Serine C-palmitoyltransferase LCB1 YMR296C

fungal protein found in Saccharomyces cerevisiae S288c
Protein protein Q27552599
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Serine C-palmitoyltransferase LCB1 YMR296C

Summary

Serine C-palmitoyltransferase LCB1 YMR296C is a protein[1].

Key Facts

  • Serine C-palmitoyltransferase LCB1 YMR296C's instance of is recorded as protein[2].
  • Serine C-palmitoyltransferase LCB1 YMR296C's UniProt protein ID is recorded as P25045[3].
  • Serine C-palmitoyltransferase LCB1 YMR296C's part of is recorded as Pyridoxal phosphate-dependent transferase, major domain[4].
  • Serine C-palmitoyltransferase LCB1 YMR296C's part of is recorded as Pyridoxal phosphate-dependent transferase domain 1[5].
  • Serine C-palmitoyltransferase LCB1 YMR296C's part of is recorded as Pyridoxal phosphate-dependent transferase[6].
  • Serine C-palmitoyltransferase LCB1 YMR296C's part of is recorded as membrane protein[7].
  • Serine C-palmitoyltransferase LCB1 YMR296C's part of is recorded as Aminotransferase, class I/classII, protein family[8].
  • Serine C-palmitoyltransferase LCB1 YMR296C's has part is recorded as Aminotransferase, class I/classII[9].
  • Serine C-palmitoyltransferase LCB1 YMR296C's RefSeq protein ID is recorded as NP_014025[10].
  • Serine C-palmitoyltransferase LCB1 YMR296C's molecular function is recorded as serine C-palmitoyltransferase activity[11].
  • Serine C-palmitoyltransferase LCB1 YMR296C's molecular function is recorded as transferase activity[12].
  • Serine C-palmitoyltransferase LCB1 YMR296C's molecular function is recorded as catalytic activity[13].
  • Serine C-palmitoyltransferase LCB1 YMR296C's molecular function is recorded as acyltransferase activity[14].
  • Serine C-palmitoyltransferase LCB1 YMR296C's molecular function is recorded as pyridoxal phosphate binding[15].
  • Serine C-palmitoyltransferase LCB1 YMR296C's molecular function is recorded as protein binding[16].
  • Serine C-palmitoyltransferase LCB1 YMR296C's cell component is recorded as integral component of membrane[17].
  • Serine C-palmitoyltransferase LCB1 YMR296C's cell component is recorded as cytoplasm[18].
  • Serine C-palmitoyltransferase LCB1 YMR296C's cell component is recorded as membrane[19].
  • Serine C-palmitoyltransferase LCB1 YMR296C's cell component is recorded as serine C-palmitoyltransferase complex[20].
  • Serine C-palmitoyltransferase LCB1 YMR296C's cell component is recorded as endoplasmic reticulum membrane[21].
  • Serine C-palmitoyltransferase LCB1 YMR296C's cell component is recorded as SPOTS complex[22].
  • Serine C-palmitoyltransferase LCB1 YMR296C's cell component is recorded as endoplasmic reticulum[23].
  • Serine C-palmitoyltransferase LCB1 YMR296C's cell component is recorded as endoplasmic reticulum[24].
  • Serine C-palmitoyltransferase LCB1 YMR296C's biological process is recorded as biosynthesis[25].
  • Serine C-palmitoyltransferase LCB1 YMR296C's biological process is recorded as lipid metabolism[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] . wikidata.org.
  8. [9] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  9. [10] . Q20641742. Retrieved . wikidata.org.
  10. [11] . Characterization of enzymatic synthesis of sphingolipid long-chain bases in Saccharomyces cerevisiae: mutant strains exhibiting long-chain-base auxotrophy are deficient in serine palmitoyltransferase activity. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [12] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] . GOA. 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] . Proteome survey reveals modularity of the yeast cell machinery. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] . GOA. 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] . Characterization of enzymatic synthesis of sphingolipid long-chain bases in Saccharomyces cerevisiae: mutant strains exhibiting long-chain-base auxotrophy are deficient in serine palmitoyltransferase activity. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] . Orm family proteins mediate sphingolipid homeostasis. 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] . GOA. 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). Serine C-palmitoyltransferase LCB1 YMR296C. Retrieved May 3, 2026, from https://4ort.xyz/entity/serine-c-palmitoyltransferase-lcb1-ymr296c
MLA “Serine C-palmitoyltransferase LCB1 YMR296C.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/serine-c-palmitoyltransferase-lcb1-ymr296c.
BibTeX @misc{4ortxyz_serine-c-palmitoyltransferase-lcb1-ymr296c_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Serine C-palmitoyltransferase LCB1 YMR296C}}, year = {2026}, url = {https://4ort.xyz/entity/serine-c-palmitoyltransferase-lcb1-ymr296c}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Serine C-palmitoyltransferase LCB1 YMR296C — https://4ort.xyz/entity/serine-c-palmitoyltransferase-lcb1-ymr296c (retrieved 2026-05-03)

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