Histona deacetilasa 2

Histona deacetilasa 2
Estructuras disponibles
PDB

Buscar ortólogos: PDBe, RCSB

 Lista de códigos PDB
3MAX , 4LXZ , 4LY1
 Estructuras enzimáticas
RCSB PDB, PDBe, PDBsum
Identificadores
Símbolos HDAC2 (HGNC: 4853) RPD3; YAF1
Identificadores
externos
 Bases de datos de enzimas
IntEnz: entrada en IntEnz
BRENDA: entrada en BRENDA
ExPASy: NiceZime view
KEGG: entrada en KEEG
PRIAM: perfil PRIAM
ExplorEnz: entrada en ExplorEnz
MetaCyc: vía metabólica
Número EC 3.5.1.98
Locus Cr. 6 q22.1
Patrón de expresión de ARNm
ancho=250px
Más información
Ortólogos
Especies
Humano Ratón
Entrez
3066 15182
Ensembl
Véase HS Véase MM
UniProt
Q92769 P70288
RefSeq
(ARNm)
NM_001527 NM_008229
RefSeq
(proteína) NCBI
NP_001518 NP_032255
Ubicación (UCSC)
Cr. 6:
114.25 – 114.33 Mb 		Cr. 10:
36.97 – 37 Mb
PubMed (Búsqueda)
[1]


[2]
[editar datos en Wikidata]

La histona deacetilasa 2 (HDAC2) es una enzima codificada en humanos por el gen hdac2.[1]​

Este producto génico pertenece a la familia de las histona deacetilasas, unas proteínas que actúan mediante la formación de grandes complejos multiproteicos y que son responsables de la deacetilación de los residuos de lisina presentes en la región N-terminal de las histonas (H2A, H2B, H3 y H4). Esta proteína también forma complejo represor transcripcional mediante su asociación con diversas proteínas como YY1, un factor de transcripción con dedos de zinc presente en mamíferos. Por ello, HDAC2 juega un importante papel en la regulación de la transcripción, en la progresión del ciclo celular y en procesos de desarrollo.[2]​

Interacciones

La histona deacetilasa 2 ha demostrado ser capaz de interaccionar con:

