DUSP10

DUSP10
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1ZZW, 2OUC, 2OUD, 3TG1
Identifiers
Aliases	DUSP10 , MKP-5, MKP5, dual specificity phosphatase 10
External IDs	OMIM: 608867 MGI: 1927070 HomoloGene: 5215 GeneCards: DUSP10
Gene location (Mouse) Chr. Chromosome 1 (mouse) [1] Band 1|1 H5 Start 183,745,499 bp [1] End 183,807,833 bp [1]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in secondary oocyte stromal cell of endometrium right lobe of liver triceps brachii muscle vastus lateralis muscle retinal pigment epithelium body of pancreas deltoid muscle monocyte amniotic fluid Top expressed in temporal muscle triceps brachii muscle sternocleidomastoid muscle skeletal muscle tissue thymus masseter muscle digastric muscle soleus muscle tibialis anterior muscle vastus lateralis muscle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function phosphatase activity protein tyrosine phosphatase activity MAP kinase tyrosine/serine/threonine phosphatase activity hydrolase activity protein tyrosine/serine/threonine phosphatase activity JUN kinase binding MAP kinase phosphatase activity mitogen-activated protein kinase p38 binding phosphoprotein phosphatase activity protein tyrosine/threonine phosphatase activity protein binding Cellular component Golgi apparatus nucleoplasm cytosol nuclear speck nucleus cytoplasm Biological process regulation of innate immune response regulation of adaptive immune response oligodendrocyte differentiation negative regulation of respiratory burst involved in inflammatory response response to organic substance response to lipopolysaccharide negative regulation of oligodendrocyte differentiation negative regulation of protein kinase activity by regulation of protein phosphorylation negative regulation of stress-activated MAPK cascade regulation of brown fat cell differentiation dephosphorylation positive regulation of regulatory T cell differentiation protein dephosphorylation negative regulation of epithelial cell migration negative regulation of cell migration peptidyl-threonine dephosphorylation negative regulation of JUN kinase activity negative regulation of JNK cascade negative regulation of epithelial cell proliferation negative regulation of ERK1 and ERK2 cascade negative regulation of p38MAPK cascade negative regulation of epithelium regeneration peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 11221 63953 Ensembl n/a ENSMUSG00000039384 UniProt Q9Y6W6 Q9ESS0 RefSeq (mRNA) NM_007207 NM_144728 NM_144729 NM_022019 RefSeq (protein) NP_009138 NP_071302 Location (UCSC) n/a Chr 1: 183.75 – 183.81 Mb PubMed search [2] [3]
Wikidata
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Dual specificity protein phosphatase 10 is an enzyme that in humans is encoded by the DUSP10 gene. ^{[4] [5] [6]}

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. ^[6]

Interactions

DUSP10 has been shown to interact with MAPK14 ^{[7] [8] [9]} and MAPK8. ^[4]

References

1. GRCm38: Ensembl release 89: ENSMUSG00000039384 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. Tanoue T, Moriguchi T, Nishida E (Aug 1999). "Molecular cloning and characterization of a novel dual specificity phosphatase, MKP-5". J Biol Chem. 274 (28): 19949–56. doi: 10.1074/jbc.274.28.19949 . PMID   10391943.
5. Theodosiou A, Smith A, Gillieron C, Arkinstall S, Ashworth A (Jan 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.
6. "Entrez Gene: DUSP10 dual specificity phosphatase 10".
7. Tanoue T, Moriguchi T, Nishida E (Jul 1999). "Molecular cloning and characterization of a novel dual specificity phosphatase, MKP-5". J. Biol. Chem. UNITED STATES. 274 (28): 19949–56. doi: 10.1074/jbc.274.28.19949 . ISSN   0021-9258. PMID   10391943.
8. Tanoue T, Yamamoto T, Maeda R, Nishida E (Jul 2001). "A Novel MAPK phosphatase MKP-7 acts preferentially on JNK/SAPK and p38 alpha and beta MAPKs". J. Biol. Chem. United States. 276 (28): 26629–39. doi: 10.1074/jbc.M101981200 . ISSN   0021-9258. PMID   11359773.
9. Tanoue T, Maeda R, Adachi M, Nishida E (Feb 2001). "Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions". EMBO J. England. 20 (3): 466–79. doi:10.1093/emboj/20.3.466. ISSN   0261-4189. PMC   133461 . PMID   11157753.

Further reading

• Martell KJ, Angelotti T, Ullrich A (1998). "The "VH1-like" dual-specificity protein tyrosine phosphatases". Mol. Cells. 8 (1): 2–11. doi: 10.1016/S1016-8478(23)13385-1 . PMID   9571625.
• 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.
• 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. PMC   2206639 . 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.
• 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.
• 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.
• 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. Bibcode:2006PNAS..103.5391N. doi: 10.1073/pnas.0507066103 . PMC   1459365 . PMID   16565220.
• 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.
• 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.
• 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. doi:10.1159/000015666. PMID   11060451. S2CID   30344543.