HDAC3 (UniProt/Swiss-Prot entry O15379) catalyses the deacetylation of lysine residues in the N-terminal part of the core histones (H2A, H2B, H3 and H4). Acetylation and deacetylation of these highly conserved lysine residues is important for the control of gene expression and HDAC activity is associated with gene repression. Histone deacetylation is established by the formation of large multiprotein complexes. HDAC3 may bind to the zinc-finger transcription factor YY1, thereby regulating transcription. It is also able to modulate cell growth and apoptosis through the interaction with p53 and is thought to be essential for the repression of the POU1F1 transcription factor.