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P56524 (HDAC4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone deacetylase 4

Short name=HD4
EC=3.5.1.98
Gene names
Name:HDAC4
Synonyms:KIAA0288
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1084 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6

Catalytic activity

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

Subunit structure

Interacts with HDAC7 By similarity. Homodimer. Homodimerization via its N-terminal domain. Interacts with MEF2C, AHRR, and NR2C1. Interacts with a 14-3-3 chaperone protein in a phosphorylation dependent manner. Interacts with BTBD14B By similarity. Interacts with KDM5B. Interacts with MYOCD By similarity. Interacts with MORC2. Interacts with ANKRA2. Ref.5 Ref.6 Ref.10 Ref.11 Ref.12 Ref.17

Subcellular location

Nucleus. Cytoplasm. Note: Shuttles between the nucleus and the cytoplasm. Upon muscle cells differentiation, it accumulates in the nuclei of myotubes, suggesting a positive role of nuclear HDAC4 in muscle differentiation. The export to cytoplasm depends on the interaction with a 14-3-3 chaperone protein and is due to its phosphorylation at Ser-246, Ser-467 and Ser-632 by CaMK4 and SIK1. The nuclear localization probably depends on sumoylation. Ref.5 Ref.8

Tissue specificity

Ubiquitous.

Domain

The nuclear export sequence mediates the shuttling between the nucleus and the cytoplasm.

Post-translational modification

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 impairs the binding of ANKRA2 but generates a high-affinity docking site for 14-3-3. Ref.7 Ref.8 Ref.13 Ref.20

Sumoylation on Lys-559 is promoted by the E3 SUMO-protein ligase RANBP2, and prevented by phosphorylation by CaMK4. Ref.11

Involvement in disease

Brachydactyly-mental retardation syndrome (BDMR) [MIM:600430]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16

Sequence similarities

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

Sequence caution

The sequence BAA22957.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   DiseaseMental retardation
   DomainCoiled coil
   LigandMetal-binding
Zinc
   Molecular functionChromatin regulator
Hydrolase
Repressor
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell activation

Traceable author statement PubMed 12711221. Source: UniProtKB

B cell differentiation

Traceable author statement PubMed 12711221. Source: UniProtKB

cardiac muscle hypertrophy in response to stress

Traceable author statement PubMed 17011572. Source: BHF-UCL

chromatin remodeling

Inferred from direct assay PubMed 18850004. Source: BHF-UCL

histone H3 deacetylation

Inferred from direct assay PubMed 12590135. Source: BHF-UCL

histone H4 deacetylation

Inferred from direct assay PubMed 12590135. Source: BHF-UCL

histone deacetylation

Inferred from direct assay PubMed 10869435. Source: BHF-UCL

inflammatory response

Traceable author statement PubMed 12711221. Source: UniProtKB

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of glycolysis

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of myotube differentiation

Inferred from mutant phenotype PubMed 10983972. Source: BHF-UCL

negative regulation of osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from mutant phenotype PubMed 18850004. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 10869435. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 10869435. Source: BHF-UCL

nervous system development

Traceable author statement PubMed 12711221. Source: UniProtKB

osteoblast development

Inferred from electronic annotation. Source: Ensembl

peptidyl-lysine deacetylation

Inferred from direct assay PubMed 18614528. Source: BHF-UCL

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 18850004. Source: BHF-UCL

positive regulation of protein sumoylation

Inferred from direct assay PubMed 17696781. Source: UniProtKB

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from mutant phenotype PubMed 19071119. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 19071119. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of cardiac muscle contraction by calcium ion signaling

Inferred from electronic annotation. Source: Ensembl

regulation of protein binding

Inferred from mutant phenotype PubMed 19071119. Source: BHF-UCL

regulation of skeletal muscle fiber development

Inferred from electronic annotation. Source: Ensembl

response to denervation involved in regulation of muscle adaptation

Inferred from sequence or structural similarity. Source: BHF-UCL

response to drug

Inferred from electronic annotation. Source: Ensembl

response to interleukin-1

Inferred from mutant phenotype PubMed 19281832. Source: BHF-UCL

skeletal system development

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentA band

Inferred from electronic annotation. Source: Ensembl

Z disc

Inferred from electronic annotation. Source: Ensembl

actomyosin

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 10869435PubMed 19281832. Source: BHF-UCL

cytosol

Inferred from electronic annotation. Source: Ensembl

histone deacetylase complex

Inferred from direct assay PubMed 11804585. Source: BHF-UCL

neuromuscular junction

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 10869435PubMed 19281832. Source: BHF-UCL

