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Q9UQL6 (HDAC5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone deacetylase 5

Short name=HD5
EC=3.5.1.98
Alternative name(s):
Antigen NY-CO-9
Gene names
Name:HDAC5
Synonyms:KIAA0600
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1122 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 by repressing transcription of myocyte enhancer MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors.

Catalytic activity

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

Subunit structure

Interacts with AHRR, BAHD1, BCOR, HDAC7, HDAC9, CTBP1, MEF2C, NCOR2, NRIP1, PHB2 and a 14-3-3 chaperone protein. Interacts with BCL6, DDIT3/CHOP, GRK5, KDM5B and MYOCD. Ref.9 Ref.11 Ref.14 Ref.15 Ref.16 Ref.19

Subcellular location

Nucleus. Cytoplasm. Note: Shuttles between the nucleus and the cytoplasm. In muscle cells, it shuttles into the cytoplasm during myocyte differentiation. The export to cytoplasm depends on the interaction with a 14-3-3 chaperone protein and is due to its phosphorylation at Ser-259 and Ser-498 by AMPK, CaMK1 and SIK1. Ref.10 Ref.17

Tissue specificity

Ubiquitous.

Domain

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

Post-translational modification

Phosphorylated by AMPK, CaMK1, SIK1 and PRKD1 at Ser-259 and Ser-498. The phosphorylation is required for the export to the cytoplasm and inhibition. Phosphorylated by the PKC kinases PKN1 and PKN2, impairing nuclear import. Phosphorylated by GRK5, leading to nuclear export of HDAC5 and allowing MEF2-mediated transcription By similarity. Ref.10 Ref.11 Ref.17 Ref.18 Ref.21

Ubiquitinated. Polyubiquitination however does not lead to its degradation. Ref.13

Sequence similarities

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

Sequence caution

The sequence AAC18040.1 differs from that shown. Reason: Frameshift at position 1085.

The sequence BAA25526.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandMetal-binding
Zinc
   Molecular functionChromatin regulator
Hydrolase
Repressor
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical termComplete 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

Notch signaling pathway

Traceable author statement. Source: Reactome

cellular response to insulin stimulus

Non-traceable author statement Ref.17. Source: BHF-UCL

chromatin modification

Traceable author statement PubMed 12711221. Source: UniProtKB

chromatin organization

Traceable author statement PubMed 12711221. Source: UniProtKB

chromatin remodeling

Traceable author statement Ref.1. Source: ProtInc

chromatin silencing

Traceable author statement PubMed 10869435. Source: ProtInc

heart development

Inferred from electronic annotation. Source: Ensembl

histone deacetylation

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

inflammatory response

Traceable author statement PubMed 12711221. Source: UniProtKB

multicellular organismal response to stress

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell migration involved in sprouting angiogenesis

Inferred from mutant phenotype PubMed 19351956. Source: BHF-UCL

negative regulation of myotube differentiation

Inferred from mutant phenotype PubMed 10983972Ref.10. Source: BHF-UCL

negative regulation of osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 10983972PubMed 19351956. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Traceable author statement PubMed 12711221. Source: UniProtKB

osteoblast development

Inferred from electronic annotation. Source: Ensembl

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

regulation of myotube differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

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 cocaine

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

cytoplasm

Inferred from direct assay PubMed 10869435Ref.10. Source: BHF-UCL

cytosol

Inferred from electronic annotation. Source: Ensembl

histone deacetylase complex

Traceable author statement PubMed 12711221. Source: UniProtKB

nuclear body

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 10869435Ref.10. 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

histone deacetylase activity

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

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein kinase C binding

Inferred from physical interaction Ref.21. Source: UniProtKB

repressing transcription factor binding

Inferred from physical interaction PubMed 12242305. Source: BHF-UCL

transcription corepressor activity

Inferred from electronic annotation. Source: Ensembl

transcription factor binding

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

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UQL6-1)

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.
Isoform 2 (identifier: Q9UQL6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     684-768: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9UQL6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     7-7: S → SA

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11221122Histone deacetylase 5
PRO_0000114701

Regions

Region684 – 1028345Histone deacetylase
Motif1081 – 112242Nuclear export signal
Compositional bias47 – 526Poly-Gly
Compositional bias85 – 928Poly-Gln
Compositional bias596 – 5994Poly-Glu
Compositional bias1099 – 11046Poly-Ala

Sites

Active site8331 By similarity
Metal binding6961Zinc By similarity
Metal binding6981Zinc By similarity
Metal binding7041Zinc By similarity
Metal binding7811Zinc By similarity

