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. 2021 Jan 22;12(1):120. doi: 10.1038/s41419-020-03361-5

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© The Author(s) 2021

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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — a A schematic representation of ubiquitylation/deubiquitylation events of target proteins and the cellular outcome. b The ubiquitylation cascade by three types of enzyme: ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2), and ubiquitin ligase (E3). c The seven lysine residues and the N-terminal methionine (M1) are projected on the structure of ubiquitin (PDB code 1UBQ⁹⁸). d Principles of substrate recognition and ubiquitin cleavage by DUBs. e. Families of DUBs classified by sequence homology of their catalytic domains.