Heat shock protein 5

mammalian protein found in Mus musculus

Protein protein Q21495560

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Heat shock protein 5

Summary

Heat shock protein 5 is a protein^[1].

Key Facts

Heat shock protein 5's instance of is recorded as protein^[2].
Heat shock protein 5's UniProt protein ID is recorded as P20029^[3].
Heat shock protein 5's part of is recorded as Heat shock protein 70kD, peptide-binding domain superfamily^[4].
Heat shock protein 5's part of is recorded as Heat shock protein 70kD, C-terminal domain superfamily^[5].
Heat shock protein 5's part of is recorded as Heat shock protein 70 family^[6].
Heat shock protein 5's part of is recorded as membrane protein^[7].
Heat shock protein 5's part of is recorded as Heat shock protein 70, conserved site, protein family^[8].
Heat shock protein 5's has part is recorded as Heat shock protein 70, conserved site^[9].
Heat shock protein 5's RefSeq protein ID is recorded as NP_001156906^[10].
Heat shock protein 5's RefSeq protein ID is recorded as NP_071705^[11].
Heat shock protein 5's molecular function is recorded as nucleotide binding^[12].
Heat shock protein 5's molecular function is recorded as protein domain specific binding^[13].
Heat shock protein 5's molecular function is recorded as ribosome binding^[14].
Heat shock protein 5's molecular function is recorded as misfolded protein binding^[15].
Heat shock protein 5's molecular function is recorded as enzyme binding^[16].
Heat shock protein 5's molecular function is recorded as ATP binding^[17].
Heat shock protein 5's molecular function is recorded as ubiquitin protein ligase binding^[18].
Heat shock protein 5's molecular function is recorded as protein binding^[19].
Heat shock protein 5's molecular function is recorded as ATPase activity^[20].
Heat shock protein 5's molecular function is recorded as hydrolase activity^[21].
Heat shock protein 5's molecular function is recorded as cadherin binding^[22].
Heat shock protein 5's molecular function is recorded as unfolded protein binding^[23].
Heat shock protein 5's molecular function is recorded as ATP binding^[24].
Heat shock protein 5's molecular function is recorded as ATPase activity^[25].
Heat shock protein 5's molecular function is recorded as heat shock protein binding^[26].

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Quick Facts

Instance of protein

Part of Heat shock protein 70kD, peptide-binding domain superfamily, Heat shock protein 70kD, C-terminal domain superfamily, Heat shock protein 70 family, membrane protein, Heat shock protein 70, conserved site, protein family

Properties

Biological process cellular response to interleukin-4, cellular response to glucose starvation, positive regulation of cell migration, maintenance of protein localization in endoplasmic reticulum, negative regulation of apoptotic process, negative regulation of transforming growth factor beta receptor signaling pathway, toxin transport, response to endoplasmic reticulum stress, cerebellum structural organization, ER overload response, cerebellar Purkinje cell layer development, cellular response to antibiotic, proteolysis involved in cellular protein catabolic process, cellular response to manganese ion, positive regulation of embryonic development, positive regulation of protein ubiquitination, response to radiation, neuron differentiation, response to cocaine, neuron apoptotic process, cellular response to calcium ion, cellular response to cAMP, stress response to metal ion, response to methamphetamine hydrochloride, cellular response to nerve growth factor stimulus, cellular response to gamma radiation, negative regulation of protein homodimerization activity, negative regulation of IRE1-mediated unfolded protein response, positive regulation of neuron projection development, endoplasmic reticulum unfolded protein response, luteolysis, response to unfolded protein, ubiquitin-dependent ERAD pathway, endoplasmic reticulum unfolded protein response, cellular response to heat, Unfolded Protein Response, protein refolding, chaperone cofactor-dependent protein refolding, posttranslational protein targeting to membrane, translocation, posttranslational protein targeting to membrane, translocation

Cell component endoplasmic reticulum lumen, endoplasmic reticulum membrane, membrane, myelin sheath, plasma membrane, endoplasmic reticulum chaperone complex, extracellular region, cell surface, integral component of endoplasmic reticulum membrane, midbody, endoplasmic reticulum, COP9 signalosome, nucleus, endoplasmic reticulum-Golgi intermediate compartment, protein-containing complex, cytoplasm, mitochondrion, smooth endoplasmic reticulum, nucleus, cytoplasm, endoplasmic reticulum lumen, membrane, endoplasmic reticulum chaperone complex, mitochondrion, cytosol, intracellular membrane-bounded organelle, cytosol, myelin sheath, intracellular membrane-bounded organelle

Encoded by Hspa5

Found in taxon house mouse

Has part(s) Heat shock protein 70, conserved site

Imported from wholeness_audit_2026-05-02

Molecular function nucleotide binding, protein domain specific binding, ribosome binding, misfolded protein binding, enzyme binding, ATP binding, ubiquitin protein ligase binding, protein binding, ATPase activity, hydrolase activity, cadherin binding, unfolded protein binding, ATP binding, ATPase activity, heat shock protein binding, protein folding chaperone activity, unfolded protein binding, misfolded protein binding

External References (3)

Ensembl protein id ENSMUSP00000028222, ENSMUSP00000097747, ENSMUSP00000141966

Refseq protein id NP_001156906, NP_071705

Uniprot protein id P20029

References

Programmatic citations — every numbered marker resolves to a verifiable graph row below.