transcriptional repressor complex

Inferred from direct assay PubMed 11804585. Source: BHF-UCL

   Molecular_functionNAD-dependent histone deacetylase activity (H3-K14 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H3-K18 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H3-K9 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H4-K16 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

activating transcription factor binding

Inferred from physical interaction PubMed 10983972. Source: BHF-UCL

core promoter binding

Inferred from electronic annotation. Source: Ensembl

histone deacetylase activity

Inferred from direct assay PubMed 10869435. Source: BHF-UCL

histone deacetylase binding

Inferred from physical interaction PubMed 10869435PubMed 12590135. Source: BHF-UCL

potassium ion binding

Inferred from direct assay PubMed 18614528. Source: BHF-UCL

protein deacetylase activity

Inferred from direct assay PubMed 18614528. Source: BHF-UCL

repressing transcription factor binding

Inferred from physical interaction PubMed 11804585. Source: BHF-UCL

transcription corepressor activity

Inferred from electronic annotation. Source: Ensembl

transcription factor binding

Inferred from physical interaction PubMed 18850004PubMed 19071119. Source: BHF-UCL

zinc ion binding

Inferred from direct assay PubMed 18614528. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10841084Histone deacetylase 4
PRO_0000114699

Regions

Region118 – 313196Interaction with MEF2A
Region655 – 1084430Histone deacetylase
Coiled coil67 – 177111 Potential
Motif1051 – 108434Nuclear export signal By similarity

Sites

Active site8031 By similarity
Metal binding6671Zinc By similarity
Metal binding6691Zinc By similarity
Metal binding6751Zinc By similarity
Metal binding7511Zinc By similarity

Amino acid modifications

Modified residue2461Phosphoserine; by CaMK4 and SIK1 Ref.7
Modified residue3501Phosphoserine Ref.15 Ref.20
Modified residue4671Phosphoserine; by CaMK4 and SIK1 Ref.7
Modified residue5651Phosphoserine
Modified residue6321Phosphoserine; by CaMK4 Ref.7 Ref.14
Modified residue6331Phosphoserine Ref.14
Cross-link559Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.11

Natural variations

Natural variant7271P → R in a breast cancer sample; somatic mutation. Ref.21
VAR_036042

Experimental info

Mutagenesis2461S → A: Reduces phosphorylation and its subsequent nuclear export. Ref.7
Mutagenesis4671S → A: Reduces phosphorylation and its subsequent nuclear export. Ref.7 Ref.8
Mutagenesis5591K → R: Abolishes sumoylation and reduces the histone deacetylase activity. Ref.11
Mutagenesis6321S → A: Reduces phosphorylation and its subsequent nuclear export. Ref.7 Ref.8
Mutagenesis8031H → L: Abolishes histone deacetylase activity. Ref.6
Mutagenesis10561V → A: Reduces CaMK-dependent nuclear export. Ref.9
Mutagenesis10621L → A: Reduces CaMK-dependent nuclear export. Ref.9
Sequence conflict3731A → T in AAD29046. Ref.1
Sequence conflict3731A → T in BAA22957. Ref.2

Secondary structure

.................................................................................... 1084
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P56524 [UniParc].

Last modified September 22, 2009. Version 3.
Checksum: BB7FD37652D12398

FASTA1,084119,040
        10         20         30         40         50         60 
MSSQSHPDGL SGRDQPVELL NPARVNHMPS TVDVATALPL QVAPSAVPMD LRLDHQFSLP 

        70         80         90        100        110        120 
VAEPALREQQ LQQELLALKQ KQQIQRQILI AEFQRQHEQL SRQHEAQLHE HIKQQQEMLA 

       130        140        150        160        170        180 
MKHQQELLEH QRKLERHRQE QELEKQHREQ KLQQLKNKEK GKESAVASTE VKMKLQEFVL 

       190        200        210        220        230        240 
NKKKALAHRN LNHCISSDPR YWYGKTQHSS LDQSSPPQSG VSTSYNHPVL GMYDAKDDFP 

       250        260        270        280        290        300 
LRKTASEPNL KLRSRLKQKV AERRSSPLLR RKDGPVVTAL KKRPLDVTDS ACSSAPGSGP 

       310        320        330        340        350        360 
SSPNNSSGSV SAENGIAPAV PSIPAETSLA HRLVAREGSA APLPLYTSPS LPNITLGLPA 

       370        380        390        400        410        420 
TGPSAGTAGQ QDAERLTLPA LQQRLSLFPG THLTPYLSTS PLERDGGAAH SPLLQHMVLL 

       430        440        450        460        470        480 
EQPPAQAPLV TGLGALPLHA QSLVGADRVS PSIHKLRQHR PLGRTQSAPL PQNAQALQHL 

       490        500        510        520        530        540 
VIQQQHQQFL EKHKQQFQQQ QLQMNKIIPK PSEPARQPES HPEETEEELR EHQALLDEPY 

       550        560        570        580        590        600 
LDRLPGQKEA HAQAGVQVKQ EPIESDEEEA EPPREVEPGQ RQPSEQELLF RQQALLLEQQ 

       610        620        630        640        650        660 
RIHQLRNYQA SMEAAGIPVS FGGHRPLSRA QSSPASATFP VSVQEPPTKP RFTTGLVYDT 

       670        680        690        700        710        720 
LMLKHQCTCG SSSSHPEHAG RIQSIWSRLQ ETGLRGKCEC IRGRKATLEE LQTVHSEAHT 

       730        740        750        760        770        780 
LLYGTNPLNR QKLDSKKLLG SLASVFVRLP CGGVGVDSDT IWNEVHSAGA ARLAVGCVVE 

       790        800        810        820        830        840 
LVFKVATGEL KNGFAVVRPP GHHAEESTPM GFCYFNSVAV AAKLLQQRLS VSKILIVDWD 

       850        860        870        880        890        900 
VHHGNGTQQA FYSDPSVLYM SLHRYDDGNF FPGSGAPDEV GTGPGVGFNV NMAFTGGLDP 

       910        920        930        940        950        960 
PMGDAEYLAA FRTVVMPIAS EFAPDVVLVS SGFDAVEGHP TPLGGYNLSA RCFGYLTKQL 

       970        980        990       1000       1010       1020 
MGLAGGRIVL ALEGGHDLTA ICDASEACVS ALLGNELDPL PEKVLQQRPN ANAVRSMEKV 

      1030       1040       1050       1060       1070       1080 
MEIHSKYWRC LQRTTSTAGR SLIEAQTCEN EEAETVTAMA SLSVGVKPAE KRPDEEPMEE 


EPPL 

« Hide

References

« Hide 'large scale' references
[1]"Three proteins define a class of human histone deacetylases related to yeast Hda1p."
Grozinger C.M., Hassig C.A., Schreiber S.L.
Proc. Natl. Acad. Sci. U.S.A. 96:4868-4873(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Leukemia.
[2]"Construction and characterization of human brain cDNA libraries suitable for analysis of cDNA clones encoding relatively large proteins."
Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Nomura N.
DNA Res. 4:53-59(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Nomura N.
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO N-TERMINUS.
[4]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"HDAC4 deacetylase associates with and represses the MEF2 transcription factor."
Miska E.A., Karlsson C., Langley E., Nielsen S.J., Pines J., Kouzarides T.
EMBO J. 18:5099-5107(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MEF2A.
[6]"HDAC4, a human histone deacetylase related to yeast HDA1, is a transcriptional corepressor."
Wang A.H., Bertos N.R., Vezmar M., Pelletier N., Crosato M., Heng H.H., Th'ng J., Han J., Yang X.-J.
Mol. Cell. Biol. 19:7816-7827(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MEF2C AND MEF2D, MUTAGENESIS OF HIS-803.
[7]"Regulation of histone deacetylase 4 by binding of 14-3-3 proteins."
Wang A.H., Kruhlak M.J., Wu J., Bertos N.R., Vezmar M., Posner B.I., Bazett-Jones D.P., Yang X.-J.
Mol. Cell. Biol. 20:6904-6912(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-246; SER-467 AND SER-632, MUTAGENESIS OF SER-246; SER-467 AND SER-632.
[8]"The modular nature of histone deacetylase HDAC4 confers phosphorylation-dependent intracellular trafficking."
Zhao X., Ito A., Kane C.D., Liao T.-S., Bolger T.A., Lemrow S.M., Means A.R., Yao T.-P.
J. Biol. Chem. 276:35042-35048(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, MUTAGENESIS OF SER-467 AND SER-632.
[9]"Identification of a signal-responsive nuclear export sequence in class II histone deacetylases."
McKinsey T.A., Zhang C.-L., Olson E.N.
Mol. Cell. Biol. 21:6312-6321(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEAR EXPORT SIGNAL, MUTAGENESIS OF VAL-1056 AND LEU-1062.
[10]"The orphan nuclear receptor TR2 interacts directly with both class I and class II histone deacetylases."
Franco P.J., Farooqui M., Seto E., Wei L.-N.
Mol. Endocrinol. 15:1318-1328(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NR2C1.
[11]"The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase."
Kirsh O., Seeler J.-S., Pichler A., Gast A., Mueller S., Miska E., Mathieu M., Harel-Bellan A., Kouzarides T., Melchior F., Dejean A.
EMBO J. 21:2682-2691(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: HOMODIMERIZATION, SUMOYLATION AT LYS-559, MUTAGENESIS OF LYS-559.
[12]"Breast cancer associated transcriptional repressor PLU-1/JARID1B interacts directly with histone deacetylases."
Barrett A., Santangelo S., Tan K., Catchpole S., Roberts K., Spencer-Dene B., Hall D., Scibetta A., Burchell J., Verdin E., Freemont P., Taylor-Papadimitriou J.
Int. J. Cancer 121:265-275(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KDM5B.
[13]"Nuclear calcium/calmodulin-dependent protein kinase IIdelta preferentially transmits signals to histone deacetylase 4 in cardiac cells."
Little G.H., Bai Y., Williams T., Poizat C.
J. Biol. Chem. 282:7219-7231(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY CAMK2D.
[14]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-632 AND SER-633, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"Haploinsufficiency of HDAC4 causes brachydactyly mental retardation syndrome, with brachydactyly type E, developmental delays, and behavioral problems."
Williams S.R., Aldred M.A., Der Kaloustian V.M., Halal F., Gowans G., McLeod D.R., Zondag S., Toriello H.V., Magenis R.E., Elsea S.H.
Am. J. Hum. Genet. 87:219-228(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN BDMR.
[17]"Involvement of histone deacetylation in MORC2-mediated down-regulation of carbonic anhydrase IX."
Shao Y., Li Y., Zhang J., Liu D., Liu F., Zhao Y., Shen T., Li F.
Nucleic Acids Res. 38:2813-2824(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MORC2.
[18]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Sequence-specific recognition of a PxLPxI/L motif by an ankyrin repeat tumbler lock."
Xu C., Jin J., Bian C., Lam R., Tian R., Weist R., You L., Nie J., Bochkarev A., Tempel W., Tan C.S., Wasney G.A., Vedadi M., Gish G.D., Arrowsmith C.H., Pawson T., Yang X.J., Min J.
Sci. Signal. 5:RA39-RA39(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 343-359 IN COMPLEX WITH ANKRA2, PHOSPHORYLATION AT SER-350.
[21]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-727.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF132607 mRNA. Translation: AAD29046.1.
AB006626 mRNA. Translation: BAA22957.2. Different initiation.
AC017028 Genomic DNA. No translation available.
RefSeqNP_006028.2. NM_006037.3.
UniGeneHs.20516.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP56524.
SMRP56524. Positions 62-129, 650-1051.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115106. 189 interactions.
IntActP56524. 30 interactions.
MINTMINT-104901.
STRING9606.ENSP00000264606.

