DUSP5

Dual specificity phosphatase 5

PDB rendering based on 2g6z.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols DUSP5 ; DUSP; HVH3
External IDs OMIM: 603069 MGI: 2685183 HomoloGene: 3256 ChEMBL: 1250380 GeneCards: DUSP5 Gene
EC number 3.1.3.16, 3.1.3.48
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 1847 240672
Ensembl ENSG00000138166 ENSMUSG00000034765
UniProt Q16690 Q1HL35
RefSeq (mRNA) NM_004419 NM_001085390
RefSeq (protein) NP_004410 NP_001078859
Location (UCSC) Chr 10:
110.5 – 110.51 Mb
Chr 19:
53.53 – 53.54 Mb
PubMed search

Dual specificity protein phosphatase 5 is an enzyme that in humans is encoded by the DUSP5 gene.[1][2]

Function

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 ERK1/2, is expressed in a variety of tissues with the highest levels in pancreas and brain, and is localized in the nucleus.[2]

Model organisms

Model organisms have been used in the study of DUSP5 function. A conditional knockout mouse line called Dusp5tm1a(KOMP)Wtsi was generated at the Wellcome Trust Sanger Institute.[3] Male and female animals underwent a standardized phenotypic screen[4] to determine the effects of deletion.[5][6][7][8] Additional screens performed: - In-depth immunological phenotyping[9]

References

  1. Martell KJ, Kwak S, Hakes DJ, Dixon JE, Trent JM (Jul 1994). "Chromosomal localization of four human VH1-like protein-tyrosine phosphatases". Genomics 22 (2): 462–4. doi:10.1006/geno.1994.1411. PMID 7806236.
  2. 1 2 "Entrez Gene: DUSP5 dual specificity phosphatase 5".
  3. Gerdin AK (2010). "The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice". Acta Ophthalmologica 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
  4. 1 2 "International Mouse Phenotyping Consortium".
  5. Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (Jun 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
  6. Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  7. Collins FS, Rossant J, Wurst W (Jan 2007). "A mouse for all reasons". Cell 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
  8. White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN, Salisbury J, Clare S, Ingham NJ, Podrini C, Houghton R, Estabel J, Bottomley JR, Melvin DG, Sunter D, Adams NC, Tannahill D, Logan DW, Macarthur DG, Flint J, Mahajan VB, Tsang SH, Smyth I, Watt FM, Skarnes WC, Dougan G, Adams DJ, Ramirez-Solis R, Bradley A, Steel KP (Jul 2013). "Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes". Cell 154 (2): 452–64. doi:10.1016/j.cell.2013.06.022. PMC 3717207. PMID 23870131.
  9. 1 2 "Infection and Immunity Immunophenotyping (3i) Consortium".

Further reading


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