DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Selective integrin endocytosis is driven by interactions between the integrin α-chain and AP2. Selective integrin endocytosis is driven by interactions between the integrin α-chain and AP2. Nature structural & molecular biology 2016 imex curation De Franceschi N., Arjonen A., Elkhatib N., Denessiouk K., Wrobel AG., Wilson TA., Pouwels J., Montagnac G., Owen DJ., Ivaska J. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined De Franceschi N., Arjonen A., Elkhatib N., Denessiouk K., Wrobel AG., Wilson TA., Pouwels J., Montagnac G., Owen DJ., Ivaska J. DIP original experiment: DIP-268835X Nature structural & molecular biology 2016 IMEx Selective integrin endocytosis is driven by interactions between the integrin α-chain and AP2. Selective integrin endocytosis is driven by interactions between the integrin α-chain and AP2. Selective integrin endocytosis is driven by interactions between the integrin α-chain and AP2. Nature structural & molecular biology 2016 imex curation De Franceschi N., Arjonen A., Elkhatib N., Denessiouk K., Wrobel AG., Wilson TA., Pouwels J., Montagnac G., Owen DJ., Ivaska J. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined De Franceschi N., Arjonen A., Elkhatib N., Denessiouk K., Wrobel AG., Wilson TA., Pouwels J., Montagnac G., Owen DJ., Ivaska J. DIP original experiment: DIP-268834X Nature structural & molecular biology 2016 IMEx Selective integrin endocytosis is driven by interactions between the integrin α-chain and AP2. Selective integrin endocytosis is driven by interactions between the integrin α-chain and AP2. Selective integrin endocytosis is driven by interactions between the integrin α-chain and AP2. Nature structural & molecular biology 2016 imex curation De Franceschi N., Arjonen A., Elkhatib N., Denessiouk K., Wrobel AG., Wilson TA., Pouwels J., Montagnac G., Owen DJ., Ivaska J. 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 De Franceschi N., Arjonen A., Elkhatib N., Denessiouk K., Wrobel AG., Wilson TA., Pouwels J., Montagnac G., Owen DJ., Ivaska J. DIP original experiment: DIP-268833X Nature structural & molecular biology 2016 IMEx Selective integrin endocytosis is driven by interactions between the integrin α-chain and AP2. Selective integrin endocytosis is driven by interactions between the integrin α-chain and AP2. Selective integrin endocytosis is driven by interactions between the integrin α-chain and AP2. Nature structural & molecular biology 2016 imex curation De Franceschi N., Arjonen A., Elkhatib N., Denessiouk K., Wrobel AG., Wilson TA., Pouwels J., Montagnac G., Owen DJ., Ivaska J. Only protein-protein interactions in vitro In vitro pull down pull down predetermined predetermined participant predetermined De Franceschi N., Arjonen A., Elkhatib N., Denessiouk K., Wrobel AG., Wilson TA., Pouwels J., Montagnac G., Owen DJ., Ivaska J. DIP original experiment: DIP-268836X Nature structural & molecular biology 2016 IMEx Selective integrin endocytosis is driven by interactions between the integrin α-chain and AP2. ap2m1_rat AP-2 complex subunit mu Adaptor protein