DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. Structure (London, England : 1993) 2012 imex curation Aitio O., Hellman M., Skehan B., Kesti T., Leong JM., Saksela K., Permi P. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Aitio O., Hellman M., Skehan B., Kesti T., Leong JM., Saksela K., Permi P. DIP original experiment: DIP-250994X Structure (London, England : 1993) 2012 IMEx Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. Structure (London, England : 1993) 2012 imex curation Aitio O., Hellman M., Skehan B., Kesti T., Leong JM., Saksela K., Permi P. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Aitio O., Hellman M., Skehan B., Kesti T., Leong JM., Saksela K., Permi P. DIP original experiment: DIP-250993X Structure (London, England : 1993) 2012 IMEx Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. Structure (London, England : 1993) 2012 imex curation Aitio O., Hellman M., Skehan B., Kesti T., Leong JM., Saksela K., Permi P. Only protein-protein interactions human Homo sapiens Human pull down pull down anti tag western anti tag western blot anti tag western Aitio O., Hellman M., Skehan B., Kesti T., Leong JM., Saksela K., Permi P. DIP original experiment: DIP-250988X Structure (London, England : 1993) 2012 IMEx Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. Structure (London, England : 1993) 2012 imex curation Aitio O., Hellman M., Skehan B., Kesti T., Leong JM., Saksela K., Permi P. 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 Aitio O., Hellman M., Skehan B., Kesti T., Leong JM., Saksela K., Permi P. DIP original experiment: DIP-250989X Structure (London, England : 1993) 2012 IMEx Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. Structure (London, England : 1993) 2012 imex curation Aitio O., Hellman M., Skehan B., Kesti T., Leong JM., Saksela K., Permi P. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Aitio O., Hellman M., Skehan B., Kesti T., Leong JM., Saksela K., Permi P. DIP original experiment: DIP-250995X Structure (London, England : 1993) 2012 IMEx Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. Structure (London, England : 1993) 2012 imex curation Aitio O., Hellman M., Skehan B., Kesti T., Leong JM., Saksela K., Permi P. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Aitio O., Hellman M., Skehan B., Kesti T., Leong JM., Saksela K., Permi P. DIP original experiment: DIP-250991X Structure (London, England : 1993) 2012 IMEx Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. Structure (London, England : 1993) 2012 imex curation Aitio O., Hellman M., Skehan B., Kesti T., Leong JM., Saksela K., Permi P. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Aitio O., Hellman M., Skehan B., Kesti T., Leong JM., Saksela K., Permi P. DIP original experiment: DIP-250996X Structure (London, England : 1993) 2012 IMEx Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. Structure (London, England : 1993) 2012 imex curation Aitio O., Hellman M., Skehan B., Kesti T., Leong JM., Saksela K., Permi P. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Aitio O., Hellman M., Skehan B., Kesti T., Leong JM., Saksela K., Permi P. DIP original experiment: DIP-250990X Structure (London, England : 1993) 2012 IMEx Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. Structure (London, England : 1993) 2012 imex curation Aitio O., Hellman M., Skehan B., Kesti T., Leong JM., Saksela K., Permi P. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Aitio O., Hellman M., Skehan B., Kesti T., Leong JM., Saksela K., Permi P. DIP original experiment: DIP-250992X Structure (London, England : 1993) 2012 IMEx Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. 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 wasl_human Neural Wiskott-Aldrich syndrome protein WASL protein protein human Homo sapiens Human MSSVQQQPPPPRRVTNVGSLLLTPQENESLFTFLGKKCVTMSSAVVQLYAADRNCMWSKKCSGVACLVKDNPQRSYFLRIFDIKDGKLLWEQELYNNFVYNSPRGYFHTFAGDTCQVALNFANEEEAKKFRKAVTDLLGRRQRKSEKRRDPPNGPNLPMATVDIKNPEITTNRFYGPQVNNISHTKEKKKGKAKKKRLTKADIGTPSNFQHIGHVGWDPNTGFDLNNLDPELKNLFDMCGISEAQLKDRETSKVIYDFIEKTGGVEAVKNELRRQAPPPPPPSRGGPPPPPPPPHNSGPPPPPARGRGAPPPPPSRAPTAAPPPPPPSRPSVAVPPPPPNRMYPPPPPALPSSAPSGPPPPPPSVLGVGPVAPPPPPPPPPPPGPPPPPGLPSDGDHQVPTTAGNKAALLDQIREGAQLKKVEQNSRPVSCSGRDALLDQIRQGIQLKSVADGQESTPPTPAPTSGIVGALMEVMQKRSKAIHSSDEDEDEDDEEDFEDDDEWED DIP protein O00401 original sequence version: 55 DIP protein O00401 original sequence version: 147 DIP protein O00401 original sequence version: 150 DIP protein O00401 original sequence version: 136 DIP protein O00401 original sequence version: 138 DIP protein O00401 original sequence version: 125 DIP protein O00401 original sequence version: 112 DIP protein O00401 original sequence version: 126 B5895C6055E23049 bi2l1_human Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1 BAIAP2L1 IRTKS Insulin receptor tyrosine kinase substrate protein protein human Homo sapiens Human MSRGPEEVNRLTESTYRNVMEQFNPGLRNLINLGKNYEKAVNAMILAGKAYYDGVAKIGEIATGSPVSTELGHVLIEISSTHKKLNESLDENFKKFHKEIIHELEKKIELDVKYMNATLKRYQTEHKNKLESLEKSQAELKKIRRKSQGSRNALKYEHKEIEYVETVTSRQSEIQKFIADGCKEALLEEKRRFCFLVDKHCGFANHIHYYHLQSAELLNSKLPRWQETCVDAIKVPEKIMNMIEEIKTPASTPVSGTPQASPMIERSNVVRKDYDTLSKCSPKMPPAPSGRAYTSPLIDMFNNPATAAPNSQRVNNSTGTSEDPSLQRSVSVATGLNMMKKQKVKTIFPHTAGSNKTLLSFAQGDVITLLIPEEKDGWLYGEHDVSKARGWFPSSYTKLLEENETEAVTVPTPSPTPVRSISTVNLSENSSVVIPPPDYLECLSMGAAADRRADSARTTSTFKAPASKPETAAPNDANGTAKPPFLSGENPFATVKLRPTVTNDRSAPIIR DIP protein Q9UHR4 original sequence version: 103 DIP protein Q9UHR4 original sequence version: 94 C2304C4444B02F02 esfu2_eco57 Secreted effector protein EspF(U) espF(U) tccP EspF-like protein encoded on prophage U Tir-cytoskeleton coupling protein TccP ECs2715 protein protein eco57 Escherichia coli O157:H7 MINNVSSLFPTVNRNITAVYKKSSFSVSPQKITLNPVKISSPFSPSSSSISATTLFRAPNAHSASFHRQSTAESSLHQQLPNVRQRLIQHLAEHGIKPARSMAEHIPPAPNWPAPPPPVQNEQSRPLPDVAQRLVQHLAEHGIQPARNMAEHIPPAPNWPAPPLPVQNEQSRPLPDVAQRLVQHLAEHGIQPARSMAEHIPPAPNWPAPPPPVQNEQSRPLPDVAQRLMQHLAEHGIQPARNMAEHIPPAPNWPAPTPPVQNEQSRPLPDVAQRLMQHLAEHGIQPARNMAEHIPPAPNWPAPTPPVQNEQSRPLPDVAQRLMQHLAEHGINTSKRS DIP protein P0DJ89 original sequence version: 5 This sequence has been withdrawn from Uniprot. 