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Protein

Histone deacetylase 4

Gene

Hdac4

Organism
Mus musculus (Mouse)
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. Deacetylates HSPA1A and HSPA1A at 'Lys-77' leading to their preferential binding to co-chaperone STUB1.By similarity

<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 bindingi664ZincBy similarity1
Metal bindingi666ZincBy similarity1
Metal bindingi672ZincBy similarity1
Metal bindingi743ZincBy 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 sitei795By 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

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-4090294 SUMOylation of intracellular receptors
R-MMU-4551638 SUMOylation of chromatin organization proteins
R-MMU-8951936 RUNX3 regulates p14-ARF

<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
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 1

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:3036234 Hdac4

<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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3832944

<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_00002810331 – 1076Histone deacetylase 4Add BLAST1076

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 residuei209PhosphoserineCombined sources1
Modified residuei245Phosphoserine; by CaMK4 and SIK11 Publication1
Modified residuei349PhosphoserineBy similarity1
Modified residuei465Phosphoserine; by CaMK4 and SIK1Combined sources1 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-linki556Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei562PhosphoserineCombined sources1
Modified residuei629Phosphoserine; by CaMK4By similarity1
Modified residuei630PhosphoserineBy similarity1

<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-245, Ser-465 and Ser-629. Phosphorylation at other residues by CaMK2D is required for the interaction with 14-3-3. Phosphorylation at Ser-349, within the PxLPxI/L motif, impairs the binding of ANKRA2 but generates a high-affinity docking site for 14-3-3 (By similarity).By similarity
Sumoylation on Lys-556 is promoted by the E3 SUMO-protein ligase RANBP2, and prevented by phosphorylation by CaMK4.2 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q6NZM9

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

More...
PaxDbi
Q6NZM9

PeptideAtlas

More...
PeptideAtlasi
Q6NZM9

PRoteomics IDEntifications database

More...
PRIDEi
Q6NZM9

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q6NZM9

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

More...
PhosphoSitePlusi
Q6NZM9

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000026313 Expressed in 240 organ(s), highest expression level in ear vesicle

CleanEx database of gene expression profiles

More...
CleanExi
MM_HDAC4

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q6NZM9 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q6NZM9 MM

<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 (By similarity). Interacts with HDAC7 (PubMed:10984530). Interacts with MEF2A, MEF2C, MEF2D, MORC2 and NR2C1. Interacts with a 14-3-3 chaperone protein in a phosphorylation dependent manner. Interacts with BTBD14B. Interacts with KDM5B. Interacts (via PxLPxI/L motif) with ANKRA2 (via ankyrin repeats). Interacts with CUL7 (as part of the 3M complex); negatively regulated by ANKRA2. Interacts with EP300 in the presence of TFAP2C (By similarity). Interacts with AHRR (PubMed:17949687). Interacts with MYOCD (PubMed:15601857). Interacts with HSPA1A and HSPA1B leading to their deacetylation at 'Lys-77' (By similarity). Interacts with ZBTB7B; the interaction allows the recruitment of HDAC4 on CD8 loci for deacetylation and possible inhibition of CD8 genes expression (PubMed:22730529). Interacts with DHX36 (PubMed:21590736).By similarity5 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)

More...
BioGridi
229009, 15 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q6NZM9

Database of interacting proteins

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DIPi
DIP-36317N

Protein interaction database and analysis system

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IntActi
Q6NZM9, 10 interactors

Molecular INTeraction database

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MINTi
Q6NZM9

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000008995

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q6NZM9

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

More...
SMRi
Q6NZM9

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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>Regioni117 – 312Interaction with MEF2ABy similarityAdd BLAST196
Regioni652 – 1076Histone deacetylaseBy similarityAdd BLAST425

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 coili66 – 169Sequence analysisAdd BLAST104

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>Motifi348 – 353PxLPxI/L motif; mediates interaction with ANKRA2 and 14-3-3 proteinsBy similarity6
Motifi1043 – 1076Nuclear export signalBy similarityAdd BLAST34

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 biasi464 – 499Gln-richAdd BLAST36
Compositional biasi561 – 568Poly-Glu8

<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.By similarity
The PxLPxI/L motif mediates interaction with ankyrin repeats of ANKRA2.By similarity

<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

More...
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

More...
HOVERGENi
HBG057100

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q6NZM9

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

More...
OrthoDBi
EOG091G0EQO

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q6NZM9

TreeFam database of animal gene trees

More...
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

More...
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

More...
PIRSFi
PIRSF037911 HDAC_II_euk, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01270 HDASUPER

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_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 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q6NZM9-1) [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 QVAPTAVPMD
60 70 80 90 100
LRLDHQFSLP LEPALREQQL QQELLALKQK QQIQRQILIA EFQRQHEQLS
110 120 130 140 150
RQHEAQLHEH IKQQQEMLAM KHQQELLEHQ RKLERHRQEQ ELEKQHREQK
160 170 180 190 200
LQQLKNKEKG KESAVASTEV KMKLQEFVLN KKKALAHRNL NHCISSDPRY
210 220 230 240 250
WYGKTQHSSL DQSSPPQSGV SASYNHPVLG MYDAKDDFPL RKTASEPNLK
260 270 280 290 300
LRSRLKQKVA ERRSSPLLRR KDGPVATALK KRPLDVTDSA CSSAPGSGPS
310 320 330 340 350
SPNSSSGNVS TENGIAPTVP SAPAETSLAH RLVTREGSVA PLPLYTSPSL
360 370 380 390 400
PNITLGLPAT GPAAGAAGQQ DAERLALPAL QQRILFPGTH LTPYLSTSPL
410 420 430 440 450
ERDGAAAHNP LLQHMVLLEQ PPTQTPLVTG LGALPLHSQS LVGADRVSPS
460 470 480 490 500
IHKLRQHRPL GRTQSAPLPQ NAQALQHLVI QQQHQQFLEK HKQQFQQQQL
510 520 530 540 550
HLSKIISKPS EPPRQPESHP EETEEELREH QALLDEPYLD RLPGQKEPSL
560 570 580 590 600
AGVQVKQEPI ESEEEEAEAT RETEPGQRPA TEQELLFRQQ ALLLEQQRIH
610 620 630 640 650
QLRNYQASME AAGIPVSFGS HRPLSRAQSS PASATFPMSV QEPPTKPRFT
660 670 680 690 700
TGLVYDTLML KHQCTCGNTN SHPEHAGRIQ SIWSRLQETG LRGKCECIRG
710 720 730 740 750
RKATLEELQT VHSEAHTLLY GTNPLNRQKL DSSLTSVFVR LPCGGVGVDS
760 770 780 790 800
DTIWNEVHSS GAARLAVGCV VELVFKVATG ELKNGFAVVR PPGHHAEEST
810 820 830 840 850
PMGFCYFNSV AVAAKLLQQR LNVSKILIVD WDVHHGNGTQ QAFYNDPNVL
860 870 880 890 900
YMSLHRYDDG NFFPGSGAPD EVGTGPGVGF NVNMAFTGGL EPPMGDAEYL
910 920 930 940 950
AAFRTVVMPI ANEFAPDVVL VSSGFDAVEG HPTPLGGYNL SAKCFGYLTK
960 970 980 990 1000
QLMGLAGGRL VLALEGGHDL TAICDASEAC VSALLGNELE PLPEKVLHQR
1010 1020 1030 1040 1050
PNANAVHSME KVMDIHSKYW RCLQRLSSTV GHSLIEAQKC EKEEAETVTA
1060 1070
MASLSVGVKP AEKRSEEEPM EEEPPL
Length:1,076
Mass (Da):118,562
Last modified:July 5, 2004 - v1
<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:iA3CCC3CCCBB903A0
GO
Isoform 2 (identifier: Q6NZM9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-171: Missing.
     732-732: S → SKKLLG

Note: No experimental confirmation available.
Show »
Length:910
Mass (Da):99,124
Checksum:i80C1A8CA5567EE19
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
A0A087WSF0A0A087WSF0_MOUSE
Histone deacetylase 4
Hdac4
112Annotation score:

Annotation score:3 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>
A0A087WQ92A0A087WQ92_MOUSE
Histone deacetylase 4
Hdac4
312Annotation score:

