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Latest news:

Feb. 06, 2014:
A total of 242 experimentally verified S-glutathionylation sites on 153 S-glutathionylation proteins from RedoxDB. (Sun, Ming-an et al., 2012) have been integrated into dbGSH.


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PTM Resources:

- UniProt KB
- PhosphoSite
- dbPTM 3.0
- dbSNO
- RegPhos
- KinasePhos
- Phospho.ELM
- OGlycBase

Version: 1.0
(Dec. 10, 2013)

Welcome to dbGSH!

dbGSH is a database that integrates the experimentally verified cysteine S-glutathionylation (GSH) sites from multiple species.

S-glutathionylation (GSH), the reversible protein post-translational modification (PTM) that generates a mixed-disulfide bond between glutathione and cysteine reside, 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 rapidly evolve to increase the dataset of experimentally determined glutathionylation sites. However, there is currently no database dedicated to the integration of all experimentally verified S-glutathionylation sites with their characteristics, structure or functional information.

Thus, the dbGSH database is created to integrate all available datasets and to provide their structural analysis. Up to December 10th 2013, the dbGSH has manually accumulated more than 2200 experimentally verified S-glutathionylated peptides from more research articles using a text mining approach. To solve the heterogeneity among the data collected from different sources, the sequence identity of these reported S-glutathionylated peptides are mapped to the UniProtKB protein entries. To delineate the structural correlation and consensus motif of these GSH sites, the dbGSH database also provides structural and functional analyses, including the motifs of substrate sites, solvent accessibility, protein secondary and tertiary structures, protein domains, and gene ontology.

Investigation of cysteine S-glutathionylation (GSH) sites

S-glutathionylation is a reversible post-translational modification in vivo that glutathione conjugates on cysteine residues of proteins by disulfide bond. This modification adds ~305 Da and introduces a net negative charge on protein. Moreover, cysteine residues having low pKa values are more facile to make addition of glutathione. To get a better understanding and characterize the potential linear consensus motif and adjacent amino acids surrounding to glutathionylated cysteine residues, 2224 S-glutathionylated cysteines are further compared with the free cysteines by two sample logo. The GSH sites contain a higher preference of negatively charged residues (D and E) than non-GSH sites.