biostudies-literatureUnknown10(4)Chen YJS-glutathionylation, the covalent attachment of a glutathione (GSH) to the sulfur atom of cysteine, is a selective and reversible protein post-translational modification (PTM) that regulates protein activity, localization, and stability. Despite its implication in the regulation of protein functions and cell signaling, the substrate specificity of cysteine S-glutathionylation remains unknown. Based on a total of 1783 experimentally identified S-glutathionylation sites from mouse macrophages, this work presents an informatics investigation on S-glutathionylation sites including structural factors such as the flanking amino acids composition and the accessible surface area (ASA). TwoSampleLogo presents that positively charged amino acids flanking the S-glutathionylated cysteine may influencePloS onee0118752https://www.ebi.ac.uk/biostudies/studies/S-EPMC4388702biostudies-literatureGSHSite: exploiting an iteratively statistical method to identify s-glutathionylation sites with substrate specificity.PMC4388702Huang KYLee TYChen YJLu CTWu HYfalseGSHSite: exploiting an iteratively statistical method to identify s-glutathionylation sites with substrate specificity.S-glutathionylation, the covalent attachment of a glutathione (GSH) to the sulfur atom of cysteine, is a selective and reversible protein post-translational modification (PTM) that regulates protein activity, localization, and stability. Despite its implication in the regulation of protein functions and cell signaling, the substrate specificity of cysteine S-glutathionylation remains unknown. Based on a total of 1783 experimentally identified S-glutathionylation sites from mouse macrophages, this work presents an informatics investigation on S-glutathionylation sites including structural factors such as the flanking amino acids composition and the accessible surface area (ASA). TwoSampleLogo presents that positively charged amino acids flanking the S-glutathionylated cysteine may influence2015-01-01T00:00:00Z20152025-04-19T02:51:55.884Z2019-03-26T23:31:54ZS-EPMC43887022584993510.1371/journal.pone.0118752