DUSP2

DUSP2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1M3G
Identifiers
Aliases	DUSP2 , PAC-1, PAC1, dual specificity phosphatase 2
External IDs	OMIM: 603068 MGI: 101911 HomoloGene: 3255 GeneCards: DUSP2
Gene location (Human)
Chr.	Chromosome 2 (human)
End	96,145,440 bp
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)
End	127,180,296 bp
RNA expression pattern
	Top expressed in
	seminal vesicula; ; lymph node; ; mucosa of urinary bladder; ; monocyte; ; spleen; ; gallbladder; ; bone marrow cells; ; appendix; ; skin of abdomen; ; anterior pituitary;
	Top expressed in
	thymus; ; spleen; ; trachea; ; blood; ; lip; ; bone marrow; ; subcutaneous adipose tissue; ; endocardial cushion; ; atrium; ; hair follicle;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	protein tyrosine phosphatase activity ; phosphatase activity ; MAP kinase tyrosine/serine/threonine phosphatase activity ; protein tyrosine/threonine phosphatase activity ; protein binding ; phosphoprotein phosphatase activity ; hydrolase activity ; protein tyrosine/serine/threonine phosphatase activity ; mitogen-activated protein kinase binding ;
Cellular component	nucleus ; nuclear membrane ; cytoplasm ;
Biological process	protein dephosphorylation ; endoderm formation ; dephosphorylation ; peptidyl-tyrosine dephosphorylation ;
	Sources:Amigo / QuickGO
Orthologs
	1844
	13537
	ENSG00000158050
	ENSMUSG00000027368
	Q05923
	Q05922
	NM_004418
	NM_010090
	NP_004409
	NP_034220
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated April 16, 2023

Dual specificity protein phosphatase 2 is an enzyme that in humans is encoded by the DUSP2 gene.^[5]^[6]^[7]^[8]

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 and ERK2, is predominantly expressed in hematopoietic tissues, and is localized in the nucleus.^[8]

Related Research Articles

A mitogen-activated protein kinase is a type of protein kinase that is specific to the amino acids serine and threonine. MAPKs are involved in directing cellular responses to a diverse array of stimuli, such as mitogens, osmotic stress, heat shock and proinflammatory cytokines. They regulate cell functions including proliferation, gene expression, differentiation, mitosis, cell survival, and apoptosis.

The MAPK/ERK pathway is a chain of proteins in the cell that communicates a signal from a receptor on the surface of the cell to the DNA in the nucleus of the cell.

Mitogen-activated protein kinase 1, (MAPK 1), also known as ERK2, is an enzyme that in humans is encoded by the MAPK1 gene.

Mitogen-activated protein kinase 14, also called p38-α, is an enzyme that in humans is encoded by the MAPK14 gene.

Mitogen-activated protein kinase 3, also known as p44MAPK and ERK1, is an enzyme that in humans is encoded by the MAPK3 gene.

Mitogen-activated protein kinase 8 is a ubiquitous enzyme that in humans is encoded by the MAPK8 gene.

Dual specificity protein phosphatase 1 is an enzyme that in humans is encoded by the DUSP1 gene.

Dual specificity phosphatase 6 (DUSP6) is an enzyme that in humans is encoded by the DUSP6 gene.

Dual specificity protein phosphatase 3 is an enzyme that in humans is encoded by the DUSP3 gene.

<span class="mw-page-title-main">DUSP4</span> Protein-coding gene in the species Homo sapiens

Dual specificity protein phosphatase 4 is an enzyme that in humans is encoded by the DUSP4 gene.

Dual specificity protein phosphatase 10 is an enzyme that in humans is encoded by the DUSP10 gene.

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

Dual specificity protein phosphatase 16 is an enzyme that in humans is encoded by the DUSP16 gene.

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

Mitogen-activated protein kinase 4 is an enzyme that in humans is encoded by the MAPK4 gene.

Dual specificity protein phosphatase 12 is an enzyme that in humans is encoded by the DUSP12 gene.

Dual-specificity phosphatase is a form of phosphatase that can act upon tyrosine or serine/threonine residues.

MAPK phosphatases (MKPs) are the largest class of phosphatases involved in down-regulating Mitogen-activated protein kinases (MAPK) signaling. MAPK signalling pathways regulate multiple features of development and homeostasis. This can involve gene regulation, cell proliferation, programmed cell death and stress responses. MAPK phosphatases are therefore important regulator components of these pathways.

Candidalysin is a cytolytic 31-amino acid α-helical amphipathic peptide toxin secreted by the opportunistic pathogen Candida albicans. This toxin is a fungal example of a classical virulence factor. Hyphal morphogenesis in C. albicans is associated with damage to host epithelial cells; during this process Candidalysin is released and intercalates in host membranes. Candidalysin promotes damage of oral epithelial cells and induces lactate dehydrogenase release and calcium ion influx. It is unique in the fact that it is the first peptide toxin to be identified in any human fungal pathogen.

