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HDAC2 (histone deacetylase 2)

Written2010-01Santiago Ropero, Manel Esteller
Departamento de Bioquimica y Biologia Molecular, Facultad de Medicina, Universidad de Alcala, 28871 Alcala de Henares, Madrid, Spain (SR); Cancer Epigenetics, Biology Program (PEBC), Catalan Institute of Oncology (ICO), Bellvitge Institute for Biomedical Research (IDIBELL), 08907 L'Hospitalet, Barcelona, Catalonia, Spain (ME)
Updated2014-01Hyun Jin Bae, Suk Woo Nam
Department of Pathology, College of Medicine, Functional RNomics Research Center, The Catholic University of Korea, Banpo-dong, Seocho-gu, Seoul, Korea

(Note : for Links provided by Atlas : click)

Identity

Alias_symbol (synonym)RPD3
YAF1
Other aliasEC 3.5.1.98
HD2
HGNC (Hugo) HDAC2
LocusID (NCBI) 3066
Atlas_Id 40803
Location 6q21  [Link to chromosome band 6q21]
Location_base_pair Starts at 113936156 and ends at 113971195 bp from pter ( according to hg19-Feb_2009)  [Mapping HDAC2.png]
Fusion genes
(updated 2016)
HDAC2 (6q21) / AK9 (6q21)HDAC2 (6q21) / MATN2 (8q22.1)HDAC2 (6q21) / TRDN (6q22.31)
UCHL5 (1q31.2) / HDAC2 (6q21)

DNA/RNA

 
Description The HDAC2 gene is composed of 14 exons that span 35.029 bp of genomic DNA.
Transcription The length of the transcribed mRNA is about 6659 bp.
Pseudogene No pseudogene has been described.

Protein

 
Description There are two proteins variants of 488 and 582 aa due to distinct pre-mRNA splicing events. The N-terminal tail of the protein contains the catalytic domain that comprises most of the protein. The N-terminal domain also has a HDAC association domain (HAD) essential for homo- and heterodimerization. A coiled-coil domain essential for protein-protein interactions is present at the C-terminal tail. It also contains three phosphorylation sites at Ser394, Ser422 and Ser424, and two S-nitrosylation sites at Cys262 and Cys274.
Expression Widely expressed.
Localisation Nucleus.
Function HDAC2 belongs to class I histone deacetylases that also comprise HDAC1, HDAC3 and HDAC8. HDAC2 acts as a transcriptional repressor through the desacetylation of lysine residues present at the N-terminal tail of histone proteins (H2A, H2B, H3 and H4). HDAC2 heterodimerise with HDAC1, but the heterodimer cannot bind to DNA, so they have to be recruited by transcription factors such as YY1, SP1/SP3, the tumor suppressor genes p53 and BRCA1. HDAC2 can also be tethered to DNA as a part of the multiprotein corepressor complexes CoREST, mSin3 and NuRD. These complexes are targeted to specific genomic sequences by interactions with sequence-specific transcription factors. For example, the HDAC2/HDAC1 containing Sin3-SAP corepressor complex is recruited by E2F family of transcription factors to repress transcription. HDAC2 containing complexes are also implicated in gene transcription-regulation mediated by nuclear receptors. These complexes also contain other epigenetic modifier genes, such as methyl-binding proteins (MeCp2), the DNA methyl transferases DNMT1, DNMT3A and DNMT3B, the histone methyl transferases SUVAR39H1 and G9a and histone demethylases (LSD1), providing another way by which HDAC2 regulates gene expression and chromatin remodelling.
HDAC2 also regulates gene expression through the deacetylation of specific transcription factors that includes STAT3 and SMAD7.
HDAC2 is a key regulator of genes regulating cell cycle, apoptosis, cell adhesion and migration. Together with HDAC1, HDAC2 regulates the transcription of genes implicated in haematopoiesis, epithelial cell differentiation, heart development and neurogenesis. Montgomery et al. (2007) find that HDAC2 and HDAC1 double-null mice show an uncontrolled ventricular proliferation, while Trivedi and collegues (2007) show the lack of cardiac hypertrophy in HDAC2 mutant mice. HDAC2 is also a key regulator of nervous system function acting as a repressor of synaptic plasticity genes that regulates learning and memory formation. HDAC2-deficient mouse have enhanced memory formation.
Homology The histone deacetylase domain of HDAC2 is highly homologous to other class I HDACs (HDAC1, HDAC3 and HDAC8) showing the greater homology with HDAC1. This domain is also highly conserved between species (from yeast to human).

