Using in silico analysis a number of potential sites for post-translational 
modifications has been revealed within the human O6-methylguanine-DNA 
methyltransferase (MGMT) protein. In particular these were the acetylation of 
Gly3 residue in the N-terminus of protein and internal residues Lys132 and 
Lys135; Arg166 residue methylation; Lys63 SUMOylation and ubiquitination of 
Lys31, Lys39, Lys49, Lys63, Lys67, Lys135, Lys156, Lys196, Lys209. Also it has 
been predicted 16 novel potential phosphorylation sites of serine residues 
(positions 13, 124, 144, 182, 183, 190, 215, 216 and 230), tyrosine residues 
(positions 100 and 189) and threonine residues (positions 23, 69, 94, 126 and 
229), as well as five binding sites for kinases and other proteins (Serl3 with 
14-3-3, Val21 and Ile172 with D-domain, Pro78 and Pro111 with SH3-domain, Pro111 
with MAPK3). Some kinases predicted by the authors are known as partners of the 
MGMT protein, that confirms the probability of modification of the given sites. 
Potential sites require further experimental confirmation of modifications and 
investigation of their influence on stability and DNA-repair activity of this 
protein.