DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Caspase-activated phosphoinositide binding by CNT-1 promotes apoptosis by inhibiting the AKT pathway. Caspase-activated phosphoinositide binding by CNT-1 promotes apoptosis by inhibiting the AKT pathway. Nature structural & molecular biology 2014 imex curation Nakagawa A., Sullivan KD., Xue D. Only protein-protein interactions in vitro In vitro protease assay protease assay autoradiography autoradiography Nakagawa A., Sullivan KD., Xue D. DIP original experiment: DIP-265522X Nature structural & molecular biology 2014 IMEx Caspase-activated phosphoinositide binding by CNT-1 promotes apoptosis by inhibiting the AKT pathway. Caspase-activated phosphoinositide binding by CNT-1 promotes apoptosis by inhibiting the AKT pathway. Caspase-activated phosphoinositide binding by CNT-1 promotes apoptosis by inhibiting the AKT pathway. Nature structural & molecular biology 2014 imex curation Nakagawa A., Sullivan KD., Xue D. Only protein-protein interactions in vitro In vitro protease assay protease assay autoradiography autoradiography Nakagawa A., Sullivan KD., Xue D. DIP original experiment: DIP-265521X Nature structural & molecular biology 2014 IMEx Caspase-activated phosphoinositide binding by CNT-1 promotes apoptosis by inhibiting the AKT pathway. q9xxh8-1 Arf-GAP with ANK repeat and PH domain-containing protein cnt-1 CED-3 protease suppressor Centaurin 1 cnt-1 cps-2 Y17G7B.15 protein protein caeel Caenorhabditis elegans MTVSNNGMAMPSVPPKIDCSEAIQDSPKFRATVAQHAMYFNRLENRLNEMLRHITAMIDFSKNYTNTFYKLTVSVNQLCDESFSGNPLASTTFQGLSEAYAHTVNLFRTYFDHSNVVTFTKLSNFIKIELTKVAESRAHFENMSQSMDDALVKNASISRQKPADATEGRNALTAVGTCFAHTTLDYVANINIAHAHKDHMILDALWTLVRESSAFFSKGHATFDEWTAADNGAIADTIQTFAAKSKLIERKMQDVHSLVPKEMFQHPSGMPIEPDVMMEGYLYKRSSNAFKTWNRRWFQIKDKQLLYSHRSTDLEPATIMEENLRICLVRPAPSNIDRIGCFELVTPTRIHLLQADSESLCQDWMRALQRTILALHEGDSVDVASTSPRNKTTSMSSGVTLTSANAISPLSNAMDVTKGRSVSDPASTYTSANTSSISTAAGFSSSTTAFEQVRRVPGNEVCADCGSPAPKWVSINLGVVLCIECSGAHRSLGVQTSKVRSLCMDSIDNELRDVLLALGNRQVNEIFLAHLPPADSIVPPQINEKSARPAREAWIKAKYVERRFAVAEDTRARSSATNRQEHLKHKTSIGGNSSSNGVNRSSSYADVQDAESGGLLDADPWSADLSVPVPTASKRLSACGSDTNLDAIGSSSIDTKTVEWDSVKEACECGDLLALMTAYAQGFDLNALHNGTTALHIATRNGQTAAVEFLLLNGAKINMLDEKLNTPLHLAAKEGHTLPVCQLLKRGADSNLANVDSKTPLDIAMECTHADIVTLFRVTIMRNDFNADFNNPMDETVEAVISDIARRAATEKEQKKTESLKSTSDI EF747E7B46A1F217 q9xxh8-2 Arf-GAP with ANK repeat and PH domain-containing protein cnt-1 Centaurin 1 CED-3 protease suppressor cnt-1 cps-2 Y17G7B.15 protein protein caeel Caenorhabditis elegans MSTKSIATSSTASSSSSHHQEHTVTELIMFFTSEEPPEPEPFSRSTEKSGIRTSKVITRTITISAETKLKMDLLEEQRREKRVKLEIEKSRIRAENLQRMQEISSEPKTRGSKRSLMRRAAKRTKGRISSLLIRDSSVDSGSITDKALKDKKRGLSLEWEVKDQGRFAESFSDSRLMEMFQHPSGMPIEPDVMMEGYLYKRSSNAFKTWNRRWFQIKDKQLLYSHRSTDLEPATIMEENLRICLVRPAPSNIDRIGCFELVTPTRIHLLQADSESLCQDWMRALQRTILALHEGDSVDVASTSPRNKTTSMSSGVTLTSANAISPLSNAMDVTKGRSVSDPASTYTSANTSSISTAAGFSSSTTAFEQVRRVPGNEVCADCGSPAPKWVSINLGVVLCIECSGAHRSLGVQTSKVRSLCMDSIDNELRDVLLALGNRQVNEIFLAHLPPADSIVPPQINEKSARPAREAWIKAKYVERRFAVAEDTRARSSATNRQEHLKHKTSIGGNSSSNGVNRSSSYADVQDAESGGLLDADPWSADLSVPVPTASKRLSACGSDTNLDAIGSSSIDTKTVEWDSVKEACECGDLLALMTAYAQGFDLNALHNGTTALHIATRNGQTAAVEFLLLNGAKINMLDEKLNTPLHLAAKEGHTLPVCQLLKRGADSNLANVDSKTPLDIAMECTHADIVTLFRVTIMRNDFNADFNNPMDETVEAVISDIARRAATEKEQKKTESLKSTSDI B08C7E5EF44C174F ced3_caeel Cell death protein 3 ced-3 Caspase ced-3 C48D1.2 protein protein caeel Caenorhabditis elegans MMRQDRRSLLERNIMMFSSHLKVDEILEVLIAKQVLNSDNGDMINSCGTVREKRREIVKAVQRRGDVAFDAFYDALRSTGHEGLAEVLEPLARSVDSNAVEFECPMSPASHRRSRALSPAGYTSPTRVHRDSVSSVSSFTSYQDIYSRARSRSRSRALHSSDRHNYSSPPVNAFPSQPSSANSSFTGCSSLGYSSSRNRSFSKASGPTQYIFHEEDMNFVDAPTISRVFDEKTMYRNFSSPRGMCLIINNEHFEQMPTRNGTKADKDNLTNLFRCMGYTVICKDNLTGRGMLLTIRDFAKHESHGDSAILVILSHGEENVIIGVDDIPISTHEIYDLLNAANAPRLANKPKIVFVQACRGERRDNGFPVLDSVDGVPAFLRRGWDNRDGPLFNFLGCVRPQVQQVWRKKPSQADILIAYATTAQYVSWRNSARGSWFIQAVCEVFSTHAKDMDVVELLTEVNKKVACGFQTSQGSNILKQMPEMTSRLLKKFYFWPEARNSAV DIP protein P42573 original sequence version: 122 DIP protein P42573 original sequence version: 131 DIP protein P42573 original sequence version: 85 722D5831F94DAA69 ced_3-cnt_1-1 2 3 enzyme target enzyme target substrate substrate unspecified role unspecified role Q9XXH8-1:p.Asp382Glu D382E mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain D E This feature has been corrected as a result of our quality control procedures. The original label was 'D382E'. Wed May 02 16:12:55 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp382glu' Tue Jun 30 16:42:13 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp382Glu' Q9XXH8-1:p.Asp609Glu D609E mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain D E This feature has been corrected as a result of our quality control procedures. The original label was 'D609E'. Wed May 02 20:17:12 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp609glu' Tue Jun 30 17:02:29 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp609Glu' 35S-label 35S-label 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 enzyme enzyme unspecified role unspecified role ecolx Escherichia coli protein cleavage protein cleavage ced_3-cnt1b-1 1 4 enzyme target enzyme target substrate substrate unspecified role unspecified role Q9XXH8-2:p.Asp298Glu D298E mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain D E Wed May 02 15:59:01 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp298glu' Tue Jun 30 17:48:43 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp298Glu' Q9XXH8-2:p.Asp525Glu D525E mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain D E Wed May 02 15:39:15 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp525glu' Tue Jun 30 19:11:32 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp525Glu' 35S-label 35S-label 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 enzyme enzyme unspecified role unspecified role ecolx Escherichia coli protein cleavage protein cleavage