IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein. The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein. Mol. Cell. Biol. (0270-7306) 1996 Borg JP., Ooi J., Levy E., Margolis B. Apoptosis - Interactions involving proteins with a function related to apoptosis Synapse - Interactions of proteins with an established role in the presynapse. in vitro In vitro anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Borg JP., Ooi J., Levy E., Margolis B. Apoptosis - Interactions involving proteins with a function related to apoptosis Accepted 2010-JAN-10 by SKERRIEN (applied to all records created before 2005-Sep-01). Mol. Cell. Biol. (0270-7306) 1996 The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein. The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein. Mol. Cell. Biol. (0270-7306) 1996 Borg JP., Ooi J., Levy E., Margolis B. Apoptosis - Interactions involving proteins with a function related to apoptosis Synapse - Interactions of proteins with an established role in the presynapse. in vitro In vitro anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Borg JP., Ooi J., Levy E., Margolis B. Apoptosis - Interactions involving proteins with a function related to apoptosis Accepted 2010-JAN-10 by SKERRIEN (applied to all records created before 2005-Sep-01). Mol. Cell. Biol. (0270-7306) 1996 The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein. The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein. Mol. Cell. Biol. (0270-7306) 1996 Borg JP., Ooi J., Levy E., Margolis B. Apoptosis - Interactions involving proteins with a function related to apoptosis Synapse - Interactions of proteins with an established role in the presynapse. human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Borg JP., Ooi J., Levy E., Margolis B. Apoptosis - Interactions involving proteins with a function related to apoptosis Accepted 2010-JAN-10 by SKERRIEN (applied to all records created before 2005-Sep-01). Mol. Cell. Biol. (0270-7306) 1996 apba1_human Amyloid-beta A4 precursor protein-binding family A member 1 APBA1 MINT1 X11 Neuron-specific X11 protein Neuronal Munc18-1-interacting protein 1 Adapter protein X11alpha protein protein human Homo sapiens Human MNHLEGSAEVEVTDEAAGGEVNESVEADLEHPEVEEEQQQPPQQQHYVGRHQRGRALEDLRAQLGQEEEERGECLARSASTESGFHNHTDTAEGDVIAAARDGYDAERAQDPEDESAYAVQYRPEAEEYTEQAEAEHAEATHRRALPNHLHFHSLEHEEAMNAAYSGYVYTHRLFHRGEDEPYSEPYADYGGLQEHVYEEIGDAPELDARDGLRLYEQERDEAAAYRQEALGARLHHYDERSDGESDSPEKEAEFAPYPRMDSYEQEEDIDQIVAEVKQSMSSQSLDKAAEDMPEAEQDLERPPTPAGGRPDSPGLQAPAGQQRAVGPAGGGEAGQRYSKEKRDAISLAIKDIKEAIEEVKTRTIRSPYTPDEPKEPIWVMRQDISPTRDCDDQRPMDGDSPSPGSSSPLGAESSSTSLHPSDPVEASTNKESRKSLASFPTYVEVPGPCDPEDLIDGIIFAANYLGSTQLLSDKTPSKNVRMMQAQEAVSRIKMAQKLAKSRKKAPEGESQPMTEVDLFISTQRIKVLNADTQETMMDHPLRTISYIADIGNIVVLMARRRMPRSNSQENVEASHPSQDGKRQYKMICHVFESEDAQLIAQSIGQAFSVAYQEFLRANGINPEDLSQKEYSDLLNTQDMYNDDLIHFSKSENCKDVFIEKQKGEILGVVIVESGWGSILPTVIIANMMHGGPAEKSGKLNIGDQIMSINGTSLVGLPLSTCQSIIKGLKNQSRVKLNIVRCPPVTTVLIRRPDLRYQLGFSVQNGIICSLMRGGIAERGGVRVGHRIIEINGQSVVATPHEKIVHILSNAVGEIHMKTMPAAMYRLLTAQEQPVYI 29C3620BBC89534B grb2_human Growth factor receptor-bound protein 2 GRB2 ASH Adapter protein GRB2 SH2/SH3 adapter GRB2 Protein Ash protein protein human Homo sapiens Human