HDAC1

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; OMA:HDAC1 - orthologs
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 129,409,897 bp [2] End 129,436,506 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in mucosa of colon mucosa of sigmoid colon mucosa of transverse colon epithelium of nasopharynx rectum lymph node pylorus right uterine tube cecum gums Top expressed in tail of embryo genital tubercle morula ventricular zone bone marrow yolk sac thymus embryo blastocyst placenta More reference expression data BioGPS More reference expression data
Gene ontology Molecular function RNA polymerase II cis-regulatory region sequence-specific DNA binding NAD-dependent histone deacetylase activity (H3-K14 specific) transcription corepressor activity histone deacetylase activity protein N-terminus binding DNA-binding transcription factor activity protein deacetylase activity histone deacetylase binding transcription cis-regulatory region binding NF-kappaB binding deacetylase activity protein binding nucleosomal DNA binding enzyme 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 nucleus chromatin heterochromatin transcription regulator complex transcription repressor complex protein-containing complex soma 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 negative regulation of apoptotic process blood coagulation negative regulation of transcription by RNA polymerase II eyelid development in camera-type eye circadian regulation of gene expression negative regulation of gene expression positive regulation of transcription, DNA-templated odontogenesis of dentin-containing tooth protein deacetylation histone H4 deacetylation fungiform papilla formation negative regulation of myotube differentiation viral process histone deacetylation negative regulation of canonical Wnt signaling pathway positive regulation of transcription by RNA polymerase II transcription, DNA-templated regulation of signal transduction by p53 class mediator DNA methylation-dependent heterochromatin assembly beta-catenin-TCF complex assembly chromatin organization positive regulation of cell population proliferation negative regulation of transcription, DNA-templated histone H3 deacetylation regulation of megakaryocyte differentiation regulation of transcription by RNA polymerase II 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: 129.41 – 129.44 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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

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]

Interactions

HDAC1 has been shown to interact with:

• Androgen receptor, ^[7]
• BCL6, ^{[8] [9]}
• BTG2, ^{[10] [11]}
• BUB1B, ^[12]
• BUB1, ^[12]
• BUB3, ^[12]
• CBFA2T3, ^{[13] [14]}
• CDC20, ^[12]
• CDH1, ^[12]
• CHD3, ^{[15] [16]}
• CHD4, ^{[15] [17] [18]}
• COUP-TFII, ^[19]
• CTBP1, ^{[20] [21] [22]}
• DDX17, ^[23]
• DDX5, ^[23]
• DNMT3A, ^[24]
• DNMT3L, ^{[25] [26]}
• Death-associated protein 6, ^[27]
• EED, ^[28]
• EVI1, ^{[29] [30]}
• EZH2, ^[28]
• FKBP3, ^[31]
• GATA1, ^[32]
• HMG20B, ^[33]
• HSPA4, ^[34]
• HUS1, ^[35]
• Histone deacetylase 2, ^{[15] [17] [28] [33] [34] [36] [37] [38] [39] [40] [41] [42] [43]}
• Homeobox protein TGIF1, ^{[20] [44]}
• Host cell factor C1, ^[45]
• IFRD1, ^[46]
• IKZF1, ^{[47] [48]}
• ING1, ^{[16] [49]}
• MBD3, ^{[41] [50] [51]}
• MIER1, ^[52]
• MLL, ^[53]
• MTA1, ^{[17] [54]}
• MTA2, ^{[17] [41] [55] [56]}
• Mad1, ^[12]
• Mdm2, ^[57]
• Methyl-CpG-binding domain protein 2, ^{[41] [58] [59]}
• Mothers against decapentaplegic homolog 2, ^[60]
• MyoD, ^{[61] [62]}
• NFKB1, ^[63]
• Nuclear receptor co-repressor 2, ^{[36] [64]}
• P21, ^[65]
• PCNA, ^[66]
• PHF21A, ^{[33] [67]}
• Prohibitin, ^{[68] [69]}
• Promyelocytic leukemia protein, ^{[70] [71]}
• RAD9A, ^[35]
• RBBP4, ^{[17] [18] [41] [42] [43] [55] [58] [72] [73] [74] [75]}
• RBBP7, ^{[17] [41] [43] [58]}
• RCOR1, ^{[33] [55]}
• RELA, ^{[40] [63] [76]}
• RFC1, ^[77]
• Retinoblastoma protein, ^{[61] [69] [78] [79] [80] [81] [82]}
• Retinoblastoma-like protein 1, ^{[78] [79]}
• Retinoblastoma-like protein 2, ^{[78] [83]}
• SAP30, ^{[16] [41] [84] [85] [86] [87]}
• SATB1, ^[56]
• SIN3A, ^{[15] [16] [17] [18] [41] [42] [55] [56] [72] [73] [88] [89] [90] [91]}
• SIN3B, ^{[41] [47]}
• SPEN, ^[92]
• SUDS3, ^{[88] [93]}
• SUV39H1, ^[94]
• Sp1 transcription factor, ^{[73] [95] [96] [97]}
• TOP2A, ^{[98] [99]}
• TOP2B, ^{[98] [99]} and
• Zinc finger and BTB domain-containing protein 16. ^{[8] [100] [101]}

