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This article is part of the supplement: Proceedings of the 2007 and 2008 Symposia on Protein N-terminal Acetylation

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Composition and biological significance of the human Nα-terminal acetyltransferases

Kristian K Starheim123, Darina Gromyko123, Rolf Velde12, Jan Erik Varhaug23 and Thomas Arnesen123*

Author Affiliations

1 Department of Molecular Biology, University of Bergen, N-5020 Bergen, Norway

2 Department of Surgical Sciences, University of Bergen, N-5020 Bergen, Norway

3 Department of Surgery, Haukeland University Hospital, N-5021 Bergen, Norway

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BMC Proceedings 2009, 3(Suppl 6):S3  doi:10.1186/1753-6561-3-S6-S3

Published: 4 August 2009


Protein Nα-terminal acetylation is one of the most common protein modifications in eukaryotic cells, occurring on approximately 80% of soluble human proteins. An increasing number of studies links Nα-terminal acetylation to cell differentiation, cell cycle, cell survival, and cancer. Thus, Nα-terminal acetylation is an essential modification for normal cell function in humans. Still, little is known about the functional role of Nα-terminal acetylation. Recently, the three major human N-acetyltransferase complexes, hNatA, hNatB and hNatC, were identified and characterized. We here summarize the identified N-terminal acetyltransferase complexes in humans, and we review the biological studies on Nα-terminal acetylation in humans and other higher eukaryotes.