DUSP5

DUSP5
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2G6Z
Identifiers
Aliases	DUSP5 , DUSP, HVH3, dual specificity phosphatase 5
External IDs	OMIM: 603069 MGI: 2685183 HomoloGene: 3256 GeneCards: DUSP5
Gene location (Human) Chr. Chromosome 10 (human) [1] Band 10q25.2 Start 110,497,907 bp [1] End 110,511,533 bp [1]
Gene location (Mouse) Chr. Chromosome 19 (mouse) [2] Band 19|19 D2 Start 53,517,540 bp [2] End 53,530,862 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in mucosa of urinary bladder gallbladder epithelium of esophagus islet of Langerhans secondary oocyte vena cava palpebral conjunctiva cavity of mouth cerebellar cortex cerebellar hemisphere Top expressed in cerebellar vermis parotid gland lacrimal gland islet of Langerhans thymus cumulus cell esophagus epithelium of stomach lip blood More reference expression data BioGPS More reference expression data
Gene ontology Molecular function phosphoprotein phosphatase activity protein binding protein tyrosine phosphatase activity MAP kinase tyrosine/serine/threonine phosphatase activity hydrolase activity phosphatase activity protein tyrosine/serine/threonine phosphatase activity Cellular component nucleoplasm nucleus cytoplasm Biological process protein dephosphorylation MAPK cascade endoderm formation peptidyl-tyrosine dephosphorylation dephosphorylation peptidyl-threonine dephosphorylation Sources:Amigo / QuickGO
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: 53.52 – 53.53 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Dual specificity protein phosphatase 5 is an enzyme that in humans is encoded by the DUSP5 gene. ^{[5] [6]}

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. ^[6]

References

1. GRCh38: Ensembl release 89: ENSG00000138166 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000034765 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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. hdl: 2027.42/31442 . PMID   7806236.
6. "Entrez Gene: DUSP5 dual specificity phosphatase 5".

Further reading

• Robertson NG, Khetarpal U, Gutiérrez-Espeleta GA, Bieber FR, Morton CC (Sep 1994). "Isolation of novel and known genes from a human fetal cochlear cDNA library using subtractive hybridization and differential screening". Genomics. 23 (1): 42–50. doi:10.1006/geno.1994.1457. PMID   7829101.
• Kwak SP, Dixon JE (Jan 1995). "Multiple dual specificity protein tyrosine phosphatases are expressed and regulated differentially in liver cell lines". The Journal of Biological Chemistry. 270 (3): 1156–60. doi: 10.1074/jbc.270.3.1156 . PMID   7836374.
• Ishibashi T, Bottaro DP, Michieli P, Kelley CA, Aaronson SA (Nov 1994). "A novel dual specificity phosphatase induced by serum stimulation and heat shock". The Journal of Biological Chemistry. 269 (47): 29897–902. doi: 10.1016/S0021-9258(18)43965-8 . PMID   7961985.
• Ueda K, Arakawa H, Nakamura Y (Aug 2003). "Dual-specificity phosphatase 5 (DUSP5) as a direct transcriptional target of tumor suppressor p53". Oncogene. 22 (36): 5586–91. doi: 10.1038/sj.onc.1206845 . PMID   12944906.
• Mandl M, Slack DN, Keyse SM (Mar 2005). "Specific inactivation and nuclear anchoring of extracellular signal-regulated kinase 2 by the inducible dual-specificity protein phosphatase DUSP5". Molecular and Cellular Biology. 25 (5): 1830–45. doi:10.1128/MCB.25.5.1830-1845.2005. PMC   549372 . PMID   15713638.
• Jeong DG, Cho YH, Yoon TS, Kim JH, Ryu SE, Kim SJ (Jan 2007). "Crystal structure of the catalytic domain of human DUSP5, a dual specificity MAP kinase protein phosphatase". Proteins. 66 (1): 253–8. doi: 10.1002/prot.21224 . PMID   17078075. S2CID   30285092.
• Sarközi R, Miller B, Pollack V, Feifel E, Mayer G, Sorokin A, Schramek H (Apr 2007). "ERK1/2-driven and MKP-mediated inhibition of EGF-induced ERK5 signaling in human proximal tubular cells". Journal of Cellular Physiology. 211 (1): 88–100. doi:10.1002/jcp.20909. PMID   17131384. S2CID   39397816.

External links

• Overview of all the structural information available in the PDB for UniProt : Q16690 (Dual specificity protein phosphatase 5) at the PDBe-KB .