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. 2021 Jul 30;2:23. doi: 10.1186/s43556-021-00043-2

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© The Author(s) 2021

Open AccessThis 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 — Different ubiquitin linkage types and their functions. Ubiquitin (Ub) a small protein consists of 76 amino acids highly conserved among all eukaryotes. Ubiquitin is characterized by its 7 lysine sites (K6, K11, K27, K29, K33, K48, K63) and N-terminal methionine1 (Met1) site, which are also functional sites. Due to these specific linkage sites, ubiquitination can be classified into different styles and then perform distinct biological functions. And ubiquitin attaches to target substrate through identifying its lysine (K) site