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 anonymous-2014u-1 Regulation of the Catalytic Activity of the Human Phosphatase PTPN4 by Its PDZ Domain in vitro In vitro enzymatic study enzymatic study predetermined predetermined participant predetermined nicolas.wolff@pasteur.fr imex curation Maisonneuve P., Caillet-Saguy C., Raynal B., Gilquin B., Chaffotte A., Pérez J., Zinn-Justin S., Delepierre M., Buc H., Cordier F., Wolff N. FEBS J. (1742-464X) 2014 Only protein-protein interactions mk12_human Mitogen-activated protein kinase 12 Extracellular signal-regulated kinase 6 Stress-activated protein kinase 3 Mitogen-activated protein kinase p38 gamma MAPK12 ERK6 SAPK3 protein protein human Homo sapiens Human MSSPPPARSGFYRQEVTKTAWEVRAVYRDLQPVGSGAYGAVCSAVDGRTGAKVAIKKLYRPFQSELFAKRAYRELRLLKHMRHENVIGLLDVFTPDETLDDFTDFYLVMPFMGTDLGKLMKHEKLGEDRIQFLVYQMLKGLRYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQADSEMTGYVVTRWYRAPEVILNWMRYTQTVDIWSVGCIMAEMITGKTLFKGSDHLDQLKEIMKVTGTPPAEFVQRLQSDEAKNYMKGLPELEKKDFASILTNASPLAVNLLEKMLVLDAEQRVTAGEALAHPYFESLHDTEDEPQVQKYDDSFDDVDRTLDEWKRVTYKEVLSFKPPRQLGARVSKETPL ptn4_human Tyrosine-protein phosphatase non-receptor type 4 Protein-tyrosine phosphatase MEG1 PTPN4 protein protein human Homo sapiens Human MTSRFRLPAGRTYNVRASELARDRQHTEVVCNILLLDNTVQAFKVNKHDQGQVLLDVVFKHLDLTEQDYFGLQLADDSTDNPRWLDPNKPIRKQLKRGSPYSLNFRVKFFVSDPNKLQEEYTRYQYFLQIKQDILTGRLPCPSNTAALLASFAVQSELGDYDQSENLSGYLSDYSFIPNQPQDFEKEIAKLHQQHIGLSPAEAEFNYLNTARTLELYGVEFHYARDQSNNEIMIGVMSGGILIYKNRVRMNTFPWLKIVKISFKCKQFFIQLRKELHESRETLLGFNMVNYRACKNLWKACVEHHTFFRLDRPLPPQKNFFAHYFTLGSKFRYCGRTEVQSVQYGKEKANKDRVFARSPSKPLARKLMDWEVVSRNSISDDRLETQSLPSRSPPGTPNHRNSTFTQEGTRLRPSSVGHLVDHMVHTSPSEVFVNQRSPSSTQANSIVLESSPSQETPGDGKPPALPPKQSKKNSWNQIHYSHSQQDLESHINETFDIPSSPEKPTPNGGIPHDNLVLIRMKPDENGRFGFNVKGGYDQKMPVIVSRVAPGTPADLCVPRLNEGDQVVLINGRDIAEHTHDQVVLFIKASCERHSGELMLLVRPNAVYDVVEEKLENEPDFQYIPEKAPLDSVHQDDHSLRESMIQLAEGLITGTVLTQFDQLYRKKPGMTMSCAKLPQNISKNRYRDISPYDATRVILKGNEDYINANYINMEIPSSSIINQYIACQGPLPHTCTDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPTGSSSYGCYQVTCHSEEGNTAYIFRKMTLFNQEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCHVRNKRAGKEEPVVVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYEEGFVKPLTTSTNK mapk12-ptpn4 1562624 n/a pTyr peptide 1562625 peptide synthesis peptide synthesis enzyme target enzyme target substrate substrate neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false n/a PTPN4_linker-PTP 1562626 predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified gst tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false dephosphorylation dephosphorylation reaction dephosphorylation false false false 1562624 f1b t1 Both linker-PTP and PDZ-PTPWT dephosphorylated the pTyr substrate following Michaelis-Menten kinetics (Fig. 1B). The Michaelis constant (KM) and the turnover number (kcat) values were deduced by fitting the experimental data to the Michaelis-Menten equation (Table 1). The kcat and KM values decreased by 6.5 fold and by 3.8 fold, respectively, when comparing linker-PTP and PDZ-PTPWT. The compensatory effects between kcat and KM explain the small change in the kcat/KM ratio of 1.7 fold (Table 1). mapk12-ptpn4-1 1562624 n/a PTPN4_PDZ-PTP 1562626 predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified gst tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false n/a pTyr peptide 1562625 peptide synthesis peptide synthesis enzyme target enzyme target substrate substrate neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false dephosphorylation dephosphorylation reaction dephosphorylation false false false 1562624 f1b t1 Both linker-PTP and PDZ-PTPWT dephosphorylated the pTyr substrate following Michaelis-Menten kinetics (Fig. 1B). The Michaelis constant (KM) and the turnover number (kcat) values were deduced by fitting the experimental data to the Michaelis-Menten equation (Table 1). The kcat and KM values decreased by 6.5 fold and by 3.8 fold, respectively, when comparing linker-PTP and PDZ-PTPWT. The compensatory effects between kcat and KM explain the small change in the kcat/KM ratio of 1.7 fold (Table 1).