Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Histone deacetylase 8

Gene

Hdac8

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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. Also involved in the deacetylation of cohesin complex protein SMC3 regulating release of cohesin complexes from chromatin. May play a role in smooth muscle cell contractility (By similarity).By similarity

Catalytic activityi

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

Cofactori

a divalent metal cationNote: Binds 1 divalent metal cation per subunit.

Enzyme regulationi

Its activity is inhibited by trichostatin A (TSA) and butyrate, 2 well known histone deacetylase inhibitors. histone deacetylase inhibitor (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei101 – 1011SubstrateBy similarity
Active sitei143 – 1431Proton acceptorBy similarity
Binding sitei151 – 1511Substrate; via carbonyl oxygenBy similarity
Metal bindingi178 – 1781Divalent metal cationBy similarity
Metal bindingi180 – 1801Divalent metal cationBy similarity
Metal bindingi267 – 2671Divalent metal cationBy similarity
Binding sitei306 – 3061SubstrateBy similarity

GO - Molecular functioni

  • histone deacetylase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
  • transcription factor binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Hydrolase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

ReactomeiREACT_321346. Separation of Sister Chromatids.
REACT_329805. Resolution of Sister Chromatid Cohesion.
REACT_334621. HDACs deacetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone deacetylase 8 (EC:3.5.1.98)
Short name:
HD8
Gene namesi
Name:Hdac8
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1917565. Hdac8.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • histone deacetylase complex Source: UniProtKB
  • nucleus Source: UniProtKB
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 377377Histone deacetylase 8PRO_0000114709Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei39 – 391PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by PKA on serine 39. Phosphorylation reduces deacetylase activity observed preferentially on histones H3 and H4 (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8VH37.
PaxDbiQ8VH37.
PRIDEiQ8VH37.

PTM databases

PhosphoSiteiQ8VH37.

Expressioni

Gene expression databases

BgeeiQ8VH37.
CleanExiMM_HDAC8.
ExpressionAtlasiQ8VH37. baseline.
GenevisibleiQ8VH37. MM.

Interactioni

Subunit structurei

Interacts with CBFA2T3. Interacts with phosphorylated SMG5/EST1B; this interaction protects SMG5 from ubiquitin-mediated degradation. Associates with alpha-SMA (smooth muscle alpha-actin) (By similarity).By similarity

Protein-protein interaction databases

BioGridi213982. 1 interaction.
STRINGi10090.ENSMUSP00000085226.

Structurei

3D structure databases

ProteinModelPortaliQ8VH37.
SMRiQ8VH37. Positions 14-377.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni14 – 324311Histone deacetylaseAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0123.
GeneTreeiENSGT00530000062889.
HOGENOMiHOG000225180.
HOVERGENiHBG057112.
InParanoidiQ8VH37.
KOiK11405.
OMAiKFHTDSY.
OrthoDBiEOG722J95.
PhylomeDBiQ8VH37.
TreeFamiTF106175.

Family and domain databases

Gene3Di3.40.800.20. 1 hit.
InterProiIPR000286. His_deacetylse.
IPR003084. His_deacetylse_1.
IPR023801. His_deacetylse_dom.
[Graphical view]
PANTHERiPTHR10625. PTHR10625. 1 hit.
PfamiPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFiPIRSF037913. His_deacetylse_1. 1 hit.
PRINTSiPR01270. HDASUPER.
PR01271. HISDACETLASE.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8VH37-1) [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
MEMPEEPANS GHSLPPVYIY SPEYVSICDS LVKVPKRASM VHSLIEAYAL
60 70 80 90 100
HKQMRIVKPK VASMEEMATF HTDAYLQHLQ KVSQEGDEDH PDSIEYGLGY
110 120 130 140 150
DCPATEGIFD YAAAIGGGTI TAAQCLIDGK CKVAINWSGG WHHAKKDEAS
160 170 180 190 200
GFCYLNDAVL GILRLRRKFD RILYVDLDLH HGDGVEDAFS FTSKVMTVSL
210 220 230 240 250
HKFSPGFFPG TGDMSDVGLG KGRYYSVNVP IQDGIQDEKY YHICESVLKE
260 270 280 290 300
VYQAFNPKAV VLQLGADTIA GDPMCSFNMT PVGIGKCLKY VLQWQLATLI
310 320 330 340 350
LGGGGYNLAN TARCWTYLTG VILGKTLSSE IPDHEFFTAY GPDYVLEITP
360 370
SCRPDRNEPH RIQQILNYIK GNLKHVV
Length:377
Mass (Da):41,772
Last modified:April 11, 2003 - v2
Checksum:iEEBD7B2517B235CD
GO
Isoform 2 (identifier: Q8VH37-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     246-253: SVLKEVYQ → RACFTRTP
     254-377: Missing.

