Acts as an atypical protein-lysine deacetylase in vitro (PubMed:31478652). Catalyzes the deacetylation of lysine residues using CoA as substrate, generating acetyl-CoA and the free amine of protein-lysine residues (PubMed:31478652). Additional experiments are however required to confirm the protein-lysine deacetylase activity in vivo (Probable). 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 (PubMed:31478652, PubMed:14672934). May activate transcription (PubMed:14672934). acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein] kcat is 2.2 min(-1) for p-nitrophenyl-acetate (PubMed:31478652). kcat is 0.6 min(-1) for p-nitrophenyl-butyrate (PubMed:31478652). kcat is 0.2 min(-1) for p-nitrophenyl-octanoate (PubMed:31478652). May interact with TAF1. Predominantly cytoplasmic. Ubiquitous (PubMed:14672934). Detected in spleen, thymus, prostate, testis, ovary, small intestine, colon, peripheral blood leukocyte, heart, placenta, lung, liver, skeletal muscle, pancreas and kidney (PubMed:14672934). 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. Additional experiments are therefore required to confirm this activity in vivo.