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Ditrans,polycis-polyprenyl diphosphate synthase YDL193W

fungal protein found in Saccharomyces cerevisiae S288c
Protein protein Q27551454
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Summary

Ditrans,polycis-polyprenyl diphosphate synthase YDL193W is a protein[1].

Key Facts

  • Ditrans,polycis-polyprenyl diphosphate synthase YDL193W's instance of is recorded as protein[2].
  • Ditrans,polycis-polyprenyl diphosphate synthase YDL193W's UniProt protein ID is recorded as Zoridae[3].
  • Ditrans,polycis-polyprenyl diphosphate synthase YDL193W's part of is recorded as Dehydrodolichyl diphosphate synthase complex subunit Nus1[4].
  • Ditrans,polycis-polyprenyl diphosphate synthase YDL193W's part of is recorded as membrane protein[5].
  • Ditrans,polycis-polyprenyl diphosphate synthase YDL193W's RefSeq protein ID is recorded as NP_010088[6].
  • Ditrans,polycis-polyprenyl diphosphate synthase YDL193W's molecular function is recorded as transferase activity[7].
  • Ditrans,polycis-polyprenyl diphosphate synthase YDL193W's molecular function is recorded as dehydrodolichyl diphosphate synthase activity[8].
  • Ditrans,polycis-polyprenyl diphosphate synthase YDL193W's molecular function is recorded as transferase activity, transferring alkyl or aryl (other than methyl) groups[9].
  • Ditrans,polycis-polyprenyl diphosphate synthase YDL193W's molecular function is recorded as protein binding[10].
  • Ditrans,polycis-polyprenyl diphosphate synthase YDL193W's cell component is recorded as integral component of membrane[11].
  • Ditrans,polycis-polyprenyl diphosphate synthase YDL193W's cell component is recorded as nucleus[12].
  • Ditrans,polycis-polyprenyl diphosphate synthase YDL193W's cell component is recorded as lipid droplet[13].
  • Ditrans,polycis-polyprenyl diphosphate synthase YDL193W's cell component is recorded as dehydrodolichyl diphosphate synthase complex[14].
  • Ditrans,polycis-polyprenyl diphosphate synthase YDL193W's cell component is recorded as nuclear membrane[15].
  • Ditrans,polycis-polyprenyl diphosphate synthase YDL193W's cell component is recorded as membrane[16].
  • Ditrans,polycis-polyprenyl diphosphate synthase YDL193W's cell component is recorded as endoplasmic reticulum membrane[17].
  • Ditrans,polycis-polyprenyl diphosphate synthase YDL193W's cell component is recorded as endoplasmic reticulum[18].
  • Ditrans,polycis-polyprenyl diphosphate synthase YDL193W's cell component is recorded as dehydrodolichyl diphosphate synthase complex[19].
  • Ditrans,polycis-polyprenyl diphosphate synthase YDL193W's cell component is recorded as nuclear envelope[20].
  • Ditrans,polycis-polyprenyl diphosphate synthase YDL193W's cell component is recorded as lipid droplet[21].
  • Ditrans,polycis-polyprenyl diphosphate synthase YDL193W's biological process is recorded as protein glycosylation[22].
  • Ditrans,polycis-polyprenyl diphosphate synthase YDL193W's biological process is recorded as dolichol biosynthetic process[23].
  • Ditrans,polycis-polyprenyl diphosphate synthase YDL193W's biological process is recorded as dolichol biosynthetic process[24].
  • Ditrans,polycis-polyprenyl diphosphate synthase YDL193W's encoded by is recorded as NUS1[25].
  • Ditrans,polycis-polyprenyl diphosphate synthase YDL193W'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] ↑ . UniProt. Retrieved . wikidata.org.
  2. [3] ↑ . UniProt. Retrieved . wikidata.org.
  3. [4] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  4. [5] ↑ . wikidata.org.
  5. [6] ↑ . Q20641742. Retrieved . wikidata.org.
  6. [7] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  7. [8] ↑ . Mutation of Nogo-B receptor, a subunit of cis-prenyltransferase, causes a congenital disorder of glycosylation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  8. [9] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  9. [10] ↑ . Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  10. [11] ↑ . GOA. 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] ↑ . Mutation of Nogo-B receptor, a subunit of cis-prenyltransferase, causes a congenital disorder of glycosylation. 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] ↑ . 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] ↑ . Assigning function to yeast proteins by integration of technologies.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] ↑ . A survey of essential gene function in the yeast cell division cycle. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] ↑ . Mutation of Nogo-B receptor, a subunit of cis-prenyltransferase, causes a congenital disorder of glycosylation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] ↑ . UniProt. Retrieved . wikidata.org.
  25. [26] ↑ . UniProt. Retrieved . wikidata.org.

Class ancestry

  1. [1] ↑ . Wikidata. wikidata.org.

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APA 4ort.xyz Knowledge Graph. (2026). Ditrans,polycis-polyprenyl diphosphate synthase YDL193W. Retrieved May 3, 2026, from https://4ort.xyz/entity/ditrans-polycis-polyprenyl-diphosphate-synthase-ydl193w
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