Putative protein-lysine deacylase ABHD14B

ABHD14B is a putative protein-lysine deacylase that catalyzes the deacetylation of lysine residues using CoA as a substrate, generating acetyl-CoA and free protein-lysine amines (UniProt: Q96IU4). The protein demonstrates hydrolase activity toward various p-nitrophenyl substrates in vitro with preference for p-nitrophenyl acetate, and may also function as a transcriptional activator, though in vivo confirmation of deacetylase activity remains pending (UniProt: Q96IU4).

ABHD14B is a 210-amino acid protein with no explicit disease associations recorded in UniProt. It represents a member of the ABHD family of hydrolases with putative regulatory roles in post-translational modification of cellular proteins.

ABHD14B is associated with Alzheimer's Disease and was detected as upregulated in human post-mortem AD brain tissue compared to age-matched controls (Chaparral AD proteomics). Analysis of TMT-labeled proteomics across four subcellular fractions showed a mean log2 fold-change of 0.91, indicating modest elevation in AD brain. This upregulation may reflect altered protein deacetylation pathways relevant to AD pathobiology, though functional significance in disease progression remains to be established.