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Entry version 211 (13 Feb 2019)
Sequence version 2 (21 Jun 2005)
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Protein

Histone deacetylase 2

Gene

HDAC2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. May be involved in the transcriptional repression of circadian target genes, such as PER1, mediated by CRY1 through histone deacetylation. Involved in MTA1-mediated transcriptional corepression of TFF1 and CDKN1A.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone. EC:3.5.1.98

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei142By similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionChromatin regulator, Hydrolase, Repressor
Biological processBiological rhythms, Transcription, Transcription regulation

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
3.5.1.98 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-193670 p75NTR negatively regulates cell cycle via SC1
R-HSA-2122947 NOTCH1 Intracellular Domain Regulates Transcription
R-HSA-2644606 Constitutive Signaling by NOTCH1 PEST Domain Mutants
R-HSA-2894862 Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants
R-HSA-3214815 HDACs deacetylate histones
R-HSA-427389 ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression
R-HSA-427413 NoRC negatively regulates rRNA expression
R-HSA-4551638 SUMOylation of chromatin organization proteins
R-HSA-6804758 Regulation of TP53 Activity through Acetylation
R-HSA-73762 RNA Polymerase I Transcription Initiation
R-HSA-8943724 Regulation of PTEN gene transcription
R-HSA-9022692 Regulation of MECP2 expression and activity
R-HSA-9022699 MECP2 regulates neuronal receptors and channels
R-HSA-9615017 FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes
R-HSA-983231 Factors involved in megakaryocyte development and platelet production

SABIO-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
Q92769

SIGNOR Signaling Network Open Resource

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SIGNORi
Q92769

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Histone deacetylase 2 (EC:3.5.1.98)
Short name:
HD2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:HDAC2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 6

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000196591.11

Human Gene Nomenclature Database

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HGNCi
HGNC:4853 HDAC2

Online Mendelian Inheritance in Man (OMIM)

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MIMi
605164 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q92769

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Organism-specific databases

DisGeNET

More...
DisGeNETi
3066

Open Targets

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OpenTargetsi
ENSG00000196591

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA29227

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL1937

Drug and drug target database

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DrugBanki
DB01223 Aminophylline
DB05015 Belinostat
DB00227 Lovastatin
DB05651 MGCD-0103
DB01303 Oxtriphylline
DB06603 Panobinostat
DB06176 Romidepsin
DB05223 SB939
DB00277 Theophylline
DB00313 Valproic Acid
DB02546 Vorinostat

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2616

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
HDAC2

Domain mapping of disease mutations (DMDM)

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DMDMi
68068066

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001146931 – 488Histone deacetylase 2Add BLAST488

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei75N6-acetyllysine; alternateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki75Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei221N6-acetyllysineBy similarity1
Modified residuei262S-nitrosocysteineBy similarity1
Modified residuei274S-nitrosocysteineBy similarity1
Modified residuei394PhosphoserineCombined sources1
Modified residuei407PhosphoserineCombined sources1
Modified residuei422PhosphoserineCombined sources1
Modified residuei424PhosphoserineCombined sources1
Cross-linki439Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki452Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki458Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki462Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki478Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki481Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

S-nitrosylated by GAPDH. In neurons, S-Nitrosylation at Cys-262 and Cys-274 does not affect the enzyme activity but abolishes chromatin-binding, leading to increases acetylation of histones and activate genes that are associated with neuronal development. In embryonic cortical neurons, S-Nitrosylation regulates dendritic growth and branching.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q92769

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q92769

MaxQB - The MaxQuant DataBase

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MaxQBi
Q92769

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q92769

PeptideAtlas

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PeptideAtlasi
Q92769

PRoteomics IDEntifications database

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PRIDEi
Q92769

ProteomicsDB human proteome resource

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ProteomicsDBi
75454

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q92769

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q92769

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Widely expressed; lower levels in brain and lung.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000196591 Expressed in 232 organ(s), highest expression level in cerebral cortex

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q92769 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q92769 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB005054
HPA011727