49A1BE2EA220E1C0 baiap2l1-eps8-1 3 10 unspecified role unspecified role prey prey Q12929:p.Ala215Trp A215W mutation increasing strength mutation increasing interaction strength mutation increasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain A W This feature has been corrected as a result of our quality control procedures. The original label was 'A215W'. Wed May 02 20:08:17 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ala215trp' Tue Jun 30 15:45:07 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ala215Trp' Myc-tag Myc-tag myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined human Homo sapiens Human 12 unspecified role unspecified role bait bait Biotin-tag Biotin-tag biotin tag biotin tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined human Homo sapiens Human physical association physical association baiap2l1-espf(u)-1 8 13 unspecified role unspecified role unspecified role unspecified role P0DJ88:p.Trp300Ala W301A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain W A Wed May 02 17:53:19 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp300ala' Tue Jun 30 15:39:46 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp300Ala' Region 292-311 Region 292-311 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 12 unspecified role unspecified role unspecified role unspecified role SH3 domain Region 339-402 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction baiap2l1-eps8-2 5 10 unspecified role unspecified role unspecified role unspecified role Region 207-226 Region 207-226 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 12 unspecified role unspecified role unspecified role unspecified role SH3 domain Region 339-402 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction espf(u)-wasl-1 9 11 unspecified role unspecified role unspecified role unspecified role GBD domain Region 207-270 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 13 unspecified role unspecified role unspecified role unspecified role Region 268-314 Region 268-314 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction baiap2l1-espf(u)-2 4 13 unspecified role unspecified role prey prey Region 292-314 Region 292-314 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain P0DJ88:p.Trp300Ala W301A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain W A Wed May 02 15:45:37 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp300ala' Tue Jun 30 20:23:48 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp300Ala' yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 12 unspecified role unspecified role bait bait SH3 domain Region 339-402 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast direct interaction direct interaction baiap2l1-espf(u)-3 1 12 unspecified role unspecified role unspecified role unspecified role SH3 domain Region 339-402 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 13 unspecified role unspecified role unspecified role unspecified role Region 268-314 Region 268-314 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction baiap2l1-espf(u)-4 7 13 unspecified role unspecified role unspecified role unspecified role Region 292-311 Region 292-311 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 12 unspecified role unspecified role unspecified role unspecified role SH3 domain Region 339-402 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction baiap2l1-eps8-3 6 10 unspecified role unspecified role unspecified role unspecified role Q12929:p.Ala215Trp A215W mutation increasing strength mutation increasing interaction strength mutation increasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain A W This feature has been corrected as a result of our quality control procedures. The original label was 'A215W'. Wed May 02 15:17:40 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ala215trp' Tue Jun 30 16:38:17 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ala215Trp' Region 207-226 Region 207-226 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 12 unspecified role unspecified role unspecified role unspecified role SH3 domain Region 339-402 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction baiap2l1-espf(u)-5 2 12 unspecified role unspecified role unspecified role unspecified role SH3 domain Region 339-402 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 11 unspecified role unspecified role unspecified role unspecified role GBD domain Region 207-270 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 13 unspecified role unspecified role unspecified role unspecified role Region 268-314 Region 268-314 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association