S-glutathionylation site databases | Post-translational modification data analysis
S-glutathionylation, the reversible protein posttranslational modification (PTM) that generates a mixed disulfide bond between glutathione and cysteine residue, critically regulates protein activity, stability and redox regulation. Due to its importance in regulating oxidative/nitrosative stress and balance in cellular response, a number of methods have been rapidly developed to study S-glutathionylation, thus expanding the dataset of experimentally determined glutathionylation sites.
Offers a collection of post-translational modifications (PTMs). dbPTM contains a dataset of experimentally verified PTMs supported by the literature and gives an access to databases and tools associated with PTM analysis. It integrates the emerging S-nitrosylation, S-glutathionylation and succinylation, from approximately 500 research articles which were extracted by text mining.
Provides information about protein oxidative modification verified by experimental studies. For each modified cysteine, the exact position, modification type and flanking sequence are provided. Additional information, including gene name, organism, sequence, literature references and links to UniProt and PDB, is also supplied. The database supports several functions including data search, blast and browsing. RedoxDB not only includes data from case-by-case studies but also integrates high-throughput data from proteomics studies. RedoxDB is useful for both experimental studies and computational analyses of protein oxidative modification.
A public resource to allow efficient access to experimentally validated S-glutathionylation sites and comprehensive bioinformatics analyses, including functional annotations, structural characteristics and substrate motifs for S-glutathionylation sites. The database not only provides a benchmark dataset for the development of computational prediction tools and their comparison but also supplies the potential glutathionylated targets for verification and other biological applications.
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