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Part of the core histone deacetylase (HDAC) complex composed of HDAC1, HDAC2, RBBP4 and RBBP7. The core complex associates with MTA2, MBD3, MTA1L1, CHD3 and CHD4 to form the nucleosome remodeling and histone deacetylation (NuRD) complex, or with SIN3, SAP18 and SAP30 to form the SIN3 HDAC complex. Component of a RCOR/GFI/KDM1A/HDAC complex. Interacts directly with GFI1 and GFI1B. Interacts with SNW1, HDAC7, PRDM6, SAP30, SETDB1 and SUV39H1. Interacts with the H2AFY (via the non-histone region). Component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B, KDM1A, RCOR1 and PHF21A. The BHC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. Part of a complex containing the core histones H2A, H2B, H3 and H4, DEK and unphosphorylated DAXX. Part of a complex containing ATR and CHD4. Forms a heterologous complex at least with YY1. Interacts with ATR, CBFA2T3, DNMT1, MINT, HDAC10, HCFC1, NRIP1, KDM4A and PELP1. Component of a mSin3A corepressor complex that contains SIN3A, SAP130, SUDS3, ARID4B, HDAC1 and HDAC2. Interacts with CHFR and SAP30L. Interacts (CK2 phosphorylated form) with SP3. Interacts with TSHZ3 (via its N-terminus). Interacts with APEX1; the interaction is not dependent on the acetylated status of APEX1. Part of a complex composed of TRIM28, HDAC1, HDAC2 and EHMT2. Interacts with PIMREG. Interacts with BCL6 (non-acetylated form). Part of a complex containing at least CDYL, MIER1, MIER2, HDAC1 and HDAC2. Interacts with CRY1, INSM1 and ZNF431. Interacts with NACC2. Interacts with MTA1, with a preference for sumoylated MTA1. Interacts with SIX3 (By similarity). Interacts with BEND3. Component of a histone deacetylase complex containing DNTTIP1, ZNF541, HDAC1 and HDAC2 (PubMed:21573134).By similarity29 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
109316, 353 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-3321 SIN3A histone deacetylase complex
CPX-3322 SIN3B histone deacetylase complex
CPX-3323 SIN3A histone deacetylase complex, ES cell-specific variant
CPX-880 MBD2/NuRD nucleosome remodeling and deacetylase complex
CPX-922 MBD3/NuRD nucleosome remodeling and deacetylase complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q92769

Database of interacting proteins

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DIPi
DIP-24220N

Protein interaction database and analysis system

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IntActi
Q92769, 174 interactors

Molecular INTeraction database

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MINTi
Q92769

STRING: functional protein association networks

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STRINGi
9606.ENSP00000430432

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q92769

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1488
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3MAXX-ray2.05A/B/C9-374[»]
4LXZX-ray1.85A/B/C8-376[»]
4LY1X-ray1.57A/B/C8-376[»]
5IWGX-ray1.66A/B/C8-375[»]
5IX0X-ray1.72A/B/C7-375[»]
6G3OX-ray2.27A/B/C7-376[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q92769

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q92769

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q92769

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni9 – 322Histone deacetylaseAdd BLAST314

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi300 – 303Poly-Gly4

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1342 Eukaryota
COG0123 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155725

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000225180

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG057112

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q92769

KEGG Orthology (KO)

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KOi
K06067

Identification of Orthologs from Complete Genome Data

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OMAi
CDIAINY

Database of Orthologous Groups

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OrthoDBi
732770at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q92769

TreeFam database of animal gene trees

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TreeFami
TF106171

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.40.800.20, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR000286 His_deacetylse
IPR003084 His_deacetylse_1
IPR023801 His_deacetylse_dom
IPR037138 His_deacetylse_dom_sf
IPR023696 Ureohydrolase_dom_sf

The PANTHER Classification System

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PANTHERi
PTHR10625 PTHR10625, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00850 Hist_deacetyl, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF037913 His_deacetylse_1, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR01270 HDASUPER
PR01271 HISDACETLASE

Superfamily database of structural and functional annotation

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SUPFAMi
SSF52768 SSF52768, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 9 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q92769-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MAYSQGGGKK KVCYYYDGDI GNYYYGQGHP MKPHRIRMTH NLLLNYGLYR
60 70 80 90 100
KMEIYRPHKA TAEEMTKYHS DEYIKFLRSI RPDNMSEYSK QMQRFNVGED
110 120 130 140 150
CPVFDGLFEF CQLSTGGSVA GAVKLNRQQT DMAVNWAGGL HHAKKSEASG
160 170 180 190 200
FCYVNDIVLA ILELLKYHQR VLYIDIDIHH GDGVEEAFYT TDRVMTVSFH
210 220 230 240 250
KYGEYFPGTG DLRDIGAGKG KYYAVNFPMR DGIDDESYGQ IFKPIISKVM
260 270 280 290 300
EMYQPSAVVL QCGADSLSGD RLGCFNLTVK GHAKCVEVVK TFNLPLLMLG
310 320 330 340 350
GGGYTIRNVA RCWTYETAVA LDCEIPNELP YNDYFEYFGP DFKLHISPSN
360 370 380 390 400
MTNQNTPEYM EKIKQRLFEN LRMLPHAPGV QMQAIPEDAV HEDSGDEDGE
410 420 430 440 450
DPDKRISIRA SDKRIACDEE FSDSEDEGEG GRRNVADHKK GAKKARIEED
460 470 480
KKETEDKKTD VKEEDKSKDN SGEKTDTKGT KSEQLSNP
Length:488
Mass (Da):55,364
Last modified:June 21, 2005 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i775419CCCDAE07FA
GO
Isoform 2 (identifier: Q92769-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: Missing.

Note: No experimental confirmation available.
Show »
Length:458
Mass (Da):51,998
Checksum:i73BF368ACAA58819
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 9 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E5RFP9E5RFP9_HUMAN
Histone deacetylase 2
HDAC2
109Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E5RHE7E5RHE7_HUMAN
Histone deacetylase 2
HDAC2
86Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E5RGV4E5RGV4_HUMAN
Histone deacetylase 2
HDAC2
71Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E5RH52E5RH52_HUMAN
Histone deacetylase 2
HDAC2
100Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E5RJ04E5RJ04_HUMAN
Histone deacetylase 2
HDAC2
65Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E5RG37E5RG37_HUMAN
Histone deacetylase 2
HDAC2
103Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H3BM24H3BM24_HUMAN
Histone deacetylase 2
HDAC2
161Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E5RFI6E5RFI6_HUMAN
Histone deacetylase 2
HDAC2
60Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E5RK19E5RK19_HUMAN
Histone deacetylase 2
HDAC2
52Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAH31055 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAG59420 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti93 – 94QR → HI in AAC50814 (PubMed:8917507).Curated2
Sequence conflicti103V → A in AAC50814 (PubMed:8917507).Curated1
Sequence conflicti146S → Y in AAC50814 (PubMed:8917507).Curated1
Sequence conflicti248K → M in BAG59420 (PubMed:14702039).Curated1
Sequence conflicti281G → D in BAG59420 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_025311230R → C1 PublicationCorresponds to variant dbSNP:rs1042903Ensembl.1
Natural variantiVAR_025312315Y → H1 PublicationCorresponds to variant dbSNP:rs17852888Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0561751 – 30Missing in isoform 2. 1 PublicationAdd BLAST30

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U31814 mRNA Translation: AAC50814.1
AK092156 mRNA Translation: BAG52487.1
AK296856 mRNA Translation: BAG59420.1 Different initiation.
AL590398 Genomic DNA No translation available.
AL671967 Genomic DNA No translation available.
FO393415 Genomic DNA No translation available.
CH471051 Genomic DNA Translation: EAW48252.1
CH471051 Genomic DNA Translation: EAW48253.1
CH471051 Genomic DNA Translation: EAW48254.1
CH471051 Genomic DNA Translation: EAW48255.1
BC031055 mRNA Translation: AAH31055.2 Different initiation.

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS43493.2 [Q92769-1]

NCBI Reference Sequences

More...
RefSeqi
NP_001518.3, NM_001527.3 [Q92769-1]
XP_011534090.1, XM_011535788.1
XP_016866288.1, XM_017010799.1 [Q92769-3]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.3352

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000368632; ENSP00000357621; ENSG00000196591 [Q92769-3]
ENST00000519065; ENSP00000430432; ENSG00000196591 [Q92769-1]
ENST00000519108; ENSP00000430008; ENSG00000196591 [Q92769-3]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
3066

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:3066

UCSC genome browser

More...
UCSCi
uc003pwc.3 human [Q92769-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31814 mRNA Translation: AAC50814.1
AK092156 mRNA Translation: BAG52487.1
AK296856 mRNA Translation: BAG59420.1 Different initiation.
AL590398 Genomic DNA No translation available.
AL671967 Genomic DNA No translation available.
FO393415 Genomic DNA No translation available.
CH471051 Genomic DNA Translation: EAW48252.1
CH471051 Genomic DNA Translation: EAW48253.1
CH471051 Genomic DNA Translation: EAW48254.1
CH471051 Genomic DNA Translation: EAW48255.1
BC031055 mRNA Translation: AAH31055.2 Different initiation.
CCDSiCCDS43493.2 [Q92769-1]
RefSeqiNP_001518.3, NM_001527.3 [Q92769-1]
XP_011534090.1, XM_011535788.1
XP_016866288.1, XM_017010799.1 [Q92769-3]
UniGeneiHs.3352

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3MAXX-ray2.05A/B/C9-374[»]
4LXZX-ray1.85A/B/C8-376[»]
4LY1X-ray1.57A/B/C8-376[»]
5IWGX-ray1.66A/B/C8-375[»]
5IX0X-ray1.72A/B/C7-375[»]
6G3OX-ray2.27A/B/C7-376[»]
ProteinModelPortaliQ92769
SMRiQ92769
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109316, 353 interactors
ComplexPortaliCPX-3321 SIN3A histone deacetylase complex
CPX-3322 SIN3B histone deacetylase complex
CPX-3323 SIN3A histone deacetylase complex, ES cell-specific variant
CPX-880 MBD2/NuRD nucleosome remodeling and deacetylase complex
CPX-922 MBD3/NuRD nucleosome remodeling and deacetylase complex
CORUMiQ92769
DIPiDIP-24220N
IntActiQ92769, 174 interactors
MINTiQ92769
STRINGi9606.ENSP00000430432

Chemistry databases

BindingDBiQ92769
ChEMBLiCHEMBL1937
DrugBankiDB01223 Aminophylline
DB05015 Belinostat
DB00227 Lovastatin
DB05651 MGCD-0103
DB01303 Oxtriphylline
DB06603 Panobinostat
DB06176 Romidepsin
DB05223 SB939
DB00277 Theophylline
DB00313 Valproic Acid
DB02546 Vorinostat
GuidetoPHARMACOLOGYi2616

PTM databases

iPTMnetiQ92769
PhosphoSitePlusiQ92769

Polymorphism and mutation databases

BioMutaiHDAC2
DMDMi68068066

Proteomic databases

EPDiQ92769
jPOSTiQ92769
MaxQBiQ92769
PaxDbiQ92769
PeptideAtlasiQ92769
PRIDEiQ92769
ProteomicsDBi75454

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
3066
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000368632; ENSP00000357621; ENSG00000196591 [Q92769-3]
ENST00000519065; ENSP00000430432; ENSG00000196591 [Q92769-1]
ENST00000519108; ENSP00000430008; ENSG00000196591 [Q92769-3]
GeneIDi3066
KEGGihsa:3066
UCSCiuc003pwc.3 human [Q92769-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3066
DisGeNETi3066
EuPathDBiHostDB:ENSG00000196591.11

GeneCards: human genes, protein and diseases

More...
GeneCardsi
HDAC2
HGNCiHGNC:4853 HDAC2
HPAiCAB005054
HPA011727
MIMi605164 gene
neXtProtiNX_Q92769
OpenTargetsiENSG00000196591
PharmGKBiPA29227

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1342 Eukaryota
COG0123 LUCA
GeneTreeiENSGT00940000155725
HOGENOMiHOG000225180
HOVERGENiHBG057112
InParanoidiQ92769
KOiK06067
OMAiCDIAINY
OrthoDBi732770at2759
PhylomeDBiQ92769
TreeFamiTF106171

Enzyme and pathway databases

BRENDAi3.5.1.98 2681
ReactomeiR-HSA-193670 p75NTR negatively regulates cell cycle via SC1
R-HSA-2122947 NOTCH1 Intracellular Domain Regulates Transcription
R-HSA-2644606 Constitutive Signaling by NOTCH1 PEST Domain Mutants
R-HSA-2894862 Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants
R-HSA-3214815 HDACs deacetylate histones
R-HSA-427389 ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression
R-HSA-427413 NoRC negatively regulates rRNA expression
R-HSA-4551638 SUMOylation of chromatin organization proteins
R-HSA-6804758 Regulation of TP53 Activity through Acetylation
R-HSA-73762 RNA Polymerase I Transcription Initiation
R-HSA-8943724 Regulation of PTEN gene transcription
R-HSA-9022692 Regulation of MECP2 expression and activity
R-HSA-9022699 MECP2 regulates neuronal receptors and channels
R-HSA-9615017 FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes
R-HSA-983231 Factors involved in megakaryocyte development and platelet production
SABIO-RKiQ92769
SIGNORiQ92769

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
HDAC2 human
EvolutionaryTraceiQ92769

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Histone_deacetylase_2

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
3066

Protein Ontology

More...
PROi
PR:Q92769

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000196591 Expressed in 232 organ(s), highest expression level in cerebral cortex
ExpressionAtlasiQ92769 baseline and differential
GenevisibleiQ92769 HS

Family and domain databases

Gene3Di3.40.800.20, 1 hit
InterProiView protein in InterPro
IPR000286 His_deacetylse
IPR003084 His_deacetylse_1
IPR023801 His_deacetylse_dom
IPR037138 His_deacetylse_dom_sf
IPR023696 Ureohydrolase_dom_sf
PANTHERiPTHR10625 PTHR10625, 1 hit
PfamiView protein in Pfam
PF00850 Hist_deacetyl, 1 hit
PIRSFiPIRSF037913 His_deacetylse_1, 1 hit
PRINTSiPR01270 HDASUPER
PR01271 HISDACETLASE
SUPFAMiSSF52768 SSF52768, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiHDAC2_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q92769
Secondary accession number(s): B3KRS5
, B4DL58, E1P561, Q5SRI8, Q5SZ86, Q8NEH4
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: June 21, 2005
Last modified: February 13, 2019
This is version 211 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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