Tfs1p YLR178C

fungal protein found in Saccharomyces cerevisiae S288c
Protein protein Q27551036
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Tfs1p YLR178C

Summary

Tfs1p YLR178C is a protein[1].

Key Facts

  • Tfs1p YLR178C's instance of is recorded as protein[2].
  • Tfs1p YLR178C's subclass of is recorded as protein[3].
  • Tfs1p YLR178C's UniProt protein ID is recorded as P14306[4].
  • Tfs1p YLR178C's part of is recorded as Phosphatidylethanolamine-binding protein, eukaryotic[5].
  • Tfs1p YLR178C's part of is recorded as PEBP-like superfamily[6].
  • Tfs1p YLR178C's part of is recorded as Phosphatidylethanolamine-binding, conserved site, protein family[7].
  • Tfs1p YLR178C's has part is recorded as Phosphatidylethanolamine-binding, conserved site[8].
  • Tfs1p YLR178C's RefSeq protein ID is recorded as NP_013279[9].
  • Tfs1p YLR178C's molecular function is recorded as phospholipid binding[10].
  • Tfs1p YLR178C's molecular function is recorded as lipid binding[11].
  • Tfs1p YLR178C's molecular function is recorded as peptidase inhibitor activity[12].
  • Tfs1p YLR178C's molecular function is recorded as serine-type endopeptidase inhibitor activity[13].
  • Tfs1p YLR178C's molecular function is recorded as protein binding[14].
  • Tfs1p YLR178C's molecular function is recorded as phospholipid binding[15].
  • Tfs1p YLR178C's molecular function is recorded as peptidase inhibitor activity[16].
  • Tfs1p YLR178C's cell component is recorded as fungal-type vacuole membrane[17].
  • Tfs1p YLR178C's cell component is recorded as fungal-type vacuole lumen[18].
  • Tfs1p YLR178C's cell component is recorded as cytoplasm[19].
  • Tfs1p YLR178C's cell component is recorded as fungal-type vacuole lumen[20].
  • Tfs1p YLR178C's cell component is recorded as fungal-type vacuole membrane[21].
  • Tfs1p YLR178C's biological process is recorded as regulation of proteolysis[22].
  • Tfs1p YLR178C's biological process is recorded as negative regulation of peptidase activity[23].
  • Tfs1p YLR178C's biological process is recorded as regulation of Ras protein signal transduction[24].
  • Tfs1p YLR178C's biological process is recorded as negative regulation of endopeptidase activity[25].
  • Tfs1p YLR178C's biological process is recorded as regulation of Ras protein signal transduction[26].

References

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

Direct Wikidata claims

  1. [2] . Q905695. Retrieved . wikidata.org.
  2. [3] . Q20641742. Retrieved . wikidata.org.
  3. [4] . Q905695. Retrieved . wikidata.org.
  4. [5] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  5. [6] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  6. [7] . wikidata.org.
  7. [8] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  8. [9] . Q20641742. Retrieved . wikidata.org.
  9. [10] . Specific membrane binding of the carboxypeptidase Y inhibitor I(C), a phosphatidylethanolamine-binding protein family member. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  10. [11] . A High-Affinity Inhibitor of Yeast Carboxypeptidase Y Is Encoded by TFS1 and Shows Homology to a Family of Lipid Binding Proteins. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [12] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [14] . Global landscape of protein complexes in the yeast Saccharomyces cerevisiae. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] . Specific membrane binding of the carboxypeptidase Y inhibitor I(C), a phosphatidylethanolamine-binding protein family member. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] . Biochemical analysis of the yeast proteinase inhibitor (IC) homolog ICh and its comparison with IC.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] . Biochemical analysis of the yeast proteinase inhibitor (IC) homolog ICh and its comparison with IC.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] . Biochemical analysis of the yeast proteinase inhibitor (IC) homolog ICh and its comparison with IC.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] . Biochemical analysis of the yeast proteinase inhibitor (IC) homolog ICh and its comparison with IC.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] . A High-Affinity Inhibitor of Yeast Carboxypeptidase Y Is Encoded by TFS1 and Shows Homology to a Family of Lipid Binding Proteins. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] . Tfs1p, a member of the PEBP family, inhibits the Ira2p but not the Ira1p Ras GTPase-activating protein in Saccharomyces cerevisiae. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] . Tfs1p, a member of the PEBP family, inhibits the Ira2p but not the Ira1p Ras GTPase-activating protein in Saccharomyces cerevisiae. 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). Tfs1p YLR178C. Retrieved May 3, 2026, from https://4ort.xyz/entity/tfs1p-ylr178c
MLA “Tfs1p YLR178C.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/tfs1p-ylr178c.
BibTeX @misc{4ortxyz_tfs1p-ylr178c_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Tfs1p YLR178C}}, year = {2026}, url = {https://4ort.xyz/entity/tfs1p-ylr178c}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Tfs1p YLR178C — https://4ort.xyz/entity/tfs1p-ylr178c (retrieved 2026-05-03)

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