Nyv1p YLR093C

fungal protein found in Saccharomyces cerevisiae S288c
Protein protein Q27550832
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Nyv1p YLR093C

Summary

Nyv1p YLR093C is a protein[1].

Key Facts

  • Nyv1p YLR093C's instance of is recorded as protein[2].
  • Nyv1p YLR093C's UniProt protein ID is recorded as Template:Location map France[3].
  • Nyv1p YLR093C's part of is recorded as Nyv1, N-terminal domain superfamily[4].
  • Nyv1p YLR093C's part of is recorded as synaptosomal vesicle fusion pore[5].
  • Nyv1p YLR093C's part of is recorded as membrane protein[6].
  • Nyv1p YLR093C's RefSeq protein ID is recorded as NP_013194[7].
  • Nyv1p YLR093C's molecular function is recorded as SNARE binding[8].
  • Nyv1p YLR093C's molecular function is recorded as SNAP receptor activity[9].
  • Nyv1p YLR093C's molecular function is recorded as protein binding[10].
  • Nyv1p YLR093C's molecular function is recorded as SNAP receptor activity[11].
  • Nyv1p YLR093C's cell component is recorded as integral component of membrane[12].
  • Nyv1p YLR093C's cell component is recorded as SNARE complex[13].
  • Nyv1p YLR093C's cell component is recorded as vacuolar membrane[14].
  • Nyv1p YLR093C's cell component is recorded as membrane[15].
  • Nyv1p YLR093C's cell component is recorded as fungal-type vacuole membrane[16].
  • Nyv1p YLR093C's cell component is recorded as vacuole[17].
  • Nyv1p YLR093C's cell component is recorded as SNARE complex[18].
  • Nyv1p YLR093C's cell component is recorded as fungal-type vacuole membrane[19].
  • Nyv1p YLR093C's biological process is recorded as vesicle fusion[20].
  • Nyv1p YLR093C's biological process is recorded as vacuole fusion, non-autophagic[21].
  • Nyv1p YLR093C's biological process is recorded as vesicle-mediated transport[22].
  • Nyv1p YLR093C's biological process is recorded as exocytosis[23].
  • Nyv1p YLR093C's biological process is recorded as vesicle fusion[24].
  • Nyv1p YLR093C's encoded by is recorded as NYV1[25].
  • Nyv1p YLR093C's found in taxon is recorded as Saccharomyces cerevisiae S288c[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] . Retrieved . wikidata.org.
  5. [6] . wikidata.org.
  6. [7] . Q20641742. Retrieved . wikidata.org.
  7. [8] . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  8. [9] . Phosphoinositides and SNARE chaperones synergistically assemble and remodel SNARE complexes for membrane fusion. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  9. [10] . The SM protein Vps33 and the t-SNARE H(abc) domain promote fusion pore opening.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  10. [11] . Phosphoinositides and SNARE chaperones synergistically assemble and remodel SNARE complexes for membrane fusion. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [12] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] . A Vacuolar v–t-SNARE Complex, the Predominant Form In Vivo and on Isolated Vacuoles, Is Disassembled and Activated for Docking and Fusion. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [14] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] . Identification of the yeast R-SNARE Nyv1p as a novel longin domain-containing protein. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] . A Vacuolar v–t-SNARE Complex, the Predominant Form In Vivo and on Isolated Vacuoles, Is Disassembled and Activated for Docking and Fusion. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] . Identification of the yeast R-SNARE Nyv1p as a novel longin domain-containing protein. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] . Compartmental specificity of cellular membrane fusion encoded in SNARE proteins. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] . Stringent 3Q.1R composition of the SNARE 0-layer can be bypassed for fusion by compensatory SNARE mutation or by lipid bilayer modification.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] . The Vid Vesicle to Vacuole Trafficking Event Requires Components of the SNARE Membrane Fusion Machinery. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] . Compartmental specificity of cellular membrane fusion encoded in SNARE proteins. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] . Q905695. Retrieved . wikidata.org.
  25. [26] . Q905695. Retrieved . 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). Nyv1p YLR093C. Retrieved May 3, 2026, from https://4ort.xyz/entity/nyv1p-ylr093c
MLA “Nyv1p YLR093C.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/nyv1p-ylr093c.
BibTeX @misc{4ortxyz_nyv1p-ylr093c_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Nyv1p YLR093C}}, year = {2026}, url = {https://4ort.xyz/entity/nyv1p-ylr093c}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Nyv1p YLR093C — https://4ort.xyz/entity/nyv1p-ylr093c (retrieved 2026-05-03)

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