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. 2024 Oct 11;56(10):2127–2144. doi: 10.1038/s12276-024-01329-5

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — Schematic representation of a nucleosome showing the principal lysine methylation sites on histones H3 and H4. The histone octamer composed of an H3-H4 tetramer combined with two H2A-H2B dimers, along with the DNA lesion surrounding them, collectively constitute the nucleosome, which is the main structural element of chromatin. The reported KMTs and KDMs for each type of lysine methylation are indicated. Modifiers whose protein stability is reported to be regulated by the UPS are highlighted in red.