Mutations

Germinal No germinal mutations have been found.
Somatic HDAC2 is mutated in sporadic tumors with microsatellite instability and in tumors arising in individuals with hereditary non-polyposis colorectal carcinoma. This mutation consists in a deletion of a nine adenines repeat present in Exon1 that produce a truncated and inactive form of the protein. The expression of the mutant form of HDAC2 induces resistance to the proapoptotic and antiproliferative effects of HDAC inhibitors. The lack of HDAC2 expression and function produces the up-regulation of tumor-growth promoting genes.

Implicated in

Note
  
Entity Various cancers
Note The deregulation of HDAC2 expression and activity has been linked to cancer development. HDAC2 is overexpressed in different tumor types including colon, gastric, cervical, prostate carcinoma, non-small cell lung cancer, and hepatocellular carcinoma. HDAC2 overexpression is implicated in cancer partly through its aberrant recruitment and consequent silencing of tumor suppressor genes. The repression of the tumor suppressor gene p21WAF1 is associated with histone hypoacetylation at the promoter region and can be reversed by the treatment with HDAC inhibitors.
Prognosis HDAC2 expression is correlated with poor prognosis and advanced stage disease in colorectal, prostate, gastric and hepatocellular carcinomas.
  
  
Entity Colon cancer
Note There are a number of studies showing HDAC2 overexpression in colon cancer. The increase of HDAC2 expression has been found at the protein and mRNA level indicating that HDAC2 overexpression is due to transcriptional activation. These studies indicate that in this tumor type HDAC2 transcription is regulated by beta-catenin-TCF-myc signaling pathway that is deregulated in colon cancer. HDAC2 overexpression is correlated with poor prognosis and advanced stage disease in colorectal carcinoma. However, Ropero et al., found an inactivating mutation of HDAC2 in colon cancers with microsatellite instability.
  
  
Entity Breast cancer
Note Different studies show an important role of HDAC2 in breast cancer. HDAC2 Knockdown induces senescence in breast cancer cells. Moreover the loss of HDAC2 activity potentiates the apoptotic effect of tamoxifen in estrogen/progesterone positive breast cancer cells.
  
  
Entity Prostate cancer
Note Weichert et al., found that HDAC2 was strongly expressed in more than 70% of prostate cancer cases analyzed. The increase in HDAC2 expression was associated with enhanced tumor cell proliferation and poor prognosis in prostate cancer suggesting HDAC2 as a novel prognostic factor in this tumor type.
  
  
Entity Hepatocellular carcinoma
Note HDAC2 regulated cell cycle and disruption of HDAC2 caused G1/S arrest in cell cycle. In G1/S transition, targeted-disruption of HDAC2 selectively induced the expression of p16(INK4A) and p21(WAF1/Cip1), and simultaneously suppressed the expression of cyclin D1, CDK4 and CDK2. Consequently, HDAC2 inhibition led to the down-regulation of E2F/DP1 target genes through a reduction in phosphorylation status of pRb protein.
  
  
Entity Gastric cancer
Note HDAC2 is aberrantly up-regulated in gastric cancers. HDAC2 inactivation significantly reduced cell motility, cell invasion, clonal expansion, and tumor growth. HDAC2 knockdown-induced G(1)-S cell cycle arrest and restored activity of p16(INK4a) and the proapoptotic factors.
  
