WikiSort.ru - Не сортированное

ПОИСК ПО САЙТУ | о проекте
Гистондеацетилаза 2
Доступные структуры
PDB Поиск ортологов: PDBe, RCSB
Идентификаторы
СимволHDAC2 ; HD2; RPD3; YAF1
Внешние IDOMIM: 605164 MGI: 1097691 HomoloGene: 68187 ChEMBL: 1937 GeneCards: HDAC2 Gene
номер EC3.5.1.98
Профиль экспрессии РНК
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

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

Функция

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

Гистондезацетилаза 2 взаимодействует с:

Примечания

  1. Betz R, Gray SG, Ekström C, Larsson C, Ekström TJ (December 1998). “Human histone deacetylase 2, HDAC2 (Human RPD3), is localized to 6q21 by radiation hybrid mapping”. Genomics. 52 (2): 245—6. DOI:10.1006/geno.1998.5435. PMID 9782097.
  2. Entrez Gene: HDAC2 histone deacetylase 2.
  3. 1 2 Schmidt DR, Schreiber SL. “Molecular association between ATR and two components of the nucleosome remodeling and deacetylating complex, HDAC2 and CHD4”. Biochemistry. 38 (44): 14711–7. DOI:10.1021/bi991614n. PMID 10545197.
  4. 1 2 3 4 Yoon YM, Baek KH, Jeong SJ, Shin HJ, Ha GH, Jeon AH, Hwang SG, Chun JS, Lee CW. “WD repeat-containing mitotic checkpoint proteins act as transcriptional repressors during interphase”. FEBS Lett. 575 (1–3): 23–9. DOI:10.1016/j.febslet.2004.07.089. PMID 15388328.
  5. 1 2 3 4 5 6 7 8 9 10 Hakimi MA, Dong Y, Lane WS, Speicher DW, Shiekhattar R. “A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes”. J. Biol. Chem. 278 (9): 7234–9. DOI:10.1074/jbc.M208992200. PMID 12493763.
  6. 1 2 3 4 5 Tong JK, Hassig CA, Schnitzler GR, Kingston RE, Schreiber SL. “Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex”. Nature. 395 (6705): 917–21. DOI:10.1038/27699. PMID 9804427.
  7. 1 2 Hakimi MA, Bochar DA, Schmiesing JA, Dong Y, Barak OG, Speicher DW, Yokomori K, Shiekhattar R. “A chromatin remodelling complex that loads cohesin onto human chromosomes”. Nature. 418 (6901): 994–8. DOI:10.1038/nature01024. PMID 12198550.
  8. Rountree MR, Bachman KE, Baylin SB. “DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci”. Nat. Genet. 25 (3): 269–77. DOI:10.1038/77023. PMID 10888872.
  9. 1 2 3 van der Vlag J, Otte AP. “Transcriptional repression mediated by the human polycomb-group protein EED involves histone deacetylation”. Nat. Genet. 23 (4): 474–8. DOI:10.1038/70602. PMID 10581039.
  10. Yang WM, Yao YL, Seto E. “The FK506-binding protein 25 functionally associates with histone deacetylases and with transcription factor YY1”. EMBO J. 20 (17): 4814–25. DOI:10.1093/emboj/20.17.4814. PMC 125595. PMID 11532945.
  11. Three-way control of fetal heart-cell proliferation could help regenerate cardiac cells (October 7, 2010).
  12. Wen YD, Cress WD, Roy AL, Seto E. “Histone deacetylase 3 binds to and regulates the multifunctional transcription factor TFII-I”. J. Biol. Chem. 278 (3): 1841–7. DOI:10.1074/jbc.M206528200. PMID 12393887.
  13. 1 2 Fischer DD, Cai R, Bhatia U, Asselbergs FA, Song C, Terry R, Trogani N, Widmer R, Atadja P, Cohen D. “Isolation and characterization of a novel class II histone deacetylase, HDAC10”. J. Biol. Chem. 277 (8): 6656–66. DOI:10.1074/jbc.M108055200. PMID 11739383.
  14. 1 2 3 Yao YL, Yang WM. “The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity”. J. Biol. Chem. 278 (43): 42560–8. DOI:10.1074/jbc.M302955200. PMID 12920132.
  15. 1 2 3 4 Hakimi MA, Bochar DA, Chenoweth J, Lane WS, Mandel G, Shiekhattar R. “A core-BRAF35 complex containing histone deacetylase mediates repression of neuronal-specific genes”. Proc. Natl. Acad. Sci. U.S.A. 99 (11): 7420–5. DOI:10.1073/pnas.112008599. PMC 124246. PMID 12032298.
  16. 1 2 Johnson CA, White DA, Lavender JS, O'Neill LP, Turner BM. “Human class I histone deacetylase complexes show enhanced catalytic activity in the presence of ATP and co-immunoprecipitate with the ATP-dependent chaperone protein Hsp70”. J. Biol. Chem. 277 (11): 9590–7. DOI:10.1074/jbc.M107942200. PMID 11777905.
  17. Fischle W, Dequiedt F, Hendzel MJ, Guenther MG, Lazar MA, Voelter W, Verdin E. “Enzymatic activity associated with class II HDACs is dependent on a multiprotein complex containing HDAC3 and SMRT/N-CoR”. Mol. Cell. 9 (1): 45–57. DOI:10.1016/s1097-2765(01)00429-4. PMID 11804585.
  18. Fischle W, Dequiedt F, Fillion M, Hendzel MJ, Voelter W, Verdin E. “Human HDAC7 histone deacetylase activity is associated with HDAC3 in vivo”. J. Biol. Chem. 276 (38): 35826–35. DOI:10.1074/jbc.M104935200. PMID 11466315.
  19. Ashburner BP, Westerheide SD, Baldwin AS. “The p65 (RelA) subunit of NF-kappaB interacts with the histone deacetylase (HDAC) corepressors HDAC1 and HDAC2 to negatively regulate gene expression”. Mol. Cell. Biol. 21 (20): 7065–77. DOI:10.1128/MCB.21.20.7065-7077.2001. PMC 99882. PMID 11564889.
  20. 1 2 3 4 Zhang Y, Ng HH, Erdjument-Bromage H, Tempst P, Bird A, Reinberg D. “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. PMC 316920. PMID 10444591.
  21. Hassig CA, Tong JK, Fleischer TC, Owa T, Grable PG, Ayer DE, Schreiber SL. “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. PMC 19868. PMID 9520398.
  22. Zhang Y, Iratni R, Erdjument-Bromage H, Tempst P, Reinberg D. “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.
  23. Wysocka J, Myers MP, Laherty CD, Eisenman RN, Herr W. “Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1”. Genes Dev. 17 (7): 896–911. DOI:10.1101/gad.252103. PMC 196026. PMID 12670868.
  24. Mazumdar A, Wang RA, Mishra SK, Adam L, Bagheri-Yarmand R, Mandal M, Vadlamudi RK, Kumar R. “Transcriptional repression of oestrogen receptor by metastasis-associated protein 1 corepressor”. Nat. Cell Biol. 3 (1): 30–7. DOI:10.1038/35050532. PMID 11146623.
  25. 1 2 Laherty CD, Yang WM, Sun JM, Davie JR, Seto E, Eisenman RN. “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.
  26. Spronk CA, Tessari M, Kaan AM, Jansen JF, Vermeulen M, Stunnenberg HG, Vuister GW. “The Mad1-Sin3B interaction involves a novel helical fold”. Nat. Struct. Biol. 7 (12): 1100–4. DOI:10.1038/81944. PMID 11101889.
  27. Brackertz M, Boeke J, Zhang R, Renkawitz R. “Two highly related p66 proteins comprise a new family of potent transcriptional repressors interacting with MBD2 and MBD3”. J. Biol. Chem. 277 (43): 40958–66. DOI:10.1074/jbc.M207467200. PMID 12183469.
  28. Ng HH, Zhang Y, Hendrich B, Johnson CA, Turner BM, Erdjument-Bromage H, Tempst P, Reinberg D, Bird A. “MBD2 is a transcriptional repressor belonging to the MeCP1 histone deacetylase complex”. Nat. Genet. 23 (1): 58–61. DOI:10.1038/12659. PMID 10471499.
  29. Iwase S, Januma A, Miyamoto K, Shono N, Honda A, Yanagisawa J, Baba T. “Characterization of BHC80 in BRAF-HDAC complex, involved in neuron-specific gene repression”. Biochem. Biophys. Res. Commun. 322 (2): 601–8. DOI:10.1016/j.bbrc.2004.07.163. PMID 15325272.
  30. Jin Q, van Eynde A, Beullens M, Roy N, Thiel G, Stalmans W, Bollen M. “The protein phosphatase-1 (PP1) regulator, nuclear inhibitor of PP1 (NIPP1), interacts with the polycomb group protein, embryonic ectoderm development (EED), and functions as a transcriptional repressor”. J. Biol. Chem. 278 (33): 30677–85. DOI:10.1074/jbc.M302273200. PMID 12788942.
  31. 1 2 Zhang Y, Dufau ML. “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.
  32. 1 2 3 Zhang Y, Dufau ML. “Silencing of transcription of the human luteinizing hormone receptor gene by histone deacetylase-mSin3A complex”. J. Biol. Chem. 277 (36): 33431–8. DOI:10.1074/jbc.M204417200. PMID 12091390.
  33. You A, Tong JK, Grozinger CM, Schreiber SL. “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. PMC 29278. PMID 11171972.
  34. Kiernan R, Brès V, Ng RW, Coudart MP, El Messaoudi S, Sardet C, Jin DY, Emiliani S, Benkirane M. “Post-activation turn-off of NF-kappa B-dependent transcription is regulated by acetylation of p65”. J. Biol. Chem. 278 (4): 2758–66. DOI:10.1074/jbc.M209572200. PMID 12419806.
