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UniProtKB - O15379 (HDAC3_HUMAN)

Entry version 224 (25 May 2022)
Sequence version 2 (15 Jul 1998)
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Protein

Histone deacetylase 3

Gene

HDAC3

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

Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4), and some other non-histone substrates (PubMed:23911289, PubMed:21030595, PubMed:21444723, PubMed:25301942, PubMed:28497810, PubMed:28167758).

Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (PubMed:23911289).

Histone deacetylases act via the formation of large multiprotein complexes (PubMed:23911289).

Participates in the BCL6 transcriptional repressor activity by deacetylating the H3 'Lys-27' (H3K27) on enhancer elements, antagonizing EP300 acetyltransferase activity and repressing proximal gene expression (PubMed:23911289).

Acts as a molecular chaperone for shuttling phosphorylated NR2C1 to PML bodies for sumoylation (By similarity).

Contributes, together with XBP1 isoform 1, to the activation of NFE2L2-mediated HMOX1 transcription factor gene expression in a PI3K/mTORC2/Akt-dependent signaling pathway leading to endothelial cell (EC) survival under disturbed flow/oxidative stress (PubMed:25190803).

Regulates both the transcriptional activation and repression phases of the circadian clock in a deacetylase activity-independent manner (By similarity).

During the activation phase, promotes the accumulation of ubiquitinated ARNTL/BMAL1 at the E-boxes and during the repression phase, blocks FBXL3-mediated CRY1/2 ubiquitination and promotes the interaction of CRY1 and ARNTL/BMAL1 (By similarity).

The NCOR1-HDAC3 complex regulates the circadian expression of the core clock gene ARTNL/BMAL1 and the genes involved in lipid metabolism in the liver (By similarity).

Also functions as deacetylase for non-histone targets, such as KAT5, MEF2D, MAPK14 and RARA (PubMed:21030595, PubMed:21444723, PubMed:25301942, PubMed:28167758).

Serves as a corepressor of RARA, mediating its deacetylation and repression, leading to inhibition of RARE DNA element binding (PubMed:28167758).

In association with RARA, plays a role in the repression of microRNA-10a and thereby in the inflammatory response (PubMed:28167758).

In addition to protein deacetylase activity, also acts as protein-lysine deacylase by recognizing other acyl groups: catalyzes removal of (2E)-butenoyl (crotonyl) and 2-hydroxyisobutanoyl (2-hydroxyisobutyryl) acyl groups from lysine residues, leading to protein decrotonylation and de-2-hydroxyisobutyrylation, respectively (PubMed:28497810, PubMed:29192674, PubMed:34608293).

Catalyzes decrotonylation of MAPRE1/EB1 (PubMed:34608293).

By similarity9 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei135By 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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, Host-virus interaction, Transcription, Transcription regulation

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.5.1.98, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		O15379

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-1368071, NR1D1 (REV-ERBA) represses gene expression
R-HSA-193670, p75NTR negatively regulates cell cycle via SC1
R-HSA-1989781, PPARA activates gene expression
R-HSA-2122947, NOTCH1 Intracellular Domain Regulates Transcription
R-HSA-2151201, Transcriptional activation of mitochondrial biogenesis
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-350054, Notch-HLH transcription pathway
R-HSA-381340, Transcriptional regulation of white adipocyte differentiation
R-HSA-390471, Association of TriC/CCT with target proteins during biosynthesis
R-HSA-400206, Regulation of lipid metabolism by PPARalpha
R-HSA-400253, Circadian Clock
R-HSA-5617472, Activation of anterior HOX genes in hindbrain development during early embryogenesis
R-HSA-8940973, RUNX2 regulates osteoblast differentiation
R-HSA-8943724, Regulation of PTEN gene transcription
R-HSA-9022537, Loss of MECP2 binding ability to the NCoR/SMRT complex
R-HSA-9022692, Regulation of MECP2 expression and activity
R-HSA-9029569, NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux
R-HSA-9609690, HCMV Early Events
R-HSA-9701898, STAT3 nuclear events downstream of ALK signaling
R-HSA-9707564, Cytoprotection by HMOX1
R-HSA-9707616, Heme signaling

