dbGSH: a database of S-glutathionylation

Area of Science:

• Biochemistry
• Molecular Biology
• Proteomics

Background:

• S-glutathionylation is a reversible protein posttranslational modification (PTM) crucial for regulating protein activity, stability, and cellular redox balance.
• The importance of S-glutathionylation in oxidative and nitrosative stress response has led to the development of various detection methods, expanding the known sites of this modification.
• A need exists for a centralized resource integrating experimentally verified S-glutathionylation sites with their associated characteristics.

Purpose of the Study:

• To create the dbGSH database, a comprehensive resource for experimentally verified S-glutathionylation sites.
• To provide integrated structural and functional information for identified S-glutathionylation sites.
• To facilitate research on the roles of S-glutathionylation in cellular processes.

Main Methods:

• Manual curation of >2200 experimentally verified S-glutathionylated peptides from 169 research articles using text-mining.
• Mapping peptide sequence identity to UniProtKB protein entries to standardize data.
• Performing structural and functional analyses, including motif identification, solvent accessibility, secondary/tertiary structure, protein domains, and gene ontology.

Main Results:

• The dbGSH database has been established, containing over 2200 experimentally verified S-glutathionylated peptides.
• Data is standardized by mapping to UniProtKB entries, addressing heterogeneity from diverse sources.
• The database offers detailed structural and functional analyses of S-glutathionylation sites.

Conclusions:

• dbGSH serves as a valuable, integrated resource for S-glutathionylation research.
• The database aids in understanding the structural basis and functional implications of S-glutathionylation.
• dbGSH is freely accessible and regularly updated, supporting ongoing research in redox biology.