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Abstract:
Posttranslational protein modification (PTM) has been studied as a regulatory mechanism to control a wide range of protein functions. Unlike irreversible PTMs (e.g. proteolysis), 1 or several specific amino acid residues of proteins are reversibly decorated by adding a chemically modifying group that potentially changes biochemical/biophysical protein properties, such as protein surface charge and structures, affecting various protein behaviors like enzyme activity, protein-protein interaction, and even protein localization (Friso and van Wijk 2015; Basak et al. 2016). Recent advances in mass spectrometry–based proteomics allow us to identify and quantify thousands of PTM sites in a more comprehensive manner, with a growing number of public databases of PTM sites available in various organism species (Doll and Burlingame 2015). According to dbPTM, a database of kingdam-wide PTM sites, phosphorylation, acetylation, and ubiquitination are the major PTMs, comprising more than 90% (∼827,000 sites out of ∼908,000) of all the reported PTMs (Li et al. 2022). Besides those, various types of PTMs were recently identified and characterized, such as nitrosylation and persulfidation (Li et al. 2022).
