N-Acetyltransferase 5 (NAT5)

NAT5 is a component of N-acetyltransferase complex B (NatB). Human NatB performs cotranslational N(alpha)-terminal acetylation of methionine residues when they are followed by asparagine .

The deduced 178-amino acid protein has a calculated molecular mass of 20.4 kD and contains a central acetyltransferase domain. NAT3 shares 41.3% amino acid identity with its yeast ortholog. Western blot analysis detected NAT3 in all human cell lines examined. Immunofluorescence analysis of HeLa cells revealed strong nuclear localization and weaker cytoplasmic localization of NAT3.The immunoprecipitated complex showed NatB activity against the synthetic peptide MDEL, but not against any other peptide examined.