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Gene Review

DDX5  -  DEAD (Asp-Glu-Ala-Asp) box helicase 5

Homo sapiens

Synonyms: DEAD box protein 5, G17P1, HELR, HLR1, HUMP68, ...
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Disease relevance of DDX5

  • RESULTS: A missense SNP in the DEAD box polypeptide 5 (DDX5) gene was significantly associated with an increased risk of advanced fibrosis in both the UCSF and the VCU cohorts (OR, 1.8 and 2.2, respectively) [1].
  • Chromosome mapping by Southern analysis of DNA from somatic cell hybrids is often unsuccessful when only cDNA probes are available. p68 is a putative RNA helicase that is antigenically related to the simian virus 40 large tumor antigen [2].
  • Intracellular interaction of EBV/C3d receptor (CR2) with p68, a calcium-binding protein present in normal but not in transformed B lymphocytes [3].
  • Cellular RNA helicase p68 relocalization and interaction with the hepatitis C virus (HCV) NS5B protein and the potential role of p68 in HCV RNA replication [4].
  • Recently, a p68 subfamily (DEAD box proteins) which share more extensive regions of homology has been identified in mouse, Drosophila, Saccharomyces cerevisiae and Escherichia coli [5].
  • Accordingly, knockdown of p68 and p72 in colon cancer cells inhibits their proliferation and diminishes their ability to form tumors in vivo [6].

High impact information on DDX5

  • We demonstrated that tyrosine phosphorylation of p68 at Y593 mediated PDGF-stimulated epithelial-mesenchymal transition (EMT) [7].
  • We showed that PDGF treatment led to phosphorylation of p68 at Y593 in the cell nucleus [7].
  • The p68 protein was first identified because of its specific immunological cross-reaction with the DNA tumour virus nuclear oncogene SV40 large T, detected with the anti-SV40 large T monoclonal antibody DL3C4, now renamed PAb204 [8].
  • The p68 protein is a highly conserved nuclear antigen that is thought to be important in the regulation of cell growth and division [8].
  • Full-length hsp70 mRNA accumulates in the nucleus near its sites of transcription following heat shock of p68 homozygotes, and hsp70 gene shutdown is delayed [9].

Biological context of DDX5

  • The expected COOH-terminal p10 fragment resulting from hydrolysis of p68 at Met484 is not released intact, but undergoes further cleavage at Asn494, Met503, and Tyr532 [10].
  • The nuclear DEAD box RNA helicase p68 interacts with the nucleolar protein fibrillarin and colocalizes specifically in nascent nucleoli during telophase [11].
  • Two diplotype groups, carrying the haplotypes composed of the DDX5 SNP and 2 neighboring POLG2 SNPs were also significantly associated with an increased risk of advanced fibrosis and had comparable or better risk estimates [1].
  • Application of this technique to DNA from human-mouse somatic cell hybrids and cell lines derived from them by chromosome-mediated gene transfer allowed us to map p68 to the distal part of the long arm of chromosome 17 [2].
  • By using the polymerase chain reaction and oligode-oxynucleotide primers based on the cDNA sequence, we have identified introns in the p68 gene [2].

Anatomical context of DDX5

  • Further, the RNA-dependent helicase p68 is also associated with both IDX and rasISS1 RNA, and suppression of p68 expression in HeLa cells by RNAi experiments results in a marked increase of IDX inclusion in the endogenous mRNA, suggesting a role for this protein in alternative splicing regulation [12].
  • Furthermore, depletion of p68 RNA helicase arrested spliceosome assembly at the prespliceosome stage, suggesting that p68 may play a role in the transition from prespliceosome to spliceosome [13].
  • Subsequently, we have analyzed regulation of p68 by wound-associated mediators in human and murine keratinocytes [14].
  • We demonstrate herein that Ab2 detected in normal B lymphocytes a 68-kDa protein, p68, that was not expressed in transformed B cells. p68 was localized in purified plasma membranes and cytosol fractions [3].
  • Treatment of co-transfected cells with phosphatidylinositol-specific phospholipase C liberated the complex of MT4-MMP and p68 ADAMTS4 from the cell membrane, but the p53 ADAMTS4 remained associated [15].

