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UniProtKB - Q99P99 (HDAC4_RAT)

Entry version 129 (29 Sep 2021)
Sequence version 2 (20 Mar 2007)
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Protein

Histone deacetylase 4

Gene

Hdac4

Organism
Rattus norvegicus (Rat)
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 HSPA1B 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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi665ZincBy similarity1
Metal bindingi667ZincBy similarity1
Metal bindingi673ZincBy similarity1
Metal bindingi744ZincBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei796By 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 processTranscription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-RNO-350054, Notch-HLH transcription pathway
R-RNO-4090294, SUMOylation of intracellular receptors
R-RNO-4551638, SUMOylation of chromatin organization proteins
R-RNO-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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<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
  • UP000002494 <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 9

Organism-specific databases

Rat genome database

More...RGDi		619979, 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

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		CHEMBL2095943

DrugCentral

More...DrugCentrali		Q99P99

<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_00002810341 – 1077Histone deacetylase 4Add BLAST1077

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 residuei209PhosphoserineBy similarity1
Modified residuei245Phosphoserine; by CaMK4 and SIK1By similarity1
Modified residuei349PhosphoserineBy similarity1
Modified residuei466Phosphoserine; by CaMK4 and SIK1By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki557Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei563PhosphoserineCombined sources1
Modified residuei630PhosphoserineCombined sources1
Modified residuei631PhosphoserineBy 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-466 and Ser-630. 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-557 is promoted by the E3 SUMO-protein ligase RANBP2, and prevented by phosphorylation by CaMK4.

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...PaxDbi		Q99P99

PRoteomics IDEntifications database

More...PRIDEi		Q99P99

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q99P99

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

More...PhosphoSitePlusi		Q99P99

<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		ENSRNOG00000020372, Expressed in frontal cortex and 21 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q99P99, RN

<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.

Interacts with HDAC7.

Interacts with MEF2A, MEF2C, MEF2D, MORC2 and NR2C1.

Interacts with a 14-3-3 chaperone protein in a phosphorylation dependent manner.

Interacts with KDM5B and AHRR (By similarity).

Interacts with BTBD14B (PubMed:16033423).

Interacts with MYOCD.

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.

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 (By similarity).

Interacts with DHX36 (By similarity).

Interacts with SIK3; this interaction leads to HDAC4 retention in the cytoplasm (By similarity).

By similarity1 Publication

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		264106, 4 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q99P99

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000027622

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q99P99

<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

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

More...SMRi		Q99P99

Database of comparative protein structure models

More...ModBasei		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
Regioni132 – 167DisorderedSequence analysisAdd BLAST36
Regioni204 – 225DisorderedSequence analysisAdd BLAST22
Regioni239 – 327DisorderedSequence analysisAdd BLAST89
Regioni508 – 530DisorderedSequence analysisAdd BLAST23
Regioni542 – 582DisorderedSequence analysisAdd BLAST41
Regioni623 – 646DisorderedSequence analysisAdd BLAST24
Regioni653 – 1077Histone deacetylaseBy similarityAdd BLAST425
Regioni1052 – 1077DisorderedSequence analysisAdd BLAST26

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
Motifi1044 – 1077Nuclear 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 type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi132 – 166Basic and acidic residuesSequence analysisAdd BLAST35
Compositional biasi204 – 224Polar residuesSequence analysisAdd BLAST21
Compositional biasi239 – 278Basic and acidic residuesSequence analysisAdd BLAST40
Compositional biasi290 – 327Polar residuesSequence analysisAdd BLAST38
Compositional biasi515 – 530Basic and acidic residuesSequence analysisAdd BLAST16
Compositional biasi1061 – 1077Basic and acidic residuesSequence analysisAdd BLAST17

<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

Belongs to the histone deacetylase family. HD type 2 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1343, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000157440

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_006530_2_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q99P99

Identification of Orthologs from Complete Genome Data

More...OMAi		AEESTPX

Database of Orthologous Groups

More...OrthoDBi		1484694at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q99P99

TreeFam database of animal gene trees

More...TreeFami		TF106174

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.800.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR033660, HDAC4/7
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

More...PANTHERi		PTHR45364, PTHR45364, 1 hit
PTHR45364:SF3, PTHR45364:SF3, 1 hit

Pfam protein domain database

More...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>. 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>Sequencei

<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.

