DUSP7

Dual specificity protein phosphatase 7 is an enzyme that in humans is encoded by the DUSP7 gene.[5][6][7]

DUSP7
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4Y2E
Identifiers
Aliases	DUSP7, MKPX, PYST2, dual specificity phosphatase 7
External IDs	OMIM: 602749 MGI: 2387100 HomoloGene: 1468 GeneCards: DUSP7
Gene location (Human) Chr. Chromosome 3 (human)[1] Band 3p21.2 Start 52,048,919 bp[1] End 52,056,571 bp[1]
Gene location (Mouse) Chr. Chromosome 9 (mouse)[2] Band 9|9 F1 Start 106,368,632 bp[2] End 106,375,724 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • phosphoprotein phosphatase activity • phosphatase activity • GO:0001948 protein binding • MAP kinase tyrosine/serine/threonine phosphatase activity • hydrolase activity • protein tyrosine phosphatase activity • protein tyrosine/serine/threonine phosphatase activity Cellular component • cytoplasm • cytosol • nucleoplasm Biological process • protein dephosphorylation • MAPK cascade • activation of MAPK activity • negative regulation of MAP kinase activity • peptidyl-tyrosine dephosphorylation • dephosphorylation • inactivation of MAPK activity Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	1849	235584
Ensembl	ENSG00000164086	ENSMUSG00000053716
UniProt	Q16829	Q91Z46
RefSeq (mRNA)	NM_001947	NM_153459
RefSeq (protein)	NP_001938	NP_703189
Location (UCSC)	Chr 3: 52.05 – 52.06 Mb	Chr 9: 106.37 – 106.38 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

Dual-specificity phosphatases (DUSPs) constitute a large heterogeneous subgroup of the type I cysteine-based protein-tyrosine phosphatase superfamily. DUSPs are characterized by their ability to de-phosphorylate both tyrosine (EC 3.1.3.48) and serine / threonine (EC 3.1.3.16) residues. DUSP7 belongs to a class of DUSPs, designated MKPs, that dephosphorylate MAPK (mitogen-activated protein kinase) proteins ERK, JNK, and p38 with specificity distinct from that of individual MKP proteins. MKPs contain a highly conserved C-terminal catalytic domain and an N-terminal Cdc25-like (CH2) domain. MAPK activation cascades mediate various physiologic processes, including cellular proliferation, apoptosis, differentiation, and stress responses.[7][8]

It is known to bind and dephosphorylate ErkII, and as it, along with the other members of the DUSP family expresses high selectively for MAP kinases, it has been suggested that it functions as a method for selectively activating/deactivating different members of that family.[9]

References

1. GRCh38: Ensembl release 89: ENSG00000164086 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000053716 - 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. Muda M, Boschert U, Dickinson R, Martinou JC, Martinou I, Camps M, Schlegel W, Arkinstall S (Jun 1996). "MKP-3, a novel cytosolic protein-tyrosine phosphatase that exemplifies a new class of mitogen-activated protein kinase phosphatase". J Biol Chem. 271 (8): 4319–26. doi:10.1074/jbc.271.8.4319. PMID 8626780.
6. Smith A, Price C, Cullen M, Muda M, King A, Ozanne B, Arkinstall S, Ashworth A (Sep 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.
7. "Entrez Gene: DUSP7 dual specificity phosphatase 7".
8. Patterson KI, Brummer T, O'Brien PM, Daly RJ (March 2009). "Dual-specificity phosphatases: critical regulators with diverse cellular targets". Biochem. J. 418 (3): 475–89. doi:10.1042/bj20082234. PMID 19228121.
9. Dowd S, Sneddon AA, Keyse SM (November 1998). "Isolation of the human genes encoding the pyst1 and Pyst2 phosphatases: characterisation of Pyst2 as a cytosolic dual-specificity MAP kinase phosphatase and its catalytic activation by both MAP and SAP kinases". J. Cell Sci. 111 (22): 3389–99. PMID 9788880.

Further reading

• Groom LA, Sneddon AA, Alessi DR, et al. (1996). "Differential regulation of the MAP, SAP and RK/p38 kinases by Pyst1, a novel cytosolic dual-specificity phosphatase". EMBO J. 15 (14): 3621–32. doi:10.1002/j.1460-2075.1996.tb00731.x. PMC 451978. PMID 8670865.
• Dowd S, Sneddon AA, Keyse SM (1999). "Isolation of the human genes encoding the pyst1 and Pyst2 phosphatases: characterisation of Pyst2 as a cytosolic dual-specificity MAP kinase phosphatase and its catalytic activation by both MAP and SAP kinases". J. Cell Sci. 111 (22): 3389–99. PMID 9788880.
• 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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Pasquali C, Curchod ML, Wälchli S, et al. (2004). "Identification of protein tyrosine phosphatases with specificity for the ligand-activated growth hormone receptor". Mol. Endocrinol. 17 (11): 2228–39. doi:10.1210/me.2003-0011. PMID 12907755.
• Levy-Nissenbaum O, Sagi-Assif O, Kapon D, et al. (2003). "Dual-specificity phosphatase Pyst2-L is constitutively highly expressed in myeloid leukemia and other malignant cells". Oncogene. 22 (48): 7649–60. doi:10.1038/sj.onc.1206971. PMID 14576828.
• Levy-Nissenbaum O, Sagi-Assif O, Witz IP (2004). "Characterization of the dual-specificity phosphatase PYST2 and its transcripts". Genes Chromosomes Cancer. 39 (1): 37–47. doi:10.1002/gcc.10295. PMID 14603440. S2CID 11333674.
• Levy-Nissenbaum O, Sagi-Assif O, Raanani P, et al. (2004). "cDNA microarray analysis reveals an overexpression of the dual-specificity MAPK phosphatase PYST2 in acute leukemia". Meth. Enzymol. Methods in Enzymology. 366: 103–13. doi:10.1016/S0076-6879(03)66009-X. ISBN 978-0-12-182269-9. PMID 14674243.
• Orlev LN, Ehud B, Tamar BG, et al. (2004). "Does the dual-specificity MAPK phosphatase Pyst2-L lead a monogamous relationship with the Erk2 protein?". Immunol. Lett. 92 (1–2): 149–56. doi:10.1016/j.imlet.2003.11.024. PMID 15081539.
• 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.

External links

• PDBe-KB provides an overview of all the structure information available in the PDB for Human Dual specificity protein phosphatase 7 (DUSP7)

This article incorporates text from the United States National Library of Medicine, which is in the public domain.