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Zim17p YNL310C

fungal protein found in Saccharomyces cerevisiae S288c
Protein protein Q27551753
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Zim17p YNL310C

Summary

Zim17p YNL310C is a protein[1].

Key Facts

  • Zim17p YNL310C's instance of is recorded as protein[2].
  • Zim17p YNL310C's UniProt protein ID is recorded as P42844[3].
  • Zim17p YNL310C's part of is recorded as Mitochondrial import protein TIM15[4].
  • Zim17p YNL310C's part of is recorded as membrane protein[5].
  • Zim17p YNL310C's part of is recorded as Zinc finger, DNL-type, protein family[6].
  • Zim17p YNL310C's has part is recorded as Zinc finger, DNL-type[7].
  • Zim17p YNL310C's RefSeq protein ID is recorded as NP_014089[8].
  • Zim17p YNL310C's molecular function is recorded as zinc ion binding[9].
  • Zim17p YNL310C's molecular function is recorded as metal ion binding[10].
  • Zim17p YNL310C's molecular function is recorded as chaperone binding[11].
  • Zim17p YNL310C's molecular function is recorded as protein binding[12].
  • Zim17p YNL310C's molecular function is recorded as chaperone binding[13].
  • Zim17p YNL310C's cell component is recorded as mitochondrial matrix[14].
  • Zim17p YNL310C's cell component is recorded as mitochondrial inner membrane[15].
  • Zim17p YNL310C's cell component is recorded as membrane[16].
  • Zim17p YNL310C's cell component is recorded as mitochondrion[17].
  • Zim17p YNL310C's cell component is recorded as mitochondrion[18].
  • Zim17p YNL310C's cell component is recorded as mitochondrion[19].
  • Zim17p YNL310C's biological process is recorded as protein transport[20].
  • Zim17p YNL310C's biological process is recorded as protein folding[21].
  • Zim17p YNL310C's biological process is recorded as response to unfolded protein[22].
  • Zim17p YNL310C's biological process is recorded as protein stabilization[23].
  • Zim17p YNL310C's biological process is recorded as protein import into mitochondrial matrix[24].
  • Zim17p YNL310C's biological process is recorded as mitochondrion organization[25].
  • Zim17p YNL310C's biological process is recorded as protein folding[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] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  4. [5] ↑ . wikidata.org.
  5. [6] ↑ . wikidata.org.
  6. [7] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  7. [8] ↑ . Q20641742. Retrieved . wikidata.org.
  8. [9] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  9. [10] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  10. [11] ↑ . Maintenance of structure and function of mitochondrial Hsp70 chaperones requires the chaperone Hep1.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [12] ↑ . Structural basis of functional cooperation of Tim15/Zim17 with yeast mitochondrial Hsp70. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] ↑ . Maintenance of structure and function of mitochondrial Hsp70 chaperones requires the chaperone Hep1.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [14] ↑ . Zim17, a novel zinc finger protein essential for protein import into mitochondria. 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] ↑ . 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] ↑ . Maintenance of structure and function of mitochondrial Hsp70 chaperones requires the chaperone Hep1.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] ↑ . Inactivation of the mitochondrial heat shock protein zim17 leads to aggregation of matrix hsp70s followed by pleiotropic effects on morphology and protein biogenesis.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] ↑ . The disaggregation activity of the mitochondrial ClpB homolog Hsp78 maintains Hsp70 function during heat stress. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . Zim17, a novel zinc finger protein essential for protein import into mitochondria. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] ↑ . Maintenance of structure and function of mitochondrial Hsp70 chaperones requires the chaperone Hep1.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] ↑ . Maintenance of structure and function of mitochondrial Hsp70 chaperones requires the chaperone Hep1.. 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). Zim17p YNL310C. Retrieved May 3, 2026, from https://4ort.xyz/entity/zim17p-ynl310c
MLA “Zim17p YNL310C.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/zim17p-ynl310c.
BibTeX @misc{4ortxyz_zim17p-ynl310c_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Zim17p YNL310C}}, year = {2026}, url = {https://4ort.xyz/entity/zim17p-ynl310c}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Zim17p YNL310C — https://4ort.xyz/entity/zim17p-ynl310c (retrieved 2026-05-03)

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