HDAC7

Histone deacetylase 7

PDB rendering based on 2nvr.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsHDAC7 ; HD7A; HDAC7A
External IDsOMIM: 606542 MGI: 1891835 HomoloGene: 9124 IUPHAR: 2661 ChEMBL: 2716 GeneCards: HDAC7 Gene
EC number3.5.1.98
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez5156456233
EnsemblENSG00000061273ENSMUSG00000022475
UniProtQ8WUI4Q8C2B3
RefSeq (mRNA)NM_001098416NM_001204275
RefSeq (protein)NP_001091886NP_001191204
Location (UCSC)Chr 12:
48.18 – 48.23 Mb
Chr 15:
97.79 – 97.84 Mb
PubMed search

Histone deacetylase 7 is an enzyme that in humans is encoded by the HDAC7 gene.[1][2][3]

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.[3]

Interactions

HDAC7A has been shown to interact with Endothelin receptor type A,[4] HDAC3,[5] HTATIP,[6] BCL6,[7] Nuclear receptor co-repressor 1[5] and IKZF1.[8]

See also

References

  1. Marks PA, Richon VM, Rifkind RA (Aug 2000). "Histone deacetylase inhibitors: inducers of differentiation or apoptosis of transformed cells". J Natl Cancer Inst 92 (15): 1210–6. doi:10.1093/jnci/92.15.1210. PMID 10922406.
  2. Kao HY, Downes M, Ordentlich P, Evans RM (Feb 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. doi:10.1101/gad.14.1.55. PMC 316336. PMID 10640276.
  3. 3.0 3.1 "Entrez Gene: HDAC7A histone deacetylase 7A".
  4. Lee, H J; Chun M; Kandror K V (May 2001). "Tip60 and HDAC7 interact with the endothelin receptor a and may be involved in downstream signaling". J. Biol. Chem. (United States) 276 (20): 16597–600. doi:10.1074/jbc.C000909200. ISSN 0021-9258. PMID 11262386.
  5. 5.0 5.1 Fischle, W; Dequiedt F; Fillion M; Hendzel M J; Voelter W; Verdin E (Sep 2001). "Human HDAC7 histone deacetylase activity is associated with HDAC3 in vivo". J. Biol. Chem. (United States) 276 (38): 35826–35. doi:10.1074/jbc.M104935200. ISSN 0021-9258. PMID 11466315.
  6. Xiao, Hui; Chung Jin; Kao Hung-Ying; Yang Yu-Chung (Mar 2003). "Tip60 is a co-repressor for STAT3". J. Biol. Chem. (United States) 278 (13): 11197–204. doi:10.1074/jbc.M210816200. ISSN 0021-9258. PMID 12551922.
  7. Lemercier, Claudie; Brocard Marie-Paule, Puvion-Dutilleul Francine, Kao Hung-Ying, Albagli Olivier, Khochbin Saadi (Jun 2002). "Class II histone deacetylases are directly recruited by BCL6 transcriptional repressor". J. Biol. Chem. (United States) 277 (24): 22045–52. doi:10.1074/jbc.M201736200. ISSN 0021-9258. PMID 11929873.
  8. Koipally, Joseph; Georgopoulos Katia (Aug 2002). "A molecular dissection of the repression circuitry of Ikaros". J. Biol. Chem. (United States) 277 (31): 27697–705. doi:10.1074/jbc.M201694200. ISSN 0021-9258. PMID 12015313.

Further reading

External links

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