MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Shc associates with the IL-3 receptor beta subunit, SHIP and Gab2 following IL-3 stimulation. Contribution of Shc PTB and SH2 domains. Shc associates with the IL-3 receptor beta subunit, SHIP and Gab2 following IL-3 stimulation. Contribution of Shc PTB and SH2 domains. Cell. Signal. (0898-6568) 2000 Bone H., Welham MJ. no Phosphatases PMID_in_GD partial coverage rapid curation in vivo in vivo coip coimmunoprecipitation co-immunoprecipitation CoIp immunoprecipitation Co-IP co-immunoprecipitation CoIp immunoprecipitation Co-IP coip predetermined predetermined participant predetermined Bone H., Welham MJ. no Phosphatases Phosphatases PMID_in_GD PMID_in_GD Cell. Signal. (0898-6568) 2000 partial coverage rapid curation Shc associates with the IL-3 receptor beta subunit, SHIP and Gab2 following IL-3 stimulation. Contribution of Shc PTB and SH2 domains. Shc associates with the IL-3 receptor beta subunit, SHIP and Gab2 following IL-3 stimulation. Contribution of Shc PTB and SH2 domains. Cell. Signal. (0898-6568) 2000 Bone H., Welham MJ. no Phosphatases PMID_in_GD partial coverage rapid curation in vitro In vitro pull down pull down predetermined predetermined participant predetermined Bone H., Welham MJ. no Phosphatases Phosphatases PMID_in_GD PMID_in_GD Cell. Signal. (0898-6568) 2000 partial coverage rapid curation Shc associates with the IL-3 receptor beta subunit, SHIP and Gab2 following IL-3 stimulation. Contribution of Shc PTB and SH2 domains. Shc associates with the IL-3 receptor beta subunit, SHIP and Gab2 following IL-3 stimulation. Contribution of Shc PTB and SH2 domains. Cell. Signal. (0898-6568) 2000 Bone H., Welham MJ. no Phosphatases PMID_in_GD partial coverage rapid curation unknown Unknown coip coimmunoprecipitation co-immunoprecipitation CoIp immunoprecipitation Co-IP co-immunoprecipitation CoIp immunoprecipitation Co-IP coip predetermined predetermined participant predetermined Bone H., Welham MJ. no Phosphatases Phosphatases PMID_in_GD PMID_in_GD Cell. Signal. (0898-6568) 2000 partial coverage rapid curation il3rb_human Cytokine receptor common subunit beta CSF2RB IL3RB IL5RB GM-CSF/IL-3/IL-5 receptor common beta subunit CDw131 protein protein human Homo sapiens Human MVLAQGLLSMALLALCWERSLAGAEETIPLQTLRCYNDYTSHITCRWADTQDAQRLVNVTLIRRVNEDLLEPVSCDLSDDMPWSACPHPRCVPRRCVIPCQSFVVTDVDYFSFQPDRPLGTRLTVTLTQHVQPPEPRDLQISTDQDHFLLTWSVALGSPQSHWLSPGDLEFEVVYKRLQDSWEDAAILLSNTSQATLGPEHLMPSSTYVARVRTRLAPGSRLSGRPSKWSPEVCWDSQPGDEAQPQNLECFFDGAAVLSCSWEVRKEVASSVSFGLFYKPSPDAGEEECSPVLREGLGSLHTRHHCQIPVPDPATHGQYIVSVQPRRAEKHIKSSVNIQMAPPSLNVTKDGDSYSLRWETMKMRYEHIDHTFEIQYRKDTATWKDSKTETLQNAHSMALPALEPSTRYWARVRVRTSRTGYNGIWSEWSEARSWDTESVLPMWVLALIVIFLTIAVLLALRFCGIYGYRLRRKWEEKIPNPSKSHLFQNGSAELWPPGSMSAFTSGSPPHQGPWGSRFPELEGVFPVGFGDSEVSPLTIEDPKHVCDPPSGPDTTPAASDLPTEQPPSPQPGPPAASHTPEKQASSFDFNGPYLGPPHSRSLPDILGQPEPPQEGGSQKSPPPGSLEYLCLPAGGQVQLVPLAQAMGPGQAVEVERRPSQGAAGSPSLESGGGPAPPALGPRVGGQDQKDSPVAIPMSSGDTEDPGVASGYVSSADLVFTPNSGASSVSLVPSLGLPSDQTPSLCPGLASGPPGAPGPVKSGFEGYVELPPIEGRSPRSPRNNPVPPEAKSPVLNPGERPADVSPTSPQPEGLLVLQQVGDYCFLPGLGPGPLSLRSKPSSPGPGPEIKNLDQAFQVKKPPGQAVPQVPVIQLFKALKQQDYLSLPPWEVNKPGEVC 3398E37FDB8F393A shc1_human SHC-transforming protein 1 SHC1 SHC SHCA Src homology 2 domain-containing-transforming protein C1 SHC-transforming protein A SHC-transforming protein 3 protein protein human Homo sapiens Human MDLLPPKPKYNPLRNESLSSLEEGASGSTPPEELPSPSASSLGPILPPLPGDDSPTTLCSFFPRMSNLRLANPAGGRPGSKGEPGRAADDGEGIVGAAMPDSGPLPLLQDMNKLSGGGGRRTRVEGGQLGGEEWTRHGSFVNKPTRGWLHPNDKVMGPGVSYLVRYMGCVEVLQSMRALDFNTRTQVTREAISLVCEAVPGAKGATRRRKPCSRPLSSILGRSNLKFAGMPITLTVSTSSLNLMAADCKQIIANHHMQSISFASGGDPDTAEYVAYVAKDPVNQRACHILECPEGLAQDVISTIGQAFELRFKQYLRNPPKLVTPHDRMAGFDGSAWDEEEEEPPDHQYYNDFPGKEPPLGGVVDMRLREGAAPGAARPTAPNAQTPSHLGATLPVGQPVGGDPEVRKQMPPPPPCPGRELFDDPSYVNVQNLDKARQAVGGAGPPNPAINGSAPRDLFDMKPFEDALRVPPPPQSVSMAEQLRGEPWFHGKLSRREAEALLQLNGDFLVRESTTTPGQYVLTGLQSGQPKHLLLVDPEGVVRTKDHRFESVSHLISYHMDNHLPIISAGSELCLQQPVERKL DIP protein P29353 original sequence version: 161 DIP protein P29353 original sequence version: 190 7EFA5CB185A548D1 il3b2_mouse Interleukin-3 receptor class 2 subunit beta Csf2rb2 Ai2ca Il3r Il3rb2 Interleukin-3 receptor class II beta chain Colony-stimulating factor 2 receptor subunit beta-2 protein protein mouse Mus musculus Mouse MDQQMALTWGLCYMALVALCWGHEVTEEEETVPLKTLECYNDYTNRIICSWADTEDAQGLINMTLLYHQLDKIQSVSCELSEKLMWSECPSSHRCVPRRCVIPYTRFSNGDNDYYSFQPDRDLGIQLMVPLAQHVQPPPPKDIHISPSGDHFLLEWSVSLGDSQVSWLSSKDIEFEVAYKRLQDSWEDASSLHTSNFQVNLEPKLFLPNSIYAARVRTRLSAGSSLSGRPSRWSPEVHWDSQPGDKAQPQNLQCFFDGIQSLHCSWEVWTQTTGSVSFGLFYRPSPAAPEEKCSPVVKEPQASVYTRYRCSLPVPEPSAHSQYTVSVKHLEQGKFIMSYYHIQMEPPILNQTKNRDSYSLHWETQKIPKYIDHTFQVQYKKKSESWKDSKTENLGRVNSMDLPQLEPDTSYCARVRVKPISDYDGIWSEWSNEYTWTTDWVMPTLWIVLILVFLIFTLLLALHFGRVYGYRTYRKWKEKIPNPSKSLLFQDGGKGLWPPGSMAAFATKNPALQGPQSRLLAEQQGVSYEHLEDNNVSPLTIEDPNIIRDPPSRPDTTPAASSESTEQLPNVQVEGPIPSSRPRKQLPSFDFNGPYLGPPQSHSLPDLPGQLGSPQVGGSLKPALPGSLEYMCLPPGGQVQLVPLSQVMGQGQAMDVQCGSSLETTGSPSVEPKENPPVELSVEKQEARDNPMTLPISSGGPEGSMMASDYVTPGDPVLTLPTGPLSTSLGPSLGLPSAQSPSLCLKLPRVPSGSPALGPPGFEDYVELPPSVSQAATSPPGHPAPPVASSPTVIPGEPREEVGPASPHPEGLLVLQQVGDYCFLPGLGPGSLSPHSKPPSPSLCSETEDLDQDLSVKKFPYQPLPQAPAIQFFKSLKY mint In mouse, there are two classes of high-affinity IL3 receptors. One contains this IL3-specific beta chain and the other contains the beta chain also shared by high-affinity IL5 and GM-CSF receptors 8EBC9092ADC24D56 gab2_human GRB2-associated-binding protein 2 Growth factor