HDAC7A

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Histone deacetylase 7A
PDB rendering based on 2nvr.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols HDAC7A ; HDAC7; DKFZP586J0917
External IDs Template:OMIM5 Template:MGI HomoloGene9124
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 7A, also known as HDAC7A, 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 has sequence homology to members of the histone deacetylase family. This gene is orthologous to mouse HDAC7 gene whose protein promotes repression mediated via transcriptional corepressor SMRT. Multiple alternatively spliced transcript variants encoding several isoforms have been found for this gene.[1]

See also

References

  1. 1.0 1.1 "Entrez Gene: HDAC7A histone deacetylase 7A".

Further reading

  • Marks PA, Richon VM, Rifkind RA (2000). "Histone deacetylase inhibitors: inducers of differentiation or apoptosis of transformed cells". J. Natl. Cancer Inst. 92 (15): 1210–6. PMID 10922406.
  • Verdin E, Dequiedt F, Kasler HG (2003). "Class II histone deacetylases: versatile regulators". Trends Genet. 19 (5): 286–93. PMID 12711221.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. PMID 8125298.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K; et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. PMID 9373149.
  • Kao HY, Downes M, Ordentlich P, Evans RM (2000). "Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression". Genes Dev. 14 (1): 55–66. PMID 10640276.
  • Lee HJ, Chun M, Kandror KV (2001). "Tip60 and HDAC7 interact with the endothelin receptor a and may be involved in downstream signaling". J. Biol. Chem. 276 (20): 16597–600. doi:10.1074/jbc.C000909200. PMID 11262386.
  • 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.
  • 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.
  • Bryant H, Farrell PJ (2002). "Signal Transduction and Transcription Factor Modification during Reactivation of Epstein-Barr Virus from Latency". J. Virol. 76 (20): 10290–8. PMID 12239305.
  • 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. doi:10.1073/pnas.242603899. PMID 12477932.
  • Xiao H, Chung J, Kao HY, Yang YC (2003). "Tip60 is a co-repressor for STAT3". J. Biol. Chem. 278 (13): 11197–204. doi:10.1074/jbc.M210816200. PMID 12551922.
  • Dequiedt F, Kasler H, Fischle W; et al. (2003). "HDAC7, a thymus-specific class II histone deacetylase, regulates Nur77 transcription and TCR-mediated apoptosis". Immunity. 18 (5): 687–98. PMID 12753745.
  • Lee CH, Chawla A, Urbiztondo N; et al. (2003). "Transcriptional repression of atherogenic inflammation: modulation by PPARdelta". Science. 302 (5644): 453–7. doi:10.1126/science.1087344. PMID 12970571.
  • 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.
  • Li X, Song S, Liu Y; et al. (2004). "Phosphorylation of the histone deacetylase 7 modulates its stability and association with 14-3-3 proteins". J. Biol. Chem. 279 (33): 34201–8. doi:10.1074/jbc.M405179200. PMID 15166223.
  • Kato H, Tamamizu-Kato S, Shibasaki F (2004). "Histone deacetylase 7 associates with hypoxia-inducible factor 1alpha and increases transcriptional activity". J. Biol. Chem. 279 (40): 41966–74. doi:10.1074/jbc.M406320200. PMID 15280364.
  • Beausoleil SA, Jedrychowski M, Schwartz D; et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMID 15302935.
  • Jin J, Smith FD, Stark C; et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.

External links

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