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Wikipedia

DUSP3

Dual specificity protein phosphatase 3 is an enzyme that in humans is encoded by the DUSP3 gene.[5][6]

DUSP3
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesDUSP3, VHR, dual specificity phosphatase 3
External IDsOMIM: 600183 MGI: 1919599 HomoloGene: 20870 GeneCards: DUSP3
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_004090

NM_028207

RefSeq (protein)

NP_004081

NP_082483

Location (UCSC)Chr 17: 43.77 – 43.78 MbChr 11: 101.86 – 101.88 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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 maps in a region that contains the BRCA1 locus which confers susceptibility to breast and ovarian cancer. Although DUSP3 is expressed in both breast and ovarian tissues, mutation screening in breast cancer pedigrees and in sporadic tumors was negative, leading to the conclusion that this gene is not BRCA1.[6]

Interactions edit

DUSP3 has been shown to interact with MAPK3[7] and MAPK1.[7]

References edit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000108861 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000003518 - 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. ^ Folander K, Douglass J, Swanson R (Feb 1995). "Confirmation of the assignment of the gene encoding Kv1.3, a voltage-gated potassium channel (KCNA3) to the proximal short arm of human chromosome 1". Genomics. 23 (1): 295–6. doi:10.1006/geno.1994.1500. PMID 7829094.
  6. ^ a b "Entrez Gene: DUSP3 dual specificity phosphatase 3 (vaccinia virus phosphatase VH1-related)".
  7. ^ a b Todd, J L; Tanner K G; Denu J M (May 1999). "Extracellular regulated kinases (ERK) 1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR. A novel role in down-regulating the ERK pathway". J. Biol. Chem. 274 (19). UNITED STATES: 13271–80. doi:10.1074/jbc.274.19.13271. ISSN 0021-9258. PMID 10224087.

Further reading edit

  • Ishibashi T, Bottaro DP, Chan A, et al. (1993). "Expression cloning of a human dual-specificity phosphatase". Proc. Natl. Acad. Sci. U.S.A. 89 (24): 12170–4. Bibcode:1992PNAS...8912170I. doi:10.1073/pnas.89.24.12170. PMC 50720. PMID 1281549.
  • Kamb A, Futreal PA, Rosenthal J, et al. (1995). "Localization of the VHR phosphatase gene and its analysis as a candidate for BRCA1". Genomics. 23 (1): 163–7. doi:10.1006/geno.1994.1473. PMID 7829067.
  • Jones KA, Black DM, Brown MA, et al. (1995). "The detailed characterisation of a 400 kb cosmid walk in the BRCA1 region: identification and localisation of 10 genes including a dual-specificity phosphatase". Hum. Mol. Genet. 3 (11): 1927–34. doi:10.1093/hmg/3.11.1927. PMID 7874108.
  • Yuvaniyama J, Denu JM, Dixon JE, Saper MA (1996). "Crystal structure of the dual specificity protein phosphatase VHR". Science. 272 (5266): 1328–31. Bibcode:1996Sci...272.1328Y. doi:10.1126/science.272.5266.1328. PMID 8650541. S2CID 33816598.
  • Todd JL, Tanner KG, Denu JM (1999). "Extracellular regulated kinases (ERK) 1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR. A novel role in down-regulating the ERK pathway". J. Biol. Chem. 274 (19): 13271–80. doi:10.1074/jbc.274.19.13271. PMID 10224087.
  • Alonso A, Saxena M, Williams S, Mustelin T (2001). "Inhibitory role for dual specificity phosphatase VHR in T cell antigen receptor and CD28-induced Erk and Jnk activation". J. Biol. Chem. 276 (7): 4766–71. doi:10.1074/jbc.M006497200. PMID 11085983.
  • Najarro P, Traktman P, Lewis JA (2001). "Vaccinia virus blocks gamma interferon signal transduction: viral VH1 phosphatase reverses Stat1 activation". J. Virol. 75 (7): 3185–96. doi:10.1128/JVI.75.7.3185-3196.2001. PMC 114112. PMID 11238845.
  • Alonso A, Rahmouni S, Williams S, et al. (2003). "Tyrosine phosphorylation of VHR phosphatase by ZAP-70". Nat. Immunol. 4 (1): 44–8. doi:10.1038/ni856. PMID 12447358. S2CID 10205773.
  • 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.
  • Kim HS, Song MC, Kwak IH, et al. (2003). "Constitutive induction of p-Erk1/2 accompanied by reduced activities of protein phosphatases 1 and 2A and MKP3 due to reactive oxygen species during cellular senescence". J. Biol. Chem. 278 (39): 37497–510. doi:10.1074/jbc.M211739200. PMID 12840032. S2CID 7806506.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • 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.
  • Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  • Rahmouni S, Cerignoli F, Alonso A, et al. (2006). "Loss of the VHR dual-specific phosphatase causes cell-cycle arrest and senescence". Nat. Cell Biol. 8 (5): 524–31. doi:10.1038/ncb1398. PMID 16604064. S2CID 20976640.
  • Hao L, ElShamy WM (2007). "BRCA1-IRIS activates cyclin D1 expression in breast cancer cells by downregulating the JNK phosphatase DUSP3/VHR". Int. J. Cancer. 121 (1): 39–46. doi:10.1002/ijc.22597. PMID 17278098. S2CID 24555741.
  • Hoyt R, Zhu W, Cerignoli F, et al. (2007). "Cutting edge: selective tyrosine dephosphorylation of interferon-activated nuclear STAT5 by the VHR phosphatase". J. Immunol. 179 (6): 3402–6. doi:10.4049/jimmunol.179.6.3402. PMC 2770724. PMID 17785772.