Show »
Length:253
Mass (Da):28,122
Checksum:i982E94F21829B340
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti88 – 881E → D in AAL47569 (Ref. 3) Curated
Sequence conflicti118 – 1181G → A in AAL47569 (Ref. 3) Curated
Sequence conflicti130 – 1301K → M in AAL47569 (Ref. 3) Curated
Sequence conflicti170 – 1701D → E in AAL47569 (Ref. 3) Curated
Sequence conflicti187 – 1871D → V in AAL47569 (Ref. 3) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei246 – 2538SVLKEVYQ → RACFTRTP in isoform 2. 1 PublicationVSP_007178
Alternative sequencei254 – 377124Missing in isoform 2. 1 PublicationVSP_007179Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011332 mRNA. Translation: BAB27550.1.
AK131998 mRNA. Translation: BAE20928.1.
BC061257 mRNA. Translation: AAH61257.1.
AK034511 mRNA. Translation: BAC28737.1.
AK041965 mRNA. Translation: BAC31116.1.
AY066003 mRNA. Translation: AAL47569.1.
CCDSiCCDS41084.1. [Q8VH37-1]
RefSeqiNP_081658.1. NM_027382.3. [Q8VH37-1]
XP_011245974.1. XM_011247672.1. [Q8VH37-2]
UniGeneiMm.328128.

Genome annotation databases

EnsembliENSMUST00000087916; ENSMUSP00000085226; ENSMUSG00000067567. [Q8VH37-1]
GeneIDi70315.
KEGGimmu:70315.
UCSCiuc009typ.1. mouse. [Q8VH37-1]
uc009tyq.1. mouse. [Q8VH37-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011332 mRNA. Translation: BAB27550.1.
AK131998 mRNA. Translation: BAE20928.1.
BC061257 mRNA. Translation: AAH61257.1.
AK034511 mRNA. Translation: BAC28737.1.
AK041965 mRNA. Translation: BAC31116.1.
AY066003 mRNA. Translation: AAL47569.1.
CCDSiCCDS41084.1. [Q8VH37-1]
RefSeqiNP_081658.1. NM_027382.3. [Q8VH37-1]
XP_011245974.1. XM_011247672.1. [Q8VH37-2]
UniGeneiMm.328128.

3D structure databases

ProteinModelPortaliQ8VH37.
SMRiQ8VH37. Positions 14-377.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi213982. 1 interaction.
STRINGi10090.ENSMUSP00000085226.

Chemistry

BindingDBiQ8VH37.
ChEMBLiCHEMBL2347.

PTM databases

PhosphoSiteiQ8VH37.

Proteomic databases

MaxQBiQ8VH37.
PaxDbiQ8VH37.
PRIDEiQ8VH37.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000087916; ENSMUSP00000085226; ENSMUSG00000067567. [Q8VH37-1]
GeneIDi70315.
KEGGimmu:70315.
UCSCiuc009typ.1. mouse. [Q8VH37-1]
uc009tyq.1. mouse. [Q8VH37-2]

Organism-specific databases

CTDi55869.
MGIiMGI:1917565. Hdac8.

Phylogenomic databases

eggNOGiCOG0123.
GeneTreeiENSGT00530000062889.
HOGENOMiHOG000225180.
HOVERGENiHBG057112.
InParanoidiQ8VH37.
KOiK11405.
OMAiKFHTDSY.
OrthoDBiEOG722J95.
PhylomeDBiQ8VH37.
TreeFamiTF106175.

Enzyme and pathway databases

ReactomeiREACT_321346. Separation of Sister Chromatids.
REACT_329805. Resolution of Sister Chromatid Cohesion.
REACT_334621. HDACs deacetylate histones.

Miscellaneous databases

NextBioi331374.
PROiQ8VH37.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VH37.
CleanExiMM_HDAC8.
ExpressionAtlasiQ8VH37. baseline.
GenevisibleiQ8VH37. MM.

Family and domain databases

Gene3Di3.40.800.20. 1 hit.
InterProiIPR000286. His_deacetylse.
IPR003084. His_deacetylse_1.
IPR023801. His_deacetylse_dom.
[Graphical view]
PANTHERiPTHR10625. PTHR10625. 1 hit.
PfamiPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFiPIRSF037913. His_deacetylse_1. 1 hit.
PRINTSiPR01270. HDASUPER.
PR01271. HISDACETLASE.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Brain, Embryo and Thymus.
  2. "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: Pituitary.
  3. "Selective regulation of class I and II histone deacetylase expression in cultured neural cells."
    Ajamian F., Suuronen T., Salminen A.
    Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 58-206.
  4. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 195-223, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.
  5. "ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with multiple histone deacetylases and binds mSin3A through its oligomerization domain."
    Amann J.M., Nip J., Strom D.K., Lutterbach B., Harada H., Lenny N., Downing J.R., Meyers S., Hiebert S.W.
    Mol. Cell. Biol. 21:6470-6483(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CBFA2T3.

Entry informationi

Entry nameiHDAC8_MOUSE
AccessioniPrimary (citable) accession number: Q8VH37
Secondary accession number(s): Q3V270, Q9D0K6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: April 11, 2003
Last modified: July 22, 2015
This is version 117 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, Direct protein sequencing, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.