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Hsp10p YOR020C

fungal protein found in Saccharomyces cerevisiae S288c
Protein protein Q27552194
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Hsp10p YOR020C

Summary

Hsp10p YOR020C is a protein[1].

Key Facts

  • Hsp10p YOR020C's instance of is recorded as protein[2].
  • Hsp10p YOR020C's subclass of is recorded as protein[3].
  • Hsp10p YOR020C's UniProt protein ID is recorded as P38910[4].
  • Hsp10p YOR020C's part of is recorded as GroES chaperonin superfamily[5].
  • Hsp10p YOR020C's part of is recorded as GroES-like superfamily[6].
  • Hsp10p YOR020C's part of is recorded as GroES chaperonin family[7].
  • Hsp10p YOR020C's part of is recorded as Chaperonin GroES, conserved site, protein family[8].
  • Hsp10p YOR020C's has part is recorded as Chaperonin GroES, conserved site[9].
  • Hsp10p YOR020C's RefSeq protein ID is recorded as NP_014663[10].
  • Hsp10p YOR020C's molecular function is recorded as ATP binding[11].
  • Hsp10p YOR020C's molecular function is recorded as unfolded protein binding[12].
  • Hsp10p YOR020C's molecular function is recorded as chaperone binding[13].
  • Hsp10p YOR020C's molecular function is recorded as metal ion binding[14].
  • Hsp10p YOR020C's molecular function is recorded as unfolded protein binding[15].
  • Hsp10p YOR020C's molecular function is recorded as chaperone binding[16].
  • Hsp10p YOR020C's cell component is recorded as mitochondrial matrix[17].
  • Hsp10p YOR020C's cell component is recorded as cytoplasm[18].
  • Hsp10p YOR020C's cell component is recorded as mitochondrion[19].
  • Hsp10p YOR020C's cell component is recorded as mitochondrial matrix[20].
  • Hsp10p YOR020C's cell component is recorded as mitochondrion[21].
  • Hsp10p YOR020C's biological process is recorded as protein refolding[22].
  • Hsp10p YOR020C's biological process is recorded as protein import into mitochondrial intermembrane space[23].
  • Hsp10p YOR020C's biological process is recorded as protein folding[24].
  • Hsp10p YOR020C's biological process is recorded as chaperone-mediated protein complex assembly[25].
  • Hsp10p YOR020C's biological process is recorded as response to unfolded protein[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] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  7. [8] ↑ . wikidata.org.
  8. [9] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  9. [10] ↑ . Q20641742. Retrieved . wikidata.org.
  10. [11] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [12] ↑ . Identification and functional analysis of chaperonin 10, the groES homolog from yeast mitochondria. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] ↑ . Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [14] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] ↑ . Identification and functional analysis of chaperonin 10, the groES homolog from yeast mitochondria. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] ↑ . Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] ↑ . GOA. 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] ↑ . Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] ↑ . Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondria. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] ↑ . Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondria. 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). Hsp10p YOR020C. Retrieved May 3, 2026, from https://4ort.xyz/entity/hsp10p-yor020c
MLA “Hsp10p YOR020C.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/hsp10p-yor020c.
BibTeX @misc{4ortxyz_hsp10p-yor020c_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Hsp10p YOR020C}}, year = {2026}, url = {https://4ort.xyz/entity/hsp10p-yor020c}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Hsp10p YOR020C — https://4ort.xyz/entity/hsp10p-yor020c (retrieved 2026-05-03)

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