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		O15379

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		O15379

SIGNOR Signaling Network Open Resource

More...SIGNORi		O15379

<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%5Fand%5Ftaxonomy%5Fsection">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 3 (EC:3.5.1.981 Publication1 Publication)
Short name:
HD3
Alternative name(s):
Protein deacetylase HDAC3 (EC:3.5.1.-2 Publications1 Publication)
Protein deacylase HDAC3Curated (EC:3.5.1.-3 Publications)
RPD3-2
SMAP45
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:HDAC3
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 5

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:4854, HDAC3

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		605166, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_O15379

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000171720

<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

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi130 – 132AGG → VRPP: Impaired protein deacetylase activity without affecting the protein decrotonylase activity. 2 Publications3
Mutagenesisi298Y → F: Strongly decreased protein deacetylase activity. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		8841

Open Targets

More...OpenTargetsi		ENSG00000171720

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA29228

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		O15379, Tclin

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1829

Drug and drug target database

More...DrugBanki		DB05015, Belinostat
DB11830, Mocetinostat
DB06603, Panobinostat
DB05223, Pracinostat
DB02546, Vorinostat

DrugCentral

More...DrugCentrali		O15379

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2617

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		HDAC3

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001146961 – 428Histone deacetylase 3Add BLAST428

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 residuei424PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Sumoylated in vitro.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		O15379

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		O15379

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		O15379

MaxQB - The MaxQuant DataBase

More...MaxQBi		O15379

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

More...PaxDbi		O15379

PeptideAtlas

More...PeptideAtlasi		O15379

PRoteomics IDEntifications database

More...PRIDEi		O15379

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		48618 [O15379-1]
48619 [O15379-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		O15379

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

More...PhosphoSitePlusi		O15379

<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.

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated by disturbed flow in umbilical vein endothelial cells in vitro (PubMed:25190803).

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000171720, Expressed in right hemisphere of cerebellum and 238 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		O15379, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		O15379, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000171720, Low tissue specificity

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with HDAC7 and HDAC9 (PubMed:11466315, PubMed:10655483).

Interacts with DAXX, KDM4A, HDAC10 and DACH1 (PubMed:10669754, PubMed:11861901, PubMed:14525983, PubMed:15927959).

Found in a complex with NCOR1 and NCOR2 (PubMed:10860984).

Component of the N-Cor repressor complex, at least composed of NCOR1, NCOR2, HDAC3, TBL1X, TBL1R, CORO2A and GPS2 (PubMed:11931768).

Interacts with BCOR, MJD2A/JHDM3A, NRIP1, PRDM6 and SRY (PubMed:10898795, PubMed:11006275, PubMed:15297880).

Interacts with BTBD14B (By similarity).

Interacts with GLIS2 (By similarity).

Interacts (via the DNA-binding domain) with NR2C1; the interaction recruits phosphorylated NR2C1 to PML bodies for sumoylation (By similarity).

Component of the Notch corepressor complex (PubMed:19409814).

Interacts with CBFA2T3 and NKAP (PubMed:11533236, PubMed:19409814).

Interacts with APEX1; the interaction is not dependent on the acetylated status of APEX1 (PubMed:14633989).

Interacts with ZMYND15 (By similarity).

Interacts with SMRT/NCOR2 and BCL6 on DNA enhancer elements (PubMed:23911289).

Interacts with INSM1 (PubMed:16569215, PubMed:18417529).

Interacts with XBP1 isoform 1; the interaction occurs in endothelial cell (EC) under disturbed flow (PubMed:25190803).

Interacts (via C-terminus) with CCAR2 (via N-terminus) (PubMed:21030595).

