ID:DUS1_HUMAN DESCRIPTION: RecName: Full=Dual specificity protein phosphatase 1; EC=3.1.3.16; EC=3.1.3.48; AltName: Full=Dual specificity protein phosphatase hVH1; AltName: Full=Mitogen-activated protein kinase phosphatase 1; Short=MAP kinase phosphatase 1; Short=MKP-1; AltName: Full=Protein-tyrosine phosphatase CL100; FUNCTION: Dual specificity phosphatase that dephosphorylates MAP kinase MAPK1/ERK2 on both 'Thr-183' and 'Tyr-185'. CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate. CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein + phosphate. INTERACTION: P28482:MAPK1; NbExp=3; IntAct=EBI-975493, EBI-959949; Q13309:SKP2; NbExp=3; IntAct=EBI-975493, EBI-456291; P0CG47:UBB; NbExp=2; IntAct=EBI-975493, EBI-413034; TISSUE SPECIFICITY: Expressed at high levels in the lung, liver placenta and pancreas. Moderate levels seen in the heart and skeletal muscle. Lower levels found in the brain and kidney. INDUCTION: By oxidative stress and heat shock. PTM: Phosphorylation at Ser-359 and Ser-364 by MAPK1/ERK2 and MAPK3/ERK1 reduces its rate of degradation (By similarity). SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily. SIMILARITY: Contains 1 rhodanese domain. SIMILARITY: Contains 1 tyrosine-protein phosphatase domain. WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/dusp1/";
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
SCOP Domains: 52799 - (Phosphotyrosine protein) phosphatases II 52821 - Rhodanese/Cell cycle control phosphatase
ModBase Predicted Comparative 3D Structure on P28562
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Gene Ontology (GO) Annotations with Structured Vocabulary
Molecular Function: GO:0004721 phosphoprotein phosphatase activity GO:0004725 protein tyrosine phosphatase activity GO:0004726 non-membrane spanning protein tyrosine phosphatase activity GO:0005515 protein binding GO:0008138 protein tyrosine/serine/threonine phosphatase activity GO:0008330 protein tyrosine/threonine phosphatase activity GO:0016787 hydrolase activity GO:0016791 phosphatase activity GO:0017017 MAP kinase tyrosine/serine/threonine phosphatase activity GO:0019838 growth factor binding
Biological Process: GO:0000188 inactivation of MAPK activity GO:0001706 endoderm formation GO:0006470 protein dephosphorylation GO:0006979 response to oxidative stress GO:0007049 cell cycle GO:0008285 negative regulation of cell proliferation GO:0009416 response to light stimulus GO:0010033 response to organic substance GO:0016311 dephosphorylation GO:0032355 response to estradiol GO:0032526 response to retinoic acid GO:0032870 cellular response to hormone stimulus GO:0033574 response to testosterone GO:0035335 peptidyl-tyrosine dephosphorylation GO:0035556 intracellular signal transduction GO:0035970 peptidyl-threonine dephosphorylation GO:0042542 response to hydrogen peroxide GO:0042981 regulation of apoptotic process GO:0043065 positive regulation of apoptotic process GO:0043066 negative regulation of apoptotic process GO:0043407 negative regulation of MAP kinase activity GO:0043409 negative regulation of MAPK cascade GO:0051384 response to glucocorticoid GO:0051447 negative regulation of meiotic cell cycle GO:0051591 response to cAMP GO:0051592 response to calcium ion GO:0070262 peptidyl-serine dephosphorylation GO:0070373 negative regulation of ERK1 and ERK2 cascade GO:0071850 mitotic cell cycle arrest GO:0090266 regulation of mitotic cell cycle spindle assembly checkpoint GO:2000279 negative regulation of DNA biosynthetic process