Welcome to iCysMod

Cysteine occupies a distinctive position in protein chemistry, while the thiol group permits cysteine residue to undergo a wide range of oxidative post-translational modifications (OxiPTMs) mainly including classical disulfide formation (-SSR), S-glutathionylation (-SSG), S-nitrosylation (-SNO), S-sulfhydration (-SSH), S-sulfenylation (-SOH), S-sulfinylation (-SO2H) and S-sulfonylation (-SO3H). Besides, the thioesterification reaction could lead to S-palmitoylation through reversibly adding one or multiple palmitoyl moieties to cysteine residues. Thus, the cysteine residues in proteins could be intensively modified by various PTMs which regulated the functions of proteins dynamically, and an integrated data resource will be useful for the research community.

Here, we presented the database iCysMod (integrative database for protein cysteine modifications in eukaryotes), which provides the manually curated cysteine modification datasets in 48 eukaryotes from published literatures. In total, 85,747 modified sites in 31,483 proteins for 8 types are collected and integrated in the database. Various browse and search options are provided in the database, and the detailed information is organized and visualized for queries.