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/ Apoptosis-linked gene 2 binds to the death domain of Fas and dissociates from Fas during Fas-mediated apoptosis in Jurkat cells. Apoptosis-linked gene 2 binds to the death domain of Fas and dissociates from Fas during Fas-mediated apoptosis in Jurkat cells. Biochem. Biophys. Res. Commun. (0006-291X) 2001 imex curation Jung YS., Kim KS., Kim KD., Lim JS., Kim JW., Kim E. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer The mutation in the Faslpr mutant is not specified. Thus this data could not be added. ehkim@mail.paichai.ac.kr 08-Jul-2008: Contacted by JYOTI. davet Only protein-protein interactions human-jurkat Homo sapiens jurkat Human T cell leukemia anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Jung YS., Kim KS., Kim KD., Lim JS., Kim JW., Kim E. Apoptosis - Interactions involving proteins with a function related to apoptosis The mutation in the Faslpr mutant is not specified. Thus this data could not be added. ehkim@mail.paichai.ac.kr Accepted 2008-JUN-13 by DAVET. 08-Jul-2008: Contacted by JYOTI. Biochem. Biophys. Res. Commun. (0006-291X) 2001 davet Only protein-protein interactions imex curation Apoptosis-linked gene 2 binds to the death domain of Fas and dissociates from Fas during Fas-mediated apoptosis in Jurkat cells. Apoptosis-linked gene 2 binds to the death domain of Fas and dissociates from Fas during Fas-mediated apoptosis in Jurkat cells. Biochem. Biophys. Res. Commun. (0006-291X) 2001 imex curation Jung YS., Kim KS., Kim KD., Lim JS., Kim JW., Kim E. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer The mutation in the Faslpr mutant is not specified. Thus this data could not be added. ehkim@mail.paichai.ac.kr 08-Jul-2008: Contacted by JYOTI. davet Only protein-protein interactions in vitro In vitro pull down pull down weight autoradiogra molecular weight estimation by autoradiography weight autoradiogra Jung YS., Kim KS., Kim KD., Lim JS., Kim JW., Kim E. Apoptosis - Interactions involving proteins with a function related to apoptosis ehkim@mail.paichai.ac.kr Accepted 2008-JUL-30 by DAVET. 08-Jul-2008: Contacted by JYOTI. Biochem. Biophys. Res. Commun. (0006-291X) 2001 davet Only protein-protein interactions imex curation Apoptosis-linked gene 2 binds to the death domain of Fas and dissociates from Fas during Fas-mediated apoptosis in Jurkat cells. Apoptosis-linked gene 2 binds to the death domain of Fas and dissociates from Fas during Fas-mediated apoptosis in Jurkat cells. Biochem. Biophys. Res. Commun. (0006-291X) 2001 imex curation Jung YS., Kim KS., Kim KD., Lim JS., Kim JW., Kim E. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer The mutation in the Faslpr mutant is not specified. Thus this data could not be added. ehkim@mail.paichai.ac.kr 08-Jul-2008: Contacted by JYOTI. davet Only protein-protein interactions yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Jung YS., Kim KS., Kim KD., Lim JS., Kim JW., Kim E. Apoptosis - Interactions involving proteins with a function related to apoptosis The coordinates for the death domain for Fas were taken from the UniProtKB entry for the protein. The mutation in the Faslpr mutant is not specified. Thus this data could not be added. ehkim@mail.paichai.ac.kr Accepted 2008-JUL-30 by DAVET. 08-Jul-2008: Contacted by JYOTI. Biochem. Biophys. Res. Commun. (0006-291X) 2001 davet Only protein-protein interactions imex curation 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 pdcd6_mouse Programmed cell death protein 6 Pdcd6 Alg2 Apoptosis-linked gene 2 protein PMP41 ALG-257 protein protein mouse Mus musculus Mouse MAAYSYRPGPGGGPGPAAGAALPDQSFLWNVFQRVDKDRSGVISDNELQQALSNGTWTPFNPVTVRSIISMFDRENKAGVNFSEFTGVWKYITDWQNVFRTYDRDNSGMIDKNELKQALSGFGYRLSDQFHDILIRKFDRQGRGQIAFDDFIQGCIVLQRLTDIFRRYDTDQDGWIQVSYEQYLSMVFSIV 2704E984BF7F6F40 pdcd6_human Programmed cell death protein 6 PDCD6 ALG2 Apoptosis-linked gene 2 protein homolog protein protein human Homo sapiens Human MAAYSYRPGPGAGPGPAAGAALPDQSFLWNVFQRVDKDRSGVISDTELQQALSNGTWTPFNPVTVRSIISMFDRENKAGVNFSEFTGVWKYITDWQNVFRTYDRDNSGMIDKNELKQALSGFGYRLSDQFHDILIRKFDRQGRGQIAFDDFIQGCIVLQRLTDIFRRYDTDQDGWIQVSYEQYLSMVFSIV DIP protein O75340 original sequence version: 73 DIP protein O75340 original sequence version: 154 D0B5944CF3C696AD fas-pdcd6 3 5 unspecified role unspecified role prey prey 4 unspecified role unspecified role bait bait region Death domain sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis range range range range physical association physical association ALG-2 interacted with Fas in yeast The coordinates for the death domain for Fas were taken from the UniProtKB entry for the protein, as they were not provided by the authors. Thus the coordinates have been given as fuzzy coordinates. pdcd6-fas 2 4 unspecified role unspecified role prey prey region 35s radiolabel 35s radiolabel 35S s35 radiolabelled S35 s35 radiolabelled 35S S35 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined in vitro In vitro 5 unspecified role unspecified role prey prey region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined n-terminal EF-1 and EF-2 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain c-terminal EF-3, EF-4 and EF-5 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecobb Escherichia coli (strain B / BL21) physical association physical association 4 These data show that the interaction of ALG-2 and Fas is Ca21-dependent and the PEF domain is sufficient to allow the binding. Calcium ions - This interaction is dependent upon the presence of Ca2+. fas-pdcd6-1 1 6 unspecified role unspecified role prey prey 4 unspecified role unspecified role bait bait physical association physical association 5 A Endogenous ALG-2 was present in the immunoprecipitates of Jurkat cels which received up to 1 h of CH11 anti-Fas Ab treatment This interaction took place in resting Jurkat cells and in cels which received up to 1 h of CH11 anti-Fas Ab treatment. This interaction was not detected when cells were treated for more than 2 h with CH11 anti-Fas Ab.