Chaperone ATPase HSP60 YLR259C

fungal protein found in Saccharomyces cerevisiae S288c
Protein protein Q27548605
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Chaperone ATPase HSP60 YLR259C

Summary

Chaperone ATPase HSP60 YLR259C is a protein[1].

Key Facts

  • Chaperone ATPase HSP60 YLR259C's instance of is recorded as protein[2].
  • Chaperone ATPase HSP60 YLR259C's subclass of is recorded as protein[3].
  • Chaperone ATPase HSP60 YLR259C's UniProt protein ID is recorded as P19882[4].
  • Chaperone ATPase HSP60 YLR259C's part of is recorded as Chaperonin Cpn60[5].
  • Chaperone ATPase HSP60 YLR259C's part of is recorded as GroEL-like apical domain superfamily[6].
  • Chaperone ATPase HSP60 YLR259C's part of is recorded as GroEL-like equatorial domain superfamily[7].
  • Chaperone ATPase HSP60 YLR259C's part of is recorded as TCP-1-like chaperonin intermediate domain superfamily[8].
  • Chaperone ATPase HSP60 YLR259C's part of is recorded as Chaperonin Cpn60, conserved site, protein family[9].
  • Chaperone ATPase HSP60 YLR259C's has part is recorded as Chaperonin Cpn60, conserved site[10].
  • Chaperone ATPase HSP60 YLR259C's RefSeq protein ID is recorded as NP_013360[11].
  • Chaperone ATPase HSP60 YLR259C's molecular function is recorded as ATPase activity[12].
  • Chaperone ATPase HSP60 YLR259C's molecular function is recorded as ATP binding[13].
  • Chaperone ATPase HSP60 YLR259C's molecular function is recorded as DNA replication origin binding[14].
  • Chaperone ATPase HSP60 YLR259C's molecular function is recorded as unfolded protein binding[15].
  • Chaperone ATPase HSP60 YLR259C's molecular function is recorded as single-stranded DNA binding[16].
  • Chaperone ATPase HSP60 YLR259C's molecular function is recorded as nucleotide binding[17].
  • Chaperone ATPase HSP60 YLR259C's molecular function is recorded as chaperone binding[18].
  • Chaperone ATPase HSP60 YLR259C's molecular function is recorded as protein folding chaperone activity[19].
  • Chaperone ATPase HSP60 YLR259C's molecular function is recorded as protein binding[20].
  • Chaperone ATPase HSP60 YLR259C's molecular function is recorded as unfolded protein binding[21].
  • Chaperone ATPase HSP60 YLR259C's cell component is recorded as mitochondrion[22].
  • Chaperone ATPase HSP60 YLR259C's cell component is recorded as cytoplasm[23].
  • Chaperone ATPase HSP60 YLR259C's cell component is recorded as mitochondrial nucleoid[24].
  • Chaperone ATPase HSP60 YLR259C's cell component is recorded as mitochondrial inner membrane[25].
  • Chaperone ATPase HSP60 YLR259C's cell component is recorded as mitochondrial intermembrane space[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] . Q905695. 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] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  8. [9] . wikidata.org.
  9. [10] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  10. [11] . Q20641742. Retrieved . wikidata.org.
  11. [12] . Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [14] . In organello formaldehyde crosslinking of proteins to mtDNA: identification of bifunctional proteins. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] . Prevention of protein denaturation under heat stress by the chaperonin Hsp60. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] . In organello formaldehyde crosslinking of proteins to mtDNA: identification of bifunctional proteins. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] . Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] . Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] . Prevention of protein denaturation under heat stress by the chaperonin Hsp60. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] . In organello formaldehyde crosslinking of proteins to mtDNA: identification of bifunctional proteins. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] . GOA. 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). Chaperone ATPase HSP60 YLR259C. Retrieved May 3, 2026, from https://4ort.xyz/entity/chaperone-atpase-hsp60-ylr259c
MLA “Chaperone ATPase HSP60 YLR259C.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/chaperone-atpase-hsp60-ylr259c.
BibTeX @misc{4ortxyz_chaperone-atpase-hsp60-ylr259c_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Chaperone ATPase HSP60 YLR259C}}, year = {2026}, url = {https://4ort.xyz/entity/chaperone-atpase-hsp60-ylr259c}, note = {Accessed: 2026-05-03}}
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