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Heat shock protein family A (Hsp70) member 5

mammalian protein found in Homo sapiens
Protein protein Q21116494
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Heat shock protein family A (Hsp70) member 5

Summary

Heat shock protein family A (Hsp70) member 5 is a protein[1].

Key Facts

  • Heat shock protein family A (Hsp70) member 5's instance of is recorded as protein[2].
  • Heat shock protein family A (Hsp70) member 5 is part of Heat shock protein 70kD, peptide-binding domain superfamily[3].
  • Heat shock protein family A (Hsp70) member 5 is part of Heat shock protein 70kD, C-terminal domain superfamily[4].
  • Heat shock protein family A (Hsp70) member 5 is part of Heat shock protein 70 family[5].
  • Heat shock protein family A (Hsp70) member 5 is part of Cation Channel-forming Heat Shock Protein-70[6].
  • Heat shock protein family A (Hsp70) member 5 is part of Heat shock protein 70, conserved site, protein family[7].
  • Heat shock protein family A (Hsp70) member 5 comprises Heat shock protein 70, conserved site[8].
  • Heat shock protein family A (Hsp70) member 5's molecular function is recorded as nucleotide binding[9].
  • Heat shock protein family A (Hsp70) member 5's molecular function is recorded as calcium ion binding[10].
  • Heat shock protein family A (Hsp70) member 5's molecular function is recorded as chaperone binding[11].
  • Heat shock protein family A (Hsp70) member 5's molecular function is recorded as protein domain specific binding[12].
  • Heat shock protein family A (Hsp70) member 5's molecular function is recorded as ribosome binding[13].
  • Heat shock protein family A (Hsp70) member 5's molecular function is recorded as misfolded protein binding[14].
  • Heat shock protein family A (Hsp70) member 5's molecular function is recorded as ATPase activity[15].
  • Heat shock protein family A (Hsp70) member 5's molecular function is recorded as protein binding[16].
  • Heat shock protein family A (Hsp70) member 5's molecular function is recorded as enzyme binding[17].
  • Heat shock protein family A (Hsp70) member 5's molecular function is recorded as ATP binding[18].
  • Heat shock protein family A (Hsp70) member 5's molecular function is recorded as ubiquitin protein ligase binding[19].
  • Heat shock protein family A (Hsp70) member 5's molecular function is recorded as unfolded protein binding[20].
  • Heat shock protein family A (Hsp70) member 5's molecular function is recorded as cadherin binding[21].
  • Heat shock protein family A (Hsp70) member 5's molecular function is recorded as ATP binding[22].
  • Heat shock protein family A (Hsp70) member 5's molecular function is recorded as hydrolase activity[23].
  • Heat shock protein family A (Hsp70) member 5's molecular function is recorded as ATPase activity[24].
  • Heat shock protein family A (Hsp70) member 5's molecular function is recorded as heat shock protein binding[25].
  • Heat shock protein family A (Hsp70) member 5's molecular function is recorded as protein folding chaperone activity[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] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: 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] ↑ . Retrieved . wikidata.org.
  6. [7] ↑ . wikidata.org.
  7. [8] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  8. [9] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  9. [10] ↑ . Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  10. [11] ↑ . Essential role of the unfolded protein response regulator GRP78/BiP in protection from neuronal apoptosis. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [12] ↑ . ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [14] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] ↑ . Role of the lectin VIP36 in post-ER quality control of human alpha1-antitrypsin. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] ↑ . Identification and Characterization of a Novel Human Methyltransferase Modulating Hsp70 Protein Function through Lysine Methylation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] ↑ . Calreticulin binds hYRNA and the 52-kDa polypeptide component of the Ro/SS-A ribonucleoprotein autoantigen. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] ↑ . Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] ↑ . E-cadherin interactome complexity and robustness resolved by quantitative proteomics. 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] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. 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). Heat shock protein family A (Hsp70) member 5. Retrieved May 3, 2026, from https://4ort.xyz/entity/heat-shock-protein-family-a-hsp70-member-5-q21116494
MLA “Heat shock protein family A (Hsp70) member 5.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/heat-shock-protein-family-a-hsp70-member-5-q21116494.
BibTeX @misc{4ortxyz_heat-shock-protein-family-a-hsp70-member-5-q21116494_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Heat shock protein family A (Hsp70) member 5}}, year = {2026}, url = {https://4ort.xyz/entity/heat-shock-protein-family-a-hsp70-member-5-q21116494}, 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 A (Hsp70) member 5 — https://4ort.xyz/entity/heat-shock-protein-family-a-hsp70-member-5-q21116494 (retrieved 2026-05-03)

Canonical URL: https://4ort.xyz/entity/heat-shock-protein-family-a-hsp70-member-5-q21116494 · Last refreshed:

Edit History

Rolling log of changes to this entity's Wikidata record. Values shown reflect the current state of each edited property — follow the history link to see the precise diff for any edit.

  1. 17d ago · Boghog · 2026-07-24 view diff on Wikidata ↗
    Found in taxon → Homo sapiens
    Mesh tree code → D12.776.580.216.375.100
    Wikidata description → mammalian protein found in Homo sapiens
    Pdb structure id → 3IUC, 3LDL, 3LDN +12
    + 15 other properties edited (see Wikidata diff for full list)
    "/* wbcreateclaim-create:1| */ [[Property:P591]]: 3.6.4.10, [[:toollabs:quickstatements/#/batch/261491|batch #261491]]"
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