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Lipid-binding protein HSP12 YFL014W

fungal protein found in Saccharomyces cerevisiae S288c
Protein protein Q27552196
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Summary

Lipid-binding protein HSP12 YFL014W is a protein[1].

Key Facts

  • Lipid-binding protein HSP12 YFL014W's instance of is recorded as protein[2].
  • Lipid-binding protein HSP12 YFL014W's subclass of is recorded as protein[3].
  • Lipid-binding protein HSP12 YFL014W's UniProt protein ID is recorded as P22943[4].
  • Lipid-binding protein HSP12 YFL014W's part of is recorded as Heat shock protein 9/12[5].
  • Lipid-binding protein HSP12 YFL014W's RefSeq protein ID is recorded as NP_116640[6].
  • Lipid-binding protein HSP12 YFL014W's molecular function is recorded as lipid binding[7].
  • Lipid-binding protein HSP12 YFL014W's molecular function is recorded as protein binding[8].
  • Lipid-binding protein HSP12 YFL014W's molecular function is recorded as lipid binding[9].
  • Lipid-binding protein HSP12 YFL014W's cell component is recorded as endosome[10].
  • Lipid-binding protein HSP12 YFL014W's cell component is recorded as plasma membrane[11].
  • Lipid-binding protein HSP12 YFL014W's cell component is recorded as cytosol[12].
  • Lipid-binding protein HSP12 YFL014W's cell component is recorded as cytosol[13].
  • Lipid-binding protein HSP12 YFL014W's cell component is recorded as plasma membrane[14].
  • Lipid-binding protein HSP12 YFL014W's cell component is recorded as nucleus[15].
  • Lipid-binding protein HSP12 YFL014W's cell component is recorded as cytoplasm[16].
  • Lipid-binding protein HSP12 YFL014W's cell component is recorded as plasma membrane[17].
  • Lipid-binding protein HSP12 YFL014W's biological process is recorded as response to stress[18].
  • Lipid-binding protein HSP12 YFL014W's biological process is recorded as cellular response to heat[19].
  • Lipid-binding protein HSP12 YFL014W's biological process is recorded as cellular response to oxidative stress[20].
  • Lipid-binding protein HSP12 YFL014W's biological process is recorded as cell adhesion[21].
  • Lipid-binding protein HSP12 YFL014W's biological process is recorded as cellular response to osmotic stress[22].
  • Lipid-binding protein HSP12 YFL014W's biological process is recorded as plasma membrane organization[23].
  • Lipid-binding protein HSP12 YFL014W's encoded by is recorded as HSP12[24].
  • Lipid-binding protein HSP12 YFL014W's found in taxon is recorded as Saccharomyces cerevisiae S288c[25].
  • Lipid-binding protein HSP12 YFL014W's Ensembl protein ID is recorded as YFL014W[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] ↑ . UniProt. Retrieved . wikidata.org.
  4. [5] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  5. [6] ↑ . Q20641742. Retrieved . wikidata.org.
  6. [7] ↑ . Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  7. [8] ↑ . Global landscape of protein complexes in the yeast Saccharomyces cerevisiae. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  8. [9] ↑ . Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  9. [10] ↑ . Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  10. [11] ↑ . Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [12] ↑ . Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] ↑ . Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [14] ↑ . The LEA-like protein HSP 12 in Saccharomyces cerevisiae has a plasma membrane location and protects membranes against desiccation and ethanol-induced stress. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] ↑ . Global analysis of protein localization in budding yeast. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] ↑ . Global analysis of protein localization in budding yeast. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] ↑ . Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] ↑ . Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] ↑ . Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] ↑ . HSP12 is essential for biofilm formation by a Sardinian wine strain of S. cerevisiae. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] ↑ . Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] ↑ . Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . UniProt. Retrieved . wikidata.org.
  24. [25] ↑ . UniProt. Retrieved . wikidata.org.
  25. [26] ↑ . ensembl Release 106. wikidata.org.

Class ancestry

  1. [1] ↑ . Wikidata. wikidata.org.

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APA 4ort.xyz Knowledge Graph. (2026). Lipid-binding protein HSP12 YFL014W. Retrieved May 3, 2026, from https://4ort.xyz/entity/lipid-binding-protein-hsp12-yfl014w
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BibTeX @misc{4ortxyz_lipid-binding-protein-hsp12-yfl014w_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Lipid-binding protein HSP12 YFL014W}}, year = {2026}, url = {https://4ort.xyz/entity/lipid-binding-protein-hsp12-yfl014w}, note = {Accessed: 2026-05-03}}
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