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Q9Z2V6

- HDAC5_MOUSE

UniProt

Q9Z2V6 - HDAC5_MOUSE

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Protein

Histone deacetylase 5

Gene

Hdac5

Organism
Mus musculus (Mouse)
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 (By similarity).By similarity

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 bindingi687 – 6871ZincBy similarity
Metal bindingi689 – 6891ZincBy similarity
Metal bindingi695 – 6951ZincBy similarity
Metal bindingi772 – 7721ZincBy similarity
Active sitei824 – 8241By similarity

GO - Molecular functioni

  1. core promoter sequence-specific DNA binding Source: UniProtKB
  2. histone deacetylase activity Source: UniProtKB
  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 binding Source: UniProtKB
  9. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: UniProtKB
  10. RNA polymerase II transcription factor binding Source: BHF-UCL
  11. transcription corepressor activity Source: MGI
  12. transcription factor binding Source: UniProtKB

GO - Biological processi

  1. B cell activation Source: UniProtKB
  2. B cell differentiation Source: UniProtKB
  3. cellular response to fluid shear stress Source: UniProtKB
  4. chromatin modification Source: UniProtKB
  5. heart development Source: MGI
  6. histone deacetylation Source: GOC
  7. inflammatory response Source: UniProtKB
  8. multicellular organismal response to stress Source: MGI
  9. negative regulation of osteoblast differentiation Source: MGI
  10. negative regulation of striated muscle tissue development Source: UniProtKB
  11. negative regulation of transcription, DNA-templated Source: UniProtKB
  12. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  13. nervous system development Source: UniProtKB
  14. osteoblast development Source: MGI
  15. positive regulation of neural precursor cell proliferation Source: BHF-UCL
  16. positive regulation of stem cell proliferation Source: BHF-UCL
  17. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  18. regulation of myotube differentiation Source: UniProtKB
  19. regulation of skeletal muscle fiber development Source: MGI
  20. regulation of striated muscle cell differentiation Source: MGI
  21. renal tubule morphogenesis Source: UniProtKB
  22. response to cocaine Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Hydrolase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Histone deacetylase 5 (EC:3.5.1.98)
Short name:
HD5
Alternative name(s):
Histone deacetylase mHDA1
Gene namesi
Name:Hdac5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:1333784. 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-250 and Ser-488 by AMPK, CaMK1 and SIK1.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: MGI
  3. histone deacetylase complex Source: UniProtKB
  4. nuclear body Source: MGI
  5. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi250 – 2501S → A: Abolishes phosphorylation by SIK1 and fails to promote beta-catenin expression; when associated with A-488. 2 Publications
Mutagenesisi488 – 4881S → A: Abolishes phosphorylation by SIK1 and fails to promote beta-catenin expression; when associated with A-250. 2 Publications
Mutagenesisi824 – 8241H → A: Abolishes deacetylase activity. 1 Publication
Mutagenesisi884 – 8841H → F: Disrupts the dot-like nuclear pattern. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11131113Histone deacetylase 5PRO_0000114702Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei250 – 2501Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD12 Publications
Modified residuei283 – 2831Phosphothreonine; by PKCBy similarity
Modified residuei488 – 4881Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD12 Publications
Modified residuei523 – 5231N6-acetyllysineBy similarity
Modified residuei650 – 6501PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by AMPK, CaMK1, SIK1 and PRKD1 at Ser-250 and Ser-488. The phosphorylation is required for the export to the cytoplasm and inhibition. Phosphorylated by the PKC kinases PKN1 and PKN2, impairing nuclear import (By similarity). Phosphorylated by GRK5, leading to nuclear export of HDAC5 and allowing MEF2-mediated transcription.By similarity3 Publications
Ubiquitinated. Polyubiquitination however does not lead to its degradation (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9Z2V6.
PaxDbiQ9Z2V6.
PRIDEiQ9Z2V6.

PTM databases

PhosphoSiteiQ9Z2V6.

Expressioni

Gene expression databases

CleanExiMM_HDAC5.
GenevestigatoriQ9Z2V6.

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.8 Publications

Protein-protein interaction databases

DIPiDIP-40855N.
IntActiQ9Z2V6. 4 interactions.
MINTiMINT-125422.

