Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity. Homodimer; disulfide-linked. Interacts with TXNIP through the redox-active site. Interacts with MAP3K5 and CASP3. In case of infection, interacts with S.typhimurium protein slrP. Interacts with APEX1; the interaction stimulates the FOS/JUN AP-1 DNA- binding activity in a redox-dependent manner. Up-regulated by ionizing radiation. Belongs to the thioredoxin family. Note: This description may include information from UniProtKB.
Molecular Function: protein binding; electron carrier activity; protein disulfide oxidoreductase activity; peptide disulfide oxidoreductase activity
Biological Process: negative regulation of protein export from nucleus; transcription, DNA-dependent; nucleobase, nucleoside and nucleotide metabolic process; nucleobase, nucleoside and nucleotide interconversion; negative regulation of transcription from RNA polymerase II promoter; signal transduction; glycerol ether metabolic process; cell proliferation; response to radiation; cell-cell signaling; cell redox homeostasis; innate immune response; regulation of protein import into nucleus, translocation; cell motility; positive regulation of DNA binding
SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.