Chemistry

BindingDBP56524.
ChEMBLCHEMBL3524.

PTM databases

PhosphoSiteP56524.

Polymorphism databases

DMDM259016348.

Proteomic databases

PaxDbP56524.
PRIDEP56524.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000345617; ENSP00000264606; ENSG00000068024.
GeneID9759.
KEGGhsa:9759.
UCSCuc002vyk.4. human.

Organism-specific databases

CTD9759.
GeneCardsGC02M239969.
HGNCHGNC:14063. HDAC4.
HPACAB004431.
MIM600430. phenotype.
605314. gene.
neXtProtNX_P56524.
Orphanet1001. 2q37 microdeletion syndrome.
PharmGKBPA29229.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0123.
HOGENOMHOG000232065.
HOVERGENHBG057100.
InParanoidP56524.
KOK11406.
OMAVSFGGHR.
OrthoDBEOG7RFTH5.
PhylomeDBP56524.
TreeFamTF106174.

Enzyme and pathway databases

BRENDA3.5.1.98. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.

Gene expression databases

ArrayExpressP56524.
BgeeP56524.
CleanExHS_HDAC4.
GenevestigatorP56524.

Family and domain databases

Gene3D3.40.800.20. 1 hit.
InterProIPR019154. Arb2_domain.
IPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
IPR024643. Hist_deacetylase_Gln_rich_N.
IPR017320. Histone_deAcase_II_euk.
[Graphical view]
PANTHERPTHR10625. PTHR10625. 1 hit.
PfamPF09757. Arb2. 1 hit.
PF12203. HDAC4_Gln. 1 hit.
PF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFPIRSF037911. HDAC_II_euk. 1 hit.
PRINTSPR01270. HDASUPER.
ProtoNetSearch...

Other

EvolutionaryTraceP56524.
GeneWikiHDAC4.
GenomeRNAi9759.
NextBio36731.
PROP56524.
SOURCESearch...

Entry information

Entry nameHDAC4_HUMAN
AccessionPrimary (citable) accession number: P56524
Secondary accession number(s): Q9UND6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: September 22, 2009
Last modified: April 16, 2014
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM