DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ morishita-2011-1 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. 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 imex curation morishita-2011-2 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. 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 imex curation morishita-2011-3 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. 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 imex curation morishita-2011-4 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. 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 imex curation 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 apc_human Adenomatous polyposis coli protein APC DP2.5 Deleted in polyposis 2.5 protein protein human Homo sapiens Human MAAASYDQLLKQVEALKMENSNLRQELEDNSNHLTKLETEASNMKEVLKQLQGSIEDEAMASSGQIDLLERLKELNLDSSNFPGVKLRSKMSLRSYGSREGSVSSRSGECSPVPMGSFPRRGFVNGSRESTGYLEELEKERSLLLADLDKEEKEKDWYYAQLQNLTKRIDSLPLTENFSLQTDMTRRQLEYEARQIRVAMEEQLGTCQDMEKRAQRRIARIQQIEKDILRIRQLLQSQATEAERSSQNKHETGSHDAERQNEGQGVGEINMATSGNGQGSTTRMDHETASVLSSSSTHSAPRRLTSHLGTKVEMVYSLLSMLGTHDKDDMSRTLLAMSSSQDSCISMRQSGCLPLLIQLLHGNDKDSVLLGNSRGSKEARARASAALHNIIHSQPDDKRGRREIRVLHLLEQIRAYCETCWEWQEAHEPGMDQDKNPMPAPVEHQICPAVCVLMKLSFDEEHRHAMNELGGLQAIAELLQVDCEMYGLTNDHYSITLRRYAGMALTNLTFGDVANKATLCSMKGCMRALVAQLKSESEDLQQVIASVLRNLSWRADVNSKKTLREVGSVKALMECALEVKKESTLKSVLSALWNLSAHCTENKADICAVDGALAFLVGTLTYRSQTNTLAIIESGGGILRNVSSLIATNEDHRQILRENNCLQTLLQHLKSHSLTIVSNACGTLWNLSARNPKDQEALWDMGAVSMLKNLIHSKHKMIAMGSAAALRNLMANRPAKYKDANIMSPGSSLPSLHVRKQKALEAELDAQHLSETFDNIDNLSPKASHRSKQRHKQSLYGDYVFDTNRHDDNRSDNFNTGNMTVLSPYLNTTVLPSSSSSRGSLDSSRSEKDRSLERERGIGLGNYHPATENPGTSSKRGLQISTTAAQIAKVMEEVSAIHTSQEDRSSGSTTELHCVTDERNALRRSSAAHTHSNTYNFTKSENSNRTCSMPYAKLEYKRSSNDSLNSVSSSDGYGKRGQMKPSIESYSEDDESKFCSYGQYPADLAHKIHSANHMDDNDGELDTPINYSLKYSDEQLNSGRQSPSQNERWARPKHIIEDEIKQSEQRQSRNQSTTYPVYTESTDDKHLKFQPHFGQQECVSPYRSRGANGSETNRVGSNHGINQNVSQSLCQEDDYEDDKPTNYSERYSEEEQHEEEERPTNYSIKYNEEKRHVDQPIDYSLKYATDIPSSQKQSFSFSKSSSGQSSKTEHMSSSSENTSTPSSNAKRQNQLHPSSAQSRSGQPQKAATCKVSSINQETIQTYCVEDTPICFSRCSSLSSLSSAEDEIGCNQTTQEADSANTLQIAEIKEKIGTRSAEDPVSEVPAVSQHPRTKSSRLQGSSLSSESARHKAVEFSSGAKSPSKSGAQTPKSPPEHYVQETPLMFSRCTSVSSLDSFESRSIASSVQSEPCSGMVSGIISPSDLPDSPGQTMPPSRSKTPPPPPQTAQTKREVPKNKAPTAEKRESGPKQAAVNAAVQRVQVLPDADTLLHFATESTPDGFSCSSSLSALSLDEPFIQKDVELRIMPPVQENDNGNETESEQPKESNENQEKEAEKTIDSEKDLLDDSDDDDIEILEECIISAMPTKSSRKAKKPAQTASKLPPPVARKPSQLPVYKLLPSQNRLQPQKHVSFTPGDDMPRVYCVEGTPINFSTATSLSDLTIESPPNELAAGEGVRGGAQSGEFEKRDTIPTEGRSTDEAQGGKTSSVTIPELDDNKAEEGDILAECINSAMPKGKSHKPFRVKKIMDQVQQASASSSAPNKNQLDGKKKKPTSPVKPIPQNTEYRTRVRKNADSKNNLNAERVFSDNKDSKKQNLKNNSKVFNDKLPNNEDRVRGSFAFDSPHHYTPIEGTPYCFSRNDSLSSLDFDDDDVDLSREKAELRKAKENKESEAKVTSHTELTSNQQSANKTQAIAKQPINRGQPKPILQKQSTFPQSSKDIPDRGAATDEKLQNFAIENTPVCFSHNSSLSSLSDIDQENNNKENEPIKETEPPDSQGEPSKPQASGYAPKSFHVEDTPVCFSRNSSLSSLSIDSEDDLLQECISSAMPKKKKPSRLKGDNEKHSPRNMGGILGEDLTLDLKDIQRPDSEHGLSPDSENFDWKAIQEGANSIVSSLHQAAAAACLSRQASSDSDSILSLKSGISLGSPFHLTPDQEEKPFTSNKGPRILKPGEKSTLETKKIESESKGIKGGKKVYKSLITGKVRSNSEISGQMKQPLQANMPSISRGRTMIHIPGVRNSSSSTSPVSKKGPPLKTPASKSPSEGQTATTSPRGAKPSVKSELSPVARQTSQIGGSSKAPSRSGSRDSTPSRPAQQPLSRPIQSPGRNSISPGRNGISPPNKLSQLPRTSSPSTASTKSSGSGKMSYTSPGRQMSQQNLTKQTGLSKNASSIPRSESASKGLNQMNNGNGANKKVELSRMSSTKSSGSESDRSERPVLVRQSTFIKEAPSPTLRRKLEESASFESLSPSSRPASPTRSQAQTPVLSPSLPDMSLSTHSSVQAGGWRKLPPNLSPTIEYNDGRPAKRHDIARSHSESPSRLPINRSGTWKREHSKHSSSLPRVSTWRRTGSSSSILSASSESSEKAKSEDEKHVNSISGTKQSKENQVSAKGTWRKIKENEFSPTNSTSQTVSSGATNGAESKTLIYQMAPAVSKTEDVWVRIEDCPINNPRSGRSPTGNTPPVIDSVSEKANPNIKDSKDNQAKQNVGNGSVPMRTVGLENRLNSFIQVDAPDQKGTEIKPGQNNPVPVSETNESSIVERTPFSSSSSSKHSSPSGTVAARVTPFNYNPSPRKSSADSTSARPSQIPTPVNNNTKKRDSKTDSTESSGTQSPKRHSGSYLVTSV q9nr80-1 Rho guanine nucleotide exchange factor 4 ARHGEF4 KIAA1112 APC-stimulated guanine nucleotide exchange factor 1 protein protein human Homo sapiens Human MPWEEPAGEKPSCSHSQKAFHMEPAQKPCFTTDMVTWALLCISAETVRGEAPSQPRGIPHRSPVSVDDLWLEKTQRKKLQKQAHVERRLHIGAVHKDGVKCWRKTIITSPESLNLPRRSHPLSQSAPTGLNHMGWPEHTPGTAMPDGALDTAVCADEVGSEEDLYDDLHSSSHHYSHPGGGGEQLAINELISDGSVVCAEALWDHVTMDDQELGFKAGDVIEVMDATNREWWWGRVADGEGWFPASFVRLRVNQDEPADDDAPLAGNSGAEDGGAEAQSSKDQMRTNVINEILSTERDYIKHLRDICEGYVRQCRKRADMFSEEQLRTIFGNIEDIYRCQKAFVKALEQRFNRERPHLSELGACFLEHQADFQIYSEYCNNHPNACVELSRLTKLSKYVYFFEACRLLQKMIDISLDGFLLTPVQKICKYPLQLAELLKYTHPQHRDFKDVEAALHAMKNVAQLINERKRRLENIDKIAQWQSSIEDWEGEDLLVRSSELIYSGELTRVTQPQAKSQQRMFFLFDHQLIYCKKDLLRRDVLYYKGRLDMDGLEVVDLEDGKDRDLHVSIKNAFRLHRGATGDSHLLCTRKPEQKQRWLKAFAREREQVQLDQETGFSITELQRKQAMLNASKQQVTGKPKAVGRPCYLTRQKHPALPSNRPQQQVLVLAEPRRKPSTFWHSISRLAPFRK apc-khdrbs1-1 3231360 N/A 3231364 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 false in vitro In vitro N/A 3231365 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 false in vitro In vitro direct interaction direct interaction false false false apc-arhgef4-5 3231361 N/A 3231366 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 false in vitro In vitro N/A 3231365 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 false 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 false in vitro In vitro direct interaction direct interaction false false false apc-khdrbs1-2 3231362 N/A 3231364 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 false in vitro In vitro N/A 3231365 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 false 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 false 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 false P25054:p.Lys516Glu mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain false in vitro In vitro direct interaction direct interaction false false false apc-khdrbs1-3 3231363 N/A 3231364 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 false 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 false 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 false 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 false in vitro In vitro N/A 3231365 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 false in vitro In vitro direct interaction direct interaction false false false