DUSP2

DUSP2

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1M3G

Identifiers

DUSP2, PAC-1, PAC1, dual specificity phosphatase 2

External IDs

OMIM: 603068; MGI: 101911; HomoloGene: 3255; GeneCards: DUSP2; OMA:DUSP2 - orthologs

Gene location (Human)

Chr.	Chromosome 2 (human)^[1]

Band	2q11.2	Start	96,143,169 bp^[1]
Band	2q11.2	End	96,145,440 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 2 (mouse)^[2]

Band	2\|2 F1	Start	127,178,079 bp^[2]
Band	2\|2 F1	End	127,180,296 bp^[2]

RNA expression pattern

Human

Mouse (ortholog)

Top expressed in

seminal vesicula

granulocyte

lymph node

mucosa of urinary bladder

monocyte

spleen

testicle

gallbladder

bone marrow cells

appendix

Top expressed in

mesenteric lymph nodes

thymus

spleen

trachea

blood

granulocyte

embryo

lip

tibiofemoral joint

bone marrow

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

Species

Human

Mouse


1844


13537


ENSG00000158050


ENSMUSG00000027368


Q05923


Q05922

RefSeq (mRNA)


NM_004418


NM_010090

RefSeq (protein)


NP_004409


NP_034220

Location (UCSC)

Chr 2: 96.14 – 96.15 Mb

Chr 2: 127.18 – 127.18 Mb

PubMed search

^[3]

^[4]

View/Edit Human

View/Edit Mouse

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]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000158050 – Ensembl, May 2017
^ ^a ^b ^c 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.
^ ^a ^b "Entrez Gene: DUSP2 dual specificity phosphatase 2".

Further reading

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.

v t e PDB gallery
1m3g: SOLUTION STRUCTURE OF THE CATALYTIC DOMAIN OF MAPK PHOSPHATASE PAC-1: INSIGHTS INTO SUBSTRATE-INDUCED ENZYMATIC ACTIVATION

Esterase: protein tyrosine phosphatases (EC 3.1.3.48)

Classical PTPs

Receptor type PTPs	PTPRA PTPRB PTPRC PTPRD PTPRE PTPRF PTPRG PTPRH PTPRJ PTPRK PTPRM PTPRN PTPRN2 PTPRO PTPRQ PTPRR PTPRS PTPRT PTPRU PTPRZ1 PTPRZ2
Non receptor type PTPs	PTPN1 PTPN2 PTPN3 PTPN4 PTPN5 PTPN6 PTPN7 PTPN9 PTPN11 PTPN12 PTPN13 PTPN14 PTPN18 PTPN20 PTPN21 PTPN22 PTPN23

VH1-like or
dual specific
phosphatases
(DSPs)

MAPK phosphatases (MKPs)	DUSP1 DUSP2 DUSP4 DUSP5 DUSP6 DUSP7 DUSP8 DUSP9 DUSP10 DUSP16 MK-STYX
Slingshots	SSH1 SSH2 SSH3
PRLs	PTP4A1 PTP4A2 PTP4A3
CDC14s	CDC14A CDC14B CDKN3 PTP9Q22
Atypical DSPs	DUSP3 DUSP11 DUSP12 DUSP13A DUSP13B DUSP14 DUSP15 DUSP18 DUSP19 DUSP21 DUSP22 DUSP23 DUSP24 DUSP25 DUSP26 DUSP27 EMP2A RNGTT STYX
Phosphatase and tensin homologs (PTENs)	PTEN TPIP TPTE TNS TENC1
Myotubularins	MTM1 MTMR2 MTMR3 MTMR4 MTMR5 MTMR6 MTMR7 MTMR8 MTMR9 MTMR10 MTMR11 MTMR12 MTMR13 MTMR14 MTMR15

ACP1

Cdc25
- CDC25A
- CDC25B
- CDC25C

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