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<br>These tails are topic to several put [up-translational covalent](http://git.xitaogo.cn/traciowsley42/solicitor-uk2012/wiki/Meals+Excessive+In+Lysine) modifications, together with acetylation, phosphorylation, ubiquitination, sumoylation and methylation (reviewed in 1 ). Methylation been found on a range of lysine residues in numerous histones: K4 (using the one-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 A number of proteins chargeable for the methylation of specific residues have been characterized, and all but considered one of these contains a SET domain |
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