gnu.orgThese tails are subject to a number of publish-translational covalent modifications, including acetylation, phosphorylation, ubiquitination, sumoylation and methylation (reviewed in 1 ). Methylation been found on a variety of lysine residues in numerous histones: K4 (utilizing the only-letter amino-acid code for lysine), K9, K27, K36 and K79 in histone H3, K20 in histone H4, K59 within the globular area of histone H4 2 and K26 of histone H1B 3 Several proteins chargeable for the methylation of specific residues have been characterised, and all but one among these accommodates a SET area