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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Peroxiredoxin TSA2

UniprotKB/SwissProt ID: Q04120 (Q04120)

Gene Name: TSA2

Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events (PubMed:10681558, PubMed:11741925, PubMed:15210711). Can act alternatively as peroxidase and molecular chaperone. Oxidative stress and heat shock exposure cause a reversible shift of the protein structure from low MW species to high MW complexes, triggering a peroxidase-to-chaperone functional switch. The chaperone function of the protein enhances resistance to heat shock (PubMed:15163410)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR000866 AhpC/TSA
IPR050217 Peroxiredoxin
IPR024706 Peroxiredoxin_AhpC-typ
IPR019479 Peroxiredoxin_C
IPR036249 Thioredoxin-like_sf
IPR013766 Thioredoxin_domain