Sacsin molecular chaperone

mammalian protein found in Homo sapiens
Protein protein Q7397398
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Sacsin molecular chaperone

Summary

Sacsin molecular chaperone is a protein[1].

Key Facts

  • Sacsin molecular chaperone's instance of is recorded as protein[2].
  • Sacsin molecular chaperone's UniProt protein ID is recorded as Q9NZJ4[3].
  • Sacsin molecular chaperone's part of is recorded as Chaperone J-domain superfamily[4].
  • Sacsin molecular chaperone's part of is recorded as Ubiquitin-like domain superfamily[5].
  • Sacsin molecular chaperone's part of is recorded as Histidine kinase/HSP90-like ATPase superfamily[6].
  • Sacsin molecular chaperone's part of is recorded as HEPN domain, protein family[7].
  • Sacsin molecular chaperone's part of is recorded as DnaJ domain, protein family[8].
  • Sacsin molecular chaperone's part of is recorded as Ubiquitin-like domain, protein family[9].
  • Sacsin molecular chaperone's has part is recorded as Ubiquitin domain[10].
  • Sacsin molecular chaperone's has part is recorded as DnaJ domain[11].
  • Sacsin molecular chaperone's has part is recorded as HEPN domain[12].
  • Sacsin molecular chaperone's RefSeq protein ID is recorded as NP_001264984[13].
  • Sacsin molecular chaperone's RefSeq protein ID is recorded as NP_055178[14].
  • Sacsin molecular chaperone's RefSeq protein ID is recorded as XP_005266395[15].
  • Sacsin molecular chaperone's RefSeq protein ID is recorded as XP_011533341[16].
  • Sacsin molecular chaperone's RefSeq protein ID is recorded as XP_016876028[17].
  • Sacsin molecular chaperone's RefSeq protein ID is recorded as XP_024305105[18].
  • Sacsin molecular chaperone's PDB structure ID is recorded as 1IUR[19].
  • Sacsin molecular chaperone's PDB structure ID is recorded as 3O10[20].
  • Sacsin molecular chaperone's molecular function is recorded as Hsp70 protein binding[21].
  • Sacsin molecular chaperone's molecular function is recorded as proteasome binding[22].
  • Sacsin molecular chaperone's molecular function is recorded as chaperone binding[23].
  • Sacsin molecular chaperone's cell component is recorded as cytoplasm[24].
  • Sacsin molecular chaperone's cell component is recorded as axon[25].
  • Sacsin molecular chaperone's cell component is recorded as dendrite[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] . wikidata.org.
  8. [9] . wikidata.org.
  9. [10] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  10. [11] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  11. [12] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  12. [13] . Q20641742. Retrieved . wikidata.org.
  13. [14] . Q20641742. Retrieved . wikidata.org.
  14. [15] . Q20641742. Retrieved . wikidata.org.
  15. [16] . Q20641742. Retrieved . wikidata.org.
  16. [17] . Q20641742. Retrieved . wikidata.org.
  17. [18] . Q20641742. Retrieved . wikidata.org.
  18. [19] . Q905695. Retrieved . wikidata.org.
  19. [20] . Q905695. Retrieved . wikidata.org.
  20. [21] . The ataxia protein sacsin is a functional co-chaperone that protects against polyglutamine-expanded ataxin-1. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] . The ataxia protein sacsin is a functional co-chaperone that protects against polyglutamine-expanded ataxin-1. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] . The ataxia protein sacsin is a functional co-chaperone that protects against polyglutamine-expanded ataxin-1. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] . The ataxia protein sacsin is a functional co-chaperone that protects against polyglutamine-expanded ataxin-1. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] . The ataxia protein sacsin is a functional co-chaperone that protects against polyglutamine-expanded ataxin-1. 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). Sacsin molecular chaperone. Retrieved May 3, 2026, from https://4ort.xyz/entity/sacsin-molecular-chaperone-q7397398
MLA “Sacsin molecular chaperone.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/sacsin-molecular-chaperone-q7397398.
BibTeX @misc{4ortxyz_sacsin-molecular-chaperone-q7397398_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Sacsin molecular chaperone}}, year = {2026}, url = {https://4ort.xyz/entity/sacsin-molecular-chaperone-q7397398}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Sacsin molecular chaperone — https://4ort.xyz/entity/sacsin-molecular-chaperone-q7397398 (retrieved 2026-05-03)

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