See also

• Histone deacetylase
• Histone deacetylase inhibitor

References

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2. GRCm38: Ensembl release 89: ENSMUSG00000028800 – Ensembl, May 2017
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Further reading

• Wolffe AP (April 1996). "Histone deacetylase: a regulator of transcription". Science. 272 (5260). New York, N.Y.: 371–372. Bibcode:1996Sci...272..371W. doi:10.1126/science.272.5260.371. PMID   8602525. S2CID   27257723.
• Ahringer J (August 2000). "NuRD and SIN3 histone deacetylase complexes in development". Trends in Genetics. 16 (8): 351–356. 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): 286–293. doi:10.1016/S0168-9525(03)00073-8. hdl: 2268/80861 . 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". The Journal of Steroid Biochemistry and Molecular Biology. 85 (2–5): 401–414. doi:10.1016/S0960-0760(03)00230-9. PMID   12943729. S2CID   28512341.
• 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. PMC   7168390 . 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): 3082–3089. 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): 171–174. 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): 905–910. doi:10.1128/JVI.68.2.905-910.1994. PMC   236527 . PMID   8289393.
• Furukawa Y, Kawakami T, Sudo K, Inazawa J, Matsumine A, Akiyama T, et al. (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): 130–133. 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): 341–347. doi: 10.1016/S0092-8674(00)80214-7 . PMID   9150133. S2CID   14233219.
• 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): 349–356. doi: 10.1016/S0092-8674(00)80215-9 . PMID   9150134. S2CID   13490886.
• 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): 357–364. 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): 9375–9382. doi:10.1128/JVI.71.12.9375-9382.1997. 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): 149–156. 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. Bibcode:1998Natur.391..597B. doi:10.1038/35404. PMID   9468139. S2CID   4326464.
• Magnaghi-Jaulin L, Groisman R, Naguibneva I, Robin P, Lorain S, Le Villain JP, et al. (February 1998). "Retinoblastoma protein represses transcription by recruiting a histone deacetylase". Nature. 391 (6667): 601–605. Bibcode:1998Natur.391..601M. doi:10.1038/35410. PMID   9468140. S2CID   4315457.
• 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): 811–814. Bibcode:1998Natur.391..811L. doi: 10.1038/35895 . PMID   9486654. S2CID   4383951.
• Luo RX, Postigo AA, Dean DC (February 1998). "Rb interacts with histone deacetylase to repress transcription". Cell. 92 (4): 463–473. doi: 10.1016/S0092-8674(00)80940-X . PMID   9491888. S2CID   18857544.

External links

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