental condition, generally referred to as L1 syndrome. Several pathogenic L1-CAM mutations have been identified in humans that cause L1 syndrome in affected individuals without affecting the level of L1-CAM-mediated homophilic cell adhesion when tested in vitro (PMID:19617634).","Subunits.comment":"None","Complex.comment":"During nervous system development different cell-to-cell communication mechanisms operate in parallel guiding migrating neurons and growing axons to generate complex arrays of neural circuits. Cross-regulatory interactions between different signalling pathways and redundancy between them can increase precision and fidelity of guidance systems. Immunoglobulin superfamily proteins of the NCAM and L1 families couple specific substrate recognition and cell adhesion with the activation of receptor tyrosine kinases. It has been shown that L1CAM binds physically erbB receptors. Different Ig-like domains located in the extracellular part of L1CAM can support this interaction. Binding of L1CAM to erbB enhances its response to neuregulins. Immunoprecipitation oferbB2 pulled down L1CAM, showing that L1CAM and erbB2receptor are physically bound when expressed in HEK293 cells.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6507,"ComplexName":"SERCA-PLN complex","Organism":"Human","Synonyms":"ATP2A2-PLN complex","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"P16615;P26678","subunits.Entrez.IDs.":"488;5350","Protein.complex.purification.method":"MI:0055-fluorescent resonance energy transfer","GO.ID":"GO:0006816;GO:1901897;GO:0003697;GO:0035198","GO.description":"calcium ion transport;regulation of relaxation of cardiac muscle;single-stranded DNA binding;miRNA binding","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26292938,"subunits.Protein.name.":"Sarcoplasmic/endoplasmic reticulum calcium ATPase 2;Cardiac phospholamban","subunits.Gene.name.":"ATP2A2;PLN","subunits.Gene.name.syn.":"ATP2B;PLB","Disease.comment":"OMIM:609909 Cardiomyopathy, dilated, 1P (PMID:25563649).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6508,"ComplexName":"L1cam-Ncam1 complex","Organism":"Mouse","Synonyms":"L1-Ncam complex","Cell.line":"N2a cells; ESb-MP cells","subunits.UniProt.IDs.":"P11627;P13595","subunits.Entrez.IDs.":"None;17967","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007155;GO:0007158","GO.description":"cell adhesion;neuron cell-cell adhesion","FunCat.ID":"34.07","FunCat.description":"cell adhesion","PubMed.ID":2295683,"subunits.Protein.name.":"Neural cell adhesion molecule L1;Neural cell adhesion molecule 1","subunits.Gene.name.":"L1cam;Ncam1","subunits.Gene.name.syn.":"Caml1;Ncam","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The neural cell adhesion molecules L1 and N-CAM interact functionally by formation of a complex. This interaction depends on appropriate carbohydrate structures.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6509,"ComplexName":"pERK-vimentin-KPNA2 complex","Organism":"Human","Synonyms":"None","Cell.line":"lung cancer cells","subunits.UniProt.IDs.":"P08670;P27361;P52292","subunits.Entrez.IDs.":"7431;5595;3838","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005737;GO:0002347;GO:0016477","GO.description":"cytoplasm;response to tumor cell;cell migration","FunCat.ID":"70.03;34.05.01","FunCat.description":"cytoplasm;cell migration","PubMed.ID":25728791,"subunits.Protein.name.":"Vimentin;Mitogen-activated protein kinase 3;Importin subunit alpha-1","subunits.Gene.name.":"VIM;MAPK3;KPNA2","subunits.Gene.name.syn.":"None;ERK1, PRKM3;RCH1, SRP1","Disease.comment":"pERK-vimentin-KPNA2 complex levels are positively associated with cancer invasiveness. The complex level is higher in advanced stage lung adenocarcinoma compared with that in early-stage cancer tissues.","Subunits.comment":"None","Complex.comment":"Vimentin binds to phosphorylated ERK1 or ERK2 (PMID:15748847).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6510,"ComplexName":"ILK-SERCA2A-PLN complex","Organism":"Human","Synonyms":"ILK-ATP22A-PLN complex","Cell.line":"None","subunits.UniProt.IDs.":"P16615;P26678;Q13418","subunits.Entrez.IDs.":"488;5350;3611","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:1901897;GO:0030018","GO.description":"regulation of relaxation of cardiac muscle;Z disc","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25208486,"subunits.Protein.name.":"Sarcoplasmic/endoplasmic reticulum calcium ATPase 2;Cardiac phospholamban;Integrin-linked protein kinase","subunits.Gene.name.":"ATP2A2;PLN;ILK","subunits.Gene.name.syn.":"ATP2B;PLB;ILK1 ILK2","Disease.comment":"OMIM:609909 Cardiomyopathy, dilated, 1P.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6511,"ComplexName":"L1cam-Itga5 complex","Organism":"Mouse","Synonyms":"L1-Vla5 complex","Cell.line":"ESb-MP cells","subunits.UniProt.IDs.":"P11627;P11688","subunits.Entrez.IDs.":"None;16402","Protein.complex.purification.method":"None","GO.ID":"GO:0098632;GO:0098743","GO.description":"protein binding involved in cell-cell adhesion;cell aggregation","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":8557754,"subunits.Protein.name.":"Neural cell adhesion molecule L1;Integrin alpha-5","subunits.Gene.name.":"L1cam;Itga5","subunits.Gene.name.syn.":"Caml1;Vla5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The L1 adhesion molecule is a member of the immunoglobulin superfamily shared by neural and immune cells. In the nervous system L1 can mediate cell binding by a homophilic mechanism. VLA-5, an RGD-specific fibronectin receptor on a wide variety of cell types, can bind to murine L1. Mouse ESb-MP cells expressing VLA-5 and L1 could be induced to aggregate in the presence of specific mAbs to CD24 (heat-stable antigen), a highly and heterogeneously glycosylated glycophosphatidylinositol-linked differentiation antigen of hematopoietic and neural cells.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6512,"ComplexName":"ILK-HSP90-CDC37 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"P07900;Q13418;Q16543","subunits.Entrez.IDs.":"3320;3611;11140","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":15882985,"subunits.Protein.name.":"Heat shock protein HSP 90-alpha;Integrin-linked protein kinase;Hsp90 co-chaperone Cdc37","subunits.Gene.name.":"HSP90AA1;ILK;CDC37","subunits.Gene.name.syn.":"HSP90A HSPC1 HSPCA;ILK1 ILK2;CDC37A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6513,"ComplexName":"MAN1-SMAD2 complex","Organism":"Human","Synonyms":"LEMD3-SMAD2 complex","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"Q15796;Q9Y2U8","subunits.Entrez.IDs.":"4087;23592","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0114-x-ray crystallography","GO.ID":"GO:0007179","GO.description":"transforming growth factor beta receptor signaling pathway","FunCat.ID":"30.05.01.18.01","FunCat.description":"TGF-beta-receptor signalling pathway","PubMed.ID":23779087,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 2;Inner nuclear membrane protein Man1","subunits.Gene.name.":"SMAD2;LEMD3","subunits.Gene.name.syn.":"MADH2, MADR2;MAN1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"MAN1 competes with transcription factors for binding to Smad2.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6514,"ComplexName":"SLN-ATP2A1 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O00631;O14983","subunits.Entrez.IDs.":"6588;487","Protein.complex.purification.method":"MI:0114-x-ray crystallography","GO.ID":"GO:0051924","GO.description":"regulation of calcium ion transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25983321,"subunits.Protein.name.":"Sarcolipin;Sarcoplasmic/endoplasmic reticulum calcium ATPase 1","subunits.Gene.name.":"SLN;ATP2A1","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6515,"ComplexName":"SLN-PLN-SERCA1A complex","Organism":"Human","Synonyms":"SLN-PLN-ATP2A1 complex","Cell.line":"Skeletal muscle fibers","subunits.UniProt.IDs.":"O00631;O14983;P26678","subunits.Entrez.IDs.":"6588;487;5350","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:1901894","GO.description":"regulation of calcium-transporting ATPase activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":24358354,"subunits.Protein.name.":"Sarcolipin;Sarcoplasmic/endoplasmic reticulum calcium ATPase 1;Cardiac phospholamban","subunits.Gene.name.":"SLN;ATP2A1;PLN","subunits.Gene.name.syn.":"None;None;PLB","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6516,"ComplexName":"SLN-PLN-SERCA2A complex","Organism":"Human","Synonyms":"SLN-PLN-ATP2A2 complex","Cell.line":"Skeletal muscle fibers","subunits.UniProt.IDs.":"O00631;P16615;P26678","subunits.Entrez.IDs.":"6588;488;5350","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:1901894","GO.description":"regulation of calcium-transporting ATPase activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":24358354,"subunits.Protein.name.":"Sarcolipin;Sarcoplasmic/endoplasmic reticulum calcium ATPase 2;Cardiac phospholamban","subunits.Gene.name.":"SLN;ATP2A2;PLN","subunits.Gene.name.syn.":"None;ATP2B;PLB","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6517,"ComplexName":"SERCA2a-alphaKAP-CaM-CaMKII complex","Organism":"Human","Synonyms":"ATP2A2-KPNA1-CAMK2A-CALM1 complex","Cell.line":"None","subunits.UniProt.IDs.":"P16615;P52294;P62158;Q9UQM7","subunits.Entrez.IDs.":"488;3836;801;815","Protein.complex.purification.method":"MI:0096-pull down","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":19671701,"subunits.Protein.name.":"Sarcoplasmic/endoplasmic reticulum calcium ATPase 2;Importin subunit alpha-5;Calmodulin;Calcium/calmodulin-dependent protein kinase type II subunit alpha","subunits.Gene.name.":"ATP2A2;KPNA1;CALM1; CAL;CAMK2A","subunits.Gene.name.syn.":"ATP2B;RCH2;CALM, CAM, CAM1, CAM2, CAMB, CALML2, CAM3, CAMC, CAMIII;CAMKA KIAA0968","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6518,"ComplexName":"CEP164-TTBK2 complex","Organism":"Human","Synonyms":"None","Cell.line":"retina","subunits.UniProt.IDs.":"Q6IQ55;Q9UPV0","subunits.Entrez.IDs.":"146057;22897","Protein.complex.purification.method":"MI:0018-two hybrid","GO.ID":"GO:0006974;GO:0060271;GO:0005814","GO.description":"cellular response to DNA damage stimulus;cilium assembly;centriole","FunCat.ID":"32.01.09","FunCat.description":"DNA damage response","PubMed.ID":22863007,"subunits.Protein.name.":"Tau-tubulin kinase 2;Centrosomal protein of 164 kDa","subunits.Gene.name.":"TTBK2;CEP164","subunits.Gene.name.syn.":"KIAA0847;KIAA1052, NPHP15","Disease.comment":"CEP164 is involved in Nephronophthisis 15 (PMID:22863007).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6519,"ComplexName":"CCDC92-CEP164 complex","Organism":"Human","Synonyms":"None","Cell.line":"retina","subunits.UniProt.IDs.":"Q53HC0;Q9UPV0","subunits.Entrez.IDs.":"80212;22897","Protein.complex.purification.method":"MI:0018-two hybrid","GO.ID":"GO:0006974","GO.description":"cellular response to DNA damage stimulus","FunCat.ID":"32.01.09","FunCat.description":"DNA damage response","PubMed.ID":22863007,"subunits.Protein.name.":"Coiled-coil domain-containing protein 92;Centrosomal protein of 164 kDa","subunits.Gene.name.":"CCDC92;CEP164","subunits.Gene.name.syn.":"None;KIAA1052, NPHP15","Disease.comment":"CEP164 is involved in Nephronophthisis 15 (PMID:22863007).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6520,"ComplexName":"Harmonin-SANS complex","Organism":"Human","Synonyms":"USH1C-USH1G complex","Cell.line":"None","subunits.UniProt.IDs.":"Q495M9;Q9Y6N9","subunits.Entrez.IDs.":"124590;10083","Protein.complex.purification.method":"MI:0096-pull down;MI:0071-molecular sieving;MI:0114-x-ray crystallography","GO.ID":"GO:0043583;GO:0007605","GO.description":"ear development;sensory perception of sound","FunCat.ID":"47.03.02.01;36.25.01.03","FunCat.description":"ear;hearing","PubMed.ID":20142502,"subunits.Protein.name.":"Usher syndrome type-1G protein;Harmonin","subunits.Gene.name.":"USH1G;USH1C","subunits.Gene.name.syn.":"SANS;AIE75","Disease.comment":"Hearing impairment mutations of harmonin and Sans in Usher syndrome (OMIM:276904) patients are found to disrupt the formation of the harmonin/Sans complex.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6521,"ComplexName":"Akt-PHLPP1-PHLPP2-FANCI-FANCD2-USP1-UAF1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"O60346;O94782;P31749;Q6ZVD8;Q8TAF3;Q9BXW9;Q9NVI1","subunits.Entrez.IDs.":"23239;7398;207;23035;57599;2177;55215","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":27097374,"subunits.Protein.name.":"PH domain leucine-rich repeat-containing protein phosphatase 1;Ubiquitin carboxyl-terminal hydrolase 1;RAC-alpha serine/threonine-protein kinase;PH domain leucine-rich repeat-containing protein phosphatase 2;WD repeat-containing protein 48;Fanconi anemia group D2 protein;Fanconi anemia group I protein","subunits.Gene.name.":"PHLPP1;USP1;AKT1;PHLPP2;WDR48;FANCD2;FANCI","subunits.Gene.name.syn.":"KIAA0606, PHLPP, PLEKHE1, SCOP;UBP;PKB, RAC;KIAA0931, PHLPPL;KIAA1449, UAF1;FACD;KIAA1794","Disease.comment":"FANCI and FANCD2 are involved in Fanconi anemia, complementation group I.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6522,"ComplexName":"Harmonin-CAD23 complex","Organism":"Human","Synonyms":"USH1C-CDH23 complex; CDH23-harmonin complex","Cell.line":"None","subunits.UniProt.IDs.":"Q9H251;Q9Y6N9","subunits.Entrez.IDs.":"64072;10083","Protein.complex.purification.method":"MI:0096-pull down","GO.ID":"GO:0043583;GO:0007605","GO.description":"ear development;sensory perception of sound","FunCat.ID":"47.03.02.01;36.25.01.03","FunCat.description":"ear;hearing","PubMed.ID":19297620,"subunits.Protein.name.":"Cadherin-23;Harmonin","subunits.Gene.name.":"CDH23;USH1C","subunits.Gene.name.syn.":"KIAA1774,KIAA1812;AIE75","Disease.comment":"Hereditary hearing-vision loss disease Usher syndrome (USH) (OMIM:276904) is caused by defects in USH1C gene.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6523,"ComplexName":"Ubiquilin-VCP-erasin complex","Organism":"Human","Synonyms":"UBQLN1-VCP-UBXN4 complex","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"P55072;Q92575;Q9UMX0","subunits.Entrez.IDs.":"7415;23190;29979","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation;MI:0096-pull down","GO.ID":"GO:0036503;GO:0034976","GO.description":"ERAD pathway;response to endoplasmic reticulum stress","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":19822669,"subunits.Protein.name.":"Transitional endoplasmic reticulum ATPase;UBX domain-containing protein 4;Ubiquilin-1","subunits.Gene.name.":"VCP;UBXN4;UBQLN1","subunits.Gene.name.syn.":"None;KIAA0242,UBXD2,UBXDC1;DA41, PLIC1","Disease.comment":"Disturbances in the ER-associated protein degradation (ERAD) pathway are involved in human diseases.","Subunits.comment":"For GST-pull down assays recombinant full-length mouse VCP(p97), human erasin and  human hHR23A was used.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6524,"ComplexName":"DZIP1-GLI3 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"P10071;Q86YF9","subunits.Entrez.IDs.":"2737;22873","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0060271;GO:0007224","GO.description":"cilium assembly;smoothened signaling pathway","FunCat.ID":"30.05.02.16","FunCat.description":"hedgehog-dependent signalling pathway","PubMed.ID":23955340,"subunits.Protein.name.":"Transcriptional activator GLI3;Zinc finger protein DZIP1","subunits.Gene.name.":"GLI3;DZIP1","subunits.Gene.name.syn.":"None;DZIP, DZIP2, KIAA0996","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6525,"ComplexName":"SPG3A-SPG33 complex","Organism":"Human","Synonyms":"ZFYVE27-Atlastin1 complex; SPG33-ATL1 complex","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"Q5T4F4;Q8WXF7","subunits.Entrez.IDs.":"118813;51062","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005783;GO:0016192;GO:0071787;GO:0071788","GO.description":"endoplasmic reticulum;vesicle-mediated transport;endoplasmic reticulum tubular network assembly;endoplasmic reticulum tubular network maintenance","FunCat.ID":"70.07;20.09.07","FunCat.description":"endoplasmic reticulum;vesicular transport (Golgi network, etc.)","PubMed.ID":24668814,"subunits.Protein.name.":"Protrudin;Atlastin-1","subunits.Gene.name.":"ZFYVE27;ATL1","subunits.Gene.name.syn.":"SPG33;GBP3,SPG3A","Disease.comment":"The protrudin gene (ZFYVE27) is mutated in a subset of individuals with hereditary spastic paraplegia (HSP), and protrudin is therefore also referred to as spastic paraplegia 33 (SPG33). It is suggested that protrudin contributes to the regulation of ER morphology and function, and that its deregulation by mutation is a causative defect in HSP.","Subunits.comment":"None","Complex.comment":"Protrudin is an integral membrane protein that regulates polarized vesicular trafficking in neurons. It possesses a hairpin domain and interacts with HSP-related proteins including myelin proteolipid protein 1 (SPG2), atlastin-1 (SPG3A), REEP1 (SPG31), REEP5 (similar to REEP1), Kif5A (SPG10), Kif5B, Kif5C, andreticulon 1, 3, and 4 (similar to reticulon 2, SPG12). Membrane topology analysis indicated that one of three hydrophobic segments of protrudin forms a hydrophobic hairpin domain similar to those of other SPG proteins. Protrudin was found to localize predominantly to the tubular endoplasmic reticulum (ER), and forced expression of protrudin promoted the formation and stabilization of the tubular ER network. Protrudin facilitates the interaction of Kif5 with Rab11, VAP family proteins, Surf4, and reticulon proteins, suggesting that it serves as an adaptor protein and that the protrudin-Kif5 complex contributes to the transport of these proteins in neurons.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6526,"ComplexName":"SPG10-SPG33 complex","Organism":"Human","Synonyms":"ZFYVE27-KIF5A complex; Protrudin-NKHC1 complex","Cell.line":"HEK293T cells; HeLa cells","subunits.UniProt.IDs.":"Q12840;Q5T4F4","subunits.Entrez.IDs.":"3798;118813","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0016192;GO:0071787;GO:0071788;GO:0005783","GO.description":"vesicle-mediated transport;endoplasmic reticulum tubular network assembly;endoplasmic reticulum tubular network maintenance;endoplasmic reticulum","FunCat.ID":"20.09.07;70.07","FunCat.description":"vesicular transport (Golgi network, etc.);endoplasmic reticulum","PubMed.ID":21976701,"subunits.Protein.name.":"Kinesin heavy chain isoform 5A;Protrudin","subunits.Gene.name.":"KIF5A;ZFYVE27","subunits.Gene.name.syn.":"NKHC1, SPG10;SPG33","Disease.comment":"The protrudin gene (ZFYVE27) is mutated in a subset of individuals with hereditary spastic paraplegia (HSP), and protrudin is therefore also referred to as spastic paraplegia 33 (SPG33). It is suggested that protrudin contributes to the regulation of ER morphology and function, and that its deregulation by mutation is a causative defect in HSP (PMID:24668814).","Subunits.comment":"None","Complex.comment":"Protrudin is a membrane protein that regulates polarized vesicular trafficking in neurons (PMID:24668814). It serves as an adaptor molecule that connects KIF5 and its cargoes in vesicular transport during process formation. Protrudin facilitated the interaction of KIF5 with Rab11, VAP-A and -B, Surf4, and RTN3, suggesting that protrudin serves as an adaptor protein and that the protrudin-KIF5 complex contributes to the transport of these proteins in neurons.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6527,"ComplexName":"FLRT3-LPHN3-UNC5B complex","Organism":"Human","Synonyms":"FLRT3-ADGRL3-UNC5B complex","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"Q8IZJ1;Q9HAR2;Q9NZU0","subunits.Entrez.IDs.":"219699;23284;23767","Protein.complex.purification.method":"MI:0054-fluorescence-activated cell sorting","GO.ID":"GO:0098609;GO:0007416;GO:0001764","GO.description":"cell-cell adhesion;synapse assembly;neuron migration","FunCat.ID":"41.05.13.01","FunCat.description":"synaptogenesis","PubMed.ID":26235030,"subunits.Protein.name.":"Netrin receptor UNC5B;Adhesion G protein-coupled receptor L3;Leucine-rich repeat transmembrane protein FLRT3","subunits.Gene.name.":"UNC5B;ADGRL3;FLRT3","subunits.Gene.name.syn.":"P53RDL1 UNC5H2;KIAA0768, LEC3, LPHN3;KIAA1469","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"FLRT3 binds the other two proteins simultaneously and bridges them, although LPHN3 and UNC5 do not directly interact with each other.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6528,"ComplexName":"FLRT3-LPHN3-UNC5D complex","Organism":"Human","Synonyms":"FLRT3-ADGRL3-UNC5D complex","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"Q6UXZ4;Q9HAR2;Q9NZU0","subunits.Entrez.IDs.":"137970;23284;23767","Protein.complex.purification.method":"MI:0054-fluorescence-activated cell sorting","GO.ID":"GO:0098609;GO:0001764;GO:0007416","GO.description":"cell-cell adhesion;neuron migration;synapse assembly","FunCat.ID":"41.05.13.01","FunCat.description":"synaptogenesis","PubMed.ID":26235030,"subunits.Protein.name.":"Netrin receptor UNC5D;Adhesion G protein-coupled receptor L3;Leucine-rich repeat transmembrane protein FLRT3","subunits.Gene.name.":"UNC5D;ADGRL3;FLRT3","subunits.Gene.name.syn.":"KIAA1777,UNC5H4;KIAA0768, LEC3, LPHN3;KIAA1469","Disease.comment":"None","Subunits.comment":"The authors mention mouse Unc5D, but describe the Uniprot entry: Q6UXZ4 (human). So the human protein was used.","Complex.comment":"FLRT3 binds the other two proteins simultaneously and bridges them, although LPHN3 and UNC5 do not directly interact with each other.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6529,"ComplexName":"FLRT3-LPHN3 complex","Organism":"Human","Synonyms":"FLRT3-ADGRL3 complex","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"Q9HAR2;Q9NZU0","subunits.Entrez.IDs.":"23284;23767","Protein.complex.purification.method":"MI:0114-x-ray crystallography","GO.ID":"GO:0007416;GO:0098609","GO.description":"synapse assembly;cell-cell adhesion","FunCat.ID":"41.05.13.01","FunCat.description":"synaptogenesis","PubMed.ID":26235030,"subunits.Protein.name.":"Adhesion G protein-coupled receptor L3;Leucine-rich repeat transmembrane protein FLRT3","subunits.Gene.name.":"ADGRL3;FLRT3","subunits.Gene.name.syn.":"KIAA0768, LEC3, LPHN3;KIAA1469","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6530,"ComplexName":"MYO7A-PDZD7 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"Q13402;Q9H5P4","subunits.Entrez.IDs.":"4647;79955","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation;MI:0096-pull down","GO.ID":"GO:0007605;GO:0060171","GO.description":"sensory perception of sound;stereocilium membrane","FunCat.ID":"36.25.01.03","FunCat.description":"hearing","PubMed.ID":27525485,"subunits.Protein.name.":"Unconventional myosin-VIIa;PDZ domain-containing protein 7","subunits.Gene.name.":"MYO7A;PDZD7","subunits.Gene.name.syn.":"USH1B;PDZK7","Disease.comment":"Mutations in MYO7A affect the development and function of the mechanically sensitive stereocilia of hair cells and are therefore associated with deafness.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6531,"ComplexName":"CEP164-DZIP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"Q86YF9;Q9UPV0","subunits.Entrez.IDs.":"22873;22897","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0042073;GO:0007224","GO.description":"intraciliary transport;smoothened signaling pathway","FunCat.ID":"30.05.02.16","FunCat.description":"hedgehog-dependent signalling pathway","PubMed.ID":23955340,"subunits.Protein.name.":"Zinc finger protein DZIP1;Centrosomal protein of 164 kDa","subunits.Gene.name.":"DZIP1;CEP164","subunits.Gene.name.syn.":"DZIP, DZIP2, KIAA0996;KIAA1052, NPHP15","Disease.comment":"CEP164 is involved in Nephronophthisis 15 (PMID:22863007).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6532,"ComplexName":"TSC2-HERC1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK283 cells","subunits.UniProt.IDs.":"P49815;Q15751","subunits.Entrez.IDs.":"7249;8925","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0031929","GO.description":"TOR signaling","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":16464865,"subunits.Protein.name.":"Tuberin;Probable E3 ubiquitin-protein ligase HERC1","subunits.Gene.name.":"TSC2;HERC1","subunits.Gene.name.syn.":"TSC4;None","Disease.comment":"Mutations in TSC2 are associated with tuberous sclerosis (OMIM:613254).In healthy subjects, interaction of TSC1 with TSC2 excludes TSC2 from interacting with HERC1. Disease mutations in TSC2 allow binding to HERC1 also in the presence of TSC1.","Subunits.comment":"TSC2 pull-down experiments were performed in mouse brain tissue.","Complex.comment":"TSC1 inhibits the interaction of TSC2 and HERC1 ubiquitin ligase by binding to TSC2.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6533,"ComplexName":"DZIP1-IFT88 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"Q13099;Q86YF9","subunits.Entrez.IDs.":"8100;22873","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0035720;GO:0060271;GO:0005814","GO.description":"intraciliary anterograde transport;cilium assembly;centriole","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":22863007,"subunits.Protein.name.":"Intraflagellar transport protein 88 homolog;Zinc finger protein DZIP1","subunits.Gene.name.":"IFT88;DZIP1","subunits.Gene.name.syn.":"TG737 TTC10;DZIP, DZIP2, KIAA0996","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6534,"ComplexName":"SPG31-SPG33 omplex","Organism":"Human","Synonyms":"ZFYVE27-REEP1 complex; Protrudin-REEP1 complex","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"Q5T4F4;Q9H902","subunits.Entrez.IDs.":"118813;65055","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005783;GO:0016192;GO:0071787;GO:0071788","GO.description":"endoplasmic reticulum;vesicle-mediated transport;endoplasmic reticulum tubular network assembly;endoplasmic reticulum tubular network maintenance","FunCat.ID":"70.07;20.09.07","FunCat.description":"endoplasmic reticulum;vesicular transport (Golgi network, etc.)","PubMed.ID":24668814,"subunits.Protein.name.":"Protrudin;Receptor expression-enhancing protein 1","subunits.Gene.name.":"ZFYVE27;REEP1","subunits.Gene.name.syn.":"SPG33;C2orf23,SPG31","Disease.comment":"The protrudin gene (ZFYVE27) is mutated in a subset of individuals with hereditary spastic paraplegia (HSP), and protrudin is therefore also referred to as spastic paraplegia 33 (SPG33). It is suggested that protrudin contributes to the regulation of ER morphology and function, and that its deregulation by mutation is a causative defect in HSP.","Subunits.comment":"None","Complex.comment":"Protrudin is an integral membrane protein that regulates polarized vesicular trafficking in neurons. It possesses a hairpin domain and interacts with HSP-related proteins including myelin proteolipid protein 1 (SPG2), atlastin-1 (SPG3A), REEP1 (SPG31), REEP5 (similar to REEP1), Kif5A (SPG10), Kif5B, Kif5C, andreticulon 1, 3, and 4 (similar to reticulon 2, SPG12). Membrane topology analysis indicated that one of three hydrophobic segments of protrudin forms a hydrophobic hairpin domain similar to those of other SPG proteins. Protrudin was found to localize predominantly to the tubular endoplasmic reticulum (ER), and forced expression of protrudin promoted the formation and stabilization of the tubular ER network. Protrudin facilitates the interaction of Kif5 with Rab11, VAP family proteins, Surf4, and reticulon proteins, suggesting that it serves as an adaptor protein and that the protrudin-Kif5 complex contributes to the transport of these proteins in neurons.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6535,"ComplexName":"Igsf9b-Magi1/2 complex","Organism":"Rat","Synonyms":"None","Cell.line":"brain lysates","subunits.UniProt.IDs.":"D3ZB51;O88382","subunits.Entrez.IDs.":"None;113970","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:1904862","GO.description":"inhibitory synapse assembly","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23751499,"subunits.Protein.name.":"Protein turtle homolog B;Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2","subunits.Gene.name.":"Igsf9b;Magi2","subunits.Gene.name.syn.":"None;Acvrinp1, Aip1, Sscam","Disease.comment":"None","Subunits.comment":"The cross-reactivity of the used anti-S-SCAM (Magi2) antibodies with Magi-1, makes it difficult to differentiate between the Magi proteins.But Magi-1 has been reported to be absent from inhibitory synapses. So Magi2 has been used.","Complex.comment":"In the brain, IgSF9b coprecipitated with MAGI proteins but not with other postsynaptic scaffolds including gephyrin, PSD-95, and Shank.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6536,"ComplexName":"REEP5-SPG33 complex","Organism":"Human","Synonyms":"ZFYVE27-REEP5 complex; Protrudin-REEP5 complex","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"Q00765;Q5T4F4","subunits.Entrez.IDs.":"7905;118813","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005783;GO:0016192;GO:0071788;GO:0071787","GO.description":"endoplasmic reticulum;vesicle-mediated transport;endoplasmic reticulum tubular network maintenance;endoplasmic reticulum tubular network assembly","FunCat.ID":"70.07;20.09.07","FunCat.description":"endoplasmic reticulum;vesicular transport (Golgi network, etc.)","PubMed.ID":24668814,"subunits.Protein.name.":"Receptor expression-enhancing protein 5;Protrudin","subunits.Gene.name.":"REEP5;ZFYVE27","subunits.Gene.name.syn.":"C5orf18,DP1,TB2;SPG33","Disease.comment":"The protrudin gene (ZFYVE27) is mutated in a subset of individuals with hereditary spastic paraplegia (HSP), and protrudin is therefore also referred to as spastic paraplegia 33 (SPG33). It is suggested that protrudin contributes to the regulation of ER morphology and function, and that its deregulation by mutation is a causative defect in HSP.","Subunits.comment":"None","Complex.comment":"Protrudin is an integral membrane protein that regulates polarized vesicular trafficking in neurons. It possesses a hairpin domain and interacts with HSP-related proteins including myelin proteolipid protein 1 (SPG2), atlastin-1 (SPG3A), REEP1 (SPG31), REEP5 (similar to REEP1), Kif5A (SPG10), Kif5B, Kif5C, andreticulon 1, 3, and 4 (similar to reticulon 2, SPG12). Membrane topology analysis indicated that one of three hydrophobic segments of protrudin forms a hydrophobic hairpin domain similar to those of other SPG proteins. Protrudin was found to localize predominantly to the tubular endoplasmic reticulum (ER), and forced expression of protrudin promoted the formation and stabilization of the tubular ER network. Protrudin facilitates the interaction of Kif5 with Rab11, VAP family proteins, Surf4, and reticulon proteins, suggesting that it serves as an adaptor protein and that the protrudin-Kif5 complex contributes to the transport of these proteins in neurons.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6537,"ComplexName":"ANKS3-ANKS6 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"kidney","subunits.UniProt.IDs.":"Q6GQX6;Q9CZK6","subunits.Entrez.IDs.":"75691;72615","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0003097","GO.description":"renal water transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26327442,"subunits.Protein.name.":"Ankyrin repeat and SAM domain-containing protein 6;Ankyrin repeat and SAM domain-containing protein 3","subunits.Gene.name.":"Anks6;Anks3","subunits.Gene.name.syn.":"Gm635,Samd6;Kiaa1977","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6538,"ComplexName":"SPG33-VAPA complex","Organism":"Human","Synonyms":"ZFYVE27-VAPA complex; Protrudin-VAP33 comple","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"Q5T4F4;Q9P0L0","subunits.Entrez.IDs.":"118813;9218","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005783;GO:0016192;GO:0071787;GO:0071788","GO.description":"endoplasmic reticulum;vesicle-mediated transport;endoplasmic reticulum tubular network assembly;endoplasmic reticulum tubular network maintenance","FunCat.ID":"70.07;20.09.07","FunCat.description":"endoplasmic reticulum;vesicular transport (Golgi network, etc.)","PubMed.ID":24668814,"subunits.Protein.name.":"Protrudin;Vesicle-associated membrane protein-associated protein A","subunits.Gene.name.":"ZFYVE27;VAPA","subunits.Gene.name.syn.":"SPG33;VAP33","Disease.comment":"The protrudin gene (ZFYVE27) is mutated in a subset of individuals with hereditary spastic paraplegia (HSP), and protrudin is therefore also referred to as spastic paraplegia 33 (SPG33). It is suggested that protrudin contributes to the regulation of ER morphology and function, and that its deregulation by mutation is a causative defect in HSP.","Subunits.comment":"None","Complex.comment":"Protrudin is an integral membrane protein that regulates polarized vesicular trafficking in neurons. It possesses a hairpin domain and interacts with HSP-related proteins including myelin proteolipid protein 1 (SPG2), atlastin-1 (SPG3A), REEP1 (SPG31), REEP5 (similar to REEP1), Kif5A (SPG10), Kif5B, Kif5C, andreticulon 1, 3, and 4 (similar to reticulon 2, SPG12). Membrane topology analysis indicated that one of three hydrophobic segments of protrudin forms a hydrophobic hairpin domain similar to those of other SPG proteins. Protrudin was found to localize predominantly to the tubular endoplasmic reticulum (ER), and forced expression of protrudin promoted the formation and stabilization of the tubular ER network. Protrudin facilitates the interaction of Kif5 with Rab11, VAP family proteins, Surf4, and reticulon proteins, suggesting that it serves as an adaptor protein and that the protrudin-Kif5 complex contributes to the transport of these proteins in neurons.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6539,"ComplexName":"Spg33-Plp1 complex","Organism":"Mouse","Synonyms":"Zfyve27-PLP1 complex; Protrudin-Spg2 complex","Cell.line":"brain","subunits.UniProt.IDs.":"P60202;Q3TXX3","subunits.Entrez.IDs.":"18823;319740","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005783;GO:0071787;GO:0071788;GO:0016192","GO.description":"endoplasmic reticulum;endoplasmic reticulum tubular network assembly;endoplasmic reticulum tubular network maintenance;vesicle-mediated transport","FunCat.ID":"70.07;20.09.07","FunCat.description":"endoplasmic reticulum;vesicular transport (Golgi network, etc.)","PubMed.ID":24668814,"subunits.Protein.name.":"Myelin proteolipid protein;Protrudin","subunits.Gene.name.":"Plp1;Zfyve27","subunits.Gene.name.syn.":"Plp, Spg2;Spg33","Disease.comment":"The protrudin gene (ZFYVE27) is mutated in a subset of human individuals with hereditary spastic paraplegia (HSP), and protrudin is therefore also referred to as spastic paraplegia 33 (SPG33). It is suggested that protrudin contributes to the regulation of ER morphology and function, and that its deregulation by mutation is a causative defect in HSP.","Subunits.comment":"None","Complex.comment":"Protrudin is an integral membrane protein that regulates polarized vesicular trafficking in neurons. It possesses a hairpin domain and interacts with HSP-related proteins including myelin proteolipid protein 1 (SPG2), atlastin-1 (SPG3A), REEP1 (SPG31), REEP5 (similar to REEP1), Kif5A (SPG10), Kif5B, Kif5C, andreticulon 1, 3, and 4 (similar to reticulon 2, SPG12). Membrane topology analysis indicated that one of three hydrophobic segments of protrudin forms a hydrophobic hairpin domain similar to those of other SPG proteins. Protrudin was found to localize predominantly to the tubular endoplasmic reticulum (ER), and forced expression of protrudin promoted the formation and stabilization of the tubular ER network. Protrudin facilitates the interaction of Kif5 with Rab11, VAP family proteins, Surf4, and reticulon proteins, suggesting that it serves as an adaptor protein and that the protrudin-Kif5 complex contributes to the transport of these proteins in neurons.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6540,"ComplexName":"GPX1-SBP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HCT116 cells","subunits.UniProt.IDs.":"P07203;Q13228","subunits.Entrez.IDs.":"2876;8991","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0045454","GO.description":"cell redox homeostasis","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20530237,"subunits.Protein.name.":"Glutathione peroxidase 1;Selenium-binding protein 1","subunits.Gene.name.":"GPX1;SELENBP1","subunits.Gene.name.syn.":"None;SBP1; hSP56","Disease.comment":"The level of SBP1 is reduced in several cancer types. GPX1 is associated with cancer risk and development.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6541,"ComplexName":"Spg33-Rtn1 complex","Organism":"Mouse","Synonyms":"Zfyve27-Rtn1 complex; Protrudin-(Reticulon-1) complex","Cell.line":"brain","subunits.UniProt.IDs.":"Q3TXX3;Q8K0T0","subunits.Entrez.IDs.":"319740;104001","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0005783;GO:0071787;GO:0071788;GO:0016192","GO.description":"endoplasmic reticulum;endoplasmic reticulum tubular network assembly;endoplasmic reticulum tubular network maintenance;vesicle-mediated transport","FunCat.ID":"70.07;20.09.07","FunCat.description":"endoplasmic reticulum;vesicular transport (Golgi network, etc.)","PubMed.ID":24668814,"subunits.Protein.name.":"Protrudin;Reticulon-1","subunits.Gene.name.":"Zfyve27;Rtn1","subunits.Gene.name.syn.":"Spg33;Nsp","Disease.comment":"The protrudin gene (ZFYVE27) is mutated in a subset of human individuals with hereditary spastic paraplegia (HSP), and protrudin is therefore also referred to as spastic paraplegia 33 (SPG33). It is suggested that protrudin contributes to the regulation of ER morphology and function, and that its deregulation by mutation is a causative defect in HSP.","Subunits.comment":"None","Complex.comment":"Protrudin is an integral membrane protein that regulates polarized vesicular trafficking in neurons. It possesses a hairpin domain and interacts with HSP-related proteins including myelin proteolipid protein 1 (SPG2), atlastin-1 (SPG3A), REEP1 (SPG31), REEP5 (similar to REEP1), Kif5A (SPG10), Kif5B, Kif5C, andreticulon 1, 3, and 4 (similar to reticulon 2, SPG12). Membrane topology analysis indicated that one of three hydrophobic segments of protrudin forms a hydrophobic hairpin domain similar to those of other SPG proteins. Protrudin was found to localize predominantly to the tubular endoplasmic reticulum (ER), and forced expression of protrudin promoted the formation and stabilization of the tubular ER network. Protrudin facilitates the interaction of Kif5 with Rab11, VAP family proteins, Surf4, and reticulon proteins, suggesting that it serves as an adaptor protein and that the protrudin-Kif5 complex contributes to the transport of these proteins in neurons.