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Protein

Histone deacetylase 4

Gene

HDAC4

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. Involved in muscle maturation via its interaction with the myocyte enhancer factors such as MEF2A, MEF2C and MEF2D. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. Deacetylates HSPA1A and HSPA1B at 'Lys-77' leading to their preferential binding to co-chaperone STUB1 (PubMed:27708256).3 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 indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi667ZincBy similarity1
Metal bindingi669ZincBy similarity1
Metal bindingi675ZincBy similarity1
Metal bindingi751ZincBy similarity1
<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 sitei803By 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 processTranscription, Transcription regulation
LigandMetal-binding, Zinc

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-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-4090294 SUMOylation of intracellular receptors
R-HSA-4551638 SUMOylation of chromatin organization proteins
R-HSA-8941284 RUNX2 regulates chondrocyte maturation
R-HSA-8951936 RUNX3 regulates p14-ARF

SIGNOR Signaling Network Open Resource

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SIGNORi
P56524

<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 4 (EC:3.5.1.98)
Short name:
HD4
<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:HDAC4
Synonyms:KIAA0288
<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 2

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000068024.16

Human Gene Nomenclature Database

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HGNCi
HGNC:14063 HDAC4

Online Mendelian Inheritance in Man (OMIM)

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MIMi
605314 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P56524

<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; 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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Brachydactyly-mental retardation syndrome (BDMR)3 Publications
The gene represented in this entry is involved in disease pathogenesis. HDAC4 point mutations and chromosomal microdeletions encompassing this gene have been found in BDMR patients (PubMed:20691407, PubMed:24715439, PubMed:23188045). However, HDAC4 haploinsufficiency is not fully penetrant and multiple genes may contribute to manifestation of the full phenotypic spectrum (PubMed:24715439, PubMed:23188045).3 Publications
Disease descriptionA syndrome resembling the physical anomalies found in Albright hereditary osteodystrophy. Common features are mild facial dysmorphism, congenital heart defects, distinct brachydactyly type E, mental retardation, developmental delay, seizures, autism spectrum disorder, and stocky build. Soft tissue ossification is absent, and there are no abnormalities in parathyroid hormone or calcium metabolism.
See also OMIM:600430

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi246S → A: Reduces phosphorylation and its subsequent nuclear export. 1 Publication1
Mutagenesisi345L → A: No effect on interaction with ANKRA2. 1 Publication1
Mutagenesisi346Y → A: No effect on interaction with ANKRA2. 1 Publication1
Mutagenesisi347T → A: No effect on interaction with ANKRA2. 1 Publication1
Mutagenesisi348S → A: No effect on interaction with ANKRA2. 1 Publication1
Mutagenesisi349P → A: May affect interaction with ANKRA2. 2 Publications1
Mutagenesisi349P → G: Decreased interaction with ANKRA2. 1 Publication1
Mutagenesisi350S → A: No effect on interaction with ANKRA2. 1 Publication1
Mutagenesisi351L → A or G: Loss of interaction with ANKRA2. 1 Publication1
Mutagenesisi352P → A: Loss of interaction with ANKRA2. 1 Publication1
Mutagenesisi353N → A: No effect on interaction with ANKRA2. 1 Publication1
Mutagenesisi354I → A: May affect interaction with ANKRA2. 2 Publications1
Mutagenesisi354I → G: Loss of interaction with ANKRA2. 1 Publication1
Mutagenesisi355T → A: No effect on interaction with ANKRA2. 1 Publication1
Mutagenesisi356L → A: No effect on interaction with ANKRA2. 1 Publication1
Mutagenesisi467S → A: Reduces phosphorylation and its subsequent nuclear export. 2 Publications1
Mutagenesisi559K → R: Abolishes sumoylation and reduces the histone deacetylase activity. 1 Publication1
Mutagenesisi632S → A: Reduces phosphorylation and its subsequent nuclear export. 2 Publications1
Mutagenesisi803H → L: Abolishes histone deacetylase activity. 1 Publication1
Mutagenesisi1056V → A: Reduces CaMK-dependent nuclear export. 1 Publication1
Mutagenesisi1062L → A: Reduces CaMK-dependent nuclear export. 1 Publication1

Keywords - Diseasei

Autism spectrum disorder, Mental retardation

Organism-specific databases

DisGeNET

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DisGeNETi
9759

MalaCards human disease database

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MalaCardsi
HDAC4
MIMi600430 phenotype

