※Computational resources of Protein Sulfation:
Last updated: May 5th, 2014
Introduction :
Protein tyrosine sulfation is an improtant post-translational modification of proteins. It was firstly observed by Bettlheim in bovine fibrinopeptide β in 1954. As the demonstration of its prevalence in mammalian cells in 1982, investigation of sulfation has been popular. Tyrosine sulfation, as one of the most universal modifications which plays an important role in secreted and transmembrane proteins, has been verified to be essential to extracelluar protein-protein interactions, intracellular protein transportation modulation, various pathophysiologial process regulation and protein proteolytic process regulation.
We apologized that the computational studies without any web links of databases or tools will not be included in this compendium, since it's not easy for experimentalists to use studies directly. We are grateful for users feedback. Please inform Zhicheng Pan, Zexian Liu, Dr. Yu Xue or Dr. Jian Ren to add, remove or update one or multiple web links below.
Index:
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<1>Protein Sulfation Databases:
1. UniProt: The Universal Protein Resource (The UniProt Consortium et al., 2012).
2. SysPTM: A systematic resource for proteomic research on post-translational modifications (Li H et al., 2009).
3. dbPTM: An information repository of protein post-translational modification (Lee TY et al., 2006).
<2> Prediction of Protein of Tyrosine Sulfation:
1. SulfoSite: Incorporating support vector machine for identifying protein tyrosine sulfation sites (Chang WC al., 2009).
2. Sulfinator: Predicts tyrosine sulfation sites in protein sequences (Monigatti F al., 2002).