Direct Wikidata claims

[2] ↑ Heat shock protein 5 — instance of (P31): protein. Q905695. Retrieved 2022-05-25. wikidata.org.
[3] ↑ Heat shock protein 5 — UniProt protein ID (P352): P20029. Q905695. Retrieved 2022-05-25. wikidata.org.
[4] ↑ Heat shock protein 5 — part of (P361): Heat shock protein 70kD, peptide-binding domain superfamily. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[5] ↑ Heat shock protein 5 — part of (P361): Heat shock protein 70kD, C-terminal domain superfamily. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[6] ↑ Heat shock protein 5 — part of (P361): Heat shock protein 70 family. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[7] ↑ Heat shock protein 5 — part of (P361): membrane protein. wikidata.org.
[8] ↑ Heat shock protein 5 — part of (P361): Heat shock protein 70, conserved site, protein family. wikidata.org.
[9] ↑ Heat shock protein 5 — has part(s) (P527): Heat shock protein 70, conserved site. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[10] ↑ Heat shock protein 5 — RefSeq protein ID (P637): NP_001156906. Q20641742. Retrieved 2022-03-20. wikidata.org.
[11] ↑ Heat shock protein 5 — RefSeq protein ID (P637): NP_071705. Q20641742. Retrieved 2022-03-20. wikidata.org.
[12] ↑ Heat shock protein 5 — molecular function (P680): nucleotide binding. GOA. Retrieved 2019-02-14. ebi.ac.uk. Provenance: wikidata.org.
[13] ↑ Heat shock protein 5 — molecular function (P680): protein domain specific binding. GOA. Retrieved 2019-02-14. ebi.ac.uk. Provenance: wikidata.org.
[14] ↑ Heat shock protein 5 — molecular function (P680): ribosome binding. A novel type of co-chaperone mediates transmembrane recruitment of DnaK-like chaperones to ribosomes. Retrieved 2019-02-14. ebi.ac.uk. Provenance: wikidata.org.
[15] ↑ Heat shock protein 5 — molecular function (P680): misfolded protein binding. SDF2L1 interacts with the ER-associated degradation machinery and retards the degradation of mutant proinsulin in pancreatic β-cells. Retrieved 2018-06-05. ebi.ac.uk. Provenance: wikidata.org.
[16] ↑ Heat shock protein 5 — molecular function (P680): enzyme binding. GOA. Retrieved 2019-02-14. ebi.ac.uk. Provenance: wikidata.org.
[17] ↑ Heat shock protein 5 — molecular function (P680): ATP binding. GOA. Retrieved 2018-06-05. ebi.ac.uk. Provenance: wikidata.org.
[18] ↑ Heat shock protein 5 — molecular function (P680): ubiquitin protein ligase binding. GOA. Retrieved 2019-02-14. ebi.ac.uk. Provenance: wikidata.org.
[19] ↑ Heat shock protein 5 — molecular function (P680): protein binding. Identification and characterization of a novel endoplasmic reticulum (ER) DnaJ homologue, which stimulates ATPase activity of BiP in vitro and is induced by ER stress. Retrieved 2019-02-14. ebi.ac.uk. Provenance: wikidata.org.
[20] ↑ Heat shock protein 5 — molecular function (P680): ATPase activity. GOA. Retrieved 2018-06-05. ebi.ac.uk. Provenance: wikidata.org.
[21] ↑ Heat shock protein 5 — molecular function (P680): hydrolase activity. GOA. Retrieved 2019-02-14. ebi.ac.uk. Provenance: wikidata.org.
[22] ↑ Heat shock protein 5 — molecular function (P680): cadherin binding. GOA. Retrieved 2018-06-05. ebi.ac.uk. Provenance: wikidata.org.
[23] ↑ Heat shock protein 5 — molecular function (P680): unfolded protein binding. GOA. Retrieved 2018-06-05. ebi.ac.uk. Provenance: wikidata.org.
[24] ↑ Heat shock protein 5 — molecular function (P680): ATP binding. GOA. Retrieved 2019-02-14. ebi.ac.uk. Provenance: wikidata.org.
[25] ↑ Heat shock protein 5 — molecular function (P680): ATPase activity. GOA. Retrieved 2019-02-14. ebi.ac.uk. Provenance: wikidata.org.
[26] ↑ Heat shock protein 5 — molecular function (P680): heat shock protein binding. Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved 2019-02-14. ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

[1] ↑ Heat shock protein 5 is an instance of protein (Q8054) [P31, primary]. 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 5. Retrieved May 3, 2026, from https://4ort.xyz/entity/heat-shock-protein-5

MLA

“Heat shock protein 5.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/heat-shock-protein-5.

BibTeX

@misc{4ortxyz_heat-shock-protein-5_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Heat shock protein 5}}, year = {2026}, url = {https://4ort.xyz/entity/heat-shock-protein-5}, 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 5 — https://4ort.xyz/entity/heat-shock-protein-5 (retrieved 2026-05-03)

Canonical URL: https://4ort.xyz/entity/heat-shock-protein-5 · Last refreshed: May 3, 2026