N-Acetyltransferase 6 (NAT6)

FUS2 has NAT activity but not histone acetyltransferase activity. It uses a binary ping-pong process involving the formation of a covalent NAT/acetyl-coA intermediate, whereby acetyl-coA binds to the nucleophile in the active site of the enzyme before the acetyl group is transferred to the substrate by nucleophilic attack. The deduced 286-amino acid conserved, soluble nuclear protein is 69% identical to the mouse protein. It contains an acetyltransferase (GNAT) domain, a proline-rich domain, an SH2 domain, a ZP motif, and a eukaryotic thiol protease signature motif. Mutations were found in approximately 5% of cell lines tested, but none of the genes identified in the search had a high frequency of mutations. An alternatively spliced form with an intron in the 5-prime untranslated region encodes an identical predicted amino acid sequence.