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Protein

Histone deacetylase 8

Gene

HDAC8

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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.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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Hydrolase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone deacetylase 8 (EC:3.5.1.98)
Short name:
HD8
Gene namesi
Name:HDAC8
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 377377Histone deacetylase 8PRO_0000389507Add
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

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000054707.

Structurei

3D structure databases

ProteinModelPortaliQ0VCB2.
SMRiQ0VCB2. Positions 14-377.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG057112.
InParanoidiQ0VCB2.
KOiK11405.

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.

Sequencei

Sequence statusi: Complete.

Q0VCB2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEESEEPADA GQSLPPVYIY SPEYVSVCDS LAKVPKRASM VHSLIEAYAL
60 70 80 90 100
HKQMRIVKPK VASMEEMASF HTDAYLQHLQ KVSEDGDDDH PDSIEYGLGY
110 120 130 140 150
DCPATEGIFD YAAAVGGATI TAAQCLIDGM CKVAINWSGG WHHAKKDEAS
160 170 180 190 200
GFCYLNDAVL GILRLRRKFD RILYVDLDLH HGDGVEDAFS FTSKVMTVSL
210 220 230 240 250
HKFSPGFFPG TGDVSDVGLG KGRYYSVNVP IQDCIQDERY YHICESVLKE
260 270 280 290 300
VYIAFNPKAV VLQLGADTIA GDPMCSFNMT PVGIGKCLKY ILQWELATLI
310 320 330 340 350
LGGGGYNLAN TARCWTYLTG VILGKTLSSE IPDHEFFTAY GPDYVLEITP
360 370
SCRPDRNEPH RVQQILNYIK GNLKHVV
Length:377
Mass (Da):41,683
Last modified:September 5, 2006 - v1
Checksum:i1120A71660F14E7D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC120257 mRNA. Translation: AAI20258.1.
RefSeqiNP_001069699.1. NM_001076231.2.
UniGeneiBt.90254.

Genome annotation databases

GeneIDi540666.
KEGGibta:540666.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC120257 mRNA. Translation: AAI20258.1.
RefSeqiNP_001069699.1. NM_001076231.2.
UniGeneiBt.90254.

3D structure databases

ProteinModelPortaliQ0VCB2.
SMRiQ0VCB2. Positions 14-377.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000054707.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi540666.
KEGGibta:540666.

Organism-specific databases

CTDi55869.

Phylogenomic databases

HOVERGENiHBG057112.
InParanoidiQ0VCB2.
KOiK11405.

Miscellaneous databases

NextBioi20878759.

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

  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Thymus.

Entry informationi

Entry nameiHDAC8_BOVIN
AccessioniPrimary (citable) accession number: Q0VCB2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 24, 2009
Last sequence update: September 5, 2006
Last modified: June 24, 2015
This is version 54 of the entry and version 1 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. 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.