  
Entity Lung cancer
Note HDAC2 is highly up-regulated in lung cancer. HDAC2 inactivation resulted in regression of tumor cell growth and activation of cellular apoptosis via p53 and Bax activation and Bcl2 suppression. In cell cycle regulation, HDAC2 inactivation caused induction of p21WAF1/CIP1 expression, and simultaneously suppressed the expressions of cyclin E2, cyclin D1, and CDK2, respectively. Consequently, this led to the hypophosphorylation of pRb protein in G1/S transition and thereby inactivated E2F/DP1 target gene transcriptions of A549 cells. HDAC2 directly regulated p21WAF1/CIP1 expression in a p53-independent manner.
  
  
Entity Chronic obstructive pulmonary disease (COPD)
Note Reduced HDAC2 activity and expression is found in chronic obstructive pulmonary disease (COPD). The reduced activity of HDAC2 produces the upregulation of genes implicated in the inflammatory response and resistance to corticosteroids in COPD.
  

Bibliography

Role of HDAC2 in the pathophysiology of COPD.
Barnes PJ.
Annu Rev Physiol. 2009;71:451-64. (REVIEW)
PMID 18817512
 
Selective inhibition of histone deacetylase 2 silences progesterone receptor-mediated signaling.
Bicaku E, Marchion DC, Schmitt ML, Munster PN.
Cancer Res. 2008 Mar 1;68(5):1513-9.
PMID 18316616
 
Histone deacetylase HDAC1/HDAC2-controlled embryonic development and cell differentiation.
Brunmeir R, Lagger S, Seiser C.
Int J Dev Biol. 2009;53(2-3):275-89. (REVIEW)
PMID 19412887
 
Histone deacetylase 1 can repress transcription by binding to Sp1.
Doetzlhofer A, Rotheneder H, Lagger G, Koranda M, Kurtev V, Brosch G, Wintersberger E, Seiser C.
Mol Cell Biol. 1999 Aug;19(8):5504-11.
PMID 10409740
 
Dnmt3a binds deacetylases and is recruited by a sequence-specific repressor to silence transcription.
Fuks F, Burgers WA, Godin N, Kasai M, Kouzarides T.
EMBO J. 2001 May 15;20(10):2536-44.
PMID 11350943
 
HDAC2 negatively regulates memory formation and synaptic plasticity.
Guan JS, Haggarty SJ, Giacometti E, Dannenberg JH, Joseph N, Gao J, Nieland TJ, Zhou Y, Wang X, Mazitschek R, Bradner JE, DePinho RA, Jaenisch R, Tsai LH.
Nature. 2009 May 7;459(7243):55-60.
PMID 19424149
 
Inhibition of histone deacetylase 2 increases apoptosis and p21Cip1/WAF1 expression, independent of histone deacetylase 1.
Huang BH, Laban M, Leung CH, Lee L, Lee CK, Salto-Tellez M, Raju GC, Hooi SC.
Cell Death Differ. 2005 Apr;12(4):395-404.
PMID 15665816
 
Histone deacetylases specifically down-regulate p53-dependent gene activation.
Juan LJ, Shia WJ, Chen MH, Yang WM, Seto E, Lin YS, Wu CW.
J Biol Chem. 2000 Jul 7;275(27):20436-43.
PMID 10777477
 
HDAC2 overexpression confers oncogenic potential to human lung cancer cells by deregulating expression of apoptosis and cell cycle proteins.
Jung KH, Noh JH, Kim JK, Eun JW, Bae HJ, Xie HJ, Chang YG, Kim MG, Park H, Lee JY, Nam SW.
J Cell Biochem. 2012 Jun;113(6):2167-77. doi: 10.1002/jcb.24090.
PMID 22492270
 
Targeted inactivation of HDAC2 restores p16INK4a activity and exerts antitumor effects on human gastric cancer.
Kim JK, Noh JH, Eun JW, Jung KH, Bae HJ, Shen Q, Kim MG, Chang YG, Kim SJ, Park WS, Lee JY, Borlak J, Nam SW.
Mol Cancer Res. 2013 Jan;11(1):62-73. doi: 10.1158/1541-7786.MCR-12-0332. Epub 2012 Nov 21.
PMID 23175521
 
Histone deacetylases 1 and 2 redundantly regulate cardiac morphogenesis, growth, and contractility.
Montgomery RL, Davis CA, Potthoff MJ, Haberland M, Fielitz J, Qi X, Hill JA, Richardson JA, Olson EN.
Genes Dev. 2007 Jul 15;21(14):1790-802.
PMID 17639084
 
Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex.
Nan X, Ng HH, Johnson CA, Laherty CD, Turner BM, Eisenman RN, Bird A.
Nature. 1998 May 28;393(6683):386-9.
PMID 9620804
 
Aberrant regulation of HDAC2 mediates proliferation of hepatocellular carcinoma cells by deregulating expression of G1/S cell cycle proteins.
Noh JH, Jung KH, Kim JK, Eun JW, Bae HJ, Xie HJ, Chang YG, Kim MG, Park WS, Lee JY, Nam SW.
PLoS One. 2011;6(11):e28103. doi: 10.1371/journal.pone.0028103. Epub 2011 Nov 23.
PMID 22132221
 
S-Nitrosylation of histone deacetylase 2 induces chromatin remodelling in neurons.
Nott A, Watson PM, Robinson JD, Crepaldi L, Riccio A.
Nature. 2008 Sep 18;455(7211):411-5. Epub 2008 Aug 27.
PMID 18754010
 
E2F mediates cell cycle-dependent transcriptional repression in vivo by recruitment of an HDAC1/mSin3B corepressor complex.
Rayman JB, Takahashi Y, Indjeian VB, Dannenberg JH, Catchpole S, Watson RJ, te Riele H, Dynlacht BD.
Genes Dev. 2002 Apr 15;16(8):933-47.
PMID 11959842
 
Transforming pathways unleashed by a HDAC2 mutation in human cancer.
Ropero S, Ballestar E, Alaminos M, Arango D, Schwartz S Jr, Esteller M.
Oncogene. 2008 Jun 26;27(28):4008-12. Epub 2008 Feb 11.
PMID 18264134
 
The role of histone deacetylases (HDACs) in human cancer.
Ropero S, Esteller M.
Mol Oncol. 2007 Jun;1(1):19-25. Epub 2007 Mar 7. (REVIEW)
PMID 19383284
 
A truncating mutation of HDAC2 in human cancers confers resistance to histone deacetylase inhibition.
Ropero S, Fraga MF, Ballestar E, Hamelin R, Yamamoto H, Boix-Chornet M, Caballero R, Alaminos M, Setien F, Paz MF, Herranz M, Palacios J, Arango D, Orntoft TF, Aaltonen LA, Schwartz S Jr, Esteller M.
Nat Genet. 2006 May;38(5):566-9. Epub 2006 Apr 16.
PMID 16642021
 
Epigenetic regulation of hematopoietic differentiation by Gfi-1 and Gfi-1b is mediated by the cofactors CoREST and LSD1.
Saleque S, Kim J, Rooke HM, Orkin SH.
Mol Cell. 2007 Aug 17;27(4):562-72.
PMID 17707228
 
Hdac2 regulates the cardiac hypertrophic response by modulating Gsk3 beta activity.
Trivedi CM, Luo Y, Yin Z, Zhang M, Zhu W, Wang T, Floss T, Goettlicher M, Noppinger PR, Wurst W, Ferrari VA, Abrams CS, Gruber PJ, Epstein JA.
Nat Med. 2007 Mar;13(3):324-31. Epub 2007 Feb 18.
PMID 17322895
 
Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases.
Vaute O, Nicolas E, Vandel L, Trouche D.
Nucleic Acids Res. 2002 Jan 15;30(2):475-81.
PMID 11788710
 
Histone deacetylases 1, 2 and 3 are highly expressed in prostate cancer and HDAC2 expression is associated with shorter PSA relapse time after radical prostatectomy.
Weichert W, Roske A, Gekeler V, Beckers T, Stephan C, Jung K, Fritzsche FR, Niesporek S, Denkert C, Dietel M, Kristiansen G.
Br J Cancer. 2008 Feb 12;98(3):604-10. Epub 2008 Jan 22.
PMID 18212746
 
HDAC expression and clinical prognosis in human malignancies.
Weichert W.
Cancer Lett. 2009 Aug 8;280(2):168-76. Epub 2008 Dec 21. (REVIEW)
PMID 19103471
 
