HDAC1

Histone deacetylase 1 (HDAC1) is an enzyme that in humans is encoded by the HDAC1 gene.[5]

HDAC1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4BKX, 5ICN
Identifiers
Aliases	HDAC1, GON-10, HD1, RPD3, RPD3L1, histone deacetylase 1, KDAC1
External IDs	OMIM: 601241 MGI: 108086 HomoloGene: 68426 GeneCards: HDAC1
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1p35.2-p35.1 Start 32,292,083 bp[1] End 32,333,635 bp[1]
Gene location (Mouse) Chr. Chromosome 4 (mouse)[2] Band 4 D2.2|4 63.26 cM Start 129,516,104 bp[2] End 129,542,713 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0000980 RNA polymerase II cis-regulatory region sequence-specific DNA binding • NAD-dependent histone deacetylase activity (H3-K14 specific) • GO:0001106 transcription corepressor activity • RNA polymerase II transcription factor binding • histone deacetylase activity • protein N-terminus binding • GO:0001131, GO:0001151, GO:0001130, GO:0001204 DNA-binding transcription factor activity • protein deacetylase activity • histone deacetylase binding • activating transcription factor binding • transcription regulatory region sequence-specific DNA binding • NF-kappaB binding • deacetylase activity • GO:0001948 protein binding • RNA polymerase II repressing transcription factor binding • nucleosomal DNA binding • enzyme binding • repressing transcription factor binding • hydrolase activity • core promoter sequence-specific DNA binding • p53 binding • transcription factor binding • RNA polymerase II core promoter sequence-specific DNA binding • DNA binding • chromatin binding • Krueppel-associated box domain binding • E-box binding • promoter-specific chromatin binding Cellular component • cytoplasm • NuRD complex • cytosol • histone deacetylase complex • Sin3 complex • nucleoplasm • nuclear chromatin • cell nucleus • chromatin • heterochromatin • transcription factor complex • transcriptional repressor complex • macromolecular complex • neuronal cell body • Sin3-type complex Biological process • hair follicle placode formation • epidermal cell differentiation • chromatin remodeling • regulation of transcription, DNA-templated • rhythmic process • negative regulation of androgen receptor signaling pathway • embryonic digit morphogenesis • positive regulation of receptor biosynthetic process • negative regulation of apoptotic process • blood coagulation • negative regulation of transcription from RNA polymerase II promoter • eyelid development in camera-type eye • circadian regulation of gene expression • negative regulation of gene expression • ATP-dependent chromatin remodeling • positive regulation of transcription, DNA-templated • odontogenesis of dentin-containing tooth • protein deacetylation • histone H4 deacetylation • fungiform papilla formation • negative regulation of myotube differentiation • GO:0022415 viral process • histone deacetylation • negative regulation of canonical Wnt signaling pathway • positive regulation of transcription from RNA polymerase II promoter • transcription, DNA-templated • regulation of signal transduction by p53 class mediator • methylation-dependent chromatin silencing • beta-catenin-TCF complex assembly • covalent chromatin modification • chromatin organization • positive regulation of cell proliferation • negative regulation of transcription, DNA-templated • histone H3 deacetylation • regulation of megakaryocyte differentiation • regulation of transcription from RNA polymerase II promoter • endoderm development • circadian rhythm • hippocampus development • neuron differentiation • negative regulation of I-kappaB kinase/NF-kappaB signaling • positive regulation of oligodendrocyte differentiation • regulation of endopeptidase activity • regulation of amyloid-beta clearance • negative regulation of intrinsic apoptotic signaling pathway Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	3065	433759
Ensembl	ENSG00000116478	ENSMUSG00000028800
UniProt	Q13547	O09106
RefSeq (mRNA)	NM_004964	NM_008228
RefSeq (protein)	NP_004955	NP_032254
Location (UCSC)	Chr 1: 32.29 – 32.33 Mb	Chr 4: 129.52 – 129.54 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

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 MTA2, it deacetylates p53 and modulates its effect on cell growth and apoptosis.[6]

Model organisms

Hdac1 knockout mouse phenotype

Characteristic	Phenotype
Homozygote viability	Abnormal
Recessive lethal study	Abnormal
Fertility	Normal
Body weight	Normal
Anxiety	Normal
Neurological assessment	Normal
Grip strength	Normal
Hot plate	Normal
Dysmorphology	Normal
Indirect calorimetry	Normal
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Normal
Body temperature	Normal
Eye morphology	Normal
Clinical chemistry	Normal
Haematology	Normal
Peripheral blood lymphocytes	Normal
Micronucleus test	Normal
Heart weight	Normal
Brain histopathology	Normal
Eye Histopathology	Normal
Salmonella infection	Normal[7]
Citrobacter infection	Normal[8]
All tests and analysis from[9][10]

Model organisms have been used in the study of HDAC1 function. A conditional knockout mouse line, called Hdac1^{tm1a(EUCOMM)Wtsi}[11][12] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists — at the Wellcome Trust Sanger Institute.[13][14][15] Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[9][16] Twenty five tests were carried out and two phenotypes were reported. A reduced number of homozygous mutant embryos were identified during gestation, and none survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice, and no significant abnormalities were observed in these animals.[9]

Interactions

HDAC1 has been shown to interact with:

