Protein tyrosine-O-sulfation in the retina

Tyrosine O Sulfation: An Overview

Tyrosine O sulfation is a post translational modification (PTM) originally discovered by Bettelheim in 1954 in the bovine protein fibrinogen. Currently, this PTM is found only in secreted and transmembrane proteins of higher eukaryotes. This article gives an overview of experimental tools to study tyrosine O sulfation and also describes the biological function of this PTM.

The biology and enzymology of protein tyrosine O-sulfation.

The Sulfinator: predicting tyrosine sulfation sites in protein sequences

UNLABELLED Protein tyrosine sulfation is an important post-translational modification of proteins that go through the secretory pathway. No clear-cut acceptor motif can be defined that allows the prediction of tyrosine sulfation sites in polypeptide chains. The Sulfinator is a software tool that can be used to predict tyrosine sulfation sites in protein sequences with an overall accuracy of 98%...

Tyrosine Sulfation of Statherin

Tyrosylprotein sulfotransferase (TPST), responsible for the sulfation of a variety of secretory and membrane proteins, has been identified and characterized in submandibular salivary glands (William et al. Arch Biochem Biophys 1997; 338: 90-96). In the present study we demonstrate the sulfation of a salivary secretory protein, statherin, by the tyrosylprotein sulfotransferase present in human s...

Incorporating support vector machine for identifying protein tyrosine sulfation sites

Tyrosine sulfation is a post-translational modification of many secreted and membrane-bound proteins. It governs protein-protein interactions that are involved in leukocyte adhesion, hemostasis, and chemokine signaling. However, the intrinsic feature of sulfated protein remains elusive and remains to be delineated. This investigation presents SulfoSite, which is a computational method based on ...