Open Targets

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OpenTargetsi
ENSG00000068024

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
1001 2q37 microdeletion syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA29229

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3524

Drug and drug target database

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DrugBanki
DB05015 Belinostat
DB06603 Panobinostat
DB06176 Romidepsin

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2659

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
HDAC4

Domain mapping of disease mutations (DMDM)

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DMDMi
259016348

<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_00001146991 – 1084Histone deacetylase 4Add BLAST1084

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 residuei210PhosphoserineBy similarity1
Modified residuei246Phosphoserine; by CaMK4 and SIK11 Publication1
Modified residuei350PhosphoserineCombined sources1 Publication1
Modified residuei467Phosphoserine; by CaMK4 and SIK11 Publication1
<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-linki559Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei565PhosphoserineBy similarity1
Modified residuei632Phosphoserine; by CaMK4Combined sources1 Publication1
Modified residuei633PhosphoserineCombined sources1

<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

Phosphorylated by CaMK4 at Ser-246, Ser-467 and Ser-632. Phosphorylation at other residues by CaMK2D is required for the interaction with 14-3-3. Phosphorylation at Ser-350, within the PxLPxI/L motif, impairs the binding of ANKRA2 but generates a high-affinity docking site for 14-3-3.2 Publications
Sumoylation on Lys-559 is promoted by the E3 SUMO-protein ligase RANBP2, and prevented by phosphorylation by CaMK4.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P56524

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P56524

MaxQB - The MaxQuant DataBase

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MaxQBi
P56524

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

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PaxDbi
P56524

PeptideAtlas

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PeptideAtlasi
P56524

PRoteomics IDEntifications database

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PRIDEi
P56524

ProteomicsDB human proteome resource

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ProteomicsDBi
56920

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P56524

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

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PhosphoSitePlusi
P56524

<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

Ubiquitous.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000068024 Expressed in 215 organ(s), highest expression level in gluteal muscle

CleanEx database of gene expression profiles

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CleanExi
HS_HDAC4

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P56524 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P56524 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB004431
HPA048723

<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

Homodimer. Homodimerization via its N-terminal domain (PubMed:12032081). Interacts with MEF2A (PubMed:10487761). Interacts with MEF2C and MEF2D (PubMed:10523670). Interacts with AHRR (By similarity). Interacts with NR2C1 (PubMed:11463856). Interacts with HDAC7 (By similarity). Interacts with a 14-3-3 chaperone protein in a phosphorylation dependent manner (PubMed:10958686). Interacts with BTBD14B (By similarity). Interacts with KDM5B (PubMed:17373667). Interacts with MYOCD (By similarity). Interacts with MORC2 (PubMed:20110259). Interacts (via PxLPxI/L motif) with ANKRA2 (via ankyrin repeats). Interacts with CUL7 (as part of the 3M complex); negatively regulated by ANKRA2 (PubMed:25752541). Interacts with EP300 in the presence of TFAP2C (PubMed:24413532). Interacts with HSPA1A and HSPA1B leading to their deacetylation at 'Lys-77' (PubMed:27708256). Interacts with ZBTB7B; the interaction allows the recruitment of HDAC4 on CD8 loci for deacetylation and possible inhibition of CD8 genes expression (By similarity). Interacts with DHX36 (By similarity).By similarity10 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
115106, 352 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P56524

Database of interacting proteins

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DIPi
DIP-34565N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P56524

Protein interaction database and analysis system

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IntActi
P56524, 85 interactors

Molecular INTeraction database

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MINTi
P56524

STRING: functional protein association networks

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STRINGi
9606.ENSP00000264606

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P56524

<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

11084
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
2H8NX-ray2.60A/B/C/D62-153[»]
2O94X-ray3.00A/B/C/D62-153[»]
2VQJX-ray2.10A648-1057[»]
2VQMX-ray1.80A648-1057[»]
2VQOX-ray2.15A/B648-1057[»]
2VQQX-ray1.90A/B648-1057[»]
2VQVX-ray3.30A/B648-1057[»]
2VQWX-ray3.00G648-1057[»]
3UXGX-ray1.85B343-359[»]
3UZDX-ray1.86B343-359[»]
3V31X-ray1.57B343-359[»]
4CBTX-ray3.03A/B/C648-1033[»]
4CBYX-ray2.72A/B/C/D648-1033[»]
5A2SX-ray2.65A/B648-1033[»]
5ZOOX-ray1.85G652-1053[»]
5ZOPX-ray2.70G652-1050[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P56524

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

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SMRi
P56524

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
P56524

<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>Regioni118 – 313Interaction with MEF2A1 PublicationAdd BLAST196
Regioni655 – 1084Histone deacetylaseAdd BLAST430

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili67 – 177Sequence analysisAdd BLAST111

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi349 – 354PxLPxI/L motif; mediates interaction with ANKRA2 and 14-3-3 proteins1 Publication6
Motifi1051 – 1084Nuclear export signalBy similarityAdd BLAST34

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The nuclear export sequence mediates the shuttling between the nucleus and the cytoplasm.
The PxLPxI/L motif mediates interaction with ankyrin repeats of ANKRA2.1 Publication

<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

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1343 Eukaryota
COG0123 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000157440

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000232065

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG057100

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P56524

KEGG Orthology (KO)

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KOi
K11406

Identification of Orthologs from Complete Genome Data

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OMAi
VEAQKCE

Database of Orthologous Groups

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OrthoDBi
1484694at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P56524

TreeFam database of animal gene trees

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TreeFami
TF106174

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
IPR033660 HDAC4
IPR000286 His_deacetylse
IPR023801 His_deacetylse_dom
IPR037138 His_deacetylse_dom_sf
IPR024643 Hist_deacetylase_Gln_rich_N
IPR017320 Histone_deAcase_II_euk
IPR023696 Ureohydrolase_dom_sf

The PANTHER Classification System

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PANTHERi
PTHR10625 PTHR10625, 1 hit
PTHR10625:SF100 PTHR10625:SF100, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF12203 HDAC4_Gln, 1 hit
PF00850 Hist_deacetyl, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF037911 HDAC_II_euk, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR01270 HDASUPER

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 5 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P56524-1) [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
MSSQSHPDGL SGRDQPVELL NPARVNHMPS TVDVATALPL QVAPSAVPMD
60 70 80 90 100
LRLDHQFSLP VAEPALREQQ LQQELLALKQ KQQIQRQILI AEFQRQHEQL
110 120 130 140 150
SRQHEAQLHE HIKQQQEMLA MKHQQELLEH QRKLERHRQE QELEKQHREQ
160 170 180 190 200
KLQQLKNKEK GKESAVASTE VKMKLQEFVL NKKKALAHRN LNHCISSDPR
210 220 230 240 250
YWYGKTQHSS LDQSSPPQSG VSTSYNHPVL GMYDAKDDFP LRKTASEPNL
260 270 280 290 300
KLRSRLKQKV AERRSSPLLR RKDGPVVTAL KKRPLDVTDS ACSSAPGSGP
310 320 330 340 350
SSPNNSSGSV SAENGIAPAV PSIPAETSLA HRLVAREGSA APLPLYTSPS
360 370 380 390 400
LPNITLGLPA TGPSAGTAGQ QDAERLTLPA LQQRLSLFPG THLTPYLSTS
410 420 430 440 450
PLERDGGAAH SPLLQHMVLL EQPPAQAPLV TGLGALPLHA QSLVGADRVS
460 470 480 490 500
PSIHKLRQHR PLGRTQSAPL PQNAQALQHL VIQQQHQQFL EKHKQQFQQQ
510 520 530 540 550
QLQMNKIIPK PSEPARQPES HPEETEEELR EHQALLDEPY LDRLPGQKEA
560 570 580 590 600
HAQAGVQVKQ EPIESDEEEA EPPREVEPGQ RQPSEQELLF RQQALLLEQQ
610 620 630 640 650
RIHQLRNYQA SMEAAGIPVS FGGHRPLSRA QSSPASATFP VSVQEPPTKP
660 670 680 690 700
RFTTGLVYDT LMLKHQCTCG SSSSHPEHAG RIQSIWSRLQ ETGLRGKCEC
710 720 730 740 750
IRGRKATLEE LQTVHSEAHT LLYGTNPLNR QKLDSKKLLG SLASVFVRLP
760 770 780 790 800
CGGVGVDSDT IWNEVHSAGA ARLAVGCVVE LVFKVATGEL KNGFAVVRPP
810 820 830 840 850
GHHAEESTPM GFCYFNSVAV AAKLLQQRLS VSKILIVDWD VHHGNGTQQA
860 870 880 890 900
FYSDPSVLYM SLHRYDDGNF FPGSGAPDEV GTGPGVGFNV NMAFTGGLDP
910 920 930 940 950
PMGDAEYLAA FRTVVMPIAS EFAPDVVLVS SGFDAVEGHP TPLGGYNLSA
960 970 980 990 1000
RCFGYLTKQL MGLAGGRIVL ALEGGHDLTA ICDASEACVS ALLGNELDPL
1010 1020 1030 1040 1050
PEKVLQQRPN ANAVRSMEKV MEIHSKYWRC LQRTTSTAGR SLIEAQTCEN
1060 1070 1080
EEAETVTAMA SLSVGVKPAE KRPDEEPMEE EPPL
Length:1,084
Mass (Da):119,040
Last modified:September 22, 2009 - v3
<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:iBB7FD37652D12398
GO
Isoform 2 (identifier: P56524-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-117: Missing.
     431-431: T → TDWYLS

Note: No experimental confirmation available.
Show »
Length:972
Mass (Da):106,367
Checksum:i86E58F178B37FDC6
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 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
C9J0X4C9J0X4_HUMAN
Histone deacetylase 4
HDAC4
123Annotation 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>
C9J481C9J481_HUMAN
Histone deacetylase 4
HDAC4
162Annotation 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>
H7C397H7C397_HUMAN
Histone deacetylase 4
HDAC4
175Annotation 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>
H7BZT3H7BZT3_HUMAN
Histone deacetylase 4
HDAC4
148Annotation 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>
F5H0B1F5H0B1_HUMAN
Histone deacetylase 4
HDAC4
29Annotation 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 BAA22957 differs from that shown. Reason: Erroneous initiation.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 conflicti373A → T in AAD29046 (PubMed:10220385).Curated1
Sequence conflicti373A → T in BAA22957 (PubMed:9179496).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_036042727P → R in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_071965754V → I1 PublicationCorresponds to variant dbSNP:rs151043798Ensembl.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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0572901 – 117Missing in isoform 2. 1 PublicationAdd BLAST117
Alternative sequenceiVSP_057291431T → TDWYLS in isoform 2. 1 Publication1

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
AF132607 mRNA Translation: AAD29046.1
AB006626 mRNA Translation: BAA22957.2 Different initiation.
AC017028 Genomic DNA No translation available.
AC062017 Genomic DNA No translation available.
KF510800 Genomic DNA No translation available.
KF510801 Genomic DNA No translation available.
CH471063 Genomic DNA Translation: EAW71165.1
BC039904 mRNA Translation: AAH39904.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS2529.1 [P56524-1]

NCBI Reference Sequences

More...
RefSeqi
NP_006028.2, NM_006037.3 [P56524-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.20516

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000345617; ENSP00000264606; ENSG00000068024 [P56524-1]
ENST00000543185; ENSP00000440481; ENSG00000068024 [P56524-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
9759

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:9759

UCSC genome browser

More...
UCSCi
uc002vyk.4 human [P56524-1]

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF132607 mRNA Translation: AAD29046.1
AB006626 mRNA Translation: BAA22957.2 Different initiation.
AC017028 Genomic DNA No translation available.
AC062017 Genomic DNA No translation available.
KF510800 Genomic DNA No translation available.
KF510801 Genomic DNA No translation available.
CH471063 Genomic DNA Translation: EAW71165.1
BC039904 mRNA Translation: AAH39904.1
CCDSiCCDS2529.1 [P56524-1]
RefSeqiNP_006028.2, NM_006037.3 [P56524-1]
UniGeneiHs.20516

