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Gene Review

DUSP5  -  dual specificity phosphatase 5

Homo sapiens

Synonyms: DUSP, Dual specificity protein phosphatase 5, Dual specificity protein phosphatase hVH3, HVH3, VH3
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Disease relevance of DUSP5

  • Using cDNA-microarray technology, we found that the expression of DUSP5 mRNA was dramatically increased by exogenous p53 in U373MG, a p53-mutant glioblastoma cell line [1].
  • IUGR affected hepatic DUSP5 mRNA levels and exon 2 DNA methylation into adulthood in the rat [2].
  • Variable region diversity in human circulating antibodies specific for the capsular polysaccharide of Haemophilus influenzae type b. Preferential usage of two types of VH3 heavy chains [3].
  • With one possible exception, none of these lymphoma VH sequences appear to represent any of the VH3 genes that may be preferentially used in the fetal repertoire [4].
  • Three different phage clones expressing anti-HS single chain variable fragment antibodies (HS4C3, HS4D10, and HS3G8) were isolated, with an amino acid sequence of the complementarity-determining region 3 of GRRLKD (VH3 gene, DP-38), SLRMNGCGAHQ (VH3 gene, DP-42), and YYHYKVN (VH1 gene, DP-8), respectively [5].

Psychiatry related information on DUSP5

  • FR3 amino acids 78-88 displayed the best-score epitopes in Ids containing a VH3-family segment, the most represented in FL Ids [6].

High impact information on DUSP5


Chemical compound and disease context of DUSP5


Biological context of DUSP5


Anatomical context of DUSP5

  • Moreover, we have identified a DUSP5-dependent negative regulatory pathway for MAPK activity in T cells [14].
  • To determine whether Abs commonly expressed by V-preB+L+ B cells show similar features, we analyzed Ig H chains from three highly expressed VH families, VH1, VH3, and VH4, and Ig-lambda [15].
  • RT-PCR amplification reveals expression of the MAPK-selective phosphatases (MKP), MKP-1, -3, and dual-specificity phosphatase 5, in granulosa cells [16].
  • Progressive decrease in VH3 gene family expression in plasma cells of HIV-infected patients [17].
  • Among naturally activated lymphocytes the VH6 gene was markedly over-represented, while expression of the VH1 and VH3 gene families was decreased [18].

Associations of DUSP5 with chemical compounds

  • Dual-specificity phosphatase 5 (DUSP5), a VH1-like enzyme that hydrolyses nuclear substrates phosphorylated on both tyrosine and serine/threonine residues, has a potential role in deactivation of mitogen- or stress-activated protein kinases [1].
  • DUSP Meet Immunology: Dual Specificity MAPK Phosphatases in Control of the Inflammatory Response [19].
  • To examine directly the available human VH3 repertoire, we have used PCR to amplify and clone candidate germ-line VH3b H chain V region genes from two unrelated subjects from whom anti-Hib polysaccharide mAb had been previously obtained [20].
  • Id-16/6 can identify a subgroup of VH3-derived antibodies we have termed the 18/2 CDR family [21].
  • Bone marrow plasma cells from RIC contained short gamma 1 heavy-chain transcripts in which a VDJ exon related to the VH2 subgroup was directly joined to the hinge exon; plasma cells from THR contained short gamma 1 transcripts with a VDJ exon related to the VH3 subgroup joined to the CH3 exon [22].

Enzymatic interactions of DUSP5


Regulatory relationships of DUSP5

  • Three tumors expressed VH3 genes and one expressed a VH1 gene, while the light chains included two V lambda and one V kappa III; one light chain was not isolated [24].

Other interactions of DUSP5

  • Overexpression of DUSP5 suppressed the growth of several types of human cancer cells, in which Erk1/2 was significantly dephosphorylated [1].
  • This distribution frequency was different from that observed in RA, where VH3 was the dominant family, followed by VH1 [25].
  • We have isolated a novel VH-1-like PTPase, hVH-3, from the human placenta and compared various aspects of its expression with previously isolated members of this subfamily [23].
  • IgM, IgD and IgG that expressed a VH3 gene family segment, were decreased in patients with low CD4 counts and to a greater extend in patients with AIDS symptoms (up to 85% for IgG) compared to adult healthy donors [26].

