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Tubulin-specific chaperone E

mammalian protein found in Mus musculus
Protein protein Q21992133
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Tubulin-specific chaperone E

Summary

Tubulin-specific chaperone E is a protein[1].

Key Facts

  • Tubulin-specific chaperone E's instance of is recorded as protein[2].
  • Tubulin-specific chaperone E's subclass of is recorded as protein[3].
  • Tubulin-specific chaperone E's UniProt protein ID is recorded as Q8CIV8[4].
  • Tubulin-specific chaperone E's part of is recorded as Leucine-rich repeat domain superfamily[5].
  • Tubulin-specific chaperone E's part of is recorded as Ubiquitin-like domain superfamily[6].
  • Tubulin-specific chaperone E's part of is recorded as CAP Gly-rich domain superfamily[7].
  • Tubulin-specific chaperone E's part of is recorded as CAP Gly-rich domain, protein family[8].
  • Tubulin-specific chaperone E's part of is recorded as Ubiquitin-like domain, protein family[9].
  • Tubulin-specific chaperone E's has part is recorded as Ubiquitin domain[10].
  • Tubulin-specific chaperone E's has part is recorded as CAP Gly-rich domain[11].
  • Tubulin-specific chaperone E's RefSeq protein ID is recorded as NP_848027[12].
  • Tubulin-specific chaperone E's RefSeq protein ID is recorded as XP_006516836[13].
  • Tubulin-specific chaperone E's RefSeq protein ID is recorded as XP_006516838[14].
  • Tubulin-specific chaperone E's RefSeq protein ID is recorded as XP_030103267[15].
  • Tubulin-specific chaperone E's RefSeq protein ID is recorded as XP_036014056[16].
  • Tubulin-specific chaperone E's PDB structure ID is recorded as 1WJN[17].
  • Tubulin-specific chaperone E's molecular function is recorded as unfolded protein binding[18].
  • Tubulin-specific chaperone E's molecular function is recorded as alpha-tubulin binding[19].
  • Tubulin-specific chaperone E's cell component is recorded as cytoplasm[20].
  • Tubulin-specific chaperone E's cell component is recorded as cytoskeleton[21].
  • Tubulin-specific chaperone E's cell component is recorded as cytoplasm[22].
  • Tubulin-specific chaperone E's biological process is recorded as tubulin complex assembly[23].
  • Tubulin-specific chaperone E's biological process is recorded as adult locomotory behavior[24].
  • Tubulin-specific chaperone E's biological process is recorded as peripheral nervous system neuron axonogenesis[25].
  • Tubulin-specific chaperone E's biological process is recorded as developmental growth[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] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: 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] ↑ . Q20641742. Retrieved . 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] ↑ . Q905695. Retrieved . wikidata.org.
  17. [18] ↑ . Missense mutation in the tubulin-specific chaperone E (Tbce) gene in the mouse mutant progressive motor neuronopathy, a model of human motoneuron disease. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. 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] ↑ . A missense mutation in Tbce causes progressive motor neuronopathy in mice. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . Bcl-2 overexpression prevents motoneuron cell body loss but not axonal degeneration in a mouse model of a neurodegenerative disease. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] ↑ . Bcl-2 overexpression prevents motoneuron cell body loss but not axonal degeneration in a mouse model of a neurodegenerative disease. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] ↑ . Bcl-2 overexpression prevents motoneuron cell body loss but not axonal degeneration in a mouse model of a neurodegenerative disease. 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). Tubulin-specific chaperone E. Retrieved May 3, 2026, from https://4ort.xyz/entity/tubulin-specific-chaperone-e
MLA “Tubulin-specific chaperone E.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/tubulin-specific-chaperone-e.
BibTeX @misc{4ortxyz_tubulin-specific-chaperone-e_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Tubulin-specific chaperone E}}, year = {2026}, url = {https://4ort.xyz/entity/tubulin-specific-chaperone-e}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Tubulin-specific chaperone E — https://4ort.xyz/entity/tubulin-specific-chaperone-e (retrieved 2026-05-03)

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