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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