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Latest news:

March 28, 2018:
MDDGlutar : a web server was constructed for identifying glutarylation sites.

Useful Link:

- UniProtKB

- dbPTM v3
- RedoxDB
- PhosphoSitePlus

Version: 1.0
(March 28, 2018)

Welcome to MDDGlutar!

MDDGlutar is a web server for identifying glutarylation sites. Lysine glutarylation, a new protein posttranslational modification (PTM), was recently identified and characterized in both prokaryotic and eukaryotic cells. These glutarylated proteins are involved in various cellular functions such as translation and metabolism and exhibit diverse subcellular localizations. So far, despite the E. coli is the sole bacterium with protein lysine glutarylation characterized ,the substrate motif of glutarylation remains unknown.

In this study, we investigated 430 glutarylated proteins to find out specific structural motifs on the glutarylated sites. Using the TwoSampleLogo we analyze the amino acid composition surrounding the glutarylation sites. The results show that in glutarylation sites, the amount of positively charged amino acids are abundant. Furthermore, to obtain statistically significant conserved motifs, the Maximal Dependence Decomposition (MDD) was utilized.

Finally, the MDD-clustered model is adopted to develop an effective web-based tool, named MDDGlutar (http://csb.cse.yzu.edu.tw/MDDGlutar/), to identify glutarylation sites on the uncharacterized protein sequences.

System Flow