Q99P99-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSSQSHPDGL SGRDQPVELL NPARVNHMPS TVDVATALPL QVAPAAVPMD 
        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 NHCMSSDPRY 
       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 STPAETSLAH RLVTREGSVA PLPLYTSPSL 
       360        370        380        390        400
PNITLGLPAT GPAAGAAGQQ DAERLALPAL QQRISLFPGT HLTPYLSTSP 
       410        420        430        440        450
LERDGGAAHN PLLQHMVLLE QPPTQTPLVT GLGALPLHTQ SLVGADRVSP 
       460        470        480        490        500
SIHKLRQHRP LGRTQSAPLP QNAQALQHLV IQQQHQQFLE KHKQQFQQQQ 
       510        520        530        540        550
LHLSKMISKP SEPPRQPESH PEETEEELRE HQALLDEPYL DRLPGQKEPS 
       560        570        580        590        600
LAGVQVKQEP IESEEEEVEA TREAEPSQRP ATEQELLFRQ QALLLEQQRI 
       610        620        630        640        650
HQLRNYQASM EAAGIPVSFG SHRPLSRAQS SPASATFPMS VQEPPTKPRF 
       660        670        680        690        700
TTGLVYDTLM LKHQCTCGNT NSHPEHAGRI QSIWSRLQET GLRGKCECIR 
       710        720        730        740        750
GRKATLEELQ TVHSEAHTLL YGTNPLNRQK LDSSLTSVFV RLPCGGVGVD 
       760        770        780        790        800
SDTIWNEVHS SGAARLAVGC VVELVFKVAT GELKNGFAVV RPPGHHAEES 
       810        820        830        840        850
TPMGFCYFNS VAIAAKLLQQ RLNVSKILIV DWDVHHGNGT QQAFYNDPNV 
       860        870        880        890        900
LYMSLHRYDD GNFFPGSGAP DEVGTGPGVG FNVNMAFTGG LDPPMGDAEY 
       910        920        930        940        950
LAAFRTVVMP IANEFAPDVV LVSSGFDAVE GHPTPLGGYN LSAKCFGYLT 
       960        970        980        990       1000
KQLMGLAGGR IVLALEGGHD LTAICDASEA CVSALLGNEL EPLPEKVLHQ 
      1010       1020       1030       1040       1050
RPNANAVHSM EKVMGIHSEY WRCLQRLSPT VGHSLIEAQK CENEEAETVT 
      1060       1070 
AMASLSVGVK PAEKRSEEEP MEEEPPL
Length:1,077
Mass (Da):118,652
Last modified:March 20, 2007 - 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:i88127299D9962DBA
GO

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
AABR03067902 Genomic DNA No translation available.
AABR03068091 Genomic DNA No translation available.
AABR03070452 Genomic DNA No translation available.
AF321132 mRNA Translation: AAK11185.1

NCBI Reference Sequences

More...RefSeqi		NP_445901.1, NM_053449.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSRNOT00000027622; ENSRNOP00000027622; ENSRNOG00000020372

Database of genes from NCBI RefSeq genomes

More...GeneIDi		363287

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:363287

UCSC genome browser

More...UCSCi		RGD:619979, rat

<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
AABR03067902 Genomic DNA No translation available.
AABR03068091 Genomic DNA No translation available.
AABR03070452 Genomic DNA No translation available.
AF321132 mRNA Translation: AAK11185.1
RefSeqiNP_445901.1, NM_053449.1

3D structure databases

SMRiQ99P99
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi264106, 4 interactors
CORUMiQ99P99
STRINGi10116.ENSRNOP00000027622

Chemistry databases

BindingDBiQ99P99
ChEMBLiCHEMBL2095943
DrugCentraliQ99P99

PTM databases

iPTMnetiQ99P99
PhosphoSitePlusiQ99P99

Proteomic databases

PaxDbiQ99P99
PRIDEiQ99P99

Genome annotation databases

EnsembliENSRNOT00000027622; ENSRNOP00000027622; ENSRNOG00000020372
GeneIDi363287
KEGGirno:363287
UCSCiRGD:619979, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		9759
RGDi619979, Hdac4

Phylogenomic databases

eggNOGiKOG1343, Eukaryota
GeneTreeiENSGT00940000157440
HOGENOMiCLU_006530_2_0_1
InParanoidiQ99P99
OMAiAEESTPX
OrthoDBi1484694at2759
PhylomeDBiQ99P99
TreeFamiTF106174

Enzyme and pathway databases

ReactomeiR-RNO-350054, Notch-HLH transcription pathway
R-RNO-4090294, SUMOylation of intracellular receptors
R-RNO-4551638, SUMOylation of chromatin organization proteins
R-RNO-8951936, RUNX3 regulates p14-ARF

Miscellaneous databases

Protein Ontology

More...PROi		PR:Q99P99

Gene expression databases

BgeeiENSRNOG00000020372, Expressed in frontal cortex and 21 other tissues
GenevisibleiQ99P99, RN

Family and domain databases

Gene3Di3.40.800.20, 1 hit
InterProiView protein in InterPro
IPR033660, HDAC4/7
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
PANTHERiPTHR45364, PTHR45364, 1 hit
PTHR45364:SF3, PTHR45364:SF3, 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

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 nameiHDAC4_RAT
<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: Q99P99
<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: March 20, 2007
Last modified: September 29, 2021
This is version 129 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

<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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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