Histone deacetylase 5

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Histone deacetylase 5
Identifiers
Symbols HDAC5 ; FLJ90614; HD5; NY-CO-9
External IDs Template:OMIM5 Template:MGI HomoloGene3995
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Histone deacetylase 5, also known as HDAC5, is a human gene.[1]

Histones play a critical role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation alters chromosome structure and affects transcription factor access to DNA. The protein encoded by this gene belongs to the class II histone deacetylase/acuc/apha family. It possesses histone deacetylase activity and represses transcription when tethered to a promoter. It coimmunoprecipitates only with HDAC3 family member and might form multicomplex proteins. It also interacts with myocyte enhancer factor-2 (MEF2) proteins, resulting in repression of MEF2-dependent genes. This gene is thought to be associated with colon cancer. Two transcript variants encoding different isoforms have been found for this gene.[1]

See also

References

  1. 1.0 1.1 "Entrez Gene: HDAC5 histone deacetylase 5".

Further reading

  • Nakajima D, Okazaki N, Yamakawa H; et al. (2003). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". DNA Res. 9 (3): 99–106. PMID 12168954.
  • Verdin E, Dequiedt F, Kasler HG (2003). "Class II histone deacetylases: versatile regulators". Trends Genet. 19 (5): 286–93. PMID 12711221.
  • Scanlan MJ, Chen YT, Williamson B; et al. (1998). "Characterization of human colon cancer antigens recognized by autologous antibodies". Int. J. Cancer. 76 (5): 652–8. PMID 9610721.
  • Nagase T, Ishikawa K, Miyajima N; et al. (1998). "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Res. 5 (1): 31–9. PMID 9628581.
  • Grozinger CM, Hassig CA, Schreiber SL (1999). "Three proteins define a class of human histone deacetylases related to yeast Hda1p". Proc. Natl. Acad. Sci. U.S.A. 96 (9): 4868–73. PMID 10220385.
  • Huang EY, Zhang J, Miska EA; et al. (2000). "Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway". Genes Dev. 14 (1): 45–54. PMID 10640275.
  • Lemercier C, Verdel A, Galloo B; et al. (2000). "mHDA1/HDAC5 histone deacetylase interacts with and represses MEF2A transcriptional activity". J. Biol. Chem. 275 (20): 15594–9. doi:10.1074/jbc.M908437199. PMID 10748098.
  • Grozinger CM, Schreiber SL (2000). "Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent cellular localization". Proc. Natl. Acad. Sci. U.S.A. 97 (14): 7835–40. doi:10.1073/pnas.140199597. PMID 10869435.
  • Huynh KD, Fischle W, Verdin E, Bardwell VJ (2000). "BCoR, a novel corepressor involved in BCL-6 repression". Genes Dev. 14 (14): 1810–23. PMID 10898795.
  • Mahlknecht U, Schnittger S, Ottmann OG; et al. (2000). "Chromosomal organization and localization of the human histone deacetylase 5 gene (HDAC5)". Biochim. Biophys. Acta. 1493 (3): 342–8. PMID 11018260.
  • Zhang CL, McKinsey TA, Lu JR, Olson EN (2001). "Association of COOH-terminal-binding protein (CtBP) and MEF2-interacting transcription repressor (MITR) contributes to transcriptional repression of the MEF2 transcription factor". J. Biol. Chem. 276 (1): 35–9. doi:10.1074/jbc.M007364200. PMID 11022042.
  • McKinsey TA, Zhang CL, Lu J, Olson EN (2000). "Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation". Nature. 408 (6808): 106–11. doi:10.1038/35040593. PMID 11081517.
  • McKinsey TA, Zhang CL, Olson EN (2001). "Activation of the myocyte enhancer factor-2 transcription factor by calcium/calmodulin-dependent protein kinase-stimulated binding of 14-3-3 to histone deacetylase 5". Proc. Natl. Acad. Sci. U.S.A. 97 (26): 14400–5. doi:10.1073/pnas.260501497. PMID 11114197.
  • Fischle W, Dequiedt F, Fillion M; et al. (2001). "Human HDAC7 histone deacetylase activity is associated with HDAC3 in vivo". J. Biol. Chem. 276 (38): 35826–35. doi:10.1074/jbc.M104935200. PMID 11466315.
  • McKinsey TA, Zhang CL, Olson EN (2001). "Identification of a signal-responsive nuclear export sequence in class II histone deacetylases". Mol. Cell. Biol. 21 (18): 6312–21. PMID 11509672.
  • Ozawa Y, Towatari M, Tsuzuki S; et al. (2001). "Histone deacetylase 3 associates with and represses the transcription factor GATA-2". Blood. 98 (7): 2116–23. PMID 11567998.
  • Potter GB, Beaudoin GM, DeRenzo CL; et al. (2001). "The hairless gene mutated in congenital hair loss disorders encodes a novel nuclear receptor corepressor". Genes Dev. 15 (20): 2687–701. doi:10.1101/gad.916701. PMID 11641275.
  • Fischle W, Dequiedt F, Hendzel MJ; et al. (2002). "Enzymatic activity associated with class II HDACs is dependent on a multiprotein complex containing HDAC3 and SMRT/N-CoR". Mol. Cell. 9 (1): 45–57. PMID 11804585.
  • Lemercier C, Brocard MP, Puvion-Dutilleul F; et al. (2002). "Class II histone deacetylases are directly recruited by BCL6 transcriptional repressor". J. Biol. Chem. 277 (24): 22045–52. doi:10.1074/jbc.M201736200. PMID 11929873.
  • Huang Y, Tan M, Gosink M; et al. (2002). "Histone deacetylase 5 is not a p53 target gene, but its overexpression inhibits tumor cell growth and induces apoptosis". Cancer Res. 62 (10): 2913–22. PMID 12019172.

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain. Template:WikiDoc Sources