  As the only thiol-bearing amino acid, cysteine (Cys) residues in proteins
have the reactive thiol side chain, which is susceptible to a series of
post-translational modifications (PTMs). These PTMs participate in a wide range
of biological activities including the alteration of enzymatic reactions,
protein-protein interactions and protein stability. Here we summarize the
advance of cysteine PTM identification technologies and the features of the
various kinds of the PTMs. We also discuss in silico approaches for the
prediction of the different types of cysteine modified sites, giving directions
for future study.
