Home | Contact us | Browse | Quick Search by UniProtKB ID or Keyword


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.


How to Link:

Users can directly link to dbGSH by SwissProt ID.
For example:



PTM Resources:

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

Version: 1.0
(Dec. 10, 2013)

Introduction of 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 October 20th 2013, the dbGSH has manually accumulated more than 2200 experimentally verified S-glutathionylated peptides from 591 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.The dbGSH is now freely accessible via http://csb.cse.yzu.edu.tw/dbGSH/. The database content is regularly updated upon collecting new data from continuously surveying research articles.

System Flow of dbGSH

The distribution of KEGG pathways annotations for S-glutathionylated proteins