Structurei

3D structure databases

ProteinModelPortaliQ9Z2V6.
SMRiQ9Z2V6. Positions 68-132, 672-1052.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni675 – 1019345Histone deacetylaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1072 – 111342Nuclear export signalBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi47 – 526Poly-Gly
Compositional biasi85 – 928Poly-Gln
Compositional biasi577 – 58812Poly-GluAdd
BLAST

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0123.
HOVERGENiHBG057100.
InParanoidiQ9Z2V6.

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.

Sequencei

Sequence statusi: Complete.

Q9Z2V6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNSPNESDGM SGREPSLGIL PRTPLHSIPV AVEVKPVLPG AMPSSMGGGG
60 70 80 90 100
GGSPSPVELR GALAGPMDPA LREQQLQQEL LVLKQQQQLQ KQLLFAEFQK
110 120 130 140 150
QHDHLTRQHE VQLQKHLKQQ QEMLAAKRQQ ELEQQRQREQ QRQEELEKQR
160 170 180 190 200
LEQQLLILRN KEKSKESAIA STEVKLRLQE FLLSKSKEPT PGGLNHSLPQ
210 220 230 240 250
HPKCWGAHHA SLDQSSPPQS GPPGTPPSYK LPLLGPYDSR DDFPLRKTAS
260 270 280 290 300
EPNLKVRSRL KQKVAERRSS PLLRRKDGTV ISTFKKRAVE ITGTGPGVSS
310 320 330 340 350
VCNSAPGSGP SSPNSSHSTI AENGFTGSVP NIPTEMIPQH RALPLDSSPN
360 370 380 390 400
QFSLYTSPSL PNISLGLQAT VTVTNSHLTA SPKLSTQQEA ERQALQSLRQ
410 420 430 440 450
GGTLTGKFMS TSSIPGCLLG VALEGDTSPH GHASLLQHVC SWTGRQQSTL
460 470 480 490 500
IAVPLHGQSP LVTGERVATS MRTVGKLPRH RPLSRTQSSP LPQSPQALQQ
510 520 530 540 550
LVMQQQHQQF LEKQKQQQMQ LGKILTKTGE LSRQPTTHPE ETEEELTEQQ
560 570 580 590 600
EALLGEGALT IPREGSTESE STQEDLEEEE EEEEEEEEDC IQVKDEDGES
610 620 630 640 650
GPDEGPDLEE SSAGYKKLFA DAQQLQPLQV YQAPLSLATV PHQALGRTQS
660 670 680 690 700
SPAAPGSMKS PTDQPTVVKH LFTTGVVYDT FMLKHQCMCG NTHVHPEHAG
710 720 730 740 750
RIQSIWSRLQ ETGLLGKCER IRGRKATLDE IQTVHSEYHT LLYGTSPLNR
760 770 780 790 800
QKLDSKKLLG PISQKMYAML PCGGIGVDSD TVWNEMHSSS AVRMAVGCLV
810 820 830 840 850
ELAFKVAAGE LKNGFAIIRP PGHHAEESTA MGFCFFNSVA ITAKLLQQKL
860 870 880 890 900
SVGKVLIVDW DIHHGNGTQQ AFYNDPSVLY ISLHRYDNGN FFPGSGAPEE
910 920 930 940 950
VGGGPGVGYN VNVAWTGGVD PPIGDVEYLT AFRTVVMPIA QEFSPDVVLV
960 970 980 990 1000
SAGFDAVEGH LSPLGGYSVT ARCFGHLTRQ LMTLAGGRVV LALEGGHDLT
1010 1020 1030 1040 1050
AICDASEACV SALLSVELQP LDEAVLQQKP SVNAVATLEK VIEIQSKHWS
1060 1070 1080 1090 1100
CVQRFAAGLG CSLREAQTGE KEEAETVSAM ALLSVGAEQA QAVATQEHSP
1110
RPAEEPMEQE PAL
Length:1,113
Mass (Da):120,942
Last modified:May 1, 2000 - v2
Checksum:i63071AF45B87815A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71S → SA in AAF31418. (PubMed:10640276)Curated
Sequence conflicti18 – 181G → E in AAF31418. (PubMed:10640276)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF006602 mRNA. Translation: AAD09834.2.
AF207748 mRNA. Translation: AAF31418.1.
UniGeneiMm.22665.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF006602 mRNA. Translation: AAD09834.2 .
AF207748 mRNA. Translation: AAF31418.1 .
UniGenei Mm.22665.