receptor bound protein 2-associated protein 2 GRB2-associated binder 2 pp100 GAB2 KIAA0571 protein protein human Homo sapiens Human MSGGGDVVCTGWLRKSPPEKKLRRYAWKKRWFILRSGRMSGDPDVLEYYKNDHSKKPLRIINLNFCEQVDAGLTFNKKELQDSFVFDIKTSERTFYLVAETEEDMNKWVQSICQICGFNQAEESTDSLRNVSSAGHGPRSSPAELSSSSQHLLRERKSSAPSHSSQPTLFTFEPPVSNHMQPTLSTSAPQEYLYLHQCISRRAENARSASFSQGTRASFLMRSDTAVQKLAQGNGHCVNGISGQVHGFYSLPKPSRHNTEFRDSTYDLPRSLASHGHTKGSLTGSETDNEDVYTFKTPSNTLCREFGDLLVDNMDVPATPLSAYQIPRTFTLDKNHNAMTVATPGDSAIAPPPRPPKPSQAETPRWGSPQQRPPISENSRSVAATIPRRNTLPAMDNSRLHRASSCETYEYPQRGGESAGRSAESMSDGVGSFLPGKMIVGRSDSTNSEDNYVPMNPGSSTLLAMERAGDNSQSVYIPMSPGAHHFDSLGYPSTTLPVHRGPSRGSEIQPPPVNRNLKPDRKAKPTPLDLRNNTVIDELPFKSPITKSWSRANHTFNSSSSQYCRPISTQSITSTDSGDSEENYVPMQNPVSASPVPSGTNSPAPKKSTGSVDYLALDFQPSSPSPHRKPSTSSVTSDEKVDYVQVDKEKTQALQNTMQEWTDVRQSSEPSKGAKL 107623FD07D884C9 ship1_human Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1 INPP5D SHIP SHIP1 Inositol polyphosphate-5-phosphatase of 145 kDa p150Ship SH2 domain-containing inositol 5'-phosphatase 1 Inositol polyphosphate-5-phosphatase D Phosphatidylinositol 4,5-bisphosphate 5-phosphatase protein protein human Homo sapiens Human MVPCWNHGNITRSKAEELLSRTGKDGSFLVRASESISRAYALCVLYRNCVYTYRILPNEDDKFTVQASEGVSMRFFTKLDQLIEFYKKENMGLVTHLQYPVPLEEEDTGDDPEEDTVESVVSPPELPPRNIPLTASSCEAKEVPFSNENPRATETSRPSLSETLFQRLQSMDTSGLPEEHLKAIQDYLSTQLAQDSEFVKTGSSSLPHLKKLTTLLCKELYGEVIRTLPSLESLQRLFDQQLSPGLRPRPQVPGEANPINMVSKLSQLTSLLSSIEDKVKALLHEGPESPHRPSLIPPVTFEVKAESLGIPQKMQLKVDVESGKLIIKKSKDGSEDKFYSHKKILQLIKSQKFLNKLVILVETEKEKILRKEYVFADSKKREGFCQLLQQMKNKHSEQPEPDMITIFIGTWNMGNAPPPKKITSWFLSKGQGKTRDDSADYIPHDIYVIGTQEDPLSEKEWLEILKHSLQEITSVTFKTVAIHTLWNIRIVVLAKPEHENRISHICTDNVKTGIANTLGNKGAVGVSFMFNGTSLGFVNSHLTSGSEKKLRRNQNYMNILRFLALGDKKLSPFNITHRFTHLFWFGDLNYRVDLPTWEAETIIQKIKQQQYADLLSHDQLLTERREQKVFLHFEEEEITFAPTYRFERLTRDKYAYTKQKATGMKYNLPSWCDRVLWKSYPLVHVVCQSYGSTSDIMTSDHSPVFATFEAGVTSQFVSKNGPGTVDSQGQIEFLRCYATLKTKSQTKFYLEFHSSCLESFVKSQEGENEEGSEGELVVKFGETLPKLKPIISDPEYLLDQHILISIKSSDSDESYGEGCIALRLEATETQLPIYTPLTHHGELTGHFQGEIKLQTSQGKTREKLYDFVKTERDESSGPKTLKSLTSHDPMKQWEVTSRAPPCSGSSITEIINPNYMGVGPFGPPMPLHVKQTLSPDQQPTAWSYDQPPKDSPLGPCRGESPPTPPGQPPISPKKFLPSTANRGLPPRTQESRPSDLGKNAGDTLPQEDLPLTKPEMFENPLYGSLSSFPKPAPRKDQESPKMPRKEPPPCPEPGILSPSIVLTKAQEADRGEGPGKQVPAPRLRSFTCSSSAEGRAAGGDKSQGKPKTPVSSQAPVPAKRPIKPSRSEINQQTPPTPTPRPPLPVKSPAVLHLQHSKGRDYRDNTELPHHGKHRPEEGPPGPLGRTAMQ 7958E91A64A4B68B shc1-csf2rb2 1 6 unspecified role unspecified role prey prey physiological level physiological level endogenous level endogenous endogenous endogenous level phosphotyrosine o4'-phospho-tyrosine 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 range MINT-413205: original sequence: 575-575 : TEQLPNVQVEGPIPSSRPRK Stoichiometry: 1.0 5 unspecified role unspecified role bait