These tails are subject to several publish-translational covalent modifications, together with acetylation, phosphorylation, ubiquitination, sumoylation and methylation (reviewed in 1 ). Methylation been found on a spread of lysine residues in various histones: K4 (using the only-letter amino-acid code for lysine), K9, solicitor 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 three A number of proteins answerable for the methylation of specific residues have been characterized, and all but considered one of these comprises a SET area