dusp3, dual, specificity, protein, phosphatase, enzyme, that, humans, encoded, gene, available, structurespdbortholog, search, pdbe, rcsblist, codes1j4x, 1vhr, 3f81identifiersaliases, dual, specificity, phosphatase, 3external, idsomim, 600183, 1919599, homolog. Dual specificity protein phosphatase 3 is an enzyme that in humans is encoded by the DUSP3 gene 5 6 DUSP3Available structuresPDBOrtholog search PDBe RCSBList of PDB id codes1J4X 1VHR 3F81IdentifiersAliasesDUSP3 VHR dual specificity phosphatase 3External IDsOMIM 600183 MGI 1919599 HomoloGene 20870 GeneCards DUSP3Gene location Human Chr Chromosome 17 human 1 Band17q21 31Start43 766 125 bp 1 End43 778 977 bp 1 Gene location Mouse Chr Chromosome 11 mouse 2 Band11 11 DStart101 861 969 bp 2 End101 877 839 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed insaphenous veinvastus lateralis musclethoracic diaphragmgastrocnemius muscleright ventriclebody of tonguetriceps brachii muscledeltoid muscleright coronary arteryatriumTop expressed inascending aortaaortic valvesubstantia nigrasuperior frontal gyrusinterventricular septumskeletal muscle tissuevastus lateralis muscletriceps brachii musclesupraoptic nucleusspermatidMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionphosphoprotein phosphatase activity MAP kinase phosphatase activity hydrolase activity protein kinase binding protein tyrosine serine threonine phosphatase activity phosphatase activity protein tyrosine phosphatase activity cytoskeletal protein binding receptor tyrosine kinase binding protein tyrosine kinase bindingCellular componentcytosol nucleoplasm immunological synapse nucleusBiological processprotein dephosphorylation positive regulation of mitotic cell cycle negative regulation of T cell receptor signaling pathway negative regulation of JNK cascade negative regulation of MAPK cascade negative regulation of ERK1 and ERK2 cascade peptidyl tyrosine dephosphorylation negative regulation of T cell activation in utero embryonic development dephosphorylation negative regulation of cell migration negative regulation of epidermal growth factor receptor signaling pathway negative regulation of chemotaxis regulation of focal adhesion assembly cellular response to epidermal growth factor stimulus positive regulation of focal adhesion disassembly peptidyl tyrosine dephosphorylation involved in inactivation of protein kinase activitySources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez184572349EnsemblENSG00000108861ENSMUSG00000003518UniProtP51452Q9D7X3RefSeq mRNA NM 004090NM 028207RefSeq protein NP 004081NP 082483Location UCSC Chr 17 43 77 43 78 MbChr 11 101 86 101 88 MbPubMed search 3 4 WikidataView Edit HumanView Edit MouseThe 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 maps in a region that contains the BRCA1 locus which confers susceptibility to breast and ovarian cancer Although DUSP3 is expressed in both breast and ovarian tissues mutation screening in breast cancer pedigrees and in sporadic tumors was negative leading to the conclusion that this gene is not BRCA1 6 Interactions editDUSP3 has been shown to interact with MAPK3 7 and MAPK1 7 References edit a b c GRCh38 Ensembl release 89 ENSG00000108861 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000003518 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 Folander K Douglass J Swanson R Feb 1995 Confirmation of the assignment of the gene encoding Kv1 3 a voltage gated potassium channel KCNA3 to the proximal short arm of human chromosome 1 Genomics 23 1 295 6 doi 10 1006 geno 1994 1500 PMID 7829094 a b Entrez Gene DUSP3 dual specificity phosphatase 3 vaccinia virus phosphatase VH1 related a b Todd J L Tanner K G Denu J M