Heat shock protein 8

mammalian protein found in Mus musculus

Protein protein Q14888957

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Heat shock protein 8

Summary

Heat shock protein 8 is a protein^[1].

Key Facts

Heat shock protein 8's instance of is recorded as protein^[2].
Heat shock protein 8's UniProt protein ID is recorded as P63017^[3].
Heat shock protein 8's part of is recorded as Heat shock protein 70kD, peptide-binding domain superfamily^[4].
Heat shock protein 8's part of is recorded as Heat shock protein 70kD, C-terminal domain superfamily^[5].
Heat shock protein 8's part of is recorded as Heat shock protein 70 family^[6].
Heat shock protein 8's part of is recorded as membrane protein^[7].
Heat shock protein 8's part of is recorded as Heat shock protein 70, conserved site, protein family^[8].
Heat shock protein 8's has part is recorded as Heat shock protein 70, conserved site^[9].
Heat shock protein 8's RefSeq protein ID is recorded as NP_112442^[10].
Heat shock protein 8's RefSeq protein ID is recorded as NP_001351409^[11].
Heat shock protein 8's PDB structure ID is recorded as 3CQX^[12].
Heat shock protein 8's molecular function is recorded as C3HC4-type RING finger domain binding^[13].
Heat shock protein 8's molecular function is recorded as ATP binding^[14].
Heat shock protein 8's molecular function is recorded as heat shock protein binding^[15].
Heat shock protein 8's molecular function is recorded as phosphatidylserine binding^[16].
Heat shock protein 8's molecular function is recorded as ATPase activity^[17].
Heat shock protein 8's molecular function is recorded as enzyme binding^[18].
Heat shock protein 8's molecular function is recorded as unfolded protein binding^[19].
Heat shock protein 8's molecular function is recorded as protein binding^[20].
Heat shock protein 8's molecular function is recorded as nucleotide binding^[21].
Heat shock protein 8's molecular function is recorded as G protein-coupled receptor binding^[22].
Heat shock protein 8's molecular function is recorded as ubiquitin protein ligase binding^[23].
Heat shock protein 8's molecular function is recorded as RNA binding^[24].
Heat shock protein 8's molecular function is recorded as signaling receptor binding^[25].
Heat shock protein 8's molecular function is recorded as transcription factor 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 regulation of transcription, DNA-templated, regulation of protein stability, transcription, DNA-templated, RNA splicing, mRNA processing, ATP metabolic process, protein folding, protein refolding, negative regulation of transcription, DNA-templated, late endosomal microautophagy, positive regulation of mRNA splicing, via spliceosome, regulation of cell cycle, negative regulation of supramolecular fiber organization, chaperone cofactor-dependent protein refolding, positive regulation by host of viral genome replication, modulation by host of viral process, protein targeting to lysosome involved in chaperone-mediated autophagy, positive regulation of T cell mediated cytotoxicity, protein import into nucleus, positive regulation of gene expression, negative regulation of cardiac muscle cell apoptotic process, positive regulation of catalytic activity, positive regulation of proteolysis, protein autophosphorylation, positive regulation of phagocytosis, chaperone-mediated protein folding, regulation of protein complex stability, chaperone-mediated autophagy, clathrin coat disassembly, positive regulation of lysosomal membrane permeability, positive regulation of protein refolding, chaperone-mediated autophagy translocation complex disassembly, response to unfolded protein, axo-dendritic transport, vesicle-mediated transport, regulation of protein stability, cellular response to heat, Unfolded Protein Response, protein refolding, negative regulation of transcription, DNA-templated, ATP metabolic process, chaperone cofactor-dependent protein refolding, chaperone-mediated protein folding, late endosomal microautophagy, protein targeting to lysosome involved in chaperone-mediated autophagy, maintenance of postsynaptic specialization structure, regulation of postsynapse organization, negative regulation of supramolecular fiber organization, chaperone-mediated autophagy translocation complex disassembly, slow axonal transport, protein refolding, protein targeting to lysosome involved in chaperone-mediated autophagy

Cell component cytosol, melanosome, nucleus, myelin sheath, nucleolus, extracellular exosome, late endosome, ubiquitin ligase complex, plasma membrane, intracellular anatomical structure, spliceosomal complex, lysosomal matrix, Prp19 complex, lysosomal membrane, membrane, photoreceptor inner segment, cytoplasm, lysosome, autophagosome, microtubule, intermediate filament, synaptic vesicle, cell surface, postsynaptic density, axon, dendrite, asymmetric synapse, protein-containing complex, neuron projection, soma, terminal bouton, dendritic spine, dendritic shaft, perikaryon, neuron spine, membrane raft, perinuclear region of cytoplasm, presynaptic cytosol, postsynaptic cytosol, chaperone complex, messenger ribonucleoprotein complex, ribonucleoprotein complex, ubiquitin ligase complex, Prp19 complex, nucleus, cytoplasm, lysosome, autophagosome, cytosol, plasma membrane, axon, dendrite, terminal bouton, myelin sheath, perinuclear region of cytoplasm, extracellular exosome, photoreceptor ribbon synapse, glycinergic synapse, presynapse, postsynapse, glutamatergic synapse, presynaptic cytosol, postsynaptic cytosol, postsynaptic specialization membrane, chaperone complex, ribonucleoprotein complex, cytosol

