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 http://mint.bio.uniroma2.it/mint nakagawa-2004-2 Tyrosine phosphatase epsilonM stimulates migration and survival of porcine aortic endothelial cells by activating c-Src. pig-endothelium Pig endothelium endothelium Endothelial cells [endothelium] anti bait coip anti bait coimmunoprecipitation anti bait coip anti tag western anti tag western blot anti tag western Nakagawa Y., Yamada N., Shimizu H., Shiota M., Tamura M., Kim-Mitsuyama S., Miyazaki H. Biochem. Biophys. Res. Commun. (0006-291X) 2004 IMEx Only protein-protein interactions partial coverage imex curation imex curation rapid curation ptpre_rat Receptor-type tyrosine-protein phosphatase epsilon Ptpre Ptpe protein protein rat Rattus norvegicus (Rat) Rat MEPFCPLLLASFSLSLATAGQGNDTTPTESNWTSTTAGPPDPGTSQPLLTWLLLPLLLLLFLLAAYFFRFRKQRKAVVNSNDKKMPNGILEEQEQQRVMLLSRSPSGPKKYFPIPVEHLEEEIRVRSADDCKRFREEFNSLPSGHIQGTFELANKEENREKNRYPNILPNDHCRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQRSATIVMLTNLKERKEEKCYQYWPDQGCWTYGNIRVCVEDCVVLVDYTIRKFCIHPQLPDSCKAPRLVSQLHFTSWPDFGVPFTPIGMLKFLKKVKTLNPSHAGPIVVHCSAGVGRTGTFIVIDAMMDMIHSEQKVDVFEFVSRIRNQRPQMVQTDVQYTFIYQALLEYYLYGDTELDVSSLERHLQTLHGTATHFDKIGLEEEFRKLTNVRIMKENMRTGNLPANMKKARVIQIIPYDFNRVILSMKRGQEFTDYINASFIDGYRQKDYFMATQGPLAHTVEDFWRMVWEWKSHTIVMLTEVQEREQDKCYQYWPTEGSVTHGDITIEIKSDTLSEAISIRDFLVTFKQPLARQEEQVRMVRQFHFHGWPEVGIPTEGKGMIDLIAAVQKQQQQTGNHPITVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQAVKSLRLQRPHMVQTLEQYEFCYKVVQDFIDIFSDYANFK fragmentation type: fragment mint k7gpr7_pig Tyrosine-protein kinase SRC protein protein pig Sus scrofa (Pig) Pig MGSNKSKPKDASQRRRSLEPAENTHGGGGGGGGGGGAFPTSQTPSKPASADGHRGPSTAFAPAAAEPKLFGGFNSSDTVTSPQRAGPLAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTRKVDVSQTWFTFRWLQREGDWWLAHSLSTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNAENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFNSLQQLVAYYSKHADGLCHRLTTVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYIVTEYMSKGSLLDFLKGETGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLACKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESLHDLMCQCWRKDPEERPTFEYLQAFLEDYFTSTEPQYQPGENL ptpre-src-1 1215114 ptpre_rat Ptp e 1215115 enzyme enzyme neutral component neutral component p.Asp302Ala trapping mutant trap-mutant trapping mutant trap-mutant certain certain sequence position certain certain certain sequence position certain false region ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false src_human Src 1215116 enzyme target enzyme target substrate substrate neutral component neutral component phosphorylated 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 false prerequisite-ptm Resulting Phenotypic qualities (properties)[PATO]: PATO:0002221 (increased phosphorylation) physical association physical association false false false f4c