Unc-119 lipid binding chaperone

mammalian protein found in Homo sapiens
Protein protein Q21112623
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Unc-119 lipid binding chaperone

Summary

Unc-119 lipid binding chaperone is a protein[1].

Key Facts

  • Unc-119 lipid binding chaperone's instance of is recorded as protein[2].
  • Unc-119 lipid binding chaperone's UniProt protein ID is recorded as Juià[3].
  • Unc-119 lipid binding chaperone's part of is recorded as GMP phosphodiesterase, delta subunit superfamily[4].
  • Unc-119 lipid binding chaperone's part of is recorded as Protein unc-119 homologue A-like[5].
  • Unc-119 lipid binding chaperone's part of is recorded as Immunoglobulin E-set[6].
  • Unc-119 lipid binding chaperone's part of is recorded as GMP phosphodiesterase, delta subunit, protein family[7].
  • Unc-119 lipid binding chaperone's has part is recorded as GMP phosphodiesterase, delta subunit[8].
  • Unc-119 lipid binding chaperone's RefSeq protein ID is recorded as NP_001317095[9].
  • Unc-119 lipid binding chaperone's RefSeq protein ID is recorded as NP_005139[10].
  • Unc-119 lipid binding chaperone's RefSeq protein ID is recorded as NP_473376[11].
  • Unc-119 lipid binding chaperone's RefSeq protein ID is recorded as XP_011523761[12].
  • Unc-119 lipid binding chaperone's PDB structure ID is recorded as 3GQQ[13].
  • Unc-119 lipid binding chaperone's PDB structure ID is recorded as 3RBQ[14].
  • Unc-119 lipid binding chaperone's PDB structure ID is recorded as 4GOJ[15].
  • Unc-119 lipid binding chaperone's PDB structure ID is recorded as 4GOK[16].
  • Unc-119 lipid binding chaperone's molecular function is recorded as lipid binding[17].
  • Unc-119 lipid binding chaperone's molecular function is recorded as protein binding[18].
  • Unc-119 lipid binding chaperone's molecular function is recorded as lipid binding[19].
  • Unc-119 lipid binding chaperone's cell component is recorded as cytoplasm[20].
  • Unc-119 lipid binding chaperone's cell component is recorded as cytosol[21].
  • Unc-119 lipid binding chaperone's cell component is recorded as centrosome[22].
  • Unc-119 lipid binding chaperone's cell component is recorded as spindle pole[23].
  • Unc-119 lipid binding chaperone's cell component is recorded as spindle[24].
  • Unc-119 lipid binding chaperone's cell component is recorded as microtubule organizing center[25].
  • Unc-119 lipid binding chaperone's cell component is recorded as intercellular bridge[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] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  8. [9] . Q20641742. Retrieved . wikidata.org.
  9. [10] . Q20641742. Retrieved . wikidata.org.
  10. [11] . Q20641742. Retrieved . wikidata.org.
  11. [12] . Q20641742. Retrieved . wikidata.org.
  12. [13] . Q905695. Retrieved . wikidata.org.
  13. [14] . Q905695. Retrieved . wikidata.org.
  14. [15] . Q905695. Retrieved . wikidata.org.
  15. [16] . Q905695. Retrieved . wikidata.org.
  16. [17] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] . Unc119, a novel activator of Lck/Fyn, is essential for T cell activation. 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] . Localization of HRG4, a photoreceptor protein homologous to Unc-119, in ribbon synapse. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] . An ARL3-UNC119-RP2 GTPase cycle targets myristoylated NPHP3 to the primary cilium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] . UNC119a bridges the transmission of Fyn signals to Rab11, leading to the completion of cytokinesis. 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). Unc-119 lipid binding chaperone. Retrieved May 3, 2026, from https://4ort.xyz/entity/unc-119-lipid-binding-chaperone
MLA “Unc-119 lipid binding chaperone.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/unc-119-lipid-binding-chaperone.
BibTeX @misc{4ortxyz_unc-119-lipid-binding-chaperone_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Unc-119 lipid binding chaperone}}, year = {2026}, url = {https://4ort.xyz/entity/unc-119-lipid-binding-chaperone}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Unc-119 lipid binding chaperone — https://4ort.xyz/entity/unc-119-lipid-binding-chaperone (retrieved 2026-05-03)

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