complex AP-2 subunit mu AP-2 mu chain Ap2m1 Mu2-adaptin Plasma membrane adaptor AP-2 50 kDa protein Clathrin coat assembly protein AP50 Clathrin coat-associated protein AP50 Clathrin assembly protein complex 2 mu medium chain Adaptor-related protein complex 2 subunit mu protein protein rat Rattus norvegicus (Rat) Rat MIGGLFIYNHKGEVLISRVYRDDIGRNAVDAFRVNVIHARQQVRSPVTNIARTSFFHVKRSNIWLAAVTKQNVNAAMVFEFLYKMCDVMAAYFGKISEENIKNNFVLIYELLDEILDFGYPQNSETGALKTFITQQGIKSQHQTKEEQSQITSQVTGQIGWRREGIKYRRNELFLDVLESVNLLMSPQGQVLSAHVSGRVVMKSYLSGMPECKFGMNDKIVIEKQGKGTADETSKSGKQSIAIDDCTFHQCVRLSKFDSERSISFIPPDGEFELMRYRTTKDIILPFRVIPLVREVGRTKLEVKVVIKSNFKPSLLAQKIEVRIPTPLNTSGVQVICMKGKAKYKASENAIVWKIKRMAGMKESQISAEIELLPTNDKKKWARPPISMNFEVPFAPSGLKVRYLKVFEPKLNYSDHDVIKWVRYIGRSGIYETRC DIP protein P84092 original sequence version: 91 DIP protein P84092 original sequence version: 42 DIP protein P84092 original sequence version: 82 DIP protein P84092 original sequence version: 67 DIP protein P84092 original sequence version: 92 DIP protein P84092 original sequence version: 105 DIP protein P84092 original sequence version: 110 82803219BA279954 ita2_human Integrin alpha-2 Platelet membrane glycoprotein Ia Collagen receptor VLA-2 subunit alpha CD49 antigen-like family member B ITGA2 CD49B protein protein human Homo sapiens Human MGPERTGAAPLPLLLVLALSQGILNCCLAYNVGLPEAKIFSGPSSEQFGYAVQQFINPKGNWLLVGSPWSGFPENRMGDVYKCPVDLSTATCEKLNLQTSTSIPNVTEMKTNMSLGLILTRNMGTGGFLTCGPLWAQQCGNQYYTTGVCSDISPDFQLSASFSPATQPCPSLIDVVVVCDESNSIYPWDAVKNFLEKFVQGLDIGPTKTQVGLIQYANNPRVVFNLNTYKTKEEMIVATSQTSQYGGDLTNTFGAIQYARKYAYSAASGGRRSATKVMVVVTDGESHDGSMLKAVIDQCNHDNILRFGIAVLGYLNRNALDTKNLIKEIKAIASIPTERYFFNVSDEAALLEKAGTLGEQIFSIEGTVQGGDNFQMEMSQVGFSADYSSQNDILMLGAVGAFGWSGTIVQKTSHGHLIFPKQAFDQILQDRNHSSYLGYSVAAISTGESTHFVAGAPRANYTGQIVLYSVNENGNITVIQAHRGDQIGSYFGSVLCSVDVDKDTITDVLLVGAPMYMSDLKKEEGRVYLFTIKKGILGQHQFLEGPEGIENTRFGSAIAALSDINMDGFNDVIVGSPLENQNSGAVYIYNGHQGTIRTKYSQKILGSDGAFRSHLQYFGRSLDGYGDLNGDSITDVSIGAFGQVVQLWSQSIADVAIEASFTPEKITLVNKNAQIILKLCFSAKFRPTKQNNQVAIVYNITLDADGFSSRVTSRGLFKENNERCLQKNMVVNQAQSCPEHIIYIQEPSDVVNSLDLRVDISLENPGTSPALEAYSETAKVFSIPFHKDCGEDGLCISDLVLDVRQIPAAQEQPFIVSNQNKRLTFSVTLKNKRESAYNTGIVVDFSENLFFASFSLPVDGTEVTCQVAASQKSVACDVGYPALKREQQVTFTINFDFNLQNLQNQASLSFQALSESQEENKADNLVNLKIPLLYDAEIHLTRSTNINFYEISSDGNVPSIVHSFEDVGPKFIFSLKVTTGSVPVSMATVIIHIPQYTKEKNPLMYLTGVQTDKAGDISCNADINPLKIGQTSSSVSFKSENFRHTKELNCRTASCSNVTCWLKDVHMKGEYFVNVTTRIWNGTFASSTFQTVQLTAAAEINTYNPEIYVIEDNTVTIPLMIMKPDEKAEVPTGVIIGSIIAGILLLLALVAILWKLGFFKRKYEKMTKNPDEIDETTELSS DIP protein P17301 original sequence version: 108 DIP protein P17301 original sequence version: 186 7E1B7ED968A94070 ita4_human Integrin alpha-4 Integrin alpha-IV VLA-4 subunit alpha CD49 antigen-like family member D ITGA4 CD49D protein protein human Homo sapiens Human