DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors. Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors. Nature structural & molecular biology 2014 imex curation Kast DJ., Yang C., Disanza A., Boczkowska M., Madasu Y., Scita G., Svitkina T., Dominguez R. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Kast DJ., Yang C., Disanza A., Boczkowska M., Madasu Y., Scita G., Svitkina T., Dominguez R. DIP original experiment: DIP-260854X Nature structural & molecular biology 2014 IMEx Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors. Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors. Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors. Nature structural & molecular biology 2014 imex curation Kast DJ., Yang C., Disanza A., Boczkowska M., Madasu Y., Scita G., Svitkina T., Dominguez R. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Kast DJ., Yang C., Disanza A., Boczkowska M., Madasu Y., Scita G., Svitkina T., Dominguez R. DIP original experiment: DIP-260853X Nature structural & molecular biology 2014 IMEx Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors. Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors. Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors. Nature structural & molecular biology 2014 imex curation Kast DJ., Yang C., Disanza A., Boczkowska M., Madasu Y., Scita G., Svitkina T., Dominguez R. Only protein-protein interactions in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Kast DJ., Yang C., Disanza A., Boczkowska M., Madasu Y., Scita G., Svitkina T., Dominguez R. DIP original experiment: DIP-260859X Nature structural & molecular biology 2014 IMEx Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors. Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors. Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors. Nature structural & molecular biology 2014 imex curation Kast DJ., Yang C., Disanza A., Boczkowska M., Madasu Y., Scita G., Svitkina T., Dominguez R. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Kast DJ., Yang C., Disanza A., Boczkowska M., Madasu Y., Scita G., Svitkina T., Dominguez R. DIP original experiment: DIP-260852X Nature structural & molecular biology 2014 IMEx Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors. Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors. Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors. Nature structural & molecular biology 2014 imex curation Kast DJ., Yang C., Disanza A., Boczkowska M., Madasu Y., Scita G., Svitkina T., Dominguez R. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Kast DJ., Yang C., Disanza A., Boczkowska M., Madasu Y., Scita G., Svitkina T., Dominguez R. DIP original experiment: DIP-260860X Nature structural & molecular biology 2014 IMEx Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors. Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors. Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors. Nature structural & molecular biology 2014 imex curation Kast DJ., Yang C., Disanza A., Boczkowska M., Madasu Y., Scita G., Svitkina T., Dominguez R. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Kast DJ., Yang C., Disanza A., Boczkowska M., Madasu Y., Scita G., Svitkina T., Dominguez R. DIP original experiment: DIP-260858X Nature structural & molecular biology 2014 IMEx Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors. Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors. Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors. Nature structural & molecular biology 2014 imex curation Kast DJ., Yang C., Disanza A., Boczkowska M., Madasu Y., Scita G., Svitkina T., Dominguez R. Only protein-protein interactions in vitro In vitro fret fluorescent resonance energy transfer FRET RET FRET analysis FRET RET FRET analysis fret predetermined predetermined participant predetermined Kast DJ., Yang C., Disanza A., Boczkowska M., Madasu Y., Scita G., Svitkina T., Dominguez R. DIP original experiment: DIP-260856X Nature structural & molecular biology 2014 IMEx Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors. Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors. Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors. Nature structural & molecular biology 2014 imex curation Kast DJ., Yang C., Disanza A., Boczkowska M., Madasu Y., Scita G., Svitkina T., Dominguez R. Only protein-protein interactions ecolx Escherichia coli solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Kast DJ., Yang C., Disanza A., Boczkowska M., Madasu Y., Scita G., Svitkina T., Dominguez R. DIP original experiment: DIP-260861X Nature structural & molecular biology 2014 IMEx Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors. Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors. Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors. Nature structural & molecular biology 2014 imex curation Kast DJ., Yang C., Disanza A., Boczkowska M., Madasu Y., Scita G., Svitkina T., Dominguez R. Only protein-protein interactions in vitro In vitro fret fluorescent resonance energy transfer FRET RET FRET analysis FRET RET FRET analysis fret predetermined predetermined participant predetermined Kast DJ., Yang C., Disanza A., Boczkowska M., Madasu Y., Scita G., Svitkina T., Dominguez R. DIP original experiment: DIP-260857X Nature structural & molecular biology 2014 IMEx Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors. Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors. Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors. Nature structural & molecular biology 2014 imex curation Kast DJ., Yang C., Disanza A., Boczkowska M., Madasu Y., Scita G., Svitkina T., Dominguez R. Only protein-protein interactions in vitro In vitro fret fluorescent resonance energy transfer FRET RET FRET analysis FRET RET FRET analysis fret predetermined predetermined participant predetermined Kast DJ., Yang C., Disanza A., Boczkowska M., Madasu Y., Scita G., Svitkina T., Dominguez R. DIP original experiment: DIP-260855X Nature structural & molecular biology 2014 IMEx Mechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectors. eps8_human Epidermal growth factor receptor kinase substrate 8 EPS8 protein protein human Homo sapiens Human MNGHISNHPSSFGMYPSQMNGYGSSPTFSQTDREHGSKTSAKALYEQRKNYARDSVSSVSDISQYRVEHLTTFVLDRKDAMITVDDGIRKLKLLDAKGKVWTQDMILQVDDRAVSLIDLESKNELENFPLNTIQHCQAVMHSCSYDSVLALVCKEPTQNKPDLHLFQCDEVKANLISEDIESAISDSKGGKQKRRPDALRMISNADPSIPPPPRAPAPAPPGTVTQVDVRSRVAAWSAWAADQGDFEKPRQYHEQEETPEMMAARIDRDVQILNHILDDIEFFITKLQKAAEAFSELSKRKKNKKGKRKGPGEGVLTLRAKPPPPDEFLDCFQKFKHGFNLLAKLKSHIQNPSAADLVHFLFTPLNMVVQATGGPELASSVLSPLLNKDTIDFLNYTVNGDERQLWMSLGGTWMKARAEWPKEQFIPPYVPRFRNGWEPPMLNFMGATMEQDLYQLAESVANVAEHQRKQEIKRLSTEHSSVSEYHPADGYAFSSNIYTRGSHLDQGEAAVAFKPTSNRHIDRNYEPLKTQPKKYAKSKYDFVARNNSELSVLKDDILEILDDRKQWWKVRNASGDSGFVPNNILDIVRPPESGLGRADPPYTHTIQKQRMEYGPRPADTPPAPSPPPTPAPVPVPLPPSTPAPVPVSKVPANITRQNSSSSDSGGSIVRDSQRHKQLPVDRRKSQMEEVQDELIHRLTIGRSAAQKKFHVPRQNVPVINITYDSTPEDVKTWLQSKGFNPVTVNSLGVLNGAQLFSLNKDELRTVCPEGARVYSQITVQKAALEDSSGSSELQEIMRRRQEKISAAASDSGVESFDEGSSH DIP protein Q12929 original sequence version: 88 DIP protein Q12929 original sequence version: 125 DIP protein Q12929 original sequence version: 109 DIP protein Q12929 original sequence version: 99 AC5EB1D28B784B3B q9uqb8-4 Brain-specific angiogenesis inhibitor 1-associated protein 2 BAIAP2-alpha BAIAP2 Fas ligand-associated factor 3 Insulin receptor substrate p53/p58 Insulin receptor substrate protein of 53 kDa protein protein human Homo sapiens Human MSLSRSEEMHRLTENVYKTIMEQFNPSLRNFIAMGKNYEKALAGVTYAAKGYFDALVKMGELASESQGSKELGDVLFQMAEVHRQIQNQLEEMLKSFHNELLTQLEQKVELDSRYLSAALKKYQTEQRSKGDALDKCQAELKKLRKKSQGSKNPQKYSDKELQYIDAISNKQGELENYVSDGYKTALTEERRRFCFLVEKQCAVAKNSAAYHSKGKELLAQKLPLWQQACADPSKIPERAVQLMQQVASNGATLPSALSASKSNLVISDPIPGAKPLPVPPELAPFVGRMSAQESTPIMNGVTGPDGEDYSPWADRKAAQPKSLSPPQSQSKLSDSYSNTLPVRKSVTPKNSYATTENKTLPRSSSMAAGLERNGRMRVKAIFSHAAGDNSTLLSFKEGDLITLLVPEARDGWHYGESEKTKMRGWFPFSYTRVLDSDGSDRLHMSLQQGKSSSTGNLLDKDDLAIPPPDYGAASRAFPAQTASGFKQRPYSVAVPAFSQGLDDYGARSMSSGSGTLVSTV DIP protein Q9UQB8-4 original sequence version: 97 DIP protein Q9UQB8-4 original sequence version: 125 618A09FDBEB3A5C3 p60953-2 Cell division control protein 42 homolog CDC42 G25K GTP-binding protein Placental protein protein human Homo sapiens Human MQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAGQEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLRDDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQKGLKNVFDEAILAALEPPEPKKSRRCVLL DIP protein P60953-2 original sequence version: 152 DIP protein P60953 original sequence version: 98 DIP protein P60953 original sequence version: 148 DIP protein P60953 original sequence version: 142 DIP protein P60953-2 original sequence version: 135 DIP protein P60953 original sequence version: 99 DIP protein P60953-2 original sequence version: 139 DIP protein P60953 original sequence version: 144 DIP protein P60953 original sequence version: 163 DIP protein P60953 original sequence version: 158 DIP protein P60953-2 original sequence version: 147 DIP protein P60953 original sequence version: 123 51A437E22A4D8FFF baiap2-cdc42-4 4 12 unspecified role unspecified role unspecified role unspecified role Region 260-291 Region 260-291 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 13 unspecified role unspecified role unspecified role unspecified role Region 1-178 Region 1-178 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P60953-2:p.Gly12Val G12V mutation mutation certain certain sequence position certain certain certain sequence position certain G V This feature has been corrected as a result of our quality control procedures. The original label was 'G12V'. Wed May 02 17:53:50 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly12val' Tue Jun 30 18:28:41 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly12Val' ecolx Escherichia coli direct interaction direct interaction baiap2-eps8-4 3 11 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 12 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction baiap2-cdc42-5 1 12 unspecified role unspecified role unspecified role unspecified role Region 1-452 Region 1-452 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain Q9UQB8-4:p.[Pro278Asp;Pro281Asp] P278D/P281D mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain P D certain certain sequence position certain certain certain sequence position certain P D This feature has been corrected as a result of our quality control procedures. The original label was 'P278D/P281D'. Wed May 02 15:10:58 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'pro278asp,pro281asp' Tue Jun 30 20:11:34 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Pro278Asp;Pro281Asp]' Q9UQB8-4:p.[Ile267Ala;Ser268Ala] I267A/S268A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain S A certain certain sequence position certain certain certain sequence position certain I A This feature has been corrected as a result of our quality control procedures. The original label was 'I267A/S268A'. Wed May 02 20:20:54 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile267ala,ser268ala' Tue Jun 30 16:21:58 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Ile267Ala;Ser268Ala]' Q9UQB8-4:p.[Leu277Glu;Phe286Glu] L277E/F286E mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain F E certain certain sequence position certain certain certain sequence position certain L E This feature has been corrected as a result of our quality control procedures. The original label was 'L277E/F286E'. Wed May 02 14:58:56 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu277glu,phe286glu' Tue Jun 30 18:19:39 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Leu277Glu;Phe286Glu]' Q9UQB8-4:p.Phe286Glu F286E mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain F E This feature has been corrected as a result of our quality control procedures. The original label was 'F286E'. Wed May 02 20:31:00 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe286glu' Tue Jun 30 18:35:43 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe286Glu' ecolx Escherichia coli 13 unspecified role unspecified role unspecified role unspecified role Region 1-178 Region 1-178 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P60953-2:p.Gly12Val G12V mutation mutation certain certain sequence position certain certain certain sequence position certain G V This feature has been corrected as a result of our quality control procedures. The original label was 'G12V'. Wed May 02 20:22:19 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly12val' Tue Jun 30 18:38:34 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly12Val' ecolx Escherichia coli direct interaction direct interaction baiap2-cdc42-6 10 12 unspecified role unspecified role fret pair fluorescence acceptor donor pair fret pair Region 1-452 Region 1-452 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Fluorescein-label Fluorescein-label fluor-5-maleimide fluorescein-5-maleimide label fluor-5-maleimide certain certain sequence position certain certain certain sequence position certain Rhodamine-label Rhodamine-label rhodamine label rhodamine label certain certain sequence position certain certain certain sequence position certain Q9UQB8-4:p.