DUSP10

Dual specificity phosphatase 10
PDB rendering based on 1zzw.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1zzw​
Identifiers
Symbols	DUSP10 ; MKP-5; MKP5
External IDs	Template:OMIM5 Template:MGI HomoloGene: 5215
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Dual specificity phosphatase 10, also known as DUSP10, is a human gene.

Dual specificity protein phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the MAPK superfamily (MAPK/ERK, SAPK/JNK, p38), which is associated with cellular proliferation and differentiation. Different members of this family of dual specificity phosphatases show distinct substrate specificities for MAPKs, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli. This gene product binds to and inactivates p38 and SAPK/JNK, but not MAPK/ERK. Its subcellular localization is unique; it is evenly distributed in both the cytoplasm and the nucleus. This gene is widely expressed in various tissues and organs, and its expression is elevated by stress stimuli. Three transcript variants encoding two different isoforms have been found for this gene.

Further reading

• Martell KJ, Angelotti T, Ullrich A (1998). "The "VH1-like" dual-specificity protein tyrosine phosphatases". Mol. Cells. 8 (1): 2–11. PMID 9571625.CS1 maint: Multiple names: authors list (link)
• Teng CH, Huang WN, Meng TC (2007). "Several dual specificity phosphatases coordinate to control the magnitude and duration of JNK activation in signaling response to oxidative stress". J. Biol. Chem. 282 (39): 28395–407. doi:10.1074/jbc.M705142200. PMID 17681939.CS1 maint: Multiple names: authors list (link)
• Tao X, Tong L (2007). "Crystal structure of the MAP kinase binding domain and the catalytic domain of human MKP5". Protein Sci. 16 (5): 880–6. doi:10.1110/ps.062712807. PMID 17400920.
• Nonn L, Duong D, Peehl DM (2007). "Chemopreventive anti-inflammatory activities of curcumin and other phytochemicals mediated by MAP kinase phosphatase-5 in prostate cells". Carcinogenesis. 28 (6): 1188–96. doi:10.1093/carcin/bgl241. PMID 17151092.CS1 maint: Multiple names: authors list (link)
• Jeong DG, Yoon TS, Kim JH; et al. (2006). "Crystal structure of the catalytic domain of human MAP kinase phosphatase 5: structural insight into constitutively active phosphatase". J. Mol. Biol. 360 (5): 946–55. doi:10.1016/j.jmb.2006.05.059. PMID 16806267.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Nousiainen M, Silljé HH, Sauer G; et al. (2006). "Phosphoproteome analysis of the human mitotic spindle". Proc. Natl. Acad. Sci. U.S.A. 103 (14): 5391–6. doi:10.1073/pnas.0507066103. PMID 16565220.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Tanoue T, Yamamoto T, Maeda R, Nishida E (2001). "A Novel MAPK phosphatase MKP-7 acts preferentially on JNK/SAPK and p38 alpha and beta MAPKs". J. Biol. Chem. 276 (28): 26629–39. doi:10.1074/jbc.M101981200. PMID 11359773.CS1 maint: Multiple names: authors list (link)
• Masuda K, Shima H, Kikuchi K; et al. (2000). "Expression and comparative chromosomal mapping of MKP-5 genes DUSP10/Dusp10". Cytogenet. Cell Genet. 90 (1–2): 71–4. PMID 11060451.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Theodosiou A, Smith A, Gillieron C; et al. (2000). "MKP5, a new member of the MAP kinase phosphatase family, which selectively dephosphorylates stress-activated kinases". Oncogene. 18 (50): 6981–8. doi:10.1038/sj.onc.1203185. PMID 10597297.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Tanoue T, Moriguchi T, Nishida E (1999). "Molecular cloning and characterization of a novel dual specificity phosphatase, MKP-5". J. Biol. Chem. 274 (28): 19949–56. PMID 10391943.CS1 maint: Multiple names: authors list (link)