Amino acid modifications

Modified residue2591Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD1 Ref.11 Ref.17 Ref.18
Modified residue2921Phosphothreonine; by PKC Ref.21
Modified residue4981Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD1 Ref.11 Ref.17 Ref.18
Modified residue5331N6-acetyllysine Ref.20
Modified residue6611Phosphoserine

Natural variations

Alternative sequence71S → SA in isoform 3.
VSP_039180
Alternative sequence684 – 76885Missing in isoform 2.
VSP_002081
Natural variant1371R → Q.
Corresponds to variant rs438096 [ dbSNP | Ensembl ].
VAR_055903
Natural variant5651G → A.
Corresponds to variant rs33916560 [ dbSNP | Ensembl ].
VAR_055904

Experimental info

Mutagenesis2591S → A: Reduces AMPK- and caMK-dependent phosphorylation and the subsequent nuclear export. Abolishes nuclear export; when associated with A-498. Does not affect phosphorylation by PKN1 and PKN2. Ref.10 Ref.17 Ref.21
Mutagenesis2791S → A: No effect. Ref.10
Mutagenesis2911S → A: Does not affect phosphorylation by PKC. Ref.21
Mutagenesis2921T → A: Abolishes phosphorylation by PKC. Ref.21
Mutagenesis4981S → A: Reduces AMPK- and CaMK-dependent phosphorylation and the subsequent nuclear export. Abolishes nuclear export; when associated with A-259. Ref.10 Ref.17
Mutagenesis6611S → A: No effect. Ref.10
Mutagenesis7131S → A: No effect. Ref.10
Mutagenesis10861V → A: Reduces CaMK-dependent nuclear export. Ref.12
Mutagenesis10921L → A: Reduces CaMK-dependent nuclear export. Ref.12
Sequence conflict371V → L in BX458255. Ref.6
Sequence conflict1391Q → R in BX458255. Ref.6
Sequence conflict1471R → G in BX458255. Ref.6
Sequence conflict5931D → E in AAD29047. Ref.1
Sequence conflict5931D → E in AAH51824. Ref.5
Sequence conflict5931D → E in AAC18040. Ref.7
Sequence conflict6711S → N in AAC18040. Ref.7
Sequence conflict6841G → S in AAC18040. Ref.7
Sequence conflict10261E → K in AAC18040. Ref.7
Sequence conflict10741E → G in AAC18040. Ref.7
Sequence conflict10931S → L in AAC18040. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: CF4BE774E3588FEC

FASTA1,122121,978
        10         20         30         40         50         60 
MNSPNESDGM SGREPSLEIL PRTSLHSIPV TVEVKPVLPR AMPSSMGGGG GGSPSPVELR 

        70         80         90        100        110        120 
GALVGSVDPT LREQQLQQEL LALKQQQQLQ KQLLFAEFQK QHDHLTRQHE VQLQKHLKQQ 

       130        140        150        160        170        180 
QEMLAAKQQQ EMLAAKRQQE LEQQRQREQQ RQEELEKQRL EQQLLILRNK EKSKESAIAS 

       190        200        210        220        230        240 
TEVKLRLQEF LLSKSKEPTP GGLNHSLPQH PKCWGAHHAS LDQSSPPQSG PPGTPPSYKL 

       250        260        270        280        290        300 
PLPGPYDSRD DFPLRKTASE PNLKVRSRLK QKVAERRSSP LLRRKDGTVI STFKKRAVEI 

       310        320        330        340        350        360 
TGAGPGASSV CNSAPGSGPS SPNSSHSTIA ENGFTGSVPN IPTEMLPQHR ALPLDSSPNQ 

       370        380        390        400        410        420 
FSLYTSPSLP NISLGLQATV TVTNSHLTAS PKLSTQQEAE RQALQSLRQG GTLTGKFMST 

       430        440        450        460        470        480 
SSIPGCLLGV ALEGDGSPHG HASLLQHVLL LEQARQQSTL IAVPLHGQSP LVTGERVATS 

       490        500        510        520        530        540 
MRTVGKLPRH RPLSRTQSSP LPQSPQALQQ LVMQQQHQQF LEKQKQQQLQ LGKILTKTGE 

       550        560        570        580        590        600 
LPRQPTTHPE ETEEELTEQQ EVLLGEGALT MPREGSTESE STQEDLEEED EEDDGEEEED 

       610        620        630        640        650        660 
CIQVKDEEGE SGAEEGPDLE EPGAGYKKLF SDAQPLQPLQ VYQAPLSLAT VPHQALGRTQ 

       670        680        690        700        710        720 
SSPAAPGGMK SPPDQPVKHL FTTGVVYDTF MLKHQCMCGN THVHPEHAGR IQSIWSRLQE 