Véase también

Referencias

  1. ↑ Betz R, Gray SG, Ekstrom C, Larsson C, Ekstrom TJ (Dec de 1998). «Human histone deacetylase 2, HDAC2 (Human RPD3), is localized to 6q21 by radiation hybrid mapping». Genomics 52 (2): 245-6. PMID 9782097. doi:10.1006/geno.1998.5435. 
  2. ↑ «Entrez Gene: HDAC2 histone deacetylase 2». 
  3. ↑ a b c d e f g h i j Hakimi, Mohamed-Ali; Dong Yuanshu, Lane William S, Speicher David W, Shiekhattar Ramin (Feb. de 2003). «A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes». J. Biol. Chem. (United States) 278 (9): 7234-9. ISSN 0021-9258. PMID 12493763. doi:10.1074/jbc.M208992200. 
  4. ↑ a b c d e Tong, J K; Hassig C A, Schnitzler G R, Kingston R E, Schreiber S L (Oct. de 1998). «Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex». Nature (ENGLAND) 395 (6705): 917-21. ISSN 0028-0836. PMID 9804427. doi:10.1038/27699. 
  5. ↑ a b Hakimi, Mohamed-Ali; Bochar Daniel A, Schmiesing John A, Dong Yuanshu, Barak Orr G, Speicher David W, Yokomori Kyoko, Shiekhattar Ramin (Aug. de 2002). «A chromatin remodelling complex that loads cohesin onto human chromosomes». Nature (England) 418 (6901): 994-8. ISSN 0028-0836. PMID 12198550. doi:10.1038/nature01024. 
  6. ↑ a b c Yao, Ya-Li; Yang Wen-Ming (Oct. de 2003). «The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity». J. Biol. Chem. (United States) 278 (43): 42560-8. ISSN 0021-9258. PMID 12920132. doi:10.1074/jbc.M302955200. 
  7. ↑ Mazumdar, A; Wang R A, Mishra S K, Adam L, Bagheri-Yarmand R, Mandal M, Vadlamudi R K, Kumar R (Jan. de 2001). «Transcriptional repression of oestrogen receptor by metastasis-associated protein 1 corepressor». Nat. Cell Biol. (England) 3 (1): 30-7. ISSN 1465-7392. PMID 11146623. doi:10.1038/35050532. 
  8. ↑ Yang, W M; Yao Y L, Seto E (Sep. de 2001). «The FK506-binding protein 25 functionally associates with histone deacetylases and with transcription factor YY1». EMBO J. (England) 20 (17): 4814-25. ISSN 0261-4189. PMID 11532945. doi:10.1093/emboj/20.17.4814. 
  9. ↑ a b Schmidt, D R; Schreiber S L (Nov. de 1999). «Molecular association between ATR and two components of the nucleosome remodeling and deacetylating complex, HDAC2 and CHD4». Biochemistry (UNITED STATES) 38 (44): 14711-7. ISSN 0006-2960. PMID 10545197. 
  10. ↑ a b c d Hakimi, Mohamed-Ali; Bochar Daniel A, Chenoweth Josh, Lane William S, Mandel Gail, Shiekhattar Ramin (mayo. de 2002). «A core-BRAF35 complex containing histone deacetylase mediates repression of neuronal-specific genes». Proc. Natl. Acad. Sci. U.S.A. (United States) 99 (11): 7420-5. ISSN 0027-8424. PMID 12032298. doi:10.1073/pnas.112008599. 
  11. ↑ You, A; Tong J K, Grozinger C M, Schreiber S L (Feb. de 2001). «CoREST is an integral component of the CoREST- human histone deacetylase complex». Proc. Natl. Acad. Sci. U.S.A. (United States) 98 (4): 1454-8. ISSN 0027-8424. PMID 11171972. doi:10.1073/pnas.98.4.1454. 
  12. ↑ Lai, A; Lee J M, Yang W M, DeCaprio J A, Kaelin W G, Seto E, Branton P E (Oct. de 1999). «RBP1 recruits both histone deacetylase-dependent and -independent repression activities to retinoblastoma family proteins». Mol. Cell. Biol. (UNITED STATES) 19 (10): 6632-41. ISSN 0270-7306. PMID 10490602. 
  13. ↑ a b c d Yoon, Young-Mee; Baek Kwan-Hyuck, Jeong Sook-Jung, Shin Hyun-Jin, Ha Geun-Hyoung, Jeon Ae-Hwa, Hwang Sang-Gu, Chun Jang-Soo, Lee Chang-Woo (Sep. de 2004). «WD repeat-containing mitotic checkpoint proteins act as transcriptional repressors during interphase». FEBS Lett. (Netherlands) 575 (1-3): 23-9. ISSN 0014-5793. PMID 15388328. doi:10.1016/j.febslet.2004.07.089. 
  14. ↑ a b Zhang, Ying; Dufau Maria L (Jun. de 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. (England) 85 (2-5): 401-14. ISSN 0960-0760. PMID 12943729. 
  15. ↑ a b c Zhang, Ying; Dufau Maria L (Sep. de 2002). «Silencing of transcription of the human luteinizing hormone receptor gene by histone deacetylase-mSin3A complex». J. Biol. Chem. (United States) 277 (36): 33431-8. ISSN 0021-9258. PMID 12091390. doi:10.1074/jbc.M204417200. 
  16. ↑ a b c van der Vlag, J; Otte A P (Dec. de 1999). «Transcriptional repression mediated by the human polycomb-group protein EED involves histone deacetylation». Nat. Genet. (UNITED STATES) 23 (4): 474-8. ISSN 1061-4036. PMID 10581039. doi:10.1038/70602. 