bait physiological level physiological level endogenous level endogenous endogenous endogenous level binding site binding region binding-associated region binding region deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain range MINT-413199: original sequence: 1-238 : MDLLPPKPKYNPLRNESLSSLEEGASGSTPPEELPSPSASSLGPILPPLPGDDSPTTLCSFFPRMSNLRLANPAGGRPGSKGEPGRAADDGEGIVGAAMPDSGPLPLLQDMNKLSGGGGRRTRVEGGQLGGEEWTRHGSFVNKPTRGWLHPNDKVMGPGVSYLVRYMGCVEVLQSMRALDFNTRTQVTREAISLVCEAVPGAKGATRRRKPCSRPLSSILGRSNLKFAGMPITLTVS Stoichiometry: 1.0 physical association physical association homomint domino mint shc1-gab2 1 5 unspecified role unspecified role bait bait physiological level physiological level endogenous level endogenous endogenous endogenous level binding site binding region binding-associated region binding region deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain range MINT-413162: original sequence: 336-473 : AWDEEEEEPPDHQYYNDFPGKEPPLGGVVDMRLREGAAPGAARPTAPNAQTPSHLGATLPVGQPVGGDPEVRKQMPPPPPCPGRELFDDPSYVNVQNLDKARQAVGGAGPPNPAINGSAPRDLFDMKPFEDALRVPP Stoichiometry: 1.0 7 unspecified role unspecified role prey prey physiological level physiological level endogenous level endogenous endogenous endogenous level Stoichiometry: 1.0 physical association physical association homomint domino mint shc1-csf2rb2-1 1 6 unspecified role unspecified role prey prey physiological level physiological level endogenous level endogenous endogenous endogenous level phosphotyrosine o4'-phospho-tyrosine 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 range MINT-413242: original sequence: 610-610 : QSHSLPDLPGQLGSPQVGGS Stoichiometry: 1.0 5 unspecified role unspecified role bait bait physiological level physiological level endogenous level endogenous endogenous endogenous level binding site binding region binding-associated region binding region deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain range MINT-413236: original sequence: 336-473 : AWDEEEEEPPDHQYYNDFPGKEPPLGGVVDMRLREGAAPGAARPTAPNAQTPSHLGATLPVGQPVGGDPEVRKQMPPPPPCPGRELFDDPSYVNVQNLDKARQAVGGAGPPNPAINGSAPRDLFDMKPFEDALRVPP Stoichiometry: 1.0 physical association physical association homomint domino mint shc1-csf2rb2-2 2 6 unspecified role unspecified role prey prey purified purified phosphotyrosine o4'-phospho-tyrosine 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 range MINT-413181: original sequence: 575-575 : TEQLPNVQVEGPIPSSRPRK Stoichiometry: 1.0 5 unspecified role unspecified role bait bait purified purified binding site binding region binding-associated region binding region deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain range MINT-413175: original sequence: 1-238 : MDLLPPKPKYNPLRNESLSSLEEGASGSTPPEELPSPSASSLGPILPPLPGDDSPTTLCSFFPRMSNLRLANPAGGRPGSKGEPGRAADDGEGIVGAAMPDSGPLPLLQDMNKLSGGGGRRTRVEGGQLGGEEWTRHGSFVNKPTRGWLHPNDKVMGPGVSYLVRYMGCVEVLQSMRALDFNTRTQVTREAISLVCEAVPGAKGATRRRKPCSRPLSSILGRSNLKFAGMPITLTVS Stoichiometry: 1.0 direct interaction direct interaction homomint domino mint shc1-gab2-1 2 5 unspecified role unspecified role bait bait purified purified binding site binding region binding-associated region binding region deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain range MINT-413188: original sequence: 336-473 : AWDEEEEEPPDHQYYNDFPGKEPPLGGVVDMRLREGAAPGAARPTAPNAQTPSHLGATLPVGQPVGGDPEVRKQMPPPPPCPGRELFDDPSYVNVQNLDKARQAVGGAGPPNPAINGSAPRDLFDMKPFEDALRVPP Stoichiometry: 1.0 7 unspecified role unspecified role prey prey purified purified Stoichiometry: 1.0 direct interaction direct interaction homomint domino mint shc1-csf2rb2-3 2 6 unspecified role unspecified role prey prey purified purified phosphotyrosine o4'-phospho-tyrosine 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 range MINT-413229: original sequence: 610-610 : QSHSLPDLPGQLGSPQVGGS Stoichiometry: 1.0 5 unspecified role unspecified role bait bait purified purified binding site binding region binding-associated region binding region deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain range MINT-413223: original sequence: 336-473 : AWDEEEEEPPDHQYYNDFPGKEPPLGGVVDMRLREGAAPGAARPTAPNAQTPSHLGATLPVGQPVGGDPEVRKQMPPPPPCPGRELFDDPSYVNVQNLDKARQAVGGAGPPNPAINGSAPRDLFDMKPFEDALRVPP Stoichiometry: 1.0 direct interaction direct interaction homomint domino mint shc1-inpp5d-2 2 8 unspecified role unspecified role prey prey purified purified Stoichiometry: 1.0 5 unspecified role unspecified role bait bait purified purified binding site binding region binding-associated region binding region deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain range MINT-413212: original sequence: 1-238 : MDLLPPKPKYNPLRNESLSSLEEGASGSTPPEELPSPSASSLGPILPPLPGDDSPTTLCSFFPRMSNLRLANPAGGRPGSKGEPGRAADDGEGIVGAAMPDSGPLPLLQDMNKLSGGGGRRTRVEGGQLGGEEWTRHGSFVNKPTRGWLHPNDKVMGPGVSYLVRYMGCVEVLQSMRALDFNTRTQVTREAISLVCEAVPGAKGATRRRKPCSRPLSSILGRSNLKFAGMPITLTVS Stoichiometry: 1.0 direct interaction direct interaction homomint domino mint csf2rb-shc1 3 SHC1_HUMAN 5 unspecified role unspecified role unspecified role unspecified role IL3RB_HUMAN 4 unspecified role unspecified role unspecified role unspecified role phosphorylated phosphorylated residue phosres phosphorylated residue PhosRes Phospho Phosphorylation Phosphorylation (O of Serine, Threonine, Tyrosine and Aspartate, N epsilon of Lysine) certain certain sequence position certain certain certain sequence position certain binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain association association homomint mint