       730        740        750        760        770        780 
TGLLSKCERI RGRKATLDEI QTVHSEYHTL LYGTSPLNRQ KLDSKKLLGP ISQKMYAVLP 

       790        800        810        820        830        840 
CGGIGVDSDT VWNEMHSSSA VRMAVGCLLE LAFKVAAGEL KNGFAIIRPP GHHAEESTAM 

       850        860        870        880        890        900 
GFCFFNSVAI TAKLLQQKLN VGKVLIVDWD IHHGNGTQQA FYNDPSVLYI SLHRYDNGNF 

       910        920        930        940        950        960 
FPGSGAPEEV GGGPGVGYNV NVAWTGGVDP PIGDVEYLTA FRTVVMPIAH EFSPDVVLVS 

       970        980        990       1000       1010       1020 
AGFDAVEGHL SPLGGYSVTA RCFGHLTRQL MTLAGGRVVL ALEGGHDLTA ICDASEACVS 

      1030       1040       1050       1060       1070       1080 
ALLSVELQPL DEAVLQQKPN INAVATLEKV IEIQSKHWSC VQKFAAGLGR SLREAQAGET 

      1090       1100       1110       1120 
EEAETVSAMA LLSVGAEQAQ AAAAREHSPR PAEEPMEQEP AL 

« Hide

Isoform 2 [UniParc].

Checksum: D4F09B907D2C1457
Show »

FASTA1,037112,191
Isoform 3 [UniParc].

Checksum: 909ED5CCFEE3FB4F
Show »

FASTA1,123122,049

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] (ISOFORM 1).
[2]"Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[3]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[4]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Eye and Testis.
[6]"Full-length cDNA libraries and normalization."
Li W.B., Gruber C., Jessee J., Polayes D.
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-176 (ISOFORM 3).
Tissue: Neuroblastoma.
[7]"Characterization of human colon cancer antigens recognized by autologous antibodies."
Scanlan M.J., Chen Y.-T., Williamson B., Gure A.O., Stockert E., Gordan J.D., Tuereci O., Sahin U., Pfreundschuh M., Old L.J.
Int. J. Cancer 76:652-658(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 189-1122 (ISOFORM 1).
Tissue: Colon carcinoma.
[8]"Chromosomal organization and localization of the human histone deacetylase 5 gene (HDAC5)."
Mahlknecht U., Schnittger S., Ottmann O.G., Schoch C., Mosebach M., Hiddemann W., Hoelzer D.
Biochim. Biophys. Acta 1493:342-348(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE ORGANIZATION.
[9]"BCoR, a novel corepressor involved in BCL-6 repression."
Huynh K.D., Fischle W., Verdin E., Bardwell V.J.
Genes Dev. 14:1810-1823(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BCOR.
[10]"Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation."
McKinsey T.A., Zhang C.-L., Lu J., Olson E.N.
Nature 408:106-111(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, MUTAGENESIS OF SER-259; SER-279; SER-498; SER-661 AND SER-713.
[11]"Activation of the myocyte enhancer factor-2 transcription factor by calcium/calmodulin-dependent protein kinase-stimulated binding of 14-3-3 to histone deacetylase 5."
McKinsey T.A., Zhang C.-L., Olson E.N.
Proc. Natl. Acad. Sci. U.S.A. 97:14400-14405(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH 14-3-3, PHOSPHORYLATION AT SER-259 AND SER-498.
[12]"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-1086 AND LEU-1092.
[13]"Histone deacetylase 6 binds polyubiquitin through its zinc finger (PAZ domain) and copurifies with deubiquitinating enzymes."
Hook S.S., Orian A., Cowley S.M., Eisenman R.N.
Proc. Natl. Acad. Sci. U.S.A. 99:13425-13430(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
[14]"Point mutations in BCL6 DNA-binding domain reveal distinct roles for the six zinc fingers."
Mascle X., Albagli O., Lemercier C.
Biochem. Biophys. Res. Commun. 300:391-396(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BCL6.
[15]"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.
[16]"Critical and functional regulation of CHOP (C/EBP homologous protein) through the N-terminal portion."
Ohoka N., Hattori T., Kitagawa M., Onozaki K., Hayashi H.
J. Biol. Chem. 282:35687-35694(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DDIT3.
[17]"AMP-activated protein kinase regulates GLUT4 transcription by phosphorylating histone deacetylase 5."
McGee S.L., van Denderen B.J., Howlett K.F., Mollica J., Schertzer J.D., Kemp B.E., Hargreaves M.
Diabetes 57:860-867(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-259 AND SER-498, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-259 AND SER-498.
[18]"Protein kinase D-dependent phosphorylation and nuclear export of histone deacetylase 5 mediates vascular endothelial growth factor-induced gene expression and angiogenesis."
Ha C.H., Wang W., Jhun B.S., Wong C., Hausser A., Pfizenmaier K., McKinsey T.A., Olson E.N., Jin Z.G.
J. Biol. Chem. 283:14590-14599(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-259 AND SER-498.
[19]"Human BAHD1 promotes heterochromatic gene silencing."
Bierne H., Tham T.N., Batsche E., Dumay A., Leguillou M., Kerneis-Golsteyn S., Regnault B., Seeler J.S., Muchardt C., Feunteun J., Cossart P.
Proc. Natl. Acad. Sci. U.S.A. 106:13826-13831(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BAHD1.
[20]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-533, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Protein kinase C-related kinase targets nuclear localization signals in a subset of class IIa histone deacetylases."
Harrison B.C., Huynh K., Lundgaard G.L., Helmke S.M., Perryman M.B., McKinsey T.A.
FEBS Lett. 584:1103-1110(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-292, MUTAGENESIS OF SER-259; SER-291 AND THR-292.
[22]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF132608 mRNA. Translation: AAD29047.1.
AB011172 mRNA. Translation: BAA25526.2. Different initiation.
AC023855 Genomic DNA. No translation available.
BC013140 mRNA. Translation: AAH13140.1. Different termination.
BC051824 mRNA. Translation: AAH51824.1.
BX458255 mRNA. No translation available.
AF039691 mRNA. Translation: AAC18040.1. Frameshift.
BK000028 Genomic DNA. Translation: DAA00017.1.
RefSeqNP_001015053.1. NM_001015053.1.
NP_005465.2. NM_005474.4.
XP_005256961.1. XM_005256904.2.
XP_005256963.1. XM_005256906.2.
UniGeneHs.438782.

