Thioredoxin TRX1 YLR043C

fungal protein found in Saccharomyces cerevisiae S288c
Protein protein Q27547493
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Summary

Thioredoxin TRX1 YLR043C is a protein[1].

Key Facts

  • Thioredoxin TRX1 YLR043C's instance of is recorded as protein[2].
  • Thioredoxin TRX1 YLR043C's UniProt protein ID is recorded as P22217[3].
  • Thioredoxin TRX1 YLR043C's part of is recorded as Thioredoxin-like superfamily[4].
  • Thioredoxin TRX1 YLR043C's part of is recorded as thioredoxins[5].
  • Thioredoxin TRX1 YLR043C's part of is recorded as membrane protein[6].
  • Thioredoxin TRX1 YLR043C's part of is recorded as Thioredoxin domain, protein family[7].
  • Thioredoxin TRX1 YLR043C's part of is recorded as Thioredoxin, conserved site, protein family[8].
  • Thioredoxin TRX1 YLR043C's has part is recorded as Thioredoxin domain[9].
  • Thioredoxin TRX1 YLR043C's has part is recorded as Thioredoxin, conserved site[10].
  • Thioredoxin TRX1 YLR043C's RefSeq protein ID is recorded as NP_013144[11].
  • Thioredoxin TRX1 YLR043C's molecular function is recorded as protein-disulfide reductase activity[12].
  • Thioredoxin TRX1 YLR043C's molecular function is recorded as disulfide oxidoreductase activity[13].
  • Thioredoxin TRX1 YLR043C's molecular function is recorded as oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor[14].
  • Thioredoxin TRX1 YLR043C's molecular function is recorded as thioredoxin-disulfide reductase activity[15].
  • Thioredoxin TRX1 YLR043C's molecular function is recorded as protein-disulfide reductase (NAD(P)) activity[16].
  • Thioredoxin TRX1 YLR043C's molecular function is recorded as protein binding[17].
  • Thioredoxin TRX1 YLR043C's molecular function is recorded as protein-disulfide reductase activity[18].
  • Thioredoxin TRX1 YLR043C's molecular function is recorded as disulfide oxidoreductase activity[19].
  • Thioredoxin TRX1 YLR043C's cell component is recorded as Golgi membrane[20].
  • Thioredoxin TRX1 YLR043C's cell component is recorded as Golgi apparatus[21].
  • Thioredoxin TRX1 YLR043C's cell component is recorded as fungal-type vacuole[22].
  • Thioredoxin TRX1 YLR043C's cell component is recorded as mitochondrial intermembrane space[23].
  • Thioredoxin TRX1 YLR043C's cell component is recorded as membrane[24].
  • Thioredoxin TRX1 YLR043C's cell component is recorded as cytosol[25].
  • Thioredoxin TRX1 YLR043C's cell component is recorded as nucleus[26].

References

Programmatic citations — every numbered marker resolves to a verifiable graph row below.

Direct Wikidata claims

  1. [2] ↑ . UniProt. Retrieved . wikidata.org.
  2. [3] ↑ . UniProt. Retrieved . wikidata.org.
  3. [4] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  4. [5] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  5. [6] ↑ . wikidata.org.
  6. [7] ↑ . wikidata.org.
  7. [8] ↑ . wikidata.org.
  8. [9] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  9. [10] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  10. [11] ↑ . Q20641742. Retrieved . wikidata.org.
  11. [12] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] ↑ . Yeast thioredoxin genes.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [14] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] ↑ . An inter-species protein-protein interaction network across vast evolutionary distance. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] ↑ . Structural and kinetic analysis of Saccharomyces cerevisiae thioredoxin Trx1: implications for the catalytic mechanism of GSSG reduced by the thioredoxin system. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] ↑ . LMA1 Binds to Vacuoles at Sec18p (NSF), Transfers upon ATP Hydrolysis to a t-SNARE (Vam3p) Complex, and Is Released during Fusion. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] ↑ . Thioredoxin is required for vacuole inheritance in Saccharomyces cerevisiae. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

  1. [1] ↑ . Wikidata. wikidata.org.

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Use these citations when quoting this entity in research, articles, AI prompts, or wherever provenance matters. We aggregate Wikidata + Wikipedia + authoritative open-data sources; the stitched, scored, cross-referenced view is what 4ort.xyz contributes.

APA 4ort.xyz Knowledge Graph. (2026). Thioredoxin TRX1 YLR043C. Retrieved May 3, 2026, from https://4ort.xyz/entity/thioredoxin-trx1-ylr043c
MLA “Thioredoxin TRX1 YLR043C.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/thioredoxin-trx1-ylr043c.
BibTeX @misc{4ortxyz_thioredoxin-trx1-ylr043c_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Thioredoxin TRX1 YLR043C}}, year = {2026}, url = {https://4ort.xyz/entity/thioredoxin-trx1-ylr043c}, note = {Accessed: 2026-05-03}}
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