Гистондеацетилаза 2

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Гистондеацетилаза 2
Доступные структуры
PDB Поиск ортологов: PDBe, RCSB
Идентификаторы
СимволHDAC2 ; HD2; RPD3; YAF1
Внешние IDOMIM: 605164 MGI1097691 HomoloGene68187 ChEMBL: 1937 GeneCards: HDAC2 Gene
номер EC3.5.1.98
Профиль экспрессии РНК
PBB GE HDAC2 201833 at tn.png
Больше информации
Ортологи
ВидЧеловекМышь
Entrez306615182
EnsemblENSG00000196591ENSMUSG00000019777
UniProtQ92769P70288
RefSeq (мРНК)NM_001527NM_008229
RefSeq (белок)NP_001518NP_032255
Локус (UCSC)Chr 6:
114.25 – 114.33 Mb
Chr 10:
36.97 – 37 Mb
Поиск в PubMed[1][2]

Гистондеацетилаза 2  — фермент из семейства деацетилаз гистонов, кодируемый у человека геном HDAC2 .[1]

Функция[править | править код]

Продукт гена HDAC2 относится к семейству деацетилаз гистонов. Гистондеацетилазы работают в составе крупных мультибелковых комплексов и отвечают за деацетилирование остатков лизина на N-концевой области кóровых гистонов (H2A, H2B, H3 и H4). Этот белок также формирует комплексы транскрипционных репрессоров, связываясь с различными белками, в том числе YY1, одним из фактором транскрипции млекопитающих. Гистондеацетилаза 2 играет важную роль в регуляции транскрипции, клеточного цикла и в развитии.[2]

Взаимодействия[править | править код]

Гистондезацетилаза 2 взаимодействует с:

Примечания[править | править код]

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  2. Entrez Gene: HDAC2 histone deacetylase 2.
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  31. 1 2 «Dual mechanisms of regulation of transcription of luteinizing hormone receptor gene by nuclear orphan receptors and histone deacetylase complexes». J. Steroid Biochem. Mol. Biol. 85 (2-5): 401-14. DOI:10.1016/s0960-0760(03)00230-9. PMID 12943729.
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  33. «CoREST is an integral component of the CoREST- human histone deacetylase complex». Proc. Natl. Acad. Sci. U.S.A. 98 (4): 1454-8. DOI:10.1073/pnas.98.4.1454. PMID 11171972.
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  36. «RBP1 recruits both histone deacetylase-dependent and -independent repression activities to retinoblastoma family proteins». Mol. Cell. Biol. 19 (10): 6632-41. PMID 10490602.
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Литература[править | править код]

  • (2000) «NuRD and SIN3 histone deacetylase complexes in development». Trends Genet. 16 (8): 351–6. DOI:10.1016/S0168-9525(00)02066-7. PMID 10904264.
  • (2003) «Class II histone deacetylases: versatile regulators». Trends Genet. 19 (5): 286–93. DOI:10.1016/S0168-9525(03)00073-8. PMID 12711221.
  • (2003) «Dual mechanisms of regulation of transcription of luteinizing hormone receptor gene by nuclear orphan receptors and histone deacetylase complexes». J. Steroid Biochem. Mol. Biol. 85 (2–5): 401–14. DOI:10.1016/S0960-0760(03)00230-9. PMID 12943729.
  • (1996) «Isolation and mapping of a human gene (RPD3L1) that is homologous to RPD3, a transcription factor in Saccharomyces cerevisiae». Cytogenet. Cell Genet. 73 (1–2): 130–3. DOI:10.1159/000134323. PMID 8646880.
  • (1996) «Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global regulator RPD3». Proc. Natl. Acad. Sci. U.S.A. 93 (23): 12845–50. DOI:10.1073/pnas.93.23.12845. PMID 8917507.
  • (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.
  • (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.
  • (1997) «Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family». J. Biol. Chem. 272 (44): 28001–7. DOI:10.1074/jbc.272.44.28001. PMID 9346952.
  • (1998) «A role for histone deacetylase activity in HDAC1-mediated transcriptional repression». Proc. Natl. Acad. Sci. U.S.A. 95 (7): 3519–24. DOI:10.1073/pnas.95.7.3519. PMID 9520398.
  • (1998) «Identification and mapping of human histone acetylation modifier gene homologues». Genomics 51 (2): 262–9. DOI:10.1006/geno.1998.5370. PMID 9722949.
  • (1998) «The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities». Cell 95 (2): 279–89. DOI:10.1016/S0092-8674(00)81758-4. PMID 9790534.
  • (1998) «Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex». Nature 395 (6705): 917–21. DOI:10.1038/27699. PMID 9804427.
  • (1999) «CIR, a corepressor linking the DNA binding factor CBF1 to the histone deacetylase complex». Proc. Natl. Acad. Sci. U.S.A. 96 (1): 23–8. DOI:10.1073/pnas.96.1.23. PMID 9874765.
  • (1999) «BRCA1 interacts with components of the histone deacetylase complex». Proc. Natl. Acad. Sci. U.S.A. 96 (9): 4983–8. DOI:10.1073/pnas.96.9.4983. PMID 10220405.
  • (1999) «Repression by Ikaros and Aiolos is mediated through histone deacetylase complexes». EMBO J. 18 (11): 3090–100. DOI:10.1093/emboj/18.11.3090. PMID 10357820.
  • (1999) «Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation». Genes Dev. 13 (15): 1924–35. DOI:10.1101/gad.13.15.1924. PMID 10444591.
  • (1999) «MBD2 is a transcriptional repressor belonging to the MeCP1 histone deacetylase complex». Nat. Genet. 23 (1): 58–61. DOI:10.1038/12659. PMID 10471499.
  • (1999) «Mi-2 complex couples DNA methylation to chromatin remodelling and histone deacetylation». Nat. Genet. 23 (1): 62–6. DOI:10.1038/12664. PMID 10471500.
  • (2000) «RBP1 Recruits Both Histone Deacetylase-Dependent and -Independent Repression Activities to Retinoblastoma Family Proteins». Mol. Cell. Biol. 19 (10): 6632–41. PMID 10490602.