Abstract
Lysine methylation is one of the most important post-translational modifications (PTMs) of proteins as it regulates various biological processes including cell growth, division, gene expression, and DNA/RNA binding. Due to lysine’s unique structure, it can undergo mono-, di-, and tri-methylation, and different degrees of methylation result in distinct functions and locations within a cell. Deregulation in lysine methylation leads to a variety of diseases. There is great interest in delineating the global role of methylated lysine PTMs in diseases. We estimate that the size of the lysine methyl proteome is significantly larger than what is currently known. Therefore, it is important to discover complete sites of lysine methyl proteome and associated PPIs to fully understand their functions. Our group has developed different chemical reactions to profile the different states of lysine methylation.
