DUSP7

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

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; OMA:DUSP7 - orthologs
Gene location (Human) Chr. Chromosome 3 (human) Band 3p21.2 Start 52,048,919 bp End 52,056,571 bp
Gene location (Mouse) Chr. Chromosome 9 (mouse) Band 9|9 F1 Start 106,245,831 bp End 106,252,923 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in oocyte gingival epithelium human penis nipple skin of thigh mucosa of pharynx vulva secondary oocyte cervix epithelium skin of abdomen Top expressed in zygote secondary oocyte genital tubercle primary oocyte tail of embryo lip lacrimal gland neural layer of retina visual cortex primary visual cortex More reference expression data BioGPS More reference expression data
Gene ontology Molecular function phosphoprotein phosphatase activity phosphatase activity 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 negative regulation of MAP kinase activity peptidyl-tyrosine dephosphorylation dephosphorylation 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: 106.25 – 106.25 Mb PubMed search
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.

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.

Further reading

• Groom LA, Sneddon AA, Alessi DR, Dowd S, Keyse SM (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. doi:10.1242/jcs.111.22.3389. PMID 9788880.
• Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD (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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Pasquali C, Curchod ML, Wälchli S, Espanel X, Guerrier M, Arigoni F, Strous G, Hooft Van Huijsduijnen R (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, Hantisteanu S, Burg T, Raanani P, Avigdor A, Ben-Bassat I, Witz IP (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, Avigdor A, Ben-Bassat I, Witz IP (2004). "CDNA Microarray Analysis Reveals an Overexpression of the Dual-Specificity MAPK Phosphatase PYST2 in Acute Leukemia". Protein Phosphatases. Methods in Enzymology. Vol. 366. pp. 103–13. doi:10.1016/S0076-6879(03)66009-X. ISBN 978-0-12-182269-9. PMID 14674243.
• Orlev LN, Ehud B, Tamar BG, Orit SA, Yoel K, Witz IP (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, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R (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.