Names & Taxonomy

Uniprot ID:
Q9BY41
Entry Name:
HDAC8_HUMAN
Status:
reviewed
Protein Names:
Histone deacetylase 8 (HD8) (EC 3.5.1.98)
Gene Names:
HDAC8 HDACL1 CDA07
Gene Names Orf:
CDA07
Gene Names Primary:
HDAC8
Organism:
Homo sapiens (Human)

Structure

Length:
377
Sequence:
MEEPEEPADSGQSLVPVYIYSPEYVSMCDSLAKIPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIEYGLGYDCPATEGIFDYAAAIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCRPDRNEPHRIQQILNYIKGNLKHVV
Proteomes:
UP000005640

Subcellular location

Subcellular Location:
Nucleus. Cytoplasm. Note=Excluded from the nucleoli. Found in the cytoplasm of cells showing smooth muscle differentiation.

Function

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.
Catalytic Activity:
Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.
Cofactor:
COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; ; Note=Binds 1 divalent metal cation per subunit.;
Enzyme Regulation:
ENZYME REGULATION: Its activity is inhibited by trichostatin A (TSA), suberoylanilide hydroxamic acid (SAHA), 3-(1-methyl-4-phenylacetyl-1H-2-pyrrolyl)-N-hydroxy-2-propenamide (APHA), 4-dimethylamino-N-(6-hydroxycarbamoyethyl)benzamide-N-hydroxy-7-(4-dimethylaminobenzoyl)aminoheptanamide (MS-344), 5-(4-methyl-benzoylamino)-biphenyl-3,4'-dicarboxylic acid 3-dimethylamide 4'-hydroxyamide (CRA-A) and butyrate.
Active Site:
ACT_SITE 143 143 Proton acceptor.
Cross Reference Drug Bank:
DB06603 DB02546
Gene Ontology Go:
cytoplasm
cytosol
histone deacetylase complex
nuclear chromosome
nucleoplasm
nucleus
plasma membrane
histone deacetylase activity
Hsp70 protein binding
Hsp90 protein binding
metal ion binding
NAD-dependent histone deacetylase activity (H3-K14 specific)
transcription factor binding
chromatin assembly or disassembly
chromatin modification
chromatin organization
mitotic cell cycle
negative regulation of protein ubiquitination
negative regulation of transcription from RNA polymerase II promoter
regulation of cohesin localization to chromatin
regulation of protein stability
regulation of telomere maintenance
sister chromatid cohesion
transcription, DNA-templated
Gene Ontology Biological Process:
chromatin assembly or disassembly
chromatin modification
chromatin organization
mitotic cell cycle
negative regulation of protein ubiquitination
negative regulation of transcription from RNA polymerase II promoter
regulation of cohesin localization to chromatin
regulation of protein stability
regulation of telomere maintenance
sister chromatid cohesion
transcription, DNA-templated
Gene Ontology Molecular Function:
histone deacetylase activity
Hsp70 protein binding
Hsp90 protein binding
metal ion binding
NAD-dependent histone deacetylase activity (H3-K14 specific)
transcription factor binding
Gene Ontology Cellular Component:
cytoplasm
cytosol
histone deacetylase complex
nuclear chromosome
nucleoplasm
nucleus
plasma membrane
Keywords:
3D-structure
Alternative splicing
Chromatin regulator
Complete proteome
Cytoplasm
Disease mutation
Hydrolase
Mental retardation
Metal-binding
Nucleus
Obesity
Phosphoprotein
Reference proteome
Repressor
Transcription
Transcription regulation

Publication

PubMed ID:
10748112 10926844 10922473 10756090 8889548 14702039 15772651 15489334 11533236 12509458 14701748 15772115 16538051 16809764 22889856 22885700 15242608 17721440 19053282