HDAC7

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Histone deacetylase 7
Protein HDAC7A PDB 2nvr.png
PDB rendering based on 2nvr.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols HDAC7 ; HD7A; HDAC7A
External IDs OMIM606542 MGI1891835 HomoloGene9124 ChEMBL: 2716 GeneCards: HDAC7 Gene
EC number 3.5.1.98
RNA expression pattern
PBB GE HDAC7A 217937 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 51564 56233
Ensembl ENSG00000061273 ENSMUSG00000022475
UniProt Q8WUI4 Q8C2B3
RefSeq (mRNA) NM_001098416 NM_001204275
RefSeq (protein) NP_001091886 NP_001191204
Location (UCSC) Chr 12:
48.18 – 48.23 Mb
Chr 15:
97.79 – 97.84 Mb
PubMed search [1] [2]

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[edit]

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[edit]

References[edit]

  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. ^ a b "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. ^ a b 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[edit]

External links[edit]

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