  17. ↑ Wen, Yu-Der; Cress W Douglas, Roy Ananda L, Seto Edward (Jan. de 2003). «Histone deacetylase 3 binds to and regulates the multifunctional transcription factor TFII-I». J. Biol. Chem. (United States) 278 (3): 1841-7. ISSN 0021-9258. PMID 12393887. doi:10.1074/jbc.M206528200. 
  18. ↑ Wysocka, Joanna; Myers Michael P, Laherty Carol D, Eisenman Robert N, Herr Winship (Apr. de 2003). «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. (United States) 17 (7): 896-911. ISSN 0890-9369. PMID 12670868. doi:10.1101/gad.252103. 
  19. ↑ Iwase, Shigeki; Januma Aya, Miyamoto Kiyoko, Shono Naomi, Honda Arata, Yanagisawa Junn, Baba Tadashi (Sep. de 2004). «Characterization of BHC80 in BRAF-HDAC complex, involved in neuron-specific gene repression». Biochem. Biophys. Res. Commun. (United States) 322 (2): 601-8. ISSN 0006-291X. PMID 15325272. doi:10.1016/j.bbrc.2004.07.163. 
  20. ↑ a b Laherty, C D; Yang W M, Sun J M, Davie J R, Seto E, Eisenman R N (mayo. de 1997). «Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression». Cell (UNITED STATES) 89 (3): 349-56. ISSN 0092-8674. PMID 9150134. 
  21. ↑ Spronk, C A; Tessari M, Kaan A M, Jansen J F, Vermeulen M, Stunnenberg H G, Vuister G W (Dec. de 2000). «The Mad1-Sin3B interaction involves a novel helical fold». Nat. Struct. Biol. (UNITED STATES) 7 (12): 1100-4. ISSN 1072-8368. PMID 11101889. doi:10.1038/81944. 
  22. ↑ a b Fischer, Denise D; Cai Richard, Bhatia Umesh, Asselbergs Fred A M, Song Chuanzheng, Terry Robert, Trogani Nancy, Widmer Roland, Atadja Peter, Cohen Dalia (Feb. de 2002). «Isolation and characterization of a novel class II histone deacetylase, HDAC10». J. Biol. Chem. (United States) 277 (8): 6656-66. ISSN 0021-9258. PMID 11739383. doi:10.1074/jbc.M108055200. 
  23. ↑ Kiernan, Rosemary; Brès Vanessa, Ng Raymond W M, Coudart Marie-Pierre, El Messaoudi Selma, Sardet Claude, Jin Dong-Yan, Emiliani Stephane, Benkirane Monsef (Jan. de 2003). «Post-activation turn-off of NF-kappa B-dependent transcription is regulated by acetylation of p65». J. Biol. Chem. (United States) 278 (4): 2758-66. ISSN 0021-9258. PMID 12419806. doi:10.1074/jbc.M209572200. 
  24. ↑ Yu, Zhiyuan; Zhang Wenzheng, Kone Bruce C (Aug. de 2002). «Histone deacetylases augment cytokine induction of the iNOS gene». J. Am. Soc. Nephrol. (United States) 13 (8): 2009-17. ISSN 1046-6673. PMID 12138131. 
  25. ↑ a b Won, Jaejoon; Yim Jeongbin, Kim Tae Kook (Oct. de 2002). «Sp1 and Sp3 recruit histone deacetylase to repress transcription of human telomerase reverse transcriptase (hTERT) promoter in normal human somatic cells». J. Biol. Chem. (United States) 277 (41): 38230-8. ISSN 0021-9258. PMID 12151407. doi:10.1074/jbc.M206064200. 
  26. ↑ a b Sun, Jian-Min; Chen Hou Yu, Moniwa Mariko, Litchfield David W, Seto Edward, Davie James R (Sep. de 2002). «The transcriptional repressor Sp3 is associated with CK2-phosphorylated histone deacetylase 2». J. Biol. Chem. (United States) 277 (39): 35783-6. ISSN 0021-9258. PMID 12176973. doi:10.1074/jbc.C200378200. 
  27. ↑ Rountree, M R; Bachman K E, Baylin S B (Jul. de 2000). «DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci». Nat. Genet. (UNITED STATES) 25 (3): 269-77. ISSN 1061-4036. PMID 10888872. doi:10.1038/77023. 
  28. ↑ a b Johnson, Colin A; White Darren A, Lavender Jayne S, O'Neill Laura P, Turner Bryan M (Mar. de 2002). «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. (United States) 277 (11): 9590-7. ISSN 0021-9258. PMID 11777905. doi:10.1074/jbc.M107942200. 
  29. ↑ Vaute, Olivier; Nicolas Estelle, Vandel Laurence, Trouche Didier (Jan. de 2002). «Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases». Nucleic Acids Res. (England) 30 (2): 475-81. PMID 11788710. 
  30. ↑ Fischle, Wolfgang; Dequiedt Franck, Hendzel Michael J, Guenther Matthew G, Lazar Mitchell A, Voelter Wolfgang, Verdin Eric (Jan. de 2002). «Enzymatic activity associated with class II HDACs is dependent on a multiprotein complex containing HDAC3 and SMRT/N-CoR». Mol. Cell (United States) 9 (1): 45-57. ISSN 1097-2765. PMID 11804585. 
  31. ↑ Fischle, W; Dequiedt F, Fillion M, Hendzel M J, Voelter W, Verdin E (Sep. de 2001). «Human HDAC7 histone deacetylase activity is associated with HDAC3 in vivo». J. Biol. Chem. (United States) 276 (38): 35826-35. ISSN 0021-9258. PMID 11466315. doi:10.1074/jbc.M104935200. 