Interacts with and deacetylates MEF2D (PubMed:21030595).

Interacts with BEND3 (PubMed:21914818).

Interacts with NKAPL (By similarity).

Interacts with DHX36; this interaction occurs in a RNA-dependent manner (PubMed:18279852).

Interacts weakly with CRY1; this interaction is enhanced in the presence of FBXL3 (By similarity).

Interacts with FBXL3 and ARNTL/BMAL1 (By similarity).

Interacts with NCOR1 (By similarity).

Interacts with RARA (PubMed:28167758).

Interacts with SETD5 (By similarity).

By similarity22 Publications

(Microbial infection) Interacts with human cytomegalovirus (HHV-5) immediate early protein IE1; this interaction decreases histone acetylation and allows transcriptional activation by the virus.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		114368, 282 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		O15379

Database of interacting proteins

More...DIPi		DIP-24253N

Protein interaction database and analysis system

More...IntActi		O15379, 110 interactors

Molecular INTeraction database

More...MINTi		O15379

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000302967

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		O15379

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		O15379, protein

<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

1428
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		O15379

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

More...SMRi		O15379

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<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>Regioni3 – 316Histone deacetylaseAdd BLAST314
Regioni388 – 428DisorderedSequence analysisAdd BLAST41

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 type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi388 – 405Basic and acidic residuesSequence analysisAdd BLAST18
Compositional biasi411 – 428Basic and acidic residuesSequence analysisAdd BLAST18

<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

Belongs to the histone deacetylase family. HD type 1 subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1342, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000160487

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_007727_7_6_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O15379

Identification of Orthologs from Complete Genome Data

More...OMAi		GWLRAFH

Database of Orthologous Groups

More...OrthoDBi		732770at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		O15379

TreeFam database of animal gene trees

More...TreeFami		TF352182

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.800.20, 1 hit

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...IDEALi		IID00428

Integrated resource of protein families, domains and functional sites

More...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

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00850, Hist_deacetyl, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF037913, His_deacetylse_1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01270, HDASUPER
PR01271, HISDACETLASE

Superfamily database of structural and functional annotation

More...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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O15379-1) [UniParc]FASTAAdd to basket
Also known as: RPD3-2B

This isoform has been chosen as the <p><strong>What is the canonical sequence?</strong><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
MAKTVAYFYD PDVGNFHYGA GHPMKPHRLA LTHSLVLHYG LYKKMIVFKP 
        60         70         80         90        100
YQASQHDMCR FHSEDYIDFL QRVSPTNMQG FTKSLNAFNV GDDCPVFPGL 
       110        120        130        140        150
FEFCSRYTGA SLQGATQLNN KICDIAINWA GGLHHAKKFE ASGFCYVNDI 
       160        170        180        190        200
VIGILELLKY HPRVLYIDID IHHGDGVQEA FYLTDRVMTV SFHKYGNYFF 
       210        220        230        240        250
PGTGDMYEVG AESGRYYCLN VPLRDGIDDQ SYKHLFQPVI NQVVDFYQPT 
       260        270        280        290        300
CIVLQCGADS LGCDRLGCFN LSIRGHGECV EYVKSFNIPL LVLGGGGYTV 
       310        320        330        340        350
RNVARCWTYE TSLLVEEAIS EELPYSEYFE YFAPDFTLHP DVSTRIENQN 
       360        370        380        390        400
SRQYLDQIRQ TIFENLKMLN HAPSVQIHDV PADLLTYDRT DEADAEERGP 
       410        420 
EENYSRPEAP NEFYDGDHDN DKESDVEI
Length:428
Mass (Da):48,848
Last modified:July 15, 1998 - 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:i94485C1EBDCF5AD0
GO
Isoform 2 (identifier: O15379-2) [UniParc]FASTAAdd to basket
Also known as: RPD3-2A

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MAKTVAYFYDPDVGN → MIVFKPYQASQHDMCR

