Histone deacetylase 2

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
3MAX, 4LXZ, 4LY1

Identifiers

Symbols

HDAC2 ; HD2; RPD3; YAF1

External IDs

OMIM: 605164 MGI: 1097691 HomoloGene: 68187 ChEMBL: 1937 GeneCards: HDAC2 Gene

EC number

3.5.1.98

Gene ontology
Molecular function	• RNA polymerase II core promoter proximal region sequence-specific DNA binding • RNA polymerase II distal enhancer sequence-specific DNA binding • core promoter binding • RNA polymerase II repressing transcription factor binding • chromatin binding • histone deacetylase activity • protein binding • transcription factor binding • deacetylase activity • enzyme binding • heat shock protein binding • nucleosomal DNA binding • NAD-dependent histone deacetylase activity (H3-K14 specific) • protein deacetylase activity • sequence-specific DNA binding • poly(A) RNA binding • NF-kappaB binding
Cellular component	• nuclear chromatin • nucleus • nucleoplasm • cytoplasm • Sin3 complex • NuRD complex • ESC/E(Z) complex • protein complex
Biological process	• negative regulation of transcription from RNA polymerase II promoter • response to amphetamine • cardiac muscle hypertrophy • chromatin organization • chromatin remodeling • maintenance of chromatin silencing • transcription, DNA-templated • blood coagulation • positive regulation of cell proliferation • epidermal cell differentiation • gene expression • positive regulation of epithelial to mesenchymal transition • positive regulation of receptor biosynthetic process • negative regulation of neuron projection development • dendrite development • histone deacetylation • response to caffeine • response to lipopolysaccharide • positive regulation of interleukin-1 production • positive regulation of tumor necrosis factor production • circadian regulation of gene expression • positive regulation of collagen biosynthetic process • cellular response to heat • response to nicotine • regulation of gene expression, epigenetic • response to cocaine • odontogenesis of dentin-containing tooth • response to drug • positive regulation of tyrosine phosphorylation of Stat3 protein • embryonic digit morphogenesis • ATP-dependent chromatin remodeling • negative regulation of apoptotic process • negative regulation of DNA binding • negative regulation of sequence-specific DNA binding transcription factor activity • negative regulation of MHC class II biosynthetic process • negative regulation of cell cycle • negative regulation of gene expression, epigenetic • positive regulation of proteolysis • negative regulation of transcription, DNA-templated • positive regulation of transcription, DNA-templated • positive regulation of transcription from RNA polymerase II promoter • neurotrophin TRK receptor signaling pathway • behavioral response to ethanol • positive regulation of oligodendrocyte differentiation • response to hyperoxia • hair follicle placode formation • negative regulation of dendritic spine development • eyelid development in camera-type eye • fungiform papilla formation • cellular response to hydrogen peroxide • histone H3 deacetylation • histone H4 deacetylation • cellular response to retinoic acid • cellular response to transforming growth factor beta stimulus • cellular response to dopamine • negative regulation of peptidyl-lysine acetylation
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 6:
113.93 – 114.01 Mb

Chr 10:
36.97 – 37 Mb

PubMed search

Histone deacetylase 2 is an enzyme that in humans is encoded by the HDAC2 gene.^[1]

Function

This gene product belongs to the histone deacetylase family. Histone deacetylases act via the formation of large multiprotein complexes and are responsible for the deacetylation of lysine residues on the N-terminal region of the core histones (H2A, H2B, H3 and H4). This protein also forms transcriptional repressor complexes by associating with many different proteins, including YY1, a mammalian zinc-finger transcription factor. Thus it plays an important role in transcriptional regulation, cell cycle progression and developmental events.^[2]

Interactions

Histone deacetylase 2 has been shown to interact with:

Ataxia telangiectasia and Rad3 related,^[3]
BUB3,^[4]
CDC20,^[4]
CDH1,^[4]
CHD3,^[5]^[6]^[7]
CHD4,^[3]^[5]^[6]
DNMT1,^[8]
EED,^[9]
EZH2^[9] and
FKBP3,^[10]
GATA4,^[11]
GTF2I,^[5]^[12]
HDAC10,^[13]
HDAC1,^[5]^[6]^[9]^[13]^[14]^[15]^[16]^[17]^[18]^[19]^[20]^[21]^[22]
HMG20B,^[5]^[15]
HSPA4,^[16]
Host cell factor C1,^[23]
MTA1,^[5]^[14]^[24]
MTA2,^[5]^[14]^[20]
MXD1,^[25]^[26]
Mad1,^[4]
Methyl-CpG-binding domain protein 2,^[20]^[27]^[28]
PHF21A,^[5]^[15]^[29]
PPP1R8,^[30]
RBBP4,^[5]^[6]^[31]^[32]
RCOR1,^[15]^[33]
RELA,^[34]^[35]
Retinoblastoma protein,^[36]
SAP30,^[20]^[37]^[38]
SIN3A,^[5]^[6]^[25]^[31]^[32]^[39]^[40]
SMARCA5,^[7]
SNW1,^[41]
SUV39H1,^[42]
Sp1 transcription factor,^[32]^[43]^[44]
Sp3 transcription factor,^[43]^[44]
TOP2B,^[45] and
YY1.^[46]^[47]^[48]

References

↑ 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.
↑ "Entrez Gene: HDAC2 histone deacetylase 2".
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.
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.
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.
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.
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.
↑ 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.
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.
↑ 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.
↑ "Three-way control of fetal heart-cell proliferation could help regenerate cardiac cells". October 7, 2010.
↑ 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.
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.
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.
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.
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.
↑ 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.
↑ 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.
↑ 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.
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.
↑ 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.
↑ 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.
↑ 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.
↑ 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.
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.
↑ 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.
↑ 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.
↑ 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.
↑ 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.
↑ 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.
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.
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.
↑ 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.
↑ 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.
↑ 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.
↑ 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.
↑ 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.
↑ 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.
↑ 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.
↑ 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.
↑ 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.
↑ 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.
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.
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.
↑ 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.
↑ 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.
↑ 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.
↑ 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.

External links

HDAC2 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)
FactorBook HDAC2

Hydrolases: carbon-nitrogen non-peptide (EC 3.5)

3.5.1: Linear amides / Amidohydrolases	Asparaginase Glutaminase Urease Biotinidase Aspartoacylase Ceramidase Aspartylglucosaminidase Fatty acid amide hydrolase Histone deacetylase Sirtuin

3.5.2: Cyclic amides/ Amidohydrolases	Barbiturase Beta-lactamase

3.5.3: Linear amidines/ Ureohydrolases	Arginase Agmatinase Protein-arginine deiminase

3.5.4: Cyclic amidines/ Aminohydrolases	Guanine deaminase Adenosine deaminase AMP deaminase Inosine monophosphate synthase DCMP deaminase GTP cyclohydrolase I Cytidine deaminase AICDA Activation-induced cytidine deaminase

3.5.5: Nitriles/ Aminohydrolases	Nitrilase

3.5.99: Other	Riboflavinase Thiaminase II

Proteins: enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

This article is issued from Wikipedia - version of the Tuesday, January 26, 2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.

Histone deacetylase 2

Function

Interactions

See also

References

Further reading

External links