Associations of DDX5 with chemical compounds


Physical interactions of DDX5

  • Competitive studies supported that CR2 and Ab2 interacted with identical sites on p68 [3].

Enzymatic interactions of DDX5

  • Furthermore, it could be shown that Tlk1 phosphorylates immunoprecipitated p68 [21].

Other interactions of DDX5

  • The DEAD box protein p68: a novel transcriptional coactivator of the p53 tumour suppressor [22].
  • We also show, by chromatin immunoprecipitation, that p68 is recruited to the p21 promoter in a p53-dependent manner, consistent with a role in promoting transcriptional initiation [22].
  • Coimmunoprecipitation experiments confirmed that p68 and fibrillarin can form complexes in cellular extracts, and deletion analysis identified regions in each protein responsible for mediating the interaction [11].
  • Direct interaction of purified CR2 with purified p68 was demonstrated [3].
  • DDX5 (p68) and its related DDX17 (p72) have also been implicated in organ/tissue differentiation [23].

Analytical, diagnostic and therapeutic context of DDX5


  1. Identification of two gene variants associated with risk of advanced fibrosis in patients with chronic hepatitis C. Huang, H., Shiffman, M.L., Cheung, R.C., Layden, T.J., Friedman, S., Abar, O.T., Yee, L., Chokkalingam, A.P., Schrodi, S.J., Chan, J., Catanese, J.J., Leong, D.U., Ross, D., Hu, X., Monto, A., McAllister, L.B., Broder, S., White, T., Sninsky, J.J., Wright, T.L. Gastroenterology (2006) [Pubmed]
  2. Chromosome mapping of the human gene encoding the 68-kDa nuclear antigen (p68) by using the polymerase chain reaction. Iggo, R., Gough, A., Xu, W., Lane, D.P., Spurr, N.K. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  3. Intracellular interaction of EBV/C3d receptor (CR2) with p68, a calcium-binding protein present in normal but not in transformed B lymphocytes. Barel, M., Gauffre, A., Lyamani, F., Fiandino, A., Hermann, J., Frade, R. J. Immunol. (1991) [Pubmed]
  4. Cellular RNA helicase p68 relocalization and interaction with the hepatitis C virus (HCV) NS5B protein and the potential role of p68 in HCV RNA replication. Goh, P.Y., Tan, Y.J., Lim, S.P., Tan, Y.H., Lim, S.G., Fuller-Pace, F., Hong, W. J. Virol. (2004) [Pubmed]
  5. Nuclear protein p68 is an RNA-dependent ATPase. Iggo, R.D., Lane, D.P. EMBO J. (1989) [Pubmed]
  6. Involvement of RNA helicases p68 and p72 in colon cancer. Shin, S., Rossow, K.L., Grande, J.P., Janknecht, R. Cancer Res. (2007) [Pubmed]
  7. P68 RNA Helicase Mediates PDGF-Induced Epithelial Mesenchymal Transition by Displacing Axin from beta-Catenin. Yang, L., Lin, C., Liu, Z.R. Cell (2006) [Pubmed]
  8. Nuclear protein with sequence homology to translation initiation factor eIF-4A. Ford, M.J., Anton, I.A., Lane, D.P. Nature (1988) [Pubmed]
  9. The Drosophila P68 RNA helicase regulates transcriptional deactivation by promoting RNA release from chromatin. Buszczak, M., Spradling, A.C. Genes Dev. (2006) [Pubmed]
  10. The differential processing of homodimers of reverse transcriptases from human immunodeficiency viruses type 1 and 2 is a consequence of the distinct specificities of the viral proteases. Fan, N., Rank, K.B., Leone, J.W., Heinrikson, R.L., Bannow, C.A., Smith, C.W., Evans, D.B., Poppe, S.M., Tarpley, W.G., Rothrock, D.J. J. Biol. Chem. (1995) [Pubmed]
