DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Crystal structures of the armadillo repeat domain of adenomatous polyposis coli and its complex with the tyrosine-rich domain of Sam68. Crystal structures of the armadillo repeat domain of adenomatous polyposis coli and its complex with the tyrosine-rich domain of Sam68. Structure (London, England : 1993) 2011 imex curation Morishita EC., Murayama K., Kato-Murayama M., Ishizuka-Katsura Y., Tomabechi Y., Hayashi T., Terada T., Handa N., Shirouzu M., Akiyama T., Yokoyama S. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Morishita EC., Murayama K., Kato-Murayama M., Ishizuka-Katsura Y., Tomabechi Y., Hayashi T., Terada T., Handa N., Shirouzu M., Akiyama T., Yokoyama S. DIP original experiment: DIP-220097X Structure (London, England : 1993) 2011 IMEx Crystal structures of the armadillo repeat domain of adenomatous polyposis coli and its complex with the tyrosine-rich domain of Sam68. Crystal structures of the armadillo repeat domain of adenomatous polyposis coli and its complex with the tyrosine-rich domain of Sam68. Crystal structures of the armadillo repeat domain of adenomatous polyposis coli and its complex with the tyrosine-rich domain of Sam68. Structure (London, England : 1993) 2011 imex curation Morishita EC., Murayama K., Kato-Murayama M., Ishizuka-Katsura Y., Tomabechi Y., Hayashi T., Terada T., Handa N., Shirouzu M., Akiyama T., Yokoyama S. 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 Morishita EC., Murayama K., Kato-Murayama M., Ishizuka-Katsura Y., Tomabechi Y., Hayashi T., Terada T., Handa N., Shirouzu M., Akiyama T., Yokoyama S. DIP original experiment: DIP-220095X Structure (London, England : 1993) 2011 IMEx Crystal structures of the armadillo repeat domain of adenomatous polyposis coli and its complex with the tyrosine-rich domain of Sam68. Crystal structures of the armadillo repeat domain of adenomatous polyposis coli and its complex with the tyrosine-rich domain of Sam68. Crystal structures of the armadillo repeat domain of adenomatous polyposis coli and its complex with the tyrosine-rich domain of Sam68. Structure (London, England : 1993) 2011 imex curation Morishita EC., Murayama K., Kato-Murayama M., Ishizuka-Katsura Y., Tomabechi Y., Hayashi T., Terada T., Handa N., Shirouzu M., Akiyama T., Yokoyama S. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Morishita EC., Murayama K., Kato-Murayama M., Ishizuka-Katsura Y., Tomabechi Y., Hayashi T., Terada T., Handa N., Shirouzu M., Akiyama T., Yokoyama S. DIP original experiment: DIP-220098X Structure (London, England : 1993) 2011 IMEx Crystal structures of the armadillo repeat domain of adenomatous polyposis coli and its complex with the tyrosine-rich domain of Sam68. Crystal structures of the armadillo repeat domain of adenomatous polyposis coli and its complex with the tyrosine-rich domain of Sam68. Crystal structures of the armadillo repeat domain of adenomatous polyposis coli and its complex with the tyrosine-rich domain of Sam68. Structure (London, England : 1993) 2011 imex curation Morishita EC., Murayama K., Kato-Murayama M., Ishizuka-Katsura Y., Tomabechi Y., Hayashi T., Terada T., Handa N., Shirouzu M., Akiyama T., Yokoyama S. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Morishita EC., Murayama K., Kato-Murayama M., Ishizuka-Katsura Y., Tomabechi Y., Hayashi T., Terada T., Handa N., Shirouzu M., Akiyama T., Yokoyama S. DIP original experiment: DIP-220096X Structure (London, England : 1993) 2011 IMEx Crystal structures of the armadillo repeat domain of adenomatous polyposis coli and its complex with the tyrosine-rich domain of Sam68. apc_human Adenomatous polyposis coli protein APC DP2.5 Deleted in polyposis 2.5 protein protein human Homo sapiens Human MAAASYDQLLKQVEALKMENSNLRQELEDNSNHLTKLETEASNMKEVLKQLQGSIEDEAMASSGQIDLLERLKELNLDSSNFPGVKLRSKMSLRSYGSREGSVSSRSGECSPVPMGSFPRRGFVNGSRESTGYLEELEKERSLLLADLDKEEKEKDWYYAQLQNLTKRIDSLPLTENFSLQTDMTRRQLEYEARQIRVAMEEQLGTCQDMEKRAQRRIARIQQIEKDILRIRQLLQSQATEAERSSQNKHETGSHDAERQNEGQGVGEINMATSGNGQGSTTRMDHETASVLSSSSTHSAPRRLTSHLGTKVEMVYSLLSMLGTHDKDDMSRTLLAMSSSQDSCISMRQSGCLPLLIQLLHGNDKDSVLLGNSRGSKEARARASAALHNIIHSQPDDKRGRREIRVLHLLEQIRAYCETCWEWQEAHEPGMDQDKNPMPAPVEHQICPAVCVLMKLSFDEEHRHAMNELGGLQAIAELLQVDCEMYGLTNDHYSITLRRYAGMALTNLTFGDVANKATLCSMKGCMRALVAQLKSESEDLQQVIASVLRNLSWRADVNSKKTLREVGSVKALMECALEVKKESTLKSVLSALWNLSAHCTENKADICAVDGALAFLVGTLTYRSQTNTLAIIESGGGILRNVSSLIATNEDHRQILRENNCLQTLLQHLKSHSLTIVSNACGTLWNLSARNPKDQEALWDMGAVSMLKNLIHSKHKMIAMGSAAALRNLMANRPAKYKDANIMSPGSSLPSLHVRKQKALEAELDAQHLSETFDNIDNLSPKASHRSKQRHKQSLYGDYVFDTNRHDDNRSDNFNTGNMTVLSPYLNTTVLPSSSSSRGSLDSSRSEKDRSLERERGIGLGNYHPATENPGTSSKRGLQISTTAAQIAKVMEEVSAIHTSQEDRSSGSTTELHCVTDERNALRRSSAAHTHSNTYNFTKSENSNRTCSMPYAKLEYKRSSNDSLNSVSSSDGYGKRGQMKPSIESYSEDDESKFCSYGQYPADLAHKIHSANHMDDNDGELDTPINYSLKYSDEQLNSGRQSPSQNERWARPKHIIEDEIKQSEQRQSRNQSTTYPVYTESTDDKHLKFQPHFGQQECVSPYRSRGANGSETNRVGSNHGINQNVSQSLCQEDDYEDDKPTNYSERYSEEEQHEEEERPTNYSIKYNEEKRHVDQPIDYSLKYATDIPSSQKQSFSFSKSSSGQSSKTEHMSSSSENTSTPSSNAKRQNQLHPSSAQSRSGQPQKAATCKVSSINQETIQTYCVEDTPICFSRCSSLSSLSSAEDEIGCNQTTQEADSANTLQIAEIKEKIGTRSAEDPVSEVPAVSQHPRTKSSRLQGSSLSSESARHKAVEFSSGAKSPSKSGAQTPKSPPEHYVQETPLMFSRCTSVSSLDSFESRSIASSVQSEPCSGMVSGIISPSDLPDSPGQTMPPSRSKTPPPPPQTAQTKREVPKNKAPTAEKRESGPKQAAVNAAVQRVQVLPDADTLLHFATESTPDGFSCSSSLSALSLDEPFIQKDVELRIMPPVQENDNGNETESEQPKESNENQEKEAEKTIDSEKDLLDDSDDDDIEILEECIISAMPTKSSRKAKKPAQTASKLPPPVARKPSQLPVYKLLPSQNRLQPQKHVSFTPGDDMPRVYCVEGTPINFSTATSLSDLTIESPPNELAAGEGVRGGAQSGEFEKRDTIPTEGRSTDEAQGGKTSSVTIPELDDNKAEEGDILAECINSAMPKGKSHKPFRVKKIMDQVQQASASSSAPNKNQLDGKKKKPTSPVKPIPQNTEYRTRVRKNADSKNNLNAERVFSDNKDSKKQNLKNNSKVFNDKLPNNEDRVRGSFAFDSPHHYTPIEGTPYCFSRNDSLSSLDFDDDDVDLSREKAELRKAKENKESEAKVTSHTELTSNQQSANKTQAIAKQPINRGQPKPILQKQSTFPQSSKDIPDRGAATDEKLQNFAIENTPVCFSHNSSLSSLSDIDQENNNKENEPIKETEPPDSQGEPSKPQASGYAPKSFHVEDTPVCFSRNSSLSSLSIDSEDDLLQECISSAMPKKKKPSRLKGDNEKHSPRNMGGILGEDLTLDLKDIQRPDSEHGLSPDSENFDWKAIQEGANSIVSSLHQAAAAACLSRQASSDSDSILSLKSGISLGSPFHLTPDQEEKPFTSNKGPRILKPGEKSTLETKKIESESKGIKGGKKVYKSLITGKVRSNSEISGQMKQPLQANMPSISRGRTMIHIPGVRNSSSSTSPVSKKGPPLKTPASKSPSEGQTATTSPRGAKPSVKSELSPVARQTSQIGGSSKAPSRSGSRDSTPSRPAQQPLSRPIQSPGRNSISPGRNGISPPNKLSQLPRTSSPSTASTKSSGSGKMSYTSPGRQMSQQNLTKQTGLSKNASSIPRSESASKGLNQMNNGNGANKKVELSRMSSTKSSGSESDRSERPVLVRQSTFIKEAPSPTLRRKLEESASFESLSPSSRPASPTRSQAQTPVLSPSLPDMSLSTHSSVQAGGWRKLPPNLSPTIEYNDGRPAKRHDIARSHSESPSRLPINRSGTWKREHSKHSSSLPRVSTWRRTGSSSSILSASSESSEKAKSEDEKHVNSISGTKQSKENQVSAKGTWRKIKENEFSPTNSTSQTVSSGATNGAESKTLIYQMAPAVSKTEDVWVRIEDCPINNPRSGRSPTGNTPPVIDSVSEKANPNIKDSKDNQAKQNVGNGSVPMRTVGLENRLNSFIQVDAPDQKGTEIKPGQNNPVPVSETNESSIVERTPFSSSSSSKHSSPSGTVAARVTPFNYNPSPRKSSADSTSARPSQIPTPVNNNTKKRDSKTDSTESSGTQSPKRHSGSYLVTSV