• Androgen receptor,[17]
• BCL6,[18][19]
• BTG2,[20][21]
• BUB1B,[22]
• BUB1,[22]
• BUB3,[22]
• CBFA2T3,[23][24]
• CDC20,[22]
• CDH1,[22]
• CHD3,[25][26]
• CHD4,[25][27][28]
• COUP-TFII,[29]
• CTBP1,[30][31][32]
• DDX17,[33]
• DDX5,[33]
• DNMT3A,[34]
• DNMT3L,[35][36]
• Death-associated protein 6,[37]
• EED,[38]
• EVI1,[39][40]
• EZH2,[38]
• FKBP3,[41]
• GATA1,[42]
• HMG20B,[43]
• HSPA4,[44]
• HUS1,[45]
• Histone deacetylase 2,[25][27][38][43][44][46][47][48][49][50][51][52][53]
• Homeobox protein TGIF1,[30][54]
• Host cell factor C1,[55]
• IFRD1,[56]
• IKZF1,[57][58]
• ING1,[26][59]
• MBD3,[51][60][61]
• MIER1,[62]
• MLL,[63]
• MTA1,[27][64]
• MTA2,[27][51][65][66]
• Mad1,[22]
• Mdm2,[67]
• Methyl-CpG-binding domain protein 2,[51][68][69]
• Mothers against decapentaplegic homolog 2,[70]
• MyoD,[71][72]
• NFKB1,[73]
• Nuclear receptor co-repressor 2,[46][74]
• P21,[75]
• PCNA,[76]
• PHF21A,[43][77]
• Prohibitin,[78][79]
• Promyelocytic leukemia protein,[80][81]
• RAD9A,[45]
• RBBP4,[27][28][51][52][53][65][68][82][83][84][85]
• RBBP7,[27][51][53][68]
• RCOR1,[43][65]
• RELA,[50][73][86]
• RFC1,[87]
• Retinoblastoma protein,[71][79][88][89][90][91][92]
• Retinoblastoma-like protein 1,[88][89]
• Retinoblastoma-like protein 2,[88][93]
• SAP30,[26][51][94][95][96][97]
• SATB1,[66]
• SIN3A,[25][26][27][28][51][52][65][66][82][83][98][99][100][101]
• SIN3B,[51][57]
• SPEN,[102]
• SUDS3,[98][103]
• SUV39H1,[104]
• Sp1 transcription factor,[83][105][106][107]
• TOP2A,[108][109]
• TOP2B,[108][109] and
• Zinc finger and BTB domain-containing protein 16.[18][110][111]

See also

• Histone deacetylase
• Histone deacetylase inhibitor

References

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Further reading

• Wolffe AP (April 1996). "Histone deacetylase: a regulator of transcription". Science. 272 (5260): 371–2. doi:10.1126/science.272.5260.371. PMID 8602525.
• Ahringer J (August 2000). "NuRD and SIN3 histone deacetylase complexes in development". Trends in Genetics. 16 (8): 351–6. doi:10.1016/S0168-9525(00)02066-7. PMID 10904264.
• 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.
• Zhang Y, Dufau ML (June 2003). "Dual mechanisms of regulation of transcription of luteinizing hormone receptor gene by nuclear orphan receptors and histone deacetylase complexes" (PDF). The Journal of Steroid Biochemistry and Molecular Biology. 85 (2–5): 401–14. doi:10.1016/S0960-0760(03)00230-9. PMID 12943729.
• Stevens M, De Clercq E, Balzarini J (September 2006). "The regulation of HIV-1 transcription: molecular targets for chemotherapeutic intervention". Medicinal Research Reviews. 26 (5): 595–625. doi:10.1002/med.20081. PMID 16838299.
• Hijmans EM, Voorhoeve PM, Beijersbergen RL, van 't Veer LJ, Bernards R (June 1995). "E2F-5, a new E2F family member that interacts with p130 in vivo". Molecular and Cellular Biology. 15 (6): 3082–9. doi:10.1128/mcb.15.6.3082. PMC 230539. PMID 7760804.
• Maruyama K, Sugano S (January 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.
• Margolis DM, Somasundaran M, Green MR (February 1994). "Human transcription factor YY1 represses human immunodeficiency virus type 1 transcription and virion production". Journal of Virology. 68 (2): 905–10. PMC 236527. PMID 8289393.
• Furukawa Y, Kawakami T, Sudo K, Inazawa J, Matsumine A, Akiyama T, Nakamura Y (1996). "Isolation and mapping of a human gene (RPD3L1) that is homologous to RPD3, a transcription factor in Saccharomyces cerevisiae". Cytogenetics and Cell Genetics. 73 (1–2): 130–3. doi:10.1159/000134323. PMID 8646880.
• Hassig CA, Fleischer TC, Billin AN, Schreiber SL, Ayer DE (May 1997). "Histone deacetylase activity is required for full transcriptional repression by mSin3A". Cell. 89 (3): 341–7. doi:10.1016/S0092-8674(00)80214-7. PMID 9150133.
• Laherty CD, Yang WM, Sun JM, Davie JR, Seto E, Eisenman RN (May 1997). "Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression". Cell. 89 (3): 349–56. doi:10.1016/S0092-8674(00)80215-9. PMID 9150134.
• Zhang Y, Iratni R, Erdjument-Bromage H, Tempst P, Reinberg D (May 1997). "Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex". Cell. 89 (3): 357–64. doi:10.1016/S0092-8674(00)80216-0. PMID 9150135.
• Romerio F, Gabriel MN, Margolis DM (December 1997). "Repression of human immunodeficiency virus type 1 through the novel cooperation of human factors YY1 and LSF". Journal of Virology. 71 (12): 9375–82. PMC 230241. PMID 9371597.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 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.
• Brehm A, Miska EA, McCance DJ, Reid JL, Bannister AJ, Kouzarides T (February 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, Robin P, Lorain S, Le Villain JP, Troalen F, Trouche D, Harel-Bellan A (February 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, Shao W, Miller WH, Evans RM (February 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 (February 1998). "Rb interacts with histone deacetylase to repress transcription". Cell. 92 (4): 463–73. doi:10.1016/S0092-8674(00)80940-X. PMID 9491888.

External links

• HDAC1+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)