[Pro278Asp;Pro281Asp] P278D/P281D mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain P D certain certain sequence position certain certain certain sequence position certain P D This feature has been corrected as a result of our quality control procedures. The original label was 'P278D/P281D'. Wed May 02 19:26:29 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'pro278asp,pro281asp' Tue Jun 30 17:00:53 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Pro278Asp;Pro281Asp]' ecolx Escherichia coli 13 unspecified role unspecified role neutral component neutral component Region 1-178 Region 1-178 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P60953-2:p.Gly12Val G12V mutation mutation certain certain sequence position certain certain certain sequence position certain G V This feature has been corrected as a result of our quality control procedures. The original label was 'G12V'. Wed May 02 19:04:33 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly12val' Tue Jun 30 18:40:09 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly12Val' ecolx Escherichia coli direct interaction direct interaction baiap2-eps8-5 9 11 unspecified role unspecified role neutral component neutral component ecolx Escherichia coli 12 unspecified role unspecified role fret pair fluorescence acceptor donor pair fret pair Region 1-452 Region 1-452 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Fluorescein-label Fluorescein-label fluor-5-maleimide fluorescein-5-maleimide label fluor-5-maleimide certain certain sequence position certain certain certain sequence position certain Rhodamine-label Rhodamine-label rhodamine label rhodamine label certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction baiap2-cdc42-7 2 12 unspecified role unspecified role unspecified role unspecified role Region 260-291 Region 260-291 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 13 unspecified role unspecified role unspecified role unspecified role Region 1-178 Region 1-178 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P60953-2:p.Gly12Val G12V mutation mutation certain certain sequence position certain certain certain sequence position certain G V This feature has been corrected as a result of our quality control procedures. The original label was 'G12V'. Wed May 02 20:17:17 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly12val' Tue Jun 30 18:17:04 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly12Val' ecolx Escherichia coli direct interaction direct interaction baiap2-1 8 12 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction baiap2-eps8-6 6 11 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 12 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction baiap2-cdc42-8 7 12 unspecified role unspecified role fret pair fluorescence acceptor donor pair fret pair Fluorescein-label Fluorescein-label fluor-5-maleimide fluorescein-5-maleimide label fluor-5-maleimide certain certain sequence position certain certain certain sequence position certain Rhodamine-label Rhodamine-label rhodamine label rhodamine label certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 13 unspecified role unspecified role neutral component neutral component Region 1-178 Region 1-178 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P60953-2:p.Gly12Val G12V mutation mutation certain certain sequence position certain certain certain sequence position certain G V This feature has been corrected as a result of our quality control procedures. The original label was 'G12V'. Wed May 02 17:13:36 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly12val' Tue Jun 30 17:33:05 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly12Val' ecolx Escherichia coli direct interaction direct interaction baiap2-5 5 12 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction