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Heat shock protein family A (Hsp70) member 1B

mammalian protein found in Rattus norvegicus
Protein protein Q55193706
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Heat shock protein family A (Hsp70) member 1B

Summary

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

Key Facts

  • Heat shock protein family A (Hsp70) member 1B's instance of is recorded as protein[2].
  • Heat shock protein family A (Hsp70) member 1B's UniProt protein ID is recorded as P0DMW1[3].
  • Heat shock protein family A (Hsp70) member 1B's part of is recorded as Heat shock protein 70 family[4].
  • Heat shock protein family A (Hsp70) member 1B's part of is recorded as Heat shock protein 70kD, peptide-binding domain superfamily[5].
  • Heat shock protein family A (Hsp70) member 1B's part of is recorded as Heat shock protein 70kD, C-terminal domain superfamily[6].
  • Heat shock protein family A (Hsp70) member 1B's part of is recorded as Heat shock protein 70, conserved site, protein family[7].
  • Heat shock protein family A (Hsp70) member 1B's has part is recorded as Heat shock protein 70, conserved site[8].
  • Heat shock protein family A (Hsp70) member 1B's RefSeq protein ID is recorded as NP_001316825[9].
  • Heat shock protein family A (Hsp70) member 1B's molecular function is recorded as nucleotide binding[10].
  • Heat shock protein family A (Hsp70) member 1B's molecular function is recorded as protease binding[11].
  • Heat shock protein family A (Hsp70) member 1B's molecular function is recorded as protein binding[12].
  • Heat shock protein family A (Hsp70) member 1B's molecular function is recorded as ATP binding[13].
  • Heat shock protein family A (Hsp70) member 1B's molecular function is recorded as ATPase activity[14].
  • Heat shock protein family A (Hsp70) member 1B's molecular function is recorded as heat shock protein binding[15].
  • Heat shock protein family A (Hsp70) member 1B's molecular function is recorded as ubiquitin protein ligase binding[16].
  • Heat shock protein family A (Hsp70) member 1B's molecular function is recorded as protein folding chaperone activity[17].
  • Heat shock protein family A (Hsp70) member 1B's molecular function is recorded as NF-kappaB binding[18].
  • Heat shock protein family A (Hsp70) member 1B's molecular function is recorded as unfolded protein binding[19].
  • Heat shock protein family A (Hsp70) member 1B's molecular function is recorded as misfolded protein binding[20].
  • Heat shock protein family A (Hsp70) member 1B's cell component is recorded as nucleus[21].
  • Heat shock protein family A (Hsp70) member 1B's cell component is recorded as cytoplasm[22].
  • Heat shock protein family A (Hsp70) member 1B's cell component is recorded as centrosome[23].
  • Heat shock protein family A (Hsp70) member 1B's cell component is recorded as microtubule organizing center[24].
  • Heat shock protein family A (Hsp70) member 1B's cell component is recorded as cytosol[25].
  • Heat shock protein family A (Hsp70) member 1B's cell component is recorded as cytoskeleton[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] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  10. [11] ↑ . Reduction of caspase-8 and -9 cleavage is associated with increased c-FLIP and increased binding of Apaf-1 and Hsp70 after neonatal hypoxic/ischemic injury in mice overexpressing Hsp70. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [12] ↑ . Inhibition of cellular proliferation by the Wilms tumor suppressor WT1 requires association with the inducible chaperone Hsp70. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [14] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. 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] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] ↑ . In vivo heat shock protein assembles with septic liver NF-kappaB/I-kappaB complex regulating NF-kappaB activity. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] ↑ . Intracellular localization of constitutive and inducible heat shock protein 70 in rat liver after in vivo heat stress. 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] ↑ . In vivo heat shock protein assembles with septic liver NF-kappaB/I-kappaB complex regulating NF-kappaB activity. 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 A (Hsp70) member 1B. Retrieved May 3, 2026, from https://4ort.xyz/entity/heat-shock-protein-family-a-hsp70-member-1b-q55193706
MLA “Heat shock protein family A (Hsp70) member 1B.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/heat-shock-protein-family-a-hsp70-member-1b-q55193706.
BibTeX @misc{4ortxyz_heat-shock-protein-family-a-hsp70-member-1b-q55193706_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Heat shock protein family A (Hsp70) member 1B}}, year = {2026}, url = {https://4ort.xyz/entity/heat-shock-protein-family-a-hsp70-member-1b-q55193706}, 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 1B — https://4ort.xyz/entity/heat-shock-protein-family-a-hsp70-member-1b-q55193706 (retrieved 2026-05-03)

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