DUSP12

Dual specificity phosphatase 12
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 4JNB​, 4KI9​
Identifiers
Symbols	DUSP12 ; DUSP1; YVH1
External IDs	OMIM: 604835 MGI: 1890614 HomoloGene: 5238 GeneCards: DUSP12 Gene
EC number	3.1.3.16, 3.1.3.48
Gene ontology Molecular function • protein tyrosine phosphatase activity • protein binding • protein tyrosine/serine/threonine phosphatase activity • zinc ion binding • kinase binding Cellular component • nucleus • cytoplasm Biological process • cellular protein modification process • positive regulation of glucokinase activity • peptidyl-tyrosine dephosphorylation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	11266	80915
Ensembl	ENSG00000081721	ENSMUSG00000026659
UniProt	Q9UNI6	Q9D0T2
RefSeq (mRNA)	NM_007240	NM_023173
RefSeq (protein)	NP_009171	NP_075662
Location (UCSC)	Chr 1: 161.75 – 161.76 Mb	Chr 1: 170.87 – 170.89 Mb
PubMed search

Dual specificity protein phosphatase 12 is an enzyme that in humans is encoded by the DUSP12 gene.^[1][2]

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.^[2]

References

1. Muda M, Manning ER, Orth K, Dixon JE (Sep 1999). "Identification of the human YVH1 protein-tyrosine phosphatase orthologue reveals a novel zinc binding domain essential for in vivo function". J Biol Chem 274 (34): 23991–5. doi:10.1074/jbc.274.34.23991. PMID 10446167.
2. "Entrez Gene: DUSP12 dual specificity phosphatase 12".

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.
• 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.
• Gregory SG, Barlow KF, McLay KE; et al. (2006). "The DNA sequence and biological annotation of human chromosome 1.". Nature 441 (7091): 315–21. 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. doi:10.1038/nature04209. PMID 16189514.
• 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. 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. PMC 451978. PMID 8670865.