May 1999 Extracellular regulated kinases ERK 1 and ERK2 are authentic substrates for the dual specificity protein tyrosine phosphatase VHR A novel role in down regulating the ERK pathway J Biol Chem 274 19 UNITED STATES 13271 80 doi 10 1074 jbc 274 19 13271 ISSN 0021 9258 PMID 10224087 Further reading editIshibashi T Bottaro DP Chan A et al 1993 Expression cloning of a human dual specificity phosphatase Proc Natl Acad Sci U S A 89 24 12170 4 Bibcode 1992PNAS 8912170I doi 10 1073 pnas 89 24 12170 PMC 50720 PMID 1281549 Kamb A Futreal PA Rosenthal J et al 1995 Localization of the VHR phosphatase gene and its analysis as a candidate for BRCA1 Genomics 23 1 163 7 doi 10 1006 geno 1994 1473 PMID 7829067 Jones KA Black DM Brown MA et al 1995 The detailed characterisation of a 400 kb cosmid walk in the BRCA1 region identification and localisation of 10 genes including a dual specificity phosphatase Hum Mol Genet 3 11 1927 34 doi 10 1093 hmg 3 11 1927 PMID 7874108 Yuvaniyama J Denu JM Dixon JE Saper MA 1996 Crystal structure of the dual specificity protein phosphatase VHR Science 272 5266 1328 31 Bibcode 1996Sci 272 1328Y doi 10 1126 science 272 5266 1328 PMID 8650541 S2CID 33816598 Todd JL Tanner KG Denu JM 1999 Extracellular regulated kinases ERK 1 and ERK2 are authentic substrates for the dual specificity protein tyrosine phosphatase VHR A novel role in down regulating the ERK pathway J Biol Chem 274 19 13271 80 doi 10 1074 jbc 274 19 13271 PMID 10224087 Alonso A Saxena M Williams S Mustelin T 2001 Inhibitory role for dual specificity phosphatase VHR in T cell antigen receptor and CD28 induced Erk and Jnk activation J Biol Chem 276 7 4766 71 doi 10 1074 jbc M006497200 PMID 11085983 Najarro P Traktman P Lewis JA 2001 Vaccinia virus blocks gamma interferon signal transduction viral VH1 phosphatase reverses Stat1 activation J Virol 75 7 3185 96 doi 10 1128 JVI 75 7 3185 3196 2001 PMC 114112 PMID 11238845 Alonso A Rahmouni S Williams S et al 2003 Tyrosine phosphorylation of VHR phosphatase by ZAP 70 Nat Immunol 4 1 44 8 doi 10 1038 ni856 PMID 12447358 S2CID 10205773 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 Kim HS Song MC Kwak IH et al 2003 Constitutive induction of p Erk1 2 accompanied by reduced activities of protein phosphatases 1 and 2A and MKP3 due to reactive oxygen species during cellular senescence J Biol Chem 278 39 37497 510 doi 10 1074 jbc M211739200 PMID 12840032 S2CID 7806506 Ota T Suzuki Y Nishikawa T et al 2004 Complete sequencing and characterization of 21 243 full length human cDNAs Nat Genet 36 1 40 5 doi 10 1038 ng1285 PMID 14702039 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 Rual JF Venkatesan K Hao T et al 2005 Towards a proteome scale map of the human protein protein interaction network Nature 437 7062 1173 8 Bibcode 2005Natur 437 1173R doi 10 1038 nature04209 PMID 16189514 S2CID 4427026 Rahmouni S Cerignoli F Alonso A et al 2006 Loss of the VHR dual specific phosphatase causes cell cycle arrest and senescence Nat Cell Biol 8 5 524 31 doi 10 1038 ncb1398 PMID 16604064 S2CID 20976640 Hao L ElShamy WM 2007 BRCA1 IRIS activates cyclin D1 expression in breast cancer cells by downregulating the JNK phosphatase DUSP3 VHR Int J Cancer 121 1 39 46 doi 10 1002 ijc 22597 PMID 17278098 S2CID 24555741 Hoyt R Zhu W Cerignoli F et al 2007 Cutting edge selective tyrosine dephosphorylation of interferon activated nuclear STAT5 by the VHR phosphatase J Immunol 179 6 3402 6 doi 10 4049 jimmunol 179 6 3402 PMC 2770724 PMID 17785772 Retrieved from https en wikipedia org w index php title DUSP3 amp oldid 1190502497, wikipedia, wiki, book, books, library,

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