HDAC1

From Wikipedia, the free encyclopedia

Histone deacetylase 1

Identifiers

HDAC1; DKFZp686H12203; GON-10; HD1; RPD3; RPD3L1

External IDs

OMIM: 601241 MGI: 108086 HomoloGene: 68426

Gene ontology
Molecular Function:	• transcription factor activity • histone deacetylase activity • transcription factor binding • hydrolase activity • enzyme binding • identical protein binding
Cellular Component:	• histone deacetylase complex • nucleus • cytoplasm
Biological Process:	• transcription • regulation of transcription, DNA-dependent • anti-apoptosis • chromatin modification • histone deacetylation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_004964 (mRNA)
NP_004955 (protein)

NM_008228 (mRNA)
NP_032254 (protein)

Location

Chr 1: 32.53 - 32.57 Mb

n/a

Pubmed search

[1]

[2]

Histone deacetylase 1, also known as HDAC1, is a human gene.

Histone acetylation and deacetylation, catalyzed by multisubunit complexes, play a key role in the regulation of eukaryotic gene expression. The protein encoded by this gene belongs to the histone deacetylase/acuc/apha family and is a component of the histone deacetylase complex. It also interacts with retinoblastoma tumor-suppressor protein and this complex is a key element in the control of cell proliferation and differentiation. Together with metastasis-associated protein-2, it deacetylates p53 and modulates its effect on cell growth and apoptosis.^[1]

1 See also
2 References
3 Further reading
4 External links

[edit] See also

[edit] References

^ Entrez Gene: HDAC1 histone deacetylase 1.

[edit] Further reading

Wolffe AP (1996). "Histone deacetylase: a regulator of transcription.". Science 272 (5260): 371–2. PMID 8602525.
Ahringer J (2000). "NuRD and SIN3 histone deacetylase complexes in development.". Trends Genet. 16 (8): 351–6. PMID 10904264.
Verdin E, Dequiedt F, Kasler HG (2003). "Class II histone deacetylases: versatile regulators.". Trends Genet. 19 (5): 286–93. PMID 12711221.
Zhang Y, Dufau ML (2003). "Dual mechanisms of regulation of transcription of luteinizing hormone receptor gene by nuclear orphan receptors and histone deacetylase complexes.". J. Steroid Biochem. Mol. Biol. 85 (2-5): 401–14. PMID 12943729.
Stevens M, De Clercq E, Balzarini J (2007). "The regulation of HIV-1 transcription: molecular targets for chemotherapeutic intervention.". Med Res Rev 26 (5): 595–625. doi:10.1002/med.20081. PMID 16838299.
Hijmans EM, Voorhoeve PM, Beijersbergen RL, et al. (1995). "E2F-5, a new E2F family member that interacts with p130 in vivo.". Mol. Cell. Biol. 15 (6): 3082–9. PMID 7760804.
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.
Margolis DM, Somasundaran M, Green MR (1994). "Human transcription factor YY1 represses human immunodeficiency virus type 1 transcription and virion production.". J. Virol. 68 (2): 905–10. PMID 8289393.
Taunton J, Hassig CA, Schreiber SL (1996). "A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p.". Science 272 (5260): 408–11. PMID 8602529.
Furukawa Y, Kawakami T, Sudo K, et al. (1996). "Isolation and mapping of a human gene (RPD3L1) that is homologous to RPD3, a transcription factor in Saccharomyces cerevisiae.". Cytogenet. Cell Genet. 73 (1-2): 130–3. PMID 8646880.
Hassig CA, Fleischer TC, Billin AN, et al. (1997). "Histone deacetylase activity is required for full transcriptional repression by mSin3A.". Cell 89 (3): 341–7. PMID 9150133.
Laherty CD, Yang WM, Sun JM, et al. (1997). "Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression.". Cell 89 (3): 349–56. PMID 9150134.
Zhang Y, Iratni R, Erdjument-Bromage H, et al. (1997). "Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex.". Cell 89 (3): 357–64. PMID 9150135.
Romerio F, Gabriel MN, Margolis DM (1997). "Repression of human immunodeficiency virus type 1 through the novel cooperation of human factors YY1 and LSF.". J. Virol. 71 (12): 9375–82. PMID 9371597.
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.
Brehm A, Miska EA, McCance DJ, et al. (1998). "Retinoblastoma protein recruits histone deacetylase to repress transcription.". Nature 391 (6667): 597–601. doi:10.1038/35404. PMID 9468139.
Magnaghi-Jaulin L, Groisman R, Naguibneva I, et al. (1998). "Retinoblastoma protein represses transcription by recruiting a histone deacetylase.". Nature 391 (6667): 601–5. doi:10.1038/35410. PMID 9468140.
Lin RJ, Nagy L, Inoue S, et al. (1998). "Role of the histone deacetylase complex in acute promyelocytic leukaemia.". Nature 391 (6669): 811–4. doi:10.1038/35895. PMID 9486654.
Luo RX, Postigo AA, Dean DC (1998). "Rb interacts with histone deacetylase to repress transcription.". Cell 92 (4): 463–73. PMID 9491888.