  35. Yu Z, Zhang W, Kone BC. “Histone deacetylases augment cytokine induction of the iNOS gene”. J. Am. Soc. Nephrol. 13 (8): 2009–17. DOI:10.1097/01.asn.0000024253.59665.f1. PMID 12138131.
  36. Lai A, Lee JM, Yang WM, DeCaprio JA, Kaelin WG, Seto E, Branton PE. “RBP1 recruits both histone deacetylase-dependent and -independent repression activities to retinoblastoma family proteins”. Mol. Cell. Biol. 19 (10): 6632–41. PMC 84642. PMID 10490602.
  37. Zhang Y, Sun ZW, Iratni R, Erdjument-Bromage H, Tempst P, Hampsey M, Reinberg D. “SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex”. Mol. Cell. 1 (7): 1021–31. DOI:10.1016/s1097-2765(00)80102-1. PMID 9651585.
  38. Kuzmichev A, Zhang Y, Erdjument-Bromage H, Tempst P, Reinberg D. “Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1)”. Mol. Cell. Biol. 22 (3): 835–48. DOI:10.1128/mcb.22.3.835-848.2002. PMC 133546. PMID 11784859.
  39. Fleischer TC, Yun UJ, Ayer DE. “Identification and characterization of three new components of the mSin3A corepressor complex”. Mol. Cell. Biol. 23 (10): 3456–67. DOI:10.1128/mcb.23.10.3456-3467.2003. PMC 164750. PMID 12724404.
  40. Yang L, Mei Q, Zielinska-Kwiatkowska A, Matsui Y, Blackburn ML, Benedetti D, Krumm AA, Taborsky GJ, Chansky HA. “An ERG (ets-related gene)-associated histone methyltransferase interacts with histone deacetylases 1/2 and transcription co-repressors mSin3A/B”. Biochem. J. 369 (Pt 3): 651–7. DOI:10.1042/BJ20020854. PMC 1223118. PMID 12398767.
  41. Zhou S, Fujimuro M, Hsieh JJ, Chen L, Hayward SD. “A role for SKIP in EBNA2 activation of CBF1-repressed promoters”. J. Virol. 74 (4): 1939–47. DOI:10.1128/jvi.74.4.1939-1947.2000. PMC 111672. PMID 10644367.
  42. Vaute O, Nicolas E, Vandel L, Trouche D. “Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases”. Nucleic Acids Res. 30 (2): 475–81. DOI:10.1093/nar/30.2.475. PMC 99834. PMID 11788710.
  43. 1 2 Won J, Yim J, Kim TK. “Sp1 and Sp3 recruit histone deacetylase to repress transcription of human telomerase reverse transcriptase (hTERT) promoter in normal human somatic cells”. J. Biol. Chem. 277 (41): 38230–8. DOI:10.1074/jbc.M206064200. PMID 12151407.
  44. 1 2 Sun JM, Chen HY, Moniwa M, Litchfield DW, Seto E, Davie JR. “The transcriptional repressor Sp3 is associated with CK2-phosphorylated histone deacetylase 2”. J. Biol. Chem. 277 (39): 35783–6. DOI:10.1074/jbc.C200378200. PMID 12176973.
  45. Tsai SC, Valkov N, Yang WM, Gump J, Sullivan D, Seto E. “Histone deacetylase interacts directly with DNA topoisomerase II”. Nat. Genet. 26 (3): 349–53. DOI:10.1038/81671. PMID 11062478.
  46. Yang WM, Yao YL, Sun JM, Davie JR, Seto E. “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.
  47. Yao YL, Yang WM, Seto E. “Regulation of transcription factor YY1 by acetylation and deacetylation”. Mol. Cell. Biol. 21 (17): 5979–91. DOI:10.1128/mcb.21.17.5979-5991.2001. PMC 87316. PMID 11486036.
  48. Kalenik JL, Chen D, Bradley ME, Chen SJ, Lee TC. “Yeast two-hybrid cloning of a novel zinc finger protein that interacts with the multifunctional transcription factor YY1”. Nucleic Acids Res. 25 (4): 843–9. DOI:10.1093/nar/25.4.843. PMC 146511. PMID 9016636.

Литература

Данная страница на сайте WikiSort.ru содержит текст со страницы сайта "Википедия".

Если Вы хотите её отредактировать, то можете сделать это на странице редактирования в Википедии.

Если сделанные Вами правки не будут кем-нибудь удалены, то через несколько дней они появятся на сайте WikiSort.ru .




Текст в блоке "Читать" взят с сайта "Википедия" и доступен по лицензии Creative Commons Attribution-ShareAlike; в отдельных случаях могут действовать дополнительные условия.

Другой контент может иметь иную лицензию. Перед использованием материалов сайта WikiSort.ru внимательно изучите правила лицензирования конкретных элементов наполнения сайта.

2019-2025
WikiSort.ru - проект по пересортировке и дополнению контента Википедии