Crystallin, alpha A

mammalian protein found in Mus musculus
Protein protein Q21173266
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Crystallin, alpha A

Summary

Crystallin, alpha An is a protein[1].

Key Facts

  • Crystallin, alpha A's instance of is recorded as protein[2].
  • Crystallin, alpha A's subclass of is recorded as protein[3].
  • Crystallin, alpha A's UniProt protein ID is recorded as P24622[4].
  • Crystallin, alpha A's part of is recorded as HSP20-like chaperone[5].
  • Crystallin, alpha A's part of is recorded as Alpha-crystallin, subunit A[6].
  • Crystallin, alpha A's part of is recorded as Alpha-crystallin, N-terminal domain, protein family[7].
  • Crystallin, alpha A's part of is recorded as Alpha crystallin/Hsp20 domain, protein family[8].
  • Crystallin, alpha A's has part is recorded as Alpha crystallin/Hsp20 domain[9].
  • Crystallin, alpha A's has part is recorded as Alpha-crystallin, N-terminal[10].
  • Crystallin, alpha A's RefSeq protein ID is recorded as NP_001265498[11].
  • Crystallin, alpha A's RefSeq protein ID is recorded as NP_001265499[12].
  • Crystallin, alpha A's RefSeq protein ID is recorded as NP_038529[13].
  • Crystallin, alpha A's molecular function is recorded as unfolded protein binding[14].
  • Crystallin, alpha A's molecular function is recorded as metal ion binding[15].
  • Crystallin, alpha A's molecular function is recorded as protein binding[16].
  • Crystallin, alpha A's molecular function is recorded as structural constituent of eye lens[17].
  • Crystallin, alpha A's molecular function is recorded as identical protein binding[18].
  • Crystallin, alpha A's cell component is recorded as cytoplasm[19].
  • Crystallin, alpha A's cell component is recorded as nucleus[20].
  • Crystallin, alpha A's cell component is recorded as nucleoplasm[21].
  • Crystallin, alpha A's cell component is recorded as cytosol[22].
  • Crystallin, alpha A's biological process is recorded as tubulin complex assembly[23].
  • Crystallin, alpha A's biological process is recorded as negative regulation of cysteine-type endopeptidase activity involved in apoptotic process[24].
  • Crystallin, alpha A's biological process is recorded as positive regulation of protein phosphorylation[25].
  • Crystallin, alpha A's biological process is recorded as response to hypoxia[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] . Q905695. Retrieved . 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] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  10. [11] . Q20641742. Retrieved . wikidata.org.
  11. [12] . Q20641742. Retrieved . wikidata.org.
  12. [13] . Q20641742. Retrieved . wikidata.org.
  13. [14] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] . Mechanism of small heat shock protein function in vivo: a knock-in mouse model demonstrates that the R49C mutation in alpha A-crystallin enhances protein insolubility and cell death. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] . Morphological characterization of the Alpha A- and Alpha B-crystallin double knockout mouse lens. 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] . GOA. 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] . Alpha-crystallin expression affects microtubule assembly and prevents their aggregation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] . Caspase-dependent secondary lens fiber cell disintegration in alphaA-/alphaB-crystallin double-knockout mice. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] . Mechanism of small heat shock protein function in vivo: a knock-in mouse model demonstrates that the R49C mutation in alpha A-crystallin enhances protein insolubility and cell death. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] . Exacerbation of retinal degeneration in the absence of alpha crystallins in an in vivo model of chemically induced hypoxia. Retrieved . ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

  1. [1] . 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). Crystallin, alpha A. Retrieved May 3, 2026, from https://4ort.xyz/entity/crystallin-alpha-a-q21173266
MLA “Crystallin, alpha A.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/crystallin-alpha-a-q21173266.
BibTeX @misc{4ortxyz_crystallin-alpha-a-q21173266_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Crystallin, alpha A}}, year = {2026}, url = {https://4ort.xyz/entity/crystallin-alpha-a-q21173266}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Crystallin, alpha A — https://4ort.xyz/entity/crystallin-alpha-a-q21173266 (retrieved 2026-05-03)

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