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Q0VCB2 (HDAC8_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone deacetylase 8

Short name=HD8
EC=3.5.1.98
Gene names
Name:HDAC8
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length377 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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. 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.

Catalytic activity

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

Cofactor

Binds 1 divalent metal cation per subunit.

Enzyme regulation

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

Subunit structure

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).

Subcellular location

Nucleus By similarity. Cytoplasm By similarity.

Post-translational modification

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

Sequence similarities

Belongs to the histone deacetylase family. HD type 1 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 377377Histone deacetylase 8
PRO_0000389507

Regions

Region14 – 324311Histone deacetylase By similarity

Sites

Active site1431Proton acceptor By similarity
Metal binding1781Divalent metal cation By similarity
Metal binding1801Divalent metal cation By similarity
Metal binding2671Divalent metal cation By similarity
Binding site1011Substrate By similarity
Binding site1511Substrate; via carbonyl oxygen By similarity
Binding site3061Substrate By similarity

Amino acid modifications

Modified residue391Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0VCB2 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 1120A71660F14E7D

FASTA37741,683
        10         20         30         40         50         60 
MEESEEPADA GQSLPPVYIY SPEYVSVCDS LAKVPKRASM VHSLIEAYAL HKQMRIVKPK 

        70         80         90        100        110        120 
VASMEEMASF HTDAYLQHLQ KVSEDGDDDH PDSIEYGLGY DCPATEGIFD YAAAVGGATI 

       130        140        150        160        170        180 
TAAQCLIDGM CKVAINWSGG WHHAKKDEAS GFCYLNDAVL GILRLRRKFD RILYVDLDLH 

       190        200        210        220        230        240 
HGDGVEDAFS FTSKVMTVSL HKFSPGFFPG TGDVSDVGLG KGRYYSVNVP IQDCIQDERY 

       250        260        270        280        290        300 
YHICESVLKE VYIAFNPKAV VLQLGADTIA GDPMCSFNMT PVGIGKCLKY ILQWELATLI 

       310        320        330        340        350        360 
LGGGGYNLAN TARCWTYLTG VILGKTLSSE IPDHEFFTAY GPDYVLEITP SCRPDRNEPH 

       370 
RVQQILNYIK GNLKHVV 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC120257 mRNA. Translation: AAI20258.1.
RefSeqNP_001069699.1. NM_001076231.2.
UniGeneBt.90254.

3D structure databases

ProteinModelPortalQ0VCB2.
SMRQ0VCB2. Positions 14-377.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID540666.
KEGGbta:540666.

Organism-specific databases

CTD55869.

Phylogenomic databases

HOVERGENHBG057112.
KOK11405.

Family and domain databases

Gene3D3.40.800.20. 1 hit.
InterProIPR000286. His_deacetylse.
IPR003084. His_deacetylse_1.
IPR023801. His_deacetylse_dom.
[Graphical view]
PANTHERPTHR10625. PTHR10625. 1 hit.
PfamPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFPIRSF037913. His_deacetylse_1. 1 hit.
PRINTSPR01270. HDASUPER.
PR01271. HISDACETLASE.
ProtoNetSearch...

Other

NextBio20878759.

Entry information

Entry nameHDAC8_BOVIN
AccessionPrimary (citable) accession number: Q0VCB2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 24, 2009
Last sequence update: September 5, 2006
Last modified: April 16, 2014
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families