Home › Entities › protein › Heat shock protein family E (Hsp10) member 1

Heat shock protein family E (Hsp10) member 1

mammalian protein found in Homo sapiens
Protein protein Q8965126
Press Enter · cited answer in seconds

Heat shock protein family E (Hsp10) member 1

Summary

Heat shock protein family E (Hsp10) member 1 is a protein[1].

Key Facts

  • Heat shock protein family E (Hsp10) member 1's instance of is recorded as protein[2].
  • Heat shock protein family E (Hsp10) member 1's UniProt protein ID is recorded as P61604[3].
  • Heat shock protein family E (Hsp10) member 1's part of is recorded as GroES chaperonin superfamily[4].
  • Heat shock protein family E (Hsp10) member 1's part of is recorded as GroES-like superfamily[5].
  • Heat shock protein family E (Hsp10) member 1's part of is recorded as GroES chaperonin family[6].
  • Heat shock protein family E (Hsp10) member 1's part of is recorded as Chaperonin GroES, conserved site, protein family[7].
  • Heat shock protein family E (Hsp10) member 1's MeSH descriptor ID is recorded as D018835[8].
  • Heat shock protein family E (Hsp10) member 1's has part is recorded as Chaperonin GroES, conserved site[9].
  • Heat shock protein family E (Hsp10) member 1's RefSeq protein ID is recorded as NP_002148[10].
  • Heat shock protein family E (Hsp10) member 1's PDB structure ID is recorded as 4PJ1[11].
  • Heat shock protein family E (Hsp10) member 1's MeSH tree code is recorded as D12.776.580.216.210.590.500[12].
  • Heat shock protein family E (Hsp10) member 1's molecular function is recorded as chaperone binding[13].
  • Heat shock protein family E (Hsp10) member 1's molecular function is recorded as protein binding[14].
  • Heat shock protein family E (Hsp10) member 1's molecular function is recorded as ATP binding[15].
  • Heat shock protein family E (Hsp10) member 1's molecular function is recorded as metal ion binding[16].
  • Heat shock protein family E (Hsp10) member 1's molecular function is recorded as unfolded protein binding[17].
  • Heat shock protein family E (Hsp10) member 1's molecular function is recorded as RNA binding[18].
  • Heat shock protein family E (Hsp10) member 1's molecular function is recorded as RNA binding[19].
  • Heat shock protein family E (Hsp10) member 1's molecular function is recorded as chaperone binding[20].
  • Heat shock protein family E (Hsp10) member 1's molecular function is recorded as chaperone binding[21].
  • Heat shock protein family E (Hsp10) member 1's cell component is recorded as cytoplasm[22].
  • Heat shock protein family E (Hsp10) member 1's cell component is recorded as extracellular exosome[23].
  • Heat shock protein family E (Hsp10) member 1's cell component is recorded as membrane[24].
  • Heat shock protein family E (Hsp10) member 1's cell component is recorded as mitochondrion[25].
  • Heat shock protein family E (Hsp10) member 1's cell component is recorded as mitochondrial matrix[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] ↑ . 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] ↑ . wikidata.org.
  8. [9] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  9. [10] ↑ . Q20641742. Retrieved . wikidata.org.
  10. [11] ↑ . Q905695. Retrieved . wikidata.org.
  11. [12] ↑ . wikidata.org.
  12. [13] ↑ . Expression in Escherichia coli, purification and functional activity of recombinant human chaperonin 10. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [14] ↑ . Menin interacts with the AP1 transcription factor JunD and represses JunD-activated transcription. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] ↑ . Genomic structure of the human mitochondrial chaperonin genes: HSP60 and HSP10 are localised head to head on chromosome 2 separated by a bidirectional promoter. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] ↑ . Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] ↑ . Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] ↑ . Expression in Escherichia coli, purification and functional activity of recombinant human chaperonin 10. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] ↑ . Expression in Escherichia coli, purification and functional activity of recombinant human chaperonin 10. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] ↑ . Proteomic analysis of podocyte exosome-enriched fraction from normal human urine. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . Differential expression profiling of membrane proteins by quantitative proteomics in a human mesenchymal stem cell line undergoing osteoblast differentiation. 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.

📑 Cite this page

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). Heat shock protein family E (Hsp10) member 1. Retrieved May 3, 2026, from https://4ort.xyz/entity/heat-shock-protein-family-e-hsp10-member-1
MLA “Heat shock protein family E (Hsp10) member 1.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/heat-shock-protein-family-e-hsp10-member-1.
BibTeX @misc{4ortxyz_heat-shock-protein-family-e-hsp10-member-1_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Heat shock protein family E (Hsp10) member 1}}, year = {2026}, url = {https://4ort.xyz/entity/heat-shock-protein-family-e-hsp10-member-1}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Heat shock protein family E (Hsp10) member 1 — https://4ort.xyz/entity/heat-shock-protein-family-e-hsp10-member-1 (retrieved 2026-05-03)

Canonical URL: https://4ort.xyz/entity/heat-shock-protein-family-e-hsp10-member-1 · Last refreshed: