DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structure (London, England : 1993) 2012 imex curation Aragón E., Goerner N., Xi Q., Gomes T., Gao S., Massagué J., Macias MJ. Only protein-protein interactions in vitro In vitro ion mobility mass spec ion mobility mass spectrometry of complexes ion mobility mass spec predetermined predetermined participant predetermined Aragón E., Goerner N., Xi Q., Gomes T., Gao S., Massagué J., Macias MJ. DIP original experiment: DIP-251010X Structure (London, England : 1993) 2012 IMEx Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structure (London, England : 1993) 2012 imex curation Aragón E., Goerner N., Xi Q., Gomes T., Gao S., Massagué J., Macias MJ. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Aragón E., Goerner N., Xi Q., Gomes T., Gao S., Massagué J., Macias MJ. DIP original experiment: DIP-251005X Structure (London, England : 1993) 2012 IMEx Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structure (London, England : 1993) 2012 imex curation Aragón E., Goerner N., Xi Q., Gomes T., Gao S., Massagué J., Macias MJ. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Aragón E., Goerner N., Xi Q., Gomes T., Gao S., Massagué J., Macias MJ. DIP original experiment: DIP-251003X Structure (London, England : 1993) 2012 IMEx Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structure (London, England : 1993) 2012 imex curation Aragón E., Goerner N., Xi Q., Gomes T., Gao S., Massagué J., Macias MJ. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Aragón E., Goerner N., Xi Q., Gomes T., Gao S., Massagué J., Macias MJ. DIP original experiment: DIP-250998X Structure (London, England : 1993) 2012 IMEx Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structure (London, England : 1993) 2012 imex curation Aragón E., Goerner N., Xi Q., Gomes T., Gao S., Massagué J., Macias MJ. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Aragón E., Goerner N., Xi Q., Gomes T., Gao S., Massagué J., Macias MJ. DIP original experiment: DIP-251002X Structure (London, England : 1993) 2012 IMEx Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structure (London, England : 1993) 2012 imex curation Aragón E., Goerner N., Xi Q., Gomes T., Gao S., Massagué J., Macias MJ. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Aragón E., Goerner N., Xi Q., Gomes T., Gao S., Massagué J., Macias MJ. DIP original experiment: DIP-250997X Structure (London, England : 1993) 2012 IMEx Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structure (London, England : 1993) 2012 imex curation Aragón E., Goerner N., Xi Q., Gomes T., Gao S., Massagué J., Macias MJ. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Aragón E., Goerner N., Xi Q., Gomes T., Gao S., Massagué J., Macias MJ. DIP original experiment: DIP-251004X Structure (London, England : 1993) 2012 IMEx Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structure (London, England : 1993) 2012 imex curation Aragón E., Goerner N., Xi Q., Gomes T., Gao S., Massagué J., Macias MJ. Only protein-protein interactions human Homo sapiens Human anti tag coip anti tag coimmunoprecipitation anti tag coip predetermined predetermined participant predetermined Aragón E., Goerner N., Xi Q., Gomes T., Gao S., Massagué J., Macias MJ. DIP original experiment: DIP-251008X Structure (London, England : 1993) 2012 IMEx Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structure (London, England : 1993) 2012 imex curation Aragón E., Goerner N., Xi Q., Gomes T., Gao S., Massagué J., Macias MJ. Only protein-protein interactions in vitro In vitro ion mobility mass spec ion mobility mass spectrometry of complexes ion mobility mass spec predetermined predetermined participant predetermined Aragón E., Goerner N., Xi Q., Gomes T., Gao S., Massagué J., Macias MJ. DIP original experiment: DIP-251001X Structure (London, England : 1993) 2012 IMEx Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structure (London, England : 1993) 2012 imex curation Aragón E., Goerner N., Xi Q., Gomes T., Gao S., Massagué J., Macias MJ. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Aragón E., Goerner N., Xi Q., Gomes T., Gao S., Massagué J., Macias MJ. DIP original experiment: DIP-250999X Structure (London, England : 1993) 2012 IMEx Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structure (London, England : 1993) 2012 imex curation Aragón E., Goerner N., Xi Q., Gomes T., Gao S., Massagué J., Macias MJ. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Aragón E., Goerner N., Xi Q., Gomes T., Gao S., Massagué J., Macias MJ. DIP original experiment: DIP-251006X Structure (London, England : 1993) 2012 IMEx Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structure (London, England : 1993) 2012 imex curation Aragón E., Goerner N., Xi Q., Gomes T., Gao S., Massagué J., Macias MJ. Only protein-protein interactions human Homo sapiens Human anti tag coip anti tag coimmunoprecipitation anti tag coip predetermined predetermined participant predetermined Aragón E., Goerner N., Xi Q., Gomes T., Gao S., Massagué J., Macias MJ. DIP original experiment: DIP-251007X Structure (London, England : 1993) 2012 IMEx Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structure (London, England : 1993) 2012 imex curation Aragón E., Goerner N., Xi Q., Gomes T., Gao S., Massagué J., Macias MJ. Only protein-protein interactions human Homo sapiens Human anti tag coip anti tag coimmunoprecipitation anti tag coip anti tag western anti tag western blot anti tag western Aragón E., Goerner N., Xi Q., Gomes T., Gao S., Massagué J., Macias MJ. DIP original experiment: DIP-251009X Structure (London, England : 1993) 2012 IMEx Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. Structure (London, England : 1993) 2012 imex curation Aragón E., Goerner N., Xi Q., Gomes T., Gao S., Massagué J., Macias MJ. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Aragón E., Goerner N., Xi Q., Gomes T., Gao S., Massagué J., Macias MJ. DIP original experiment: DIP-251000X Structure (London, England : 1993) 2012 IMEx Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways. yap1_human Transcriptional coactivator YAP1 YAP1 YAP65 Protein yorkie homolog Yes-associated protein YAP65 homolog protein protein human Homo sapiens Human MDPGQQPPPQPAPQGQGQPPSQPPQGQGPPSGPGQPAPAATQAAPQAPPAGHQIVHVRGDSETDLEALFNAVMNPKTANVPQTVPMRLRKLPDSFFKPPEPKSHSRQASTDAGTAGALTPQHVRAHSSPASLQLGAVSPGTLTPTGVVSGPAATPTAQHLRQSSFEIPDDVPLPAGWEMAKTSSGQRYFLNHIDQTTTWQDPRKAMLSQMNVTAPTSPPVQQNMMNSASGPLPDGWEQAMTQDGEIYYINHKNKTTSWLDPRLDPRFAMNQRISQSAPVKQPPPLAPQSPQGGVMGGSNSNQQQQMRLQQLQMEKERLRLKQQELLRQAMRNINPSTANSPKCQELALRSQLPTLEQDGGTQNPVSSPGMSQELRTMTTNSSDPFLNSGTYHSRDESTDSGLSMSSYSVPRTPDDFLNSVDEMDTGDTINQSTLPSQQNRFPDYLEAIPGTNVDLGTLEGDGMNIEGEELMPSLQEALSSDILNDMESVLAATKLDKESFLTWL DIP protein P46937 original sequence version: 143 DIP protein P46937 original sequence version: 98 DIP protein P46937-1 original sequence version: 110 DIP protein P46937 original sequence version: 149 DIP protein P46937 original sequence version: 153 DIP protein P46937 original sequence version: 157 DIP protein P46937 original sequence version: 160 DIP protein P46937 original sequence version: 122 DIP protein P46937 original sequence version: 124 6145F7049ED338AE q96pu5-5 E3 ubiquitin-protein ligase NEDD4-like NEDD4L KIAA0439 NEDD4.2 NEDL3 Nedd4-2 NEDD4Ld HECT-type E3 ubiquitin transferase NED4L protein protein human Homo sapiens Human