Harmonizome 3.0

From GeneRIF Biological Term Annotations

genes co-occuring with the biological term thioredoxin in literature-supported statements describing functions of genes from the GeneRIF Biological Term Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Thioredoxin protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of thioredoxin peroxidase activity by peptidyl-threonine phosphorylation biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the thioredoxin peroxidase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the thioredoxin-disulfide reductase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From HumanCyc Pathways

proteins participating in the thioredoxin pathway pathway from the HumanCyc Pathways dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Phosducin, thioredoxin-like domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Thioredoxin/glutathione reductase selenoprotein protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Thioredoxin-like fold protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the DSBA-like thioredoxin domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Thioredoxin domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the mRNA splicing factor, thioredoxin-like U5 snRNP protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Thioredoxin, conserved site protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Protein of unknown function DUF953, thioredoxin-like protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From GO Biological Process Annotations 2023

genes participating in the negative regulation of thioredoxin peroxidase activity by peptidyl-threonine phosphorylation biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the thioredoxin peroxidase activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the thioredoxin-dependent peroxiredoxin activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the L-methionine:thioredoxin-disulfide S-oxidoreductase activity molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Biological Process Annotations 2025

genes participating in the negative regulation of thioredoxin peroxidase activity by peptidyl-threonine phosphorylation biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the thioredoxin peroxidase activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the thioredoxin-dependent peroxiredoxin activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the L-methionine:thioredoxin-disulfide S-oxidoreductase activity molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the thioredoxin-disulfide reductase complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the ferredoxin-thioredoxin reductase complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.