DUSP6

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DUSP6
Protein DUSP6 PDB 1hzm.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases DUSP6, HH19, MKP3, PYST1, dual specificity phosphatase 6
External IDs MGI: 1914853 HomoloGene: 55621 GeneCards: 1848
RNA expression pattern
PBB GE DUSP6 208891 at tn.png

PBB GE DUSP6 208892 s at tn.png

PBB GE DUSP6 208893 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_022652
NM_001946

NM_026268

RefSeq (protein)

NP_001937.2
NP_073143.2

NP_080544.1

Location (UCSC) Chr 12: 89.35 – 89.35 Mb Chr 10: 99.26 – 99.27 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

Dual specificity phosphatase 6, also known as DUSP6, is an enzyme that in humans is encoded by the DUSP6 gene.[1][2][3]

Function[edit]

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 are 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 inactivates ERK2, is expressed in a variety of tissues with the highest levels in heart and pancreas and, unlike most other members of this family, is localized in the cytoplasm. Two transcript variants encoding different isoforms have been found for this gene.[1] Upregulation of spinal MKP-3 has been shown to alleviate chronic postoperative pain.[4]

Interactions[edit]

DUSP6 has been shown to interact with MAPK3.[5]

References[edit]

  1. ^ a b "Entrez Gene: DUSP6 dual specificity phosphatase 6". 
  2. ^ Muda M, Boschert U, Dickinson R, Martinou JC, Martinou I, Camps M, Schlegel W, Arkinstall S (Feb 1996). "MKP-3, a novel cytosolic protein-tyrosine phosphatase that exemplifies a new class of mitogen-activated protein kinase phosphatase". The Journal of Biological Chemistry 271 (8): 4319–26. doi:10.1074/jbc.271.8.4319. PMID 8626780. 
  3. ^ Smith A, Price C, Cullen M, Muda M, King A, Ozanne B, Arkinstall S, Ashworth A (Jun 1997). "Chromosomal localization of three human dual specificity phosphatase genes (DUSP4, DUSP6, and DUSP7)". Genomics 42 (3): 524–7. doi:10.1006/geno.1997.4756. PMID 9205128. 
  4. ^ Saha M, Skopelja S, Martinez E, Alvarez DL, Liponis BS, Romero-Sandoval EA (Oct 2013). "Spinal mitogen-activated protein kinase phosphatase-3 (MKP-3) is necessary for the normal resolution of mechanical allodynia in a mouse model of acute postoperative pain". The Journal of Neuroscience 33 (43): 17182–7. doi:10.1523/JNEUROSCI.5605-12.2013. PMID 24155322. 
  5. ^ Muda M, Theodosiou A, Gillieron C, Smith A, Chabert C, Camps M, Boschert U, Rodrigues N, Davies K, Ashworth A, Arkinstall S (Apr 1998). "The mitogen-activated protein kinase phosphatase-3 N-terminal noncatalytic region is responsible for tight substrate binding and enzymatic specificity". The Journal of Biological Chemistry 273 (15): 9323–9. doi:10.1074/jbc.273.15.9323. PMID 9535927. 

Further reading[edit]