HDAC7

Histone deacetylase 7
PDB rendering based on 2nvr.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 3C0Y​, 3C0Z​, 3C10​, 3ZNR​, 3ZNS​
Identifiers
Symbols	HDAC7 ; HD7; HD7A; HDAC7A
External IDs	OMIM: 606542 MGI: 1891835 HomoloGene: 9124 ChEMBL: 2716 GeneCards: HDAC7 Gene
EC number	3.5.1.98
Gene ontology Molecular function • chromatin binding • transcription corepressor activity • protein kinase C binding • protein binding • protein kinase binding • NAD-dependent histone deacetylase activity (H3-K14 specific) • activating transcription factor binding • metal ion binding • repressing transcription factor binding • 14-3-3 protein binding Cellular component • histone deacetylase complex • nucleus • nucleoplasm • cytoplasm Biological process • negative regulation of transcription from RNA polymerase II promoter • vasculogenesis • transcription, DNA-templated • cell-cell junction assembly • Notch signaling pathway • protein sumoylation • negative regulation of interleukin-2 production • post-translational protein modification • cellular protein metabolic process • negative regulation of osteoblast differentiation • histone H3 deacetylation • positive regulation of cell migration involved in sprouting angiogenesis • negative regulation of NIK/NF-kappaB signaling Sources: Amigo / QuickGO
RNA expression pattern
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: 47.78 – 47.83 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]

Function

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:

• BCL6,^[4]
• Endothelin receptor type A,^[5]
• HDAC3,^[6]
• HTATIP,^[7]
• IKZF1,^[8] and
• Nuclear receptor co-repressor 1l.^[6]

See also

• Histone deacetylase

References

1. Marks PA, Richon VM, Rifkind RA (Aug 2000). "Histone deacetylase inhibitors: inducers of differentiation or apoptosis of transformed cells". Journal of the National Cancer Institute 92 (15): 1210–6. doi:10.1093/jnci/92.15.1210. PMID 10922406.
2. Kao HY, Downes M, Ordentlich P, Evans RM (Jan 2000). "Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression". Genes & Development 14 (1): 55–66. doi:10.1101/gad.14.1.55. PMC 316336. PMID 10640276.
3. "Entrez Gene: HDAC7A histone deacetylase 7A".
4. Lemercier C, Brocard MP, Puvion-Dutilleul F, Kao HY, Albagli O, Khochbin S (Jun 2002). "Class II histone deacetylases are directly recruited by BCL6 transcriptional repressor". The Journal of Biological Chemistry 277 (24): 22045–52. doi:10.1074/jbc.M201736200. PMID 11929873.
5. Lee HJ, Chun M, Kandror KV (May 2001). "Tip60 and HDAC7 interact with the endothelin receptor a and may be involved in downstream signaling". The Journal of Biological Chemistry 276 (20): 16597–600. doi:10.1074/jbc.C000909200. PMID 11262386.
6. Fischle W, Dequiedt F, Fillion M, Hendzel MJ, Voelter W, Verdin E (Sep 2001). "Human HDAC7 histone deacetylase activity is associated with HDAC3 in vivo". The Journal of Biological Chemistry 276 (38): 35826–35. doi:10.1074/jbc.M104935200. PMID 11466315.
7. Xiao H, Chung J, Kao HY, Yang YC (Mar 2003). "Tip60 is a co-repressor for STAT3". The Journal of Biological Chemistry 278 (13): 11197–204. doi:10.1074/jbc.M210816200. PMID 12551922.
8. Koipally J, Georgopoulos K (Aug 2002). "A molecular dissection of the repression circuitry of Ikaros". The Journal of Biological Chemistry 277 (31): 27697–705. doi:10.1074/jbc.M201694200. PMID 12015313.

Further reading

• Verdin E, Dequiedt F, Kasler HG (May 2003). "Class II histone deacetylases: versatile regulators". Trends in Genetics 19 (5): 286–93. doi:10.1016/S0168-9525(03)00073-8. PMID 12711221.
• Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Lee HJ, Chun M, Kandror KV (May 2001). "Tip60 and HDAC7 interact with the endothelin receptor a and may be involved in downstream signaling". The Journal of Biological Chemistry 276 (20): 16597–600. doi:10.1074/jbc.C000909200. PMID 11262386.
• Fischle W, Dequiedt F, Fillion M, Hendzel MJ, Voelter W, Verdin E (Sep 2001). "Human HDAC7 histone deacetylase activity is associated with HDAC3 in vivo". The Journal of Biological Chemistry 276 (38): 35826–35. doi:10.1074/jbc.M104935200. PMID 11466315.
• Lemercier C, Brocard MP, Puvion-Dutilleul F, Kao HY, Albagli O, Khochbin S (Jun 2002). "Class II histone deacetylases are directly recruited by BCL6 transcriptional repressor". The Journal of Biological Chemistry 277 (24): 22045–52. doi:10.1074/jbc.M201736200. PMID 11929873.
• Bryant H, Farrell PJ (Oct 2002). "Signal Transduction and Transcription Factor Modification during Reactivation of Epstein-Barr Virus from Latency". Journal of Virology 76 (20): 10290–8. doi:10.1128/JVI.76.20.10290-10298.2002. PMC 136559. PMID 12239305.
• Xiao H, Chung J, Kao HY, Yang YC (Mar 2003). "Tip60 is a co-repressor for STAT3". The Journal of Biological Chemistry 278 (13): 11197–204. doi:10.1074/jbc.M210816200. PMID 12551922.
• Dequiedt F, Kasler H, Fischle W, Kiermer V, Weinstein M, Herndier BG, Verdin E (May 2003). "HDAC7, a thymus-specific class II histone deacetylase, regulates Nur77 transcription and TCR-mediated apoptosis". Immunity 18 (5): 687–98. doi:10.1016/S1074-7613(03)00109-2. PMID 12753745.
• Lee CH, Chawla A, Urbiztondo N, Liao D, Boisvert WA, Evans RM, Curtiss LK (Oct 2003). "Transcriptional repression of atherogenic inflammation: modulation by PPARdelta". Science 302 (5644): 453–7. doi:10.1126/science.1087344. PMID 12970571.
• Li X, Song S, Liu Y, Ko SH, Kao HY (Aug 2004). "Phosphorylation of the histone deacetylase 7 modulates its stability and association with 14-3-3 proteins". The Journal of Biological Chemistry 279 (33): 34201–8. doi:10.1074/jbc.M405179200. PMID 15166223.
• Kato H, Tamamizu-Kato S, Shibasaki F (Oct 2004). "Histone deacetylase 7 associates with hypoxia-inducible factor 1alpha and increases transcriptional activity". The Journal of Biological Chemistry 279 (40): 41966–74. doi:10.1074/jbc.M406320200. PMID 15280364.
• Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (Aug 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
• Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S, Metalnikov P, O'Donnell P, Taylor P, Taylor L, Zougman A, Woodgett JR, Langeberg LK, Scott JD, Pawson T (Aug 2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Current Biology 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.

External links

• HDAC7A protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)

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