Search Results
Overview
| Uniprot ID | P10599 |
|---|---|
| Protein Name | Thioredoxin |
| Gene Name | TXN |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 3 | *****MVKQIESKTA |
| 36 | ATWCGPCKMIKPFFH |
| 39 | CGPCKMIKPFFHSLS |
| 8 | MVKQIESKTAFQEAL |
| 85 | QFFKKGQKVGEFSGA |
| 94 | GEFSGANKEKLEATI |
| 96 | FSGANKEKLEATINE |
Function
Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (PubMed:17182577, PubMed:19032234, PubMed:2176490). 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 (PubMed:16408020, PubMed:17606900). 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 (PubMed:11118054, PubMed:9108029)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005576 | extracellular region |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0042803 | protein homodimerization activity |
| Molecular Function | GO:0047134 | protein-disulfide reductase [NAD(P)H] activity |
| Molecular Function | GO:0015035 | protein-disulfide reductase activity |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0004791 | thioredoxin-disulfide reductase (NADPH) activity |
| Biological Process | GO:0045454 | cell redox homeostasis |
| Biological Process | GO:0061692 | cellular detoxification of hydrogen peroxide |
| Biological Process | GO:0006351 | DNA-templated transcription |
| Biological Process | GO:0043388 | positive regulation of DNA binding |
| Biological Process | GO:0051897 | positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction |
| Biological Process | GO:0071731 | response to nitric oxide |
| Biological Process | GO:0009314 | response to radiation |
Reference
[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.
[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[3] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.
[4] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.
[5] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.