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 A novel regulatory mechanism of MAP kinases activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphatase. A novel regulatory mechanism of MAP kinases activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphatase. J. Cell Biol. (0021-9525) 1999 Blanco-Aparicio C., Torres J., Pulido R. partial coverage rapid curation chlae Chlorocebus aethiops Cercopithecus aethiops Grivet Green monkey fluorescence imaging fluorescence microscopy fluorescence imaging predetermined predetermined participant predetermined Blanco-Aparicio C., Torres J., Pulido R. J. Cell Biol. (0021-9525) 1999 partial coverage rapid curation A novel regulatory mechanism of MAP kinases activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphatase. A novel regulatory mechanism of MAP kinases activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphatase. J. Cell Biol. (0021-9525) 1999 Blanco-Aparicio C., Torres J., Pulido R. partial coverage rapid curation in vitro In vitro phosphatase assay phosphatase assay predetermined predetermined participant predetermined Blanco-Aparicio C., Torres J., Pulido R. J. Cell Biol. (0021-9525) 1999 partial coverage rapid curation A novel regulatory mechanism of MAP kinases activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphatase. A novel regulatory mechanism of MAP kinases activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphatase. J. Cell Biol. (0021-9525) 1999 Blanco-Aparicio C., Torres J., Pulido R. partial coverage rapid curation human Homo sapiens Human pull down pull down predetermined predetermined participant predetermined Blanco-Aparicio C., Torres J., Pulido R. J. Cell Biol. (0021-9525) 1999 partial coverage rapid curation mk14_human Mitogen-activated protein kinase 14 Mitogen-activated protein kinase p38 alpha Cytokine suppressive anti-inflammatory drug-binding protein MAX-interacting protein 2 MAP kinase MXI2 SAPK2A MAPK14 CSBP CSBP1 CSBP2 CSPB1 MXI2 Stress-activated protein kinase 2a protein protein human Homo sapiens Human MSQERPTFYRQELNKTIWEVPERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLEEFNDVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGTPGAELLKKISSESARNYIQSLTQMPKMNFANVFIGANPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHDPDDEPVADPYDQSFESRDLLIDEWKSLTYDEVISFVPPPLDQEEMES 286C81D0487618B3 mk01_human Mitogen-activated protein kinase 1 MAPK1 ERK2 PRKM1 Extracellular signal-regulated kinase 2 Mitogen-activated protein kinase 2 MAP kinase isoform p42 ERT1 PRKM2 protein protein human Homo sapiens Human MAAAAAAGAGPEMVRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNVNKVRVAIKKISPFEHQTYCQRTLREIKILLRFRHENIIGINDIIRAPTIEQMKDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVADPDHDHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQYYDPSDEPIAEAPFKFDMELDDLPKEKLKELIFEETARFQPGYRS DIP protein P28482 original sequence version: 173 DIP protein P28482 original sequence version: 103 DIP protein P28482 original sequence version: 101 DIP protein P28482 original sequence version: 131 DIP protein P28482 original sequence version: 156 DIP protein P28482 original sequence version: 166 DIP protein P28482 original sequence version: 144 E85D0B2A5D2D724E ptprr_human Receptor-type tyrosine-protein phosphatase R PTPRR ECPTP PTPRQ Protein-tyrosine phosphatase PCPTP1 NC-PTPCOM1 Ch-1PTPase protein protein human Homo sapiens Human MRRAVCFPALCLLLNLHAAGCFSGNNDHFLAINQKKSGKPVFIYKHSQDIEKSLDIAPQKIYRHSYHSSSEAQVSKRHQIVNSAFPRPAYDPSLNLLAMDGQDLEVENLPIPAANVIVVTLQMDVNKLNITLLRIFRQGVAAALGLLPQQVHINRLIGKKNSIELFVSPINRKTGISDALPSEEVLRSLNINVLHQSLSQFGITEVSPEKNVLQGQHEADKIWSKEGFYAVVIFLSIFVIIVTCLMILYRLKERFQLSLRQDKEKNQEIHLSPITLQPALSEAKTVHSMVQPEQAPKVLNVVVDPQGRGAPEIKATTATSVCPSPFKMKPIGLQERRGSNVSLTLDMSSLGNIEPFVSIPTPREKVAMEYLQSASRILTRSQLRDVVASSHLLQSEFMEIPMNFVDPKEIDIPRHGTKNRYKTILPNPLSRVCLRPKNVTDSLSTYINANYIRGYSGKEKAFIATQGPMINTVDDFWQMVWQEDSPVIVMITKLKEKNEKCVLYWPEKRGIYGKVEVLVISVNECDNYTIRNLVLKQGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASQGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRMDRGGMVQTSEQYEFVHHALCLYESRLSAETVQ 42CD98F37AC5B638 ptprr-mapk14-1 3 PTPRR 6 unspecified role unspecified role bait bait over-expressed over expressed level over-expressed living cell living cell Q15256:p.Ser339Glu mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain S E Tue Jul 12 10:10:30 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation disrupting' Wed May 02 15:47:47 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser339glu' Tue Jun 30 19:27:33 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser339Glu' p38 4 unspecified role unspecified role prey prey living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level physical association physical association f2c homomint mint mapk1-ptprr-4 2 ERK2 5 enzyme target enzyme target substrate substrate neutral component neutral component Resulting Phenotypic qualities (properties)[PATO]: PATO:0002221 (increased phosphorylation) PTPRR 6 enzyme enzyme neutral component neutral component Q15256:p.Ser339Glu mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain S E Tue Jul 12 10:14:12 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation disrupting' Wed May 02 19:31:17 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser339glu' Tue Jun 30 18:19:53 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser339Glu' physical association physical association f2d homomint mint mapk14-ptprr 2 p38 4 enzyme target enzyme target substrate substrate neutral component neutral component Resulting Phenotypic qualities (properties)[PATO]: PATO:0002221 (increased phosphorylation) PTPRR 6 enzyme enzyme neutral component neutral component Q15256:p.Ser339Glu mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain S E Tue Jul 12 10:53:31 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation disrupting' Wed May 02 15:11:58 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser339glu' Tue Jun 30 16:02:47 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser339Glu' physical association physical association f2d homomint mint mapk1-ptprr-5 1 ERK2 5 unspecified role unspecified role neutral component neutral component PTPRR 6 unspecified role unspecified role neutral component neutral component colocalization colocalization f3 homomint mint mapk14-ptprr-1 1 PTPRR 6 unspecified role unspecified role neutral component neutral component p38 4 unspecified role unspecified role neutral component neutral component colocalization colocalization f3 homomint mint