Histone deacetylase inhibitors: molecular mechanisms of action.
Xu WS, Parmigiani RB, Marks PA.
Oncogene. 2007 Aug 13;26(37):5541-52. (REVIEW)
PMID 17694093
 
Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global regulator RPD3.
Yang WM, Inouye C, Zeng Y, Bearss D, Seto E.
Proc Natl Acad Sci U S A. 1996 Nov 12;93(23):12845-50.
PMID 8917507
 
The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men.
Yang XJ, Seto E.
Nat Rev Mol Cell Biol. 2008 Mar;9(3):206-18. (REVIEW)
PMID 18292778
 
BRCA1 interacts with components of the histone deacetylase complex.
Yarden RI, Brody LC.
Proc Natl Acad Sci U S A. 1999 Apr 27;96(9):4983-8.
PMID 10220405
 
Induction of HDAC2 expression upon loss of APC in colorectal tumorigenesis.
Zhu P, Martin E, Mengwasser J, Schlag P, Janssen KP, Gottlicher M.
Cancer Cell. 2004 May;5(5):455-63.
PMID 15144953
 

Citation

This paper should be referenced as such :
Bae, HJ ; Nam, SW
HDAC2 (histone deacetylase 2)
Atlas Genet Cytogenet Oncol Haematol. 2014;18(8):594-597.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/HDAC2ID40803ch6q22.html
History of this paper:
Ropero, S ; Esteller, M. HDAC2 (histone deacetylase 2). Atlas Genet Cytogenet Oncol Haematol. 2010;14(10):966-969.
http://documents.irevues.inist.fr/bitstream/handle/2042/44871/01-2010-HDAC2ID40803ch6q22.pdf


Other Leukemias implicated (Data extracted from papers in the Atlas) [ 7 ]
  del(11)(q23q23) KMT2A/CBL::t(11;11)(q23;q23) KMT2A/CBL
del(11)(q23q23) KMT2A/ARHGEF12
t(1;11)(p32;q23) KMT2A/EPS15
t(2;11)(q37;q23) KMT2A/SEPT2
t(3;11)(q21;q23) KMT2A/EEFSEC
t(9;13)(p12;q21) PAX5/DACH1
t(9;17)(p13;p12) PAX5/NCOR1


External links

Nomenclature
HGNC (Hugo)HDAC2   4853
Cards
AtlasHDAC2ID40803ch6q22
Entrez_Gene (NCBI)HDAC2  3066  histone deacetylase 2
AliasesHD2; RPD3; YAF1
GeneCards (Weizmann)HDAC2
Ensembl hg19 (Hinxton)ENSG00000196591 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000196591 [Gene_View]  chr6:113936156-113971195 [Contig_View]  HDAC2 [Vega]
ICGC DataPortalENSG00000196591
TCGA cBioPortalHDAC2
AceView (NCBI)HDAC2
Genatlas (Paris)HDAC2
WikiGenes3066
SOURCE (Princeton)HDAC2
Genetics Home Reference (NIH)HDAC2
Genomic and cartography
GoldenPath hg38 (UCSC)HDAC2  -     chr6:113936156-113971195 -  6q21   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)HDAC2  -     6q21   [Description]    (hg19-Feb_2009)
EnsemblHDAC2 - 6q21 [CytoView hg19]  HDAC2 - 6q21 [CytoView hg38]
Mapping of homologs : NCBIHDAC2 [Mapview hg19]  HDAC2 [Mapview hg38]
OMIM605164   
Gene and transcription
Genbank (Entrez)AA704179 AB209190 AK092156 AK097376 AK296856
RefSeq transcript (Entrez)NM_001527
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)HDAC2
Cluster EST : UnigeneHs.3352 [ NCBI ]
CGAP (NCI)Hs.3352
Alternative Splicing GalleryENSG00000196591
Gene ExpressionHDAC2 [ NCBI-GEO ]   HDAC2 [ EBI - ARRAY_EXPRESS ]   HDAC2 [ SEEK ]   HDAC2 [ MEM ]
Gene Expression Viewer (FireBrowse)HDAC2 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)3066
GTEX Portal (Tissue expression)HDAC2
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ92769   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ92769  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ92769
Splice isoforms : SwissVarQ92769
PhosPhoSitePlusQ92769
Domains : Interpro (EBI)His_deacetylse    His_deacetylse_1    His_deacetylse_dom   
Domain families : Pfam (Sanger)Hist_deacetyl (PF00850)   
Domain families : Pfam (NCBI)pfam00850   
Conserved Domain (NCBI)HDAC2
DMDM Disease mutations3066
Blocks (Seattle)HDAC2
PDB (SRS)3MAX    4LXZ    4LY1    5IWG    5IX0   
PDB (PDBSum)3MAX    4LXZ    4LY1    5IWG    5IX0   
PDB (IMB)3MAX    4LXZ    4LY1    5IWG    5IX0   
PDB (RSDB)3MAX    4LXZ    4LY1    5IWG    5IX0   
Structural Biology KnowledgeBase3MAX    4LXZ    4LY1    5IWG    5IX0   
SCOP (Structural Classification of Proteins)3MAX    4LXZ    4LY1    5IWG    5IX0   
CATH (Classification of proteins structures)3MAX    4LXZ    4LY1    5IWG    5IX0   
SuperfamilyQ92769
Human Protein AtlasENSG00000196591
Peptide AtlasQ92769
HPRD05521
IPIIPI00555868   IPI00289601   IPI00982901   IPI00972999   IPI00980006   IPI00978755   IPI00964796   IPI00976604   IPI00976554   IPI00979387   IPI00974336   IPI00976946   
Protein Interaction databases
DIP (DOE-UCLA)Q92769
IntAct (EBI)Q92769
FunCoupENSG00000196591
BioGRIDHDAC2
STRING (EMBL)HDAC2
ZODIACHDAC2
Ontologies - Pathways
QuickGOQ92769
Ontology : AmiGOnegative regulation of transcription from RNA polymerase II promoter  nuclear chromatin  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  response to amphetamine  cardiac muscle hypertrophy  chromatin binding  RNA binding  histone deacetylase activity  histone deacetylase activity  protein binding  nucleus  nucleoplasm  cytoplasm  cytoplasm  chromatin remodeling  maintenance of chromatin silencing  transcription, DNA-templated  blood coagulation  transcription factor binding  positive regulation of cell proliferation  epidermal cell differentiation  positive regulation of epithelial to mesenchymal transition  positive regulation of receptor biosynthetic process  negative regulation of neuron projection development  dendrite development  histone deacetylation  Sin3 complex  NuRD complex  deacetylase activity  enzyme binding  response to caffeine  heat shock protein binding  nucleosomal DNA binding  NAD-dependent histone deacetylase activity (H3-K14 specific)  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  protein deacetylase activity  cellular response to heat  response to nicotine  ESC/E(Z) complex  response to cocaine  odontogenesis of dentin-containing tooth  response to drug  embryonic digit morphogenesis  ATP-dependent chromatin remodeling  negative regulation of apoptotic process  protein complex  negative regulation of DNA binding  negative regulation of sequence-specific DNA binding transcription factor activity  sequence-specific DNA binding  negative regulation of MHC class II biosynthetic process  positive regulation of proteolysis  negative regulation of transcription, DNA-templated  negative regulation of transcription, DNA-templated  positive regulation of transcription, DNA-templated  positive regulation of transcription from RNA polymerase II promoter  behavioral response to ethanol  positive regulation of oligodendrocyte differentiation  NF-kappaB binding  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  regulation of signal transduction by p53 class mediator  cellular response to dopamine  negative regulation of peptidyl-lysine acetylation  
