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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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How to Link:

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

http://csb.cse.yzu.
edu.tw/dbgsh/
search_result.php?swiss_id
=FAS_HUMAN

 

PTM Resources:

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

Version: 1.0
(Dec. 10, 2013)



Tutorial in Search Page

Step 1. Three major queries in search page. Users can query their interested protein by input the protein name, gene name, UniProtKB ID or AC in search field of homepage. It was also allowed the users to query the amino acid sequence against the release 2013_03 of Swiss-Prot protein sequences.

Step 2. The search result. Since users input the keyword of protein name or gene name, UniProtKB ID or AC in search field of homepage. The proteins matching the query keywords were shown in a table. Then, users can click on the URL link "show" to view the detailed information about the protein, such as protein function, S-glutathionylation sites, protein doamin, etc.

Step 3. The detail information about S-glutathionylation. Users can view the experimental S-glutathionylation sites and graphical visualizations. Graphical visualization could reveal an overview of the S-glutathionylation sites, the solvent accessibility of the residues, protein variations, protein secondary structures and protein functional domains in protein sequence. (a) Quick search by IDs and keywords. (b) Basic information. (c) Graphical visualization of S-glutathionylation sites with structural characteristics and functional domains. (d) Table of S-glutathionylation sites with reported literatures. (e) Visualization of tertiary structure.

Step 4. The substrate motifs conserved regions. Users can investigate whether a S-glutathionylation site located in substrate motifs conserved regions by click on the URL in the table of S-glutathionylation sites.




Tutorial in Browse Page

Step 1. The summary table of S-glutathionylations. To facilitate the investigation in each type of S-glutathionylation, we developed a summary table for users to browse all the types of S-glutathionylation in the release 1.0 of dbGSH. In the table, each type of S-glutathionylation was categorized by their modified amino acids with the number of experimentally verified sites. For example, users can choose the H. sapiens (Human) to take the more detailed information such as the position of modification on amino acid, the location of modification on protein sequence, the modified chemical formula, and the mass difference.

Step 2. Users can investigate the detailed information H. sapiens (Human) on proteins, such as the position of modification on amino acid, the location of modification on protein sequence, the modified chemical formula, and the mass difference. Especially, the formula structure was visualized by the Jmol program which was implemented in JAVA Applet. However, the most effective knowledge about the S-glutathionylation is the substrate site specificity including the frequency of amino acids, the average solvent accessibility, and the frequency of secondary structure surrounding the modified site. The sequence logo which represents the frequency of amino acids and the frequency of secondary structure surrounding the modified sites was provided.