  32. ↑ Ashburner, B P; Westerheide S D, Baldwin A S (Oct. de 2001). «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. (United States) 21 (20): 7065-77. ISSN 0270-7306. PMID 11564889. doi:10.1128/MCB.21.20.7065-7077.2001. 
  33. ↑ a b c d Zhang, Y; Ng H H, Erdjument-Bromage H, Tempst P, Bird A, Reinberg D (Aug. de 1999). «Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation». Genes Dev. (UNITED STATES) 13 (15): 1924-35. ISSN 0890-9369. PMID 10444591. 
  34. ↑ Hassig, C A; Tong J K, Fleischer T C, Owa T, Grable P G, Ayer D E, Schreiber S L (Mar. de 1998). «A role for histone deacetylase activity in HDAC1-mediated transcriptional repression». Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 95 (7): 3519-24. ISSN 0027-8424. PMID 9520398. 
  35. ↑ Zhang, Y; Iratni R, Erdjument-Bromage H, Tempst P, Reinberg D (mayo. de 1997). «Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex». Cell (UNITED STATES) 89 (3): 357-64. ISSN 0092-8674. PMID 9150135. 
  36. ↑ Brackertz, Marc; Boeke Joern, Zhang Ru, Renkawitz Rainer (Oct. de 2002). «Two highly related p66 proteins comprise a new family of potent transcriptional repressors interacting with MBD2 and MBD3». J. Biol. Chem. (United States) 277 (43): 40958-66. ISSN 0021-9258. PMID 12183469. doi:10.1074/jbc.M207467200. 
  37. ↑ Ng, H H; Zhang Y, Hendrich B, Johnson C A, Turner B M, Erdjument-Bromage H, Tempst P, Reinberg D, Bird A (Sep. de 1999). «MBD2 is a transcriptional repressor belonging to the MeCP1 histone deacetylase complex». Nat. Genet. (UNITED STATES) 23 (1): 58-61. ISSN 1061-4036. PMID 10471484. doi:10.1038/12659. 
  38. ↑ Fleischer, Tracey C; Yun Ui Jeong, Ayer Donald E (mayo. de 2003). «Identification and characterization of three new components of the mSin3A corepressor complex». Mol. Cell. Biol. (United States) 23 (10): 3456-67. ISSN 0270-7306. PMID 12724404. 
  39. ↑ Yang, Liu; Mei Qi, Zielinska-Kwiatkowska Anna, Matsui Yoshito, Blackburn Michael L, Benedetti Daniel, Krumm Anton A, Taborsky Gerald J, Chansky Howard A (Feb. de 2003). «An ERG (ets-related gene)-associated histone methyltransferase interacts with histone deacetylases 1/2 and transcription co-repressors mSin3A/B». Biochem. J. (England) 369 (Pt 3): 651-7. ISSN 0264-6021. PMID 12398767. doi:10.1042/BJ20020854. 
  40. ↑ Zhang, Y; Sun Z W, Iratni R, Erdjument-Bromage H, Tempst P, Hampsey M, Reinberg D (Jun. de 1998). «SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex». Mol. Cell (UNITED STATES) 1 (7): 1021-31. ISSN 1097-2765. PMID 9651585. 
  41. ↑ Kuzmichev, A; Zhang Y, Erdjument-Bromage H, Tempst P, Reinberg D (Feb. de 2002). «Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1)». Mol. Cell. Biol. (United States) 22 (3): 835-48. ISSN 0270-7306. PMID 11784859. 
  42. ↑ Zhou, S; Fujimuro M, Hsieh J J, Chen L, Hayward S D (Feb. de 2000). «A role for SKIP in EBNA2 activation of CBF1-repressed promoters». J. Virol. (UNITED STATES) 74 (4): 1939-47. ISSN 0022-538X. PMID 10644367. 
  43. ↑ Jin, Qiming; van Eynde Aleyde, Beullens Monique, Roy Nivedita, Thiel Gerald, Stalmans Willy, Bollen Mathieu (Aug. de 2003). «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. (United States) 278 (33): 30677-85. ISSN 0021-9258. PMID 12788942. doi:10.1074/jbc.M302273200. 
  44. ↑ Tsai, S C; Valkov N, Yang W M, Gump J, Sullivan D, Seto E (Nov. de 2000). «Histone deacetylase interacts directly with DNA topoisomerase II». Nat. Genet. (UNITED STATES) 26 (3): 349-53. ISSN 1061-4036. PMID 11062478. doi:10.1038/81671. 
  45. ↑ Yang, W M; Yao Y L, Sun J M, Davie J R, Seto E (Oct. de 1997). «Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family». J. Biol. Chem. (UNITED STATES) 272 (44): 28001-7. ISSN 0021-9258. PMID 9346952. 
  46. ↑ Yao, Y L; Yang W M, Seto E (Sep. de 2001). «Regulation of transcription factor YY1 by acetylation and deacetylation». Mol. Cell. Biol. (United States) 21 (17): 5979-91. ISSN 0270-7306. PMID 11486036. 
  47. ↑ Kalenik, J L; Chen D, Bradley M E, Chen S J, Lee T C (Feb. de 1997). «Yeast two-hybrid cloning of a novel zinc finger protein that interacts with the multifunctional transcription factor YY1». Nucleic Acids Res. (ENGLAND) 25 (4): 843-9. ISSN 0305-1048. PMID 9016636. 

Enlaces externos