3D structure databases

ProteinModelPortalQ9UQL6.
SMRQ9UQL6. Positions 67-133, 681-1081.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115331. 332 interactions.
DIPDIP-38260N.
IntActQ9UQL6. 28 interactions.
MINTMINT-1407477.
STRING9606.ENSP00000225983.

Chemistry

ChEMBLCHEMBL2563.

PTM databases

PhosphoSiteQ9UQL6.

Polymorphism databases

DMDM296434519.

Proteomic databases

PaxDbQ9UQL6.
PRIDEQ9UQL6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000225983; ENSP00000225983; ENSG00000108840. [Q9UQL6-3]
ENST00000336057; ENSP00000337290; ENSG00000108840. [Q9UQL6-2]
ENST00000393622; ENSP00000377244; ENSG00000108840. [Q9UQL6-1]
ENST00000586802; ENSP00000468004; ENSG00000108840. [Q9UQL6-1]
GeneID10014.
KEGGhsa:10014.
UCSCuc002ifd.1. human. [Q9UQL6-1]
uc002iff.1. human. [Q9UQL6-3]
uc010czp.1. human. [Q9UQL6-2]

Organism-specific databases

CTD10014.
GeneCardsGC17M042159.
H-InvDBHIX0013862.
HGNCHGNC:14068. HDAC5.
HPACAB019400.
HPA030991.
MIM605315. gene.
neXtProtNX_Q9UQL6.
PharmGKBPA29230.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0123.
HOGENOMHOG000232065.
HOVERGENHBG057100.
InParanoidQ9UQL6.
KOK11406.
OMALGPYDSR.
OrthoDBEOG7RFTH5.
PhylomeDBQ9UQL6.
TreeFamTF106174.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.

Gene expression databases

ArrayExpressQ9UQL6.
BgeeQ9UQL6.
CleanExHS_HDAC5.
GenevestigatorQ9UQL6.

Family and domain databases

Gene3D3.40.800.20. 1 hit.
InterProIPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
IPR024643. Hist_deacetylase_Gln_rich_N.
IPR017320. Histone_deAcase_II_euk.
[Graphical view]
PANTHERPTHR10625. PTHR10625. 1 hit.
PfamPF12203. HDAC4_Gln. 1 hit.
PF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFPIRSF037911. HDAC_II_euk. 1 hit.
PRINTSPR01270. HDASUPER.
ProtoNetSearch...

Other

ChiTaRSHDAC5. human.
GeneWikiHistone_deacetylase_5.
GenomeRNAi10014.
NextBio37831.
PROQ9UQL6.
SOURCESearch...

Entry information

Entry nameHDAC5_HUMAN
AccessionPrimary (citable) accession number: Q9UQL6
Secondary accession number(s): C9JFV9 expand/collapse secondary AC list , O60340, O60528, Q96DY4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 150 of the entry and version 2 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

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 17

Human chromosome 17: entries, gene names and cross-references to MIM