Annotation score:3 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 conflicti569A → S in BAE33147 (PubMed:16141072).Curated1
Sequence conflicti904R → K in BAE33147 (PubMed:16141072).Curated1

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_0239521 – 171Missing in isoform 2. 1 PublicationAdd BLAST171
Alternative sequenceiVSP_023953732S → SKKLLG in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AK029933 mRNA Translation: BAE43272.1
AK155250 mRNA Translation: BAE33147.1
AK162369 mRNA Translation: BAE36877.1
BC066052 mRNA Translation: AAH66052.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS48324.1 [Q6NZM9-1]

NCBI Reference Sequences

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RefSeqi
NP_997108.1, NM_207225.2 [Q6NZM9-1]
XP_017174977.1, XM_017319488.1 [Q6NZM9-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.318567

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000008995; ENSMUSP00000008995; ENSMUSG00000026313 [Q6NZM9-1]
ENSMUST00000097644; ENSMUSP00000095249; ENSMUSG00000026313 [Q6NZM9-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
208727

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:208727

UCSC genome browser

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UCSCi
uc007cbe.2 mouse [Q6NZM9-2]
uc007cbf.2 mouse [Q6NZM9-1]

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK029933 mRNA Translation: BAE43272.1
AK155250 mRNA Translation: BAE33147.1
AK162369 mRNA Translation: BAE36877.1
BC066052 mRNA Translation: AAH66052.1
CCDSiCCDS48324.1 [Q6NZM9-1]
RefSeqiNP_997108.1, NM_207225.2 [Q6NZM9-1]
XP_017174977.1, XM_017319488.1 [Q6NZM9-1]
UniGeneiMm.318567

3D structure databases

ProteinModelPortaliQ6NZM9
SMRiQ6NZM9
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi229009, 15 interactors
CORUMiQ6NZM9
DIPiDIP-36317N
IntActiQ6NZM9, 10 interactors
MINTiQ6NZM9
STRINGi10090.ENSMUSP00000008995

Chemistry databases

ChEMBLiCHEMBL3832944

PTM databases

iPTMnetiQ6NZM9
PhosphoSitePlusiQ6NZM9

Proteomic databases

EPDiQ6NZM9
PaxDbiQ6NZM9
PeptideAtlasiQ6NZM9
PRIDEiQ6NZM9

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000008995; ENSMUSP00000008995; ENSMUSG00000026313 [Q6NZM9-1]
ENSMUST00000097644; ENSMUSP00000095249; ENSMUSG00000026313 [Q6NZM9-1]
GeneIDi208727
KEGGimmu:208727
UCSCiuc007cbe.2 mouse [Q6NZM9-2]
uc007cbf.2 mouse [Q6NZM9-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
9759
MGIiMGI:3036234 Hdac4

Phylogenomic databases

eggNOGiKOG1343 Eukaryota
COG0123 LUCA
GeneTreeiENSGT00940000157440
HOGENOMiHOG000232065
HOVERGENiHBG057100
InParanoidiQ6NZM9
KOiK11406
OMAiVEAQKCE
OrthoDBiEOG091G0EQO
PhylomeDBiQ6NZM9
TreeFamiTF106174

Enzyme and pathway databases

ReactomeiR-MMU-4090294 SUMOylation of intracellular receptors
R-MMU-4551638 SUMOylation of chromatin organization proteins
R-MMU-8951936 RUNX3 regulates p14-ARF

Miscellaneous databases

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

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ChiTaRSi
Hdac4 mouse

Protein Ontology

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PROi
PR:Q6NZM9

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000026313 Expressed in 240 organ(s), highest expression level in ear vesicle
CleanExiMM_HDAC4
ExpressionAtlasiQ6NZM9 baseline and differential
GenevisibleiQ6NZM9 MM

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

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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_MOUSE
<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: Q6NZM9
Secondary accession number(s): Q3TRZ9, Q3U2J3, Q3V3Y4
<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: March 20, 2007
Last sequence update: July 5, 2004
Last modified: December 5, 2018
This is version 131 of the entry and version 1 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

<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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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