MAWEARREPGPRRAAVRETVMLLLCLGVPTGRPYNVDTESALLYQGPHNTLFGYSVVLHSHGANRWLLVGAPTANWLANASVINPGAIYRCRIGKNPGQTCEQLQLGSPNGEPCGKTCLEERDNQWLGVTLSRQPGENGSIVTCGHRWKNIFYIKNENKLPTGGCYGVPPDLRTELSKRIAPCYQDYVKKFGENFASCQAGISSFYTKDLIVMGAPGSSYWTGSLFVYNITTNKYKAFLDKQNQVKFGSYLGYSVGAGHFRSQHTTEVVGGAPQHEQIGKAYIFSIDEKELNILHEMKGKKLGSYFGASVCAVDLNADGFSDLLVGAPMQSTIREEGRVFVYINSGSGAVMNAMETNLVGSDKYAARFGESIVNLGDIDNDGFEDVAIGAPQEDDLQGAIYIYNGRADGISSTFSQRIEGLQISKSLSMFGQSISGQIDADNNGYVDVAVGAFRSDSAVLLRTRPVVIVDASLSHPESVNRTKFDCVENGWPSVCIDLTLCFSYKGKEVPGYIVLFYNMSLDVNRKAESPPRFYFSSNGTSDVITGSIQVSSREANCRTHQAFMRKDVRDILTPIQIEAAYHLGPHVISKRSTEEFPPLQPILQQKKEKDIMKKTINFARFCAHENCSADLQVSAKIGFLKPHENKTYLAVGSMKTLMLNVSLFNAGDDAYETTLHVKLPVGLYFIKILELEEKQINCEVTDNSGVVQLDCSIGYIYVDHLSRIDISFLLDVSSLSRAEEDLSITVHATCENEEEMDNLKHSRVTVAIPLKYEVKLTVHGFVNPTSFVYGSNDENEPETCMVEKMNLTFHVINTGNSMAPNVSVEIMVPNSFSPQTDKLFNILDVQTTTGECHFENYQRVCALEQQKSAMQTLKGIVRFLSKTDKRLLYCIKADPHCLNFLCNFGKMESGKEASVHIQLEGRPSILEMDETSALKFEIRATGFPEPNPRVIELNKDENVAHVLLEGLHHQRPKRYFTIVIISSSLLLGLIVLLLISYVMWKAGFFKRQYKSILQEENRRDSWSYINSKSNDD DIP protein P13612 original sequence version: 131 DIP protein P13612-1 original sequence version: 171 DIP protein P13612 original sequence version: 138 73EC1204DE78CD35 ap2m1-itga4-1 3 7 unspecified role unspecified role unspecified role unspecified role Region 1008-1015 Region 1008-1015 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 5 unspecified role unspecified role unspecified role unspecified role Region 160-435 Region 160-435 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 ap2m1-itga2-1 1 6 unspecified role unspecified role unspecified role unspecified role Region 1154-1181 Region 1154-1181 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 5 unspecified role unspecified role unspecified role unspecified role Region 160-435 Region 160-435 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 ap2m1-itga4-2 2 7 unspecified role unspecified role unspecified role unspecified role Region 1008-1015 Region 1008-1015 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain pY1009 pY1009 optyr O4'-phospho-L-tyrosine (2S)-2-amino-3-(4-phosphonooxyphenyl)propanoic acid 2-azanyl-3-(4-phosphonooxyphenyl)propanoic acid MOD_RES Phosphotyrosine O4-phosphotyrosine tyrosine phosphate 2-amino-3-(4-hydroxyphenyl)propanoic acid 4'-phosphate O4'-phospho-L-tyrosine O4'-phosphorylated L-tyrosine OPTyr Phospho Phospho Tyrosinyl Phosphorylation phosphorylationy certain certain sequence position certain certain certain sequence position certain disrupting-ptm ptm disrupting an interaction disrupting-ptm in vitro In vitro 5 unspecified role unspecified role unspecified role unspecified role Region 160-435 Region 160-435 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 itga2-ap2m1-1 4 6 unspecified role unspecified role bait bait Region 1154-1181 Region 1154-1181 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Biotin-tag Biotin-tag biotin tag biotin tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range P17301:p.[Tyr1163Ala;Met1166Ala] Y1163A/M1166A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain M A 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 'Y1163A/M1166A'. Wed May 02 16:05:22 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr1163ala,met1166ala' Tue Jun 30 15:36:51 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Tyr1163Ala;Met1166Ala]' in vitro In vitro 5 unspecified role unspecified role prey prey Region 160-435 Region 160-435 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