MEAIAKYDFKATADDELSFKRGDILKVLNEECDQNWYKAELNGKDGFIPKNYIEMKPHPWFFGKIPRAKAEEMLSKQRHDGAFLIRESESAPGDFSLSVKFGNDVQHFKVLRDGAGKYFLWVVKFNSLNELVDYHRSTSVSRNQQIFLRDIEQVPQQPTYVQALFDFDPQEDGELGFRRGDFIHVMDNSDPNWWKGACHGQTGMFPRNYVTPVNRNV 83A4B0BA1B248DC4 apbb1_human Amyloid beta precursor protein binding family B member 1 APBB1 FE65 RIR Protein Fe65 Amyloid-beta A4 precursor protein-binding family B member 1 protein protein human Homo sapiens Human MSVPSSLSQSAINANSHGGPALSLPLPLHAAHNQLLNAKLQATAVGPKDLRSAMGEGGGPEPGPANAKWLKEGQNQLRRAATAHRDQNRNVTLTLAEEASQEPEMAPLGPKGLIHLYSELELSAHNAANRGLRGPGLIISTQEQGPDEGEEKAAGEAEEEEEDDDDEEEEEDLSSPPGLPEPLESVEAPPRPQALTDGPREHSKSASLLFGMRNSAASDEDSSWATLSQGSPSYGSPEDTDSFWNPNAFETDSDLPAGWMRVQDTSGTYYWHIPTGTTQWEPPGRASPSQGSSPQEESQLTWTGFAHGEGFEDGEFWKDEPSDEAPMELGLKEPEEGTLTFPAQSLSPEPLPQEEEKLPPRNTNPGIKCFAVRSLGWVEMTEEELAPGRSSVAVNNCIRQLSYHKNNLHDPMSGGWGEGKDLLLQLEDETLKLVEPQSQALLHAQPIISIRVWGVGRDSGRERDFAYVARDKLTQMLKCHVFRCEAPAKNIATSLHEICSKIMAERRNARCLVNGLSLDHSKLVDVPFQVEFPAPKNELVQKFQVYYLGNVPVAKPVGVDVINGALESVLSSSSREQWTPSHVSVAPATLTILHQQTEAVLGECRVRFLSFLAVGRDVHTFAFIMAAGPASFCCHMFWCEPNAASLSEAVQAACMLRYQKCLDARSQASTSCLPAPPAESVARRVGWTVRRGVQSLWGSLKPKRLGAHTP DIP protein O00213 original sequence version: 77 FD4A2EF7E8D8E884 egfr_human Epidermal growth factor receptor ERBB1 EGFR Receptor tyrosine-protein kinase erbB-1 Proto-oncogene c-ErbB-1 ERBB HER1 protein protein human Homo sapiens Human MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTEDSIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPSRDPHYQDPHSTAVGNPEYLNTVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRVAPQSSEFIGA DIP protein P00533 original sequence version: 213 DIP protein P00533 original sequence version: 214 DIP protein P00533 original sequence version: 119 DIP protein P00533 original sequence version: 207 DIP protein P00533 original sequence version: 132 DIP protein P00533-1 original sequence version: 197 DIP protein P00533 original sequence version: 163 DIP protein P00533-1 original sequence version: 159 DIP protein P00533 original sequence version: 184 DIP protein P00533-1 original sequence version: 174 DIP protein P00533-1 original sequence version: 191 DIP protein P00533 original sequence version: 218 DIP protein P00533 original sequence version: 221 DIP protein P00533-1 original sequence version: 221 DIP protein P00533 original sequence version: 226 DIP protein P00533 original sequence version: 166 DIP protein P00533-1 original sequence version: 166 DIP protein P00533 original sequence version: 194 DIP protein P00533-1 original sequence version: 194 DIP protein P00533-1 original sequence version: 224 DIP protein P00533 original sequence version: 189 DIP protein P00533-1 original sequence version: 207 DIP protein P00533 original sequence version: 177 DIP protein P00533 original sequence version: 168 D8A2A50B4EFB6ED2 apbb1_rat Amyloid beta precursor protein binding family B member 1 Protein Fe65 Apbb1 Fe65 Amyloid-beta A4 precursor protein-binding family B member 1 Rir protein protein rat Rattus norvegicus (Rat) Rat MSVPSSLSQSAINANSHGGPALSFPFPLHAAHNQLLNAKLQATAVVPKDLRSAMGEGSVPEPGPANAKWLKEGQNQLRRAATAHRDQNRNVTLTLAEEASQEAETAPLGPKGLMHLYSELELSAHNAANRGLHGSALIINTQGLGPDEGEEKAAGEVEEEDEDEEEEDEEEEDLSSPQGLPEPLENVEVPSGPQVLTDGPREHSKSASLLFGMRNSAASDEDSSWATLSQGSPSYGSPEDTDSFWNPNAFETDSDLPAGWMRVQDTSGTYYWHIPTGTTQWEPPGRASPSQGNSPQEESQLTWTGFAHQEGFEEGEFWKDEPSEEAPMELGLKDPEEGTLPFSAQSLSPEPVPQEEENLPQRNANPGIKCFAVRSLGWVEMTEEELAPGRSSVAVNNCIRQLSYHKNNLHDPMSGGWGEGKDLLLQLEDETLKLVEPQNQTLLHAQPIVSIRVWGVGRDSGRERDFAYVARDKLTQMLKCHVFRCEAPAKNIATSLHEICSKIMSERRNARCLVNGLSLDHSKLVDVPFQVEFPAPKNELVQKFQVYYLGNVPVAKPVGVDVINGALESVLSSSSREQWTPSHVSVAPATLTILHQQTEAVLGECRVRFLSFLAVGRDVHTFAFIMAAGPASFCCHMFWCEPNAASLSEAVQAACMLRYQKCLDARSQTSTSCLPAPPAESVARRVGWTVRRGVQSLWGSLKPKRLGSQTP A6C9820F5D2BD7BE shc1_mouse SHC-transforming protein 1 ShcA Shc1 Shc Src homology 2 domain-containing-transforming protein C1 SHC-transforming protein A protein protein mouse Mus musculus Mouse MDLLPPKPKYNPLRNESLSSLEEGASGSTPPEELPSPSASSLGPILPPLPGDDSPTTLCSFFPRMSNLKLANPAGGRLGPKGEPGKAAEDGEGSAGAALRDSGLLPLLQDMNKLSGGGGRRTRVEGGQLGGEEWTRHGSFVNKPTRGWLHPNDKVMGPGVSYLVRYMGCVEVLQSMRALDFNTRTQVTREAISLVCEAVPGAKGATRRRKPCSRPLSSILGRSNLKFAGMPITLTVSTSSLNLMAADCKQIIANHHMQSISFASGGDPDTAEYVAYVAKDPVNQRACHILECPEGLAQDVISTIGQAFELRFKQYLRNPPKLVTPHDRMAGFDGSAWDEEEEEPPDHQYYNDFPGKEPPLGGVVDMRLREGAARPTLPSAQMSSHLGATLPIGQHAAGDHEVRKQMLPPPPCPGRELFDDPSYVNIQNLDKARQAGGGAGPPNPSLNGSAPRDLFDMKPFEDALRVPPPPQSMSMAEQLQGEPWFHGKLSRREAEALLQLNGDFLVRESTTTPGQYVLTGLQSGQPKHLLLVDPEGVVRTKDHRFESVSHLISYHMDNHLPIISAGSELCLQQPVDRKV 99C22E64412B6236 a4_human Amyloid-beta precursor protein APP A4 AD1 Alzheimer disease amyloid protein ABPP PreA4 Cerebral vascular amyloid peptide Protease nexin-II APPI Amyloid precursor protein Amyloid-beta A4 protein Alzheimer disease amyloid A4 protein homolog Amyloid-beta (A4) precursor protein protein protein human Homo sapiens Human MLPGLALLLLAAWTARALEVPTDGNAGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDNVDSADAEEDDSDVWWGGADTDYADGSEDKVVEVAEEEEVAEVEEEEADDDEDDEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCAPFFYGGCGGNRNNFDTEEYCMAVCGSAMSQSLLKTTQEPLARDPVKLPTTAASTPDAVDKYLETPGDENEHAHFQKAKERLEAKHRERMSQVMREWEEAERQAKNLPKADKKAVIQHFQEKVESLEQEAANERQQLVETHMARVEAMLNDRRRLALENYITALQAVPPRPRHVFNMLKKYVRAEQKDRQHTLKHFEHVRMVDPKKAAQIRSQVMTHLRVIYERMNQSLSLLYNVPAVAEEIQDEVDELLQKEQNYSDDVLANMISEPRISYGNDALMPSLTETKTTVELLPVNGEFSLDDLQPWHSFGADSVPANTENEVEPVDARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLKKKQYTSIHHGVVEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQN DIP protein P05067 original sequence version: 160 DIP protein P05067 original sequence version: 207 DIP protein P05067 original sequence version: 185 DIP protein P05067 original sequence version: 188 A12EE761403740F5 app-apba1-1 2 10 unspecified role unspecified role prey prey human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. 4 unspecified role unspecified role bait bait ecoli Escherichia coli (strain K12) physical association physical association Revisit when Protein Editor in place Prey:betaAPP cytoplasmic domain, amino acids 649-695. Bait: Phosphotyrosine domain of X11 tagged with GST. The authors also showed that a) beta APP phosphorylation is not required for this interaction b) deletion of the last 18 amino acids of the cytplasmic domain of beta APP abolishes this interaction c)Y862G mutation of beta-APP abolishes this interaction d) N684A mutation of beta-APP abolishes this interaction. app-apbb1-1 2 10 unspecified role unspecified role prey prey human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. 