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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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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)




Feb. 06, 2014

RedoxDB data sets have been integrated!!!

A total of 242 experimentally verified S-glutathionylation sites on 153 S-glutathionylation proteins from RedoxDB:a curated database for experimentally verified protein oxidative modification. (Sun, Ming-an et al., 2012) have been integrated into dbGSH.

153 S-glutathionylation proteins: A. thaliana:10、B. taurus:6、C. incerta:1、C. reinhardtii:3、E. caballus:1、E. coli:3、G. gallus:1、G. partita:1、Glycine max:1、H. sapiens:46、Haemophilus influenzae:1、Human immunodeficiency virus:1、Human immunodeficiency virus 1:1、M. mulatta:1、M. musculus:11、O. cuniculus:5、P. falciparum:2、P. haloplanktis:2、P. mirabilis:1、P. trichocarpa:1、R. norvegicus:10、S. cerevisiae:42、S. scrofa:1、Triticum aestivum:1
242 S-glutathionylation sites: A. thaliana:14、B. taurus:7、C. incerta:1、C. reinhardtii:5、E. caballus:1、E. coli:3、G. gallus:1、G. partita:2、Glycine max:1、H. sapiens:79、Haemophilus influenzae:1、Human immunodeficiency virus:2、Human immunodeficiency virus 1:1、M. mulatta:1、M. musculus:20、O. cuniculus:21、P. falciparum:2、P. haloplanktis:2、P. mirabilis:1、P. trichocarpa:1、R. norvegicus:18、S. cerevisiae:56、S. scrofa:1、Triticum aestivum:1

Feb. 05, 2014

Chenglei Sun data sets have been integrated!!!

A total of 75 experimentally verified S-glutathionylation sites on 37 S-glutathionylation proteins from Prediction of S-Glutathionylation Sites Based on Protein Sequences SGDB. (Chenglei Sun et al., 2013) have been integrated into dbGSH.

37 S-glutathionylation proteins: B. taurus:1、C. papaya:1、H. sapiens:23、Human immunodeficiency virus:1、M. musculus:4、O. cuniculus:4 and R. norvegicus:3
75 S-glutathionylation sites: B. taurus:1、C. papaya:1、H. sapiens:38、Human immunodeficiency virus:2、M. musculus:4、O. cuniculus:21 and R. norvegicus:8

Jan. 02, 2014

Dian Su data sets have been integrated!!!

A total of 1816 experimentally verified S-glutathionylation sites on 1011 S-glutathionylation proteins from Proteomic identification and quantification of S-glutathionylation in mouse macrophages using resin-assisted enrichment and isobaric labeling. (Dian Su et al., 2013) have been integrated into dbGSH.

1011 S-glutathionylation proteins: B. taurus:1、H. sapiens:3、M. musculus:1006 and S. scrofa:1
1816 S-glutathionylation sites: B. taurus:21、H. sapiens:5、M. musculus:1788 and S. scrofa:2

Dec. 20, 2013

Protein disorder region will be annotated on dbGSH!

It was proposed that protein modification is associated with the protein disorder region. Thus, we integrate the protein disorder prediction tool, DISOPRED 2, to comprehensively annotate the protein entries in dbGSH. Users can investigate more structural information for protein modifications.



Dec. 23, 2013

The S-glutathionylation (GSH) sites in UniProt is integrated in dbGSH!

A total of 19 experimentally verified S-glutathionylation (GSH) sites in UniProt release 2013-03 were integrated.



Dec. 20, 2013

The orthologous conserved region of protein sequences is considered!

In order to observe whether a S-glutathionylation (GSH) sites located in the conserved regions of protein orthologous sequences, the Clusters of Orthologous Groups of proteins (COGs), was integrated. The alignment of the protein sequences in each cluster, which was implemented by ClustalW, is provided in the resource.



Dec. 15, 2013

dbGSH 1.0 is starting up!

dbGSH is a knowledge base comprising the experimental S-glutathionylation (GSH) sites, solvent accessibility of substrate, protein secondary and tertiary structures, protein domains and protein disorder. Literature related to PTM, protein conservations and substrate specificity are also analyzed. The interface is also redesigned and enhanced to facilitate access to the resource.