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 Functional importance of Shc tyrosine 317 on insulin signaling in Rat1 fibroblasts expressing insulin receptors. Functional importance of Shc tyrosine 317 on insulin signaling in Rat1 fibroblasts expressing insulin receptors. J. Biol. Chem. (0021-9258) 1997 Ishihara H., Sasaoka T., Ishiki M., Takata Y., Imamura T., Usui I., Langlois WJ., Sawa T., Kobayashi M. SH2 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 Ishihara H., Sasaoka T., Ishiki M., Takata Y., Imamura T., Usui I., Langlois WJ., Sawa T., Kobayashi M. SH2 PMID_in_GD PMID_in_GD J. Biol. Chem. (0021-9258) 1997 partial coverage rapid curation 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 grb2_rat Growth factor receptor-bound protein 2 Grb2 Ash Adapter protein GRB2 SH2/SH3 adapter GRB2 Protein Ash protein protein rat Rattus norvegicus (Rat) Rat MEAIAKYDFKATADDELSFKRGDILKVLNEECDQNWYKAELNGKDGFIPKNYIEMKPHPWFFGKIPRAKAEEMLSKQRHDGAFLIRESESAPGDFSLSVKFGNDVQHFKVLRDGAGKYFLWVVKFNSLNELVDYHRSTSVSRNQQIFLRDIEQVPQQPTYVQALFDFDPQEDGELGFRRGDFIHVMDNSDPNWWKGACHGQTGMFPRNYVTPVNRNV 83A4B0BA1B248DC4 grb2-shc1-9 1 GRB2_RAT 3 unspecified role unspecified role unspecified role unspecified role SHC1_HUMAN 2 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