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Q9UQL6

- HDAC5_HUMAN

UniProt

Q9UQL6 - HDAC5_HUMAN

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Protein

Histone deacetylase 5

Gene

HDAC5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 by repressing transcription of myocyte enhancer MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi696 – 6961ZincBy similarity
Metal bindingi698 – 6981ZincBy similarity
Metal bindingi704 – 7041ZincBy similarity
Metal bindingi781 – 7811ZincBy similarity
Active sitei833 – 8331By similarity

GO - Molecular functioni

  1. core promoter binding Source: UniProtKB
  2. histone deacetylase activity Source: BHF-UCL
  3. metal ion binding Source: UniProtKB-KW
  4. NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
  5. NAD-dependent histone deacetylase activity (H3-K18 specific) Source: UniProtKB-EC
  6. NAD-dependent histone deacetylase activity (H3-K9 specific) Source: UniProtKB-EC
  7. NAD-dependent histone deacetylase activity (H4-K16 specific) Source: UniProtKB-EC
  8. protein kinase C binding Source: UniProtKB
  9. repressing transcription factor binding Source: BHF-UCL
  10. transcription corepressor activity Source: Ensembl
  11. transcription factor binding Source: BHF-UCL

GO - Biological processi

  1. B cell activation Source: UniProtKB
  2. B cell differentiation Source: UniProtKB
  3. cellular response to insulin stimulus Source: BHF-UCL
  4. chromatin modification Source: UniProtKB
  5. chromatin organization Source: UniProtKB
  6. chromatin remodeling Source: ProtInc
  7. chromatin silencing Source: ProtInc
  8. heart development Source: Ensembl
  9. histone deacetylation Source: BHF-UCL
  10. inflammatory response Source: UniProtKB
  11. multicellular organismal response to stress Source: Ensembl
  12. negative regulation of cell migration involved in sprouting angiogenesis Source: BHF-UCL
  13. negative regulation of myotube differentiation Source: BHF-UCL
  14. negative regulation of osteoblast differentiation Source: Ensembl
  15. negative regulation of transcription, DNA-templated Source: UniProtKB
  16. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  17. Notch signaling pathway Source: Reactome
  18. osteoblast development Source: Ensembl
  19. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  20. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  21. regulation of gene expression, epigenetic Source: UniProtKB
  22. regulation of myotube differentiation Source: UniProtKB
  23. regulation of protein binding Source: BHF-UCL
  24. regulation of skeletal muscle fiber development Source: Ensembl
  25. response to cocaine Source: Ensembl
  26. response to drug Source: Ensembl
  27. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Hydrolase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone deacetylase 5 (EC:3.5.1.98)
Short name:
HD5
Alternative name(s):
Antigen NY-CO-9
Gene namesi
Name:HDAC5
Synonyms:KIAA0600
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:14068. HDAC5.

Subcellular locationi

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.

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. cytosol Source: Ensembl
  3. Golgi apparatus Source: HPA
  4. histone deacetylase complex Source: UniProtKB
  5. nuclear body Source: Ensembl
  6. nucleoplasm Source: Reactome
  7. nucleus Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi259 – 2591S → 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. 3 Publications
Mutagenesisi279 – 2791S → A: No effect. 1 Publication
Mutagenesisi291 – 2911S → A: Does not affect phosphorylation by PKC. 1 Publication
Mutagenesisi292 – 2921T → A: Abolishes phosphorylation by PKC. 1 Publication
Mutagenesisi498 – 4981S → A: Reduces AMPK- and CaMK-dependent phosphorylation and the subsequent nuclear export. Abolishes nuclear export; when associated with A-259. 2 Publications
Mutagenesisi661 – 6611S → A: No effect. 1 Publication
Mutagenesisi713 – 7131S → A: No effect. 1 Publication
Mutagenesisi1086 – 10861V → A: Reduces CaMK-dependent nuclear export. 1 Publication
Mutagenesisi1092 – 10921L → A: Reduces CaMK-dependent nuclear export. 1 Publication

Organism-specific databases

PharmGKBiPA29230.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11221122Histone deacetylase 5PRO_0000114701Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei259 – 2591Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD13 Publications
Modified residuei292 – 2921Phosphothreonine; by PKC1 Publication
Modified residuei498 – 4981Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD13 Publications
Modified residuei533 – 5331N6-acetyllysine1 Publication
Modified residuei661 – 6611Phosphoserine1 Publication

Post-translational modificationi

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).By similarity
Ubiquitinated. Polyubiquitination however does not lead to its degradation.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9UQL6.
PaxDbiQ9UQL6.
PRIDEiQ9UQL6.

