Catalytic activity:Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.,Caution:The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.,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.,miscellaneous:Its activity is inhibited by trichostatin A (TSA) and butyrate, two well known histone deacetylase inhibitors.,similarity:Belongs to the histone deacetylase family. Type 1 subfamily.,subcellular location:Excluded from the nucleoli.,subunit:Interacts with PEPB2-MYH11, a fusion protein consisting of the 165 N-terminal residues of CBF-beta (PEPB2) with the tail region of MYH11 produced by the inversion Inv(16)(p13q22), a translocation associated with acute myeloid leukemia of M4EO subtype. The PEPB2-MYH1 fusion protein also interacts with RUNX1, a well known transcriptional regulator, suggesting that the interaction with HDAC8 may participate in the conversion of RUNX1 into a constitutive transcriptional repressor. Interacts with CBFA2T3.,tissue specificity:Weakly expressed in most tissues. Expressed at higher level in heart, brain, kidney and pancreas.,
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