MATGLGEPVYGLSEDEGESRILRVKVVSGIDLAKKDIFGASDPYVKLSLYVADENRELALVQTKTIKKTLNPKWNEEFYFRVNPSNHRLLFEVFDENRLTRDDFLGQVDVPLSHLPTEDPTMERPYTFKDFLLRPRSHKSRVKGFLRLKMAYMPKNGGQDEENSDQRDDMEHGWEVVDSNDSASQHQEELPPPPLPPGWEEKVDNLGRTYYVNHNNRTTQWHRPSLMDVSSESDNNIRQINQEAAHRRFRSRRHISEDLEPEPSEGGDVPEPWETISEEVNIAGDSLGLALPPPPASPGSRTSPQELSEELSRRLQITPDSNGEQFSSLIQREPSSRLRSCSVTDAVAEQGHLPPPSVAYVHTTPGLPSGWEERKDAKGRTYYVNHNNRTTTWTRPIMQLAEDGASGSATNSNNHLIEPQIRRPRSLSSPTVTLSAPLEGAKDSPVRRAVKDTLSNPQSPQPSPYNSPKPQHKVTQSFLPPGWEMRIAPNGRPFFIDHNTKTTTWEDPRLKFPVHMRSKTSLNPNDLGPLPPGWEERIHLDGRTFYIDHNSKITQWEDPRLQNPAITGPAVPYSREFKQKYDYFRKKLKKPADIPNRFEMKLHRNNIFEESYRRIMSVKRPDVLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDNYTLQINPNSGLCNEDHLSYFTFIGRVAGLAVFHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWILENDPTELDLMFCIDEENFGQTYQVDLKPNGSEIMVTNENKREYIDLVIQWRFVNRVQKQMNAFLEGFTELLPIDLIKIFDENELELLMCGLGDVDVNDWRQHSIYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELYGSNGPQLFTIEQWGSPEKLPRAHTCFNRLDLPPYETFEDLREKLLMAVENAQGFEGVD DIP protein Q96PU5-5 original sequence version: 108 mint homomint A8BB278A37F6A6B5 smad7_human Mothers against decapentaplegic homolog 7 SMAD7 MADH7 MADH8 Mothers against decapentaplegic homolog 8 SMAD family member 7 protein protein human Homo sapiens Human MFRTKRSALVRRLWRSRAPGGEDEEEGAGGGGGGGELRGEGATDSRAHGAGGGGPGRAGCCLGKAVRGAKGHHHPHPPAAGAGAAGGAEADLKALTHSVLKKLKERQLELLLQAVESRGGTRTACLLLPGRLDCRLGPGAPAGAQPAQPPSSYSLPLLLCKVFRWPDLRHSSEVKRLCCCESYGKINPELVCCNPHHLSRLCELESPPPPYSRYPMDFLKPTADCPDAVPSSAETGGTNYLAPGGLSDSQLLLEPGDRSHWCVVAYWEEKTRVGRLYCVQEPSLDIFYDLPQGNGFCLGQLNSDNKSQLVQKVRSKIGCGIQLTREVDGVWVYNRSSYPIFIKSATLDNPDSRTLLVHKVFPGFSIKAFDYEKAYSLQRPNDHEFMQQPWTGFTVQISFVKGWGQCYTRQFISSCPCWLEVIFNSR DIP protein O15105 original sequence version: 121 DIP protein O15105 original sequence version: 131 DIP protein O15105 original sequence version: 139 smuf2_human E3 ubiquitin-protein ligase SMURF2 SMURF2 SMAD ubiquitination regulatory factor 2 SMAD-specific E3 ubiquitin-protein ligase 2 HECT-type E3 ubiquitin transferase SMURF2 protein protein human Homo sapiens Human MSNPGGRRNGPVKLRLTVLCAKNLVKKDFFRLPDPFAKVVVDGSGQCHSTDTVKNTLDPKWNQHYDLYIGKSDSVTISVWNHKKIHKKQGAGFLGCVRLLSNAINRLKDTGYQRLDLCKLGPNDNDTVRGQIVVSLQSRDRIGTGGQVVDCSRLFDNDLPDGWEERRTASGRIQYLNHITRTTQWERPTRPASEYSSPGRPLSCFVDENTPISGTNGATCGQSSDPRLAERRVRSQRHRNYMSRTHLHTPPDLPEGYEQRTTQQGQVYFLHTQTGVSTWHDPRVPRDLSNINCEELGPLPPGWEIRNTATGRVYFVDHNNRTTQFTDPRLSANLHLVLNRQNQLKDQQQQQVVSLCPDDTECLTVPRYKRDLVQKLKILRQELSQQQPQAGHCRIEVSREEIFEESYRQVMKMRPKDLWKRLMIKFRGEEGLDYGGVAREWLYLLSHEMLNPYYGLFQYSRDDIYTLQINPDSAVNPEHLSYFHFVGRIMGMAVFHGHYIDGGFTLPFYKQLLGKSITLDDMELVDPDLHNSLVWILENDITGVLDHTFCVEHNAYGEIIQHELKPNGKSIPVNEENKKEYVRLYVNWRFLRGIEAQFLALQKGFNEVIPQHLLKTFDEKELELIICGLGKIDVNDWKVNTRLKHCTPDSNIVKWFWKAVEFFDEERRARLLQFVTGSSRVPLQGFKALQGAAGPRLFTIHQIDACTNNLPKAHTCFNRIDIPPYESYEKLYEKLLTAIEETCGFAVE DIP protein Q9HAU4 original sequence version: 112 DIP protein Q9HAU4 original sequence version: 123 DIP protein Q9HAU4 original sequence version: 144 3042B443A3755762 q9hce7-1 E3 ubiquitin-protein ligase SMURF1 SMURF1 KIAA1625 HECT-type E3 ubiquitin transferase SMURF1 SMAD ubiquitination regulatory factor 1 SMAD-specific E3 ubiquitin-protein ligase 1 protein protein human Homo sapiens Human MSNPGTRRNGSSIKIRLTVLCAKNLAKKDFFRLPDPFAKIVVDGSGQCHSTDTVKNTLDPKWNQHYDLYVGKTDSITISVWNHKKIHKKQGAGFLGCVRLLSNAISRLKDTGYQRLDLCKLNPSDTDAVRGQIVVSLQTRDRIGTGGSVVDCRGLLENEGTVYEDSGPGRPLSCFMEEPAPYTDSTGAAAGGGNCRFVESPSQDQRLQAQRLRNPDVRGSLQTPQNRPHGHQSPELPEGYEQRTTVQGQVYFLHTQTGVSTWHDPRIPSPSGTIPGGDAAFLYEFLLQGHTSEPRDLNSVNCDELGPLPPGWEVRSTVSGRIYFVDHNNRTTQFTDPRLHHIMNHQCQLKEPSQPLPLPSEGSLEDEELPAQRYERDLVQKLKVLRHELSLQQPQAGHCRIEVSREEIFEESYRQIMKMRPKDLKKRLMVKFRGEEGLDYGGVAREWLYLLCHEMLNPYYGLFQYSTDNIYMLQINPDSSINPDHLSYFHFVGRIMGLAVFHGHYINGGFTVPFYKQLLGKPIQLSDLESVDPELHKSLVWILENDITPVLDHTFCVEHNAFGRILQHELKPNGRNVPVTEENKKEYVRLYVNWRFMRGIEAQFLALQKGFNELIPQHLLKPFDQKELELIIGGLDKIDLNDWKSNTRLKHCVADSNIVRWFWQAVETFDEERRARLLQFVTGSTRVPLQGFKALQGSTGAAGPRLFTIHLIDANTDNLPKAHTCFNRIDIPPYESYEKLYEKLLTAVEETCGFAVE DIP protein Q9HCE7-1 original sequence version: 105 DIP protein Q9HCE7 original sequence version: 116 smad3_human Mothers against decapentaplegic homolog 3 SMAD3 MADH3 SMAD family member 3 JV15-2 protein protein human Homo sapiens Human