Dual specificity phosphatase 8 is a protein that in humans is encoded by the DUSP8 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000158050 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000027368 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Martell KJ, Kwak S, Hakes DJ, Dixon JE, Trent JM (Jan 1995). "Chromosomal localization of four human VH1-like protein-tyrosine phosphatases" (PDF). Genomics. 22 (2): 462–4. doi:10.1006/geno.1994.1411. hdl: 2027.42/31442 . PMID 7806236.
↑ Yi H, Morton CC, Weremowicz S, McBride OW, Kelly K (Dec 1995). "Genomic organization and chromosomal localization of the DUSP2 gene, encoding a MAP kinase phosphatase, to human 2p11.2-q11". Genomics. 28 (1): 92–6. doi:10.1006/geno.1995.1110. PMID 7590752.
↑ Yin Y, Liu YX, Jin YJ, Hall EJ, Barrett JC (Apr 2003). "PAC1 phosphatase is a transcription target of p53 in signalling apoptosis and growth suppression". Nature. 422 (6931): 527–31. Bibcode:2003Natur.422..527Y. doi:10.1038/nature01519. PMID 12673251. S2CID 4363302.
1 2 "Entrez Gene: DUSP2 dual specificity phosphatase 2".

Wu J, Jin YJ, Calaf GM, et al. (2007). "PAC1 is a direct transcription target of E2F-1 in apoptotic signaling". Oncogene. 26 (45): 6526–35. doi: 10.1038/sj.onc.1210484 . PMID 17471234.
Zhang Q, Muller M, Chen CH, et al. (2006). "New insights into the catalytic activation of the MAPK phosphatase PAC-1 induced by its substrate MAPK ERK2 binding". J. Mol. Biol. 354 (4): 777–88. doi:10.1016/j.jmb.2005.10.006. PMID 16288922.
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.
Kothapalli R, Yoder SJ, Kusmartseva I, Loughran TP (2004). "Characterization of a variant of PAC-1 in large granular lymphocyte leukemia". Protein Expr. Purif. 32 (1): 52–60. doi:10.1016/S1046-5928(03)00237-7. PMID 14680939.
Zhang Y, Guan DL, Xia CQ, et al. (2004). "Relationship between the expression levels of CD61, CD63, and PAC-1 on platelet surface in peripheral blood and the transplanted kidney function". Transplant. Proc. 35 (4): 1360–3. doi:10.1016/S0041-1345(03)00469-X. PMID 12826159.
Farooq A, Plotnikova O, Chaturvedi G, et al. (2003). "Solution structure of the MAPK phosphatase PAC-1 catalytic domain. Insights into substrate-induced enzymatic activation of MKP". Structure. 11 (2): 155–64. doi: 10.1016/S0969-2126(02)00943-7 . PMID 12575935.
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. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC 139241 . PMID 12477932.
Ward Y, Gupta S, Jensen P, et al. (1994). "Control of MAP kinase activation by the mitogen-induced threonine/tyrosine phosphatase PAC1". Nature. 367 (6464): 651–4. Bibcode:1994Natur.367..651W. doi:10.1038/367651a0. PMID 8107850. S2CID 4257340.
Rohan PJ, Davis P, Moskaluk CA, et al. (1993). "PAC-1: a mitogen-induced nuclear protein tyrosine phosphatase". Science. 259 (5102): 1763–6. Bibcode:1993Sci...259.1763R. doi:10.1126/science.7681221. PMID 7681221.
Raingeaud J, Gupta S, Rogers JS, et al. (1995). "Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine". J. Biol. Chem. 270 (13): 7420–6. doi: 10.1074/jbc.270.13.7420 . PMID 7535770.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000158050 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000027368 - 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.

[pmid7806236-5] Martell KJ, Kwak S, Hakes DJ, Dixon JE, Trent JM (Jan 1995). "Chromosomal localization of four human VH1-like protein-tyrosine phosphatases" (PDF). Genomics. 22 (2): 462–4. doi:10.1006/geno.1994.1411. hdl: 2027.42/31442 . PMID 7806236.

[pmid7590752-6] Yi H, Morton CC, Weremowicz S, McBride OW, Kelly K (Dec 1995). "Genomic organization and chromosomal localization of the DUSP2 gene, encoding a MAP kinase phosphatase, to human 2p11.2-q11". Genomics. 28 (1): 92–6. doi:10.1006/geno.1995.1110. PMID 7590752.

[pmid12673251-7] Yin Y, Liu YX, Jin YJ, Hall EJ, Barrett JC (Apr 2003). "PAC1 phosphatase is a transcription target of p53 in signalling apoptosis and growth suppression". Nature. 422 (6931): 527–31. Bibcode:2003Natur.422..527Y. doi:10.1038/nature01519. PMID 12673251. S2CID 4363302.

[entrez-8] 1 2 "Entrez Gene: DUSP2 dual specificity phosphatase 2".

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DUSP2

Related Research Articles

References

Further reading