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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: Thioredoxin-1

UniprotKB/SwissProt ID: P22217 (P22217)

Gene Name: TRX1

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

Function: Participates as a hydrogen donor in redox reactions through the reversible oxidation of its active center dithiol to a disulfide, accompanied by the transfer of 2 electrons and 2 protons. It is involved in many cellular processes, including deoxyribonucleotide synthesis, repair of oxidatively damaged proteins, protein folding, sulfur metabolism, and redox homeostasis. Thioredoxin-dependent enzymes include phosphoadenosine-phosphosulfate reductase MET16, alkyl-hydroperoxide reductase DOT5, thioredoxin peroxidases TSA1 and TSA2, alkyl hydroperoxide reductase AHP1, and peroxiredoxin HYR1. Thioredoxin is also involved in protection against reducing stress. As part of the LMA1 complex, it is involved in the facilitation of vesicle fusion such as homotypic vacuole and ER-derived COPII vesicle fusion with the Golgi. This activity does not require the redox mechanism

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Nucleus. Cytoplasm. Golgi apparatus membrane. Mitochondrion intermembrane space

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR005746 Thioredoxin
IPR036249 Thioredoxin-like_sf
IPR017937 Thioredoxin_CS
IPR013766 Thioredoxin_domain