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Heat shock protein family A (Hsp70) member 1A

mammalian protein found in Homo sapiens
Protein protein Q21118347
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Heat shock protein family A (Hsp70) member 1A

Summary

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

Key Facts

  • Heat shock protein family A (Hsp70) member 1A's instance of is recorded as protein[2].
  • Heat shock protein family A (Hsp70) member 1A's UniProt protein ID is recorded as P0DMV9[3].
  • Heat shock protein family A (Hsp70) member 1A's part of is recorded as Heat shock protein 70kD, peptide-binding domain superfamily[4].
  • Heat shock protein family A (Hsp70) member 1A's part of is recorded as Heat shock protein 70kD, C-terminal domain superfamily[5].
  • Heat shock protein family A (Hsp70) member 1A's part of is recorded as Heat shock protein 70 family[6].
  • Heat shock protein family A (Hsp70) member 1A's part of is recorded as Heat shock protein 70, conserved site, protein family[7].
  • Heat shock protein family A (Hsp70) member 1A's has part is recorded as Heat shock protein 70, conserved site[8].
  • Heat shock protein family A (Hsp70) member 1A's RefSeq protein ID is recorded as NP_005336[9].
  • Heat shock protein family A (Hsp70) member 1A's PDB structure ID is recorded as 3D2E[10].
  • Heat shock protein family A (Hsp70) member 1A's molecular function is recorded as nucleotide binding[11].
  • Heat shock protein family A (Hsp70) member 1A's molecular function is recorded as heat shock protein binding[12].
  • Heat shock protein family A (Hsp70) member 1A's molecular function is recorded as virus receptor activity[13].
  • Heat shock protein family A (Hsp70) member 1A's molecular function is recorded as protein folding chaperone activity[14].
  • Heat shock protein family A (Hsp70) member 1A's molecular function is recorded as histone deacetylase binding[15].
  • Heat shock protein family A (Hsp70) member 1A's molecular function is recorded as C3HC4-type RING finger domain binding[16].
  • Heat shock protein family A (Hsp70) member 1A's molecular function is recorded as ATPase activity[17].
  • Heat shock protein family A (Hsp70) member 1A's molecular function is recorded as protein binding[18].
  • Heat shock protein family A (Hsp70) member 1A's molecular function is recorded as enzyme binding[19].
  • Heat shock protein family A (Hsp70) member 1A's molecular function is recorded as signaling receptor binding[20].
  • Heat shock protein family A (Hsp70) member 1A's molecular function is recorded as G protein-coupled receptor binding[21].
  • Heat shock protein family A (Hsp70) member 1A's molecular function is recorded as ATP binding[22].
  • Heat shock protein family A (Hsp70) member 1A's molecular function is recorded as ubiquitin protein ligase binding[23].
  • Heat shock protein family A (Hsp70) member 1A's molecular function is recorded as RNA binding[24].
  • Heat shock protein family A (Hsp70) member 1A's molecular function is recorded as protein N-terminus binding[25].
  • Heat shock protein family A (Hsp70) member 1A's molecular function is recorded as unfolded protein binding[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] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  8. [9] ↑ . Q20641742. Retrieved . wikidata.org.
  9. [10] ↑ . Q905695. Retrieved . wikidata.org.
  10. [11] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [12] ↑ . HDJC9, a novel human type C DnaJ/HSP40 member interacts with and cochaperones HSP70 through the J domain. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [14] ↑ . BAG5 inhibits parkin and enhances dopaminergic neuron degeneration. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] ↑ . Histone deacetylase 8 safeguards the human ever-shorter telomeres 1B (hEST1B) protein from ubiquitin-mediated degradation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] ↑ . RING finger protein RNF207, a novel regulator of cardiac excitation. 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] ↑ . ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] ↑ . Identification and Characterization of a Novel Human Methyltransferase Modulating Hsp70 Protein Function through Lysine Methylation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] ↑ . The Molecular Chaperone HSP70 Binds to and Stabilizes NOD2, an Important Protein Involved in Crohn Disease. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] ↑ . CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] ↑ . CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . The mRNA-Bound Proteome and Its Global Occupancy Profile on Protein-Coding Transcripts. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] ↑ . Inhibition of cellular proliferation by the Wilms tumor suppressor WT1 requires association with the inducible chaperone Hsp70. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] ↑ . Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis. 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 1A. Retrieved May 3, 2026, from https://4ort.xyz/entity/heat-shock-protein-family-a-hsp70-member-1a
MLA “Heat shock protein family A (Hsp70) member 1A.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/heat-shock-protein-family-a-hsp70-member-1a.
BibTeX @misc{4ortxyz_heat-shock-protein-family-a-hsp70-member-1a_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Heat shock protein family A (Hsp70) member 1A}}, year = {2026}, url = {https://4ort.xyz/entity/heat-shock-protein-family-a-hsp70-member-1a}, 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 1A — https://4ort.xyz/entity/heat-shock-protein-family-a-hsp70-member-1a (retrieved 2026-05-03)

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