DUSP12

DUSP12
Identifiers
Aliases	DUSP12, DUSP1, YVH1, dual specificity phosphatase 12
External IDs	OMIM: 604835; MGI: 1890614; GeneCards: DUSP12
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4JNB, 4KI9
Enzyme activity EC # BRENDA ExPASy KEGG MetaCyc 3.1.3.16 ↗ ↗ ↗ ↗ 3.1.3.48 ↗ ↗ ↗ ↗
Gene location (Human) Chr. Chromosome 1 (human) Band 1q23.3 Start 161,749,758 bp End 161,757,238 bp
Gene location (Mouse) Chr. Chromosome 1 (mouse) Band 1|1 H3 Start 170,873,498 bp End 170,885,540 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in oocyte cerebellar hemisphere right hemisphere of cerebellum granulocyte embryo cerebellar vermis ganglionic eminence body of uterus left ovary gonad Top expressed in primary oocyte zygote embryo secondary oocyte embryo neural layer of retina morula morula neural tube epiblast More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein tyrosine phosphatase activity protein binding phosphoprotein phosphatase activity hydrolase activity protein tyrosine/serine/threonine phosphatase activity metal ion binding zinc ion binding phosphatase activity nucleic acid binding kinase binding Cellular component cytosol nucleus cytoplasm Biological process protein dephosphorylation positive regulation of glucokinase activity peptidyl-tyrosine dephosphorylation dephosphorylation Sources:Amigo / QuickGO
Orthologs Databases NCBI: entry; OMA: entry Species Human Mouse Entrez 11266 80915 Ensembl ENSG00000081721 ENSMUSG00000026659 UniProt Q9UNI6 Q9D0T2 RefSeq (mRNA) NM_007240 NM_023173 RefSeq (protein) NP_009171 NP_075662 NP_001343414 NP_001343415 Location (UCSC) Chr 1: 161.75 – 161.76 Mb Chr 1: 170.87 – 170.89 Mb PubMed search
Wikidata
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Dual specificity protein phosphatase 12 is an enzyme that in humans is encoded by the DUSP12 gene.

The protein encoded by this gene is a member of the dual specificity protein phosphatase subfamily. These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the mitogen-activated protein (MAP) kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which is associated with cellular proliferation and differentiation.

Different members of the family of dual specificity phosphatases show distinct substrate specificities for various MAP kinases, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli.

This gene product is the human ortholog of the Saccharomyces cerevisiae YVH1 protein tyrosine phosphatase. It is localized predominantly in the nucleus, and is novel in that it contains, and is regulated by a zinc finger domain.

Further reading

• Hasstedt SJ, Chu WS, Das SK, et al. (2008). "Type 2 diabetes susceptibility genes on chromosome 1q21-24". Ann. Hum. Genet. 72 (Pt 2): 163–9. doi:10.1111/j.1469-1809.2007.00416.x. PMID 18269685. S2CID 272577.
• Das SK, Chu WS, Hale TC, et al. (2006). "Polymorphisms in the glucokinase-associated, dual-specificity phosphatase 12 (DUSP12) gene under chromosome 1q21 linkage peak are associated with type 2 diabetes". Diabetes. 55 (9): 2631–9. doi:10.2337/db05-1369. PMID 16936214. S2CID 24401721.
• Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. Bibcode:2006Natur.441..315G. doi:10.1038/nature04727. PMID 16710414.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Groom LA, Sneddon AA, Alessi DR, et al. (1996). "Differential regulation of the MAP, SAP and RK/p38 kinases by Pyst1, a novel cytosolic dual-specificity phosphatase". EMBO J. 15 (14): 3621–32. doi:10.1002/j.1460-2075.1996.tb00731.x. PMC 451978. PMID 8670865.

External links

• Overview of all the structural information available in the PDB for UniProt: Q9UNI6 (Dual specificity protein phosphatase 12) at the PDBe-KB.