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 moon-2010-4 Wild-type p53-induced phosphatase 1 dephosphorylates histone variant gamma-H2AX and suppresses DNA double strand break repair. human Homo sapiens Human anti tag coip anti tag coimmunoprecipitation anti tag coip predetermined predetermined participant predetermined Moon SH., Lin L., Zhang X., Nguyen TA., Darlington Y., Waldman AS., Lu X., Donehower LA. J. Biol. Chem. (0021-9258) 2010 partial coverage rapid curation rapid curation moon-2010-1 Wild-type p53-induced phosphatase 1 dephosphorylates histone variant gamma-H2AX and suppresses DNA double strand break repair. in vitro In vitro phosphatase assay phosphatase assay predetermined predetermined participant predetermined Moon SH., Lin L., Zhang X., Nguyen TA., Darlington Y., Waldman AS., Lu X., Donehower LA. J. Biol. Chem. (0021-9258) 2010 partial coverage rapid curation rapid curation h2ax_human Histone H2AX H2AX H2AFX Histone H2A.X protein protein human Homo sapiens Human MSGRGKTGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGHYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGGVTIAQGGVLPNIQAVLLPKKTSATVGPKAPSGGKKATQASQEY ppm1d_human Protein phosphatase 1D Protein phosphatase 2C isoform delta p53-induced protein phosphatase 1 Protein phosphatase magnesium-dependent 1 delta PPM1D WIP1 protein protein human Homo sapiens Human MAGLYSLGVSVFSDQGGRKYMEDVTQIVVEPEPTAEEKPSPRRSLSQPLPPRPSPAALPGGEVSGKGPAVAAREARDPLPDAGASPAPSRCCRRRSSVAFFAVCDGHGGREAAQFAREHLWGFIKKQKGFTSSEPAKVCAAIRKGFLACHLAMWKKLAEWPKTMTGLPSTSGTTASVVIIRGMKMYVAHVGDSGVVLGIQDDPKDDFVRAVEVTQDHKPELPKERERIEGLGGSVMNKSGVNRVVWKRPRLTHNGPVRRSTVIDQIPFLAVARALGDLWSYDFFSGEFVVSPEPDTSVHTLDPQKHKYIILGSDGLWNMIPPQDAISMCQDQEEKKYLMGEHGQSCAKMLVNRALGRWRQRMLRADNTSAIVICISPEVDNQGNFTNEDELYLNLTDSPSYNSQETCVMTPSPCSTPPVKSLEEDPWPRVNSKDHIPALVRSNAFSENFLEVSAEIARENVQGVVIPSKDPEPLEENCAKALTLRIHDSLNNSLPIGLVPTNSTNTVMDQKNLKMSTPGQMKAQEIERTPPTNFKRTLEESNSGPLMKKHRRNGLSRSSGAQPASLPTTSQRKNSVKLTMRRRLRGQKKIGNPLLHQHRKTVCVC ppm1d-h2afx 1240536 h2ax_human 1240538 unspecified role unspecified role prey prey ppm1d_human 1240539 unspecified role unspecified role bait bait physical association physical association false false false f2d homomint mint h2afx-ppm1d-4 1240536 h2ax_human 1240538 unspecified role unspecified role bait bait ppm1d_human 1240539 unspecified role unspecified role prey prey physical association physical association false false false f2d homomint mint h2afx-ppm1d 1240537 h2ax_human H2A.x 1240538 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 binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false Resulting Phenotypic qualities (properties)[PATO]: PATO:0002263 (dephosphorylated) ppm1d_human WIP1 1240539 enzyme enzyme neutral component neutral component dephosphorylation dephosphorylation reaction dephosphorylation false false false f1 homomint mint