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6542,"ComplexName":"Spg33-Rtn3 complex","Organism":"Mouse","Synonyms":"Zfyve27-Rtn3 complex; Protrudin-Reticulon3 complex","Cell.line":"brain","subunits.UniProt.IDs.":"Q3TXX3;Q9ES97","subunits.Entrez.IDs.":"319740;20168","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0005783;GO:0071787;GO:0071788;GO:0016192","GO.description":"endoplasmic reticulum;endoplasmic reticulum tubular network assembly;endoplasmic reticulum tubular network maintenance;vesicle-mediated transport","FunCat.ID":"70.07;20.09.07","FunCat.description":"endoplasmic reticulum;vesicular transport (Golgi network, etc.)","PubMed.ID":24668814,"subunits.Protein.name.":"Protrudin;Reticulon-3","subunits.Gene.name.":"Zfyve27;Rtn3","subunits.Gene.name.syn.":"Spg33;None","Disease.comment":"The protrudin gene (ZFYVE27) is mutated in a subset of human individuals with hereditary spastic paraplegia (HSP), and protrudin is therefore also referred to as spastic paraplegia 33 (SPG33). It is suggested that protrudin contributes to the regulation of ER morphology and function, and that its deregulation by mutation is a causative defect in HSP.","Subunits.comment":"None","Complex.comment":"Protrudin is an integral membrane protein that regulates polarized vesicular trafficking in neurons. It possesses a hairpin domain and interacts with HSP-related proteins including myelin proteolipid protein 1 (SPG2), atlastin-1 (SPG3A), REEP1 (SPG31), REEP5 (similar to REEP1), Kif5A (SPG10), Kif5B, Kif5C, andreticulon 1, 3, and 4 (similar to reticulon 2, SPG12). Membrane topology analysis indicated that one of three hydrophobic segments of protrudin forms a hydrophobic hairpin domain similar to those of other SPG proteins. Protrudin was found to localize predominantly to the tubular endoplasmic reticulum (ER), and forced expression of protrudin promoted the formation and stabilization of the tubular ER network. Protrudin facilitates the interaction of Kif5 with Rab11, VAP family proteins, Surf4, and reticulon proteins, suggesting that it serves as an adaptor protein and that the protrudin-Kif5 complex contributes to the transport of these proteins in neurons.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6543,"ComplexName":"Spg33-Rtn4 complex","Organism":"Mouse","Synonyms":"Zfyve27-Rtn4 complex; Protrudin-Reticulon4 complex","Cell.line":"brain","subunits.UniProt.IDs.":"Q3TXX3;Q99P72","subunits.Entrez.IDs.":"319740;68585","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0005783;GO:0071787;GO:0071788;GO:0016192","GO.description":"endoplasmic reticulum;endoplasmic reticulum tubular network assembly;endoplasmic reticulum tubular network maintenance;vesicle-mediated transport","FunCat.ID":"70.07;20.09.07","FunCat.description":"endoplasmic reticulum;vesicular transport (Golgi network, etc.)","PubMed.ID":24668814,"subunits.Protein.name.":"Protrudin;Reticulon-4","subunits.Gene.name.":"Zfyve27;Rtn4","subunits.Gene.name.syn.":"Spg33;Kiaa0886 Nogo","Disease.comment":"The protrudin gene (ZFYVE27) is mutated in a subset of human individuals with hereditary spastic paraplegia (HSP), and protrudin is therefore also referred to as spastic paraplegia 33 (SPG33). It is suggested that protrudin contributes to the regulation of ER morphology and function, and that its deregulation by mutation is a causative defect in HSP.","Subunits.comment":"None","Complex.comment":"Protrudin is an integral membrane protein that regulates polarized vesicular trafficking in neurons. It possesses a hairpin domain and interacts with HSP-related proteins including myelin proteolipid protein 1 (SPG2), atlastin-1 (SPG3A), REEP1 (SPG31), REEP5 (similar to REEP1), Kif5A (SPG10), Kif5B, Kif5C, andreticulon 1, 3, and 4 (similar to reticulon 2, SPG12). Membrane topology analysis indicated that one of three hydrophobic segments of protrudin forms a hydrophobic hairpin domain similar to those of other SPG proteins. Protrudin was found to localize predominantly to the tubular endoplasmic reticulum (ER), and forced expression of protrudin promoted the formation and stabilization of the tubular ER network. Protrudin facilitates the interaction of Kif5 with Rab11, VAP family proteins, Surf4, and reticulon proteins, suggesting that it serves as an adaptor protein and that the protrudin-Kif5 complex contributes to the transport of these proteins in neurons.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6544,"ComplexName":"Spg33-Kif5a complex","Organism":"Mouse","Synonyms":"Zfyve27-Kif5a complex; Protrudin-Spg10 complex","Cell.line":"brain","subunits.UniProt.IDs.":"P33175;Q3TXX3","subunits.Entrez.IDs.":"16572;319740","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0005783;GO:0071787;GO:0071788;GO:0016192","GO.description":"endoplasmic reticulum;endoplasmic reticulum tubular network assembly;endoplasmic reticulum tubular network maintenance;vesicle-mediated transport","FunCat.ID":"70.07;20.09.07","FunCat.description":"endoplasmic reticulum;vesicular transport (Golgi network, etc.)","PubMed.ID":24668814,"subunits.Protein.name.":"Kinesin heavy chain isoform 5A;Protrudin","subunits.Gene.name.":"Kif5a;Zfyve27","subunits.Gene.name.syn.":"Kiaa4086 Kif5 Nkhc1;Spg33","Disease.comment":"The protrudin gene (ZFYVE27) is mutated in a subset of human individuals with hereditary spastic paraplegia (HSP), and protrudin is therefore also referred to as spastic paraplegia 33 (SPG33). It is suggested that protrudin contributes to the regulation of ER morphology and function, and that its deregulation by mutation is a causative defect in HSP.","Subunits.comment":"None","Complex.comment":"Protrudin is an integral membrane protein that regulates polarized vesicular trafficking in neurons. It possesses a hairpin domain and interacts with HSP-related proteins including myelin proteolipid protein 1 (SPG2), atlastin-1 (SPG3A), REEP1 (SPG31), REEP5 (similar to REEP1), Kif5A (SPG10), Kif5B, Kif5C, andreticulon 1, 3, and 4 (similar to reticulon 2, SPG12). Membrane topology analysis indicated that one of three hydrophobic segments of protrudin forms a hydrophobic hairpin domain similar to those of other SPG proteins. Protrudin was found to localize predominantly to the tubular endoplasmic reticulum (ER), and forced expression of protrudin promoted the formation and stabilization of the tubular ER network. Protrudin facilitates the interaction of Kif5 with Rab11, VAP family proteins, Surf4, and reticulon proteins, suggesting that it serves as an adaptor protein and that the protrudin-Kif5 complex contributes to the transport of these proteins in neurons.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6545,"ComplexName":"DCDC2-MAPK8IP1 complex","Organism":"Human","Synonyms":"DCDC2-JIP1 complex","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"Q9UHG0;Q9UQF2","subunits.Entrez.IDs.":"51473;9479","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007254","GO.description":"JNK cascade","FunCat.ID":"30.01.05.01.02","FunCat.description":"JNK cascade","PubMed.ID":25557784,"subunits.Protein.name.":"Doublecortin domain-containing protein 2;C-Jun-amino-terminal kinase-interacting protein 1","subunits.Gene.name.":"DCDC2;MAPK8IP1","subunits.Gene.name.syn.":"KIAA1154, RU2, NPHP19;IB1, JIP1, PRKM8IP","Disease.comment":"DCDC2 is involved in Nephronophthisis 19.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6546,"ComplexName":"Igsf9b-Nlgn2 complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"D3ZB51;Q62888","subunits.Entrez.IDs.":"None;117096","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:1904862","GO.description":"inhibitory synapse assembly","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23751499,"subunits.Protein.name.":"Protein turtle homolog B;Neuroligin-2","subunits.Gene.name.":"Igsf9b;Nlgn2","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"IgSF9b formed a weak complex with neuroligin 2 but not with neuroligin 1, which is consistent with its inhibitory synaptic localization.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6547,"ComplexName":"Spg33-Kif5b complex","Organism":"Mouse","Synonyms":"Zfyve27-Kif5b complex; Protrudin-Kif5b complex","Cell.line":"brain","subunits.UniProt.IDs.":"Q3TXX3;Q61768","subunits.Entrez.IDs.":"319740;16573","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0005783;GO:0071787;GO:0071788;GO:0016192","GO.description":"endoplasmic reticulum;endoplasmic reticulum tubular network assembly;endoplasmic reticulum tubular network maintenance;vesicle-mediated transport","FunCat.ID":"70.07;20.09.07","FunCat.description":"endoplasmic reticulum;vesicular transport (Golgi network, etc.)","PubMed.ID":24668814,"subunits.Protein.name.":"Protrudin;Kinesin-1 heavy chain","subunits.Gene.name.":"Zfyve27;Kif5b","subunits.Gene.name.syn.":"Spg33;Khcs, Kns1","Disease.comment":"The protrudin gene (ZFYVE27) is mutated in a subset of human individuals with hereditary spastic paraplegia (HSP), and protrudin is therefore also referred to as spastic paraplegia 33 (SPG33). It is suggested that protrudin contributes to the regulation of ER morphology and function, and that its deregulation by mutation is a causative defect in HSP.","Subunits.comment":"None","Complex.comment":"Protrudin is an integral membrane protein that regulates polarized vesicular trafficking in neurons. It possesses a hairpin domain and interacts with HSP-related proteins including myelin proteolipid protein 1 (SPG2), atlastin-1 (SPG3A), REEP1 (SPG31), REEP5 (similar to REEP1), Kif5A (SPG10), Kif5B, Kif5C, andreticulon 1, 3, and 4 (similar to reticulon 2, SPG12). Membrane topology analysis indicated that one of three hydrophobic segments of protrudin forms a hydrophobic hairpin domain similar to those of other SPG proteins. Protrudin was found to localize predominantly to the tubular endoplasmic reticulum (ER), and forced expression of protrudin promoted the formation and stabilization of the tubular ER network. Protrudin facilitates the interaction of Kif5 with Rab11, VAP family proteins, Surf4, and reticulon proteins, suggesting that it serves as an adaptor protein and that the protrudin-Kif5 complex contributes to the transport of these proteins in neurons.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6548,"ComplexName":"Spg33-Kif5c complex","Organism":"Mouse","Synonyms":"Zfyve27-Kif5c complex; Protrudin-Nkhc2 complex","Cell.line":"brain","subunits.UniProt.IDs.":"P28738;Q3TXX3","subunits.Entrez.IDs.":"16574;319740","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0005783;GO:0071787;GO:0071788;GO:0016192","GO.description":"endoplasmic reticulum;endoplasmic reticulum tubular network assembly;endoplasmic reticulum tubular network maintenance;vesicle-mediated transport","FunCat.ID":"70.07;20.09.07","FunCat.description":"endoplasmic reticulum;vesicular transport (Golgi network, etc.)","PubMed.ID":24668814,"subunits.Protein.name.":"Kinesin heavy chain isoform 5C;Protrudin","subunits.Gene.name.":"Kif5c;Zfyve27","subunits.Gene.name.syn.":"Nkhc2;Spg33","Disease.comment":"The protrudin gene (ZFYVE27) is mutated in a subset of human individuals with hereditary spastic paraplegia (HSP), and protrudin is therefore also referred to as spastic paraplegia 33 (SPG33). It is suggested that protrudin contributes to the regulation of ER morphology and function, and that its deregulation by mutation is a causative defect in HSP.","Subunits.comment":"None","Complex.comment":"Protrudin is an integral membrane protein that regulates polarized vesicular trafficking in neurons. It possesses a hairpin domain and interacts with HSP-related proteins including myelin proteolipid protein 1 (SPG2), atlastin-1 (SPG3A), REEP1 (SPG31), REEP5 (similar to REEP1), Kif5A (SPG10), Kif5B, Kif5C, andreticulon 1, 3, and 4 (similar to reticulon 2, SPG12). Membrane topology analysis indicated that one of three hydrophobic segments of protrudin forms a hydrophobic hairpin domain similar to those of other SPG proteins. Protrudin was found to localize predominantly to the tubular endoplasmic reticulum (ER), and forced expression of protrudin promoted the formation and stabilization of the tubular ER network. Protrudin facilitates the interaction of Kif5 with Rab11, VAP family proteins, Surf4, and reticulon proteins, suggesting that it serves as an adaptor protein and that the protrudin-Kif5 complex contributes to the transport of these proteins in neurons.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6549,"ComplexName":"SEP15-UGGT1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"prostate","subunits.UniProt.IDs.":"Q923V8;Q9JLA3","subunits.Entrez.IDs.":"113922;171129","Protein.complex.purification.method":"MI:0404-comigration in non denaturing gel electropho;MI:0091-chromatography technologies;MI:0019-coimmunoprecipitation","GO.ID":"GO:0044322;GO:0071218","GO.description":"endoplasmic reticulum quality control compartment;cellular response to misfolded protein","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":11278576,"subunits.Protein.name.":"15 kDa selenoprotein;UDP-glucose:glycoprotein glucosyltransferase 1","subunits.Gene.name.":"Sep15;Uggt1","subunits.Gene.name.syn.":"None;Gt,Ugcgl1,Uggt,Ugt1,Ugtr","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The identical complex has been isolated from mouse liver.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6550,"ComplexName":"CUL4B-DDB1-TLE1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"Q04724;Q13619;Q16531","subunits.Entrez.IDs.":"7088;8451;1642","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0010498","GO.description":"proteasomal protein catabolic process","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":17041588,"subunits.Protein.name.":"Transducin-like enhancer protein 1;Cullin-4A;DNA damage-binding protein 1","subunits.Gene.name.":"TLE1;CUL4A;DDB1","subunits.Gene.name.syn.":"None;None;XAP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6551,"ComplexName":"Igsf9b-Nlgn2-Magi2 complex","Organism":"Rat","Synonyms":"None","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"D3ZB51;O88382;Q62888","subunits.Entrez.IDs.":"None;113970;117096","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:1904862","GO.description":"inhibitory synapse assembly","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23751499,"subunits.Protein.name.":"Protein turtle homolog B;Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2;Neuroligin-2","subunits.Gene.name.":"Igsf9b;Magi2;Nlgn2","subunits.Gene.name.syn.":"None;Acvrinp1, Aip1, Sscam;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Magi2 (Sscam) bridges Igsf9b and neuroligin 2. The formation of the ternary complex containing Igsf9b, Sscam, and neuroligin 2 can be driven  bidirectionally, initiating from neuroligin 2 or Igsf9b.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6552,"ComplexName":"KIF5B-SPG33 complex","Organism":"Human","Synonyms":"ZFYVE27-KIF5B complex; Protrudin-KNS1 complex","Cell.line":"HEK293T cells; HeLa cells","subunits.UniProt.IDs.":"P33176;Q5T4F4","subunits.Entrez.IDs.":"3799;118813","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005783;GO:0071787;GO:0071788;GO:0016192","GO.description":"endoplasmic reticulum;endoplasmic reticulum tubular network assembly;endoplasmic reticulum tubular network maintenance;vesicle-mediated transport","FunCat.ID":"70.07;20.09.07","FunCat.description":"endoplasmic reticulum;vesicular transport (Golgi network, etc.)","PubMed.ID":21976701,"subunits.Protein.name.":"Kinesin-1 heavy chain;Protrudin","subunits.Gene.name.":"KIF5B;ZFYVE27","subunits.Gene.name.syn.":"KNS, KNS1;SPG33","Disease.comment":"The protrudin gene (ZFYVE27) is mutated in a subset of individuals with hereditary spastic paraplegia (HSP), and protrudin is therefore also referred to as spastic paraplegia 33 (SPG33). It is suggested that protrudin contributes to the regulation of ER morphology and function, and that its deregulation by mutation is a causative defect in HSP (PMID:24668814).","Subunits.comment":"None","Complex.comment":"Protrudin is a membrane protein that regulates polarized vesicular trafficking in neurons (PMID:24668814). It serves as an adaptor molecule that connects KIF5 and its cargoes in vesicular transport during process formation. Protrudin facilitated the interaction of KIF5 with Rab11, VAP-A and -B, Surf4, and RTN3, suggesting that protrudin serves as an adaptor protein and that the protrudin-KIF5 complex contributes to the transport of these proteins in neurons.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6553,"ComplexName":"CUL4B-DDB1-TLE3 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"Q04726;Q13620;Q16531","subunits.Entrez.IDs.":"7090;8450;1642","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0010498","GO.description":"proteasomal protein catabolic process","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":17041588,"subunits.Protein.name.":"Transducin-like enhancer protein 3;Cullin-4B;DNA damage-binding protein 1","subunits.Gene.name.":"TLE3;CUL4B;DDB1","subunits.Gene.name.syn.":"KIAA1547;KIAA0695;XAP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6554,"ComplexName":"KIF5C-SPG33 complex","Organism":"Human","Synonyms":"ZFYVE27-KIF5C complex; Protrudin-NKHC2 complex","Cell.line":"HEK293T cells; HeLa cells","subunits.UniProt.IDs.":"O60282;Q5T4F4","subunits.Entrez.IDs.":"3800;118813","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005783;GO:0071787;GO:0071788;GO:0016192","GO.description":"endoplasmic reticulum;endoplasmic reticulum tubular network assembly;endoplasmic reticulum tubular network maintenance;vesicle-mediated transport","FunCat.ID":"70.07;20.09.07","FunCat.description":"endoplasmic reticulum;vesicular transport (Golgi network, etc.)","PubMed.ID":21976701,"subunits.Protein.name.":"Kinesin heavy chain isoform 5C;Protrudin","subunits.Gene.name.":"KIF5C;ZFYVE27","subunits.Gene.name.syn.":"KIAA0531,NKHC2;SPG33","Disease.comment":"The protrudin gene (ZFYVE27) is mutated in a subset of individuals with hereditary spastic paraplegia (HSP), and protrudin is therefore also referred to as spastic paraplegia 33 (SPG33). It is suggested that protrudin contributes to the regulation of ER morphology and function, and that its deregulation by mutation is a causative defect in HSP (PMID:24668814).","Subunits.comment":"None","Complex.comment":"Protrudin is a membrane protein that regulates polarized vesicular trafficking in neurons (PMID:24668814). It serves as an adaptor molecule that connects KIF5 and its cargoes in vesicular transport during process formation. Protrudin facilitated the interaction of KIF5 with Rab11, VAP-A and -B, Surf4, and RTN3, suggesting that protrudin serves as an adaptor protein and that the protrudin-KIF5 complex contributes to the transport of these proteins in neurons.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6555,"ComplexName":"Dcdc2-Dvl1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"NIH 3T3 cells","subunits.UniProt.IDs.":"P51141;Q5DU00","subunits.Entrez.IDs.":"13542;195208","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0016055","GO.description":"Wnt signaling pathway","FunCat.ID":"30.05.02.20","FunCat.description":"Wnt signalling pathway","PubMed.ID":25557784,"subunits.Protein.name.":"Segment polarity protein dishevelled homolog DVL-1;Doublecortin domain-containing protein 2","subunits.Gene.name.":"Dvl1;Dcdc2","subunits.Gene.name.syn.":"Dvl;Dcdc2a, Kiaa1154","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6556,"ComplexName":"Dcdc2-Dvl2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"NIH 3T3 cells","subunits.UniProt.IDs.":"Q5DU00;Q60838","subunits.Entrez.IDs.":"195208;13543","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0016055","GO.description":"Wnt signaling pathway","FunCat.ID":"30.05.02.20","FunCat.description":"Wnt signalling pathway","PubMed.ID":25557784,"subunits.Protein.name.":"Doublecortin domain-containing protein 2;Segment polarity protein dishevelled homolog DVL-2","subunits.Gene.name.":"Dcdc2;Dvl2","subunits.Gene.name.syn.":"Dcdc2a, Kiaa1154;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6557,"ComplexName":"Dcdc2-Dvl3 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"NIH 3T3 cells","subunits.UniProt.IDs.":"Q5DU00;Q61062","subunits.Entrez.IDs.":"195208;13544","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0016055","GO.description":"Wnt signaling pathway","FunCat.ID":"30.05.02.20","FunCat.description":"Wnt signalling pathway","PubMed.ID":25557784,"subunits.Protein.name.":"Doublecortin domain-containing protein 2;Segment polarity protein dishevelled homolog DVL-3","subunits.Gene.name.":"Dcdc2;Dvl3","subunits.Gene.name.syn.":"Dcdc2a, Kiaa1154;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6558,"ComplexName":"Dcdc2-Kif3a complex","Organism":"Rat","Synonyms":"None","Cell.line":"primary hippocampal neurons","subunits.UniProt.IDs.":"D3ZR10;Q9WV62","subunits.Entrez.IDs.":"291130;84392","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005929","GO.description":"cilium","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":21698230,"subunits.Protein.name.":"Doublecortin domain-containing protein 2;Kinesin-like protein KIF3A","subunits.Gene.name.":"Dcdc2;Kif3a","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6559,"ComplexName":"RAB11B-SPG10-SPG33 complex","Organism":"Human","Synonyms":"ZFYVE27-KIF5A-RAB11B complex; Protrudin-NKHC1-YPT3 complex","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"Q12840;Q15907;Q5T4F4","subunits.Entrez.IDs.":"3798;9230;118813","Protein.complex.purification.method":"MI:0051-fluorescence technologies;MI:0428-imaging techniques","GO.ID":"GO:0005783;GO:0071787;GO:0071788;GO:0016192","GO.description":"endoplasmic reticulum;endoplasmic reticulum tubular network assembly;endoplasmic reticulum tubular network maintenance;vesicle-mediated transport","FunCat.ID":"70.07;20.09.07","FunCat.description":"endoplasmic reticulum;vesicular transport (Golgi network, etc.)","PubMed.ID":21976701,"subunits.Protein.name.":"Kinesin heavy chain isoform 5A;Ras-related protein Rab-11B;Protrudin","subunits.Gene.name.":"KIF5A;RAB11B;ZFYVE27","subunits.Gene.name.syn.":"NKHC1, SPG10;YPT3;SPG33","Disease.comment":"The protrudin gene (ZFYVE27) is mutated in a subset of individuals with hereditary spastic paraplegia (HSP), and protrudin is therefore also referred to as spastic paraplegia 33 (SPG33). It is suggested that protrudin contributes to the regulation of ER morphology and function, and that its deregulation by mutation is a causative defect in HSP (PMID:24668814).Mutations of protrudin or KIF5 are a cause of human hereditary spastic paraplegia (HSP).","Subunits.comment":"None","Complex.comment":"Protrudin is a membrane protein that regulates polarized vesicular trafficking in neurons (PMID:24668814). It serves as an adaptor molecule that connects KIF5 and its cargoes in vesicular transport during process formation. Protrudin facilitated the interaction of KIF5 with Rab11, VAP-A and -B, Surf4, and RTN3, suggesting that protrudin serves as an adaptor protein and that the protrudin-KIF5 complex contributes to the transport of these proteins in neurons.Protrudin, KIF5, and Rab11b form a membrane-associated complex, consistent with the fact that protrudin has two putative transmembrane domains.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6560,"ComplexName":"PHB-ANX2-CD36 complex","Organism":"Mouse","Synonyms":"Adipocytes","Cell.line":"Adypocytes","subunits.UniProt.IDs.":"P07356;P67778;Q08857","subunits.Entrez.IDs.":"12306;18673;12491","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0015908","GO.description":"fatty acid transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":27468426,"subunits.Protein.name.":"Annexin A2;Prohibitin;Platelet glycoprotein 4","subunits.Gene.name.":"Anxa2;Phb;Cd36","subunits.Gene.name.syn.":"Anx2, Cal1h;Bap32;FAT, GPIV, Scarb3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6561,"ComplexName":"RAB11A-SPG33 complex","Organism":"Human","Synonyms":"ZFYVE27-RAB11A complex; Protrudin-RAB11 complex","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"P62491;Q5T4F4","subunits.Entrez.IDs.":"8766;118813","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005783;GO:0016192","GO.description":"endoplasmic reticulum;vesicle-mediated transport","FunCat.ID":"70.07;20.09.07","FunCat.description":"endoplasmic reticulum;vesicular transport (Golgi network, etc.)","PubMed.ID":21976701,"subunits.Protein.name.":"Ras-related protein Rab-11A;Protrudin","subunits.Gene.name.":"RAB11A;ZFYVE27","subunits.Gene.name.syn.":"RAB11;SPG33","Disease.comment":"The protrudin gene (ZFYVE27) is mutated in a subset of individuals with hereditary spastic paraplegia (HSP), and protrudin is therefore also referred to as spastic paraplegia 33 (SPG33). It is suggested that protrudin contributes to the regulation of ER morphology and function, and that its deregulation by mutation is a causative defect in HSP (PMID:24668814).","Subunits.comment":"None","Complex.comment":"Protrudin is a membrane protein that regulates polarized vesicular trafficking in neurons (PMID:24668814). It serves as an adaptor molecule that connects KIF5 and its cargoes in vesicular transport during process formation. Protrudin facilitated the interaction of KIF5 with Rab11, VAP-A and -B, Surf4, and RTN3, suggesting that protrudin serves as an adaptor protein and that the protrudin-KIF5 complex contributes to the transport of these proteins in neurons.  Coimmunoprecipitation experiments in HeLa revealed that protrudin also associated with GDP-Rab11a and GDP-Rab11b to similar extents.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6562,"ComplexName":"RAB11B-SPG33 complex","Organism":"Human","Synonyms":"ZFYVE27-RAB11B complex; Protrudin-YPT3 complex","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"Q15907;Q5T4F4","subunits.Entrez.IDs.":"9230;118813","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005783;GO:0016192","GO.description":"endoplasmic reticulum;vesicle-mediated transport","FunCat.ID":"70.07;20.09.07","FunCat.description":"endoplasmic reticulum;vesicular transport (Golgi network, etc.)","PubMed.ID":21976701,"subunits.Protein.name.":"Ras-related protein Rab-11B;Protrudin","subunits.Gene.name.":"RAB11B;ZFYVE27","subunits.Gene.name.syn.":"YPT3;SPG33","Disease.comment":"The protrudin gene (ZFYVE27) is mutated in a subset of individuals with hereditary spastic paraplegia (HSP), and protrudin is therefore also referred to as spastic paraplegia 33 (SPG33). It is suggested that protrudin contributes to the regulation of ER morphology and function, and that its deregulation by mutation is a causative defect in HSP (PMID:24668814).","Subunits.comment":"None","Complex.comment":"Protrudin is a membrane protein that regulates polarized vesicular trafficking in neurons (PMID:24668814). It serves as an adaptor molecule that connects KIF5 and its cargoes in vesicular transport during process formation. Protrudin facilitated the interaction of KIF5 with Rab11, VAP-A and -B, Surf4, and RTN3, suggesting that protrudin serves as an adaptor protein and that the protrudin-KIF5 complex contributes to the transport of these proteins in neurons. Coimmunoprecipitation experiments in HeLa revealed that protrudin also associated with GDP-Rab11a and GDP-Rab11b to similar extents.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6563,"ComplexName":"SPG33-SURF4 complex","Organism":"Human","Synonyms":"ZFYVE27-SURF4 complex; Protrudin-SURF4 complex","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O15260;Q5T4F4","subunits.Entrez.IDs.":"6836;118813","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005783;GO:0016192","GO.description":"endoplasmic reticulum;vesicle-mediated transport","FunCat.ID":"70.07;20.09.07","FunCat.description":"endoplasmic reticulum;vesicular transport (Golgi network, etc.)","PubMed.ID":21976701,"subunits.Protein.name.":"Surfeit locus protein 4;Protrudin","subunits.Gene.name.":"SURF4;ZFYVE27","subunits.Gene.name.syn.":"None;SPG33","Disease.comment":"The protrudin gene (ZFYVE27) is mutated in a subset of individuals with hereditary spastic paraplegia (HSP), and protrudin is therefore also referred to as spastic paraplegia 33 (SPG33). It is suggested that protrudin contributes to the regulation of ER morphology and function, and that its deregulation by mutation is a causative defect in HSP (PMID:24668814).","Subunits.comment":"None","Complex.comment":"Protrudin is a membrane protein that regulates polarized vesicular trafficking in neurons (PMID:24668814). It serves as an adaptor molecule that connects KIF5 and its cargoes in vesicular transport during process formation. Protrudin facilitated the interaction of KIF5 with Rab11, VAP-A and -B, Surf4, and RTN3, suggesting that protrudin serves as an adaptor protein and that the protrudin-KIF5 complex contributes to the transport of these proteins in neurons. The binding of Surf4 and protrudin was also confirmed in a coimmunoprecipitation assay.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6564,"ComplexName":"Nek8-Pkd2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"kidney","subunits.UniProt.IDs.":"O35245;Q91ZR4","subunits.Entrez.IDs.":"18764;140859","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0060271;GO:0005929","GO.description":"cilium assembly;cilium","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":18235101,"subunits.Protein.name.":"Polycystin-2;Serine/threonine-protein kinase Nek8","subunits.Gene.name.":"Pkd2;Nek8","subunits.Gene.name.syn.":"TRPP2;Jck, Nphp9","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6565,"ComplexName":"RTN3-SPG33 complex","Organism":"Human","Synonyms":"ZFYVE27- RTN3 complex; Protrudin-NSPL2 complex","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O95197;Q5T4F4","subunits.Entrez.IDs.":"10313;118813","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0096-pull down","GO.ID":"GO:0005783;GO:0016192","GO.description":"endoplasmic reticulum;vesicle-mediated transport","FunCat.ID":"70.07;20.09.07","FunCat.description":"endoplasmic reticulum;vesicular transport (Golgi network, etc.)","PubMed.ID":21976701,"subunits.Protein.name.":"Reticulon-3;Protrudin","subunits.Gene.name.":"RTN3;ZFYVE27","subunits.Gene.name.syn.":"ASYIP, NSPL2;SPG33","Disease.comment":"The protrudin gene (ZFYVE27) is mutated in a subset of individuals with hereditary spastic paraplegia (HSP), and protrudin is therefore also referred to as spastic paraplegia 33 (SPG33). It is suggested that protrudin contributes to the regulation of ER morphology and function, and that its deregulation by mutation is a causative defect in HSP (PMID:24668814).","Subunits.comment":"None","Complex.comment":"Protrudin is a membrane protein that regulates polarized vesicular trafficking in neurons (PMID:24668814). It serves as an adaptor molecule that connects KIF5 and its cargoes in vesicular transport during process formation. Protrudin facilitated the interaction of KIF5 with Rab11, VAP-A and -B, Surf4, and RTN3, suggesting that protrudin serves as an adaptor protein and that the protrudin-KIF5 complex contributes to the transport of these proteins in neurons.Coimmunoprecipitation experiments also revealed that protrudin interacted directly with RTN3 and promoted the binding of the latter to KIF5A.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6566,"ComplexName":"SPG33-VAPB complex","Organism":"Human","Synonyms":"ZFYVE27-VAPB complex; Protrudin-VAPB complex","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O95292;Q5T4F4","subunits.Entrez.IDs.":"9217;118813","Protein.complex.purification.method":"MI:0096-pull down","GO.ID":"GO:0005783;GO:0016192","GO.description":"endoplasmic reticulum;vesicle-mediated transport","FunCat.ID":"70.07;20.09.07","FunCat.description":"endoplasmic reticulum;vesicular transport (Golgi network, etc.)","PubMed.ID":21976701,"subunits.Protein.name.":"Vesicle-associated membrane protein-associated protein B/C;Protrudin","subunits.Gene.name.":"VAPB;ZFYVE27","subunits.Gene.name.syn.":"None;SPG33","Disease.comment":"The protrudin gene (ZFYVE27) is mutated in a subset of individuals with hereditary spastic paraplegia (HSP), and protrudin is therefore also referred to as spastic paraplegia 33 (SPG33). It is suggested that protrudin contributes to the regulation of ER morphology and function, and that its deregulation by mutation is a causative defect in HSP (PMID:24668814).","Subunits.comment":"None","Complex.comment":"Protrudin is a membrane protein that regulates polarized vesicular trafficking in neurons (PMID:24668814). It serves as an adaptor molecule that connects KIF5 and its cargoes in vesicular transport during process formation. Protrudin facilitated the interaction of KIF5 with Rab11, VAP-A and -B, Surf4, and RTN3, suggesting that protrudin serves as an adaptor protein and that the protrudin-KIF5 complex contributes to the transport of these proteins in neurons. A pulldown assay revealed also the direct interaction of protrudin with VAP-B.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6567,"ComplexName":"SWELL1-containing complex","Organism":"Human","Synonyms":"LRRC8A-containing complex","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"Q6NSJ5;Q6P9F7;Q7L1W4;Q8IWT6;Q8TDW0","subunits.Entrez.IDs.":"80131;23507;55144;56262;84230","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies;MI:0019-coimmunoprecipitation","GO.ID":"GO:0005225;GO:0006884","GO.description":"volume-sensitive anion channel activity;cell volume homeostasis","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26824658,"subunits.Protein.name.":"Volume-regulated anion channel subunit LRRC8E;Volume-regulated anion channel subunit LRRC8B;Volume-regulated anion channel subunit LRRC8D;Volume-regulated anion channel subunit LRRC8A;Volume-regulated anion channel subunit LRRC8C","subunits.Gene.name.":"LRRC8E;LRRC8B;LRRC8D;LRRC8A;LRRC8C","subunits.Gene.name.syn.":"None;KIAA0231;LRRC5;KIAA1437,LRRC8,SWELL1;AD158,FAD158","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"For full channel activity LRRC8A plus at least one other family member (LRRC8B, LRRC8C, LRRC8D or LRRC8E) is necessary. LRRC8C-E subunits associated with SWELL1 (LRRC8A) contribute to ion selectivity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6568,"ComplexName":"3M core complex","Organism":"Human","Synonyms":"CUL7-CCDC8-OBSL1 complex","Cell.line":"293T cells","subunits.UniProt.IDs.":"O75147;Q14999;Q9H0W5","subunits.Entrez.IDs.":"23363;9820;83987","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0000226;GO:0005813;GO:0005737","GO.description":"microtubule cytoskeleton organization;centrosome;cytoplasm","FunCat.ID":"42.04.05;70.05;70.03","FunCat.description":"microtubule cytoskeleton;centrosome;cytoplasm","PubMed.ID":24793695,"subunits.Protein.name.":"Obscurin-like protein 1;Cullin-7;Coiled-coil domain-containing protein 8","subunits.Gene.name.":"OBSL1;CUL7;CCDC8","subunits.Gene.name.syn.":"KIAA0657;KIAA0076;None","Disease.comment":"Besides CUL7, two additional genes, OBSL1 and CCDC8, have been foundto be mutated in 3M syndrome. These three genes are mutated in a mutually exclusive manner, with CUL7 being the most frequently mutated (~65%), followed by OBSL1 (~30%) and CCDC8 (~5%).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6569,"ComplexName":"SPG4-SPG33 complex","Organism":"Human","Synonyms":"ZFYVE27-Spastin complex; Protrudin-SPAST complex","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"Q5T4F4;Q9UBP0","subunits.Entrez.IDs.":"118813;6683","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0051-fluorescence technologies","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":16826525,"subunits.Protein.name.":"Protrudin;Spastin","subunits.Gene.name.":"ZFYVE27;SPAST","subunits.Gene.name.syn.":"SPG33;ADPSP,FSP2,KIAA1083,SPG4","Disease.comment":"Mutated protrudin (SPG33) shows an aberrant intracellular pattern in its tubular structure. Its interaction with spastin (SPG4) is severely affected. It is postulated that this specific mutation in protrudin affects neuronal intracellular trafficking in the corticospinal tract, which is consistent with the pathology of Hereditary Spastic Paraplegia (HSP (PMID:16826525).","Subunits.comment":"None","Complex.comment":"ZFYVE27, a novel member of the FYVE-finger family of proteins, is a specific spastin-binding protein.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6570,"ComplexName":"Anks3-Bicc1 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"Q99MQ1;Q9CZK6","subunits.Entrez.IDs.":"83675;72615","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0001822;GO:0005929","GO.description":"kidney development;cilium","FunCat.ID":"47.03.07.01","FunCat.description":"kidney","PubMed.ID":25671767,"subunits.Protein.name.":"Protein bicaudal C homolog 1;Ankyrin repeat and SAM domain-containing protein 3","subunits.Gene.name.":"Bicc1;Anks3","subunits.Gene.name.syn.":"None;Kiaa1977","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6571,"ComplexName":"KCNE1-KCNH2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P15382;Q12809","subunits.Entrez.IDs.":"3753;3757","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0086008","GO.description":"voltage-gated potassium channel activity involved in cardiac muscle cell action potential repolarization","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":9230439,"subunits.Protein.name.":"Potassium voltage-gated channel subfamily E member 1;Potassium voltage-gated channel subfamily H member 2","subunits.Gene.name.":"KCNE1;KCNH2","subunits.Gene.name.syn.":"None;ERG, ERG1, HERG","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6572,"ComplexName":"Anks3-Anks6 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"P0C0T2;Q9CZK6","subunits.Entrez.IDs.":"362515;72615","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0001822;GO:0005929","GO.description":"kidney development;cilium","FunCat.ID":"47.03.07.01","FunCat.description":"kidney","PubMed.ID":25671767,"subunits.Protein.name.":"Ankyrin repeat and SAM domain-containing protein 6;Ankyrin repeat and SAM domain-containing protein 3","subunits.Gene.name.":"Anks6;Anks3","subunits.Gene.name.syn.":"Pkdr1, Samd6;Kiaa1977","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Mus musculus (Mouse)"}
{"ComplexID":6573,"ComplexName":"Anks6-Bicc1 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"P0C0T2;Q99MQ1","subunits.Entrez.IDs.":"362515;83675","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0001822;GO:0005929","GO.description":"kidney development;cilium","FunCat.ID":"47.03.07.01","FunCat.description":"kidney","PubMed.ID":25671767,"subunits.Protein.name.":"Ankyrin repeat and SAM domain-containing protein 6;Protein bicaudal C homolog 1","subunits.Gene.name.":"Anks6;Bicc1","subunits.Gene.name.syn.":"Pkdr1, Samd6;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Mus musculus (Mouse)"}
{"ComplexID":6574,"ComplexName":"Anks3-NPHP1 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"O15259;Q9CZK6","subunits.Entrez.IDs.":"4867;72615","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0001822;GO:0005929","GO.description":"kidney development;cilium","FunCat.ID":"47.03.07.01","FunCat.description":"kidney","PubMed.ID":25671767,"subunits.Protein.name.":"Nephrocystin-1;Ankyrin repeat and SAM domain-containing protein 3","subunits.Gene.name.":"NPHP1;Anks3","subunits.Gene.name.syn.":"NPH1;Kiaa1977","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Mus musculus (Mouse)"}
{"ComplexID":6575,"ComplexName":"Anks3-Nek8 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"Q91ZR4;Q9CZK6","subunits.Entrez.IDs.":"140859;72615","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0001822;GO:0005929","GO.description":"kidney development;cilium","FunCat.ID":"47.03.07.01","FunCat.description":"kidney","PubMed.ID":25671767,"subunits.Protein.name.":"Serine/threonine-protein kinase Nek8;Ankyrin repeat and SAM domain-containing protein 3","subunits.Gene.name.":"Nek8;Anks3","subunits.Gene.name.syn.":"Jck, Nphp9;Kiaa1977","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6576,"ComplexName":"Anks3-Hif1an complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"Q8BLR9;Q9CZK6","subunits.Entrez.IDs.":"319594;72615","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0001822;GO:0005929","GO.description":"kidney development;cilium","FunCat.ID":"47.03.07.01","FunCat.description":"kidney","PubMed.ID":25671767,"subunits.Protein.name.":"Hypoxia-inducible factor 1-alpha inhibitor;Ankyrin repeat and SAM domain-containing protein 3","subunits.Gene.name.":"Hif1an;Anks3","subunits.Gene.name.syn.":"None;Kiaa1977","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6577,"ComplexName":"3M complex","Organism":"Human","Synonyms":"CUL7-CCDC8-OBSL1-CUL9-p53-ROC1-FBXW8 complex","Cell.line":"293T cells","subunits.UniProt.IDs.":"O75147;P04637;P62877;Q14999;Q8IWT3;Q8N3Y1;Q9H0W5","subunits.Entrez.IDs.":"23363;7157;9978;9820;23113;26259;83987","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0071-molecular sieving","GO.ID":"GO:0000226","GO.description":"microtubule cytoskeleton organization","FunCat.ID":"42.04.05","FunCat.description":"microtubule cytoskeleton","PubMed.ID":24793695,"subunits.Protein.name.":"Obscurin-like protein 1;Cellular tumor antigen p53;E3 ubiquitin-protein ligase RBX1;Cullin-7;Cullin-9;F-box/WD repeat-containing protein 8;Coiled-coil domain-containing protein 8","subunits.Gene.name.":"OBSL1;TP53;RBX1;CUL7;CUL9;FBXW8;CCDC8","subunits.Gene.name.syn.":"KIAA0657;P53;RNF75, ROC1;KIAA0076;H7AP1,KIAA0708,PARC;FBW6 FBW8 FBX29 FBXO29 FBXW6;None","Disease.comment":"Besides CUL7, two additional genes, OBSL1 and CCDC8, have been foundto be mutated in 3M syndrome. These three genes are mutated in a mutually exclusive manner, with CUL7 being the most frequently mutated (~65%), followed by OBSL1 (~30%) and CCDC8 (~5%).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6578,"ComplexName":"KCNE2-KCNH2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q9Y6J6","subunits.Entrez.IDs.":"9992","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0086008","GO.description":"voltage-gated potassium channel activity involved in cardiac muscle cell action potential repolarization","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":10219239,"subunits.Protein.name.":"Potassium voltage-gated channel subfamily E member 2","subunits.Gene.name.":"KCNE2","subunits.Gene.name.syn.":"ATFB4, LQT5, LQT6, MIRP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":6579,"ComplexName":"USF1-USF2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P22415;Q15853","subunits.Entrez.IDs.":"7391;7392","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006357;GO:0000981","GO.description":"regulation of transcription from RNA polymerase II promoter;RNA polymerase II transcription factor activity, sequence-specific DNA binding","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":14573800,"subunits.Protein.name.":"Upstream stimulatory factor 1;Upstream stimulatory factor 2","subunits.Gene.name.":"USF1;USF2","subunits.Gene.name.syn.":"BHLHB11 USF;BHLHB12","Disease.comment":"Varicella-zoster virus infection.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6580,"ComplexName":"Pggt1b-Fnta complex","Organism":"Rat","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P53610;Q04631","subunits.Entrez.IDs.":"81746;25318","Protein.complex.purification.method":"MI:0114-x-ray crystallography","GO.ID":"GO:0048814","GO.description":"regulation of dendrite morphogenesis","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":15451670,"subunits.Protein.name.":"Geranylgeranyl transferase type-1 subunit beta;Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha","subunits.Gene.name.":"Pggt1b;Fnta","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6581,"ComplexName":"LRRC8A-LRRC8C complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"Q8IWT6;Q8TDW0","subunits.Entrez.IDs.":"56262;84230","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006884;GO:0005225","GO.description":"cell volume homeostasis;volume-sensitive anion channel activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26824658,"subunits.Protein.name.":"Volume-regulated anion channel subunit LRRC8A;Volume-regulated anion channel subunit LRRC8C","subunits.Gene.name.":"LRRC8A;LRRC8C","subunits.Gene.name.syn.":"KIAA1437,LRRC8,SWELL1;AD158,FAD158","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"For full channel activity LRRC8A plus at least one other family member (LRRC8B, LRRC8C, LRRC8D or LRRC8E) is necessary. LRRC8C-E subunits associated with SWELL1 (LRRC8A) contribute to ion selectivity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6582,"ComplexName":"LRRC8A-LRRC8D complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"Q7L1W4;Q8IWT6","subunits.Entrez.IDs.":"55144;56262","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006884;GO:0005225","GO.description":"cell volume homeostasis;volume-sensitive anion channel activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26824658,"subunits.Protein.name.":"Volume-regulated anion channel subunit LRRC8D;Volume-regulated anion channel subunit LRRC8A","subunits.Gene.name.":"LRRC8D;LRRC8A","subunits.Gene.name.syn.":"LRRC5;KIAA1437,LRRC8,SWELL1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"For full channel activity LRRC8A plus at least one other family member (LRRC8B, LRRC8C, LRRC8D or LRRC8E) is necessary. LRRC8C-E subunits associated with SWELL1 (LRRC8A) contribute to ion selectivity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6583,"ComplexName":"LRRC8A-LRRC8E complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"Q6NSJ5;Q8IWT6","subunits.Entrez.IDs.":"80131;56262","Protein.complex.purification.method":"None","GO.ID":"GO:0006884;GO:0005225","GO.description":"cell volume homeostasis;volume-sensitive anion channel activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26824658,"subunits.Protein.name.":"Volume-regulated anion channel subunit LRRC8E;Volume-regulated anion channel subunit LRRC8A","subunits.Gene.name.":"LRRC8E;LRRC8A","subunits.Gene.name.syn.":"None;KIAA1437,LRRC8,SWELL1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"For full channel activity LRRC8A plus at least one other family member (LRRC8B, LRRC8C, LRRC8D or LRRC8E) is necessary. LRRC8C-E subunits associated with SWELL1 (LRRC8A) contribute to ion selectivity.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6584,"ComplexName":"CHRNA9-CHRNA10 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q9GZZ6;Q9UGM1","subunits.Entrez.IDs.":"57053;55584","Protein.complex.purification.method":"MI:0045-experimental","GO.ID":"GO:0022848;GO:0010996","GO.description":"acetylcholine-gated cation channel activity;response to auditory stimulus","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":11752216,"subunits.Protein.name.":"Neuronal acetylcholine receptor subunit alpha-10;Neuronal acetylcholine receptor subunit alpha-9","subunits.Gene.name.":"CHRNA10;CHRNA9","subunits.Gene.name.syn.":"NACHRA10;NACHRA9","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6585,"ComplexName":"Intraflagellar transport complex A","Organism":"Human","Synonyms":"IFT-A complex","Cell.line":"telomerase immortalized hTERT RPE-1 cells","subunits.UniProt.IDs.":"Q7Z4L5;Q8NEZ3;Q96RY7;Q9HBG6;Q9P2L0","subunits.Entrez.IDs.":"79809;57728;9742;55764;57539","Protein.complex.purification.method":"MI:0676-tandem affinity purification","GO.ID":"GO:0005929;GO:0035721;GO:0007224","GO.description":"cilium;intraciliary retrograde transport;smoothened signaling pathway","FunCat.ID":"30.05.02.16","FunCat.description":"hedgehog-dependent signalling pathway","PubMed.ID":20889716,"subunits.Protein.name.":"Tetratricopeptide repeat protein 21B;WD repeat-containing protein 19;Intraflagellar transport protein 140 homolog;Intraflagellar transport protein 122 homolog;WD repeat-containing protein 35","subunits.Gene.name.":"TTC21B;WDR19;IFT140;IFT122;WDR35","subunits.Gene.name.syn.":"IFT139, KIAA1992, Nbla10696, THM1;IFT144, KIAA1638, NPHP13;KIAA0590, WDTC2;SPG, WDR10, WDR140;IFT121, KIAA1336","Disease.comment":"WDR19 is involved in Nephronophthisis 13 (PMID:22819833). WDR19 is involved in Senior-Loken syndrome 8 (PMID:23683095). IFT140 is involved in Short-rib thoracic dysplasia 9 with or without polydactyly (PMID:23418020). IFT122 is involved in Cranioectodermal dysplasia 1 (PMID:20493458). TTC21B is involved in Nephronophthisis 12 (PMID:25635582). WDR35 is involved in Cranioectodermal dysplasia 2 (PMID:20817137). WDR35 is involved in Short-rib thoracic dysplasia 7 with or without polydactyly (PMID:21473986).","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6586,"ComplexName":"VEcad-VEGFR complex","Organism":"Human","Synonyms":"None","Cell.line":"HUVEC cells","subunits.UniProt.IDs.":"P33151;P35916;P35968","subunits.Entrez.IDs.":"1003;2324;3791","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:1900746;GO:0097704","GO.description":"regulation of vascular endothelial growth factor signaling pathway;cellular response to oscillatory fluid shear stress","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25800053,"subunits.Protein.name.":"Cadherin-5;Vascular endothelial growth factor receptor 3;Vascular endothelial growth factor receptor 2","subunits.Gene.name.":"CDH5;FLT4;KDR","subunits.Gene.name.syn.":"None;VEGFR3;FLK1, VEGFR2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6587,"ComplexName":"CAP-cbl-flotilin complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293T complex","subunits.UniProt.IDs.":"O75955;P22681;Q9BX66","subunits.Entrez.IDs.":"10211;867;10580","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0046324","GO.description":"regulation of glucose import","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":11001060,"subunits.Protein.name.":"Flotillin-1;E3 ubiquitin-protein ligase CBL;Sorbin and SH3 domain-containing protein 1","subunits.Gene.name.":"FLOT1;CBL;SORBS1","subunits.Gene.name.syn.":"None;CBL2, RNF55;KIAA0894, KIAA1296, SH3D5, CAP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6588,"ComplexName":"E2F-1-DP-1 complex","Organism":"Human","Synonyms":"E2F1-TFDP1 complex","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"Q01094;Q14186","subunits.Entrez.IDs.":"1869;7027","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":7969176,"subunits.Protein.name.":"Transcription factor E2F1;Transcription factor Dp-1","subunits.Gene.name.":"E2F1;TFDP1","subunits.Gene.name.syn.":"RBBP3;DP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6589,"ComplexName":"E2F-1-DP-1-cyclinA-CDK2 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P24941;P78396;Q01094;Q14186","subunits.Entrez.IDs.":"1017;8900;1869;7027","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0003677;GO:0006355","GO.description":"DNA binding;regulation of transcription, DNA-templated","FunCat.ID":"16.03.01;11.02.03.04","FunCat.description":"DNA binding;transcriptional control","PubMed.ID":7969176,"subunits.Protein.name.":"Cyclin-dependent kinase 2;Cyclin-A1;Transcription factor E2F1;Transcription factor Dp-1","subunits.Gene.name.":"CDK2;CCNA1;E2F1;TFDP1","subunits.Gene.name.syn.":"CDKN2;None;RBBP3;DP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6590,"ComplexName":"FOXO3-CBP complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O43524;Q92793","subunits.Entrez.IDs.":"2309;1387","Protein.complex.purification.method":"MI:0077-nuclear magnetic resonance","GO.ID":"GO:0003713","GO.description":"transcription coactivator activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":22474372,"subunits.Protein.name.":"Forkhead box protein O3;CREB-binding protein","subunits.Gene.name.":"FOXO3;CREBBP","subunits.Gene.name.syn.":"FKHRL1, FOXO3A;CBP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6591,"ComplexName":"Hsp90-p23 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P07900;Q15185","subunits.Entrez.IDs.":"3320;10728","Protein.complex.purification.method":"MI:0069-mass spectrometry studies of complexes;MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":16403413,"subunits.Protein.name.":"Heat shock protein HSP 90-alpha;Prostaglandin E synthase 3","subunits.Gene.name.":"HSP90AA1;PTGES3","subunits.Gene.name.syn.":"HSP90A HSPC1 HSPCA;P23 TEBP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6592,"ComplexName":"c-Abl-CAS-Abi1 complex","Organism":"Human","Synonyms":"None","Cell.line":"Airway smooth muscle cells","subunits.UniProt.IDs.":"P00519;P56945;Q8IZP0","subunits.Entrez.IDs.":"25;9564;10006","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006940","GO.description":"regulation of smooth muscle contraction","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23740246,"subunits.Protein.name.":"Tyrosine-protein kinase ABL1;Breast cancer anti-estrogen resistance protein 1;Abl interactor 1","subunits.Gene.name.":"ABL1;BCAR1;ABI1","subunits.Gene.name.syn.":"ABL, JTK7;CAS CASS1 CRKAS;SSH3BP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6593,"ComplexName":"Kinesin II complex (Kif3a-Kif3b-Kifap3)","Organism":"Mouse","Synonyms":"Kif3a-Kif3b-Kap3 complex","Cell.line":"testis","subunits.UniProt.IDs.":"P28741;P70188;Q61771","subunits.Entrez.IDs.":"16568;16579;16569","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0035720;GO:0005929","GO.description":"intraciliary anterograde transport;cilium","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":8710890,"subunits.Protein.name.":"Kinesin-like protein KIF3A;Kinesin-associated protein 3;Kinesin-like protein KIF3B","subunits.Gene.name.":"Kif3a;Kifap3;Kif3b","subunits.Gene.name.syn.":"Kif3;Kap3;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6594,"ComplexName":"CCP110-CEP290 complex","Organism":"Human","Synonyms":"None","Cell.line":"Human 293T cells","subunits.UniProt.IDs.":"O15078;O43303","subunits.Entrez.IDs.":"80184;9738","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0060271","GO.description":"cilium assembly","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":18694559,"subunits.Protein.name.":"Centrosomal protein of 290 kDa;Centriolar coiled-coil protein of 110 kDa","subunits.Gene.name.":"CEP290;CCP110","subunits.Gene.name.syn.":"BBS14, KIAA0373, NPHP6;CEP110, CP110, KIAA0419","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6595,"ComplexName":"Ccp110-Cep290-Rab8a complex","Organism":"Mouse","Synonyms":"None","Cell.line":"Mouse 3T3 cells","subunits.UniProt.IDs.":"P55258;Q6A078;Q7TSH4","subunits.Entrez.IDs.":"17274;216274;101565","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0060271","GO.description":"cilium assembly","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":18694559,"subunits.Protein.name.":"Ras-related protein Rab-8A;Centrosomal protein of 290 kDa;Centriolar coiled-coil protein of 110 kDa","subunits.Gene.name.":"Rab8a;Cep290;Ccp110","subunits.Gene.name.syn.":"Mel, Rab8;Kiaa0373, Nphp6;Cep110, Cp110, Kiaa0419","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6596,"ComplexName":"Tectonic complex","Organism":"Mouse","Synonyms":"None","Cell.line":"NIH-3T3 cells","subunits.UniProt.IDs.":"Q2MV57;Q5SW45;Q6A078;Q8BR76;Q8BZ64;Q8CFW7;Q8R2Q6;Q9CQC4;Q9R1S0","subunits.Entrez.IDs.":"67978;380718;216274;329795;654470;231214;67590;68642;27078","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0676-tandem affinity purification","GO.ID":"GO:0060271;GO:0035869","GO.description":"cilium assembly;ciliary transition zone","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":21725307,"subunits.Protein.name.":"Tectonic-2;Meckel syndrome type 1 protein homolog;Centrosomal protein of 290 kDa;Meckelin;Tectonic-1;Coiled-coil and C2 domain-containing protein 2A;Tectonic-3;Transmembrane protein 216;B9 domain-containing protein 1","subunits.Gene.name.":"Tctn2;Mks1;Cep290;Tmem67;Tctn1;Cc2d2a;Tctn3;Tmem216;B9d1","subunits.Gene.name.syn.":"Tect2;None;Kiaa0373, Nphp6;Mks3;Tect1;None;Tect3;None;Eppb9","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6597,"ComplexName":"CEP290-IQCB1 complex","Organism":"Human","Synonyms":"CEP290-NPHP5 complex","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"O15078;Q15051","subunits.Entrez.IDs.":"80184;9657","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0060271;GO:0005813","GO.description":"cilium assembly;centrosome","FunCat.ID":"70.05","FunCat.description":"centrosome","PubMed.ID":23446637,"subunits.Protein.name.":"Centrosomal protein of 290 kDa;IQ calmodulin-binding motif-containing protein 1","subunits.Gene.name.":"CEP290;IQCB1","subunits.Gene.name.syn.":"BBS14, KIAA0373, NPHP6;KIAA0036, NPHP5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6598,"ComplexName":"CC2D2A-CEP290 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O15078;Q9P2K1","subunits.Entrez.IDs.":"80184;57545","Protein.complex.purification.method":"MI:0018-two hybrid;MI:0096-pull down","GO.ID":"GO:0036064","GO.description":"ciliary basal body","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":18950740,"subunits.Protein.name.":"Centrosomal protein of 290 kDa;Coiled-coil and C2 domain-containing protein 2A","subunits.Gene.name.":"CEP290;CC2D2A","subunits.Gene.name.syn.":"BBS14, KIAA0373, NPHP6;KIAA1345","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6599,"ComplexName":"CTNND1-GLIS2 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"O60716;Q9BZE0","subunits.Entrez.IDs.":"1500;84662","Protein.complex.purification.method":"MI:0018-two hybrid;MI:0096-pull down;MI:0019-coimmunoprecipitation","GO.ID":"GO:0005634","GO.description":"nucleus","FunCat.ID":"70.1","FunCat.description":"nucleus","PubMed.ID":17344476,"subunits.Protein.name.":"Catenin delta-1;Zinc finger protein GLIS2","subunits.Gene.name.":"CTNND1;GLIS2","subunits.Gene.name.syn.":"KIAA0384;NKL, NPHP7","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6600,"ComplexName":"NPHP1-PKD1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"O15259;P98161","subunits.Entrez.IDs.":"4867;5310","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006915","GO.description":"apoptotic process","FunCat.ID":"40.10.02","FunCat.description":"apoptosis (type I programmed cell death)","PubMed.ID":20856870,"subunits.Protein.name.":"Nephrocystin-1;Polycystin-1","subunits.Gene.name.":"NPHP1;PKD1","subunits.Gene.name.syn.":"NPH1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6601,"ComplexName":"BBS1-BBS4-BBS5-PKD1-TTC8 complex","Organism":"Human","Synonyms":"BBS1-BBS4-BBS5-PKD1-BBS8 complex","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"P98161;Q8N3I7;Q8NFJ9;Q8TAM2;Q96RK4","subunits.Entrez.IDs.":"5310;129880;582;123016;585","Protein.complex.purification.method":"MI:0018-two hybrid;MI:0096-pull down;MI:0019-coimmunoprecipitation","GO.ID":"GO:0005929;GO:0042073","GO.description":"cilium;intraciliary transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":24939912,"subunits.Protein.name.":"Polycystin-1;Bardet-Biedl syndrome 5 protein;Bardet-Biedl syndrome 1 protein;Tetratricopeptide repeat protein 8;Bardet-Biedl syndrome 4 protein","subunits.Gene.name.":"PKD1;BBS5;BBS1;TTC8;BBS4","subunits.Gene.name.syn.":"None;None;BBS2L2;BBS8;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6602,"ComplexName":"AP5-SPG11-SPG15 complex","Organism":"Human","Synonyms":"AP5Z1-AP5B1- AP5M1-AP5S1-SPG11-SPG15 complex","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O43299;Q2VPB7;Q68DK2;Q96JI7;Q9H0R1;Q9NUS5","subunits.Entrez.IDs.":"9907;91056;23503;80208;55745;55317","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005768;GO:0005764;GO:0044599;GO:0005794;GO:0006886;GO:0006605;GO:0030133","GO.description":"endosome;lysosome;AP-5 adaptor complex;Golgi apparatus;intracellular protein transport;protein targeting;transport vesicle","FunCat.ID":"70.22;70.25;70.08;14.04;70.09","FunCat.description":"endosome;vacuole or lysosome;Golgi;protein targeting, sorting and translocation;intracellular transport vesicles","PubMed.ID":23825025,"subunits.Protein.name.":"AP-5 complex subunit zeta-1;AP-5 complex subunit beta-1;Zinc finger FYVE domain-containing protein 26;Spatacsin;AP-5 complex subunit mu-1;AP-5 complex subunit sigma-1","subunits.Gene.name.":"AP5Z1;AP5B1;ZFYVE26;SPG11;AP5M1;AP5S1","subunits.Gene.name.syn.":"KIAA0415,SPG48;PP1030;KIAA0321, SPG15;KIAA1840;C14orf108,MUDENG;C20orf29","Disease.comment":"SPG11 (ALS5) and SPG15 (ZFYVE26) are mutated in patients with hereditary spastic paraplegia (HSP).","Subunits.comment":"The four AP-5 subunits can be coimmunoprecipitated with SPG11 andSPG15, both from cytosol and from detergent-extracted membranes, with a stoichiometry of ?1:1:1:1:1:1.","Complex.comment":"AP-5 complex (constisting of  AP5Z1, AP5B1, AP5M1, and AP5S1) is a recently identified but evolutionarily ancient member oft he family of heterotetrameric adaptor proteins (AP complexes). It is associated with the two proteins SPG11 and SPG15. AP-5, SPG11, and SPG15 colocalize on a late endosomal/lysosomal compartment.  Both SPG11 and SPG15 have predicted secondary structures containing alpha-solenoids related to those of clathrin heavy chain and COPI subunits. SPG11 also has an N-terminal, beta-propeller\\u2013like domain, which interacts in vitro with AP-5. It is proposed that AP-5, SPG15, and SPG11 form a coat-like complex, with AP-5 involved in protein sorting, SPG15 facilitating the docking of the coat onto membranes by interacting with PI3P via its FYVE domain, and SPG11 (possibly together with SPG15) forming a scaffold.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6603,"ComplexName":"ANKRA2-CCDC8-OBSL1-CUL7 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"O75147;Q14999;Q9H0W5;Q9H9E1","subunits.Entrez.IDs.":"23363;9820;83987;57763","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25752541,"subunits.Protein.name.":"Obscurin-like protein 1;Cullin-7;Coiled-coil domain-containing protein 8;Ankyrin repeat family A protein 2","subunits.Gene.name.":"OBSL1;CUL7;CCDC8;ANKRA2","subunits.Gene.name.syn.":"KIAA0657;KIAA0076;None;ANKRA","Disease.comment":"The CCDC8, CUL7, and OBSL1 genes are mutated in patients with 3M syndrome. The unexpected identification of CCDC8 as a major partner of ANKRA2 suggests an important role of ANKRA2 in 3M syndrome.","Subunits.comment":"ANKRA2 inhibits CUL7 interaction with HDAC4/5.","Complex.comment":"These results indicate that OBSL1 serves as a scaffold to bridge interaction ofCUL7 with CCDC8, which in turn associates with ANKRA2.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6604,"ComplexName":"Gli3-Kif7 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"NIH 3T3 cells","subunits.UniProt.IDs.":"B7ZNG0;Q61602","subunits.Entrez.IDs.":"None;14634","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007224","GO.description":"smoothened signaling pathway","FunCat.ID":"30.05.02.16","FunCat.description":"hedgehog-dependent signalling pathway","PubMed.ID":19592253,"subunits.Protein.name.":"Kinesin-like protein KIF7;Transcriptional activator GLI3","subunits.Gene.name.":"Kif7;Gli3","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6605,"ComplexName":"Gli1-Kif7 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"NIH 3T3 cells","subunits.UniProt.IDs.":"B7ZNG0;P47806","subunits.Entrez.IDs.":"None;14632","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007224","GO.description":"smoothened signaling pathway","FunCat.ID":"30.05.02.16","FunCat.description":"hedgehog-dependent signalling pathway","PubMed.ID":19592253,"subunits.Protein.name.":"Kinesin-like protein KIF7;Zinc finger protein GLI1","subunits.Gene.name.":"Kif7;Gli1","subunits.Gene.name.syn.":"None;Gli","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6606,"ComplexName":"Gli2-Kif7 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"NIH 3T3 cells","subunits.UniProt.IDs.":"B7ZNG0;Q0VGT2","subunits.Entrez.IDs.":"None;14633","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007224","GO.description":"smoothened signaling pathway","FunCat.ID":"30.05.02.16","FunCat.description":"hedgehog-dependent signalling pathway","PubMed.ID":19592253,"subunits.Protein.name.":"Kinesin-like protein KIF7;Zinc finger protein GLI2","subunits.Gene.name.":"Kif7;Gli2","subunits.Gene.name.syn.":"None;Thp","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6607,"ComplexName":"Kif7-Sufu homolog","Organism":"Mouse","Synonyms":"None","Cell.line":"NIH 3T3 cells","subunits.UniProt.IDs.":"B7ZNG0;Q9Z0P7","subunits.Entrez.IDs.":"None;24069","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007224","GO.description":"smoothened signaling pathway","FunCat.ID":"30.05.02.16","FunCat.description":"hedgehog-dependent signalling pathway","PubMed.ID":19592253,"subunits.Protein.name.":"Kinesin-like protein KIF7;Suppressor of fused homolog","subunits.Gene.name.":"Kif7;Sufu","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6608,"ComplexName":"OBSL1-CUL7 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"293T cells","subunits.UniProt.IDs.":"O75147;Q14999","subunits.Entrez.IDs.":"23363;9820","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005794;GO:0007030;GO:0048813","GO.description":"Golgi apparatus;Golgi organization;dendrite morphogenesis","FunCat.ID":"70.08;42.08","FunCat.description":"Golgi;Golgi","PubMed.ID":21572988,"subunits.Protein.name.":"Obscurin-like protein 1;Cullin-7","subunits.Gene.name.":"OBSL1;CUL7","subunits.Gene.name.syn.":"KIAA0657;KIAA0076","Disease.comment":"None","Subunits.comment":"All subunits are annotated as human proteins.","Complex.comment":"OBSL1 forms a physical complex with the scaffold protein Cul7, and thereby localizes Cul7 at the Golgi apparatus in neurons and promotes Golgi and dendrite morphogenesis.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6609,"ComplexName":"ATL2-SPG33 complex","Organism":"Human","Synonyms":"Protrudin-Atlastin2 complex; ZFYVE27-ARL6IP2 complex","Cell.line":"HeLa cells; HEK293T cells","subunits.UniProt.IDs.":"Q5T4F4;Q8NHH9","subunits.Entrez.IDs.":"118813;64225","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005783;GO:0071787;GO:0071788;GO:0016192","GO.description":"endoplasmic reticulum;endoplasmic reticulum tubular network assembly;endoplasmic reticulum tubular network maintenance;vesicle-mediated transport","FunCat.ID":"70.07;20.09.07","FunCat.description":"endoplasmic reticulum;vesicular transport (Golgi network, etc.)","PubMed.ID":23969831,"subunits.Protein.name.":"Protrudin;Atlastin-2","subunits.Gene.name.":"ZFYVE27;ATL2","subunits.Gene.name.syn.":"SPG33;ARL6IP2","Disease.comment":"The protrudin gene (ZFYVE27) is mutated in a subset of individuals with hereditary spastic paraplegia (HSP), and protrudin is therefore also referred to as spastic paraplegia 33 (SPG33). It is suggested that protrudin contributes to the regulation of ER morphology and function, and that its deregulation by mutation is a causative defect in HSP (PMID:24668814).","Subunits.comment":"None","Complex.comment":"Protrudin binds all three human atlastins (atlastin-1, atlastin-2, and atlastin-3) and endoplasmic reticulum-shaping proteins and regulates network formation. The interaction with atlastins required protrudin residues 1-205.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6610,"ComplexName":"Fbxw8-Grasp65 complex","Organism":"Rat","Synonyms":"Fbxw8-Gorasp1 complex","Cell.line":"cortical neurons","subunits.UniProt.IDs.":"O35254;P0DL28","subunits.Entrez.IDs.":"56082;None","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0048813;GO:0007030;GO:0005794","GO.description":"dendrite morphogenesis;Golgi organization;Golgi apparatus","FunCat.ID":"42.08;70.08","FunCat.description":"Golgi;Golgi","PubMed.ID":21572988,"subunits.Protein.name.":"Golgi reassembly-stacking protein 1;F-box/WD repeat-containing protein 8","subunits.Gene.name.":"Gorasp1;Fbxw8","subunits.Gene.name.syn.":"Grasp65;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors identified the Golgi protein Grasp65 as a novel and physiologically relevant substrate of Cul7(Fbxw8) in organizing the normal organelle structure of the Golgi complex and for the elaboration of dendrites in neurons.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6611,"ComplexName":"PDZD11-nectin1 complex","Organism":"Human","Synonyms":"PDZD11-NECTIN1 complex","Cell.line":"Colon carcinoma cells","subunits.UniProt.IDs.":"Q15223;Q5EBL8","subunits.Entrez.IDs.":"5818;51248","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0055074","GO.description":"calcium ion homeostasis","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":27044745,"subunits.Protein.name.":"Nectin-1;PDZ domain-containing protein 11","subunits.Gene.name.":"NECTIN1;PDZD11","subunits.Gene.name.syn.":"HVEC,PRR1,PVRL1;AIPP1 PDZK11 PISP","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6612,"ComplexName":"PDZD11-nectin3 complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"Q5EBL8;Q9NQS3","subunits.Entrez.IDs.":"51248;25945","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0055074","GO.description":"calcium ion homeostasis","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":27044745,"subunits.Protein.name.":"PDZ domain-containing protein 11;Nectin-3","subunits.Gene.name.":"PDZD11;NECTIN3","subunits.Gene.name.syn.":"AIPP1 PDZK11 PISP;PRR3,PVRL3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6613,"ComplexName":"ATL3-SPG33 complex","Organism":"Human","Synonyms":"Protrudin-Atlastin3 complex; ZFYVE27-HSN1F complex","Cell.line":"HeLa cells; HEK293T cells","subunits.UniProt.IDs.":"Q5T4F4;Q6DD88","subunits.Entrez.IDs.":"118813;25923","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005783;GO:0071787;GO:0071788;GO:0016192","GO.description":"endoplasmic reticulum;endoplasmic reticulum tubular network assembly;endoplasmic reticulum tubular network maintenance;vesicle-mediated transport","FunCat.ID":"70.07;20.09.07","FunCat.description":"endoplasmic reticulum;vesicular transport (Golgi network, etc.)","PubMed.ID":23969831,"subunits.Protein.name.":"Protrudin;Atlastin-3","subunits.Gene.name.":"ZFYVE27;ATL3","subunits.Gene.name.syn.":"SPG33;None","Disease.comment":"The protrudin gene (ZFYVE27) is mutated in a subset of individuals with hereditary spastic paraplegia (HSP), and protrudin is therefore also referred to as spastic paraplegia 33 (SPG33). It is suggested that protrudin contributes to the regulation of ER morphology and function, and that its deregulation by mutation is a causative defect in HSP (PMID:24668814).","Subunits.comment":"None","Complex.comment":"Protrudin binds all three human atlastins (atlastin-1, atlastin-2, and atlastin-3) and endoplasmic reticulum-shaping proteins and regulates network formation. The interaction with atlastins required protrudin residues 1-205.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6614,"ComplexName":"GAP-43-Galphai complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"B2RSH2;P06837","subunits.Entrez.IDs.":"14677;14432","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0051302","GO.description":"regulation of cell division","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26380950,"subunits.Protein.name.":"Guanine nucleotide-binding protein G(i) subunit alpha-1;Neuromodulin","subunits.Gene.name.":"Gnai1;Gap43","subunits.Gene.name.syn.":"None;Basp2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6615,"ComplexName":"SPG4-SPG12 complex","Organism":"Human","Synonyms":"RNT2-SPAST complex","Cell.line":"HeLa cells;","subunits.UniProt.IDs.":"O75298;Q9UBP0","subunits.Entrez.IDs.":"6253;6683","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":22232211,"subunits.Protein.name.":"Reticulon-2;Spastin","subunits.Gene.name.":"RTN2;SPAST","subunits.Gene.name.syn.":"NSPL1, SPG12;ADPSP,FSP2,KIAA1083,SPG4","Disease.comment":"Mutations in the ER-shaping protein reticulon 2 cause the axon-degenerative disorder hereditary spastic paraplegia type 12 (SPG12).","Subunits.comment":"None","Complex.comment":"It is shown that the RTN2 protein interacts with spastin and that this interaction requires sequences of the spastin protein that contain the predicted hairpin membrane domain.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6616,"ComplexName":"CADM1-4.1B-MPP3 complex","Organism":"Human","Synonyms":"CADM1-EPB41L3-MPP3 complex","Cell.line":"None","subunits.UniProt.IDs.":"Q13368;Q9BY67;Q9Y2J2","subunits.Entrez.IDs.":"4356;23705;23136","Protein.complex.purification.method":"MI:0051-fluorescence technologies","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25780926,"subunits.Protein.name.":"MAGUK p55 subfamily member 3;Cell adhesion molecule 1;Band 4.1-like protein 3","subunits.Gene.name.":"MPP3;CADM1;EPB41L3","subunits.Gene.name.syn.":"DLG3;IGSF4,IGSF4A,NECL2,SYNCAM,TSLC1;DAL1 KIAA0987","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6617,"ComplexName":"NF2-WWC1 complex","Organism":"Human","Synonyms":"KIBRA-Merlin complex","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"P35240;Q8IX03","subunits.Entrez.IDs.":"4771;23286","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0035329","GO.description":"hippo signaling","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20159599,"subunits.Protein.name.":"Merlin;Protein KIBRA","subunits.Gene.name.":"NF2;WWC1","subunits.Gene.name.syn.":"SCH;KIAA0869","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6618,"ComplexName":"RhBG-kAE1-ankyrin-G complex","Organism":"Human","Synonyms":"None","Cell.line":"Kidney epithelial cells","subunits.UniProt.IDs.":"P02730;Q12955;Q9H310","subunits.Entrez.IDs.":"6521;288;57127","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25616663,"subunits.Protein.name.":"Band 3 anion transport protein;Ankyrin-3;Ammonium transporter Rh type B","subunits.Gene.name.":"SLC4A1;ANK3;RHBG","subunits.Gene.name.syn.":"AE1,DI,EPB3;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6619,"ComplexName":"MGAT1-NGT complex","Organism":"Human","Synonyms":"MGAT1-SLC35A3 complex","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"P26572;Q9Y2D2","subunits.Entrez.IDs.":"4245;23443","Protein.complex.purification.method":"MI:0055-fluorescent resonance energy transfer;MI:0053-fluorescence polarization spectroscopy","GO.ID":"GO:0015788;GO:0000139","GO.description":"UDP-N-acetylglucosamine transport;Golgi membrane","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25944901,"subunits.Protein.name.":"Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase;UDP-N-acetylglucosamine transporter","subunits.Gene.name.":"MGAT1;SLC35A3","subunits.Gene.name.syn.":"GGNT1, GLCT1, GLYT1, MGAT;NGT, AMRS","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6620,"ComplexName":"MGAT1-SLC35A2(splice variant 2) complex","Organism":"Human","Synonyms":"Mgat1-UGT1 complex","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"P26572;P78381-2","subunits.Entrez.IDs.":"4245;7355","Protein.complex.purification.method":"MI:0053-fluorescence polarization spectroscopy;MI:0055-fluorescent resonance energy transfer","GO.ID":"GO:0015785;GO:0000139","GO.description":"UDP-galactose transport;Golgi membrane","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25944901,"subunits.Protein.name.":"Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase;UDP-galactose translocator","subunits.Gene.name.":"MGAT1;SLC35A2","subunits.Gene.name.syn.":"GGNT1, GLCT1, GLYT1, MGAT;UGT1, UGALT, UGT, UGTL","Disease.comment":"None","Subunits.comment":"One of the subunits of this complex is a splice variant 2 of SLC35A2 protein.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6621,"ComplexName":"NEK2A-SAV1-STK3 complex","Organism":"Human","Synonyms":"NEK2A-SAV1-MST2 complex","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"P51955-1;Q13188;Q9H4B6","subunits.Entrez.IDs.":"4751;6788;60485","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0018-two hybrid","GO.ID":"GO:0051297;GO:0051225","GO.description":"centrosome organization;spindle assembly","FunCat.ID":"42.05;10.03.05.01","FunCat.description":"centrosome;spindle pole body/centrosome and microtubule cycle","PubMed.ID":21076410,"subunits.Protein.name.":"Serine/threonine-protein kinase Nek2;Serine/threonine-protein kinase 3;Protein salvador homolog 1","subunits.Gene.name.":"NEK2;STK3;SAV1","subunits.Gene.name.syn.":"NEK2A, NLK1;KRS1, MST2;WW45","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6622,"ComplexName":"MGAT2-SLC35A3 complex","Organism":"Human","Synonyms":"MGAT2-NGT complex","Cell.line":"HEK293T","subunits.UniProt.IDs.":"Q10469;Q9Y2D2","subunits.Entrez.IDs.":"4247;23443","Protein.complex.purification.method":"MI:0053-fluorescence polarization spectroscopy;MI:0055-fluorescent resonance energy transfer","GO.ID":"GO:0015788;GO:0000139","GO.description":"UDP-N-acetylglucosamine transport;Golgi membrane","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25944901,"subunits.Protein.name.":"Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase;UDP-N-acetylglucosamine transporter","subunits.Gene.name.":"MGAT2;SLC35A3","subunits.Gene.name.syn.":"None;NGT, AMRS","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6623,"ComplexName":"MGAT2-SLC35A2(splice variant 2) complex","Organism":"Human","Synonyms":"MGAT2-UGT1 complex","Cell.line":"None","subunits.UniProt.IDs.":"P78381-;Q10469","subunits.Entrez.IDs.":"7355;4247","Protein.complex.purification.method":"MI:0053-fluorescence polarization spectroscopy;MI:0055-fluorescent resonance energy transfer","GO.ID":"GO:0015785;GO:0000139","GO.description":"UDP-galactose transport;Golgi membrane","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25944901,"subunits.Protein.name.":"UDP-galactose translocator;Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase","subunits.Gene.name.":"SLC35A2;MGAT2","subunits.Gene.name.syn.":"UGALT, UGT1, UGTL;None","Disease.comment":"None","Subunits.comment":"One of the subunits of this complex is a splice variant 2 of SLC35A2 protein.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6624,"ComplexName":"MGAT4B-SLC35A3 complex","Organism":"Human","Synonyms":"MGAT4B-NGT complex","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"Q9UQ53;Q9Y2D2","subunits.Entrez.IDs.":"11282;23443","Protein.complex.purification.method":"MI:0053-fluorescence polarization spectroscopy;MI:0055-fluorescent resonance energy transfer","GO.ID":"GO:0015788;GO:0000139","GO.description":"UDP-N-acetylglucosamine transport;Golgi membrane","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25944901,"subunits.Protein.name.":"Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B;UDP-N-acetylglucosamine transporter","subunits.Gene.name.":"MGAT4B;SLC35A3","subunits.Gene.name.syn.":"GNT-IV, GNT-IVB;NGT, AMRS","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6625,"ComplexName":"MGAT4B-SLC35A2(splice variant 1) complex","Organism":"Human","Synonyms":"MGAT4B-UGT2 complex","Cell.line":"HEK93T cells","subunits.UniProt.IDs.":"P78381-1;Q9UQ53","subunits.Entrez.IDs.":"7355;11282","Protein.complex.purification.method":"MI:0053-fluorescence polarization spectroscopy;MI:0055-fluorescent resonance energy transfer","GO.ID":"GO:0015785;GO:0000139","GO.description":"UDP-galactose transport;Golgi membrane","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25944901,"subunits.Protein.name.":"UDP-galactose translocator;Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B","subunits.Gene.name.":"SLC35A2;MGAT4B","subunits.Gene.name.syn.":"UGALT, UGT2, UGTL;GNT-IV, GNT-IVB","Disease.comment":"None","Subunits.comment":"One of the subunits in this complex is a splice varient 1 of SLC35A2 protein.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6626,"ComplexName":"AP5 adaptor complex","Organism":"Human","Synonyms":"AP-5 adaptor complex","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O43299;Q2VPB7;Q9H0R1;Q9NUS5","subunits.Entrez.IDs.":"9907;91056;55745;55317","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0044599;GO:0005768;GO:0005764;GO:0005794;GO:0006886;GO:0030133;GO:0006605;GO:0015031","GO.description":"AP-5 adaptor complex;endosome;lysosome;Golgi apparatus;intracellular protein transport;transport vesicle;protein targeting;protein transport","FunCat.ID":"70.22;70.25;70.08;14.04;70.09;20.01.10","FunCat.description":"endosome;vacuole or lysosome;Golgi;protein targeting, sorting and translocation;intracellular transport vesicles;protein transport","PubMed.ID":22022230,"subunits.Protein.name.":"AP-5 complex subunit zeta-1;AP-5 complex subunit beta-1;AP-5 complex subunit mu-1;AP-5 complex subunit sigma-1","subunits.Gene.name.":"AP5Z1;AP5B1;AP5M1;AP5S1","subunits.Gene.name.syn.":"KIAA0415,SPG48;PP1030;C14orf108,MUDENG;C20orf29","Disease.comment":"Mutations in AP5Z1,a gene playing a role in intracellular membrane trafficking, have been reported to be associated with spastic paraplegia type 48 (SPG48) (PMID:25333062).","Subunits.comment":"None","Complex.comment":"Adaptor protein (AP) complexes (AP1-5) facilitate the trafficking of cargo from one membrane compartment of the cell to another by recruiting other proteins to particular types of vesicles. All of the AP complexes are involved in post-Golgi trafficking pathways. AP-5 is an evolutionarily ancient complex, which is involved in endosomal sorting.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6627,"ComplexName":"AMOT130-Lats2 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"Q4VCS5-1;Q7TSJ6","subunits.Entrez.IDs.":"154796;50523","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0035329","GO.description":"hippo signaling","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23791731,"subunits.Protein.name.":"Angiomotin;Serine/threonine-protein kinase LATS2","subunits.Gene.name.":"AMOT;Lats2","subunits.Gene.name.syn.":"KIAA1071;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Mus musculus (Mouse)"}
{"ComplexID":6628,"ComplexName":"MGAT4B-SLC35A2(splice variant 2) complex","Organism":"Human","Synonyms":"MGAT4B-UGT1 complex","Cell.line":"HEK93T cells","subunits.UniProt.IDs.":"P78381-2;Q9UQ53","subunits.Entrez.IDs.":"7355;11282","Protein.complex.purification.method":"MI:0053-fluorescence polarization spectroscopy;MI:0055-fluorescent resonance energy transfer","GO.ID":"GO:0015785;GO:0000139","GO.description":"UDP-galactose transport;Golgi membrane","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25944901,"subunits.Protein.name.":"UDP-galactose translocator;Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B","subunits.Gene.name.":"SLC35A2;MGAT4B","subunits.Gene.name.syn.":"UGT1, UGALT, UGT, UGTL;GNT-IV, GNT-IVB","Disease.comment":"None","Subunits.comment":"One of the subunits in this complex is a splice variant 1 of SLC35A2 protein.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6629,"ComplexName":"MAGT5-SLC35A3 complex","Organism":"Human","Synonyms":"MAGT5-NGT complex","Cell.line":"HEK93T cells","subunits.UniProt.IDs.":"Q09328;Q9Y2D2","subunits.Entrez.IDs.":"4249;23443","Protein.complex.purification.method":"MI:0053-fluorescence polarization spectroscopy;MI:0053-fluorescence polarization spectroscopy","GO.ID":"GO:0015788;GO:0000139","GO.description":"UDP-N-acetylglucosamine transport;Golgi membrane","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25944901,"subunits.Protein.name.":"Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A;UDP-N-acetylglucosamine transporter","subunits.Gene.name.":"MGAT5;SLC35A3","subunits.Gene.name.syn.":"GGNT5;NGT, AMRS","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6630,"ComplexName":"MGAT5-SLC352A(splice variant 2) complex","Organism":"Human","Synonyms":"MGAT5-UGT1 complex","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"P78381;Q09328","subunits.Entrez.IDs.":"7355;4249","Protein.complex.purification.method":"MI:0053-fluorescence polarization spectroscopy;MI:0055-fluorescent resonance energy transfer","GO.ID":"GO:0015788;GO:0000139","GO.description":"UDP-N-acetylglucosamine transport;Golgi membrane","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25944901,"subunits.Protein.name.":"UDP-galactose translocator;Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A","subunits.Gene.name.":"SLC35A2;MGAT5","subunits.Gene.name.syn.":"UGALT, UGT1, UGTL;GGNT5","Disease.comment":"None","Subunits.comment":"One of the subunits in this complex is a splice variant 2of SLC35A2 protein.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6631,"ComplexName":"VANGL2-PSD95 complex","Organism":"Rat","Synonyms":"VANGL2-DLG4 complex","Cell.line":"brain","subunits.UniProt.IDs.":"P31016;P84889","subunits.Entrez.IDs.":"29495;289229","Protein.complex.purification.method":"MI:0663-confocal microscopy;MI:0019-coimmunoprecipitation;MI:0096-pull down","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23567299,"subunits.Protein.name.":"Disks large homolog 4;Vang-like protein 2","subunits.Gene.name.":"Dlg4;Vangl2","subunits.Gene.name.syn.":"Dlgh4, Psd95;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Vangl2 specifically binds to the third PDZ domain of PSD-95 (DLG4).","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6632,"ComplexName":"Merlin-ERM-moesin-CD44 complex","Organism":"Rat","Synonyms":"Cd44-Ezr-Msn-Nf2 complex","Cell.line":"None","subunits.UniProt.IDs.":"O35763;P26051;P31977;Q63648","subunits.Entrez.IDs.":"81521;25406;54319;25744","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0001558","GO.description":"regulation of cell growth","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26692764,"subunits.Protein.name.":"Moesin;CD44 antigen;Ezrin;Merlin","subunits.Gene.name.":"Msn;Cd44;Ezr;Nf2","subunits.Gene.name.syn.":"None;None;Vil2;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6633,"ComplexName":"Rbx1- Cul1-Skp1-Fbxw8-Cul7-Rbx1","Organism":"Mouse","Synonyms":"None","Cell.line":"lysates of placenta of E13.5 embryos; primary mouse embryonic ?broblasts (MEFs)","subunits.UniProt.IDs.":"P62878;Q8BIA4;Q8VE73;Q9WTX5;Q9WTX6","subunits.Entrez.IDs.":"56438;231672;66515;21402;26965","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation;MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0001890;GO:0016567","GO.description":"placenta development;protein ubiquitination","FunCat.ID":"47.03.15.05;14.07.05","FunCat.description":"placenta;modification by ubiquitination, deubiquitination","PubMed.ID":16880526,"subunits.Protein.name.":"E3 ubiquitin-protein ligase RBX1;F-box/WD repeat-containing protein 8;Cullin-7;S-phase kinase-associated protein 1;Cullin-1","subunits.Gene.name.":"Rbx1;Fbxw8;Cul7;Skp1;Cul1","subunits.Gene.name.syn.":"None;None;Kiaa0076;Skp1a;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Cul7 has Fbxw8-dependent and -independent functions. Thelatter functions might be mediated by substrate recognitionsubunits other than Fbxw8 that associate with Cul7 to form anE3 ligase or by ubiquitylation-independent activity of Cul7.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6634,"ComplexName":"WDR20-USP12-UAF1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O75317;Q8TAF3;Q8TBZ3","subunits.Entrez.IDs.":"219333;57599;91833","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0016579","GO.description":"protein deubiquitination","FunCat.ID":"14.07.05","FunCat.description":"modification by ubiquitination, deubiquitination","PubMed.ID":20147737,"subunits.Protein.name.":"Ubiquitin carboxyl-terminal hydrolase 12;WD repeat-containing protein 48;WD repeat-containing protein 20","subunits.Gene.name.":"USP12;WDR48;WDR20","subunits.Gene.name.syn.":"UBH1,USP12L1;KIAA1449, UAF1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"WDR20 has a stimulatory activity to the USP12\\u00b7UAF1 complex. It is speculated that WDR20 serves as a specific adaptor subunit for recruiting specific substrates. This complex is not involved in the Fanconi anemia  DNA repair pathway.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6635,"ComplexName":"WDR20-USP46-UAF1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"P62068;Q8TAF3;Q8TBZ3","subunits.Entrez.IDs.":"64854;57599;91833","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0016579","GO.description":"protein deubiquitination","FunCat.ID":"14.07.05","FunCat.description":"modification by ubiquitination, deubiquitination","PubMed.ID":20147737,"subunits.Protein.name.":"Ubiquitin carboxyl-terminal hydrolase 46;WD repeat-containing protein 48;WD repeat-containing protein 20","subunits.Gene.name.":"USP46;WDR48;WDR20","subunits.Gene.name.syn.":"None;KIAA1449, UAF1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex is not involved in the Fanconi anemia DNA repair pathway.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6636,"ComplexName":"USP12-UAF1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O75317;Q8TAF3","subunits.Entrez.IDs.":"219333;57599","Protein.complex.purification.method":"MI:0027-cosedimentation;MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0005634;GO:0016579","GO.description":"nucleus;protein deubiquitination","FunCat.ID":"70.10;14.07.05","FunCat.description":"nucleus;modification by ubiquitination, deubiquitination","PubMed.ID":19075014,"subunits.Protein.name.":"Ubiquitin carboxyl-terminal hydrolase 12;WD repeat-containing protein 48","subunits.Gene.name.":"USP12;WDR48","subunits.Gene.name.syn.":"UBH1,USP12L1;KIAA1449, UAF1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The complex is not involved in the regulation of the Fanconi anemia pathway.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6637,"ComplexName":"USP46-UAF1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"P62068;Q8TAF3","subunits.Entrez.IDs.":"64854;57599","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation;MI:0027-cosedimentation","GO.ID":"GO:0016579;GO:0005634","GO.description":"protein deubiquitination;nucleus","FunCat.ID":"14.07.05;70.10","FunCat.description":"modification by ubiquitination, deubiquitination;nucleus","PubMed.ID":19075014,"subunits.Protein.name.":"Ubiquitin carboxyl-terminal hydrolase 46;WD repeat-containing protein 48","subunits.Gene.name.":"USP46;WDR48","subunits.Gene.name.syn.":"None;KIAA1449, UAF1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This complex is not involved in the regulation of the Fanconi anemia pathway.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6638,"ComplexName":"USP1-UAF1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O94782;Q8TAF3","subunits.Entrez.IDs.":"7398;57599","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0005634;GO:0016579","GO.description":"nucleus;protein deubiquitination","FunCat.ID":"70.10;14.07.05","FunCat.description":"nucleus;modification by ubiquitination, deubiquitination","PubMed.ID":19075014,"subunits.Protein.name.":"Ubiquitin carboxyl-terminal hydrolase 1;WD repeat-containing protein 48","subunits.Gene.name.":"USP1;WDR48","subunits.Gene.name.syn.":"UBP;KIAA1449, UAF1","Disease.comment":"This complex regulates the Fanconi anemia (OMIM:227646) pathway by deubiquitinating FANCD2.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6639,"ComplexName":"CCC-Wash (WASH1, FAM21C) multiprotein complex","Organism":"Human","Synonyms":"CCC (COMMDs1-10, CCDC22, CCDC93)-C16orf62-WASH (WASH1, FAM21C) complex","Cell.line":"HEK293T cells; HeLa cells","subunits.UniProt.IDs.":"A8K0Z3;O60826;Q567U6;Q7Z3J2;Q7Z4G1;Q86VX2;Q86X83;Q8N668;Q9GZQ3;Q9H0A8;Q9NX08;Q9P000;Q9UBI1;Q9Y4E1;Q9Y6G5","subunits.Entrez.IDs.":"100287171;28952;54520;57020;170622;149951;51122;150684;28991;54939;54951;29099;23412;253725;51397","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0051-fluorescence technologies","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25355947,"subunits.Protein.name.":"WAS protein family homolog 1;Coiled-coil domain-containing protein 22;Coiled-coil domain-containing protein 93;UPF0505 protein C16orf62;COMM domain-containing protein 6;COMM domain-containing protein 7;COMM domain-containing protein 2;COMM domain-containing protein 1;COMM domain-containing protein 5;COMM domain-containing protein 4;COMM domain-containing protein 8;COMM domain-containing protein 9;COMM domain-containing protein 3;WASH complex subunit FAM21C;COMM domain-containing protein 10","subunits.Gene.name.":"WASH1;CCDC22;CCDC93;C16orf62;COMMD6;COMMD7;COMMD2;COMMD1;COMMD5;COMMD4;COMMD8;COMMD9;COMMD3;FAM21C;COMMD10","subunits.Gene.name.syn.":"FAM39E;CXorf37,JM1;None;None;MSTP076;C20orf92;HSPC042,My004;C2orf5, MURR1;HT002;None;MDS022;HSPC166;BUP,C10orf8;KIAA0592;HSPC305,PTD002","Disease.comment":"Depletion of CCC complex components leads to lack of copper-dependent movement of the copper transporterATP7A from endosomes, resulting in intracellular copper accumulation and modest alterations in copper homeostasis in humans with CCDC22 mutations.","Subunits.comment":"None","Complex.comment":"All 10 human COMMD family members coprecipitated endogenous CCDC93. The interaction experiments validated the notion that these factors form a multiprotein complex. COMMD1 is directly linked to early endosomes through its interaction with a protein complex containing CCDC22, CCDC93, and C16orf62. This COMMD/CCDC22/CCDC93 (CCC) complex interacts with the multisubunit WASH complex, an evolutionarily conserved system, which is required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. Interactions between the WASH complex subunit FAM21, and the carboxyl-terminal ends of CCDC22 and CCDC93 are responsible for CCC complex recruitment to endosomes. In the absence of the CCC complex or its recruitment to endosomes, ATP7A is mislocalized and does not traffic in response to copper availability, resulting in altered copper handling.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6640,"ComplexName":"Phosphorylase kinase complex","Organism":"Human","Synonyms":"PHKA1-PHKB-PHKG1-CALM1 complex","Cell.line":"None","subunits.UniProt.IDs.":"P46020;P62158;Q16816;Q93100","subunits.Entrez.IDs.":"5255;801;5260;5257","Protein.complex.purification.method":"MI:0069-mass spectrometry studies of complexes","GO.ID":"GO:0005977","GO.description":"glycogen metabolic process","FunCat.ID":"01.05.03.01","FunCat.description":"glycogen metabolism","PubMed.ID":22964223,"subunits.Protein.name.":"Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform;Calmodulin;Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform;Phosphorylase b kinase regulatory subunit beta","subunits.Gene.name.":"PHKA1;CALM1; CAL;PHKG1;PHKB","subunits.Gene.name.syn.":"PHKA;CALM, CAM, CAM1, CAM2, CAMB, CALML2, CAM3, CAMC, CAMIII;PHKG;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6641,"ComplexName":"USP22-SAGA complex","Organism":"Human","Synonyms":"hSAGA transcriptional cofactor complex; SAGA transcription coactivator HAT complex; Histone acetyltransferase complex USP22-SAGA","Cell.line":"H1299 cells (lung cancer cell line)","subunits.UniProt.IDs.":"O75528;Q12962;Q14CW9;Q86TJ2;Q92830;Q9HBM6;Q9UPT9;Q9Y4A5","subunits.Entrez.IDs.":"10474;6881;56970;93624;2648;51616;23326;8295","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0005634;GO:0004402;GO:1902562;GO:0016578;GO:0010564;GO:0009299","GO.description":"nucleus;histone acetyltransferase activity;H4 histone acetyltransferase complex;histone deubiquitination;regulation of cell cycle process;mRNA transcription","FunCat.ID":"70.10;11.02.03","FunCat.description":"nucleus;mRNA synthesis","PubMed.ID":18206973,"subunits.Protein.name.":"Transcriptional adapter 3;Transcription initiation factor TFIID subunit 10;Ataxin-7-like protein 3;Transcriptional adapter 2-beta;Histone acetyltransferase KAT2A;Transcription initiation factor TFIID subunit 9B;Ubiquitin carboxyl-terminal hydrolase 22;Transformation/transcription domain-associated protein","subunits.Gene.name.":"TADA3;TAF10;ATXN7L3;TADA2B;KAT2A;TAF9B;USP22;TRRAP","subunits.Gene.name.syn.":"ADA3, TADA3L;TAF2A TAF2H TAFII30;None;ADA2B;GCN5, GCN5L2, HGCN5;TAF9L;KIAA1063,USP3L;PAF400","Disease.comment":"USP22 is a cancer stem cell marker and is required for the biological activity of the MYC oncoprotein.","Subunits.comment":"The authors did not specify ADA2, but according to PMID:26468280 the subunit of the SAGA complex is ADA2B.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6642,"ComplexName":"ODC-OAZ1-CCND1 complex","Organism":"Human","Synonyms":"ODC-AZ-CCND1","Cell.line":"None","subunits.UniProt.IDs.":"P11926;P24385;P54368","subunits.Entrez.IDs.":"4953;595;4946","Protein.complex.purification.method":"MI:0028-cosedimentation in solution","GO.ID":"GO:0030163","GO.description":"protein catabolic process","FunCat.ID":"14.13","FunCat.description":"protein/peptide degradation","PubMed.ID":26172301,"subunits.Protein.name.":"Ornithine decarboxylase;G1/S-specific cyclin-D1;Ornithine decarboxylase antizyme 1","subunits.Gene.name.":"ODC1;CCND1;OAZ1","subunits.Gene.name.syn.":"None;BCL1 PRAD1;OAZ","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors found that the ODC-AZ-CCND1 ternary complex may exist in equilibrium and that the AZ-mediated degradation of ODC and CCND1 is inhibited by ternary complex formation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6643,"ComplexName":"SAGA complex, GCN5-linked","Organism":"Human","Synonyms":"Histone acetyltransferase (HAT) complex SAGA","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O75486;O75528;O75529;O94864;P00813;Q12962;Q14CW9;Q16514;Q16594;Q5T6C5;Q86TJ2;Q8NEM7;Q92830;Q96ES7;Q9HBM6;Q9ULK2;Q9UPT9;Q9Y4A5;Q9Y6J9","subunits.Entrez.IDs.":"8464;10474;27097;9913;100;6881;56970;6883;6880;127002;93624;55578;2648;112869;51616;222255;23326;8295;10629","Protein.complex.purification.method":"MI:0676-tandem affinity purification;MI:0019-coimmunoprecipitation","GO.ID":"GO:0016573;GO:0005634;GO:0044154","GO.description":"histone acetylation;nucleus;histone H3-K14 acetylation","FunCat.ID":"70.1","FunCat.description":"nucleus","PubMed.ID":26468280,"subunits.Protein.name.":"Transcription initiation protein SPT3 homolog;Transcriptional adapter 3;TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L;STAGA complex 65 subunit gamma;Adenosine deaminase;Transcription initiation factor TFIID subunit 10;Ataxin-7-like protein 3;Transcription initiation factor TFIID subunit 12;Transcription initiation factor TFIID subunit 9;Ataxin-7-like protein 2;Transcriptional adapter 2-beta;Transcription factor SPT20 homolog;Histone acetyltransferase KAT2A;SAGA-associated factor 29;Transcription initiation factor TFIID subunit 9B;Ataxin-7-like protein 1;Ubiquitin carboxyl-terminal hydrolase 22;Transformation/transcription domain-associated protein;TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L","subunits.Gene.name.":"SUPT3H;TADA3;TAF5L;SUPT7L;ADA;TAF10;ATXN7L3;TAF12;TAF9;ATXN7L2;TADA2B;SUPT20H;KAT2A;SGF29;TAF9B;ATXN7L1;USP22;TRRAP;TAF6L","subunits.Gene.name.syn.":"SPT3;ADA3, TADA3L;PAF65B;KIAA0764, STAF65gamma;ADA1;TAF2A TAF2H TAFII30;None;TAF15 TAF2J TAFII20;TAF2G TAFII31;None;ADA2B;C13orf19,FAM48A,FP757;GCN5, GCN5L2, HGCN5;CCDC101;TAF9L;ATXN7L4,KIAA1218;KIAA1063,USP3L;PAF400;PAF65A","Disease.comment":"None","Subunits.comment":"It is not clear whether ATXN7 (O15265) is also a subunit of the complex.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6644,"ComplexName":"CCDC22-COMMD1-CUL2 complex","Organism":"Human","Synonyms":"CCDC22-MURR1-CUL2 complex","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"O60826;Q13617;Q8N668","subunits.Entrez.IDs.":"28952;8453;150684","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0016567","GO.description":"protein ubiquitination","FunCat.ID":"14.07.05","FunCat.description":"modification by ubiquitination, deubiquitination","PubMed.ID":23563313,"subunits.Protein.name.":"Coiled-coil domain-containing protein 22;Cullin-2;COMM domain-containing protein 1","subunits.Gene.name.":"CCDC22;CUL2;COMMD1","subunits.Gene.name.syn.":"CXorf37,JM1;None;C2orf5, MURR1","Disease.comment":"CCDC22 is a factor recently implicated in X-linked intellectual disability (XLID).","Subunits.comment":"None","Complex.comment":"It is demonstrated that all COMMD proteins bind to CCDC22. COMMD1 binds preferentially to Cul2, whereas COMMD8 binds better to Cul1 and Cul3. These data suggested that despite the ability of COMMDs, CCDC22, and Cullin to form a triple complex, none of them seems to play a scaffold role. The high level of CCDC22 expression observed in the immune system, particularly in myeloid and T cells, suggests an important immunological role, in keeping with the NFkappaB regulatory function. The involvement of CCDC22 and COMMD8 in the ubiquitination of IkappaB represents a novel aspect in the regulation of this critical pathway that might be amenable to therapeutic manipulation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6645,"ComplexName":"CCC complex","Organism":"Human","Synonyms":"CCC (COMMDs1-10, CCDC22, CCDC93, C16orf62) multiprotein complex","Cell.line":"HEK293T cells; HeLa cells","subunits.UniProt.IDs.":"O60826;Q567U6;Q7Z3J2;Q7Z4G1;Q86VX2;Q86X83;Q8N668;Q9GZQ3;Q9H0A8;Q9NX08;Q9P000;Q9UBI1;Q9Y6G5","subunits.Entrez.IDs.":"28952;54520;57020;170622;149951;51122;150684;28991;54939;54951;29099;23412;51397","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0051-fluorescence technologies","GO.ID":"GO:0005769","GO.description":"early endosome","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25355947,"subunits.Protein.name.":"Coiled-coil domain-containing protein 22;Coiled-coil domain-containing protein 93;UPF0505 protein C16orf62;COMM domain-containing protein 6;COMM domain-containing protein 7;COMM domain-containing protein 2;COMM domain-containing protein 1;COMM domain-containing protein 5;COMM domain-containing protein 4;COMM domain-containing protein 8;COMM domain-containing protein 9;COMM domain-containing protein 3;COMM domain-containing protein 10","subunits.Gene.name.":"CCDC22;CCDC93;C16orf62;COMMD6;COMMD7;COMMD2;COMMD1;COMMD5;COMMD4;COMMD8;COMMD9;COMMD3;COMMD10","subunits.Gene.name.syn.":"CXorf37,JM1;None;None;MSTP076;C20orf92;HSPC042,My004;C2orf5, MURR1;HT002;None;MDS022;HSPC166;BUP,C10orf8;HSPC305,PTD002","Disease.comment":"Depletion of CCC complex components leads to lack of copper-dependent movement of the copper transporter ATP7A from endosomes, resulting in intracellular copper accumulation and modest alterations in copper homeostasis in humans with CCDC22 mutations.","Subunits.comment":"None","Complex.comment":"All 10 human COMMD family members coprecipitated endogenous CCDC93. The interaction experiments validated the notion that these factors form a multiprotein complex. COMMD1 is directly linked to early endosomes through its interaction with a protein complex containing CCDC22, CCDC93, and C16orf62. In the absence of the CCC complex or its recruitment to endosomes, ATP7A is mislocalized and does not traffic in response to copper availability, resulting in altered copper handling.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6646,"ComplexName":"SMAD2-SMAD4-WWTR1 complex","Organism":"Human","Synonyms":"SMAD2-SMAD4-TAZ complex","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"Q13485;Q15796;Q9GZV5","subunits.Entrez.IDs.":"4089;4087;25937","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006351","GO.description":"transcription, DNA-templated","FunCat.ID":"11","FunCat.description":"TRANSCRIPTION","PubMed.ID":18568018,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 4;Mothers against decapentaplegic homolog 2;WW domain-containing transcription regulator protein 1","subunits.Gene.name.":"SMAD4;SMAD2;WWTR1","subunits.Gene.name.syn.":"DPC4 MADH4;MADH2, MADR2;TAZ","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6647,"ComplexName":"MED15-WWTR1 complex","Organism":"Human","Synonyms":"ARC105-TAZ complex","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"Q96RN5;Q9GZV5","subunits.Entrez.IDs.":"51586;25937","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006351","GO.description":"transcription, DNA-templated","FunCat.ID":"11","FunCat.description":"TRANSCRIPTION","PubMed.ID":18568018,"subunits.Protein.name.":"Mediator of RNA polymerase II transcription subunit 15;WW domain-containing transcription regulator protein 1","subunits.Gene.name.":"MED15;WWTR1","subunits.Gene.name.syn.":"ARC105 CTG7A PCQAP TIG1 TNRC7;TAZ","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6648,"ComplexName":"KCND3-KCNIP4(splice variant 4) complex","Organism":"Human","Synonyms":"Kv4.3- KChIP4a complex","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"Q6PIL6;Q9UK17","subunits.Entrez.IDs.":"80333;3752","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:1901379","GO.description":"regulation of potassium ion transmembrane transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26039167,"subunits.Protein.name.":"Kv channel-interacting protein 4;Potassium voltage-gated channel subfamily D member 3","subunits.Gene.name.":"KCNIP4;KCND3","subunits.Gene.name.syn.":"CALP, KCHIP4;KV4.3, SCA19, SCA22, BRGDA9, KCND3L, KCND3S, KSHIVB","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6649,"ComplexName":"SMAD3-SMAD4-WWTR1 complex","Organism":"Human","Synonyms":"SMAD3-SMAD4-TAZ complex","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"P84022;Q13485;Q9GZV5","subunits.Entrez.IDs.":"4088;4089;25937","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006351","GO.description":"transcription, DNA-templated","FunCat.ID":"11","FunCat.description":"TRANSCRIPTION","PubMed.ID":18568018,"subunits.Protein.name.":"Mothers against decapentaplegic homolog 3;Mothers against decapentaplegic homolog 4;WW domain-containing transcription regulator protein 1","subunits.Gene.name.":"SMAD3;SMAD4;WWTR1","subunits.Gene.name.syn.":"MADH3;DPC4 MADH4;TAZ","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6650,"ComplexName":"KCND3-KCNIP4 complex","Organism":"Human","Synonyms":"Kv4.3-KChIP4bl complex","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"Q6PIL6;Q9UK17","subunits.Entrez.IDs.":"80333;3752","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:1901379","GO.description":"regulation of potassium ion transmembrane transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26039167,"subunits.Protein.name.":"Kv channel-interacting protein 4;Potassium voltage-gated channel subfamily D member 3","subunits.Gene.name.":"KCNIP4;KCND3","subunits.Gene.name.syn.":"CALP, KCHIP4;KV4.3, SCA19, SCA22, BRGDA9, KCND3L, KCND3S, KSHIVB","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6651,"ComplexName":"WWTR1-YAP1 complex","Organism":"Human","Synonyms":"TAZ-YAP complex","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"P46937;Q9GZV5","subunits.Entrez.IDs.":"10413;25937","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006351","GO.description":"transcription, DNA-templated","FunCat.ID":"11","FunCat.description":"TRANSCRIPTION","PubMed.ID":16332960,"subunits.Protein.name.":"Transcriptional coactivator YAP1;WW domain-containing transcription regulator protein 1","subunits.Gene.name.":"YAP1;WWTR1","subunits.Gene.name.syn.":"YAP65;TAZ","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6652,"ComplexName":"WWTR1 homodimer","Organism":"Human","Synonyms":"TAZ homodimer","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"Q9GZV5","subunits.Entrez.IDs.":"25937","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006351","GO.description":"transcription, DNA-templated","FunCat.ID":"11","FunCat.description":"TRANSCRIPTION","PubMed.ID":16332960,"subunits.Protein.name.":"WW domain-containing transcription regulator protein 1","subunits.Gene.name.":"WWTR1","subunits.Gene.name.syn.":"TAZ","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":6653,"ComplexName":"EP300-KAT2B-TBX5-WWTR1 complex","Organism":"Human","Synonyms":"P300-PCAF-TBX5-TAZ complex","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"Q09472;Q92831;Q99593;Q9GZV5","subunits.Entrez.IDs.":"2033;8850;6910;25937","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006351","GO.description":"transcription, DNA-templated","FunCat.ID":"11","FunCat.description":"TRANSCRIPTION","PubMed.ID":16332960,"subunits.Protein.name.":"Histone acetyltransferase p300;Histone acetyltransferase KAT2B;T-box transcription factor TBX5;WW domain-containing transcription regulator protein 1","subunits.Gene.name.":"EP300;KAT2B;TBX5;WWTR1","subunits.Gene.name.syn.":"P300;PCAF;None;TAZ","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6654,"ComplexName":"KCNJ11-ABCC9(splice variant 1) complex","Organism":"Human","Synonyms":"KIR6.2-SUR2A complex","Cell.line":"COS cells, cardiomyocytes","subunits.UniProt.IDs.":"O60706-;Q14654","subunits.Entrez.IDs.":"10060;3767","Protein.complex.purification.method":"MI:0045-experimental","GO.ID":"GO:1901379","GO.description":"regulation of potassium ion transmembrane transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":9831708,"subunits.Protein.name.":"ATP-binding cassette sub-family C member 9;ATP-sensitive inward rectifier potassium channel 11","subunits.Gene.name.":"ABCC9;KCNJ11","subunits.Gene.name.syn.":"SUR2A;BIR, HHF2, IKATP, KIR6.2, MODY13, PHHI, TNDM3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6655,"ComplexName":"CTNNB1-TBX5-YAP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"P35222;P46937;Q99593","subunits.Entrez.IDs.":"1499;10413;6910","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006351","GO.description":"transcription, DNA-templated","FunCat.ID":"11","FunCat.description":"TRANSCRIPTION","PubMed.ID":23245941,"subunits.Protein.name.":"Catenin beta-1;Transcriptional coactivator YAP1;T-box transcription factor TBX5","subunits.Gene.name.":"CTNNB1;YAP1;TBX5","subunits.Gene.name.syn.":"CTNNB;YAP65;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6656,"ComplexName":"Nherf1-Fzd4-Vangl2 complex","Organism":"Mouse","Synonyms":"Slc9a3r1-Fzd4-Vangl2 complex","Cell.line":"HEK293S GnTI cells","subunits.UniProt.IDs.":"P70441;Q61088;Q91ZD4","subunits.Entrez.IDs.":"26941;14366;93840","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0051-fluorescence technologies","GO.ID":"GO:0060271;GO:0060071","GO.description":"cilium assembly;Wnt signaling pathway, planar cell polarity pathway","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":27055101,"subunits.Protein.name.":"Na(+)/H(+) exchange regulatory cofactor NHE-RF1;Frizzled-4;Vang-like protein 2","subunits.Gene.name.":"Slc9a3r1;Fzd4;Vangl2","subunits.Gene.name.syn.":"Nherf, Nherf1;None;Lpp1, Ltap","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"NHERF1 promotes the interaction of Vangl2 with Fzd4 by acting as a scaffold linking both proteins. NHERF1 is required for the apical localization of Vangl2 in ependyma.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6657,"ComplexName":"ATAC complex, GCN5-linked","Organism":"Human","Synonyms":"Histone acetyltransferase (HAT) complex ATAC","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O75478;O75528;P61964;Q01658;Q8IYH5;Q92830;Q96ES7;Q9H8E8;Q9NS73;Q9ULM3","subunits.Entrez.IDs.":"6871;10474;11091;1810;26009;2648;112869;57325;51562;55689","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation;MI:0676-tandem affinity purification","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26468280,"subunits.Protein.name.":"Transcriptional adapter 2-alpha;Transcriptional adapter 3;WD repeat-containing protein 5;Protein Dr1;ZZ-type zinc finger-containing protein 3;Histone acetyltransferase KAT2A;SAGA-associated factor 29;Cysteine-rich protein 2-binding protein;MAP3K12-binding inhibitory protein 1;YEATS domain-containing protein 2","subunits.Gene.name.":"TADA2A;TADA3;WDR5;DR1;ZZZ3;KAT2A;SGF29;KAT14;MBIP;YEATS2","subunits.Gene.name.syn.":"TADA2L, ADA2A;ADA3, TADA3L;BIG3;NC2beta;None;GCN5, GCN5L2, HGCN5;CCDC101;CSRP2BP, ATAC2;None;KIAA1197","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6658,"ComplexName":"CCDC22-COMMD8-CUL1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"O60826;Q13616;Q9NX08","subunits.Entrez.IDs.":"28952;8454;54951","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0008384;GO:0016567","GO.description":"IkappaB kinase activity;protein ubiquitination","FunCat.ID":"14.07.05","FunCat.description":"modification by ubiquitination, deubiquitination","PubMed.ID":23563313,"subunits.Protein.name.":"Coiled-coil domain-containing protein 22;Cullin-1;COMM domain-containing protein 8","subunits.Gene.name.":"CCDC22;CUL1;COMMD8","subunits.Gene.name.syn.":"CXorf37,JM1;None;MDS022","Disease.comment":"CCDC22 is a factor recently implicated in X-linked intellectual disability (XLID).","Subunits.comment":"None","Complex.comment":"It is demonstrated that all COMMD proteins bind to CCDC22. COMMD1 binds preferentially to Cul2, whereas COMMD8 binds better to Cul1 and Cul3. These data suggested that despite the ability of COMMDs, CCDC22, and Cullin to form a triple complex, none of them seems to play a scaffold role. The high level of CCDC22 expression observed in the immune system, particularly in myeloid and T cells, suggests an important immunological role, in keeping with the NFkappaB regulatory function. The involvement of CCDC22 and COMMD8 in the ubiquitination of IkappaB represents a novel aspect in the regulation of this critical pathway that might be amenable to therapeutic manipulation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6659,"ComplexName":"CCDC22-COMMD8-CUL3 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"O60826;Q13618;Q9NX08","subunits.Entrez.IDs.":"28952;8452;54951","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0008384;GO:0016567","GO.description":"IkappaB kinase activity;protein ubiquitination","FunCat.ID":"14.07.05","FunCat.description":"modification by ubiquitination, deubiquitination","PubMed.ID":23563313,"subunits.Protein.name.":"Coiled-coil domain-containing protein 22;Cullin-3;COMM domain-containing protein 8","subunits.Gene.name.":"CCDC22;CUL3;COMMD8","subunits.Gene.name.syn.":"CXorf37,JM1;KIAA0617;MDS022","Disease.comment":"CCDC22 is a factor recently implicated in X-linked intellectual disability (XLID).","Subunits.comment":"None","Complex.comment":"It is demonstrated that all COMMD proteins bind to CCDC22. COMMD1 binds preferentially to Cul2, whereas COMMD8 binds better to Cul1 and Cul3. These data suggested that despite the ability of COMMDs, CCDC22, and Cullin to form a triple complex, none of them seems to play a scaffold role. The high level of CCDC22 expression observed in the immune system, particularly in myeloid and T cells, suggests an important immunological role, in keeping with the NFkappaB regulatory function. The involvement of CCDC22 and COMMD8 in the ubiquitination of IkappaB represents a novel aspect in the regulation of this critical pathway that might be amenable to therapeutic manipulation.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6660,"ComplexName":"LATS1-NPHP4 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"O75161;O95835","subunits.Entrez.IDs.":"261734;9113","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0035329","GO.description":"hippo signaling","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":21555462,"subunits.Protein.name.":"Nephrocystin-4;Serine/threonine-protein kinase LATS1","subunits.Gene.name.":"NPHP4;LATS1","subunits.Gene.name.syn.":"KIAA0673;WARTS","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6661,"ComplexName":"NEK8-WWTR1 complex","Organism":"Human","Synonyms":"NPHP9-TAZ complex","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"Q86SG6;Q9GZV5","subunits.Entrez.IDs.":"284086;25937","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005634;GO:0035329","GO.description":"nucleus;hippo signaling","FunCat.ID":"70.1","FunCat.description":"nucleus","PubMed.ID":23026745,"subunits.Protein.name.":"Serine/threonine-protein kinase Nek8;WW domain-containing transcription regulator protein 1","subunits.Gene.name.":"NEK8;WWTR1","subunits.Gene.name.syn.":"JCK, NEK12A, NPHP9;TAZ","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6662,"ComplexName":"Kcnj8-Kcnj11-Abcc9(splice variant 2) complex","Organism":"Mouse","Synonyms":"Kir6.1-Kir6.2-SUR2B complex","Cell.line":"None","subunits.UniProt.IDs.":"P70170-2;P97794;Q61743","subunits.Entrez.IDs.":"20928;16523;16514","Protein.complex.purification.method":"MI:0045-experimental","GO.ID":"GO:0071805","GO.description":"potassium ion transmembrane transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":21984445,"subunits.Protein.name.":"ATP-binding cassette sub-family C member 9;ATP-sensitive inward rectifier potassium channel 8;ATP-sensitive inward rectifier potassium channel 11","subunits.Gene.name.":"Abcc9;Kcnj8;Kcnj11","subunits.Gene.name.syn.":"Sur2B;None;Kir6.2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6663,"ComplexName":"Ezrin-Nherf1-Irbit-NHE3 complex","Organism":"Mouse","Synonyms":"Ezr-Slc9a3r1-Ahcyl1-Slc9a3 complex","Cell.line":"BBM (intestinal brush border membrane) vesicles (BBMVs)","subunits.UniProt.IDs.":"P26040;P70441;Q80SW1;Q9WUJ5","subunits.Entrez.IDs.":"22350;26941;229709;None","Protein.complex.purification.method":"MI:0404-comigration in non denaturing gel electropho","GO.ID":"GO:0042045;GO:0035725;GO:1902600;GO:0051668","GO.description":"epithelial fluid transport;sodium ion transmembrane transport;hydrogen ion transmembrane transport;localization within membrane","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26258413,"subunits.Protein.name.":"Ezrin;Na(+)/H(+) exchange regulatory cofactor NHE-RF1;Putative adenosylhomocysteinase 2;Na+/H+ exchanger","subunits.Gene.name.":"Ezr;Slc9a3r1;Ahcyl1;Slc9a3","subunits.Gene.name.syn.":"Vil2;Nherf, Nherf1;Irbit;NHE-3","Disease.comment":"The restoration of fluid absorption by activation of NHE3 by insulin or LPA indicates that NHE3 can act as a therapeutic target for the treatment of impaired fluid absorption in diabetes.","Subunits.comment":"None","Complex.comment":"NHE3 activation by insulin requires IRBIT, NHERF1, and ezrin to incorporate NHE3 in macromolecular complexes that form the physical basis for NHE3 trafficking to the BBM (brush border membrane) of IECs ( intestinal epithelial cells).","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6664,"ComplexName":"STAGA complex, SPT3-linked","Organism":"Human","Synonyms":"HAT complex STAGA; Histone acetyltransferase complex STAGA","Cell.line":"HeLa S3 cells; HEK293 cells","subunits.UniProt.IDs.":"O15265;O75486;O75528;O75529;O94864;Q12962;Q14CW9;Q16514;Q16594;Q86TJ2;Q8NEM7;Q92830;Q96BN2;Q96ES7;Q9H0E3;Q9NPA8;Q9UPT9;Q9Y4A5;Q9Y6J9","subunits.Entrez.IDs.":"6314;8464;10474;27097;9913;6881;56970;6883;6880;93624;55578;2648;117143;112869;79595;56943;23326;8295;10629","Protein.complex.purification.method":"MI:0096-pull down;MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0016573;GO:0005634","GO.description":"histone acetylation;nucleus","FunCat.ID":"70.1","FunCat.description":"nucleus","PubMed.ID":18838386,"subunits.Protein.name.":"Ataxin-7;Transcription initiation protein SPT3 homolog;Transcriptional adapter 3;TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L;STAGA complex 65 subunit gamma;Transcription initiation factor TFIID subunit 10;Ataxin-7-like protein 3;Transcription initiation factor TFIID subunit 12;Transcription initiation factor TFIID subunit 9;Transcriptional adapter 2-beta;Transcription factor SPT20 homolog;Histone acetyltransferase KAT2A;Transcriptional adapter 1;SAGA-associated factor 29;Histone deacetylase complex subunit SAP130;Transcription and mRNA export factor ENY2;Ubiquitin carboxyl-terminal hydrolase 22;Transformation/transcription domain-associated protein;TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L","subunits.Gene.name.":"ATXN7;SUPT3H;TADA3;TAF5L;SUPT7L;TAF10;ATXN7L3;TAF12;TAF9;TADA2B;SUPT20H;KAT2A;TADA1;SGF29;SAP130;ENY2;USP22;TRRAP;TAF6L","subunits.Gene.name.syn.":"SCA7;SPT3;ADA3, TADA3L;PAF65B;KIAA0764, STAF65gamma;TAF2A TAF2H TAFII30;None;TAF15 TAF2J TAFII20;TAF2G TAFII31;ADA2B;C13orf19,FAM48A,FP757;GCN5, GCN5L2, HGCN5;TADA1L, STAF42;CCDC101;None;DC6;KIAA1063,USP3L;PAF400;PAF65A","Disease.comment":"None","Subunits.comment":"The authors indicate that the interaction of USP22 to ATAC complex is only weak, but is observed under physiological salt concentrations.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6665,"ComplexName":"ATAC complex, YEATS2-linked","Organism":"Human","Synonyms":"HAT complex ATAC; Histone acetyltransferase complex ATAC","Cell.line":"HeLa S3 cells; HEK293 cells","subunits.UniProt.IDs.":"O43318;O75478;O75528;P61964;Q01658;Q14157;Q8IYH5;Q92830;Q96ES7;Q9H8E8;Q9NR33;Q9NRF9;Q9NS73;Q9ULM3","subunits.Entrez.IDs.":"6885;6871;10474;11091;1810;9898;26009;2648;112869;57325;56655;54107;51562;55689","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation;MI:0096-pull down","GO.ID":"GO:0005634;GO:0016573","GO.description":"nucleus;histone acetylation","FunCat.ID":"70.1","FunCat.description":"nucleus","PubMed.ID":18838386,"subunits.Protein.name.":"Mitogen-activated protein kinase kinase kinase 7;Transcriptional adapter 2-alpha;Transcriptional adapter 3;WD repeat-containing protein 5;Protein Dr1;Ubiquitin-associated protein 2-like;ZZ-type zinc finger-containing protein 3;Histone acetyltransferase KAT2A;SAGA-associated factor 29;Cysteine-rich protein 2-binding protein;DNA polymerase epsilon subunit 4;DNA polymerase epsilon subunit 3;MAP3K12-binding inhibitory protein 1;YEATS domain-containing protein 2","subunits.Gene.name.":"MAP3K7;TADA2A;TADA3;WDR5;DR1;UBAP2L;ZZZ3;KAT2A;SGF29;KAT14;POLE4;POLE3;MBIP;YEATS2","subunits.Gene.name.syn.":"TAK1;TADA2L, ADA2A;ADA3, TADA3L;BIG3;NC2beta;KIAA0144, NICE4;None;GCN5, GCN5L2, HGCN5;CCDC101;CSRP2BP, ATAC2;None;CHRAC17;None;KIAA1197","Disease.comment":"None","Subunits.comment":"The authors indicate that the interaction of UBAP2L to ATAC complex is only weak, but is observed under physiological salt concentrations.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6667,"ComplexName":"Glis3-Wwtr1 complex","Organism":"Mouse","Synonyms":"Glis3-Taz complex","Cell.line":"None","subunits.UniProt.IDs.":"Q6XP49;Q9EPK5","subunits.Entrez.IDs.":"226075;97064","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0018-two hybrid;MI:0096-pull down","GO.ID":"GO:0005929;GO:0006351","GO.description":"cilium;transcription, DNA-templated","FunCat.ID":"11","FunCat.description":"TRANSCRIPTION","PubMed.ID":19273592,"subunits.Protein.name.":"Zinc finger protein GLIS3;WW domain-containing transcription regulator protein 1","subunits.Gene.name.":"Glis3;Wwtr1","subunits.Gene.name.syn.":"None;Taz","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6668,"ComplexName":"GLIS3-SUFU complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"Q8NEA6;Q9UMX1","subunits.Entrez.IDs.":"169792;51684","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006351;GO:0005634","GO.description":"transcription, DNA-templated;nucleus","FunCat.ID":"11;70.10","FunCat.description":"TRANSCRIPTION;nucleus","PubMed.ID":21543335,"subunits.Protein.name.":"Zinc finger protein GLIS3;Suppressor of fused homolog","subunits.Gene.name.":"GLIS3;SUFU","subunits.Gene.name.syn.":"ZNF515;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6669,"ComplexName":"B9 complex","Organism":"Mouse","Synonyms":"Ciliary transition zone complex","Cell.line":"None","subunits.UniProt.IDs.":"Q2MV57;Q3U284;Q3UK10;Q5SW45;Q8BZ64;Q8CFW7;Q8K0U3;Q8K3E5;Q922M3","subunits.Entrez.IDs.":"67978;234740;232987;380718;654470;231214;103765;None;330171","Protein.complex.purification.method":"MI:0676-tandem affinity purification","GO.ID":"GO:0035869","GO.description":"ciliary transition zone","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":22179047,"subunits.Protein.name.":"Tectonic-2;Transmembrane protein 231;B9 domain-containing protein 2;Meckel syndrome type 1 protein homolog;Tectonic-1;Coiled-coil and C2 domain-containing protein 2A;Transmembrane protein 17;Jouberin;BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 3","subunits.Gene.name.":"Tctn2;Tmem231;B9d2;Mks1;Tctn1;Cc2d2a;Tmem17;Ahi1;Kctd10","subunits.Gene.name.syn.":"Tect2;None;None;None;Tect1;None;None;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6670,"ComplexName":"KCNJ11-ABCC8 complex","Organism":"Mammalia","Synonyms":"Kir6.2-SUR1 complex","Cell.line":"None","subunits.UniProt.IDs.":"Q09427;Q61743","subunits.Entrez.IDs.":"None;16514","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0071805","GO.description":"potassium ion transmembrane transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":12941953,"subunits.Protein.name.":"ATP-binding cassette sub-family C member 8;ATP-sensitive inward rectifier potassium channel 11","subunits.Gene.name.":"ABCC8;Kcnj11","subunits.Gene.name.syn.":"SUR;Kir6.2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Cricetus cricetus (Black-bellied hamster);Mus musculus (Mouse)"}
{"ComplexID":6671,"ComplexName":"PI4K2A-WASH complex","Organism":"Human","Synonyms":"None","Cell.line":"SHSY-5Y neuroblastoma cells","subunits.UniProt.IDs.":"O00203;P46934;P47756;P50570;P52907;Q00610;Q12768;Q2M389;Q5T1M5;Q641Q2;Q92888;Q92974;Q96N67;Q9BTU6","subunits.Entrez.IDs.":"8546;4734;832;1785;829;1213;9897;23325;23307;387680;9138;9181;85440;55361","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0096-pull down;MI:0069-mass spectrometry studies of complexes","GO.ID":"GO:0005769","GO.description":"early endosome","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23676666,"subunits.Protein.name.":"AP-3 complex subunit beta-1;E3 ubiquitin-protein ligase NEDD4;F-actin-capping protein subunit beta;Dynamin-2;F-actin-capping protein subunit alpha-1;Clathrin heavy chain 1;WASH complex subunit strumpellin;WASH complex subunit SWIP;FK506-binding protein 15;WASH complex subunit FAM21A;Rho guanine nucleotide exchange factor 1;Rho guanine nucleotide exchange factor 2;Dedicator of cytokinesis protein 7;Phosphatidylinositol 4-kinase type 2-alpha","subunits.Gene.name.":"AP3B1;NEDD4;CAPZB;DNM2;CAPZA1;CLTC;KIAA0196;KIAA1033;FKBP15;FAM21A;ARHGEF1;ARHGEF2;DOCK7;PI4K2A","subunits.Gene.name.syn.":"ADTB3A;KIAA0093, PIG53;CAPB, CAPPB, CAPZ;DYN2;CAPPA1, CAPZ, CAZ1;CLH17, CLTCL2, KIAA0034, CHC;SPG8, RTSC, RTSC1, WASHC5;MRT43, SWIP, WASHC4;KIAA0674, FKBP133, PPP1R76;FAM21B, WASHC2A;None;KIAA0651, LFP40, GEF-H1, GEFH1;KIAA1771, EIEE23, ZIR2;PI4KII, PIK42A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Two complexes, the WASH complex (an endosomal Arp2/3 activator) and the biogenesis of lysosome-related organelles complex-1 (BLOC-1), interact with and are regulated by the lipid kinase phosphatidylinositol-4-kinase type IIalpha (PI4K2A). (Novel) regulators of these complexes that copurify with PI4K2A are additionally displayed.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6672,"ComplexName":"Ank2-Kcnj11-Abcc8 complex","Organism":"Mouse","Synonyms":"Ankyrin-B-Kir6.2-SUR1 complex","Cell.line":"cardiomyocites","subunits.UniProt.IDs.":"Q61743;Q6PGE2;Q8C8R3","subunits.Entrez.IDs.":"16514;20927;109676","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0071805","GO.description":"potassium ion transmembrane transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20610380,"subunits.Protein.name.":"ATP-sensitive inward rectifier potassium channel 11;Abcc8 protein;Ankyrin-2","subunits.Gene.name.":"Kcnj11;Abcc8;Ank2","subunits.Gene.name.syn.":"Kir6.2;SUR1, Sur;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6673,"ComplexName":"Foxo1-Yap1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"cardiomyocytes","subunits.UniProt.IDs.":"P46938;Q9R1E0","subunits.Entrez.IDs.":"22601;56458","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0096-pull down","GO.ID":"GO:0006351;GO:0005634","GO.description":"transcription, DNA-templated;nucleus","FunCat.ID":"11;70.10","FunCat.description":"TRANSCRIPTION;nucleus","PubMed.ID":24525530,"subunits.Protein.name.":"Transcriptional coactivator YAP1;Forkhead box protein O1","subunits.Gene.name.":"Yap1;Foxo1","subunits.Gene.name.syn.":"Yap Yap65;Fkhr,Foxo1a","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6674,"ComplexName":"Ank2-Kcnj11-Abcc9(splice variant 1) complex","Organism":"Human","Synonyms":"Ankyrin-2-Kir6.2-Sur2a complex","Cell.line":"cardiomyocytes","subunits.UniProt.IDs.":"P70170-1;Q61743;Q8C8R3","subunits.Entrez.IDs.":"20928;16514;109676","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0071805","GO.description":"potassium ion transmembrane transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20610380,"subunits.Protein.name.":"ATP-binding cassette sub-family C member 9;ATP-sensitive inward rectifier potassium channel 11;Ankyrin-2","subunits.Gene.name.":"Abcc9;Kcnj11;Ank2","subunits.Gene.name.syn.":"Sur2A;Kir6.2;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6675,"ComplexName":"PI4K2A-PRDX1 complex","Organism":"Human","Synonyms":"None","Cell.line":"SHSY-5Y neuroblastoma cells","subunits.UniProt.IDs.":"Q06830;Q9BTU6","subunits.Entrez.IDs.":"5052;55361","Protein.complex.purification.method":"MI:0069-mass spectrometry studies of complexes;MI:0096-pull down","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23676666,"subunits.Protein.name.":"Peroxiredoxin-1;Phosphatidylinositol 4-kinase type 2-alpha","subunits.Gene.name.":"PRDX1;PI4K2A","subunits.Gene.name.syn.":"PAGA, PAGB, TDPX2;PI4KII, PIK42A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Two complexes, the WASH complex (an endosomal Arp2/3 activator) and the biogenesis of lysosome-related organelles complex-1 (BLOC-1), interact with and are regulated by the lipid kinase phosphatidylinositol-4-kinase type IIalpha (PI4K2A). It was also found that PI4KIIA interacts with the antioxidant enzyme peroxiredoxin-1 (Prdx-1).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6676,"ComplexName":"WWTR1-YWHAQ complex","Organism":"Human","Synonyms":"TAZ-14-3-3 complex","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"P27348;Q9GZV5","subunits.Entrez.IDs.":"10971;25937","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0035329;GO:0006351","GO.description":"hippo signaling;transcription, DNA-templated","FunCat.ID":"11","FunCat.description":"TRANSCRIPTION","PubMed.ID":21555462,"subunits.Protein.name.":"14-3-3 protein theta;WW domain-containing transcription regulator protein 1","subunits.Gene.name.":"YWHAQ;WWTR1","subunits.Gene.name.syn.":"None;TAZ","Disease.comment":"None","Subunits.comment":"The authors did not mention which 14-3-3 protein was used.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6677,"ComplexName":"Nphp1-Nphp4-Rpgrip1l complex","Organism":"Mouse","Synonyms":"Nphp1-Nphp4-Nphp8 complex","Cell.line":"IMCD3 cells","subunits.UniProt.IDs.":"P59240;Q8CG73;Q9QY53","subunits.Entrez.IDs.":"260305;244585;53885","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0044291;GO:0035869","GO.description":"cell-cell contact zone;ciliary transition zone","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":21565611,"subunits.Protein.name.":"Nephrocystin-4;Protein fantom;Nephrocystin-1","subunits.Gene.name.":"Nphp4;Rpgrip1l;Nphp1","subunits.Gene.name.syn.":"None;Ftm,Nphp8;Nph1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6678,"ComplexName":"Cep290-Iqcb1 complex","Organism":"Mouse","Synonyms":"Nphp6-Nphp5 complex","Cell.line":"IMCD3 cells","subunits.UniProt.IDs.":"Q6A078;Q8BP00","subunits.Entrez.IDs.":"216274;320299","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005813","GO.description":"centrosome","FunCat.ID":"70.05","FunCat.description":"centrosome","PubMed.ID":21565611,"subunits.Protein.name.":"Centrosomal protein of 290 kDa;IQ calmodulin-binding motif-containing protein 1","subunits.Gene.name.":"Cep290;Iqcb1","subunits.Gene.name.syn.":"Kiaa0373, Nphp6;Kiaa0036, Nphp5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6679,"ComplexName":"Ctbp1-Glis2-Hdac3 complex","Organism":"Mammalia","Synonyms":"Glis2 transcription silencing complex","Cell.line":"CHO cells","subunits.UniProt.IDs.":"O88712;O88895;Q8VDL9","subunits.Entrez.IDs.":"13016;15183;83396","Protein.complex.purification.method":"MI:0018-two hybrid","GO.ID":"GO:0005634;GO:0017053","GO.description":"nucleus;transcriptional repressor complex","FunCat.ID":"70.1","FunCat.description":"nucleus","PubMed.ID":16326862,"subunits.Protein.name.":"C-terminal-binding protein 1;Histone deacetylase 3;Zinc finger protein GLIS2","subunits.Gene.name.":"Ctbp1;Hdac3;Glis2","subunits.Gene.name.syn.":"None;None;Gli5,Nkl","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6680,"ComplexName":"CTNNB1-GLIS2 complex","Organism":"Human","Synonyms":"None","Cell.line":"HCT116 cells","subunits.UniProt.IDs.":"P35222;Q9BZE0","subunits.Entrez.IDs.":"1499;84662","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0060070","GO.description":"canonical Wnt signaling pathway","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":17289029,"subunits.Protein.name.":"Catenin beta-1;Zinc finger protein GLIS2","subunits.Gene.name.":"CTNNB1;GLIS2","subunits.Gene.name.syn.":"CTNNB;NKL, NPHP7","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6681,"ComplexName":"DVL2-INVS-NPHP4-RPGRIP1L complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"O14641;O75161;Q68CZ1;Q9Y283","subunits.Entrez.IDs.":"1856;261734;23322;27130","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":22927466,"subunits.Protein.name.":"Segment polarity protein dishevelled homolog DVL-2;Nephrocystin-4;Protein fantom;Inversin","subunits.Gene.name.":"DVL2;NPHP4;RPGRIP1L;INVS","subunits.Gene.name.syn.":"None;KIAA0673;FTM, KIAA1005, NPHP8;INV NPHP2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6682,"ComplexName":"MKS1-TMEM67 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"Q5HYA8;Q9NXB0","subunits.Entrez.IDs.":"91147;54903","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0060271","GO.description":"cilium assembly","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":17185389,"subunits.Protein.name.":"Meckelin;Meckel syndrome type 1 protein","subunits.Gene.name.":"TMEM67;MKS1","subunits.Gene.name.syn.":"MKS3;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6683,"ComplexName":"SYNE2-TMEM67 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293 cells","subunits.UniProt.IDs.":"Q5HYA8;Q8WXH0","subunits.Entrez.IDs.":"91147;23224","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0060271;GO:0031532","GO.description":"cilium assembly;actin cytoskeleton reorganization","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":19596800,"subunits.Protein.name.":"Meckelin;Nesprin-2","subunits.Gene.name.":"TMEM67;SYNE2","subunits.Gene.name.syn.":"MKS3;KIAA1011,NUA","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6684,"ComplexName":"TNFR2 signaling complex","Organism":"Human","Synonyms":"TNF-TNFRSF1B-XPNPEP3 complex; TNF-TNFR2-APP3m complex","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"P01375;P20333;Q9NQH7-1","subunits.Entrez.IDs.":"7124;7133;63929","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0002947;GO:0033209","GO.description":"tumor necrosis factor receptor superfamily complex;tumor necrosis factor-mediated signaling pathway","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25609706,"subunits.Protein.name.":"Tumor necrosis factor;Tumor necrosis factor receptor superfamily member 1B;Probable Xaa-Pro aminopeptidase 3","subunits.Gene.name.":"TNF;TNFRSF1B;XPNPEP3","subunits.Gene.name.syn.":"TNFA, TNFSF2;TNFBR, TNFR2;APP3","Disease.comment":"None","Subunits.comment":"The mitochondrial 57 kDa isoform of XPNPEP3 (APP3m) was found in the complex.","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6685,"ComplexName":"IL13RA1-TRAF3IP1 complex","Organism":"Human","Synonyms":"IL-13Ralpha1 - MIP-T3 complex","Cell.line":"293T cells","subunits.UniProt.IDs.":"P78552;Q8TDR0","subunits.Entrez.IDs.":"3597;26146","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0019973;GO:0007165","GO.description":"interleukin-13 binding;signal transduction","FunCat.ID":"30","FunCat.description":"CELLULAR COMMUNICATION/SIGNAL TRANSDUCTION MECHANISM","PubMed.ID":12935900,"subunits.Protein.name.":"Interleukin-13 receptor subunit alpha-1;TRAF3-interacting protein 1","subunits.Gene.name.":"IL13RA1;TRAF3IP1","subunits.Gene.name.syn.":"IL13R, IL13RA;IFT54, MIPT3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6686,"ComplexName":"ACTN4-ALMS1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"kidney","subunits.UniProt.IDs.":"O43707;Q8TCU4","subunits.Entrez.IDs.":"81;7840","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0032456","GO.description":"endocytic recycling","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":22693585,"subunits.Protein.name.":"Alpha-actinin-4;Alstrom syndrome protein 1","subunits.Gene.name.":"ACTN4;ALMS1","subunits.Gene.name.syn.":"None;KIAA0328","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6687,"ComplexName":"Arl6-Sec61b complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"COS cells","subunits.UniProt.IDs.":"O88848;Q9CQS8","subunits.Entrez.IDs.":"56297;66212","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005829","GO.description":"cytosol","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":10508919,"subunits.Protein.name.":"ADP-ribosylation factor-like protein 6;Protein transport protein Sec61 subunit beta","subunits.Gene.name.":"Arl6;Sec61b","subunits.Gene.name.syn.":"Bbs3;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6688,"ComplexName":"GLIS2-TRIM32 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"Q13049;Q9BZE0","subunits.Entrez.IDs.":"22954;84662","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005634;GO:0006351","GO.description":"nucleus;transcription, DNA-templated","FunCat.ID":"70.10;11","FunCat.description":"nucleus;TRANSCRIPTION","PubMed.ID":24500717,"subunits.Protein.name.":"E3 ubiquitin-protein ligase TRIM32;Zinc finger protein GLIS2","subunits.Gene.name.":"TRIM32;GLIS2","subunits.Gene.name.syn.":"HT2A, BBS11;NKL, NPHP7","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6689,"ComplexName":"DTNBP1-TRIM32 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"Q13049;Q96EV8","subunits.Entrez.IDs.":"22954;84062","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0016567","GO.description":"protein ubiquitination","FunCat.ID":"14.07.05","FunCat.description":"modification by ubiquitination, deubiquitination","PubMed.ID":19349376,"subunits.Protein.name.":"E3 ubiquitin-protein ligase TRIM32;Dysbindin","subunits.Gene.name.":"TRIM32;DTNBP1","subunits.Gene.name.syn.":"HT2A, BBS11;BLOC1S8","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6690,"ComplexName":"NEDD4-PI4K2A complex","Organism":"Human","Synonyms":"None","Cell.line":"SHSY-5Y neuroblastoma cells","subunits.UniProt.IDs.":"P46934;Q9BTU6","subunits.Entrez.IDs.":"4734;55361","Protein.complex.purification.method":"MI:0069-mass spectrometry studies of complexes;MI:0019-coimmunoprecipitation;MI:0096-pull down","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23676666,"subunits.Protein.name.":"E3 ubiquitin-protein ligase NEDD4;Phosphatidylinositol 4-kinase type 2-alpha","subunits.Gene.name.":"NEDD4;PI4K2A","subunits.Gene.name.syn.":"KIAA0093, PIG53;PI4KII, PIK42A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Two complexes, the WASH complex (an endosomal Arp2/3 activator) and the biogenesis of lysosome-related organelles complex-1 (BLOC-1), interact with and are regulated by the lipid kinase phosphatidylinositol-4-kinase type IIalpha (PI4K2A). It was also found that PI4KIIA interacts with the ubiquitin ligase Nedd4-1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6691,"ComplexName":"CLTC-PI4K2A complex","Organism":"Human","Synonyms":"CHC-PIK42A complex","Cell.line":"SHSY-5Y neuroblastoma cells","subunits.UniProt.IDs.":"Q00610;Q9BTU6","subunits.Entrez.IDs.":"1213;55361","Protein.complex.purification.method":"MI:0096-pull down;MI:0019-coimmunoprecipitation;MI:0069-mass spectrometry studies of complexes","GO.ID":"GO:0030133","GO.description":"transport vesicle","FunCat.ID":"70.09","FunCat.description":"intracellular transport vesicles","PubMed.ID":23676666,"subunits.Protein.name.":"Clathrin heavy chain 1;Phosphatidylinositol 4-kinase type 2-alpha","subunits.Gene.name.":"CLTC;PI4K2A","subunits.Gene.name.syn.":"CLH17, CLTCL2, KIAA0034, CHC;PI4KII, PIK42A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Two complexes, the WASH complex (an endosomal Arp2/3 activator) and the biogenesis of lysosome-related organelles complex-1 (BLOC-1), interact with and are regulated by the lipid kinase phosphatidylinositol-4-kinase type IIalpha (PI4K2A). It was also found that PI4KIIA interacts with vesicle-mediated transport proteins such as clathrin heavy chain.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6692,"ComplexName":"PI4K2A-PLDN complex","Organism":"Human","Synonyms":"None","Cell.line":"SHSY-5Y neuroblastoma cells","subunits.UniProt.IDs.":"Q9BTU6;Q9UL45","subunits.Entrez.IDs.":"55361;26258","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0096-pull down;MI:0069-mass spectrometry studies of complexes","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23676666,"subunits.Protein.name.":"Phosphatidylinositol 4-kinase type 2-alpha;Biogenesis of lysosome-related organelles complex 1 subunit 6","subunits.Gene.name.":"PI4K2A;BLOC1S6","subunits.Gene.name.syn.":"PI4KII, PIK42A;PA, PLDN","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Two complexes, the WASH complex (an endosomal Arp2/3 activator) and the biogenesis of lysosome-related organelles complex-1 (BLOC-1), interact with and are regulated by the lipid kinase phosphatidylinositol-4-kinase type IIalpha (PI4K2A). It was also found that PI4KIIA interacts with the pallidin subunit of BLOC-1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6693,"ComplexName":"DVL1-PI4K2A complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"O14640;Q9BTU6","subunits.Entrez.IDs.":"1855;55361","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0047-far western blotting;MI:0096-pull down","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":19561074,"subunits.Protein.name.":"Segment polarity protein dishevelled homolog DVL-1;Phosphatidylinositol 4-kinase type 2-alpha","subunits.Gene.name.":"DVL1;PI4K2A","subunits.Gene.name.syn.":"None;PI4KII, PIK42A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Dvl directly interacts with and activates PI4KII alpha by increasing its V(max) for ATP and PtdIns.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6694,"ComplexName":"Cxcr2-Nherf1-PLC-beta-2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"bone marrow neutrophils","subunits.UniProt.IDs.":"A3KGF7;P35343;P70441","subunits.Entrez.IDs.":"18796;12765;26941","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:1990266;GO:0019722;GO:0030593;GO:0070098","GO.description":"neutrophil migration;calcium-mediated signaling;neutrophil chemotaxis;chemokine-mediated signaling pathway","FunCat.ID":"30.01.09.03","FunCat.description":"Ca2+ mediated signal transduction","PubMed.ID":22203670,"subunits.Protein.name.":"1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2;C-X-C chemokine receptor type 2;Na(+)/H(+) exchange regulatory cofactor NHE-RF1","subunits.Gene.name.":"Plcb2;Cxcr2;Slc9a3r1","subunits.Gene.name.syn.":"None;Cmkar2, Gpcr16, Il8rb;Nherf, Nherf1","Disease.comment":"CXCR2 macromolecular complex might be a potential therapeutic target for neutrophil infiltration-associated inflammatory diseases.","Subunits.comment":"None","Complex.comment":"The macromolecular Cxcr2-Nherf1-PLC-beta-2 signaling complex  enables CXCR2 to transduce its signal to PLC-\\u00012 with efficiency and specificity, and this complex is a prerequisite for the CXCR2 ligand-induced calcium signaling and the resultant neutrophil migration during various inflammatory diseases, such as atherosclerosis, cystic fibrosis, and inflammatory bowel disease.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6695,"ComplexName":"MKKS-BBS12 complex","Organism":"Human","Synonyms":"BBS6-BBS12 complex","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"Q6ZW61;Q9NPJ1","subunits.Entrez.IDs.":"166379;8195","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005929;GO:0060271","GO.description":"cilium;cilium assembly","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26900326,"subunits.Protein.name.":"Bardet-Biedl syndrome 12 protein;McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin","subunits.Gene.name.":"BBS12;MKKS","subunits.Gene.name.syn.":"C4orf24;BBS6","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6696,"ComplexName":"CPLANE complex","Organism":"Mouse","Synonyms":"Ciliogenesis and planar polarity effectors complex","Cell.line":"IMCD3 cells","subunits.UniProt.IDs.":"Q059U7;Q3UYI6;Q8C456","subunits.Entrez.IDs.":"380614;70300;216560","Protein.complex.purification.method":"MI:0676-tandem affinity purification","GO.ID":"GO:0042073","GO.description":"intraciliary transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":27158779,"subunits.Protein.name.":"Protein inturned;Protein fuzzy homolog;WD repeat-containing and planar cell polarity effector protein fritz homolog","subunits.Gene.name.":"Intu;Fuz;Wdpcp","subunits.Gene.name.syn.":"Kiaa1284, Pdzd6;None;Bbs15, Fritz","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6697,"ComplexName":"TBCD-ARL2 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK-293T cells; SH-SY5Y cells","subunits.UniProt.IDs.":"P36404;Q9BTW9","subunits.Entrez.IDs.":"402;6904","Protein.complex.purification.method":"MI:0071-molecular sieving;MI:0276-blue native page","GO.ID":"GO:0000226","GO.description":"microtubule cytoskeleton organization","FunCat.ID":"42.04.05","FunCat.description":"microtubule cytoskeleton","PubMed.ID":28126905,"subunits.Protein.name.":"ADP-ribosylation factor-like protein 2;Tubulin-specific chaperone D","subunits.Gene.name.":"ARL2;TBCD","subunits.Gene.name.syn.":"None;KIAA0988, SSD1, TFCD","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6698,"ComplexName":"G-calpain","Organism":"Mouse","Synonyms":"None","Cell.line":"gastric mucosa","subunits.UniProt.IDs.":"Q91VA3;Q9D805","subunits.Entrez.IDs.":"170725;73647","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006508","GO.description":"proteolysis","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20686710,"subunits.Protein.name.":"Calpain-8;Calpain-9","subunits.Gene.name.":"Capn8;Capn9","subunits.Gene.name.syn.":"Ncl2;Ncl4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6699,"ComplexName":"KCNQ1 homotetramer","Organism":"Human","Synonyms":"Kv1.7 homotetramer","Cell.line":"None","subunits.UniProt.IDs.":"P51787","subunits.Entrez.IDs.":"3784","Protein.complex.purification.method":"MI:0051-fluorescence technologies","GO.ID":"GO:0071805;GO:0005249","GO.description":"potassium ion transmembrane transport;voltage-gated potassium channel activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20962273,"subunits.Protein.name.":"Potassium voltage-gated channel subfamily KQT member 1","subunits.Gene.name.":"KCNQ1","subunits.Gene.name.syn.":"KCNA8, KCNA9, KVLQT1, Kv1.7","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":6700,"ComplexName":"KCNQ1-Kcne1 complex","Organism":"Mammalia","Synonyms":"Kv1.7-Kcne1 complex","Cell.line":"None","subunits.UniProt.IDs.":"P15383;P51787","subunits.Entrez.IDs.":"25471;3784","Protein.complex.purification.method":"MI:0051-fluorescence technologies","GO.ID":"GO:0071805;GO:0005249","GO.description":"potassium ion transmembrane transport;voltage-gated potassium channel activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20962273,"subunits.Protein.name.":"Potassium voltage-gated channel subfamily E member 1;Potassium voltage-gated channel subfamily KQT member 1","subunits.Gene.name.":"Kcne1;KCNQ1","subunits.Gene.name.syn.":"Isk, m;KCNA8, KCNA9, KVLQT1, Kv1.7","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Homo sapiens (Human)"}
{"ComplexID":6701,"ComplexName":"DVL1-PIP5K1B-PI4K2A complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"O14640;O14986;Q9BTU6","subunits.Entrez.IDs.":"1855;8395;55361","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":19561074,"subunits.Protein.name.":"Segment polarity protein dishevelled homolog DVL-1;Phosphatidylinositol 4-phosphate 5-kinase type-1 beta;Phosphatidylinositol 4-kinase type 2-alpha","subunits.Gene.name.":"DVL1;PIP5K1B;PI4K2A","subunits.Gene.name.syn.":"None;STM7, PIP5KI;PI4KII, PIK42A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In a coimmunoprecipitation experiment PI4K2A, PIP5K1B proteins were pulled down with Dvl in HEK293T cells. Wnt promotes the formation of this Dvl, PI4K2A, and PIP5K1B  \\u0001complex as Wnt3a is able to induce the binding of Dvl to the PIP5K1B and PI4K2A complex, leading to a more stable interaction between PIP5K1B and PI4K2A.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6702,"ComplexName":"CXCR2-NHERF1-PLC-beta-3 complex","Organism":"Human","Synonyms":"CXCR2-SLC9A3R1-PLCB3 complex","Cell.line":"normal human pancreatic duct epithelial (HPDE) cells, Colo357; pancreatic ductal adenocarcinoma (PDA","subunits.UniProt.IDs.":"O14745;P25025;Q01970","subunits.Entrez.IDs.":"9368;3579;5331","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0008283;GO:0070098","GO.description":"cell proliferation;chemokine-mediated signaling pathway","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23544174,"subunits.Protein.name.":"Na(+)/H(+) exchange regulatory cofactor NHE-RF1;C-X-C chemokine receptor type 2;1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3","subunits.Gene.name.":"SLC9A3R1;CXCR2;PLCB3","subunits.Gene.name.syn.":"NHERF, NHERF1;IL8RB;None","Disease.comment":"Disrupting the CXCR2 complex significantly inhibited the malignant cellular functions (i.e., proliferation and invasion) in vitro and pancreatic tumor growth in vivo.","Subunits.comment":"None","Complex.comment":"The authors observed significantly reduced cell proliferation in Colo357 and HPAC cells, stimulated by CXCL5 and CXCL8.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6703,"ComplexName":"TBCD-tubulin(alpha)-tubulin(beta) complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"P07437;Q71U36;Q9BTW9","subunits.Entrez.IDs.":"203068;7846;6904","Protein.complex.purification.method":"MI:0071-molecular sieving;MI:0276-blue native page","GO.ID":"GO:0000226","GO.description":"microtubule cytoskeleton organization","FunCat.ID":"42.04.05","FunCat.description":"microtubule cytoskeleton","PubMed.ID":28126905,"subunits.Protein.name.":"Tubulin beta chain;Tubulin alpha-1A chain;Tubulin-specific chaperone D","subunits.Gene.name.":"TUBB;TUBA1A;TBCD","subunits.Gene.name.syn.":"TUBB5;TUBA3;KIAA0988, SSD1, TFCD","Disease.comment":"None","Subunits.comment":"Since the authors did not specify tubulin-alpha and tubulin-beta, we used Tubulin alpha-1A chain (Q71U36) and Tubulin beta chain (P07437).","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6704,"ComplexName":"KCNQ1-KCNE2 complex","Organism":"Human","Synonyms":"Kv7.1-KCNE2 complex","Cell.line":"COS cells","subunits.UniProt.IDs.":"P51787;Q9Y6J6","subunits.Entrez.IDs.":"3784;9992","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0071805;GO:0005249","GO.description":"potassium ion transmembrane transport;voltage-gated potassium channel activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":11101505,"subunits.Protein.name.":"Potassium voltage-gated channel subfamily KQT member 1;Potassium voltage-gated channel subfamily E member 2","subunits.Gene.name.":"KCNQ1;KCNE2","subunits.Gene.name.syn.":"KCNA8, KCNA9, KVLQT1, Kv1.7;ATFB4, LQT5, LQT6, MIRP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6705,"ComplexName":"KCNQ1-KCNE3 complex","Organism":"Human","Synonyms":"Kv7.1-KCNE3 complex","Cell.line":"None","subunits.UniProt.IDs.":"P51787;Q9Y6H6","subunits.Entrez.IDs.":"3784;10008","Protein.complex.purification.method":"MI:0013-biophysical","GO.ID":"GO:0034765;GO:0005249","GO.description":"regulation of ion transmembrane transport;voltage-gated potassium channel activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":27626070,"subunits.Protein.name.":"Potassium voltage-gated channel subfamily KQT member 1;Potassium voltage-gated channel subfamily E member 3","subunits.Gene.name.":"KCNQ1;KCNE3","subunits.Gene.name.syn.":"KCNA8, KCNA9, KVLQT1, Kv1.7;HOKPP, HYPP, MiRP2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6706,"ComplexName":"CAPN1-HSP90AB1 complex","Organism":"Human","Synonyms":"None","Cell.line":"human leukemic T cell JA3 cells","subunits.UniProt.IDs.":"P07384;P08238","subunits.Entrez.IDs.":"823;3326","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006508","GO.description":"proteolysis","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25575026,"subunits.Protein.name.":"Calpain-1 catalytic subunit;Heat shock protein HSP 90-beta","subunits.Gene.name.":"CAPN1;HSP90AB1","subunits.Gene.name.syn.":"CANPL1;HSP90B HSPC2 HSPCB","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6707,"ComplexName":"PIP5K1B-PI4K2A complex","Organism":"Human","Synonyms":"PIP5KI-PI4KII complex","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"O14986;Q9BTU6","subunits.Entrez.IDs.":"8395;55361","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":19561074,"subunits.Protein.name.":"Phosphatidylinositol 4-phosphate 5-kinase type-1 beta;Phosphatidylinositol 4-kinase type 2-alpha","subunits.Gene.name.":"PIP5K1B;PI4K2A","subunits.Gene.name.syn.":"STM7, PIP5KI;PI4KII, PIK42A","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Wnt3a is able to induce the binding of Dvl to the PIP5K1B and PI4K2A complex, leading to a more stable interaction between PIP5K1B and PI4K2A.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6708,"ComplexName":"KCNQ1-KCNE4 complex","Organism":"Human","Synonyms":"Kv7.1-KCNE5 complex","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"P51787;Q8WWG9","subunits.Entrez.IDs.":"3784;23704","Protein.complex.purification.method":"MI:0028-cosedimentation in solution;MI:0051-fluorescence technologies","GO.ID":"GO:0071805;GO:0005249","GO.description":"potassium ion transmembrane transport;voltage-gated potassium channel activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20533308,"subunits.Protein.name.":"Potassium voltage-gated channel subfamily KQT member 1;Potassium voltage-gated channel subfamily E member 4","subunits.Gene.name.":"KCNQ1;KCNE4","subunits.Gene.name.syn.":"KCNA8, KCNA9, KVLQT1, Kv1.7;MIRP3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6709,"ComplexName":"KCNQ1-KCNE5 complex","Organism":"Human","Synonyms":"Kv7.1-KCNE5 complex","Cell.line":"None","subunits.UniProt.IDs.":"P51787;Q9UJ90","subunits.Entrez.IDs.":"3784;23630","Protein.complex.purification.method":"MI:0028-cosedimentation in solution;MI:0051-fluorescence technologies","GO.ID":"GO:0071805;GO:0005249","GO.description":"potassium ion transmembrane transport;voltage-gated potassium channel activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20533308,"subunits.Protein.name.":"Potassium voltage-gated channel subfamily KQT member 1;Potassium voltage-gated channel subfamily E regulatory beta subunit 5","subunits.Gene.name.":"KCNQ1;KCNE5","subunits.Gene.name.syn.":"KCNA8, KCNA9, KVLQT1, Kv1.7;AMMECR2, KCNE1L","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6710,"ComplexName":"Calpain 1","Organism":"Human","Synonyms":"mu-Calpain","Cell.line":"erythrocytes","subunits.UniProt.IDs.":"P04632;P07384","subunits.Entrez.IDs.":"826;823","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006508","GO.description":"proteolysis","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":8886026,"subunits.Protein.name.":"Calpain small subunit 1;Calpain-1 catalytic subunit","subunits.Gene.name.":"CAPNS1;CAPN1","subunits.Gene.name.syn.":"CAPN4,CAPNS;CANPL1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6711,"ComplexName":"Calpain 2","Organism":"Bovine","Synonyms":"m-Calpain","Cell.line":"myocardial cells","subunits.UniProt.IDs.":"P13135;Q27971","subunits.Entrez.IDs.":"281664;281662","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006508","GO.description":"proteolysis","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":8886026,"subunits.Protein.name.":"Calpain small subunit 1;Calpain-2 catalytic subunit","subunits.Gene.name.":"CAPNS1;CAPN2","subunits.Gene.name.syn.":"CAPN4;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Bos taurus (Bovine);Bos taurus (Bovine)"}
{"ComplexID":6712,"ComplexName":"KCNQ2-KCNQ3 complex","Organism":"Human","Synonyms":"Kv7.2-Kv3.3 complex","Cell.line":"brain","subunits.UniProt.IDs.":"O43525;O43526","subunits.Entrez.IDs.":"3786;3785","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0071805;GO:0005249","GO.description":"potassium ion transmembrane transport;voltage-gated potassium channel activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":10781098,"subunits.Protein.name.":"Potassium voltage-gated channel subfamily KQT member 3;Potassium voltage-gated channel subfamily KQT member 2","subunits.Gene.name.":"KCNQ3;KCNQ2","subunits.Gene.name.syn.":"BFNC2, EBN2, KV7.3;BFNC, EBN, EBN1, ENB1, HNSPC, KCNA11, KV7.2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6713,"ComplexName":"TBCD-ARL2-tubulin(beta) complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"P07437;P36404;Q9BTW9","subunits.Entrez.IDs.":"203068;402;6904","Protein.complex.purification.method":"MI:0071-molecular sieving;MI:0276-blue native page","GO.ID":"GO:0000226;GO:0046785","GO.description":"microtubule cytoskeleton organization;microtubule polymerization","FunCat.ID":"42.04.05","FunCat.description":"microtubule cytoskeleton","PubMed.ID":28126905,"subunits.Protein.name.":"Tubulin beta chain;ADP-ribosylation factor-like protein 2;Tubulin-specific chaperone D","subunits.Gene.name.":"TUBB;ARL2;TBCD","subunits.Gene.name.syn.":"TUBB5;None;KIAA0988, SSD1, TFCD","Disease.comment":"None","Subunits.comment":"The authors state that it was impossible to specify the isoform of tubulin-beta. We used Tubulin beta chain (P07437).","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6714,"ComplexName":"TBCE-TBCB-tubulin(alpha) complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"Q15813;Q71U36;Q99426","subunits.Entrez.IDs.":"6905;7846;1155","Protein.complex.purification.method":"MI:0071-molecular sieving","GO.ID":"GO:0000226","GO.description":"microtubule cytoskeleton organization","FunCat.ID":"42.04.05","FunCat.description":"microtubule cytoskeleton","PubMed.ID":28126905,"subunits.Protein.name.":"Tubulin-specific chaperone E;Tubulin alpha-1A chain;Tubulin-folding cofactor B","subunits.Gene.name.":"TBCE;TUBA1A;TBCB","subunits.Gene.name.syn.":"None;TUBA3;CG22,CKAP1","Disease.comment":"None","Subunits.comment":"Since the authors did not specify tubulin-alpha, we used Tubulin alpha-1A chain (Q71U36).","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6715,"ComplexName":"TBCD-ARL2-tubulin(beta)-TBCE complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"P07437;P36404;Q15813;Q9BTW9","subunits.Entrez.IDs.":"203068;402;6905;6904","Protein.complex.purification.method":"None","GO.ID":"GO:0000226","GO.description":"microtubule cytoskeleton organization","FunCat.ID":"42.04.05","FunCat.description":"microtubule cytoskeleton","PubMed.ID":28126905,"subunits.Protein.name.":"Tubulin beta chain;ADP-ribosylation factor-like protein 2;Tubulin-specific chaperone E;Tubulin-specific chaperone D","subunits.Gene.name.":"TUBB;ARL2;TBCE;TBCD","subunits.Gene.name.syn.":"TUBB5;None;None;KIAA0988, SSD1, TFCD","Disease.comment":"None","Subunits.comment":"Since the authors did not specify tubulin-beta, we used Tubulin beta chain (P07437).","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6716,"ComplexName":"DLG5-MST1-MST2 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"Q13043;Q13188;Q8TDM6","subunits.Entrez.IDs.":"6789;6788;9231","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0030010;GO:0035330","GO.description":"establishment of cell polarity;regulation of hippo signaling","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":28087714,"subunits.Protein.name.":"Serine/threonine-protein kinase 4;Serine/threonine-protein kinase 3;Disks large homolog 5","subunits.Gene.name.":"STK4;STK3;DLG5","subunits.Gene.name.syn.":"KRS2, MST1;KRS1, MST2;KIAA0583 PDLG","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6717,"ComplexName":"KCNQ3-KCNQ5 complex","Organism":"Human","Synonyms":"Kv7.3-Kv7,5 complex","Cell.line":"brain","subunits.UniProt.IDs.":"O43525;Q9NR82","subunits.Entrez.IDs.":"3786;56479","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0071805;GO:0005249;GO:0007268","GO.description":"potassium ion transmembrane transport;voltage-gated potassium channel activity;synaptic transmission","FunCat.ID":"34.03.01","FunCat.description":"synaptic transmission","PubMed.ID":12890507,"subunits.Protein.name.":"Potassium voltage-gated channel subfamily KQT member 3;Potassium voltage-gated channel subfamily KQT member 5","subunits.Gene.name.":"KCNQ3;KCNQ5","subunits.Gene.name.syn.":"BFNC2, EBN2, KV7.3;Kv7.5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6718,"ComplexName":"CALM1-KCNQ4(splice variant 1) complex","Organism":"Human","Synonyms":"CaM-Kv7.4(splice variant 1) complex","Cell.line":"None","subunits.UniProt.IDs.":"P56696-;P62158","subunits.Entrez.IDs.":"9132;801","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0043266","GO.description":"regulation of potassium ion transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26515070,"subunits.Protein.name.":"Potassium voltage-gated channel subfamily KQT member 4;Calmodulin","subunits.Gene.name.":"KCNQ4;CALM1; CAL","subunits.Gene.name.syn.":"DFNA2, DFNA2A, KV7.4;CALM, CAM, CAM1, CAM2, CAMB, CALML2, CAM3, CAMC, CAMIII","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6719,"ComplexName":"CALM1- KCNQ4(splice variant 2) complex","Organism":"Human","Synonyms":"CaM-Kv4.1(splice varian 2) complex","Cell.line":"None","subunits.UniProt.IDs.":"P56696-2;P62158","subunits.Entrez.IDs.":"9132;801","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0043266","GO.description":"regulation of potassium ion transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26515070,"subunits.Protein.name.":"Potassium voltage-gated channel subfamily KQT member 4;Calmodulin","subunits.Gene.name.":"KCNQ4;CALM1; CAL","subunits.Gene.name.syn.":"DFNA2, DFNA2A, KV7.4;CALM, CAM, CAM1, CAM2, CAMB, CALML2, CAM3, CAMC, CAMIII","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6720,"ComplexName":"FILIP1-FLNA complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"P21333;Q7Z7B0","subunits.Entrez.IDs.":"2316;27145","Protein.complex.purification.method":"MI:0096-pull down","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23087206,"subunits.Protein.name.":"Filamin-A;Filamin-A-interacting protein 1","subunits.Gene.name.":"FLNA;FILIP1","subunits.Gene.name.syn.":"FLN, FLN1;KIAA1275","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"FILIP1 is a RhoD/Rif effector and an FLNa-binding protein.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6721,"ComplexName":"CALM1-KCNQ2-KCNQ3 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"O88944;P62161;Q9Z351","subunits.Entrez.IDs.":"29682;24242;16536","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0043266","GO.description":"regulation of potassium ion transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":24333508,"subunits.Protein.name.":"Potassium voltage-gated channel subfamily KQT member 3;Calmodulin;Potassium voltage-gated channel subfamily KQT member 2","subunits.Gene.name.":"Kcnq3;Calm1; Cal;Kcnq2","subunits.Gene.name.syn.":"None;Calm, Cam, Cam1, Cam2, Camb, Cam3, Camc;Kqt2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Mus musculus (Mouse)"}
{"ComplexID":6722,"ComplexName":"FILIP1-RhoD complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"O00212;Q7Z7B0","subunits.Entrez.IDs.":"29984;27145","Protein.complex.purification.method":"MI:0047-far western blotting;MI:0096-pull down","GO.ID":"GO:0046847;GO:0051017","GO.description":"filopodium assembly;actin filament bundle assembly","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23087206,"subunits.Protein.name.":"Rho-related GTP-binding protein RhoD;Filamin-A-interacting protein 1","subunits.Gene.name.":"RHOD;FILIP1","subunits.Gene.name.syn.":"ARHD;KIAA1275","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"RhoD induces the formation of filopodia and actin bundles and binds FILIP1 in a GTP-dependent manner.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6723,"ComplexName":"Grk6-Ags3-Galphai2 complex, CXCL8 activated","Organism":"Mammalia","Synonyms":"Grk6-Gpsm1-Gnai2 complex, CXCL8 activated","Cell.line":"RBL-2H3 cells (rat basophilic leukemia cells), expressing CXCR2, human neutrophils, murine neutrophi","subunits.UniProt.IDs.":"O70293;P08752;Q6IR34","subunits.Entrez.IDs.":"26385;14678;67839","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0070098","GO.description":"chemokine-mediated signaling pathway","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":24510965,"subunits.Protein.name.":"G protein-coupled receptor kinase 6;Guanine nucleotide-binding protein G;G-protein-signaling modulator 1","subunits.Gene.name.":"Grk6;Gnai2;Gpsm1","subunits.Gene.name.syn.":"Gprk6;Gnai-2;Ags3,C10a","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"AGS3 complexes with Galphai2 and GRK6 to modulate CXCR2-mediated cellular functions including second messenger production, MAP kinase activation and chemotaxis.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6724,"ComplexName":"WHAMM-RhoD complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"O00212;Q8TF30","subunits.Entrez.IDs.":"29984;123720","Protein.complex.purification.method":"MI:0096-pull down","GO.ID":"GO:0031532","GO.description":"actin cytoskeleton reorganization","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23087206,"subunits.Protein.name.":"Rho-related GTP-binding protein RhoD;WASP homolog-associated protein with actin, membranes and microtubules","subunits.Gene.name.":"RHOD;WHAMM","subunits.Gene.name.syn.":"ARHD;KIAA1971,WHDC1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"WHAMM is required for RhoD-dependent actin reorganization. RhoD binds WHAMM in a GTP-dependent manner.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6725,"ComplexName":"ARP3-WHAMM complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293T cell","subunits.UniProt.IDs.":"P61158;Q8TF30","subunits.Entrez.IDs.":"10096;123720","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0031532","GO.description":"actin cytoskeleton reorganization","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23087206,"subunits.Protein.name.":"Actin-related protein 3;WASP homolog-associated protein with actin, membranes and microtubules","subunits.Gene.name.":"ACTR3;WHAMM","subunits.Gene.name.syn.":"ARP3;KIAA1971,WHDC1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"WHAMM is required for RhoD-dependent actin reorganization and binds to the Arp2/3 complex. The presence of the Arp2/3 complex in the immunoprecipitates was revealed using antibodies against Arp3A.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6726,"ComplexName":"GRASP1-GRIP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"Q4V328;Q9Y3R0","subunits.Entrez.IDs.":"56850;23426","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005088","GO.description":"Ras guanyl-nucleotide exchange factor activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":10896157,"subunits.Protein.name.":"GRIP1-associated protein 1;Glutamate receptor-interacting protein 1","subunits.Gene.name.":"GRIPAP1;GRIP1","subunits.Gene.name.syn.":"KIAA1167;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6727,"ComplexName":"Grasp1-Grip1-Glur2 complex","Organism":"Rat","Synonyms":"Grasp1-Grip1-AMPA receptor complex","Cell.line":"cortical neurons","subunits.UniProt.IDs.":"P19491;P97879;Q9JHZ4","subunits.Entrez.IDs.":"29627;84016;116493","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0008039;GO:0005088;GO:2000311","GO.description":"synaptic target recognition;Ras guanyl-nucleotide exchange factor activity;regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":10896157,"subunits.Protein.name.":"Glutamate receptor 2;Glutamate receptor-interacting protein 1;GRIP1-associated protein 1","subunits.Gene.name.":"Gria2;Grip1;Gripap1","subunits.Gene.name.syn.":"Glur2;None;Grasp1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6728,"ComplexName":"9-1-1-RHINO complex","Organism":"Human","Synonyms":"RHINO-Rad9-Hus1-Rad1 complex","Cell.line":"HEK293 Flp-In T-REx cells; transfected Sf21 cells","subunits.UniProt.IDs.":"O60671;O60921;Q99638;Q9BSD3","subunits.Entrez.IDs.":"5810;3364;5883;83695","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0000077;GO:0006281;GO:0000785;GO:0005634","GO.description":"DNA damage checkpoint;DNA repair;chromatin;nucleus","FunCat.ID":"10.01.05.01;70.10","FunCat.description":"DNA repair;nucleus","PubMed.ID":25602520,"subunits.Protein.name.":"Cell cycle checkpoint protein RAD1;Checkpoint protein HUS1;Cell cycle checkpoint control protein RAD9A;RAD9, HUS1, RAD1-interacting nuclear orphan protein 1","subunits.Gene.name.":"RAD1;HUS1;RAD9A;RHNO1","subunits.Gene.name.syn.":"REC1;None;None;C12orf32,RHINO,HKMT1188","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6729,"ComplexName":"IQGAP1-CXCR2 complex","Organism":"Human","Synonyms":"None","Cell.line":"differentiated HL-60 cells, overexpressing CXCR2","subunits.UniProt.IDs.":"P25025;P46940","subunits.Entrez.IDs.":"3579;8826","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0070098","GO.description":"chemokine-mediated signaling pathway","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":21876773,"subunits.Protein.name.":"C-X-C chemokine receptor type 2;Ras GTPase-activating-like protein IQGAP1","subunits.Gene.name.":"CXCR2;IQGAP1","subunits.Gene.name.syn.":"IL8RB;KIAA0051","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The signaling scaffolding protein IQGAP1 was consistently identified with both the unstimulated and activated receptor immunoprecipitations. CXCR2 colocalizes with IQGAP1 at the leading edge of polarized human neutrophils.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6730,"ComplexName":"14-3-3 gamma-CXCR2 complex, unstimulated","Organism":"Human","Synonyms":"YWHAG-CXCR2 complex, unstimulated","Cell.line":"differentiated HL-60 cells, overexpressing CXCR2","subunits.UniProt.IDs.":"P25025;P61981","subunits.Entrez.IDs.":"3579;7532","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":21876773,"subunits.Protein.name.":"C-X-C chemokine receptor type 2;14-3-3 protein gamma","subunits.Gene.name.":"CXCR2;YWHAG","subunits.Gene.name.syn.":"IL8RB;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The interaction of CXCR2 with 14-3-3 gamma represents a potential novel link to signaling pathways through its function as an adaptor molecule that is a known regulator of G-protein signaling (RGS) proteins.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6731,"ComplexName":"VASP-CXCR2 complex, CXCL8 stimulated","Organism":"Human","Synonyms":"None","Cell.line":"differentiated HL-60 cells, overexpressing CXCR2","subunits.UniProt.IDs.":"P25025;P50552","subunits.Entrez.IDs.":"3579;7408","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0030036","GO.description":"actin cytoskeleton organization","FunCat.ID":"42.04.03","FunCat.description":"actin cytoskeleton","PubMed.ID":21876773,"subunits.Protein.name.":"C-X-C chemokine receptor type 2;Vasodilator-stimulated phosphoprotein","subunits.Gene.name.":"CXCR2;VASP","subunits.Gene.name.syn.":"IL8RB;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The actin regulating protein VASP may provide a link betweenthe activated chemokine receptor and the acting cytoskeleton.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6732,"ComplexName":"RHINO-TopBP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293 Flp-In T-REx cells; transfected Sf21 cells","subunits.UniProt.IDs.":"Q92547;Q9BSD3","subunits.Entrez.IDs.":"11073;83695","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0006281;GO:0000077;GO:0000785;GO:0005634","GO.description":"DNA repair;DNA damage checkpoint;chromatin;nucleus","FunCat.ID":"10.01.05.01;70.10","FunCat.description":"DNA repair;nucleus","PubMed.ID":25602520,"subunits.Protein.name.":"DNA topoisomerase 2-binding protein 1;RAD9, HUS1, RAD1-interacting nuclear orphan protein 1","subunits.Gene.name.":"TOPBP1;RHNO1","subunits.Gene.name.syn.":"KIAA0259;C12orf32,RHINO,HKMT1188","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6733,"ComplexName":"9b-1-1 complex","Organism":"Human","Synonyms":"RAD9B-HUS1-RAD1 complex","Cell.line":"K562 cells","subunits.UniProt.IDs.":"O60671;O60921;Q6WBX8","subunits.Entrez.IDs.":"5810;3364;144715","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0006281;GO:0000077;GO:0005634","GO.description":"DNA repair;DNA damage checkpoint;nucleus","FunCat.ID":"10.01.05.01;70.10","FunCat.description":"DNA repair;nucleus","PubMed.ID":14611806,"subunits.Protein.name.":"Cell cycle checkpoint protein RAD1;Checkpoint protein HUS1;Cell cycle checkpoint control protein RAD9B","subunits.Gene.name.":"RAD1;HUS1;RAD9B","subunits.Gene.name.syn.":"REC1;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6734,"ComplexName":"9b-1b-1 complex","Organism":"Human","Synonyms":"RAD9B-HUS1B-RAD1 complex","Cell.line":"K562 cells","subunits.UniProt.IDs.":"O60671;Q6WBX8;Q8NHY5","subunits.Entrez.IDs.":"5810;144715;135458","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0005634;GO:0000077;GO:0006281","GO.description":"nucleus;DNA damage checkpoint;DNA repair","FunCat.ID":"70.10;10.01.05.01","FunCat.description":"nucleus;DNA repair","PubMed.ID":14611806,"subunits.Protein.name.":"Cell cycle checkpoint protein RAD1;Cell cycle checkpoint control protein RAD9B;Checkpoint protein HUS1B","subunits.Gene.name.":"RAD1;RAD9B;HUS1B","subunits.Gene.name.syn.":"REC1;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6735,"ComplexName":"SIGMAR1-KCNH2 complex","Organism":"Human","Synonyms":"sigma-1 receptor-hERG complex","Cell.line":"HEK-293 cells","subunits.UniProt.IDs.":"Q12809;Q99720","subunits.Entrez.IDs.":"3757;10280","Protein.complex.purification.method":"MI:0051-fluorescence technologies","GO.ID":"GO:1901379","GO.description":"regulation of potassium ion transmembrane transport","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25266722,"subunits.Protein.name.":"Potassium voltage-gated channel subfamily H member 2;Sigma non-opioid intracellular receptor 1","subunits.Gene.name.":"KCNH2;SIGMAR1","subunits.Gene.name.syn.":"ERG, ERG1, HERG;OPRS1, SRBP, AAG8","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6736,"ComplexName":"PRAME-Cullin2 ubiquitin ligase complex","Organism":"Human","Synonyms":"None","Cell.line":"K562 cells","subunits.UniProt.IDs.":"P78395;Q13617","subunits.Entrez.IDs.":"23532;8453","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0005634;GO:0003682;GO:0016567","GO.description":"nucleus;chromatin binding;protein ubiquitination","FunCat.ID":"70.10;14.07.05","FunCat.description":"nucleus;modification by ubiquitination, deubiquitination","PubMed.ID":21822215,"subunits.Protein.name.":"Melanoma antigen preferentially expressed in tumors;Cullin-2","subunits.Gene.name.":"PRAME;CUL2","subunits.Gene.name.syn.":"MAPE,OIP4;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6737,"ComplexName":"H2A-H2B-TDIF2-PCNA complex","Organism":"Human","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P12004;Q16777;Q16778;Q5QJE6","subunits.Entrez.IDs.":"5111;8338;8349;30836","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006338;GO:0005634;GO:0003677","GO.description":"chromatin remodeling;nucleus;DNA binding","FunCat.ID":"70.10;16.03.01","FunCat.description":"nucleus;DNA binding","PubMed.ID":12786946,"subunits.Protein.name.":"Proliferating cell nuclear antigen;Histone H2A type 2-C;Histone H2B type 2-E;Deoxynucleotidyltransferase terminal-interacting protein 2","subunits.Gene.name.":"PCNA;HIST2H2AC;HIST2H2BE;DNTTIP2","subunits.Gene.name.syn.":"None;H2AFQ;H2BFQ;ERBP, TDIF2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TdIF2 takes H2A/H2B away from the core histone in the presence of PCNA to form aH2A-H2B-TdIF2-PCNA complex, indicating that TdIF2 functions as a chromatin remodeling protein.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6738,"ComplexName":"PRAME-ElonginBC ubiquitin ligase","Organism":"Human","Synonyms":"None","Cell.line":"K562 cells","subunits.UniProt.IDs.":"P78395;Q15369;Q15370","subunits.Entrez.IDs.":"23532;6921;6923","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0003682;GO:0005634;GO:0016567","GO.description":"chromatin binding;nucleus;protein ubiquitination","FunCat.ID":"70.10;14.07.05","FunCat.description":"nucleus;modification by ubiquitination, deubiquitination","PubMed.ID":21822215,"subunits.Protein.name.":"Melanoma antigen preferentially expressed in tumors;Transcription elongation factor B polypeptide 1;Transcription elongation factor B polypeptide 2","subunits.Gene.name.":"PRAME;TCEB1;TCEB2","subunits.Gene.name.syn.":"MAPE,OIP4;elongin c;elongin b","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6740,"ComplexName":"AURKA-INPP5E complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"O14965;Q9NRR6","subunits.Entrez.IDs.":"6790;56623","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0005929;GO:0048015;GO:0061523","GO.description":"cilium;phosphatidylinositol-mediated signaling;cilium disassembly","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25395580,"subunits.Protein.name.":"Aurora kinase A;72 kDa inositol polyphosphate 5-phosphatase","subunits.Gene.name.":"AURKA;INPP5E","subunits.Gene.name.syn.":"AIK, AIRK1, ARK1, AURA, AYK1, BTAK, IAK1, STK15, STK6;JBTS1, MORMS","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6741,"ComplexName":"INPP5E-PDE6D-RPGR complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"O43924;Q92834;Q9NRR6","subunits.Entrez.IDs.":"5147;6103;56623","Protein.complex.purification.method":"MI:0676-tandem affinity purification","GO.ID":"GO:0061512","GO.description":"protein localization to cilium","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":27554114,"subunits.Protein.name.":"Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta;X-linked retinitis pigmentosa GTPase regulator;72 kDa inositol polyphosphate 5-phosphatase","subunits.Gene.name.":"PDE6D;RPGR;INPP5E","subunits.Gene.name.syn.":"PDED;RP3, XLRP3;JBTS1, MORMS","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6742,"ComplexName":"SMG1-UPF2-Y14-MAGOH-UPF3B-EIF4A3 complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"P38919;P61326;Q96Q15;Q9BZI7;Q9HAU5;Q9Y5S9","subunits.Entrez.IDs.":"9775;4116;23049;65109;26019;9939","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0000184","GO.description":"nuclear-transcribed mRNA catabolic process, nonsense-mediated decay","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":16452507,"subunits.Protein.name.":"Eukaryotic initiation factor 4A-III;Protein mago nashi homolog;Serine/threonine-protein kinase SMG1;Regulator of nonsense transcripts 3B;Regulator of nonsense transcripts 2;RNA-binding protein 8A","subunits.Gene.name.":"EIF4A3;MAGOH;SMG1;UPF3B;UPF2;RBM8A","subunits.Gene.name.syn.":"DDX48, KIAA0111;MAGOHA;ATX, KIAA0421, LIP;RENT3B, UPF3X;KIAA1408, RENT2;RBM8, Y14","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SMG-1 associates with the known EJC components Upf2, Y14, Magoh, Upf3b, and eIF4A3 through the CD region in the absence of RNA.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6743,"ComplexName":"AHI1-NPHP1 heterodimer","Organism":"Human","Synonyms":"None","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"O15259;Q8N157","subunits.Entrez.IDs.":"4867;54806","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0060271","GO.description":"cilium assembly","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23532844,"subunits.Protein.name.":"Nephrocystin-1;Jouberin","subunits.Gene.name.":"NPHP1;AHI1","subunits.Gene.name.syn.":"NPH1;JBTS3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6744,"ComplexName":"AHI1-HAP1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"P54257;Q8N157","subunits.Entrez.IDs.":"9001;54806","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0018-two hybrid","GO.ID":"GO:0007420","GO.description":"brain development","FunCat.ID":"47.03.01.01.01","FunCat.description":"brain","PubMed.ID":23532844,"subunits.Protein.name.":"Huntingtin-associated protein 1;Jouberin","subunits.Gene.name.":"HAP1;AHI1","subunits.Gene.name.syn.":"HAP2, HLP1;JBTS3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6745,"ComplexName":"Fgf12-Nav1.2 complex","Organism":"Rat","Synonyms":"Fgf12-Scn2a complex","Cell.line":"rat brain","subunits.UniProt.IDs.":"P04775;P61150","subunits.Entrez.IDs.":"24766;170630","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0663-confocal microscopy","GO.ID":"GO:0034706;GO:0005272;GO:0099610;GO:0043194","GO.description":"sodium channel complex;sodium channel activity;action potential initiation;axon initial segment","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25724910,"subunits.Protein.name.":"Sodium channel protein type 2 subunit alpha;Fibroblast growth factor 12","subunits.Gene.name.":"Scn2a;Fgf12","subunits.Gene.name.syn.":"Scn2a1, Nav1.2;Fhf1, Fhf1b","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Using confocal microscopy native FGF12 was visualized in the brain tissue and confirmed that FGF12 forms a complex with Nav1.2 channels at the axonal initial segment, the subcellular specialized domain of neurons required for action potential initiation. Co-immunoprecipitation studies in a heterologous expression system validate Nav1.2 and FGF12 as interactors.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6746,"ComplexName":"Fhf1b-Nav1.9 complex","Organism":"Rat","Synonyms":"Fgf12-Scn11a complex","Cell.line":"brain","subunits.UniProt.IDs.":"O88457;P61150","subunits.Entrez.IDs.":"29701;170630","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0096-pull down;MI:0047-far western blotting","GO.ID":"GO:0005272","GO.description":"sodium channel activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":11376006,"subunits.Protein.name.":"Sodium channel protein type 11 subunit alpha;Fibroblast growth factor 12","subunits.Gene.name.":"Scn11a;Fgf12","subunits.Gene.name.syn.":"Nan, Sns2, Nav1.9, Nav1.9a;Fhf1, Fhf1b","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"FHF1B binds directly to the C-terminal polypeptide of rNa(v)1.9a both in vitro and in mammalian cell lines. Although the functional significance of this interaction is not clear, FHF1B may affect the rNa(v)1.9a channel directly or by recruiting other proteins to the channel complex. Alternatively, it is possible that rNa(v)1.9a may help deliver this factor to the cell membrane, where it exerts its function.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6747,"ComplexName":"AQP1 homotetramer","Organism":"Human","Synonyms":"Aquaporin complex","Cell.line":"erythrocyte","subunits.UniProt.IDs.":"P29972","subunits.Entrez.IDs.":"358","Protein.complex.purification.method":"MI:0040-electron microscopy","GO.ID":"GO:0006833;GO:0005372","GO.description":"water transport;water transmembrane transporter activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":7693713,"subunits.Protein.name.":"Aquaporin-1","subunits.Gene.name.":"AQP1","subunits.Gene.name.syn.":"CHIP28","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human)"}
{"ComplexID":6748,"ComplexName":"KCNMA1-LRRC26 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"Q12791;Q2I0M4","subunits.Entrez.IDs.":"3778;389816","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20613726,"subunits.Protein.name.":"Calcium-activated potassium channel subunit alpha-1;Leucine-rich repeat-containing protein 26","subunits.Gene.name.":"KCNMA1;LRRC26","subunits.Gene.name.syn.":"KCNMA SLO;CAPC","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6749,"ComplexName":"ITGB1BP1-KRIT1-RAP1A complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"Baby Hamster Kidney (BHK) cells","subunits.UniProt.IDs.":"O00522;O14713;P62834","subunits.Entrez.IDs.":"889;9270;5906","Protein.complex.purification.method":"MI:0096-pull down","GO.ID":"GO:0005546;GO:0005886","GO.description":"phosphatidylinositol-4,5-bisphosphate binding;plasma membrane","FunCat.ID":"70.02","FunCat.description":"eukaryotic plasma membrane / membrane attached","PubMed.ID":17916086,"subunits.Protein.name.":"Krev interaction trapped protein 1;Integrin beta-1-binding protein 1;Ras-related protein Rap-1A","subunits.Gene.name.":"KRIT1;ITGB1BP1;RAP1A","subunits.Gene.name.syn.":"CCM1;ICAP1;KREV1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6750,"ComplexName":"AHI1-NPHP1 heterotetramer","Organism":"Human","Synonyms":"None","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"O15259;Q8N157","subunits.Entrez.IDs.":"4867;54806","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0060271","GO.description":"cilium assembly","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23532844,"subunits.Protein.name.":"Nephrocystin-1;Jouberin","subunits.Gene.name.":"NPHP1;AHI1","subunits.Gene.name.syn.":"NPH1;JBTS3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6751,"ComplexName":"Stx7-Unc13d-Vamp8 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"B2RUP2;O70404;O70439","subunits.Entrez.IDs.":"70450;22320;53331","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0006897;GO:0005768","GO.description":"endocytosis;endosome","FunCat.ID":"20.09.18.09.01;70.22","FunCat.description":"endocytosis;endosome","PubMed.ID":26680738,"subunits.Protein.name.":"Protein unc-13 homolog D;Vesicle-associated membrane protein 8;Syntaxin-7","subunits.Gene.name.":"Unc13d;Vamp8;Stx7","subunits.Gene.name.syn.":"Munc13-4;None;Syn7","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6752,"ComplexName":"Smad3-mSin3A-Hdac1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"cardiac fibroblasts","subunits.UniProt.IDs.":"O09106;Q60520;Q8BUN5","subunits.Entrez.IDs.":"433759;20466;17127","Protein.complex.purification.method":"MI:0402-chromatin immunoprecipitation assays","GO.ID":"GO:0045892","GO.description":"negative regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.03","FunCat.description":"transcription repression","PubMed.ID":27941310,"subunits.Protein.name.":"Histone deacetylase 1;Paired amphipathic helix protein Sin3a;Mothers against decapentaplegic homolog 3","subunits.Gene.name.":"Hdac1;Sin3a;Smad3","subunits.Gene.name.syn.":"None;Kiaa4126;Madh3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"TGF-beta-1-induced inhibition of Pparg transcription depends on formation of a functional transcriptional regulatory complex that includes Smad3, mSin3A and Hdac1 at the Pparg promoter.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6753,"ComplexName":"SOG complex","Organism":"Human","Synonyms":"SZT2-orchestrated GATOR complex; SZT2\\u2013GATOR1\\u2013GATOR2 complex","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"P55735;Q12980;Q5T011;Q6PJI9;Q8WTW4;Q96EE3;Q96S15;Q9NXC5","subunits.Entrez.IDs.":"6396;8131;23334;79726;10641;81929;84219;54468","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation;MI:0071-molecular sieving","GO.ID":"GO:0032418;GO:1904262","GO.description":"lysosome localization;negative regulation of TORC1 signaling","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":28199315,"subunits.Protein.name.":"Protein SEC13 homolog;Nitrogen permease regulator 3-like protein;Protein SZT2;WD repeat-containing protein 59;Nitrogen permease regulator 2-like protein;Nucleoporin SEH1;WD repeat-containing protein 24;WD repeat-containing protein mio","subunits.Gene.name.":"SEC13;NPRL3;SZT2;WDR59;NPRL2;SEH1L;WDR24;MIOS","subunits.Gene.name.syn.":"D3S1231E SEC13L1 SEC13R;C16orf35 CGTHBA MARE;C1orf84,KIAA0467;KIAA1923;TUSC4;SEC13L SEH1;C16orf21;None","Disease.comment":"Mutations in the metazoan-specific SZT2 gene cause epilepsy, a disease frequently associated with mTORC1 hyperactivation.SZT2 deficiency results in constitutive mTORC1 signalling in cells under nutrient-deprived conditions and neonatal lethality in mice, which was associated with failure to inactivate mTORC1 during fasting.","Subunits.comment":"None","Complex.comment":"The SOG complex has a molecular weight of around 1.06 MDa.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6754,"ComplexName":"KICSTOR complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"Q5T011;Q969R8;Q96MD2;Q9Y664","subunits.Entrez.IDs.":"23334;55846;144577;11133","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation;MI:0071-molecular sieving","GO.ID":"GO:0032418;GO:1904262;GO:0010506","GO.description":"lysosome localization;negative regulation of TORC1 signaling;regulation of autophagy","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":28199306,"subunits.Protein.name.":"Protein SZT2;Integrin-alpha FG-GAP repeat-containing protein 2;UPF0536 protein C12orf66;Kaptin","subunits.Gene.name.":"SZT2;ITFG2;C12orf66;KPTN","subunits.Gene.name.syn.":"C1orf84,KIAA0467;None;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"KICSTOR localizes to lysosomes; binds andrecruits GATOR1, but not GATOR2, to the lysosomal surface; and is necessary for the interaction of GATOR1 with its substrates, the Rag GTPases, and with GATOR2.HEK293T cells that lack any of the KICSTOR subunits, amino acid deprivation did not inhibit mTORC1 signalling, or induce autophagy.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6755,"ComplexName":"DYRK1A-HAN11 complex","Organism":"Rabbit","Synonyms":"DYRK1A-DCAF7 complex","Cell.line":"rabbit skeletal muscle","subunits.UniProt.IDs.":"G1TAE4;P85051","subunits.Entrez.IDs.":"100347842;None","Protein.complex.purification.method":"MI:0227-reverse phase chromatography;MI:0226-ion exchange chromatography","GO.ID":"GO:0006468;GO:0070873","GO.description":"protein phosphorylation;regulation of glycogen metabolic process","FunCat.ID":"14.07.03","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation","PubMed.ID":14593110,"subunits.Protein.name.":"Uncharacterized protein;Dual specificity tyrosine-phosphorylation-regulated kinase 1A","subunits.Gene.name.":"DCAF7;DYRK1A","subunits.Gene.name.syn.":"None;DYRK","Disease.comment":"None","Subunits.comment":"Experimental results  indicate that the 3a-kinase is an oligomeric protein.","Complex.comment":"DYRK1A-HAN11 complex inactivates glycogen synthase by phosphorylation of site 3a.","SWISSPROT.organism":"Oryctolagus cuniculus (Rabbit);Oryctolagus cuniculus (Rabbit)"}
{"ComplexID":6756,"ComplexName":"RasGAP-AURKB-survivin complex","Organism":"Human","Synonyms":"None","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O15392;P20936;Q96GD4","subunits.Entrez.IDs.":"332;5921;9212","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0096-pull down","GO.ID":"GO:0007186;GO:0000278;GO:0051726","GO.description":"G-protein coupled receptor signaling pathway;mitotic cell cycle;regulation of cell cycle","FunCat.ID":"30.05.02.24;10.03.01.01;10.03.01","FunCat.description":"G-protein coupled receptor signalling pathway;mitotic cell cycle;mitotic cell cycle and cell cycle control","PubMed.ID":11976319,"subunits.Protein.name.":"Baculoviral IAP repeat-containing protein 5;Ras GTPase-activating protein 1;Aurora kinase B","subunits.Gene.name.":"BIRC5;RASA1;AURKB","subunits.Gene.name.syn.":"API4, IAP4;GAP, RASA;AIK2, AIM1, AIRK2, ARK2 STK1, STK12, STK5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors define this ternary complex by several protein-protein interactions. RasGAP binds to the kinase domain of Aurora and this interaction inhibits the kinase activity of AURKA and AURKB.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6757,"ComplexName":"DYRK1B-HAN11 complex","Organism":"Rabbit","Synonyms":"DYRK1B-DCAF7 complex","Cell.line":"COSM9 cells","subunits.UniProt.IDs.":"G1TAE4;G1U355","subunits.Entrez.IDs.":"100347842;None","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0006468;GO:0070874","GO.description":"protein phosphorylation;negative regulation of glycogen metabolic process","FunCat.ID":"14.07.03","FunCat.description":"modification by phosphorylation, dephosphorylation, autophosphorylation","PubMed.ID":14593110,"subunits.Protein.name.":"Uncharacterized protein;Uncharacterized protein","subunits.Gene.name.":"DCAF7;DYRK1B","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The DYRK1B-HAN11 complex inactivates glycogen synthase by phosphorylation of site 3a.","SWISSPROT.organism":"Oryctolagus cuniculus (Rabbit);Oryctolagus cuniculus (Rabbit)"}
{"ComplexID":6758,"ComplexName":"IL10 receptor","Organism":"Human","Synonyms":"Interleukin-10 receptor","Cell.line":"peripheral blood mononuclear cells","subunits.UniProt.IDs.":"Q08334;Q13651","subunits.Entrez.IDs.":"3588;3587","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0050728;GO:0042100;GO:0070662","GO.description":"negative regulation of inflammatory response;B cell proliferation;mast cell proliferation","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":9312047,"subunits.Protein.name.":"Interleukin-10 receptor subunit beta;Interleukin-10 receptor subunit alpha","subunits.Gene.name.":"IL10RB;IL10RA","subunits.Gene.name.syn.":"CRFB4,D21S58,D21S66;IL10R","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6759,"ComplexName":"Vangl1-Dvl1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"E13.5 mouse embryos","subunits.UniProt.IDs.":"P51141;Q80Z96","subunits.Entrez.IDs.":"13542;229658","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation;MI:0096-pull down;MI:0018-two hybrid","GO.ID":"GO:0005886","GO.description":"plasma membrane","FunCat.ID":"70.02","FunCat.description":"eukaryotic plasma membrane / membrane attached","PubMed.ID":15456783,"subunits.Protein.name.":"Segment polarity protein dishevelled homolog DVL-1;Vang-like protein 1","subunits.Gene.name.":"Dvl1;Vangl1","subunits.Gene.name.syn.":"Dvl;Lpp2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6760,"ComplexName":"Vangl1-Dvl2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"E13.5 mouse embryos","subunits.UniProt.IDs.":"Q60838;Q80Z96","subunits.Entrez.IDs.":"13543;229658","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation;MI:0096-pull down;MI:0018-two hybrid","GO.ID":"GO:0005886","GO.description":"plasma membrane","FunCat.ID":"70.02","FunCat.description":"eukaryotic plasma membrane / membrane attached","PubMed.ID":15456783,"subunits.Protein.name.":"Segment polarity protein dishevelled homolog DVL-2;Vang-like protein 1","subunits.Gene.name.":"Dvl2;Vangl1","subunits.Gene.name.syn.":"None;Lpp2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6761,"ComplexName":"Vangl1-Dvl3 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"E13.5 mouse embryos","subunits.UniProt.IDs.":"Q61062;Q80Z96","subunits.Entrez.IDs.":"13544;229658","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation;MI:0096-pull down;MI:0018-two hybrid","GO.ID":"GO:0005886","GO.description":"plasma membrane","FunCat.ID":"70.02","FunCat.description":"eukaryotic plasma membrane / membrane attached","PubMed.ID":15456783,"subunits.Protein.name.":"Segment polarity protein dishevelled homolog DVL-3;Vang-like protein 1","subunits.Gene.name.":"Dvl3;Vangl1","subunits.Gene.name.syn.":"None;Lpp2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6762,"ComplexName":"Vangl2-Dvl1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"E13.5 mouse embryos","subunits.UniProt.IDs.":"P51141;Q91ZD4","subunits.Entrez.IDs.":"13542;93840","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation;MI:0096-pull down;MI:0018-two hybrid","GO.ID":"GO:0005886","GO.description":"plasma membrane","FunCat.ID":"70.02","FunCat.description":"eukaryotic plasma membrane / membrane attached","PubMed.ID":15456783,"subunits.Protein.name.":"Segment polarity protein dishevelled homolog DVL-1;Vang-like protein 2","subunits.Gene.name.":"Dvl1;Vangl2","subunits.Gene.name.syn.":"Dvl;Lpp1, Ltap","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6763,"ComplexName":"Vangl2-Dvl2 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"E13.5 mouse embryos","subunits.UniProt.IDs.":"Q60838;Q91ZD4","subunits.Entrez.IDs.":"13543;93840","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation;MI:0096-pull down;MI:0018-two hybrid","GO.ID":"GO:0005886","GO.description":"plasma membrane","FunCat.ID":"70.02","FunCat.description":"eukaryotic plasma membrane / membrane attached","PubMed.ID":15456783,"subunits.Protein.name.":"Segment polarity protein dishevelled homolog DVL-2;Vang-like protein 2","subunits.Gene.name.":"Dvl2;Vangl2","subunits.Gene.name.syn.":"None;Lpp1, Ltap","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6764,"ComplexName":"Vangl2-Dvl3 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"E13.5 mouse embryos","subunits.UniProt.IDs.":"Q61062;Q91ZD4","subunits.Entrez.IDs.":"13544;93840","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation;MI:0096-pull down;MI:0018-two hybrid","GO.ID":"GO:0005886","GO.description":"plasma membrane","FunCat.ID":"70.02","FunCat.description":"eukaryotic plasma membrane / membrane attached","PubMed.ID":15456783,"subunits.Protein.name.":"Segment polarity protein dishevelled homolog DVL-3;Vang-like protein 2","subunits.Gene.name.":"Dvl3;Vangl2","subunits.Gene.name.syn.":"None;Lpp1, Ltap","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6765,"ComplexName":"CCR4-NOT complex","Organism":"Human","Synonyms":"None","Cell.line":"HE K293 cells","subunits.UniProt.IDs.":"A5YKK6;O75175;Q92600;Q96LI5;Q9H9A5;Q9NZN8;Q9UIV1;Q9UKZ1;Q9ULM6","subunits.Entrez.IDs.":"23019;4849;9125;246175;25904;4848;29883;55571;57472","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0030014;GO:0043928;GO:0003723;GO:0006355","GO.description":"CCR4-NOT complex;exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay;RNA binding;regulation of transcription, DNA-templated","FunCat.ID":"16.03.03;11.02.03.04","FunCat.description":"RNA binding;transcriptional control","PubMed.ID":23232451,"subunits.Protein.name.":"CCR4-NOT transcription complex subunit 1;CCR4-NOT transcription complex subunit 3;Cell differentiation protein RCD1 homolog;CCR4-NOT transcription complex subunit 6-like;CCR4-NOT transcription complex subunit 10;CCR4-NOT transcription complex subunit 2;CCR4-NOT transcription complex subunit 7;CCR4-NOT transcription complex subunit 11;CCR4-NOT transcription complex subunit 6","subunits.Gene.name.":"CNOT1;CNOT3;RQCD1;CNOT6L;CNOT10;CNOT2;CNOT7;CNOT11;CNOT6","subunits.Gene.name.syn.":"CDC39 KIAA1007 NOT1;KIAA0691 LENG2 NOT3;CNOT9,RCD1;CCR4B;None;CDC36 NOT2;CAF1;C2orf29,C40;CCR4 CCR4a KIAA1194","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In eukaryotes, degradation of functional mRNAs is most often initiated by progressive shortening of their poly(A) tails. This step is predominantly catalyzed by two interacting deadenylases called CCR4 and CAF1.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6766,"ComplexName":"Arnt-Ahrr complex","Organism":"Mouse","Synonyms":"None","Cell.line":"None","subunits.UniProt.IDs.":"P53762;Q3U1U7","subunits.Entrez.IDs.":"11863;11624","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0009410","GO.description":"response to xenobiotic stimulus","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":9887096,"subunits.Protein.name.":"Aryl hydrocarbon receptor nuclear translocator;Aryl hydrocarbon receptor repressor","subunits.Gene.name.":"Arnt;Ahrr","subunits.Gene.name.syn.":"None;Kiaa1234","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6767,"ComplexName":"GCH1-GCHFR complex","Organism":"Rat","Synonyms":"None","Cell.line":"liver","subunits.UniProt.IDs.":"P22288;P70552","subunits.Entrez.IDs.":"29244;171128","Protein.complex.purification.method":"MI:0004-affinity chromatography technologies","GO.ID":"GO:0046146","GO.description":"tetrahydrobiopterin metabolic process","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":8702680,"subunits.Protein.name.":"GTP cyclohydrolase 1;GTP cyclohydrolase 1 feedback regulatory protein","subunits.Gene.name.":"Gch1;Gchfr","subunits.Gene.name.syn.":"Gch;Gfrp","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"In the presence of tetrahydrobiopterin (BH4) GCHFR binds to GTP cyclohydrolase 1 thus inhibiting GCH1 activity.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6768,"ComplexName":"TBX20-TBX18 repressor complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"O95935;Q9UMR3","subunits.Entrez.IDs.":"9096;57057","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0045892","GO.description":"negative regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.03","FunCat.description":"transcription repression","PubMed.ID":24024827,"subunits.Protein.name.":"T-box transcription factor TBX18;T-box transcription factor TBX20","subunits.Gene.name.":"TBX18;TBX20","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6769,"ComplexName":"TBX20-TLE1 repressor complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"Q04724;Q9UMR3","subunits.Entrez.IDs.":"7088;57057","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0045892;GO:0007507","GO.description":"negative regulation of transcription, DNA-templated;heart development","FunCat.ID":"11.02.03.04.03;45.03.12.03","FunCat.description":"transcription repression;heart muscle","PubMed.ID":24024827,"subunits.Protein.name.":"Transducin-like enhancer protein 1;T-box transcription factor TBX20","subunits.Gene.name.":"TLE1;TBX20","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6770,"ComplexName":"TBX20-TLE3 repressor complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"Q04726;Q9UMR3","subunits.Entrez.IDs.":"7090;57057","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0007507;GO:0045892","GO.description":"heart development;negative regulation of transcription, DNA-templated","FunCat.ID":"45.03.12.03;11.02.03.04.03","FunCat.description":"heart muscle;transcription repression","PubMed.ID":24024827,"subunits.Protein.name.":"Transducin-like enhancer protein 3;T-box transcription factor TBX20","subunits.Gene.name.":"TLE3;TBX20","subunits.Gene.name.syn.":"KIAA1547;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6771,"ComplexName":"TBX20-HDAC2 repressor complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293cells","subunits.UniProt.IDs.":"Q92769;Q9UMR3","subunits.Entrez.IDs.":"3066;57057","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0045892","GO.description":"negative regulation of transcription, DNA-templated","FunCat.ID":"11.02.03.04.03","FunCat.description":"transcription repression","PubMed.ID":24024827,"subunits.Protein.name.":"Histone deacetylase 2;T-box transcription factor TBX20","subunits.Gene.name.":"HDAC2;TBX20","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6772,"ComplexName":"Tbx20-Tle1 repressor complex","Organism":"Mouse","Synonyms":"None","Cell.line":"embryonic heart","subunits.UniProt.IDs.":"Q62440;Q9ES03","subunits.Entrez.IDs.":"21885;57246","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0045892;GO:0007507","GO.description":"negative regulation of transcription, DNA-templated;heart development","FunCat.ID":"11.02.03.04.03;45.03.12.03","FunCat.description":"transcription repression;heart muscle","PubMed.ID":24024827,"subunits.Protein.name.":"Transducin-like enhancer protein 1;T-box transcription factor TBX20","subunits.Gene.name.":"Tle1;Tbx20","subunits.Gene.name.syn.":"Grg1;Tbx12","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This demonstrates that Tbx20 assembles a TLE repressor complex in the embryonic heart at the time at which Tbx20 functions in cardiacdevelopment.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6773,"ComplexName":"Tbx20-Tle3 repressor complex","Organism":"Mouse","Synonyms":"None","Cell.line":"embryonic heart","subunits.UniProt.IDs.":"Q08122;Q9ES03","subunits.Entrez.IDs.":"21887;57246","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0045892;GO:0007507","GO.description":"negative regulation of transcription, DNA-templated;heart development","FunCat.ID":"11.02.03.04.03;45.03.12.03","FunCat.description":"transcription repression;heart muscle","PubMed.ID":24024827,"subunits.Protein.name.":"Transducin-like enhancer protein 3;T-box transcription factor TBX20","subunits.Gene.name.":"Tle3;Tbx20","subunits.Gene.name.syn.":"Esg;Tbx12","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"This demonstrates that Tbx20 assembles a TLErepressor complex in the embryonic heart at the time at which Tbx20 functions in cardiac development.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6774,"ComplexName":"Fhl1-Pdlim1-Gsn-Actn1 complex","Organism":"Mouse","Synonyms":"None","Cell.line":"cardiac ventricle lysates","subunits.UniProt.IDs.":"O70400;P13020;P97447;Q7TPR4","subunits.Entrez.IDs.":"54132;227753;14199;109711","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation;MI:0416-fluorescence microscopy","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":21246116,"subunits.Protein.name.":"PDZ and LIM domain protein 1;Gelsolin;Four and a half LIM domains protein 1;Alpha-actinin-1","subunits.Gene.name.":"Pdlim1;Gsn;Fhl1;Actn1","subunits.Gene.name.syn.":"Clim1;Gsb;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Endogenous immunoprecipitation of the complex has been shown in wild type mouse  and transgenic R9C cardiac ventricle lysates using anti-FHL1 antibody.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6775,"ComplexName":"Pdlim1-Alpha-actinin-1 complex","Organism":"Rat","Synonyms":"Clp36-Alpha-actinin-1 complex","Cell.line":"PC12 cells, dorsal root ganglion neurons","subunits.UniProt.IDs.":"P52944;Q9Z1P2","subunits.Entrez.IDs.":"54133;81634","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0030036;GO:0031175","GO.description":"actin cytoskeleton organization;neuron projection development","FunCat.ID":"42.04.03","FunCat.description":"actin cytoskeleton","PubMed.ID":19780892,"subunits.Protein.name.":"PDZ and LIM domain protein 1;Alpha-actinin-1","subunits.Gene.name.":"Pdlim1;Actn1","subunits.Gene.name.syn.":"Clim1,Clp36;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Clp36 and a-actinin form protein complexes in undifferentiated PC12 cells andthese complexes are recruited to the growth cones after stimulation by NGF.","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6776,"ComplexName":"Igfn1-Ky-Flnc complex","Organism":"Mouse","Synonyms":"None","Cell.line":"C2C12 myotubes","subunits.UniProt.IDs.":"Q3KNY0;Q8C8H8;Q8VHX6","subunits.Entrez.IDs.":"226438;None;68794","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0030018;GO:0045214","GO.description":"Z disc;sarcomere organization","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20206623,"subunits.Protein.name.":"Immunoglobulin-like and fibronectin type III domain-containing protein 1;Kyphoscoliosis peptidase;Filamin-C","subunits.Gene.name.":"Igfn1;Ky;Flnc","subunits.Gene.name.syn.":"None;None;Abpl,Fln2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Yeast two-hybrid, biochemical and immunofluorescence data support the notion that KY, IGFN1 and FLNC are part of a Z-band associated protein complex likely to provide structural support to the skeletal muscle sarcomere.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6777,"ComplexName":"SCRIB-NOS1AP-VANGL1 complex","Organism":"Human","Synonyms":"None","Cell.line":"MDA-MB-231 breast cancer cells","subunits.UniProt.IDs.":"O75052;Q14160;Q8TAA9","subunits.Entrez.IDs.":"9722;23513;81839","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation;MI:0416-fluorescence microscopy","GO.ID":"GO:0007163;GO:0016477;GO:0030027","GO.description":"establishment or maintenance of cell polarity;cell migration;lamellipodium","FunCat.ID":"34.05.01","FunCat.description":"cell migration","PubMed.ID":22179838,"subunits.Protein.name.":"Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein;Protein scribble homolog;Vang-like protein 1","subunits.Gene.name.":"NOS1AP;SCRIB;VANGL1","subunits.Gene.name.syn.":"CAPON,KIAA0464;CRIB1, KIAA0147, LAP4, SCRB1, VARTUL;STB2","Disease.comment":"The data point to the relevance of NOS1AP and SCRIB protein complexes in breast cancer.","Subunits.comment":"None","Complex.comment":"NOS1AP colocalizes with both SCRIB and VANGL1 along cellular protrusions in metastatic breast cancer cells, but does not colocalize with either SCRIB or VANGL1 at cell junctions in normal breast cells. SCRIB, NOS1AP and VANGL1 regulate the migration of human breast cancer cells.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6778,"ComplexName":"SCRIB-ARHGEF7-PAK1-GIT1 complex","Organism":"Human","Synonyms":"None","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"Q13153;Q14155;Q14160;Q9Y2X7","subunits.Entrez.IDs.":"5058;8874;23513;28964","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007163;GO:0016477","GO.description":"establishment or maintenance of cell polarity;cell migration","FunCat.ID":"34.05.01","FunCat.description":"cell migration","PubMed.ID":22179838,"subunits.Protein.name.":"Serine/threonine-protein kinase PAK 1;Rho guanine nucleotide exchange factor 7;Protein scribble homolog;ARF GTPase-activating protein GIT1","subunits.Gene.name.":"PAK1;ARHGEF7;SCRIB;GIT1","subunits.Gene.name.syn.":"None;COOL1, KIAA0142, P85SPR, PAK3BP, PIXB;CRIB1, KIAA0147, LAP4, SCRB1, VARTUL;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SCRIB associates independently with ARHGEF\\u2013PAK\\u2013GIT protein complexes and with NOS1AP\\u2013VANGL protein complexes.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6779,"ComplexName":"SCRIB-GIT1-ARHGEF7-PAK complex","Organism":"Human","Synonyms":"SCRIB-GIT1-beta-PIX and PAK complex","Cell.line":"T47D human breast cancer cells","subunits.UniProt.IDs.":"Q13153;Q14155;Q14160;Q9Y2X7","subunits.Entrez.IDs.":"5058;8874;23513;28964","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0016477;GO:0031252;GO:0007163","GO.description":"cell migration;cell leading edge;establishment or maintenance of cell polarity","FunCat.ID":"34.05.01","FunCat.description":"cell migration","PubMed.ID":18716323,"subunits.Protein.name.":"Serine/threonine-protein kinase PAK 1;Rho guanine nucleotide exchange factor 7;Protein scribble homolog;ARF GTPase-activating protein GIT1","subunits.Gene.name.":"PAK1;ARHGEF7;SCRIB;GIT1","subunits.Gene.name.syn.":"None;COOL1, KIAA0142, P85SPR, PAK3BP, PIXB;CRIB1, KIAA0147, LAP4, SCRB1, VARTUL;None","Disease.comment":"None","Subunits.comment":"Since the authors did not specify PAK, we used isoform PAK1.","Complex.comment":"The data demonstrate that the HRG (heregulin b1, a growth factor triggering cell motility)-dependent migration of T47D cells is controlled by the ability of Scrib to interact with the beta-PIX-PAK complex.Scrib interacts with the beta-PIX-PAK protein complex and is required for the retention of the protein complex at the leading edge of migratory cells.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6780,"ComplexName":"RAD6A-KCMF1-UBR4 complex","Organism":"Human","Synonyms":"UBE2A-KCMF1-UBR4 complex","Cell.line":"HEK 293 T-REx cells","subunits.UniProt.IDs.":"P49459;Q5T4S7;Q9P0J7","subunits.Entrez.IDs.":"7319;23352;56888","Protein.complex.purification.method":"MI:0400-affinity technologies","GO.ID":"GO:1905146","GO.description":"lysosomal protein catabolic process","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25582440,"subunits.Protein.name.":"Ubiquitin-conjugating enzyme E2 A;E3 ubiquitin-protein ligase UBR4;E3 ubiquitin-protein ligase KCMF1","subunits.Gene.name.":"UBE2A;UBR4;KCMF1","subunits.Gene.name.syn.":"RAD6A;KIAA0462,KIAA1307,RBAF600,ZUBR1;FIGC, ZZZ1","Disease.comment":"Two different RAD6A point mutants (R7W and R11Q) found inX-linked intellectual disability (XLID) patients specifically losethe interactions with KCMF1 and UBR4.","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6781,"ComplexName":"Cpt1a-Acsl1-Vdac1 complex","Organism":"Rat","Synonyms":"None","Cell.line":"liver mitochondrial outer membrane","subunits.UniProt.IDs.":"P18163;P32198;Q9Z2L0","subunits.Entrez.IDs.":"25288;25757;83529","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0015908;GO:0005741","GO.description":"fatty acid transport;mitochondrial outer membrane","FunCat.ID":"70.16.01","FunCat.description":"mitochondrial outer membrane","PubMed.ID":21622568,"subunits.Protein.name.":"Long-chain-fatty-acid--CoA ligase 1;Carnitine O-palmitoyltransferase 1, liver isoform;Voltage-dependent anion-selective channel protein 1","subunits.Gene.name.":"Acsl1;Cpt1a;Vdac1","subunits.Gene.name.syn.":"Acs1,Acsl2,Facl2;Cpt1;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"None","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6782,"ComplexName":"mitochondrial permeability  transition pore (PTP) complex (PPIF-SPG7-VDAC1)","Organism":"Human","Synonyms":"PPIF-SPG7-VDAC1 complex","Cell.line":"HEK293T cells, HeLa cells, COS7 cells","subunits.UniProt.IDs.":"P21796;P30405;Q9UQ90","subunits.Entrez.IDs.":"7416;10105;6687","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0051882;GO:0005743;GO:0005741","GO.description":"mitochondrial depolarization;mitochondrial inner membrane;mitochondrial outer membrane","FunCat.ID":"70.16.05;70.16.01","FunCat.description":"mitochondrial inner membrane;mitochondrial outer membrane","PubMed.ID":26387735,"subunits.Protein.name.":"Voltage-dependent anion-selective channel protein 1;Peptidyl-prolyl cis-trans isomerase F, mitochondrial;Paraplegin","subunits.Gene.name.":"VDAC1;PPIF;SPG7","subunits.Gene.name.syn.":"VDAC;CYP3, Cyp-D, CypD;CAR,PGN","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"SPG7 is a core component of the PTP (permeability  transition pore) which not only interacts with matrix protein CypD (PPIF) but also with the OMM channel VDAC1 at OMM/IMM (outer mitochondrial membrane/inner mitochondrial membrane) contact sites. Silencing or disruption of SPG7-CypD binding prevented Ca2+ and ROS-induced mitochondrial membrane potential depolarization and cell death.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6783,"ComplexName":"CLIC5A-EZR-PODXL complex","Organism":"Human","Synonyms":"CLIC5A-Ezrin-podocalyxin complex","Cell.line":"renal glomeruli","subunits.UniProt.IDs.":"O00592;P15311;Q9NZA1","subunits.Entrez.IDs.":"5420;7430;53405","Protein.complex.purification.method":"MI:0663-confocal microscopy","GO.ID":"GO:0098846;GO:0031532","GO.description":"podocyte foot;actin cytoskeleton reorganization","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20335315,"subunits.Protein.name.":"Podocalyxin;Ezrin;Chloride intracellular channel protein 5","subunits.Gene.name.":"PODXL;EZR;CLIC5","subunits.Gene.name.syn.":"PCLP, PCLP1;VIL2;None","Disease.comment":"The authors postulate that the interaction between podocalyxin and subjacentfilamentous actin, which requires ezrin, is compromised in podocytes of CLIC5A-deficient mice, leading to dysfunction under unfavorable genetic or environmental conditions.","Subunits.comment":"None","Complex.comment":"Ezrin and podocalyxin colocalize with CLIC5A in glomeruli, and podocalyxin coimmunoprecipitates with CLIC5A from glomerular lysates.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6784,"ComplexName":"SCHIP1-EZR-NHERF2 complex","Organism":"Human","Synonyms":"SCHIP1-EZR-SLC9A3R2 complex","Cell.line":"cultured podocytes","subunits.UniProt.IDs.":"P15311;Q15599;Q9P0W5","subunits.Entrez.IDs.":"7430;9351;100505385","Protein.complex.purification.method":"MI:0663-confocal microscopy;MI:0055-fluorescent resonance energy transfer","GO.ID":"GO:0098846;GO:0031532","GO.description":"podocyte foot;actin cytoskeleton reorganization","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25807495,"subunits.Protein.name.":"Ezrin;Na(+)/H(+) exchange regulatory cofactor NHE-RF2;Schwannomin-interacting protein 1","subunits.Gene.name.":"EZR;SLC9A3R2;SCHIP1","subunits.Gene.name.syn.":"VIL2;NHERF2;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The authors propose that Schip1 is an adaptor protein in complex with ezrin-Nherf2 that links actin cytoskeleton to the podocyte foot process plasma membrane and mediates its dynamics in response to PDGF-beta.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6785,"ComplexName":"Podxl-Nherf2-Ezr complex","Organism":"Rat","Synonyms":"Podocalyxin-Nherf2-ezrin complex","Cell.line":"glomerular lysates","subunits.UniProt.IDs.":"P31977;Q920G2;Q9WTQ2","subunits.Entrez.IDs.":"54319;116501;192181","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0031532;GO:0098846;GO:0003094","GO.description":"actin cytoskeleton reorganization;podocyte foot;glomerular filtration","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":11457882,"subunits.Protein.name.":"Ezrin;Na(+)/H(+) exchange regulatory cofactor NHE-RF2;Podocalyxin","subunits.Gene.name.":"Ezr;Slc9a3r2;Podxl","subunits.Gene.name.syn.":"Vil2;Nherf2;Pclp1","Disease.comment":"Treatments that affect foot process organization of GECs  (glomerular epithelium cells) disrupt the PC/NHERF2/ezrin/actin cytoskeleton association.","Subunits.comment":"None","Complex.comment":"The results indicate that PC (Podocalyxin, Podxl), NHERF2, and ezrin associate in a multimeric complex along the apical PM (plasma membrane) of GEC (glomerular epithelium cells).","SWISSPROT.organism":"Rattus norvegicus (Rat);Rattus norvegicus (Rat);Rattus norvegicus (Rat)"}
{"ComplexID":6787,"ComplexName":"NHE3-NHERF2-ACTN4, Ca(2+) induced","Organism":"Human","Synonyms":"NHE3-E3KARP-alpha-actinin-4 complex","Cell.line":"PS120/NHE3V/E3KARP fibroblast cells stably transfected with ACTN4","subunits.UniProt.IDs.":"O43707;P48764;Q15599","subunits.Entrez.IDs.":"81;6550;9351","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation;MI:0663-confocal microscopy","GO.ID":"GO:0002028;GO:0006885","GO.description":"regulation of sodium ion transport;regulation of pH","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":11948184,"subunits.Protein.name.":"Alpha-actinin-4;Sodium/hydrogen exchanger 3;Na(+)/H(+) exchange regulatory cofactor NHE-RF2","subunits.Gene.name.":"ACTN4;SLC9A3;SLC9A3R2","subunits.Gene.name.syn.":"None;NHE3;NHERF2","Disease.comment":"Inhibition of Na(+)/H(+) exchange induced by elevation of Ca(2+) is involved in normal intestinal physiology and in the pathophysiology of diarrheal disease (PMID: 2873653).","Subunits.comment":"None","Complex.comment":"E3KARP (NHERF2) is specifically involved in the inhibition of NHE3 activity by elevation of Ca(2+) through an interaction with ACTN4. Elevation of Ca(2+) induces NHE3 oligomerization and endocytosis of NHE3 with formation of a protein complex containing NHE3, E3KARP (NHERF2), and ACTN4.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6788,"ComplexName":"SLC9A3R1-ACTN4 complex","Organism":"Human","Synonyms":"NHERF1-Alpha-actinin-4 complex","Cell.line":"HeLa cells","subunits.UniProt.IDs.":"O14745;O43707","subunits.Entrez.IDs.":"9368;81","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0096-pull down","GO.ID":"GO:0030036","GO.description":"actin cytoskeleton organization","FunCat.ID":"42.04.03","FunCat.description":"actin cytoskeleton","PubMed.ID":26432781,"subunits.Protein.name.":"Na(+)/H(+) exchange regulatory cofactor NHE-RF1;Alpha-actinin-4","subunits.Gene.name.":"SLC9A3R1;ACTN4","subunits.Gene.name.syn.":"NHERF, NHERF1;None","Disease.comment":"The results indicate that NHERF1 may regulate tumor cell invasion and metastasis through modulation of a-actinin-4 protein expression levels.","Subunits.comment":"None","Complex.comment":"The NHERF1/a-actinin-4 interaction increased a-actinin-4 ubiquitination and decreased its expression levels, resulting in actin cytoskeleton disassembly.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6789,"ComplexName":"PTEN-NHERF1-EGFR complex","Organism":"Human","Synonyms":"PTEN-EBP50-EGFR complex","Cell.line":"COS-7 cells, U-373 MG (U373) cells","subunits.UniProt.IDs.":"O14745;P00533;P60484","subunits.Entrez.IDs.":"9368;1956;5728","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0096-pull down","GO.ID":"GO:0051898","GO.description":"negative regulation of protein kinase B signaling","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26531778,"subunits.Protein.name.":"Na(+)/H(+) exchange regulatory cofactor NHE-RF1;Epidermal growth factor receptor;Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN","subunits.Gene.name.":"SLC9A3R1;EGFR;PTEN","subunits.Gene.name.syn.":"NHERF, NHERF1;ERBB, ERBB1, HER1;MMAC1, TEP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The PTEN-EBP50-EGFR complex attenuated EGF-induced AKT signaling. The disruption of this complex led to an increase of EGF-induced AKT activation level.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6790,"ComplexName":"NHERF1-PRKCZ complex","Organism":"Human","Synonyms":"EBP50-PKC Zeta complex; SLC9A3R1-PRKCZ complex","Cell.line":"CHO cells, transfected","subunits.UniProt.IDs.":"O14745;Q05513","subunits.Entrez.IDs.":"9368;5590","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0007249","GO.description":"I-kappaB kinase/NF-kappaB signaling","FunCat.ID":"30.01.05.01.04","FunCat.description":"NIK-I-kappaB/NF-kappaB cascade","PubMed.ID":24196963,"subunits.Protein.name.":"Na(+)/H(+) exchange regulatory cofactor NHE-RF1;Protein kinase C zeta type","subunits.Gene.name.":"SLC9A3R1;PRKCZ","subunits.Gene.name.syn.":"NHERF, NHERF1;PKC2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Inflammatory stimuli promote the formation of an EBP50-PKC-Zeta complex at the cell membrane that induces NF-kappaB signaling.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6791,"ComplexName":"NHERF1-NPT2A-EZR complex","Organism":"Human","Synonyms":"Npt2a-NHERF1-ezrin complex","Cell.line":"OKH cells (a subclone of opossum kidney (OK)), transfected","subunits.UniProt.IDs.":"O14745;P15311;Q06495","subunits.Entrez.IDs.":"9368;7430;6569","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0006817;GO:0071374","GO.description":"phosphate ion transport;cellular response to parathyroid hormone stimulus","FunCat.ID":"20.01.01.07.07","FunCat.description":"phosphate transport","PubMed.ID":22628548,"subunits.Protein.name.":"Na(+)/H(+) exchange regulatory cofactor NHE-RF1;Ezrin;Sodium-dependent phosphate transport protein 2A","subunits.Gene.name.":"SLC9A3R1;EZR;SLC34A1","subunits.Gene.name.syn.":"NHERF, NHERF1;VIL2;NPT2, SLC17A2, NPTIIa","Disease.comment":"The failure to assemble and regulate the Npt2a-NHERF1-ezrin ternary complex is responsible for the loss of function of the NHERF1 mutants and defines a novel molecular mechanism of PTH (parathyroid hormone) resistance and hyperphosphaturia.","Subunits.comment":"None","Complex.comment":"The NHERF1 ternary complex is required for PTH (parathyroid hormone)-sensitive Pi (phosphate) transport. Mutations in Npt2a, NHERF1, or ezrin that interfere with theformation of the ternary complex or its phosphorylation impedes the normal function and regulatory influence of PTH.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6792,"ComplexName":"NHERF1-ARRB2-PTH1R complex, PTH stimulated","Organism":"Mammalia","Synonyms":"NHERF1-beta-arrestin2-PTHR, PTH stimulated","Cell.line":"HEK 293T cells","subunits.UniProt.IDs.":"O14745;P32120;Q03431","subunits.Entrez.IDs.":"9368;None;5745","Protein.complex.purification.method":"MI:0663-confocal microscopy;MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0007188;GO:0004991","GO.description":"adenylate cyclase-modulating G-protein coupled receptor signaling pathway;parathyroid hormone receptor activity","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20656684,"subunits.Protein.name.":"Na(+)/H(+) exchange regulatory cofactor NHE-RF1;Beta-arrestin-2;Parathyroid hormone/parathyroid hormone-related peptide receptor","subunits.Gene.name.":"SLC9A3R1;ARRB2;PTH1R","subunits.Gene.name.syn.":"NHERF, NHERF1;None;PTHR, PTHR1","Disease.comment":"None","Subunits.comment":"For cDNA constructs the authors used human NHERF1, human PTH1R and bovine beta-arrestin2.","Complex.comment":"Although NHERF1 interacts constitutively with the PTHR, beta-arrestin2 binding is promoted by receptor activation.","SWISSPROT.organism":"Homo sapiens (Human);Bos taurus (Bovine);Homo sapiens (Human)"}
{"ComplexID":6793,"ComplexName":"PDZK1-NHERF1-EZR complex","Organism":"Human","Synonyms":"PDZK1-EBP50-ezrin complex","Cell.line":"JEG3 cells, LLC-PK1 cells","subunits.UniProt.IDs.":"O14745;P15311;Q5T2W1","subunits.Entrez.IDs.":"9368;7430;5174","Protein.complex.purification.method":"MI:0096-pull down","GO.ID":"GO:0032528","GO.description":"microvillus organization","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":20237154,"subunits.Protein.name.":"Na(+)/H(+) exchange regulatory cofactor NHE-RF1;Ezrin;Na(+)/H(+) exchange regulatory cofactor NHE-RF3","subunits.Gene.name.":"SLC9A3R1;EZR;PDZK1","subunits.Gene.name.syn.":"NHERF, NHERF1;VIL2;CAP70, NHERF3, PDZD1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"PDZK1 shuttles from the nucleus in low con?uence cells to microvilli in high con?uence cells, and this regulates the formation of the PDZK1/EBP50/ezrin complex in vivo.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6794,"ComplexName":"LPAR2-TRIP6-NHERF2 complex, LPA stimulated","Organism":"Mammalia","Synonyms":"LPAR2-TRIP6-SLC9A3R2 complex, LPA stimulated","Cell.line":"SKOV-3 cells, HEK 293T cells, LPA1/2 double knock-out  mouse embryonic fibroblasts","subunits.UniProt.IDs.":"Q15599;Q15654;Q9HBW0","subunits.Entrez.IDs.":"9351;7205;9170","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0416-fluorescence microscopy","GO.ID":"GO:0043066","GO.description":"negative regulation of apoptotic process","FunCat.ID":"40.10.02.01","FunCat.description":"anti-apoptosis","PubMed.ID":19293149,"subunits.Protein.name.":"Na(+)/H(+) exchange regulatory cofactor NHE-RF2;Thyroid receptor-interacting protein 6;Lysophosphatidic acid receptor 2","subunits.Gene.name.":"SLC9A3R2;TRIP6;LPAR2","subunits.Gene.name.syn.":"NHERF2;OIP1;EDG4, LPA2","Disease.comment":"The LPA2-mediated antiapoptotic effect was abolished only when both CXXC- and PDZ-binding motifs were disrupted, indicating that the supramolecular complexes formed via the C-terminal tail of LPA2 are required for the full antiapoptotic function of LPA2, and thus play a critical role in the chemoprotective action of LPA in can-cer cells.","Subunits.comment":"None","Complex.comment":"LPA2-TRIP6-NHERF2 ternary complex provides a novel ligand-dependent signal amplification mechanism that is required for LPA2-mediated full activation of antiapoptotic signaling. LPA2, TRIP6, and NHERF2 colocalize in cells as shown in LPA1/2 DKO MEFs (LPA1/2 double knock-out  mouse embryonic fibroblasts) by fluorescence microscopy.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6795,"ComplexName":"LPAR2-SIVA1 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"HEK 293T cells, LPA1/2 double knock-out mouse embryonic fibroblasts","subunits.UniProt.IDs.":"O15304;Q9HBW0","subunits.Entrez.IDs.":"10572;9170","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0416-fluorescence microscopy","GO.ID":"GO:0042981","GO.description":"regulation of apoptotic process","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":19293149,"subunits.Protein.name.":"Apoptosis regulatory protein Siva;Lysophosphatidic acid receptor 2","subunits.Gene.name.":"SIVA1;LPAR2","subunits.Gene.name.syn.":"SIVA;EDG4, LPA2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Siva-1 colocalized with LPA2 and S1P4 but not S1P1 in the cytosol in LPA1/2 DKO MEFs (double knock-out mouse embryonic fibroblasts).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6796,"ComplexName":"SIVA1-S1PR4 complex","Organism":"Mammalia","Synonyms":"SIVA1-S1P4 complex","Cell.line":"HEK 293T cells, LPA1/2 double knock-out mouse embryonic fibroblasts","subunits.UniProt.IDs.":"O15304;O95977","subunits.Entrez.IDs.":"10572;8698","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0416-fluorescence microscopy","GO.ID":"None","GO.description":"None","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":19293149,"subunits.Protein.name.":"Apoptosis regulatory protein Siva;Sphingosine 1-phosphate receptor 4","subunits.Gene.name.":"SIVA1;S1PR4","subunits.Gene.name.syn.":"SIVA;EDG6, S1P4","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Siva-1 colocalized with LPA2 and S1P4 but not S1P1 in the cytosol in LPA1/2 DKO MEFs (double knock-out mouse embryonic fibroblasts).","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6797,"ComplexName":"LPAR2-SIVA1 complex","Organism":"Mammalia","Synonyms":"None","Cell.line":"HEK 293T cells, HeLa cells, LPA1/2 double knock-out mouse embryonic fibroblasts, NIH 3T3 cells","subunits.UniProt.IDs.":"O15304;Q9HBW0","subunits.Entrez.IDs.":"10572;9170","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0416-fluorescence microscopy","GO.ID":"GO:0042981","GO.description":"regulation of apoptotic process","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":17965021,"subunits.Protein.name.":"Apoptosis regulatory protein Siva;Lysophosphatidic acid receptor 2","subunits.Gene.name.":"SIVA1;LPAR2","subunits.Gene.name.syn.":"SIVA;EDG4, LPA2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"Endogenous Siva-1 was found to co-immunoprecipitate with the LPA2receptor in DKO-LPA2 MEFs (LPA1/2 double knock-out mouse embryonic fibroblasts).Prolonged LPA stimulation promotes the association of Siva-1 with the LPA2receptor and targets both proteins for ubiquitination and degradation.Siva-1 is predominantly present in the nucleus but co-localizes with the LPA2receptor in the cytosol or on the plasma membrane","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6798,"ComplexName":"S1PR1-c-Met-ITGB4 complex, HGF- or S1P-induced","Organism":"Human","Synonyms":"c-Met signaling complex, HGF- or S1P-induced","Cell.line":"Human lung microvascular EC (endothelial cells), (HLMVEC), Human pulmonary artery EC (HPAEC)","subunits.UniProt.IDs.":"P08581;P16144;P21453","subunits.Entrez.IDs.":"4233;3691;1901","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0061028;GO:0045121","GO.description":"establishment of endothelial barrier;membrane raft","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":23212923,"subunits.Protein.name.":"Hepatocyte growth factor receptor;Integrin beta-4;Sphingosine 1-phosphate receptor 1","subunits.Gene.name.":"MET;ITGB4;S1PR1","subunits.Gene.name.syn.":"None;None;CHEDG1, EDG1, S1P1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The c-Met-S1PR1-ITGB4 complex is dynamically regulated within the lipid rafts in response to HGF.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6799,"ComplexName":"VEGFR2-S1PR1-ERK1/2-PKC-alpha complex","Organism":"Human","Synonyms":"None","Cell.line":"ML-1 thyroid follicular cancer cells","subunits.UniProt.IDs.":"P17252;P21453;P27361;P28482;P35968","subunits.Entrez.IDs.":"5578;1901;5595;5594;3791","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0016477;GO:0070371","GO.description":"cell migration;ERK1 and ERK2 cascade","FunCat.ID":"34.05.01","FunCat.description":"cell migration","PubMed.ID":20501673,"subunits.Protein.name.":"Protein kinase C alpha type;Sphingosine 1-phosphate receptor 1;Mitogen-activated protein kinase 3;Mitogen-activated protein kinase 1;Vascular endothelial growth factor receptor 2","subunits.Gene.name.":"PRKCA;S1PR1;MAPK3;MAPK1;KDR","subunits.Gene.name.syn.":"PKCA PRKACA;CHEDG1, EDG1, S1P1;ERK1, PRKM3;ERK2, PRKM1, PRKM2;FLK1, VEGFR2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"S1P receptors form complexes with VEGFR-2 and the S1P1/VEGFR-2 complex associates with protein kinase C (PKC)-alpha and ERK1/2.The authors hypothesize that VEGFR-2 forms a signaling complex with S1P1, evoking bidirectional signaling regulating both ERK1/2 phosphorylation and haptotaxis of ML-1 cells.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6800,"ComplexName":"VEGFR2-S1PR2-ERK1/2-PKC-alpha complex","Organism":"Human","Synonyms":"KDR-S1P2-ERK1/2-PKC-alpha complex","Cell.line":"ML-1 thyroid follicular cancer cells","subunits.UniProt.IDs.":"O95136;P17252;P27361;P28482;P35968","subunits.Entrez.IDs.":"9294;5578;5595;5594;3791","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0016477;GO:0070371","GO.description":"cell migration;ERK1 and ERK2 cascade","FunCat.ID":"34.05.01","FunCat.description":"cell migration","PubMed.ID":20501673,"subunits.Protein.name.":"Sphingosine 1-phosphate receptor 2;Protein kinase C alpha type;Mitogen-activated protein kinase 3;Mitogen-activated protein kinase 1;Vascular endothelial growth factor receptor 2","subunits.Gene.name.":"S1PR2;PRKCA;MAPK3;MAPK1;KDR","subunits.Gene.name.syn.":"EDG5, S1P2;PKCA PRKACA;ERK1, PRKM3;ERK2, PRKM1, PRKM2;FLK1, VEGFR2","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"S1P receptors form complexes with VEGFR-2 and the S1P2/VEGFR-2 complex associates with protein kinase C (PKC)-alpha and ERK1/2.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6801,"ComplexName":"VEGFR2-S1PR3-ERK1/2-PKC-alpha complex","Organism":"Human","Synonyms":"KDR-S1P3-ERK1/2-PKC-alpha complex","Cell.line":"ML-1 thyroid follicular cancer cells","subunits.UniProt.IDs.":"P17252;P27361;P28482;P35968;Q99500","subunits.Entrez.IDs.":"5578;5595;5594;3791;1903","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0016477;GO:0070371","GO.description":"cell migration;ERK1 and ERK2 cascade","FunCat.ID":"34.05.01","FunCat.description":"cell migration","PubMed.ID":20501673,"subunits.Protein.name.":"Protein kinase C alpha type;Mitogen-activated protein kinase 3;Mitogen-activated protein kinase 1;Vascular endothelial growth factor receptor 2;Sphingosine 1-phosphate receptor 3","subunits.Gene.name.":"PRKCA;MAPK3;MAPK1;KDR;S1PR3","subunits.Gene.name.syn.":"PKCA PRKACA;ERK1, PRKM3;ERK2, PRKM1, PRKM2;FLK1, VEGFR2;EDG3, S1P3","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"S1P receptors form complexes with VEGFR-2 and the S1P3/VEGFR-2 complex associates with protein kinase C (PKC)-alpha and ERK1/2.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6802,"ComplexName":"VEGFR2-S1PR5-ERK1/2-PKC-alpha complex","Organism":"Human","Synonyms":"KDR-S1P5-ERK1/2-PKC-alpha complex","Cell.line":"ML-1 thyroid follicular cancer cells","subunits.UniProt.IDs.":"P17252;P27361;P28482;P35968;Q9H228","subunits.Entrez.IDs.":"5578;5595;5594;3791;53637","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0016477;GO:0070371","GO.description":"cell migration;ERK1 and ERK2 cascade","FunCat.ID":"34.05.01","FunCat.description":"cell migration","PubMed.ID":20501673,"subunits.Protein.name.":"Protein kinase C alpha type;Mitogen-activated protein kinase 3;Mitogen-activated protein kinase 1;Vascular endothelial growth factor receptor 2;Sphingosine 1-phosphate receptor 5","subunits.Gene.name.":"PRKCA;MAPK3;MAPK1;KDR;S1PR5","subunits.Gene.name.syn.":"PKCA PRKACA;ERK1, PRKM3;ERK2, PRKM1, PRKM2;FLK1, VEGFR2;EDG8, S1P5","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"S1P receptors form complexes with VEGFR-2 and the S1P5/VEGFR-2 complex associates with protein kinase C (PKC)-alpha and ERK1/2.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6803,"ComplexName":"Pdgfbr-S1pr1 complex","Organism":"Mammalia","Synonyms":"PDGF-beta receptor-S1P1 receptor complex","Cell.line":"ASM (Airway smooth muscle) cells of guinea pig","subunits.UniProt.IDs.":"H0V6S9;H0V7G9","subunits.Entrez.IDs.":"None;100723228","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0070371","GO.description":"ERK1 and ERK2 cascade","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":12480944,"subunits.Protein.name.":"Platelet-derived growth factor receptor beta;Uncharacterized protein","subunits.Gene.name.":"PDGFRB;S1PR1","subunits.Gene.name.syn.":"None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"These receptors are co-internalized together as a functional signaling unit to regulate the p42/p44 MAPK pathway (ERK1/ERK2).","SWISSPROT.organism":"Cavia porcellus (Guinea pig);Cavia porcellus (Guinea pig)"}
{"ComplexID":6804,"ComplexName":"Pdgfrb-S1pr1-phosphorylated p42/p44 Mapk complex, PDGF stimulated","Organism":"Mammalia","Synonyms":"None","Cell.line":"ASM (Airway smooth muscle) cells of guinea pig","subunits.UniProt.IDs.":"H0V0F7;H0V6S9;H0V7G9;H0VMU3","subunits.Entrez.IDs.":"None;None;100723228;None","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0070371","GO.description":"ERK1 and ERK2 cascade","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":12480944,"subunits.Protein.name.":"Mitogen-activated protein kinase;Platelet-derived growth factor receptor beta;Uncharacterized protein;Mitogen-activated protein kinase","subunits.Gene.name.":"MAPK3;PDGFRB;S1PR1;MAPK1","subunits.Gene.name.syn.":"None;None;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The treatment of ASM cells with PDGF-AB stimulated the phosphorylation of p42/p44 MAPK (ERK1/ERK2), and this phosphorylated p42/p44 MAPK associates with the PDGF-beta receptor-S1P1 receptor complex.S1P and PDGF promoted the co-internalization of PDG-beta receptor andS1P1 receptor in the same endocytic vesicles.","SWISSPROT.organism":"Cavia porcellus (Guinea pig);Cavia porcellus (Guinea pig);Cavia porcellus (Guinea pig);Cavia porcellus (Guinea pig)"}
{"ComplexID":6805,"ComplexName":"S1PR1\\u2013beta-arrestin 2 complex, ApoM(+)HDL-S1P stimulated","Organism":"Human","Synonyms":"S1P1-ARRB2 complex,  ApoM(+)HDL-S1P stimulated","Cell.line":"HUVECs (Human umbilical vein endothelial cells)","subunits.UniProt.IDs.":"P21453;P32121","subunits.Entrez.IDs.":"1901;409","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0050728;GO:0043124","GO.description":"negative regulation of inflammatory response;negative regulation of I-kappaB kinase/NF-kappaB signaling","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":26268607,"subunits.Protein.name.":"Sphingosine 1-phosphate receptor 1;Beta-arrestin-2","subunits.Gene.name.":"S1PR1;ARRB2","subunits.Gene.name.syn.":"CHEDG1, EDG1, S1P1;ARB2, ARR2","Disease.comment":"Mouse endothelial S1P1 acted as an anti-inflammatory and anti-atherosclerotic GPCR (G protein-coupled receptor) in vivo.","Subunits.comment":"None","Complex.comment":"Exposure of HUVECs to ApoM(+)HDL-S1P, but not to albumin-S1P, promoted the formation of a cell surface S1P1\\u2013beta-arrestin 2 complex and attenuated the ability of the proinflammatory cytokine TNF? to activate NF-kappaB and increase ICAM-1 abundance.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6806,"ComplexName":"IGF1R-CXCR4-GNAI2-GNB1 complex","Organism":"Human","Synonyms":"None","Cell.line":"highly metastatic MDA-MB-231, non-metastatic MCF-7 breast cancer cells","subunits.UniProt.IDs.":"P04899;P08069;P61073;P62873","subunits.Entrez.IDs.":"2771;3480;7852;2782","Protein.complex.purification.method":"MI:0006-anti bait coimmunoprecipitation","GO.ID":"GO:0016477","GO.description":"cell migration","FunCat.ID":"34.05.01","FunCat.description":"cell migration","PubMed.ID":16172123,"subunits.Protein.name.":"Guanine nucleotide-binding protein G(i) subunit alpha-2;Insulin-like growth factor 1 receptor;C-X-C chemokine receptor type 4;Guanine nucleotide-binding protein G","subunits.Gene.name.":"GNAI2;IGF1R;CXCR4;GNB1","subunits.Gene.name.syn.":"GNAI2B;None;None;None","Disease.comment":"CXCR4 seems to play an important role for in cancer.","Subunits.comment":"None","Complex.comment":"The results show the existence of a constitutive complex between IGF-1R, CXCR4, Gialpha2, and Gbeta.Both Gialpha2 and Gbeta are associated with the complex in both cell lines; however, activation of the complex, as determined by release of Gialpha2 and Gbeta from CXCR4, only occurs in MDA-MB-231 cells.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6807,"ComplexName":"ADRA1A-CXCR4 complex","Organism":"Human","Synonyms":"Alpha-1-adrenergic receptor-CXCR4 complex","Cell.line":"VSMCs (vascular smooth muscle cells), HeLa cells","subunits.UniProt.IDs.":"P35348;P61073","subunits.Entrez.IDs.":"148;7852","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0008217","GO.description":"regulation of blood pressure","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25775528,"subunits.Protein.name.":"Alpha-1A adrenergic receptor;C-X-C chemokine receptor type 4","subunits.Gene.name.":"ADRA1A;CXCR4","subunits.Gene.name.syn.":"ADRA1C;None","Disease.comment":"Compounds targeting the alpha-1A/B-adrenergic receptor-CXCR4 heteromeric complexes could provide an alternative pharmacological approach tomodulating blood pressure.","Subunits.comment":"None","Complex.comment":"Disruption of alpha-1A/B-adrenergic receptor-CXCR4 heteromeric complexes inhibits alpha1-AR\\u2013mediated functions in vascular smooth muscle cells and treatment with CXCR4 agonists enhances the potency of the alpha-1-AR agonist phenylephrine to increase blood pressure.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6808,"ComplexName":"ADRB1-CXCR4 complex","Organism":"Human","Synonyms":"Beta-1-adrenergic receptor-CXCR4 complex","Cell.line":"VSMCs (vascular smooth muscle cells), HeLa cells","subunits.UniProt.IDs.":"P08588;P61073","subunits.Entrez.IDs.":"153;7852","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0008217","GO.description":"regulation of blood pressure","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":25775528,"subunits.Protein.name.":"Beta-1 adrenergic receptor;C-X-C chemokine receptor type 4","subunits.Gene.name.":"ADRB1;CXCR4","subunits.Gene.name.syn.":"ADRB1R, B1AR;None","Disease.comment":"Compounds targeting the alpha-1A/B-adrenergic receptor-CXCR4 heteromeric complexes could provide an alternative pharmacological approach to modulating blood pressure.","Subunits.comment":"None","Complex.comment":"Disruption of alpha-1A/B-adrenergic receptor-CXCR4 heteromeric complexes inhibits alpha1-AR\\u2013mediated functions in vascular smooth muscle cells and treatment with CXCR4 agonists enhances the potency of the alpha-1-AR agonist phenylephrine to increase blood pressure.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6809,"ComplexName":"Arrb2-Akt-Ppp2ca complex","Organism":"Mouse","Synonyms":"None","Cell.line":"striatal extracts","subunits.UniProt.IDs.":"P31750;P63330;Q91YI4","subunits.Entrez.IDs.":"11651;19052;216869","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0043491;GO:0007186","GO.description":"protein kinase B signaling;G-protein coupled receptor signaling pathway","FunCat.ID":"30.05.02.24","FunCat.description":"G-protein coupled receptor signalling pathway","PubMed.ID":18191226,"subunits.Protein.name.":"RAC-alpha serine/threonine-protein kinase;Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform;Beta-arrestin-2","subunits.Gene.name.":"Akt1;Ppp2ca;Arrb2","subunits.Gene.name.syn.":"Akt, Rac;None;None","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The formation of the Akt:bArr2:PP2A signaling complex normally promotes Akt dephosphorylation (PMID: 16051150).Lithium treatment shifts this equilibrium toward the activated state by destabilization of the complex , thereby resulting in increased phosphorylation/inactivation of GSK3-beta.bArr2 scaffolds Akt and PP2A in response to stimulation of GPCRs, such as the dopamine  D2 receptor.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6810,"ComplexName":"Akt-Arrb2-Ppp2ca-Ppp2r2a complex","Organism":"Mouse","Synonyms":"None","Cell.line":"striatal extracts","subunits.UniProt.IDs.":"P31750;P63330;Q6P1F6;Q91YI4","subunits.Entrez.IDs.":"11651;19052;71978;216869","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0096-pull down","GO.ID":"GO:0043491;GO:0007186","GO.description":"protein kinase B signaling;G-protein coupled receptor signaling pathway","FunCat.ID":"30.05.02.24","FunCat.description":"G-protein coupled receptor signalling pathway","PubMed.ID":16051150,"subunits.Protein.name.":"RAC-alpha serine/threonine-protein kinase;Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform;Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform;Beta-arrestin-2","subunits.Gene.name.":"Akt1;Ppp2ca;Ppp2r2a;Arrb2","subunits.Gene.name.syn.":"Akt, Rac;None;None;None","Disease.comment":"None","Subunits.comment":"Since the authors did not specify protein phosphatase 2A regulatory subunit B, we used isoform Ppp2r2a.","Complex.comment":"None","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6811,"ComplexName":"RXFP1 signalosome","Organism":"Human","Synonyms":"RXFP1-AKAP79-AC2-ARRB2-PDE4D3-PKA-alpha","Cell.line":"HEK293 cells","subunits.UniProt.IDs.":"P17612;P24588;P32121;Q08462;Q08499-2;Q9HBX9","subunits.Entrez.IDs.":"5566;9495;409;108;5144;59350","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation;MI:0096-pull down","GO.ID":"GO:0007186;GO:0043949;GO:0009725","GO.description":"G-protein coupled receptor signaling pathway;regulation of cAMP-mediated signaling;response to hormone","FunCat.ID":"30.05.02.24","FunCat.description":"G-protein coupled receptor signalling pathway","PubMed.ID":20664520,"subunits.Protein.name.":"cAMP-dependent protein kinase catalytic subunit alpha;A-kinase anchor protein 5;Beta-arrestin-2;Adenylate cyclase type 2;cAMP-specific 3',5'-cyclic phosphodiesterase 4D;Relaxin receptor 1","subunits.Gene.name.":"PRKACA;AKAP5;ARRB2;ADCY2;PDE4D;RXFP1","subunits.Gene.name.syn.":"PKACA;AKAP79;ARB2, ARR2;KIAA1060, AC2;DPDE3, PDE4D3;LGR7","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"AC2 interacts with RXFP1 through AKAP79, whereas the association with PDE4D3 and PKA depends upon beta-arrestin 2 binding to Ser(704).The experiments present a constitutively active GPCR signalosome, that couples the relaxin receptor, RXFP1, to cAMP following receptor stimulation with sub-picomolar concentrations of peptide.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":6812,"ComplexName":"Arrb1-Becn1-Pik3c3 complex, induced by (OGD) oxygen-glucose deprivation","Organism":"Mouse","Synonyms":"None","Cell.line":"primary neurons","subunits.UniProt.IDs.":"O88597;Q6PF93;Q8BWG8","subunits.Entrez.IDs.":"56208;225326;109689","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0010506;GO:0000045","GO.description":"regulation of autophagy;autophagosome assembly","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":24988431,"subunits.Protein.name.":"Beclin-1;Phosphatidylinositol 3-kinase catalytic subunit type 3;Beta-arrestin-1","subunits.Gene.name.":"Becn1;Pik3c3;Arrb1","subunits.Gene.name.syn.":"None;Vps34;None","Disease.comment":"Arrb1 is recruited to the Becn1 core complex upon ischemic stress in neurons.Deletion of Arrb1 impaired the interaction between Becn1 and Pik3c3, which is a critical event for autophagosome formation upon ischemic stress, and markedly reduced the kinase activity of PIK3C3.","Subunits.comment":"None","Complex.comment":"The interaction between Arrb1 and Becn1-Pik3c3 was detected under the OGD condition (oxygen-glucose deprivation) but not normal conditions in WT neurons.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6813,"ComplexName":"Arrb2-Akt-Src complex, insulin induced","Organism":"Mouse","Synonyms":"None","Cell.line":"livers of C57BL/6 mice","subunits.UniProt.IDs.":"P05480;P31750;Q91YI4","subunits.Entrez.IDs.":"20779;11651;216869","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0043491;GO:0032868","GO.description":"protein kinase B signaling;response to insulin","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":19122674,"subunits.Protein.name.":"Neuronal proto-oncogene tyrosine-protein kinase Src;RAC-alpha serine/threonine-protein kinase;Beta-arrestin-2","subunits.Gene.name.":"Src;Akt1;Arrb2","subunits.Gene.name.syn.":"pp60c-src;Akt, Rac;None","Disease.comment":"Loss or dysfunction of beta-arrestin-2 results in deficiency of this signal complexand disturbance of insulin signalling in vivo, thereby contributing to the development of insulin resistance and progression of type 2 diabetes.","Subunits.comment":"None","Complex.comment":"Beta-arrestin-2 promotes Akt activation and glucose metabolism through Src.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6814,"ComplexName":"Insr-Arrb2-Akt-Src complex, insulin induced","Organism":"Mouse","Synonyms":"Insulin receptor subunit beta-Arrb2-Akt-Src complex","Cell.line":"livers of C57BL/6 mice","subunits.UniProt.IDs.":"P05480;P15208;P31750;Q91YI4","subunits.Entrez.IDs.":"20779;16337;11651;216869","Protein.complex.purification.method":"MI:0019-coimmunoprecipitation","GO.ID":"GO:0043491;GO:0032868;GO:0008286;GO:0042593","GO.description":"protein kinase B signaling;response to insulin;insulin receptor signaling pathway;glucose homeostasis","FunCat.ID":"30.05.01.12.05;34.01.04","FunCat.description":"insulin receptor signalling pathway;glucose homeostasis","PubMed.ID":19122674,"subunits.Protein.name.":"Neuronal proto-oncogene tyrosine-protein kinase Src;Insulin receptor;RAC-alpha serine/threonine-protein kinase;Beta-arrestin-2","subunits.Gene.name.":"Src;Insr;Akt1;Arrb2","subunits.Gene.name.syn.":"pp60c-src;None;Akt, Rac;None","Disease.comment":"Loss or dysfunction of beta-arrestin-2 results in deficiency of this signal complexand disturbance of insulin signalling in vivo, thereby contributing to the development of insulin resistance and progression of type 2 diabetes.","Subunits.comment":"None","Complex.comment":"Insulin stimulates the formation of a new beta-arrestin-2 signal complex, in which beta-arrestin-2 scaffolds Akt and Src to insulin receptor.","SWISSPROT.organism":"Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse);Mus musculus (Mouse)"}
{"ComplexID":6815,"ComplexName":"DRD4-KLHL12-CUL3 complex","Organism":"Human","Synonyms":"D4 receptor-KLHL12-CUL3 complex","Cell.line":"HEK293T cells","subunits.UniProt.IDs.":"P21917;Q13618;Q53G59","subunits.Entrez.IDs.":"1815;8452;59349","Protein.complex.purification.method":"MI:0007-anti tag coimmunoprecipitation","GO.ID":"GO:0031396","GO.description":"regulation of protein ubiquitination","FunCat.ID":"None","FunCat.description":"None","PubMed.ID":18303015,"subunits.Protein.name.":"D(4) dopamine receptor;Cullin-3;Kelch-like protein 12","subunits.Gene.name.":"DRD4;CUL3;KLHL12","subunits.Gene.name.syn.":"D4DR;KIAA0617;C3IP1","Disease.comment":"None","Subunits.comment":"None","Complex.comment":"The D4 receptor does not directly interact with Cul3 but is recruited to the E3 ligase via KLHL12 as an adaptor. This complex formation specifically targets the D4receptor for ubiquitination. The experiments indicate that the D4-KLHL12 association could be human (primate)-specific.","SWISSPROT.organism":"Homo sapiens (Human);Homo sapiens (Human);Homo sapiens (Human)"}
{"ComplexID":10000,"ComplexName":"Exosomal_Core","Organism":"Human","Synonyms":"None","Cell.line":"Unknown","subunits.UniProt.IDs.":"Q9Y3B2;Q13868;Q9NQT5;Q9NPD3;Q9NQT4;Q5RKV6;Q15024;Q96B26;Q06265;Q01780","subunits.Entrez.IDs.":"Unknown","Protein.complex.purification.method":"","GO.ID":"","GO.description":"","FunCat.ID":"","FunCat.description":"","PubMed.ID":11719186,"subunits.Protein.name.":"","subunits.Gene.name.":"","subunits.Gene.name.syn.":"","Disease.comment":"","Subunits.comment":"","Complex.comment":"","SWISSPROT.organism":""}
{"ComplexID":10001,"ComplexName":"SKI_complex","Organism":"Human","Synonyms":"None","Cell.line":"Unknown","subunits.UniProt.IDs.":"P42285;Q15477;Q9Y2L1;Q9GZS3;Q6PGP7","subunits.Entrez.IDs.":"Unknown","Protein.complex.purification.method":"","GO.ID":"","GO.description":"","FunCat.ID":"","FunCat.description":"","PubMed.ID":8722763,"subunits.Protein.name.":"","subunits.Gene.name.":"","subunits.Gene.name.syn.":"","Disease.comment":"","Subunits.comment":"","Complex.comment":"","SWISSPROT.organism":""}
{"ComplexID":10002,"ComplexName":"TRAMP_complex","Organism":"Human","Synonyms":"None","Cell.line":"Unknown","subunits.UniProt.IDs.":"Q8NDF8;Q8N3Z6;Q5XG87;Q9VC07;P42285;Q9NZM5;Q9Y5J1","subunits.Entrez.IDs.":"Unknown","Protein.complex.purification.method":"","GO.ID":"","GO.description":"","FunCat.ID":"","FunCat.description":"","PubMed.ID":18172165,"subunits.Protein.name.":"","subunits.Gene.name.":"","subunits.Gene.name.syn.":"","Disease.comment":"","Subunits.comment":"","Complex.comment":"","SWISSPROT.organism":""}
{"ComplexID":10003,"ComplexName":"NEXT_complex","Organism":"Human","Synonyms":"None","Cell.line":"Unknown","subunits.UniProt.IDs.":"Q9Y580;Q6NZY4;P42285","subunits.Entrez.IDs.":"Unknown","Protein.complex.purification.method":"","GO.ID":"","GO.description":"","FunCat.ID":"","FunCat.description":"","PubMed.ID":12634307,"subunits.Protein.name.":"","subunits.Gene.name.":"","subunits.Gene.name.syn.":"","Disease.comment":"","Subunits.comment":"","Complex.comment":"","SWISSPROT.organism":""}
{"ComplexID":10004,"ComplexName":"MITO:Coenzyme Q10 and Cytochrome-c biogenesis","Organism":"Mouse","Synonyms":"None","Cell.line":"Unknown","subunits.UniProt.IDs.":"Q9D0L4;Q6NSR3;Q60936;Q566J8;Q80V03;Q66JT7;Q8BMS4;Q8BGB8;Q9CXI0;Q8R1S0;P97478;Q8K1Z0;E9Q3H6;Q3THF9;P62897;P53702;Q33DR2;Q33DR3","subunits.Entrez.IDs.":"Unknown","Protein.complex.purification.method":"","GO.ID":"","GO.description":"","FunCat.ID":"","FunCat.description":"","PubMed.ID":1,"subunits.Protein.name.":"","subunits.Gene.name.":"","subunits.Gene.name.syn.":"","Disease.comment":"","Subunits.comment":"","Complex.comment":"","SWISSPROT.organism":""}
{"ComplexID":10005,"ComplexName":"MITO:Complex_I Assembly Factors","Organism":"Mouse","Synonyms":"None","Cell.line":"Unknown","subunits.UniProt.IDs.":"Q9CWX2;Q59J78;Q9JKL4;Q9D1H6;A2APY7;A2AIL4;Q8JZN5;Q3TQB2;Q9QZH6;Q9CWD8;Q8BGA9","subunits.Entrez.IDs.":"Unknown","Protein.complex.purification.method":"","GO.ID":"","GO.description":"","FunCat.ID":"","FunCat.description":"","PubMed.ID":1,"subunits.Protein.name.":"","subunits.Gene.name.":"","subunits.Gene.name.syn.":"","Disease.comment":"","Subunits.comment":"","Complex.comment":"","SWISSPROT.organism":""}
{"ComplexID":10006,"ComplexName":"MITO:Complex_I Mitochondrial encoded subunit","Organism":"Mouse","Synonyms":"None","Cell.line":"Unknown","subunits.UniProt.IDs.":"P03888;P03893;P03899;P03911;P03903;P03921;P03925","subunits.Entrez.IDs.":"Unknown","Protein.complex.purification.method":"","GO.ID":"","GO.description":"","FunCat.ID":"","FunCat.description":"","PubMed.ID":1,"subunits.Protein.name.":"","subunits.Gene.name.":"","subunits.Gene.name.syn.":"","Disease.comment":"","Subunits.comment":"","Complex.comment":"","SWISSPROT.organism":""}
{"ComplexID":10007,"ComplexName":"MITO:Complex_I Nuclear encoded subunit","Organism":"Mouse","Synonyms":"None","Cell.line":"Unknown","subunits.UniProt.IDs.":"Q91YT0;Q9D6J6;Q8BK30;Q91VD9;Q91WD5;Q9DCT2;Q9CXZ1;Q99LY9;P52503;Q9DC70;Q8K3J1;O35683;Q9CQ75;Q9CQ91;Q9CPP6;Q9CQZ5;Q9Z1P6;Q9DCJ5;Q9DC69;Q99LC3;Q9D8B4;Q7TMF3;Q9ERS2;Q9CR21;P0DN34;Q9CPU2;Q9CQZ6;Q9CQC7;Q9CQH3;Q3UIU2;Q9CR61;Q9D6J5;Q9CQJ8;Q9DCS9;O09111;Q9CQY9;Q9CQ54","subunits.Entrez.IDs.":"Unknown","Protein.complex.purification.method":"","GO.ID":"","GO.description":"","FunCat.ID":"","FunCat.description":"","PubMed.ID":1,"subunits.Protein.name.":"","subunits.Gene.name.":"","subunits.Gene.name.syn.":"","Disease.comment":"","Subunits.comment":"","Complex.comment":"","SWISSPROT.organism":""}
{"ComplexID":10008,"ComplexName":"MITO:Complex_II Assembly Factors","Organism":"Mouse","Synonyms":"None","Cell.line":"Unknown","subunits.UniProt.IDs.":"Q3U276;Q8C6I2;Q8BQU3;Q8BTE0","subunits.Entrez.IDs.":"Unknown","Protein.complex.purification.method":"","GO.ID":"","GO.description":"","FunCat.ID":"","FunCat.description":"","PubMed.ID":1,"subunits.Protein.name.":"","subunits.Gene.name.":"","subunits.Gene.name.syn.":"","Disease.comment":"","Subunits.comment":"","Complex.comment":"","SWISSPROT.organism":""}
{"ComplexID":10009,"ComplexName":"MITO:Complex_II Nuclear encoded subunits","Organism":"Mouse","Synonyms":"None","Cell.line":"Unknown","subunits.UniProt.IDs.":"Q8K2B3;Q9CQA3;Q9CZB0;Q9CXV1","subunits.Entrez.IDs.":"Unknown","Protein.complex.purification.method":"","GO.ID":"","GO.description":"","FunCat.ID":"","FunCat.description":"","PubMed.ID":1,"subunits.Protein.name.":"","subunits.Gene.name.":"","subunits.Gene.name.syn.":"","Disease.comment":"","Subunits.comment":"","Complex.comment":"","SWISSPROT.organism":""}
{"ComplexID":10010,"ComplexName":"MITO:Complex_III Assembly Factors","Organism":"Mouse","Synonyms":"None","Cell.line":"Unknown","subunits.UniProt.IDs.":"Q9CZP5;Q9CWU6;Q9CQY6;Q8K2T4","subunits.Entrez.IDs.":"Unknown","Protein.complex.purification.method":"","GO.ID":"","GO.description":"","FunCat.ID":"","FunCat.description":"","PubMed.ID":1,"subunits.Protein.name.":"","subunits.Gene.name.":"","subunits.Gene.name.syn.":"","Disease.comment":"","Subunits.comment":"","Complex.comment":"","SWISSPROT.organism":""}
{"ComplexID":10011,"ComplexName":"MITO:Complex_III Mitochondrial encoded subunits","Organism":"Mouse","Synonyms":"None","Cell.line":"Unknown","subunits.UniProt.IDs.":"P00158","subunits.Entrez.IDs.":"Unknown","Protein.complex.purification.method":"","GO.ID":"","GO.description":"","FunCat.ID":"","FunCat.description":"","PubMed.ID":1,"subunits.Protein.name.":"","subunits.Gene.name.":"","subunits.Gene.name.syn.":"","Disease.comment":"","Subunits.comment":"","Complex.comment":"","SWISSPROT.organism":""}
{"ComplexID":10012,"ComplexName":"MITO:Complex_III Nuclear encoded subunit","Organism":"Mouse","Synonyms":"None","Cell.line":"Unknown","subunits.UniProt.IDs.":"Q9D0M3;Q8CC21;Q9D855;Q9CZ13;Q9DB77;P99028;Q8R1I1;Q9CPX8;Q9CR68;Q9CQ69","subunits.Entrez.IDs.":"Unknown","Protein.complex.purification.method":"","GO.ID":"","GO.description":"","FunCat.ID":"","FunCat.description":"","PubMed.ID":1,"subunits.Protein.name.":"","subunits.Gene.name.":"","subunits.Gene.name.syn.":"","Disease.comment":"","Subunits.comment":"","Complex.comment":"","SWISSPROT.organism":""}
{"ComplexID":10013,"ComplexName":"MITO:Complex_IV Assembly Factors","Organism":"Mouse","Synonyms":"None","Cell.line":"Unknown","subunits.UniProt.IDs.":"Q9D2R6;Q99M07;Q8BGD8;Q921H9;Q8CFY5;Q6P8I6;Q8BH51;Q8BJ03;Q9CR63;P56394;Q8VC74;Q8K0C8;Q9D7J4;Q922E6;P46656;Q6PB66;Q8BGA9;Q5SUC9;Q8VCL2;P09925;Q8K0Z7","subunits.Entrez.IDs.":"Unknown","Protein.complex.purification.method":"","GO.ID":"","GO.description":"","FunCat.ID":"","FunCat.description":"","PubMed.ID":1,"subunits.Protein.name.":"","subunits.Gene.name.":"","subunits.Gene.name.syn.":"","Disease.comment":"","Subunits.comment":"","Complex.comment":"","SWISSPROT.organism":""}
{"ComplexID":10014,"ComplexName":"MITO:Complex_IV Mitochondrial encoded subunits","Organism":"Mouse","Synonyms":"None","Cell.line":"Unknown","subunits.UniProt.IDs.":"P00397;P00405;P00416","subunits.Entrez.IDs.":"Unknown","Protein.complex.purification.method":"","GO.ID":"","GO.description":"","FunCat.ID":"","FunCat.description":"","PubMed.ID":1,"subunits.Protein.name.":"","subunits.Gene.name.":"","subunits.Gene.name.syn.":"","Disease.comment":"","Subunits.comment":"","Complex.comment":"","SWISSPROT.organism":""}
{"ComplexID":10015,"ComplexName":"MITO:Complex_IV Nuclear encoded subunits","Organism":"Mouse","Synonyms":"None","Cell.line":"Unknown","subunits.UniProt.IDs.":"P19783;Q91W29;P12787;P19536;P43024;P43023;P56391;P56392;P48771;Q61387;P56393;P17665;Q64445;P48772;A6H666;Q62425","subunits.Entrez.IDs.":"Unknown","Protein.complex.purification.method":"","GO.ID":"","GO.description":"","FunCat.ID":"","FunCat.description":"","PubMed.ID":1,"subunits.Protein.name.":"","subunits.Gene.name.":"","subunits.Gene.name.syn.":"","Disease.comment":"","Subunits.comment":"","Complex.comment":"","SWISSPROT.organism":""}
{"ComplexID":10016,"ComplexName":"MITO:Complex_V Assembly Factors","Organism":"Mouse","Synonyms":"None","Cell.line":"Unknown","subunits.UniProt.IDs.":"Q811I0;Q91YY4;Q921N7;Q8BGA9","subunits.Entrez.IDs.":"Unknown","Protein.complex.purification.method":"","GO.ID":"","GO.description":"","FunCat.ID":"","FunCat.description":"","PubMed.ID":1,"subunits.Protein.name.":"","subunits.Gene.name.":"","subunits.Gene.name.syn.":"","Disease.comment":"","Subunits.comment":"","Complex.comment":"","SWISSPROT.organism":""}
{"ComplexID":10017,"ComplexName":"MITO:Complex_V Mitochondrial encoded subunits","Organism":"Mouse","Synonyms":"None","Cell.line":"Unknown","subunits.UniProt.IDs.":"P00848;P03930","subunits.Entrez.IDs.":"Unknown","Protein.complex.purification.method":"","GO.ID":"","GO.description":"","FunCat.ID":"","FunCat.description":"","PubMed.ID":1,"subunits.Protein.name.":"","subunits.Gene.name.":"","subunits.Gene.name.syn.":"","Disease.comment":"","Subunits.comment":"","Complex.comment":"","SWISSPROT.organism":""}
{"ComplexID":10018,"ComplexName":"MITO:Complex_V Nuclear encoded subunits","Organism":"Mouse","Synonyms":"None","Cell.line":"Unknown","subunits.UniProt.IDs.":"Q03265;P56480;Q91VR2;Q9D3D9;P56382;Q9CQQ7;Q9CR84;P56383;P56384;Q9DCX2;Q06185;P97450;P56135;Q9CPQ8;Q9DB20;Q9CRA7;O35143","subunits.Entrez.IDs.":"Unknown","Protein.complex.purification.method":"","GO.ID":"","GO.description":"","FunCat.ID":"","FunCat.description":"","PubMed.ID":1,"subunits.Protein.name.":"","subunits.Gene.name.":"","subunits.Gene.name.syn.":"","Disease.comment":"","Subunits.comment":"","Complex.comment":"","SWISSPROT.organism":""}
{"ComplexID":10019,"ComplexName":"MITO:Fe-S biogenesis","Organism":"Mouse","Synonyms":"None","Cell.line":"Unknown","subunits.UniProt.IDs.":"Q61102;Q9D8S9;Q8BGS2;Q8CEI1;Q8WTY4;P46656;Q9CPW2;Q61578;O35943;P56213;Q80Y14;Q99LP6;O88396;P31315;P31316;Q8K3A0;P38647;Q8CAK1;Q9D924;Q9DCB8;Q9D7P6;Q8K215;Q920G8;Q8R0Z5;Q9CWD8;Q9Z1J3;Q9QZ23","subunits.Entrez.IDs.":"Unknown","Protein.complex.purification.method":"","GO.ID":"","GO.description":"","FunCat.ID":"","FunCat.description":"","PubMed.ID":1,"subunits.Protein.name.":"","subunits.Gene.name.":"","subunits.Gene.name.syn.":"","Disease.comment":"","Subunits.comment":"","Complex.comment":"","SWISSPROT.organism":""}
{"ComplexID":10020,"ComplexName":"MITO:mt-DNA Repair","Organism":"Mouse","Synonyms":"None","Cell.line":"Unknown","subunits.UniProt.IDs.":"P28352;Q68G58;Q6ZQJ5;Q8VCG1;O08600;Q8BHK9;Q8CFD5;P39749;P97386;P26187;Q04841;P43247;Q99P21;Q8K4Q6;O35980;P53368;O08760;P02340;P11103;Q80SX8;P54099;Q08297;Q9CYR0;P40630;O08550;P97931","subunits.Entrez.IDs.":"Unknown","Protein.complex.purification.method":"","GO.ID":"","GO.description":"","FunCat.ID":"","FunCat.description":"","PubMed.ID":1,"subunits.Protein.name.":"","subunits.Gene.name.":"","subunits.Gene.name.syn.":"","Disease.comment":"","Subunits.comment":"","Complex.comment":"","SWISSPROT.organism":""}
{"ComplexID":10021,"ComplexName":"MITO:mt-DNA Replication Transcription and Translation","Organism":"Mouse","Synonyms":"None","Cell.line":"Unknown","subunits.UniProt.IDs.":"Q8CIW5;Q80VP5;Q8K0D5;Q8R2Q4;P19258;Q9D6S7;Q8CHZ9;B9EJ57;Q8BKY8;Q8R3J4;Q8BVN4;Q9D799;Q91YJ5;Q9D0D3;Q8K126;Q8BJU9;P54099;Q9QZM2;Q8BKF1;Q9WU56;Q9CYR0;P40630;Q8JZM0;Q3TL26;Q8R4U6;Q9DAT5;Q9CZR8;Q8BFR5;Q8BKY8;Q9CZD5","subunits.Entrez.IDs.":"Unknown","Protein.complex.purification.method":"","GO.ID":"","GO.description":"","FunCat.ID":"","FunCat.description":"","PubMed.ID":1,"subunits.Protein.name.":"","subunits.Gene.name.":"","subunits.Gene.name.syn.":"","Disease.comment":"","Subunits.comment":"","Complex.comment":"","SWISSPROT.organism":""}
{"ComplexID":10022,"ComplexName":"MITO:mtDNA dNTP Pool","Organism":"Mouse","Synonyms":"None","Cell.line":"Unknown","subunits.UniProt.IDs.":"Q9WTP6;Q9QX60;Q9R088;Q9WV84;O88425;Q8VCE6;Q6PEE3;Q9Z2I9;Q9WUM5;Q9Z2I8","subunits.Entrez.IDs.":"Unknown","Protein.complex.purification.method":"","GO.ID":"","GO.description":"","FunCat.ID":"","FunCat.description":"","PubMed.ID":1,"subunits.Protein.name.":"","subunits.Gene.name.":"","subunits.Gene.name.syn.":"","Disease.comment":"","Subunits.comment":"","Complex.comment":"","SWISSPROT.organism":""}
{"ComplexID":10023,"ComplexName":"MITO:mtDNA Nucleoid-associated proteins","Organism":"Mouse","Synonyms":"None","Cell.line":"Unknown","subunits.UniProt.IDs.":"P50544;Q925I1;Q9JHS4;Q8C196;P53395;Q9CWT6;Q99PU8;Q8BMS1;Q99JY0;Q61696;Q8CGK3;Q9CQY6;P58281;P67778;O35129;Q91VA6;Q9CZN7;P51881;P09671;Q80YD1;Q60932;Q60930;Q60931","subunits.Entrez.IDs.":"Unknown","Protein.complex.purification.method":"","GO.ID":"","GO.description":"","FunCat.ID":"","FunCat.description":"","PubMed.ID":1,"subunits.Protein.name.":"","subunits.Gene.name.":"","subunits.Gene.name.syn.":"","Disease.comment":"","Subunits.comment":"","Complex.comment":"","SWISSPROT.organism":""}
{"ComplexID":10024,"ComplexName":"MITO:mtDNA Ribosomal Proteins","Organism":"Mouse","Synonyms":"None","Cell.line":"Unknown","subunits.UniProt.IDs.":"Q99N96;Q9D773;Q99N95;Q9DCU6;Q99N94;Q3TBW2;Q9CQF0;Q9DB15;Q9D1P0;Q9D1I6;Q9CPR5;Q99N93;Q9D8P4;Q9CQL5;Q9D338;Q9CQL4;Q9D1N9;Q8BU88;O35972;Q9CQ06;Q99N92;Q9D1B9;Q9D7N6;Q9DCI9;Q9CQP0;Q99N91;Q9CQL6;Q99N90;Q921S7;Q8K2M0;Q9JKF7;Q9Z2Q5;Q9CQN7;Q9CPV3;Q99N89;Q9CY73;Q9D0Q7;Q9EQI8;Q8K2Y7;Q8JZS9;Q9CQ40;Q8VDT9;Q9CPY1;Q9D0Y8;Q9D1H8;Q9CPW3;Q9CZ83;Q9CQF8;Q9ER88;Q921Y2;Q924T2;Q99N87;P58064;Q80X85;Q9D7N3;Q80ZK0;Q9DCA2;O35680;Q9CR88;Q9DC71;Q9CPX7;Q9CQE3;Q99N85;Q99N84;Q8R2L5;P58059;Q9CXW2;Q8VE22;Q9CQV5;Q9D125;Q80ZS3;Q8BK72;Q9CY16;Q9D0G0;Q61733;Q9D2R8;Q9JIK9;Q8BJZ4;Q9CQX8","subunits.Entrez.IDs.":"Unknown","Protein.complex.purification.method":"","GO.ID":"","GO.description":"","FunCat.ID":"","FunCat.description":"","PubMed.ID":1,"subunits.Protein.name.":"","subunits.Gene.name.":"","subunits.Gene.name.syn.":"","Disease.comment":"","Subunits.comment":"","Complex.comment":"","SWISSPROT.organism":""}
{"ComplexID":10025,"ComplexName":"MITO:mtDNA tRNA Synthetases","Organism":"Mouse","Synonyms":"None","Cell.line":"Unknown","subunits.UniProt.IDs.":"Q14CH7;Q8BYM8;Q8BIP0;Q9CXJ1;Q99M01;Q9CZD3;Q99KK9;Q8BIJ6;Q99MN1;Q8VDC0;Q499X9;Q8BGV0;Q8CFI5;Q3U186;Q9JJL8;Q3UQ84;Q3U2A8;Q9CYK1;Q8BYL4","subunits.Entrez.IDs.":"Unknown","Protein.complex.purification.method":"","GO.ID":"","GO.description":"","FunCat.ID":"","FunCat.description":"","PubMed.ID":1,"subunits.Protein.name.":"","subunits.Gene.name.":"","subunits.Gene.name.syn.":"","Disease.comment":"","Subunits.comment":"","Complex.comment":"","SWISSPROT.organism":""}