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. 2022 Sep 28;2(4):277–290. doi: 10.1016/j.jncc.2022.09.002

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© 2022 Chinese National Cancer Center. Published by Elsevier B.V.

This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

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Fig 1 — Histone modifications. Various modifications could occur on tails of four core histones, H2A, H2B, H3 and H4. And variants of H2A and H3 can also be modified by different modifications, such as acetylation or phosphorylation on H2A.X, methylation or phosphorylation on CENP-A, and phosphorylation or biotinylation on H3.3. Histone methylation and acetylation are the most common modifications and usually occur on the same lysine sites of the four histones (i.e., H2AK5/13, H2BK5/46/108, H3K4/9/14/23/27/36/56/64/79/122 and H4K5/8/12/20/31/79). What's more, several amino acid sites on histone tails could be commonly modified with more than two different modifications, including H2AK13me/ac/ar/bio, H3K9me/ac/cr, H3K14me/ac/pr/bu, H3K18me/ac/la/cr, H4K5me/ac/pr/bu/la, H4K8me/ac/pr/bio/cr and H4K12me/ac/pr/bu/bio, illustrating the role that these sites play in gene regulation and cell fate determination.