Phospholipase D YKR031C

fungal protein found in Saccharomyces cerevisiae S288c
Protein protein Q27547260
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Phospholipase D YKR031C

Summary

Phospholipase D YKR031C is a protein[1].

Key Facts

  • Phospholipase D YKR031C's instance of is recorded as protein[2].
  • Phospholipase D YKR031C's subclass of is recorded as protein[3].
  • Phospholipase D YKR031C's UniProt protein ID is recorded as P36126[4].
  • Phospholipase D YKR031C's part of is recorded as PX domain superfamily[5].
  • Phospholipase D YKR031C's part of is recorded as Phospholipase D, eukaryotic type[6].
  • Phospholipase D YKR031C's part of is recorded as pleckstrin homology domain, protein family[7].
  • Phospholipase D YKR031C's part of is recorded as Phox homologous domain, protein family[8].
  • Phospholipase D YKR031C's part of is recorded as Phospholipase D/Transphosphatidylase family[9].
  • Phospholipase D YKR031C's has part is recorded as pleckstrin homology domain[10].
  • Phospholipase D YKR031C's has part is recorded as Phox homologous domain[11].
  • Phospholipase D YKR031C's has part is recorded as Phospholipase D/Transphosphatidylase[12].
  • Phospholipase D YKR031C's RefSeq protein ID is recorded as NP_012956[13].
  • Phospholipase D YKR031C's molecular function is recorded as catalytic activity[14].
  • Phospholipase D YKR031C's molecular function is recorded as phospholipase D activity[15].
  • Phospholipase D YKR031C's molecular function is recorded as N-acylphosphatidylethanolamine-specific phospholipase D activity[16].
  • Phospholipase D YKR031C's molecular function is recorded as phosphatidylinositol-3-phosphate binding[17].
  • Phospholipase D YKR031C's molecular function is recorded as hydrolase activity[18].
  • Phospholipase D YKR031C's molecular function is recorded as phosphatidylinositol binding[19].
  • Phospholipase D YKR031C's cell component is recorded as prospore membrane[20].
  • Phospholipase D YKR031C's cell component is recorded as endosome[21].
  • Phospholipase D YKR031C's cell component is recorded as nucleus[22].
  • Phospholipase D YKR031C's biological process is recorded as sporulation resulting in formation of a cellular spore[23].
  • Phospholipase D YKR031C's biological process is recorded as exocytosis[24].
  • Phospholipase D YKR031C's biological process is recorded as meiosis[25].
  • Phospholipase D YKR031C's biological process is recorded as cell morphogenesis involved in conjugation with cellular 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] . 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] . 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] . InterPro Release 71.0. ebi.ac.uk. Provenance: 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] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] . All phox homology (PX) domains from Saccharomyces cerevisiae specifically recognize phosphatidylinositol 3-phosphate.. 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] . ADP-Ribosylation Factors Do Not Activate Yeast Phospholipase Ds but Are Required for Sporulation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] . Identification of a novel family of nonclassic yeast phosphatidylinositol transfer proteins whose function modulates phospholipase D activity and Sec14p-independent cell growth. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] . The conserved foot domain of RNA pol II associates with proteins involved in transcriptional initiation and/or early elongation.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] . SPO14 separation-of-function mutations define unique roles for phospholipase D in secretion and cellular differentiation in Saccharomyces cerevisiae. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] . Phospholipase D1 is required for efficient mating projection formation in Saccharomyces cerevisiae. 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). Phospholipase D YKR031C. Retrieved May 3, 2026, from https://4ort.xyz/entity/phospholipase-d-ykr031c
MLA “Phospholipase D YKR031C.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/phospholipase-d-ykr031c.
BibTeX @misc{4ortxyz_phospholipase-d-ykr031c_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Phospholipase D YKR031C}}, year = {2026}, url = {https://4ort.xyz/entity/phospholipase-d-ykr031c}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Phospholipase D YKR031C — https://4ort.xyz/entity/phospholipase-d-ykr031c (retrieved 2026-05-03)

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