N-terminal acetylation is one of the most abundant protein modifications in eukaryotes and is catalysed in humans by seven N-terminal acetyltransferases. AtNAA50 interreact with the NatA complex (NAA1
NAA10 serves as the catalytic subunit for both the NatA and N-terminal acetyltransferase E (NatE) complexes. To investigate the impact of the NAA10p.S37P mutation on N-terminal acetylation in COs, we
The human N-terminal acetyltransferase E (NatE) including its associated NatA co-translationally acetylates the N-terminus of about 40-60% of the proteome to mediate diverse biological processes inclu
Protein N-terminal acetylation (Nα-acetylation) is one of the most common modifications in both eukaryotes and prokaryotes. Although studies have shown that Nα-acetylation plays important roles in pro
Quantitative COFRADIC-based analysis of N-terminal acetylation in yeast (S. cerevisiae) and HeLa proteomes determined the acetylation status of 648 and 1345 unique N-termini in the two species, respec