Encoded by Hspa8

Found in taxon house mouse

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

Imported from wholeness_audit_2026-05-02

Molecular function C3HC4-type RING finger domain binding, ATP binding, heat shock protein binding, phosphatidylserine binding, ATPase activity, enzyme binding, unfolded protein binding, protein binding, nucleotide binding, G protein-coupled receptor binding, ubiquitin protein ligase binding, RNA binding, signaling receptor binding, transcription factor binding, protein-macromolecule adaptor activity, A1 adenosine receptor binding, peptide binding, ADP binding, cadherin binding, chaperone binding, prostaglandin binding, clathrin-uncoating ATPase activity, G protein-coupled receptor binding, ATP binding, ATPase activity, enzyme binding, protein-macromolecule adaptor activity, heat shock protein binding, ubiquitin protein ligase binding, protein folding chaperone activity, unfolded protein binding, chaperone binding, misfolded protein binding, C3HC4-type RING finger domain binding, clathrin-uncoating ATPase activity, ATPase activity, heat shock protein binding, unfolded protein binding

External References (4)

Ensembl protein id ENSMUSP00000015800, ENSMUSP00000113722, ENSMUSP00000117285

Pdb structure id 3CQX

Refseq protein id NP_112442, NP_001351409

Uniprot protein id P63017

References

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

Direct Wikidata claims

[2] ↑ Heat shock protein 8 — instance of (P31): protein. Q905695. Retrieved 2022-05-25. wikidata.org.
[3] ↑ Heat shock protein 8 — UniProt protein ID (P352): P63017. Q905695. Retrieved 2022-05-25. wikidata.org.
[4] ↑ Heat shock protein 8 — 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 8 — 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 8 — part of (P361): Heat shock protein 70 family. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[7] ↑ Heat shock protein 8 — part of (P361): membrane protein. wikidata.org.
[8] ↑ Heat shock protein 8 — part of (P361): Heat shock protein 70, conserved site, protein family. wikidata.org.
[9] ↑ Heat shock protein 8 — has part(s) (P527): Heat shock protein 70, conserved site. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[10] ↑ Heat shock protein 8 — RefSeq protein ID (P637): NP_112442. Q20641742. Retrieved 2022-03-20. wikidata.org.
[11] ↑ Heat shock protein 8 — RefSeq protein ID (P637): NP_001351409. Q20641742. Retrieved 2022-03-20. wikidata.org.
[12] ↑ Heat shock protein 8 — PDB structure ID (P638): 3CQX. Q905695. Retrieved 2016-08-09. wikidata.org.
[13] ↑ Heat shock protein 8 — molecular function (P680): C3HC4-type RING finger domain binding. GOA. Retrieved 2019-05-09. ebi.ac.uk. Provenance: wikidata.org.
[14] ↑ Heat shock protein 8 — molecular function (P680): ATP binding. GOA. Retrieved 2018-04-24. ebi.ac.uk. Provenance: wikidata.org.
[15] ↑ Heat shock protein 8 — molecular function (P680): heat shock protein binding. GOA. Retrieved 2018-04-24. ebi.ac.uk. Provenance: wikidata.org.
[16] ↑ Heat shock protein 8 — molecular function (P680): phosphatidylserine binding. Microautophagy of cytosolic proteins by late endosomes. Retrieved 2019-05-09. ebi.ac.uk. Provenance: wikidata.org.
[17] ↑ Heat shock protein 8 — molecular function (P680): ATPase activity. GOA. Retrieved 2018-04-24. ebi.ac.uk. Provenance: wikidata.org.
[18] ↑ Heat shock protein 8 — molecular function (P680): enzyme binding. GOA. Retrieved 2019-05-09. ebi.ac.uk. Provenance: wikidata.org.
[19] ↑ Heat shock protein 8 — molecular function (P680): unfolded protein binding. GOA. Retrieved 2018-04-24. ebi.ac.uk. Provenance: wikidata.org.
[20] ↑ Heat shock protein 8 — molecular function (P680): protein binding. Chaperone-assisted selective autophagy is essential for muscle maintenance. Retrieved 2019-05-09. ebi.ac.uk. Provenance: wikidata.org.
[21] ↑ Heat shock protein 8 — molecular function (P680): nucleotide binding. GOA. Retrieved 2019-05-09. ebi.ac.uk. Provenance: wikidata.org.
[22] ↑ Heat shock protein 8 — molecular function (P680): G protein-coupled receptor binding. GOA. Retrieved 2019-05-09. ebi.ac.uk. Provenance: wikidata.org.
[23] ↑ Heat shock protein 8 — molecular function (P680): ubiquitin protein ligase binding. GOA. Retrieved 2019-05-09. ebi.ac.uk. Provenance: wikidata.org.
[24] ↑ Heat shock protein 8 — molecular function (P680): RNA binding. GOA. Retrieved 2019-05-09. ebi.ac.uk. Provenance: wikidata.org.
[25] ↑ Heat shock protein 8 — molecular function (P680): signaling receptor binding. GOA. Retrieved 2019-05-09. ebi.ac.uk. Provenance: wikidata.org.
[26] ↑ Heat shock protein 8 — molecular function (P680): transcription factor binding. GOA. Retrieved 2019-05-09. ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

[1] ↑ Heat shock protein 8 is an instance of protein (Q8054) [P31, primary]. Wikidata. wikidata.org.

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APA

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MLA

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BibTeX

@misc{4ortxyz_heat-shock-protein-8_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Heat shock protein 8}}, year = {2026}, url = {https://4ort.xyz/entity/heat-shock-protein-8}, 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 8 — https://4ort.xyz/entity/heat-shock-protein-8 (retrieved 2026-05-03)

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