PTM databases

PhosphoSiteiQ9UQL6.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ9UQL6.
CleanExiHS_HDAC5.
ExpressionAtlasiQ9UQL6. baseline and differential.
GenevestigatoriQ9UQL6.

Organism-specific databases

HPAiCAB019400.
HPA030991.

Interactioni

Subunit structurei

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. Interacts with EP300 in the presence of TFAP2C.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BRMS1Q9HCU92EBI-715576,EBI-714781
ICP0P083933EBI-715576,EBI-6148881From a different organism.
RUNX3Q137615EBI-715576,EBI-925990
SFNP319473EBI-715576,EBI-476295
YWHAZP631042EBI-715576,EBI-347088

Protein-protein interaction databases

BioGridi115331. 338 interactions.
DIPiDIP-38260N.
IntActiQ9UQL6. 28 interactions.
MINTiMINT-1407477.
STRINGi9606.ENSP00000225983.

Structurei

3D structure databases

ProteinModelPortaliQ9UQL6.
SMRiQ9UQL6. Positions 96-133, 681-1061.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni684 – 1028345Histone deacetylaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1081 – 112242Nuclear export signalAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi47 – 526Poly-Gly
Compositional biasi85 – 928Poly-Gln
Compositional biasi596 – 5994Poly-Glu
Compositional biasi1099 – 11046Poly-Ala

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0123.
GeneTreeiENSGT00530000062809.
HOGENOMiHOG000232065.
HOVERGENiHBG057100.
InParanoidiQ9UQL6.
KOiK11406.
OMAiLGPYDSR.
OrthoDBiEOG7RFTH5.
PhylomeDBiQ9UQL6.
TreeFamiTF106174.

Family and domain databases

Gene3Di3.40.800.20. 1 hit.
InterProiIPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
IPR024643. Hist_deacetylase_Gln_rich_N.
IPR017320. Histone_deAcase_II_euk.
[Graphical view]
PANTHERiPTHR10625. PTHR10625. 1 hit.
PfamiPF12203. HDAC4_Gln. 1 hit.
PF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFiPIRSF037911. HDAC_II_euk. 1 hit.
PRINTSiPR01270. HDASUPER.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UQL6-1) [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
MNSPNESDGM SGREPSLEIL PRTSLHSIPV TVEVKPVLPR AMPSSMGGGG
60 70 80 90 100
GGSPSPVELR GALVGSVDPT LREQQLQQEL LALKQQQQLQ KQLLFAEFQK
110 120 130 140 150
QHDHLTRQHE VQLQKHLKQQ QEMLAAKQQQ EMLAAKRQQE LEQQRQREQQ
160 170 180 190 200
RQEELEKQRL EQQLLILRNK EKSKESAIAS TEVKLRLQEF LLSKSKEPTP
210 220 230 240 250
GGLNHSLPQH PKCWGAHHAS LDQSSPPQSG PPGTPPSYKL PLPGPYDSRD
260 270 280 290 300
DFPLRKTASE PNLKVRSRLK QKVAERRSSP LLRRKDGTVI STFKKRAVEI
310 320 330 340 350
TGAGPGASSV CNSAPGSGPS SPNSSHSTIA ENGFTGSVPN IPTEMLPQHR
360 370 380 390 400
ALPLDSSPNQ FSLYTSPSLP NISLGLQATV TVTNSHLTAS PKLSTQQEAE
410 420 430 440 450
RQALQSLRQG GTLTGKFMST SSIPGCLLGV ALEGDGSPHG HASLLQHVLL
460 470 480 490 500
LEQARQQSTL IAVPLHGQSP LVTGERVATS MRTVGKLPRH RPLSRTQSSP
510 520 530 540 550
LPQSPQALQQ LVMQQQHQQF LEKQKQQQLQ LGKILTKTGE LPRQPTTHPE
560 570 580 590 600
ETEEELTEQQ EVLLGEGALT MPREGSTESE STQEDLEEED EEDDGEEEED
610 620 630 640 650
CIQVKDEEGE SGAEEGPDLE EPGAGYKKLF SDAQPLQPLQ VYQAPLSLAT
660 670 680 690 700
VPHQALGRTQ SSPAAPGGMK SPPDQPVKHL FTTGVVYDTF MLKHQCMCGN
710 720 730 740 750
THVHPEHAGR IQSIWSRLQE TGLLSKCERI RGRKATLDEI QTVHSEYHTL
760 770 780 790 800
LYGTSPLNRQ KLDSKKLLGP ISQKMYAVLP CGGIGVDSDT VWNEMHSSSA
810 820 830 840 850
VRMAVGCLLE LAFKVAAGEL KNGFAIIRPP GHHAEESTAM GFCFFNSVAI
860 870 880 890 900
TAKLLQQKLN VGKVLIVDWD IHHGNGTQQA FYNDPSVLYI SLHRYDNGNF
910 920 930 940 950
FPGSGAPEEV GGGPGVGYNV NVAWTGGVDP PIGDVEYLTA FRTVVMPIAH
960 970 980 990 1000
EFSPDVVLVS AGFDAVEGHL SPLGGYSVTA RCFGHLTRQL MTLAGGRVVL
1010 1020 1030 1040 1050
ALEGGHDLTA ICDASEACVS ALLSVELQPL DEAVLQQKPN INAVATLEKV
1060 1070 1080 1090 1100
IEIQSKHWSC VQKFAAGLGR SLREAQAGET EEAETVSAMA LLSVGAEQAQ
1110 1120
AAAAREHSPR PAEEPMEQEP AL
Length:1,122
Mass (Da):121,978
Last modified:May 18, 2010 - v2
Checksum:iCF4BE774E3588FEC
GO
Isoform 2 (identifier: Q9UQL6-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     684-768: Missing.

Note: No experimental confirmation available.

Show »
Length:1,037
Mass (Da):112,191
Checksum:iD4F09B907D2C1457
GO
Isoform 3 (identifier: Q9UQL6-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,123
Mass (Da):122,049
Checksum:i909ED5CCFEE3FB4F
GO

Sequence cautioni

The sequence AAC18040.1 differs from that shown. Reason: Frameshift at position 1085. Curated
The sequence BAA25526.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371V → L in BX458255. 1 PublicationCurated
Sequence conflicti139 – 1391Q → R in BX458255. 1 PublicationCurated
Sequence conflicti147 – 1471R → G in BX458255. 1 PublicationCurated
Sequence conflicti593 – 5931D → E in AAD29047. (PubMed:10220385)Curated
Sequence conflicti593 – 5931D → E in AAH51824. (PubMed:15489334)Curated
Sequence conflicti593 – 5931D → E in AAC18040. (PubMed:9610721)Curated
Sequence conflicti671 – 6711S → N in AAC18040. (PubMed:9610721)Curated
Sequence conflicti684 – 6841G → S in AAC18040. (PubMed:9610721)Curated
Sequence conflicti1026 – 10261E → K in AAC18040. (PubMed:9610721)Curated
Sequence conflicti1074 – 10741E → G in AAC18040. (PubMed:9610721)Curated
Sequence conflicti1093 – 10931S → L in AAC18040. (PubMed:9610721)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti137 – 1371R → Q.
Corresponds to variant rs438096 [ dbSNP | Ensembl ].
VAR_055903
Natural varianti565 – 5651G → A.
Corresponds to variant rs33916560 [ dbSNP | Ensembl ].
VAR_055904

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei7 – 71S → SA in isoform 3. 1 PublicationVSP_039180
Alternative sequencei684 – 76885Missing in isoform 2. 1 PublicationVSP_002081Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS32663.1. [Q9UQL6-3]
CCDS45696.1. [Q9UQL6-1]
RefSeqiNP_001015053.1. NM_001015053.1. [Q9UQL6-3]
NP_005465.2. NM_005474.4. [Q9UQL6-1]
XP_005256961.1. XM_005256904.2. [Q9UQL6-3]
XP_005256963.1. XM_005256906.2. [Q9UQL6-1]
UniGeneiHs.438782.

Genome annotation databases

EnsembliENST00000225983; ENSP00000225983; ENSG00000108840. [Q9UQL6-3]
ENST00000336057; ENSP00000337290; ENSG00000108840. [Q9UQL6-2]
ENST00000586802; ENSP00000468004; ENSG00000108840. [Q9UQL6-1]
GeneIDi10014.
KEGGihsa:10014.
UCSCiuc002ifd.1. human. [Q9UQL6-1]
uc002iff.1. human. [Q9UQL6-3]
uc010czp.1. human. [Q9UQL6-2]

Polymorphism databases

DMDMi296434519.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS32663.1. [Q9UQL6-3 ]
CCDS45696.1. [Q9UQL6-1 ]
RefSeqi NP_001015053.1. NM_001015053.1. [Q9UQL6-3 ]
NP_005465.2. NM_005474.4. [Q9UQL6-1 ]
XP_005256961.1. XM_005256904.2. [Q9UQL6-3 ]
XP_005256963.1. XM_005256906.2. [Q9UQL6-1 ]
UniGenei Hs.438782.

3D structure databases

ProteinModelPortali Q9UQL6.
SMRi Q9UQL6. Positions 96-133, 681-1061.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115331. 338 interactions.
DIPi DIP-38260N.
IntActi Q9UQL6. 28 interactions.
MINTi MINT-1407477.
STRINGi 9606.ENSP00000225983.

Chemistry

BindingDBi Q9UQL6.
ChEMBLi CHEMBL3038483.
GuidetoPHARMACOLOGYi 2660.

PTM databases

PhosphoSitei Q9UQL6.

Polymorphism databases

DMDMi 296434519.

Proteomic databases

MaxQBi Q9UQL6.
PaxDbi Q9UQL6.
PRIDEi Q9UQL6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000225983 ; ENSP00000225983 ; ENSG00000108840 . [Q9UQL6-3 ]
ENST00000336057 ; ENSP00000337290 ; ENSG00000108840 . [Q9UQL6-2 ]
ENST00000586802 ; ENSP00000468004 ; ENSG00000108840 . [Q9UQL6-1 ]
GeneIDi 10014.
KEGGi hsa:10014.
UCSCi uc002ifd.1. human. [Q9UQL6-1 ]
uc002iff.1. human. [Q9UQL6-3 ]
uc010czp.1. human. [Q9UQL6-2 ]

Organism-specific databases

CTDi 10014.
GeneCardsi GC17M042159.
H-InvDB HIX0013862.
HGNCi HGNC:14068. HDAC5.
HPAi CAB019400.
HPA030991.
MIMi 605315. gene.
neXtProti NX_Q9UQL6.
PharmGKBi PA29230.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0123.
GeneTreei ENSGT00530000062809.
HOGENOMi HOG000232065.
HOVERGENi HBG057100.
InParanoidi Q9UQL6.
KOi K11406.
OMAi LGPYDSR.
OrthoDBi EOG7RFTH5.
PhylomeDBi Q9UQL6.
TreeFami TF106174.

Enzyme and pathway databases

Reactomei REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.

Miscellaneous databases

ChiTaRSi HDAC5. human.
GeneWikii Histone_deacetylase_5.
GenomeRNAii 10014.
NextBioi 37831.
PROi Q9UQL6.
SOURCEi Search...

Gene expression databases

Bgeei Q9UQL6.
CleanExi HS_HDAC5.
ExpressionAtlasi Q9UQL6. baseline and differential.
Genevestigatori Q9UQL6.

Family and domain databases

Gene3Di 3.40.800.20. 1 hit.
InterProi IPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
IPR024643. Hist_deacetylase_Gln_rich_N.
IPR017320. Histone_deAcase_II_euk.
[Graphical view ]
PANTHERi PTHR10625. PTHR10625. 1 hit.
Pfami PF12203. HDAC4_Gln. 1 hit.
PF00850. Hist_deacetyl. 1 hit.
[Graphical view ]
PIRSFi PIRSF037911. HDAC_II_euk. 1 hit.
PRINTSi PR01270. HDASUPER.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Differential regulation of estrogen receptor alpha expression in breast cancer cells by metastasis-associated protein 1."
    Kang H.J., Lee M.H., Kang H.L., Kim S.H., Ahn J.R., Na H., Na T.Y., Kim Y.N., Seong J.K., Lee M.O.
    Cancer Res. 74:1484-1494(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EP300.

Entry informationi

Entry nameiHDAC5_HUMAN
AccessioniPrimary (citable) accession number: Q9UQL6
Secondary accession number(s): C9JFV9
, O60340, O60528, Q96DY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 18, 2010
Last modified: November 26, 2014
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3