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, 35 (22), 4849-4850

MetOSite: An Integrated Resource for the Study of Methionine Residues Sulfoxidation

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MetOSite: An Integrated Resource for the Study of Methionine Residues Sulfoxidation

Héctor Valverde et al. Bioinformatics.

Abstract

Motivation: The oxidation of protein-bound methionine to form methionine sulfoxide has traditionally been regarded as an oxidative damage. However, growing evidences support the view of this reversible reaction also as a regulatory post-translational modification. Thus, the oxidation of methionine residues has been reported to have multiple and varied implications for protein function. However, despite the importance of this modification and the abundance of reports, all these data are scattered in the literature. No database/resource on methionine sulfoxidation exists currently. Since this information is useful to gain further insights into the redox regulation of cellular proteins, we have created a primary database of experimentally confirmed sulfoxidation sites.

Results: MetOSite currently contains 7242 methionine sulfoxide sites found in 3562 different proteins from 23 species, with Homo sapiens, Arabidopsis thaliana and Bacillus cereus as the main contributors. Each collected site has been classified according to the effect of its sulfoxidation on the biological properties of the modified protein. Thus, MetOSite documents cases where the sulfoxidation of methionine leads to (i) gain of activity, (ii) loss of activity, (iii) increased protein-protein interaction susceptibility, (iv) decreased protein-protein interaction susceptibility, (v) changes in protein stability and (vi) changes in subcellular location.

Availability and implementation: MetOSite is available at https://metosite.uma.es.

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