  11. The nuclear DEAD box RNA helicase p68 interacts with the nucleolar protein fibrillarin and colocalizes specifically in nascent nucleoli during telophase. Nicol, S.M., Causevic, M., Prescott, A.R., Fuller-Pace, F.V. Exp. Cell Res. (2000) [Pubmed]
  12. Roles of hnRNP A1, SR proteins, and p68 helicase in c-H-ras alternative splicing regulation. Guil, S., Gattoni, R., Carrascal, M., Abián, J., Stévenin, J., Bach-Elias, M. Mol. Cell. Biol. (2003) [Pubmed]
  13. p68 RNA helicase is an essential human splicing factor that acts at the U1 snRNA-5' splice site duplex. Liu, Z.R. Mol. Cell. Biol. (2002) [Pubmed]
  14. p68 DEAD box RNA helicase expression in keratinocytes. Regulation, nucleolar localization, and functional connection to proliferation and vascular endothelial growth factor gene expression. Kahlina, K., Goren, I., Pfeilschifter, J., Frank, S. J. Biol. Chem. (2004) [Pubmed]
  15. ADAMTS4 (aggrecanase-1) activation on the cell surface involves C-terminal cleavage by glycosylphosphatidyl inositol-anchored membrane type 4-matrix metalloproteinase and binding of the activated proteinase to chondroitin sulfate and heparan sulfate on syndecan-1. Gao, G., Plaas, A., Thompson, V.P., Jin, S., Zuo, F., Sandy, J.D. J. Biol. Chem. (2004) [Pubmed]
  16. Nucleocytoplasmic sorting of macromolecules following mitosis: fate of nuclear constituents after inhibition of pore complex function. Benavente, R., Scheer, U., Chaly, N. Eur. J. Cell Biol. (1989) [Pubmed]
  17. A nuclear juvenile hormone-binding protein from larvae of Manduca sexta: a putative receptor for the metamorphic action of juvenile hormone. Palli, S.R., Touhara, K., Charles, J.P., Bonning, B.C., Atkinson, J.K., Trowell, S.C., Hiruma, K., Goodman, W.G., Kyriakides, T., Prestwich, G.D. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  18. Functional expression and RNA binding analysis of the interferon-induced, double-stranded RNA-activated, 68,000-Mr protein kinase in a cell-free system. Katze, M.G., Wambach, M., Wong, M.L., Garfinkel, M., Meurs, E., Chong, K., Williams, B.R., Hovanessian, A.G., Barber, G.N. Mol. Cell. Biol. (1991) [Pubmed]
  19. Crystallization of p68 on lipid monolayers and as three-dimensional single crystals. Newman, R., Tucker, A., Ferguson, C., Tsernoglou, D., Leonard, K., Crumpton, M.J. J. Mol. Biol. (1989) [Pubmed]
  20. Characterization of Ca2(+)-dependent phospholipid binding, vesicle aggregation and membrane fusion by annexins. Blackwood, R.A., Ernst, J.D. Biochem. J. (1990) [Pubmed]
  21. Identification of the human DEAD-box protein p68 as a substrate of Tlk1. Kodym, R., Henöckl, C., Fürweger, C. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  22. The DEAD box protein p68: a novel transcriptional coactivator of the p53 tumour suppressor. Bates, G.J., Nicol, S.M., Wilson, B.J., Jacobs, A.M., Bourdon, J.C., Wardrop, J., Gregory, D.J., Lane, D.P., Perkins, N.D., Fuller-Pace, F.V. EMBO J. (2005) [Pubmed]
  23. RNA helicases: regulators of differentiation. Abdelhaleem, M. Clin. Biochem. (2005) [Pubmed]
  24. The highly related DEAD box RNA helicases p68 and p72 exist as heterodimers in cells. Ogilvie, V.C., Wilson, B.J., Nicol, S.M., Morrice, N.A., Saunders, L.R., Barber, G.N., Fuller-Pace, F.V. Nucleic Acids Res. (2003) [Pubmed]
  25. Structure and expression of the human p68 RNA helicase gene. Rössler, O.G., Hloch, P., Schütz, N., Weitzenegger, T., Stahl, H. Nucleic Acids Res. (2000) [Pubmed]
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