Reduces disulfide protein thioredoxin (Trx) to its dithiol-containing form (PubMed:8577704). Homodimeric flavoprotein involved in the regulation of cellular redox reactions, growth and differentiation. A selenocysteine residue at the C-terminal active site is essential for catalysis (Probable).
Also has reductase activity on hydrogen peroxide (H2O2) (PubMed:10849437)
Homodimer (PubMed:17512005, PubMed:8577704). Interacts with HERC5
Interacts with ESR1 and ESR2
Expressed predominantly in Leydig cells (at protein level). Also expressed in ovary, spleen, heart, liver, kidney and pancreas and in a number of cancer cell lines
Widely expressed with highest levels in kidney, testis, uterus, ovary, prostate, placenta and fetal liver
The N-terminal glutaredoxin domain does not contain the C-P-Y-C redox-active motif normally found in glutaredoxins and has been found to be inactive in classical glutaredoxin assays
Click a pathway to open the interactive Reactome viewer.
Genes with an experimentally identified or computationally predicted synthetic-lethal relationship to TXNRD1, aggregated across our SSL data sources. Click any partner node to view that gene’s page.
Nodes and edges are coloured by the SSL data source. Partners appearing in more than one source are shown in grey.
No clinical trials information available.