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 Regulation of the Catalytic Activity of the Human Phosphatase PTPN4 by Its PDZ Domain. Regulation of the Catalytic Activity of the Human Phosphatase PTPN4 by Its PDZ Domain. FEBS J. (1742-464X) 2014 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. nicolas.wolff@pasteur.fr 18-Sep-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro enzymatic study enzymatic study predetermined predetermined participant predetermined nicolas.wolff@pasteur.fr Accepted 2014-JUL-28 by MARTA imex curation 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 DIP protein P53778 original sequence version: 169 EF680401D8E40610 ptn4_human Tyrosine-protein phosphatase non-receptor type 4 Protein-tyrosine phosphatase MEG1 PTPN4 protein protein human Homo sapiens Human MTSRFRLPAGRTYNVRASELARDRQHTEVVCNILLLDNTVQAFKVNKHDQGQVLLDVVFKHLDLTEQDYFGLQLADDSTDNPRWLDPNKPIRKQLKRGSPYSLNFRVKFFVSDPNKLQEEYTRYQYFLQIKQDILTGRLPCPSNTAALLASFAVQSELGDYDQSENLSGYLSDYSFIPNQPQDFEKEIAKLHQQHIGLSPAEAEFNYLNTARTLELYGVEFHYARDQSNNEIMIGVMSGGILIYKNRVRMNTFPWLKIVKISFKCKQFFIQLRKELHESRETLLGFNMVNYRACKNLWKACVEHHTFFRLDRPLPPQKNFFAHYFTLGSKFRYCGRTEVQSVQYGKEKANKDRVFARSPSKPLARKLMDWEVVSRNSISDDRLETQSLPSRSPPGTPNHRNSTFTQEGTRLRPSSVGHLVDHMVHTSPSEVFVNQRSPSSTQANSIVLESSPSQETPGDGKPPALPPKQSKKNSWNQIHYSHSQQDLESHINETFDIPSSPEKPTPNGGIPHDNLVLIRMKPDENGRFGFNVKGGYDQKMPVIVSRVAPGTPADLCVPRLNEGDQVVLINGRDIAEHTHDQVVLFIKASCERHSGELMLLVRPNAVYDVVEEKLENEPDFQYIPEKAPLDSVHQDDHSLRESMIQLAEGLITGTVLTQFDQLYRKKPGMTMSCAKLPQNISKNRYRDISPYDATRVILKGNEDYINANYINMEIPSSSIINQYIACQGPLPHTCTDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPTGSSSYGCYQVTCHSEEGNTAYIFRKMTLFNQEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCHVRNKRAGKEEPVVVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYEEGFVKPLTTSTNK DIP protein P29074 original sequence version: 116 4DAC6A87A675CFB0 mapk12-ptpn4 1 pTyr peptide 2 peptide synthesis peptide synthesis predetermined predetermined participant predetermined 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 PTPN4_linker-PTP 3 predetermined predetermined participant predetermined 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 range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain dephosphorylation dephosphorylation reaction dephosphorylation 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 1 PTPN4_PDZ-PTP 3 predetermined predetermined participant predetermined 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 range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain pTyr peptide 2 peptide synthesis peptide synthesis predetermined predetermined participant predetermined 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 dephosphorylation dephosphorylation reaction dephosphorylation 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).