DUSP10

Dual specificity protein phosphatase 10 is an enzyme that in humans is encoded by the DUSP10 gene.[4][5][6]

DUSP10
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesDUSP10, MKP-5, MKP5, dual specificity phosphatase 10
External IDsOMIM: 608867 MGI: 1927070 HomoloGene: 5215 GeneCards: DUSP10
Orthologs
SpeciesHumanMouse
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/aChr 1: 183.75 – 183.81 Mb
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

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


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