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2H8NX-ray2.60A/B/C/D62-153[»]
2O94X-ray3.00A/B/C/D62-153[»]
2VQJX-ray2.10A648-1057[»]
2VQMX-ray1.80A648-1057[»]
2VQOX-ray2.15A/B648-1057[»]
2VQQX-ray1.90A/B648-1057[»]
2VQVX-ray3.30A/B648-1057[»]
2VQWX-ray3.00G648-1057[»]
3UXGX-ray1.85B343-359[»]
3UZDX-ray1.86B343-359[»]
3V31X-ray1.57B343-359[»]
4CBTX-ray3.03A/B/C648-1033[»]
4CBYX-ray2.72A/B/C/D648-1033[»]
5A2SX-ray2.65A/B648-1033[»]
5ZOOX-ray1.85G652-1053[»]
5ZOPX-ray2.70G652-1050[»]
ProteinModelPortaliP56524
SMRiP56524
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115106, 352 interactors
CORUMiP56524
DIPiDIP-34565N
ELMiP56524
IntActiP56524, 85 interactors
MINTiP56524
STRINGi9606.ENSP00000264606

Chemistry databases

BindingDBiP56524
ChEMBLiCHEMBL3524
DrugBankiDB05015 Belinostat
DB06603 Panobinostat
DB06176 Romidepsin
GuidetoPHARMACOLOGYi2659

PTM databases

iPTMnetiP56524
PhosphoSitePlusiP56524

Polymorphism and mutation databases

BioMutaiHDAC4
DMDMi259016348

Proteomic databases

EPDiP56524
jPOSTiP56524
MaxQBiP56524
PaxDbiP56524
PeptideAtlasiP56524
PRIDEiP56524
ProteomicsDBi56920

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000345617; ENSP00000264606; ENSG00000068024 [P56524-1]
ENST00000543185; ENSP00000440481; ENSG00000068024 [P56524-2]
GeneIDi9759
KEGGihsa:9759
UCSCiuc002vyk.4 human [P56524-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
9759
DisGeNETi9759
EuPathDBiHostDB:ENSG00000068024.16

GeneCards: human genes, protein and diseases

More...
GeneCardsi
HDAC4
HGNCiHGNC:14063 HDAC4
HPAiCAB004431
HPA048723
MalaCardsiHDAC4
MIMi600430 phenotype
605314 gene
neXtProtiNX_P56524
OpenTargetsiENSG00000068024
Orphaneti1001 2q37 microdeletion syndrome
PharmGKBiPA29229

Human Unidentified Gene-Encoded large proteins database

More...
HUGEi
Search...

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1343 Eukaryota
COG0123 LUCA
GeneTreeiENSGT00940000157440
HOGENOMiHOG000232065
HOVERGENiHBG057100
InParanoidiP56524
KOiK11406
OMAiVEAQKCE
OrthoDBi1484694at2759
PhylomeDBiP56524
TreeFamiTF106174

Enzyme and pathway databases

BRENDAi3.5.1.98 2681
ReactomeiR-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-4090294 SUMOylation of intracellular receptors
R-HSA-4551638 SUMOylation of chromatin organization proteins
R-HSA-8941284 RUNX2 regulates chondrocyte maturation
R-HSA-8951936 RUNX3 regulates p14-ARF
SIGNORiP56524

Miscellaneous databases

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

More...
ChiTaRSi
HDAC4 human
EvolutionaryTraceiP56524

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
HDAC4

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

More...
GenomeRNAii
9759

Protein Ontology

More...
PROi
PR:P56524

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000068024 Expressed in 215 organ(s), highest expression level in gluteal muscle
CleanExiHS_HDAC4
ExpressionAtlasiP56524 baseline and differential
GenevisibleiP56524 HS

Family and domain databases

Gene3Di3.40.800.20, 1 hit
InterProiView protein in InterPro
IPR033660 HDAC4
IPR000286 His_deacetylse
IPR023801 His_deacetylse_dom
IPR037138 His_deacetylse_dom_sf
IPR024643 Hist_deacetylase_Gln_rich_N
IPR017320 Histone_deAcase_II_euk
IPR023696 Ureohydrolase_dom_sf
PANTHERiPTHR10625 PTHR10625, 1 hit
PTHR10625:SF100 PTHR10625:SF100, 1 hit
PfamiView protein in Pfam
PF12203 HDAC4_Gln, 1 hit
PF00850 Hist_deacetyl, 1 hit
PIRSFiPIRSF037911 HDAC_II_euk, 1 hit
PRINTSiPR01270 HDASUPER
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 nameiHDAC4_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: P56524
Secondary accession number(s): E9PGB9
, F5GX36, Q86YH7, Q9UND6
<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: September 22, 2009
Last modified: January 16, 2019
This is version 198 of the entry and version 3 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 chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  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. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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