Calnexin

mammalian protein found in Rattus norvegicus
Protein protein Q28557226
Press Enter · cited answer in seconds

Calnexin

Summary

Calnexin is a protein[1].

Key Facts

  • Calnexin's instance of is recorded as protein[2].
  • Calnexin's UniProt protein ID is recorded as P35565[3].
  • Calnexin's part of is recorded as Calreticulin/calnexin[4].
  • Calnexin's part of is recorded as Calreticulin/calnexin, P domain superfamily[5].
  • Calnexin's part of is recorded as Concanavalin A-like lectin/glucanase domain superfamily[6].
  • Calnexin's part of is recorded as membrane protein[7].
  • Calnexin's part of is recorded as Calreticulin/calnexin, conserved site, protein family[8].
  • Calnexin's has part is recorded as Calreticulin/calnexin, conserved site[9].
  • Calnexin's RefSeq protein ID is recorded as NP_742005[10].
  • Calnexin's RefSeq protein ID is recorded as XP_008765901[11].
  • Calnexin's RefSeq protein ID is recorded as XP_008765902[12].
  • Calnexin's molecular function is recorded as calcium ion binding[13].
  • Calnexin's molecular function is recorded as protein binding[14].
  • Calnexin's molecular function is recorded as carbohydrate binding[15].
  • Calnexin's molecular function is recorded as apolipoprotein binding[16].
  • Calnexin's molecular function is recorded as ionotropic glutamate receptor binding[17].
  • Calnexin's molecular function is recorded as metal ion binding[18].
  • Calnexin's molecular function is recorded as unfolded protein binding[19].
  • Calnexin's cell component is recorded as cytoplasm[20].
  • Calnexin's cell component is recorded as endoplasmic reticulum[21].
  • Calnexin's cell component is recorded as endoplasmic reticulum membrane[22].
  • Calnexin's cell component is recorded as smooth endoplasmic reticulum[23].
  • Calnexin's cell component is recorded as rough endoplasmic reticulum[24].
  • Calnexin's cell component is recorded as ribosome[25].
  • Calnexin's cell component is recorded as membrane[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] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  9. [10] . Q20641742. Retrieved . wikidata.org.
  10. [11] . Q20641742. Retrieved . wikidata.org.
  11. [12] . Q20641742. Retrieved . wikidata.org.
  12. [13] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [14] . Biosynthesis of inositol trisphosphate receptors: selective association with the molecular chaperone calnexin. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] . Apolipoprotein[a] secretion from hepatoma cells is regulated in a size-dependent manner by alterations in disulfide bond formation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] . Calnexin and the immunoglobulin binding protein (BiP) coimmunoprecipitate with AMPA receptors. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] . Identification of novel proteins associated with both alpha-synuclein and DJ-1. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] . An interaction map of endoplasmic reticulum chaperones and foldases. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] . The endoplasmic reticulum of Purkinje neuron body and dendrites: molecular identity and specializations for Ca2+ transport. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] . Phosphorylation by CK2 and MAPK enhances calnexin association with ribosomes.. 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). Calnexin. Retrieved May 3, 2026, from https://4ort.xyz/entity/calnexin-q28557226
MLA “Calnexin.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/calnexin-q28557226.
BibTeX @misc{4ortxyz_calnexin-q28557226_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Calnexin}}, year = {2026}, url = {https://4ort.xyz/entity/calnexin-q28557226}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Calnexin — https://4ort.xyz/entity/calnexin-q28557226 (retrieved 2026-05-03)

Canonical URL: https://4ort.xyz/entity/calnexin-q28557226 · Last refreshed: