IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Modulation of the CD95-induced apoptosis: the role of CD95 N-glycosylation. Modulation of the CD95-induced apoptosis: the role of CD95 N-glycosylation. PLoS ONE 2011 imex curation Shatnyeva O.M., Kubarenko A.V., Weber C.E., Pappa A., Schwartz-Albiez R., Weber A.N., Krammer P.H., Lavrik I.N. Apoptosis - Interactions involving proteins with a function related to apoptosis i.lavrik@dkfz.de 21-Dec-2011: Contacted by JYOTI. Only protein-protein interactions human-hela Homo sapiens epitheloid cervix carcinoma cells Human hela Human epitheloid cervix carcinoma HeLa cells derivation: cervix; epithelial; adenocarcinoma ATCC no:CCL-2 anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Shatnyeva O.M., Kubarenko A.V., Weber C.E., Pappa A., Schwartz-Albiez R., Weber A.N., Krammer P.H., Lavrik I.N. Apoptosis - Interactions involving proteins with a function related to apoptosis i.lavrik@dkfz.de Accepted 2011-OCT-11 by ORCHARD PLoS ONE 2011 Only protein-protein interactions imex curation Modulation of the CD95-induced apoptosis: the role of CD95 N-glycosylation. Modulation of the CD95-induced apoptosis: the role of CD95 N-glycosylation. PLoS ONE 2011 imex curation Shatnyeva O.M., Kubarenko A.V., Weber C.E., Pappa A., Schwartz-Albiez R., Weber A.N., Krammer P.H., Lavrik I.N. Apoptosis - Interactions involving proteins with a function related to apoptosis i.lavrik@dkfz.de 21-Dec-2011: Contacted by JYOTI. Only protein-protein interactions human-skw6.4 Human B-lymphoblastoid EBV-transformed cell line skw6.4 Human B-lymphoblastoid EBV-transformed cell line anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Shatnyeva O.M., Kubarenko A.V., Weber C.E., Pappa A., Schwartz-Albiez R., Weber A.N., Krammer P.H., Lavrik I.N. Apoptosis - Interactions involving proteins with a function related to apoptosis i.lavrik@dkfz.de Accepted 2011-OCT-11 by ORCHARD 21-Dec-2011: Contacted by JYOTI. PLoS ONE 2011 Only protein-protein interactions imex curation Modulation of the CD95-induced apoptosis: the role of CD95 N-glycosylation. Modulation of the CD95-induced apoptosis: the role of CD95 N-glycosylation. PLoS ONE 2011 imex curation Shatnyeva O.M., Kubarenko A.V., Weber C.E., Pappa A., Schwartz-Albiez R., Weber A.N., Krammer P.H., Lavrik I.N. Apoptosis - Interactions involving proteins with a function related to apoptosis i.lavrik@dkfz.de 21-Dec-2011: Contacted by JYOTI. Only protein-protein interactions human-hut78 Homo sapiens HUT-78 T cell lymphoma hut78 HUT-78 human T cell lymphoma anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Shatnyeva O.M., Kubarenko A.V., Weber C.E., Pappa A., Schwartz-Albiez R., Weber A.N., Krammer P.H., Lavrik I.N. Apoptosis - Interactions involving proteins with a function related to apoptosis i.lavrik@dkfz.de Accepted 2011-OCT-11 by ORCHARD 21-Dec-2011: Contacted by JYOTI. PLoS ONE 2011 Only protein-protein interactions imex curation fadd_human FAS-associated death domain protein FAS-associating death domain-containing protein Mediator of receptor induced toxicity FADD MORT1 GIG3 Growth-inhibiting gene 3 protein protein protein human Homo sapiens Human MDPFLVLLHSVSSSLSSSELTELKFLCLGRVGKRKLERVQSGLDLFSMLLEQNDLEPGHTELLRELLASLRRHDLLRRVDDFEAGAAAGAAPGEEDLCAAFNVICDNVGKDWRRLARQLKVSDTKIDSIEDRYPRNLTERVRESLRIWKNTEKENATVAHLVGALRSCQMNLVADLVQEVQQARDLQNRSGAMSPMSWNSDASTSEAS DIP protein Q13158 original sequence version: 155 DIP protein Q13158 original sequence version: 130 DIP protein Q13158 original sequence version: 110 DIP protein Q13158 original sequence version: 118 DIP protein Q13158 original sequence version: 141 DIP protein Q13158 original sequence version: 166 0E65E2F852E83507 q14790-pro_0000004629 Caspase-8 subunit p18 CASP8 MCH5 Apoptotic cysteine protease Apoptotic protease Mch-5 CAP4 FADD-homologous ICE/ced-3-like protease FADD-like ICE ICE-like apoptotic protease 5 MORT1-associated ced-3 homolog protein protein human Homo sapiens Human SESQTLDKVYQMKSKPRGYCLIINNHNFAKAREKVPKLHSIRDRNGTHLDAGALTTTFEELHFEIKPHDDCTVEQIYEILKIYQLMDHSNMDCFICCILSHGDKGIIYGTDGQEAPIYELTSQFTGLKCPSLAGKPKVFFIQACQGDNYQKGIPVETD 217 374 B7C51C40CE9EF10E casp8_human Caspase-8 CASP8 MCH5 ICE-like apoptotic protease 5 MORT1-associated ced-3 homolog FADD-homologous ICE/ced-3-like protease FADD-like ICE Apoptotic cysteine protease Apoptotic protease Mch-5 CAP4 protein protein human Homo sapiens Human MDFSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLNTRKEEMERELQTPGRAQISAYRVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINKSLLKIINDYEEFSKERSSSLEGSPDEFSNGEELCGVMTISDSPREQDSESQTLDKVYQMKSKPRGYCLIINNHNFAKAREKVPKLHSIRDRNGTHLDAGALTTTFEELHFEIKPHDDCTVEQIYEILKIYQLMDHSNMDCFICCILSHGDKGIIYGTDGQEAPIYELTSQFTGLKCPSLAGKPKVFFIQACQGDNYQKGIPVETDSEEQPYLEMDLSSPQTRYIPDEADFLLGMATVNNCVSYRNPAEGTWYIQSLCQSLRERCPRGDDILTILTEVNYEVSNKDDKKNMGKQMPQPTFTLRKKLVFPSD DIP protein Q14790 original sequence version: 184 DIP protein Q14790 original sequence version: 135 DIP protein Q14790 original sequence version: 136 DIP protein Q14790 original sequence version: 147 DIP protein Q14790 original sequence version: 146 DIP protein Q14790 original sequence version: 170 DIP protein Q14790 original sequence version: 198 DIP protein Q14790-1 original sequence version: 197 DIP protein Q14790 original sequence version: 158 7A5FEAA6B39B582F tnr6_human Tumor necrosis factor receptor superfamily member 6 FASLG receptor Apoptosis-mediating surface antigen FAS Apo-1 antigen FAS APT1 TNFRSF6 FAS1 protein protein human Homo sapiens Human MLGIWTLLPLVLTSVARLSSKSVNAQVTDINSKGLELRKTVTTVETQNLEGLHHDGQFCHKPCPPGERKARDCTVNGDEPDCVPCQEGKEYTDKAHFSSKCRRCRLCDEGHGLEVEINCTRTQNTKCRCKPNFFCNSTVCEHCDPCTKCEHGIIKECTLTSNTKCKEEGSRSNLGWLCLLLLPIPLIVWVKRKEVQKTCRKHRKENQGSHESPTLNPETVAINLSDVDLSKYITTIAGVMTLSQVKGFVRKNGVNEAKIDEIKNDNVQDTAEQKVQLLRNWHQLHGKKEAYDTLIKDLKKANLCTLAEKIQTIILKDITSDSENSNFRNEIQSLV 0139942535111410 o15519-pro_0000004678 CASP8 and FADD-like apoptosis regulator subunit p43 CFLAR CASH CASP8AP1 CLARP MRIT Caspase homolog Caspase-eight-related protein Caspase-like apoptosis regulatory protein Cellular FLICE-like inhibitory protein FADD-like antiapoptotic molecule 1 Inhibitor of FLICE MACH-related inducer of toxicity Usurpin protein protein human Homo sapiens Human MSAEVIHQVEEALDTDEKEMLLFLCRDVAIDVVPPNVRDLLDILRERGKLSVGDLAELLYRVRRFDLLKRILKMDRKAVETHLLRNPHLVSDYRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKISKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDLKTKIQKYKQSVQGAGTSYRNVLQAAIQKSLKDPSNNFRLHNGRSKEQRLKEQLGAQQEPVKKSIQESEAFLPQSIPEERYKMKSKPLGICLIIDCIGNETELLRDTFTSLGYEVQKFLHLSMHGISQILGQFACMPEHRDYDSFVCVLVSRGGSQSVYGVDQTHSGLPLHHIRRMFMGDSCPYLAGKPKMFFIQNYVVSEGQLEDSSLLEVD 1 376 D6127C24F8840C2D fas-casp8-10 1 5 unspecified role unspecified role prey prey Interaction with this fragment is slightly reduced when a mutant version of fas (N118Q) is used as bait. 6 unspecified role unspecified role prey prey Both the inactive form (p55/p53) and the cleaved, active fragment p43/p41 were co-inmunoprecipitated in this experiment. 4 unspecified role unspecified role prey prey 7 unspecified role unspecified role bait bait association association 5c These three protein plus FLIP form the DISC complex, involved in induction of apoptosis via the extrinsic pathway. Treatment with anti-APO-1 antibody (recognizes an epitope on the extracellular part of fas) is required for the complex to be formed. fas-casp8-12 3 8 unspecified role unspecified role prey prey 7 unspecified role unspecified role bait bait 6 unspecified role unspecified role prey prey Both the inactive form (p55/p53) and the cleaved, active fragment p43/p41 were co-inmunoprecipitated in this experiment. association association 6b and S5a These three protein plus FADD form the DISC complex, involved in induction of apoptosis via the extrinsic pathway. Treatment with anti-APO-1 antibody (recognizes an epitope on the extracellular part of fas) is required for the complex to be formed. The presence of CASP8 and cflar (FLIP) processed fragments was decreased upon Vibrio cholerae sialidase (VCN, reduces glycosilation of fas by cutting sialic acid unions) treatment (fig. 6b). The presence of cflar processed fragment was decreased upon treatment with tunicamycin (inhibits fas glycosylation at the ER level, fig. S5a). fas-casp8-11 2 8 unspecified role unspecified role prey prey 7 unspecified role unspecified role bait bait 6 unspecified role unspecified role prey prey Both the inactive form (p55/p53) and the cleaved, active fragment p43/p41 were co-inmunoprecipitated in this experiment. association association 6b and S5a These three protein plus FADD form the DISC complex, involved in induction of apoptosis via the extrinsic pathway. Treatment with anti-APO-1 antibody (recognizes an epitope on the extracellular part of fas) is required for the complex to be formed. The presence of CASP8 and cflar (FLIP) processed fragments was decreased upon Vibrio cholerae sialidase (VCN, reduces glycosilation of fas by cutting sialic acid unions) treatment (fig. 6b). The presence of cflar processed fragment was decreased upon treatment with tunicamycin (inhibits fas glycosylation at the ER level, fig. S5a). fas-casp8-8 2 6 unspecified role unspecified role prey prey Both the inactive form (p55/p53) and the cleaved, active fragment p43/p41 were co-inmunoprecipitated in this experiment. The presence of the p43/p41 fragment was disrupted when the mannosidase inhibitor DMM was used. 4 unspecified role unspecified role prey prey 7 unspecified role unspecified role bait bait association association 7a These three protein plus FLIP form the DISC complex, involved in induction of apoptosis via the extrinsic pathway. Treatment with anti-APO-1 antibody (recognizes an epitope on the extracellular part of fas) is required for the complex to be formed. The presence of the p43/p41 fragment of casp8 and of fadd was disrupted when the mannosidase inhibitor DMM (causes inmature glycosylation of fas) was used.