Vam7p YGL212W

fungal protein found in Saccharomyces cerevisiae S288c
Protein protein Q27552554
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Vam7p YGL212W

Summary

Vam7p YGL212W is a protein[1].

Key Facts

  • Vam7p YGL212W's instance of is recorded as protein[2].
  • Vam7p YGL212W's subclass of is recorded as protein[3].
  • Vam7p YGL212W's UniProt protein ID is recorded as P32912[4].
  • Vam7p YGL212W's part of is recorded as PX domain superfamily[5].
  • Vam7p YGL212W's part of is recorded as synaptosomal vesicle fusion pore[6].
  • Vam7p YGL212W's part of is recorded as Phox homologous domain, protein family[7].
  • Vam7p YGL212W's part of is recorded as Target SNARE coiled-coil homology domain, protein family[8].
  • Vam7p YGL212W's has part is recorded as Target SNARE coiled-coil homology domain[9].
  • Vam7p YGL212W's has part is recorded as Phox homologous domain[10].
  • Vam7p YGL212W's RefSeq protein ID is recorded as NP_011303[11].
  • Vam7p YGL212W's molecular function is recorded as phosphatidylinositol binding[12].
  • Vam7p YGL212W's molecular function is recorded as SNAP receptor activity[13].
  • Vam7p YGL212W's molecular function is recorded as SNARE binding[14].
  • Vam7p YGL212W's molecular function is recorded as protein binding[15].
  • Vam7p YGL212W's molecular function is recorded as phosphatidylinositol-3-phosphate binding[16].
  • Vam7p YGL212W's molecular function is recorded as SNAP receptor activity[17].
  • Vam7p YGL212W's cell component is recorded as vacuole[18].
  • Vam7p YGL212W's cell component is recorded as fungal-type vacuole membrane[19].
  • Vam7p YGL212W's cell component is recorded as integral component of membrane[20].
  • Vam7p YGL212W's cell component is recorded as SNARE complex[21].
  • Vam7p YGL212W's cell component is recorded as endomembrane system[22].
  • Vam7p YGL212W's cell component is recorded as phagophore assembly site[23].
  • Vam7p YGL212W's cell component is recorded as SNARE complex[24].
  • Vam7p YGL212W's cell component is recorded as fungal-type vacuole membrane[25].
  • Vam7p YGL212W's biological process is recorded as vesicle fusion[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] . Q20641742. Retrieved . wikidata.org.
  3. [4] . Q905695. Retrieved . wikidata.org.
  4. [5] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  5. [6] . Retrieved . 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] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] . A conserved domain is present in different families of vesicular fusion proteins: a new superfamily. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [14] . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] . The V-ATPase proteolipid cylinder promotes the lipid-mixing stage of SNARE-dependent fusion of yeast vacuoles.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] . The Central Polybasic Region of the Soluble SNARE (Soluble N-Ethylmaleimide-sensitive Factor Attachment Protein Receptor) Vam7 Affects Binding to Phosphatidylinositol 3-Phosphate by the PX (Phox Homology) Domain. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] . A conserved domain is present in different families of vesicular fusion proteins: a new superfamily. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] . Molecular mechanism of membrane docking by the Vam7p PX domain. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] . Vam7p, a vacuolar SNAP-25 homolog, is required for SNARE complex integrity and vacuole docking and fusion. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] . The Atg17-Atg31-Atg29 Complex Coordinates with Atg11 to Recruit the Vam7 SNARE and Mediate Autophagosome-Vacuole Fusion. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] . Vam7p, a vacuolar SNAP-25 homolog, is required for SNARE complex integrity and vacuole docking and fusion. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] . Molecular mechanism of membrane docking by the Vam7p PX domain. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] . Compartmental specificity of cellular membrane fusion encoded in SNARE proteins. 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). Vam7p YGL212W. Retrieved May 3, 2026, from https://4ort.xyz/entity/vam7p-ygl212w
MLA “Vam7p YGL212W.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/vam7p-ygl212w.
BibTeX @misc{4ortxyz_vam7p-ygl212w_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Vam7p YGL212W}}, year = {2026}, url = {https://4ort.xyz/entity/vam7p-ygl212w}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Vam7p YGL212W — https://4ort.xyz/entity/vam7p-ygl212w (retrieved 2026-05-03)

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