Show »
Length:429
Mass (Da):49,111
Checksum:i0B654598513D284B
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E7ESJ6E7ESJ6_HUMAN
Histone deacetylase
HDAC3
218Annotation score:

Annotation score:2 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>
E7EW19E7EW19_HUMAN
Histone deacetylase 3
HDAC3
53Annotation 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>

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 conflicti359R → L in AAC52038 (PubMed:9464271).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_033988411N → S. Corresponds to variant dbSNP:rs34901743EnsemblClinVar.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_0020791 – 15MAKTV…PDVGN → MIVFKPYQASQHDMCR in isoform 2. 1 PublicationAdd BLAST15

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
U66914 mRNA Translation: AAC52038.1
U75697 mRNA Translation: AAB88241.1
U75696 mRNA Translation: AAB88240.1
AF005482 mRNA Translation: AAB87752.1
AF039703 mRNA Translation: AAC98927.1
AF059650 Genomic DNA Translation: AAC26509.1
CH471062 Genomic DNA Translation: EAW61915.1
CH471062 Genomic DNA Translation: EAW61916.1
BC000614 mRNA Translation: AAH00614.1
AF053138, AF053137 Genomic DNA Translation: AAC08351.1
AF053139 Genomic DNA Translation: AAC08352.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS4264.1 [O15379-1]

Protein sequence database of the Protein Information Resource

More...PIRi		JC5834

NCBI Reference Sequences

More...RefSeqi		NP_003874.2, NM_003883.3 [O15379-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000305264.8; ENSP00000302967.3; ENSG00000171720.10

Database of genes from NCBI RefSeq genomes

More...GeneIDi		8841

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:8841

Matched Annotation from NCBI and EMBL-EBI (MANE) - Phase one

More...MANE-Selecti		ENST00000305264.8; ENSP00000302967.3; NM_003883.4; NP_003874.2

UCSC genome browser

More...UCSCi		uc003llf.3, human [O15379-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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%5Freferences%5Fsection">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
U66914 mRNA Translation: AAC52038.1
U75697 mRNA Translation: AAB88241.1
U75696 mRNA Translation: AAB88240.1
AF005482 mRNA Translation: AAB87752.1
AF039703 mRNA Translation: AAC98927.1
AF059650 Genomic DNA Translation: AAC26509.1
CH471062 Genomic DNA Translation: EAW61915.1
CH471062 Genomic DNA Translation: EAW61916.1
BC000614 mRNA Translation: AAH00614.1
AF053138, AF053137 Genomic DNA Translation: AAC08351.1
AF053139 Genomic DNA Translation: AAC08352.1
CCDSiCCDS4264.1 [O15379-1]
PIRiJC5834
RefSeqiNP_003874.2, NM_003883.3 [O15379-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4A69X-ray2.06A/B1-376[»]
AlphaFoldDBiO15379
SMRiO15379
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi114368, 282 interactors
CORUMiO15379
DIPiDIP-24253N
IntActiO15379, 110 interactors
MINTiO15379
STRINGi9606.ENSP00000302967

Chemistry databases

BindingDBiO15379
ChEMBLiCHEMBL1829
DrugBankiDB05015, Belinostat
DB11830, Mocetinostat
DB06603, Panobinostat
DB05223, Pracinostat
DB02546, Vorinostat
DrugCentraliO15379
GuidetoPHARMACOLOGYi2617

PTM databases

iPTMnetiO15379
PhosphoSitePlusiO15379

Genetic variation databases

BioMutaiHDAC3

Proteomic databases

EPDiO15379
jPOSTiO15379
MassIVEiO15379
MaxQBiO15379
PaxDbiO15379
PeptideAtlasiO15379
PRIDEiO15379
ProteomicsDBi48618 [O15379-1]
48619 [O15379-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		3568, 958 antibodies from 48 providers

