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 gregorieff-1998-1 Sequence requirements for association of protein-tyrosine phosphatase PEP with the Src homology 3 domain of inhibitory tyrosine protein kinase p50(csk). in vitro In vitro pull down pull down predetermined predetermined participant predetermined Gregorieff A., Cloutier JF., Veillette A. Phosphatases J. Biol. Chem. (0021-9258) 1998 partial coverage rapid curation ptn22_mouse Tyrosine-protein phosphatase non-receptor type 22 Ptpn22 Ptpn8 Hematopoietic cell protein-tyrosine phosphatase 70Z-PEP PEST-domain phosphatase protein protein mouse Mus musculus Mouse MDQREILQQLLKEAQKKKLNSEEFASEFLKLKRQSTKYKADKIYPTTVAQRPKNIKKNRYKDILPYDHSLVELSLLTSDEDSSYINASFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYRILVIVMACMEFEMGKKKCERYWAEPGETQLQFGPFSISCEAEKKKSDYKIRTLKAKFNNETRIIYQFHYKNWPDHDVPSSIDPILQLIWDMRCYQEDDCVPICIHCSAGCGRTGVICAVDYTWMLLKDGIIPKNFSVFNLIQEMRTQRPSLVQTQEQYELVYSAVLELFKRHMDVISDNHLGREIQAQCSIPEQSLTVEADSCPLDLPKNAMRDVKTTNQHSKQGAEAESTGGSSLGLRTSTMNAEEELVLHSAKSSPSFNCLELNCGCNNKAVITRNGQARASPVVGEPLQKYQSLDFGSMLFGSCPSALPINTADRYHNSKGPVKRTKSTPFELIQQRKTNDLAVGDGFSCLESQLHEHYSLRELQVQRVAHVSSEELNYSLPGACDASCVPRHSPGALRVHLYTSLAEDPYFSSSPPNSADSKMSFDLPEKQDGATSPGALLPASSTTSFFYSNPHDSLVMNTLTSFSPPLNQETAVEAPSRRTDDEIPPPLPERTPESFIVVEEAGEPSPRVTESLPLVVTFGASPECSGTSEMKSHDSVGFTPSKNVKLRSPKSDRHQDGSPPPPLPERTLESFFLADEDCIQAQAVQTSSTSYPETTENSTSSKQTLRTPGKSFTRSKSLKIFRNMKKSVCNSSSPSKPTERVQPKNSSSFLNFGFGNRFSKPKGPRNPPSAWNM mint homomint May be an effector and/or regulator of tyrosine-protein kinase CSK in T-cells and other hemopoietic cells csk_rat Tyrosine-protein kinase CSK Csk C-Src kinase protein protein rat Rattus norvegicus (Rat) Rat MSAIQASWPSGTECIAKYNFHGTAEQDLPFCKGDVLTIVAVTKDPNWYKAKNKVGREGIIPANYVQKREGVKAGTKLSLMPWFHGKITREQAERLLYPPETGLFLVRESTNYPGDYTLCVSCEGKVEHYRIMYHASKLSIDEEVYFENLMQLVEHYTTDADGLCTRLIKPKVMEGTVAAQDEFYRSGWALNMKELKLLQTIGKGEFGDVMLGDYRGNKVAVKCIKNDATAQAFLAEASVMTQLRHSNLVQLLGVIVEEKGGLYIVTEYMAKGSLVDYLRSRGRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEASSTQDTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPRVEKGYKMDAPDGCPPAVYDVMKNCWHLDAATRPTFLQLREQLEHIRTHELHL Specifically phosphorylates 'Tyr-504' on LCK, which acts as a negative regulatory site. Can also act on the LYN and FYN kinases mint homomint csk-ptpn22 5439 ptn22_mouse 5440 unspecified role unspecified role prey prey purified purified binding site binding region binding-associated region binding region alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain false PEP P1 Stoichiometry: 1.0 csk_rat 5441 unspecified role unspecified role bait bait purified purified binding site binding region binding-associated region binding region deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false Stoichiometry: 1.0 direct interaction direct interaction false false false The alanine scanning reveals the importance of the following residues in the sequence 613PPPLPERTPESFIV626: P614;L616;P617;R619, in the proline rich core of class 2, and T620;I625;V626 in the carboxy-terminal part. Mutation of these residues reduce binding by 10- and 5-fold in vitro.The L616;P617 are not required in vivo. Approximatively 25-50% of PEP is bound to Csk in hematopoietic cells. homomint mint