Ontology : EGO-EBInegative regulation of transcription from RNA polymerase II promoter  nuclear chromatin  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  response to amphetamine  cardiac muscle hypertrophy  chromatin binding  RNA binding  histone deacetylase activity  histone deacetylase activity  protein binding  nucleus  nucleoplasm  cytoplasm  cytoplasm  chromatin remodeling  maintenance of chromatin silencing  transcription, DNA-templated  blood coagulation  transcription factor binding  positive regulation of cell proliferation  epidermal cell differentiation  positive regulation of epithelial to mesenchymal transition  positive regulation of receptor biosynthetic process  negative regulation of neuron projection development  dendrite development  histone deacetylation  Sin3 complex  NuRD complex  deacetylase activity  enzyme binding  response to caffeine  heat shock protein binding  nucleosomal DNA binding  NAD-dependent histone deacetylase activity (H3-K14 specific)  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  protein deacetylase activity  cellular response to heat  response to nicotine  ESC/E(Z) complex  response to cocaine  odontogenesis of dentin-containing tooth  response to drug  embryonic digit morphogenesis  ATP-dependent chromatin remodeling  negative regulation of apoptotic process  protein complex  negative regulation of DNA binding  negative regulation of sequence-specific DNA binding transcription factor activity  sequence-specific DNA binding  negative regulation of MHC class II biosynthetic process  positive regulation of proteolysis  negative regulation of transcription, DNA-templated  negative regulation of transcription, DNA-templated  positive regulation of transcription, DNA-templated  positive regulation of transcription from RNA polymerase II promoter  behavioral response to ethanol  positive regulation of oligodendrocyte differentiation  NF-kappaB binding  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  regulation of signal transduction by p53 class mediator  cellular response to dopamine  negative regulation of peptidyl-lysine acetylation  
Pathways : BIOCARTAThe PRC2 Complex Sets Long-term Gene Silencing Through Modification of Histone Tails [Genes]    Role of MEF2D in T-cell Apoptosis [Genes]    CARM1 and Regulation of the Estrogen Receptor [Genes]    METS affect on Macrophage Differentiation [Genes]   
Pathways : KEGG   
REACTOMEQ92769 [protein]
REACTOME PathwaysR-HSA-983231 [pathway]   
NDEx NetworkHDAC2
Atlas of Cancer Signalling NetworkHDAC2
Wikipedia pathwaysHDAC2
Orthology - Evolution
OrthoDB3066
GeneTree (enSembl)ENSG00000196591
Phylogenetic Trees/Animal Genes : TreeFamHDAC2
HOVERGENQ92769
HOGENOMQ92769
Homologs : HomoloGeneHDAC2
Homology/Alignments : Family Browser (UCSC)HDAC2
Gene fusions - Rearrangements
Fusion : MitelmanHDAC2/TRDN [6q21/6q22.31]  
Fusion: TCGAHDAC2 6q21 TRDN 6q22.31 BRCA
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerHDAC2 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)HDAC2
dbVarHDAC2
ClinVarHDAC2
1000_GenomesHDAC2 
Exome Variant ServerHDAC2
ExAC (Exome Aggregation Consortium)HDAC2 (select the gene name)
Genetic variants : HAPMAP3066
Genomic Variants (DGV)HDAC2 [DGVbeta]
DECIPHERHDAC2 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisHDAC2 
Mutations
ICGC Data PortalHDAC2 
TCGA Data PortalHDAC2 
Broad Tumor PortalHDAC2
OASIS PortalHDAC2 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICHDAC2  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDHDAC2
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch HDAC2
DgiDB (Drug Gene Interaction Database)HDAC2
DoCM (Curated mutations)HDAC2 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)HDAC2 (select a term)
intoGenHDAC2
NCG5 (London)HDAC2
Cancer3DHDAC2(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM605164   
Orphanet
MedgenHDAC2
Genetic Testing Registry HDAC2
NextProtQ92769 [Medical]
TSGene3066
GENETestsHDAC2
Target ValidationHDAC2
Huge Navigator HDAC2 [HugePedia]
snp3D : Map Gene to Disease3066
BioCentury BCIQHDAC2
ClinGenHDAC2
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD3066
Chemical/Pharm GKB GenePA29227
Clinical trialHDAC2
Miscellaneous
canSAR (ICR)HDAC2 (select the gene name)
Probes
Litterature
PubMed499 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineHDAC2
EVEXHDAC2
GoPubMedHDAC2
iHOPHDAC2
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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