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/ The RET proto-oncogene induces apoptosis: a novel mechanism for Hirschsprung disease. The RET proto-oncogene induces apoptosis: a novel mechanism for Hirschsprung disease. EMBO J. (0261-4189) 2000 imex curation Bordeaux M.C., Forcet C., Granger L., Corset V., Bidaud C., Billaud M., Bredesen D.E., Edery P., Mehlen P. Apoptosis - Interactions involving proteins with a function related to apoptosis mehlen@univ-lyon1.fr 21-Dec-2011: Contacted by JYOTI. Only protein-protein interactions in vitro In vitro protease assay protease assay weight autoradiogra molecular weight estimation by autoradiography weight autoradiogra Bordeaux M.C., Forcet C., Granger L., Corset V., Bidaud C., Billaud M., Bredesen D.E., Edery P., Mehlen P. Apoptosis - Interactions involving proteins with a function related to apoptosis mehlen@univ-lyon1.fr Accepted 2011-OCT-12 by ORCHARD EMBO J. (0261-4189) 2000 Only protein-protein interactions imex curation p07949-2 Proto-oncogene tyrosine-protein kinase receptor Ret RET9 RET CDHF12 Cadherin family member 12 Proto-oncogene c-Ret CDHR16 PTC RET51 protein protein human Homo sapiens Human MAKATSGAAGLRLLLLLLLPLLGKVALGLYFSRDAYWEKLYVDQAAGTPLLYVHALRDAPEEVPSFRLGQHLYGTYRTRLHENNWICIQEDTGLLYLNRSLDHSSWEKLSVRNRGFPLLTVYLKVFLSPTSLREGECQWPGCARVYFSFFNTSFPACSSLKPRELCFPETRPSFRIRENRPPGTFHQFRLLPVQFLCPNISVAYRLLEGEGLPFRCAPDSLEVSTRWALDREQREKYELVAVCTVHAGAREEVVMVPFPVTVYDEDDSAPTFPAGVDTASAVVEFKRKEDTVVATLRVFDADVVPASGELVRRYTSTLLPGDTWAQQTFRVEHWPNETSVQANGSFVRATVHDYRLVLNRNLSISENRTMQLAVLVNDSDFQGPGAGVLLLHFNVSVLPVSLHLPSTYSLSVSRRARRFAQIGKVCVENCQAFSGINVQYKLHSSGANCSTLGVVTSAEDTSGILFVNDTKALRRPKCAELHYMVVATDQQTSRQAQAQLLVTVEGSYVAEEAGCPLSCAVSKRRLECEECGGLGSPTGRCEWRQGDGKGITRNFSTCSPSTKTCPDGHCDVVETQDINICPQDCLRGSIVGGHEPGEPRGIKAGYGTCNCFPEEEKCFCEPEDIQDPLCDELCRTVIAAAVLFSFIVSVLLSAFCIHCYHKFAHKPPISSAEMTFRRPAQAFPVSYSSSGARRPSLDSMENQVSVDAFKILEDPKWEFPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSLRGFLRESRKVGPGYLGSGGSRNSSSLDHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMMVKRRDYLDLAASTPSDSLIYDDGLSEEETPLVDCNNAPLPRALPSTWIENKLYGRISHAFTRF 85868CBFCEA0D24C casp3_human Caspase-3 Apopain Cysteine protease CPP32 Protein Yama SREBP cleavage activity 1 CASP3 CPP32 protein protein human Homo sapiens Human MENTENSVDSKSIKNLEPKIIHGSESMDSGISLDNSYKMDYPEMGLCIIINNKNFHKSTGMTSRSGTDVDAANLRETFRNLKYEVRNKNDLTREEIVELMRDVSKEDHSKRSSFVCVLLSHGEEGIIFGTNGPVDLKKITNFFRGDRCRSLTGKPKLFIIQACRGTELDCGIETDSGVDDDMACHKIPVEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCAMLKQYADKLEFMHILTRVNRKVATEFESFSFDATFHAKKQIPCIVSMLTKELYFYH DIP protein P42574 original sequence version: 108 DIP protein P42574 original sequence version: 171 DIP protein P42574 original sequence version: 111 DIP protein P42574 original sequence version: 105 DIP protein P42574 original sequence version: 131 DIP protein P42574 original sequence version: 132 DIP protein P42574 original sequence version: 134 DIP protein P42574 original sequence version: 162 DIP protein P42574 original sequence version: 189 DIP protein P42574 original sequence version: 167 2F35CD3BCF7FF64A casp3-ret 1 3 enzyme enzyme unspecified role unspecified role purified purified his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range ecoli Escherichia coli (strain K12) 2 enzyme target enzyme target substrate substrate unspecified role unspecified role cell lysate cell lysate P07949-2:p.Asp707Asn mutation mutation mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain D N Wed May 02 14:47:13 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp707asn' Tue Jun 30 17:11:32 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp707Asn' This mutation partially prevents the cleavage of ret and the formation of the 42 and 36 kDa fragments that result from casp3 proteolysis of the wild type. intracellular domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain [35s] labelling 35s radiolabel 35s radiolabel 35S s35 radiolabelled S35 s35 radiolabelled 35S S35 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined P07949-2:p.Asp1017Asn mutation mutation mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain D N Wed May 02 16:18:30 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp1017asn' Tue Jun 30 16:48:54 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp1017Asn' This mutation partially prevents the cleavage of ret and the formation of the 40 and 36 kDa fragments that result from casp3 proteolysis of the wild type. rabit-reticulocyte Oryctolagus cuniculus reticulocyte reticulocyte Reticulocytes protein cleavage protein cleavage 5a and 5b Mutations asp707asn and asp1017asn partially prevent the cleavage of ret and the formation of the 42 and 36 kDa fragments that result from casp3 proteolysis of the wild type.