SIRT2 is a member of the sirtuin family of proteins. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. SIRT2 interacts with HDAC6, suggesting that these proteins belong to a large complex that deacetylate the cytoskeleton.
SIRT2 is a NAD-dependent deacetylase, which deacetylates the 'Lys-40' of alpha-tubulin. Involved in the control of mitotic exit in the cell cycle, probably via its role in the regulation of cytoskeleton. Despite some ability to deacetylate histones in vitro, it is unlikely in vivo.