DUSP12

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Dual specificity phosphatase 12
Identifiers
Symbol(s) DUSP12; DUSP1; YVH1
External IDs OMIM: 604835 MGI1890614 HomoloGene5238
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 11266 80915
Ensembl ENSG00000081721 ENSMUSG00000026659
Uniprot Q9UNI6 Q4KL39
Refseq NM_007240 (mRNA)
NP_009171 (protein)
NM_023173 (mRNA)
NP_075662 (protein)
Location Chr 1: 159.99 - 159.99 Mb Chr 1: 172.71 - 172.72 Mb
Pubmed search [1] [2]

Dual specificity phosphatase 12, also known as DUSP12, is a human gene.[1]

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.[1]

[edit] References

[edit] Further reading

  • Hasstedt SJ, Chu WS, Das SK, et al.. "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. 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. PMID 12477932. 
  • Muda M, Manning ER, Orth K, Dixon JE (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. PMID 10446167. 
  • 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. PMID 8670865.