8 unspecified role unspecified role bait bait ecoli Escherichia coli (strain K12) physical association physical association Revisit when Protein Editor in place Prey:betaAPP cytoplasmic domain, amino acids 649-695. Bait: Phosphotyrosine domain of FE65 (C) tagged with GST. The authors also showed that a)beta APP phosphorylation is not required for this interaction b) deletion of the last 18 amino acids of the cytoplasmic domain of beta APP abolishes this interaction c)Y862G mutation of beta-APP abolishes this interaction. egfr-grb2 1 7 unspecified role unspecified role prey prey mouse-3t3 Mus musculus embryo cells 3t3 Mouse embryo fibroblast cells 5 unspecified role unspecified role bait bait in vitro In vitro physical association physical association Prey:HER14 cells which are NIH-3T3 cells expressing the human EGF receptor. Interaction dependent on stimulation of cells with EGF. Revisit when Protein Editor in place Bait: GST tagged Grb2 egfr-shc1-2 1 7 unspecified role unspecified role prey prey mouse-3t3 Mus musculus embryo cells 3t3 Mouse embryo fibroblast cells 9 unspecified role unspecified role bait bait ecoli Escherichia coli (strain K12) physical association physical association Prey:HER14 cells which are NIH-3T3 cells expressing the human EGF receptor. Revisit when Protein Editor in place Bait: GST tagged shc1 phosphotyrosine domain described in PMID 7798194 app-apb1-1 3 10 unspecified role unspecified role prey prey 4 unspecified role unspecified role bait bait physical association physical association Revisit when Protein Editor in place Deletion analysis showed that the PDZ domains of X11 (Q02410) are not necessary for this interaction. Bait: myc-tagged(Q02410) was expressed full-length protein. Prey: beta APP (amino acids 18-671 of P05067)was used in the expression contruct.Proteins were transiently expressed. Bait:X11 (Q02410)F479V mutation abolishes this interaction. Prey:APP(P05067)Y682G mutation abolishes this interaction. app-apbb1-2 3 10 unspecified role unspecified role prey prey 6 unspecified role unspecified role bait bait physical association physical association Revisit when Protein Editor in place Proteins were transiently expressed. Prey:beta APP (amino acids 18-671 of P05067)was used in the expression contruct. Bait:myc-tagged(O00213) was expressed full-length protein. Bait:FE65 (O00213)C443V mutation abolishes this interaction. Prey:APP(P05067)Y682G mutation abolishes this interaction. Prey:APP(P05067)N684A mutation abolishes this interaction. apba1-app-1 2 4 unspecified role unspecified role prey prey human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. 10 unspecified role unspecified role bait bait ecoli Escherichia coli (strain K12) physical association physical association Revisit when Protein Editor in place Bait:GST-tagged betaAPP cytoplasmic domain, amino acids 649-695. Prey: full length myc-tagged X11. Deletion analysis of X11 (Q02410)showed that the PDZ domains are not necessary for this interaction. app-apbb1-5 2 10 unspecified role unspecified role bait bait ecoli Escherichia coli (strain K12) 6 unspecified role unspecified role prey prey human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. physical association physical association Revisit when Protein Editor in place Prey:GST-tagged betaAPP cytoplasmic domain, amino acids 649-695. Bait: full length myc-tagged X11. Deletion analysis of X11 (Q02410)showed that the PDZ domains are not necessary for this interaction.