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It is prediction of Redox-Sensitive Cysteineproteine online server. And, this server is freely available to any user, but without any warranty.

About Redox-Sensitive Cysteine

Cysteine residues bear a thiol group that represents the most reduced state of sulfur in proteins. These thiol groups can be oxidized to disulfide (S-S), sulfenic acid (S-OH), sulfinic acid (SO2H), sulfonic acid (SO3H), S-nitrosothiol (S-NO) or S-glutathione (S-SG). Sulfenic acids are usually the intermediate of thiol-modification, which can react with other thiols or be further oxidized. Sulfinic acid and sulfonic acid represent the irreversibly oxidized products. Redox-sensitive cysteines undergo reversible thiol modifications in response to ROS or RNS, thereby modulate protein function, activity or localization, and serve as a regulatory switch for proteins in response to cellular redox state

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Copyright © 2017; Hiroyuki Kurata's Lab, Department of Bioscience and Bioinformatics, Kyushu Institute of Technology (Kyutech), Japan.