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Background：
Lysine butyrylation is a newly discovered reversible post-translational modification, which is structurally analogous to lysine acetylation and lysine propionylation and participates in the regulation of protein biological activity. By virtue of integrated proteomic strategies and biochemical analysis, lysine butyrylation has been extensively identified in prokaryotes and eukaryotes, occurring on a large number of substrates including histones and non-histone proteins. Multiple lysine residues of histones and key non-histone proteins such as p53 and p300/CBP can undergo butyrylation modification. Lysine butyrylation exerts essential regulatory functions in epigenetic modulation, mainly by affecting chromatin dynamics and plasticity, mediating DNA transcription regulation, and participating in the occurrence and development of tumorigenesis and other pathological processes.
