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Ditrans,polycis-polyprenyl diphosphate synthase YBR002C

fungal protein found in Saccharomyces cerevisiae S288c
Protein protein Q27548217
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Summary

Ditrans,polycis-polyprenyl diphosphate synthase YBR002C is a protein[1].

Key Facts

  • Ditrans,polycis-polyprenyl diphosphate synthase YBR002C's instance of is recorded as protein[2].
  • Ditrans,polycis-polyprenyl diphosphate synthase YBR002C's UniProt protein ID is recorded as P35196[3].
  • Ditrans,polycis-polyprenyl diphosphate synthase YBR002C's part of is recorded as Decaprenyl diphosphate synthase-like superfamily[4].
  • Ditrans,polycis-polyprenyl diphosphate synthase YBR002C's part of is recorded as Decaprenyl diphosphate synthase-like[5].
  • Ditrans,polycis-polyprenyl diphosphate synthase YBR002C's part of is recorded as membrane protein[6].
  • Ditrans,polycis-polyprenyl diphosphate synthase YBR002C's has part is recorded as Di-trans-poly-cis-decaprenylcistransferase-like, conserved site[7].
  • Ditrans,polycis-polyprenyl diphosphate synthase YBR002C's RefSeq protein ID is recorded as NP_009556[8].
  • Ditrans,polycis-polyprenyl diphosphate synthase YBR002C's molecular function is recorded as transferase activity[9].
  • Ditrans,polycis-polyprenyl diphosphate synthase YBR002C's molecular function is recorded as prenyltransferase activity[10].
  • Ditrans,polycis-polyprenyl diphosphate synthase YBR002C's molecular function is recorded as dehydrodolichyl diphosphate synthase activity[11].
  • Ditrans,polycis-polyprenyl diphosphate synthase YBR002C's molecular function is recorded as transferase activity, transferring alkyl or aryl (other than methyl) groups[12].
  • Ditrans,polycis-polyprenyl diphosphate synthase YBR002C's molecular function is recorded as polyprenyltransferase activity[13].
  • Ditrans,polycis-polyprenyl diphosphate synthase YBR002C's molecular function is recorded as dehydrodolichyl diphosphate synthase activity[14].
  • Ditrans,polycis-polyprenyl diphosphate synthase YBR002C's cell component is recorded as endoplasmic reticulum[15].
  • Ditrans,polycis-polyprenyl diphosphate synthase YBR002C's cell component is recorded as membrane[16].
  • Ditrans,polycis-polyprenyl diphosphate synthase YBR002C's cell component is recorded as lipid droplet[17].
  • Ditrans,polycis-polyprenyl diphosphate synthase YBR002C's cell component is recorded as endoplasmic reticulum membrane[18].
  • Ditrans,polycis-polyprenyl diphosphate synthase YBR002C's cell component is recorded as dehydrodolichyl diphosphate synthase complex[19].
  • Ditrans,polycis-polyprenyl diphosphate synthase YBR002C's cell component is recorded as endoplasmic reticulum[20].
  • Ditrans,polycis-polyprenyl diphosphate synthase YBR002C's cell component is recorded as dehydrodolichyl diphosphate synthase complex[21].
  • Ditrans,polycis-polyprenyl diphosphate synthase YBR002C's cell component is recorded as lipid droplet[22].
  • Ditrans,polycis-polyprenyl diphosphate synthase YBR002C's cell component is recorded as intrinsic component of membrane[23].
  • Ditrans,polycis-polyprenyl diphosphate synthase YBR002C's cell component is recorded as endoplasmic reticulum[24].
  • Ditrans,polycis-polyprenyl diphosphate synthase YBR002C's biological process is recorded as dolichol biosynthetic process[25].
  • Ditrans,polycis-polyprenyl diphosphate synthase YBR002C's biological process is recorded as endoplasmic reticulum to Golgi vesicle-mediated transport[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] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  5. [6] ↑ . wikidata.org.
  6. [7] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  7. [8] ↑ . Q20641742. Retrieved . wikidata.org.
  8. [9] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  9. [10] ↑ . Precise bacterial polyprenol length control fails in Saccharomyces cerevisiae. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  10. [11] ↑ . Yeast Saccharomyces cerevisiae has two cis-prenyltransferases with different properties and localizations. Implication for their distinct physiological roles in dolichol synthesis.. 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] ↑ . Yeast Saccharomyces cerevisiae has two cis-prenyltransferases with different properties and localizations. Implication for their distinct physiological roles in dolichol synthesis.. 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] ↑ . High confidence proteomic analysis of yeast LDs identifies additional droplet proteins and reveals connections to dolichol synthesis and sterol acetylation.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] ↑ . Mutation of Nogo-B receptor, a subunit of cis-prenyltransferase, causes a congenital disorder of glycosylation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] ↑ . Mutation of Nogo-B receptor, a subunit of cis-prenyltransferase, causes a congenital disorder of glycosylation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] ↑ . High confidence proteomic analysis of yeast LDs identifies additional droplet proteins and reveals connections to dolichol synthesis and sterol acetylation.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] ↑ . Mutation of Nogo-B receptor, a subunit of cis-prenyltransferase, causes a congenital disorder of glycosylation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] ↑ . Yeast functional analysis: identification of two essential genes involved in ER to Golgi trafficking. Retrieved . ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

  1. [1] ↑ . Wikidata. wikidata.org.

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