3D structure databases

ProteinModelPortali Q9Z2V6.
SMRi Q9Z2V6. Positions 68-132, 672-1052.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-40855N.
IntActi Q9Z2V6. 4 interactions.
MINTi MINT-125422.

Chemistry

BindingDBi Q9Z2V6.
ChEMBLi CHEMBL2768.

PTM databases

PhosphoSitei Q9Z2V6.

Proteomic databases

MaxQBi Q9Z2V6.
PaxDbi Q9Z2V6.
PRIDEi Q9Z2V6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

MGIi MGI:1333784. Hdac5.

Phylogenomic databases

eggNOGi COG0123.
HOVERGENi HBG057100.
InParanoidi Q9Z2V6.

Miscellaneous databases

ChiTaRSi HDAC5. mouse.
PROi Q9Z2V6.
SOURCEi Search...

Gene expression databases

CleanExi MM_HDAC5.
Genevestigatori Q9Z2V6.

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

  1. "Identification of a new family of higher eukaryotic histone deacetylases. Coordinate expression of differentiation-dependent chromatin modifiers."
    Verdel A., Khochbin S.
    J. Biol. Chem. 274:2440-2445(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
    Tissue: Fetus.
  2. "Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression."
    Kao H.-Y., Downes M., Ordentlich P., Evans R.M.
    Genes Dev. 14:55-66(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH NCOR2.
    Strain: C57BL/6.
  3. Cited for: INTERACTION WITH HDAC7, NUCLEAR EXPORT, MUTAGENESIS OF HIS-824 AND HIS-884.
  4. "Association of COOH-terminal-binding protein (CtBP) and MEF2-interacting transcription repressor (MITR) contributes to transcriptional repression of the MEF2 transcription factor."
    Zhang C.L., McKinsey T.A., Lu J.R., Olson E.N.
    J. Biol. Chem. 276:35-39(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CTBP1 AND HDAC9.
  5. "Transcriptional regulation by the repressor of estrogen receptor activity via recruitment of histone deacetylases."
    Kurtev V., Margueron R., Kroboth K., Ogris E., Cavailles V., Seiser C.
    J. Biol. Chem. 279:24834-24843(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PHB2.
  6. "Multiple domains of the receptor-interacting protein 140 contribute to transcription inhibition."
    Castet A., Boulahtouf A., Versini G., Bonnet S., Augereau P., Vignon F., Khochbin S., Jalaguier S., Cavailles V.
    Nucleic Acids Res. 32:1957-1966(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NRIP1.
  7. "Modulation of smooth muscle gene expression by association of histone acetyltransferases and deacetylases with myocardin."
    Cao D., Wang Z., Zhang C.L., Oh J., Xing W., Li S., Richardson J.A., Wang D.Z., Olson E.N.
    Mol. Cell. Biol. 25:364-376(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MYOCD.
  8. "SIK1 is a class II HDAC kinase that promotes survival of skeletal myocytes."
    Berdeaux R., Goebel N., Banaszynski L., Takemori H., Wandless T., Shelton G.D., Montminy M.
    Nat. Med. 13:597-603(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-250 AND SER-488, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-250 AND SER-488.
  9. "Molecular mechanism of transcriptional repression of AhR repressor involving ANKRA2, HDAC4, and HDAC5."
    Oshima M., Mimura J., Yamamoto M., Fujii-Kuriyama Y.
    Biochem. Biophys. Res. Commun. 364:276-282(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AHRR.
  10. "Uncovering G protein-coupled receptor kinase-5 as a histone deacetylase kinase in the nucleus of cardiomyocytes."
    Martini J.S., Raake P., Vinge L.E., DeGeorge B.R. Jr., Chuprun J.K., Harris D.M., Gao E., Eckhart A.D., Pitcher J.A., Koch W.J.
    Proc. Natl. Acad. Sci. U.S.A. 105:12457-12462(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GRK5, PHOSPHORYLATION.
  11. "AMP-activated protein kinase regulates beta-catenin transcription via histone deacetylase 5."
    Zhao J.X., Yue W.F., Zhu M.J., Du M.
    J. Biol. Chem. 286:16426-16434(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-250 AND SER-488, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-250 AND SER-488.

Entry informationi

Entry nameiHDAC5_MOUSE
AccessioniPrimary (citable) accession number: Q9Z2V6
Secondary accession number(s): Q9JL73
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3