DIP protein P25054 original sequence version: 143 DIP protein P25054-1 original sequence version: 157 DIP protein P25054 original sequence version: 158 77E194AE4A91DC5A khdr1_human KH domain-containing, RNA-binding, signal transduction-associated protein 1 SAM68 Src-associated in mitosis 68 kDa protein KHDRBS1 p21 Ras GTPase-activating protein-associated p62 GAP-associated tyrosine phosphoprotein p62 p68 protein protein human Homo sapiens Human MQRRDDPAARMSRSSGRSGSMDPSGAHPSVRQTPSRQPPLPHRSRGGGGGSRGGARASPATQPPPLLPPSATGPDATVGGPAPTPLLPPSATASVKMEPENKYLPELMAEKDSLDPSFTHAMQLLTAEIEKIQKGDSKKDDEENYLDLFSHKNMKLKERVLIPVKQYPKFNFVGKILGPQGNTIKRLQEETGAKISVLGKGSMRDKAKEEELRKGGDPKYAHLNMDLHVFIEVFGPPCEAYALMAHAMEEVKKFLVPDMMDDICQEQFLELSYLNGVPEPSRGRGVPVRGRGAAPPPPPVPRGRGVGPPRGALVRGTPVRGAITRGATVTRGVPPPPTVRGAPAPRARTAGIQRIPLPPPPAPETYEEYGYDDTYAEQSYEGYEGYYSQSQGDSEYYDYGHGEVQDSYEAYGQDDWNGTRPSLKAPPARPVKGAYREHPYGRY DIP protein Q07666 original sequence version: 55 DIP protein Q07666-1 original sequence version: 116 59FB4DB6FB4DBE98 q9nr80-1 Rho guanine nucleotide exchange factor 4 ARHGEF4 KIAA1112 APC-stimulated guanine nucleotide exchange factor 1 protein protein human Homo sapiens Human MPWEEPAGEKPSCSHSQKAFHMEPAQKPCFTTDMVTWALLCISAETVRGEAPSQPRGIPHRSPVSVDDLWLEKTQRKKLQKQAHVERRLHIGAVHKDGVKCWRKTIITSPESLNLPRRSHPLSQSAPTGLNHMGWPEHTPGTAMPDGALDTAVCADEVGSEEDLYDDLHSSSHHYSHPGGGGEQLAINELISDGSVVCAEALWDHVTMDDQELGFKAGDVIEVMDATNREWWWGRVADGEGWFPASFVRLRVNQDEPADDDAPLAGNSGAEDGGAEAQSSKDQMRTNVINEILSTERDYIKHLRDICEGYVRQCRKRADMFSEEQLRTIFGNIEDIYRCQKAFVKALEQRFNRERPHLSELGACFLEHQADFQIYSEYCNNHPNACVELSRLTKLSKYVYFFEACRLLQKMIDISLDGFLLTPVQKICKYPLQLAELLKYTHPQHRDFKDVEAALHAMKNVAQLINERKRRLENIDKIAQWQSSIEDWEGEDLLVRSSELIYSGELTRVTQPQAKSQQRMFFLFDHQLIYCKKDLLRRDVLYYKGRLDMDGLEVVDLEDGKDRDLHVSIKNAFRLHRGATGDSHLLCTRKPEQKQRWLKAFAREREQVQLDQETGFSITELQRKQAMLNASKQQVTGKPKAVGRPCYLTRQKHPALPSNRPQQQVLVLAEPRRKPSTFWHSISRLAPFRK DIP protein Q9NR80-1 original sequence version: 115 DIP protein Q9NR80 original sequence version: 93 apc-khdrbs1-1 2 6 unspecified role unspecified role unspecified role unspecified role Tyrosine-rich domain Region 365-419 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain in vitro In vitro 5 unspecified role unspecified role unspecified role unspecified role Armadillo domain Region 396-732 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain in vitro In vitro direct interaction direct interaction apc-arhgef4-5 1 7 unspecified role unspecified role unspecified role unspecified role ABR-SH3 domain Region 164-253 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain in vitro In vitro 5 unspecified role unspecified role unspecified role unspecified role Armadillo domain Region 396-732 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain P25054:p.Lys516Asn K516N mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K N This feature has been corrected as a result of our quality control procedures. The original label was 'K516N'. Wed May 02 18:37:41 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys516asn' Tue Jun 30 17:58:41 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys516Asn' in vitro In vitro direct interaction direct interaction apc-khdrbs1-2 4 6 unspecified role unspecified role unspecified role unspecified role Tyrosine-rich domain Region 365-419 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain in vitro In vitro 5 unspecified role unspecified role unspecified role unspecified role Armadillo domain Region 396-732 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain P25054:p.Lys516Asn K516E/N mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K N Wed May 02 18:14:33 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys516asn' Tue Jun 30 16:24:28 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys516Asn' P25054:p.Arg549Glu R549E mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation 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 'R549E'. Wed May 02 18:27:35 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg549glu' Tue Jun 30 19:24:44 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg549Glu' P25054:p.Lys516Glu mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain K E Wed May 02 19:20:54 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys516glu' Tue Jun 30 20:12:44 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys516Glu' in vitro In vitro direct interaction direct interaction apc-khdrbs1-3 3 6 unspecified role unspecified role unspecified role unspecified role Region 379-389 Region 379-389 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Q07666:p.Glu381Lys E381K mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain E K This feature has been corrected as a result of our quality control procedures. The original label was 'E381K'. Wed May 02 18:27:36 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu381lys' Tue Jun 30 16:42:17 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu381Lys' Q07666:p.Glu384Lys E384K mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain E K This feature has been corrected as a result of our quality control procedures. The original label was 'E384K'. Wed May 02 18:26:17 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu384lys' Tue Jun 30 17:41:19 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu384Lys' Q07666:p.Tyr383Ala Y383A mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Y A This feature has been corrected as a result of our quality control procedures. The original label was 'Y383A'. Wed May 02 14:54:33 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr383ala' Tue Jun 30 19:37:28 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr383Ala' in vitro In vitro 5 unspecified role unspecified role unspecified role unspecified role Armadillo domain Region 396-732 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain in vitro In vitro direct interaction direct interaction