MSSILPFTPPIVKRLLGWKKGEQNGQEEKWCEKAVKSLVKKLKKTGQLDELEKAITTQNVNTKCITIPRSLDGRLQVSHRKGLPHVIYCRLWRWPDLHSHHELRAMELCEFAFNMKKDEVCVNPYHYQRVETPVLPPVLVPRHTEIPAEFPPLDDYSHSIPENTNFPAGIEPQSNIPETPPPGYLSEDGETSDHQMNHSMDAGSPNLSPNPMSPAHNNLDLQPVTYCEPAFWCSISYYELNQRVGETFHASQPSMTVDGFTDPSNSERFCLGLLSNVNRNAAVELTRRHIGRGVRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIELHLNGPLQWLDKVLTQMGSPSIRCSSVS DIP protein P84022 original sequence version: 57 DIP protein P84022 original sequence version: 112 DIP protein P84022-1 original sequence version: 146 DIP protein P84022-1 original sequence version: 111 46DF5E8B371321AC nedd4l-smad7-1 6 16 unspecified role unspecified role unspecified role unspecified role WW2 domain Region 364-403 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain Q96PU5-5:p.[Lys378Glu;Arg380Glu] K378E/R380E 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 R E certain certain sequence position certain certain certain sequence position certain K E This feature has been corrected as a result of our quality control procedures. The original label was 'K378E/R380E'. Wed May 02 19:10:05 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys378glu,arg380glu' Tue Jun 30 19:07:50 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Lys378Glu;Arg380Glu]' Q96PU5-5:p.Arg380Glu R380E 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 R E This feature has been corrected as a result of our quality control procedures. The original label was 'R380E'. Wed May 02 20:15:54 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg380glu' Tue Jun 30 18:54:53 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg380Glu' Q96PU5-5:p.Lys378Glu K378E 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 K E This feature has been corrected as a result of our quality control procedures. The original label was 'K378E'. Wed May 02 18:44:35 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys378glu' Tue Jun 30 17:52:02 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys378Glu' WW1 domain Region 193-228 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain WW3 domain Region 476-515 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain WW4 domain Region 528-563 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 17 unspecified role unspecified role unspecified role unspecified role Region 203-217 Region 203-217 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro direct interaction direct interaction smad7-yap1-4 14 15 unspecified role unspecified role unspecified role unspecified role WW1 domain Region 163-206 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain WW2 domain Region 227-266 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain P46937:p.Gln186Glu Q186E 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 Q E This feature has been corrected as a result of our quality control procedures. The original label was 'Q186E'. Wed May 02 16:10:48 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gln186glu' Tue Jun 30 19:33:36 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln186Glu' P46937:p.[Asp243Ser;Glu245Gln] D243S/E245Q 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 E Q certain certain sequence position certain certain certain sequence position certain D S This feature has been corrected as a result of our quality control procedures. The original label was 'D243S/E245Q'. Wed May 02 16:09:13 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp243ser,glu245gln' Tue Jun 30 19:22:58 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Asp243Ser;Glu245Gln]' ecolx Escherichia coli 17 unspecified role unspecified role unspecified role unspecified role Region 203-217 Region 203-217 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro direct interaction direct interaction smad3-nedd4l-1 8 16 unspecified role unspecified role prey prey HA-tag HA-tag ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined human Homo sapiens Human 20 unspecified role unspecified role bait bait P84022:p.[Pro181Ala;Pro182Ala] P181A/P182A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain P A certain certain sequence position certain certain certain sequence position certain P A This feature has been corrected as a result of our quality control procedures. The original label was 'P181A/P182A'. Wed May 02 18:47:03 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'pro181ala,pro182ala' Tue Jun 30 16:20:29 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Pro181Ala;Pro182Ala]' P84022:p.Thr179Ala T179A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain T A This feature has been corrected as a result of our quality control procedures. The original label was 'T179A'. Wed May 02 15:49:27 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'thr179ala' Tue Jun 30 18:38:37 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr179Ala' Flag-tag Flag-tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged n-term range n-terminal range n-term range n-term range n-terminal range n-term range human Homo sapiens Human physical association physical association smad7-smurf2-4 7 18 unspecified role unspecified role unspecified role unspecified role WW3 domain Region 297-333 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 17 unspecified role unspecified role unspecified role unspecified role Region 203-217 Region 203-217 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro direct interaction direct interaction smad7-yap1-5 2 15 unspecified role unspecified role unspecified role unspecified role WW1 domain Region 163-206 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 17 unspecified role unspecified role unspecified role unspecified role Region 203-217 Region 203-217 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro direct interaction direct interaction smad7-smurf1-2 9 19 unspecified role unspecified role unspecified role unspecified role WW1/2 domain Region 232-314 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 17 unspecified role unspecified role unspecified role unspecified role Region 203-217 Region 203-217 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro direct interaction direct interaction smad7-smurf1-3 4 19 unspecified role unspecified role unspecified role unspecified role WW2 domain Region 277-314 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain Q9HCE7-1:p.[Gln247Glu;Gln249Glu] Q247E/Q249E 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 Q E certain certain sequence position certain certain certain sequence position certain Q E This feature has been corrected as a result of our quality control procedures. The original label was 'Q247E/Q249E'. Wed May 02 18:39:39 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gln247glu,gln249glu' Tue Jun 30 20:01:56 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Gln247Glu;Gln249Glu]' Q9HCE7-1:p.Gln249Glu Q249E 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 Q E This feature has been corrected as a result of our quality control procedures. The original label was 'Q249E'. Wed May 02 18:38:24 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gln249glu' Tue Jun 30 19:25:39 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln249Glu' Q9HCE7-1:p.Arg243Glu R243E 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 R E This feature has been corrected as a result of our quality control procedures. The original label was 'R243E'. Wed May 02 14:35:49 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg243glu' Tue Jun 30 19:53:45 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg243Glu' Q9HCE7-1:p.Arg243Ala R243A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain R A This feature has been corrected as a result of our quality control procedures. The original label was 'R243A'. Wed May 02 16:36:04 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg243ala' Tue Jun 30 19:38:47 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg243Ala' ecolx