Acts as an atypical protein-lysine deacetylase in vitro. Catalyzes the deacetylation of lysine residues using CoA as substrate, generating acetyl-CoA and the free amine of protein-lysine residues. Additional experiments are however required to confirm the protein-lysine deacetylase activity in vivo. Has hydrolase activity towards various surrogate p-nitrophenyl (pNp) substrates, such as pNp-butyrate, pNp-acetate and pNp-octanoate in vitro, with a strong preference for pNp-acetate. May activate transcription. acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein] May interact with TAF1. Predominantly cytoplasmic. Belongs to the AB hydrolase superfamily. ABHD14 family. The protein-lysine deacetylase activity using CoA as substrate is unclear as this protein belongs to a family of serine hydrolases, and that the reaction shown in the publication is not hydrolyzing H(2)O (By similarity). Additional experiments are therefore required to confirm this activity in vivo (By similarity).