Analytical, diagnostic and therapeutic context of DUSP5

  • Binding to SPA in ELISA occurred with 15 of 15 VH3 IgM, but none of 12 IgM from the VH1, VH4, VH5, or VH6 families [27].
  • DUSP expression was analyzed for possible correlation with patient age, disease stage, tumor grade, histological grade, chemotherapy status, and survival [28].
  • In this study, we have performed sequence analysis of 104-day human fetal liver-derived, randomly isolated constant region C+ mu transcripts and demonstrate a consistent preference during fetal life for a small subset of three highly conserved VH3 family gene segments [29].
  • Surface plasmon resonance measurements demonstrated that domain D and native SpA had the strongest binding interactions with an IgM-kappa encoded by the germline configuration of the VH3 gene VH26c [30].
  • A larger number of clonally related VH sequences could be obtained by using a VH3 gene-specific PCR so that genealogical trees depicting the process of diversification could be drawn [31].


  1. Dual-specificity phosphatase 5 (DUSP5) as a direct transcriptional target of tumor suppressor p53. Ueda, K., Arakawa, H., Nakamura, Y. Oncogene (2003) [Pubmed]
  2. Growth retardation alters the epigenetic characteristics of hepatic dual specificity phosphatase 5. Fu, Q., McKnight, R.A., Yu, X., Callaway, C.W., Lane, R.H. FASEB J. (2006) [Pubmed]
  3. Variable region diversity in human circulating antibodies specific for the capsular polysaccharide of Haemophilus influenzae type b. Preferential usage of two types of VH3 heavy chains. Silverman, G.J., Lucas, A.H. J. Clin. Invest. (1991) [Pubmed]
  4. Ig VH gene expression among human follicular lymphomas. Bahler, D.W., Campbell, M.J., Hart, S., Miller, R.A., Levy, S., Levy, R. Blood (1991) [Pubmed]
  5. Generation and application of type-specific anti-heparan sulfate antibodies using phage display technology. Further evidence for heparan sulfate heterogeneity in the kidney. van Kuppevelt, T.H., Dennissen, M.A., van Venrooij, W.J., Hoet, R.M., Veerkamp, J.H. J. Biol. Chem. (1998) [Pubmed]
  6. Analysis of the intraclonal diversity of HLA-A0201-restricted T lymphocyte epitopes in follicular lymphoma idiotype. Molinier-Frenkel, V., Popa, N., Poulot, V., Chaise, C., Marquet, J., Haioun, C., Gaulard, P., Farcet, J.P., Delfau-Larue, M.H. Br. J. Haematol. (2006) [Pubmed]
  7. Immunoglobulin VH3 gene products: natural ligands for HIV gp120. Berberian, L., Goodglick, L., Kipps, T.J., Braun, J. Science (1993) [Pubmed]
  8. Human rheumatoid factor cross-idiotypes. IV. Studies on WA XId-positive IgM without rheumatoid factor activity provide evidence that the WA XId is not unique to rheumatoid factors and is distinct from the 17.109 and G6 XIds. Knight, G.B., Agnello, V., Bonagura, V., Barnes, J.L., Panka, D.J., Zhang, Q.X. J. Exp. Med. (1993) [Pubmed]
  9. Restricted use of fetal VH3 immunoglobulin genes by unselected B cells in the adult. Predominance of 56p1-like VH genes in common variable immunodeficiency. Braun, J., Berberian, L., King, L., Sanz, I., Govan, H.L. J. Clin. Invest. (1992) [Pubmed]
  10. Analysis of genetic variation reveals human immunoglobulin VH-region gene organization. Walter, M.A., Cox, D.W. Am. J. Hum. Genet. (1988) [Pubmed]
  11. Specific inactivation and nuclear anchoring of extracellular signal-regulated kinase 2 by the inducible dual-specificity protein phosphatase DUSP5. Mandl, M., Slack, D.N., Keyse, S.M. Mol. Cell. Biol. (2005) [Pubmed]
  12. Identification of transcription factor binding sites upstream of human genes regulated by the phosphatidylinositol 3-kinase and MEK/ERK signaling pathways. Tullai, J.W., Schaffer, M.E., Mullenbrock, S., Kasif, S., Cooper, G.M. J. Biol. Chem. (2004) [Pubmed]
  13. Crystal structure of the catalytic domain of human DUSP5, a dual specificity MAP kinase protein phosphatase. Jeong, D.G., Cho, Y.H., Yoon, T.S., Kim, J.H., Ryu, S.E., Kim, S.J. Proteins (2007) [Pubmed]
  14. Analysis of gamma c-family cytokine target genes. Identification of dual-specificity phosphatase 5 (DUSP5) as a regulator of mitogen-activated protein kinase activity in interleukin-2 signaling. Kovanen, P.E., Rosenwald, A., Fu, J., Hurt, E.M., Lam, L.T., Giltnane, J.M., Wright, G., Staudt, L.M., Leonard, W.J. J. Biol. Chem. (2003) [Pubmed]
  15. Circulating human B cells that express surrogate light chains display a unique antibody repertoire. Meffre, E., Chiorazzi, M., Nussenzweig, M.C. J. Immunol. (2001) [Pubmed]
  16. Phosphatase activation by epidermal growth factor family ligands regulates extracellular regulated kinase signaling in undifferentiated hen granulosa cells. Woods, D.C., Johnson, A.L. Endocrinology (2006) [Pubmed]
  17. Progressive decrease in VH3 gene family expression in plasma cells of HIV-infected patients. David, D., Demaison, C., Bani, L., Thèze, J. Int. Immunol. (1996) [Pubmed]
  18. Selective usage of VH genes in adult human B lymphocyte repertoires. Davidkova, G., Pettersson, S., Holmberg, D., Lundkvist, I. Scand. J. Immunol. (1997) [Pubmed]
  19. DUSP Meet Immunology: Dual Specificity MAPK Phosphatases in Control of the Inflammatory Response. Lang, R., Hammer, M., Mages, J. J. Immunol. (2006) [Pubmed]
  20. The human VH3b gene subfamily is highly polymorphic. Adderson, E.E., Azmi, F.H., Wilson, P.M., Shackelford, P.G., Carroll, W.L. J. Immunol. (1993) [Pubmed]
  21. Molecular analysis of a germ line-encoded idiotypic marker of pathogenic human lupus autoantibodies. Young, F., Tucker, L., Rubinstein, D., Guillaume, T., André-Schwartz, J., Barrett, K.J., Schwartz, R.S., Logtenberg, T. J. Immunol. (1990) [Pubmed]
  22. Structure of abnormal heavy chains in human heavy-chain-deposition disease. Khamlichi, A.A., Aucouturier, P., Preud'homme, J.L., Cogné, M. Eur. J. Biochem. (1995) [Pubmed]
  23. Multiple dual specificity protein tyrosine phosphatases are expressed and regulated differentially in liver cell lines. Kwak, S.P., Dixon, J.E. J. Biol. Chem. (1995) [Pubmed]
  24. Immunoglobulin gene sequence analysis to further assess B-cell origin of multiple myeloma. Biggs, D.D., Kraj, P., Goldman, J., Jefferies, L., Carchidi, C., Anderson, K., Silberstein, L.E. Clin. Diagn. Lab. Immunol. (1995) [Pubmed]
  25. Rheumatoid factors in primary Sjögren's syndrome (pSS) use diverse VH region genes, the majority of which show no evidence of somatic hypermutation. Elagib, K.E., Børretzen, M., Jonsson, R., Haga, H.J., Thoen, J., Thompson, K.M., Natvig, J.B. Clin. Exp. Immunol. (1999) [Pubmed]
  26. Selective variations in vivo of VH3 and VH1 gene family expression in peripheral B cell IgM, IgD and IgG during HIV infection. David, D., Demaison, C., Bani, L., Zouali, M., Thèze, J. Eur. J. Immunol. (1995) [Pubmed]
  27. The structural basis of germline-encoded VH3 immunoglobulin binding to staphylococcal protein A. Hillson, J.L., Karr, N.S., Oppliger, I.R., Mannik, M., Sasso, E.H. J. Exp. Med. (1993) [Pubmed]
  28. The PAC-1 dual specificity phosphatase predicts poor outcome in serous ovarian carcinoma. Givant-Horwitz, V., Davidson, B., Goderstad, J.M., Nesland, J.M., Tropé, C.G., Reich, R. Gynecol. Oncol. (2004) [Pubmed]
  29. Preferential utilization of conserved immunoglobulin heavy chain variable gene segments during human fetal life. Schroeder, H.W., Wang, J.Y. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  30. VH3 family antibodies bind domain D of staphylococcal protein A. Roben, P.W., Salem, A.N., Silverman, G.J. J. Immunol. (1995) [Pubmed]
  31. Accumulation of clonally related B lymphocytes in the cerebrospinal fluid of multiple sclerosis patients. Colombo, M., Dono, M., Gazzola, P., Roncella, S., Valetto, A., Chiorazzi, N., Mancardi, G.L., Ferrarini, M. J. Immunol. (2000) [Pubmed]
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