Escherichia coli 17 unspecified role unspecified role unspecified role unspecified role Region 203-217 Region 203-217 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro direct interaction direct interaction smad7-yap1-6 11 15 unspecified role unspecified role unspecified role unspecified role WW2 domain Region 227-266 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 17 unspecified role unspecified role unspecified role unspecified role Region 203-217 Region 203-217 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro direct interaction direct interaction nedd4l-smad7-2 5 16 unspecified role unspecified role unspecified role unspecified role WW2 domain Region 364-403 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 17 unspecified role unspecified role unspecified role unspecified role Region 203-217 Region 203-217 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro direct interaction direct interaction smad7-yap1-7 13 15 unspecified role unspecified role prey prey HA-tag HA-tag ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range human Homo sapiens Human 17 unspecified role unspecified role bait bait O15105:p.[Pro208Ala;Pro209Ala] P208A/P209A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain P A certain certain sequence position certain certain certain sequence position certain P A This feature has been corrected as a result of our quality control procedures. The original label was 'P208A/P209A'. Wed May 02 16:42:35 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'pro208ala,pro209ala' Tue Jun 30 18:25:02 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Pro208Ala;Pro209Ala]' Flag-tag Flag-tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged n-term range n-terminal range n-term range n-term range n-terminal range n-term range human Homo sapiens Human physical association physical association smad7-smurf2-5 10 18 unspecified role unspecified role unspecified role unspecified role WW3 domain Region 297-333 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 17 unspecified role unspecified role unspecified role unspecified role Region 203-217 Region 203-217 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro direct interaction direct interaction smad7-nedd4l-1 12 16 unspecified role unspecified role prey prey HA-tag HA-tag ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined human Homo sapiens Human 17 unspecified role unspecified role bait bait O15105:p.[Pro208Ala;Pro209Ala] P208A/P209A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain P A certain certain sequence position certain certain certain sequence position certain P A This feature has been corrected as a result of our quality control procedures. The original label was 'P208A/P209A'. Wed May 02 20:10:52 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'pro208ala,pro209ala' Tue Jun 30 17:24:47 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Pro208Ala;Pro209Ala]' Flag-tag Flag-tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged n-term range n-terminal range n-term range n-term range n-terminal range n-term range human Homo sapiens Human physical association physical association smad7-smurf1-4 3 19 unspecified role unspecified role unspecified role unspecified role WW2 domain Region 277-314 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 17 unspecified role unspecified role unspecified role unspecified role Region 203-217 Region 203-217 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro direct interaction direct interaction smad7-smurf2-6 1 18 unspecified role unspecified role unspecified role unspecified role WW2/3 domain Region 250-333 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 17 unspecified role unspecified role unspecified role unspecified role Region 203-217 Region 203-217 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro direct interaction direct interaction