The DNASU plasmid repository

More...DNASUi		8841

Genome annotation databases

EnsembliENST00000305264.8; ENSP00000302967.3; ENSG00000171720.10
GeneIDi8841
KEGGihsa:8841
MANE-SelectiENST00000305264.8; ENSP00000302967.3; NM_003883.4; NP_003874.2
UCSCiuc003llf.3, human [O15379-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		8841
DisGeNETi8841

GeneCards: human genes, protein and diseases

More...GeneCardsi		HDAC3
HGNCiHGNC:4854, HDAC3
HPAiENSG00000171720, Low tissue specificity
MIMi605166, gene
neXtProtiNX_O15379
OpenTargetsiENSG00000171720
PharmGKBiPA29228
VEuPathDBiHostDB:ENSG00000171720

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1342, Eukaryota
GeneTreeiENSGT00940000160487
HOGENOMiCLU_007727_7_6_1
InParanoidiO15379
OMAiGWLRAFH
OrthoDBi732770at2759
PhylomeDBiO15379
TreeFamiTF352182

Enzyme and pathway databases

BRENDAi3.5.1.98, 2681
PathwayCommonsiO15379
ReactomeiR-HSA-1368071, NR1D1 (REV-ERBA) represses gene expression
R-HSA-193670, p75NTR negatively regulates cell cycle via SC1
R-HSA-1989781, PPARA activates gene expression
R-HSA-2122947, NOTCH1 Intracellular Domain Regulates Transcription
R-HSA-2151201, Transcriptional activation of mitochondrial biogenesis
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-350054, Notch-HLH transcription pathway
R-HSA-381340, Transcriptional regulation of white adipocyte differentiation
R-HSA-390471, Association of TriC/CCT with target proteins during biosynthesis
R-HSA-400206, Regulation of lipid metabolism by PPARalpha
R-HSA-400253, Circadian Clock
R-HSA-5617472, Activation of anterior HOX genes in hindbrain development during early embryogenesis
R-HSA-8940973, RUNX2 regulates osteoblast differentiation
R-HSA-8943724, Regulation of PTEN gene transcription
R-HSA-9022537, Loss of MECP2 binding ability to the NCoR/SMRT complex
R-HSA-9022692, Regulation of MECP2 expression and activity
R-HSA-9029569, NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux
R-HSA-9609690, HCMV Early Events
R-HSA-9701898, STAT3 nuclear events downstream of ALK signaling
R-HSA-9707564, Cytoprotection by HMOX1
R-HSA-9707616, Heme signaling
SABIO-RKiO15379
SignaLinkiO15379
SIGNORiO15379

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		8841, 713 hits in 1084 CRISPR screens

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

More...ChiTaRSi		HDAC3, human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		HDAC3

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

More...GenomeRNAii		8841
PharosiO15379, Tclin

Protein Ontology

More...PROi		PR:O15379
RNActiO15379, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000171720, Expressed in right hemisphere of cerebellum and 238 other tissues
ExpressionAtlasiO15379, baseline and differential
GenevisibleiO15379, HS

Family and domain databases

Gene3Di3.40.800.20, 1 hit
IDEALiIID00428
InterProiView protein in InterPro
IPR000286, His_deacetylse
IPR003084, His_deacetylse_1
IPR023801, His_deacetylse_dom
IPR037138, His_deacetylse_dom_sf
IPR023696, Ureohydrolase_dom_sf
PfamiView protein in Pfam
PF00850, Hist_deacetyl, 1 hit
PIRSFiPIRSF037913, His_deacetylse_1, 1 hit
PRINTSiPR01270, HDASUPER
PR01271, HISDACETLASE
SUPFAMiSSF52768, SSF52768, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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 nameiHDAC3_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: O15379
Secondary accession number(s): D3DQE1
, O43268, Q9UEI5, Q9UEV0
<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%5Fand%5Fisoforms">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: July 15, 1998
Last modified: May 25, 2022
This is version 224 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, Reference proteome

Documents

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