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Lipid-binding protein PIL1 YGR086C

fungal protein found in Saccharomyces cerevisiae S288c
Protein protein Q27548244
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Summary

Lipid-binding protein PIL1 YGR086C is a protein[1].

Key Facts

  • Lipid-binding protein PIL1 YGR086C's instance of is recorded as protein[2].
  • Lipid-binding protein PIL1 YGR086C's subclass of is recorded as protein[3].
  • Lipid-binding protein PIL1 YGR086C's UniProt protein ID is recorded as P53252[4].
  • Lipid-binding protein PIL1 YGR086C's part of is recorded as Eisosome component PIL1/LSP1[5].
  • Lipid-binding protein PIL1 YGR086C's part of is recorded as AH/BAR domain superfamily[6].
  • Lipid-binding protein PIL1 YGR086C's RefSeq protein ID is recorded as NP_011600[7].
  • Lipid-binding protein PIL1 YGR086C's molecular function is recorded as lipid binding[8].
  • Lipid-binding protein PIL1 YGR086C's molecular function is recorded as protein binding[9].
  • Lipid-binding protein PIL1 YGR086C's molecular function is recorded as lipid binding[10].
  • Lipid-binding protein PIL1 YGR086C's cell component is recorded as eisosome[11].
  • Lipid-binding protein PIL1 YGR086C's cell component is recorded as lipid droplet[12].
  • Lipid-binding protein PIL1 YGR086C's cell component is recorded as eisosome filament[13].
  • Lipid-binding protein PIL1 YGR086C's cell component is recorded as plasma membrane[14].
  • Lipid-binding protein PIL1 YGR086C's cell component is recorded as cytoplasm[15].
  • Lipid-binding protein PIL1 YGR086C's cell component is recorded as mitochondrion[16].
  • Lipid-binding protein PIL1 YGR086C's cell component is recorded as mitochondrial outer membrane[17].
  • Lipid-binding protein PIL1 YGR086C's cell component is recorded as plasma membrane[18].
  • Lipid-binding protein PIL1 YGR086C's cell component is recorded as cell periphery[19].
  • Lipid-binding protein PIL1 YGR086C's biological process is recorded as eisosome assembly[20].
  • Lipid-binding protein PIL1 YGR086C's biological process is recorded as endocytosis[21].
  • Lipid-binding protein PIL1 YGR086C's biological process is recorded as negative regulation of protein kinase activity[22].
  • Lipid-binding protein PIL1 YGR086C's biological process is recorded as response to heat[23].
  • Lipid-binding protein PIL1 YGR086C's biological process is recorded as protein localization[24].
  • Lipid-binding protein PIL1 YGR086C's biological process is recorded as protein localization to eisosome filament[25].
  • Lipid-binding protein PIL1 YGR086C's biological process is recorded as negative regulation of protein kinase activity[26].

References

Programmatic citations — every numbered marker resolves to a verifiable graph row below.

Direct Wikidata claims

  1. [2] ↑ . UniProt. Retrieved . wikidata.org.
  2. [3] ↑ . UniProt. Retrieved . wikidata.org.
  3. [4] ↑ . UniProt. 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] ↑ . Q20641742. Retrieved . wikidata.org.
  7. [8] ↑ . Eisosome proteins assemble into a membrane scaffold. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  8. [9] ↑ . Eisosomes mark static sites of endocytosis.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  9. [10] ↑ . Eisosome proteins assemble into a membrane scaffold. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  10. [11] ↑ . Eisosomes mark static sites of endocytosis.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [12] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. 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] ↑ . Global analysis of protein localization in budding yeast. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] ↑ . Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] ↑ . Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] ↑ . One library to make them all: streamlining the creation of yeast libraries via a SWAp-Tag strategy. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] ↑ . The sphingolipid long-chain base-Pkh1/2-Ypk1/2 signaling pathway regulates eisosome assembly and turnover. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] ↑ . Eisosomes mark static sites of endocytosis.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] ↑ . Pil1p and Lsp1p negatively regulate the 3-phosphoinositide-dependent protein kinase-like kinase Pkh1p and downstream signaling pathways Pkc1p and Ypk1p. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] ↑ . Pil1p and Lsp1p negatively regulate the 3-phosphoinositide-dependent protein kinase-like kinase Pkh1p and downstream signaling pathways Pkc1p and Ypk1p. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . Eisosomes mark static sites of endocytosis.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] ↑ . Evolutionarily conserved 5'-3' exoribonuclease Xrn1 accumulates at plasma membrane-associated eisosomes in post-diauxic yeast.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] ↑ . Pil1p and Lsp1p negatively regulate the 3-phosphoinositide-dependent protein kinase-like kinase Pkh1p and downstream signaling pathways Pkc1p and Ypk1p. 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). Lipid-binding protein PIL1 YGR086C. Retrieved May 3, 2026, from https://4ort.xyz/entity/lipid-binding-protein-pil1-ygr086c
MLA “Lipid-binding protein PIL1 YGR086C.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/lipid-binding-protein-pil1-ygr086c.
BibTeX @misc{4ortxyz_lipid-binding-protein-pil1-ygr086c_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Lipid-binding protein PIL1 YGR086C}}, year = {2026}, url = {https://4ort.xyz/entity/lipid-binding-protein-pil1-ygr086c}, note = {Accessed: 2026-05-03}}
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