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Ditrans,polycis-polyprenyl diphosphate synthase YMR101C

fungal protein found in Saccharomyces cerevisiae S288c
Protein protein Q27551790
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Summary

Ditrans,polycis-polyprenyl diphosphate synthase YMR101C is a protein[1].

Key Facts

  • Ditrans,polycis-polyprenyl diphosphate synthase YMR101C's instance of is recorded as protein[2].
  • Ditrans,polycis-polyprenyl diphosphate synthase YMR101C's subclass of is recorded as protein[3].
  • Ditrans,polycis-polyprenyl diphosphate synthase YMR101C's UniProt protein ID is recorded as Q03175[4].
  • Ditrans,polycis-polyprenyl diphosphate synthase YMR101C's RefSeq protein ID is recorded as NP_013819[5].
  • Ditrans,polycis-polyprenyl diphosphate synthase YMR101C's molecular function is recorded as transferase activity[6].
  • Ditrans,polycis-polyprenyl diphosphate synthase YMR101C's molecular function is recorded as dehydrodolichyl diphosphate synthase activity[7].
  • Ditrans,polycis-polyprenyl diphosphate synthase YMR101C's molecular function is recorded as transferase activity, transferring alkyl or aryl (other than methyl) groups[8].
  • Ditrans,polycis-polyprenyl diphosphate synthase YMR101C's molecular function is recorded as prenyltransferase activity[9].
  • Ditrans,polycis-polyprenyl diphosphate synthase YMR101C's molecular function is recorded as polyprenyltransferase activity[10].
  • Ditrans,polycis-polyprenyl diphosphate synthase YMR101C's molecular function is recorded as dehydrodolichyl diphosphate synthase activity[11].
  • Ditrans,polycis-polyprenyl diphosphate synthase YMR101C's molecular function is recorded as dehydrodolichyl diphosphate synthase activity[12].
  • Ditrans,polycis-polyprenyl diphosphate synthase YMR101C's cell component is recorded as dehydrodolichyl diphosphate synthase complex[13].
  • Ditrans,polycis-polyprenyl diphosphate synthase YMR101C's cell component is recorded as lipid droplet[14].
  • Ditrans,polycis-polyprenyl diphosphate synthase YMR101C's cell component is recorded as endoplasmic reticulum[15].
  • Ditrans,polycis-polyprenyl diphosphate synthase YMR101C's cell component is recorded as dehydrodolichyl diphosphate synthase complex[16].
  • Ditrans,polycis-polyprenyl diphosphate synthase YMR101C's cell component is recorded as lipid droplet[17].
  • Ditrans,polycis-polyprenyl diphosphate synthase YMR101C's cell component is recorded as intrinsic component of membrane[18].
  • Ditrans,polycis-polyprenyl diphosphate synthase YMR101C's cell component is recorded as lipid droplet[19].
  • Ditrans,polycis-polyprenyl diphosphate synthase YMR101C's biological process is recorded as protein glycosylation[20].
  • Ditrans,polycis-polyprenyl diphosphate synthase YMR101C's biological process is recorded as dolichol biosynthetic process[21].
  • Ditrans,polycis-polyprenyl diphosphate synthase YMR101C's biological process is recorded as polyprenol biosynthetic process[22].
  • Ditrans,polycis-polyprenyl diphosphate synthase YMR101C's biological process is recorded as dolichol biosynthetic process[23].
  • Ditrans,polycis-polyprenyl diphosphate synthase YMR101C's biological process is recorded as protein glycosylation[24].
  • Ditrans,polycis-polyprenyl diphosphate synthase YMR101C's encoded by is recorded as SRT1[25].
  • Ditrans,polycis-polyprenyl diphosphate synthase YMR101C'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] ↑ . UniProt. Retrieved . wikidata.org.
  4. [5] ↑ . Q20641742. Retrieved . wikidata.org.
  5. [6] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  6. [7] ↑ . 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.
  7. [8] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  8. [9] ↑ . Precise bacterial polyprenol length control fails in Saccharomyces cerevisiae. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  9. [10] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. 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] ↑ . Mutation of Nogo-B receptor, a subunit of cis-prenyltransferase, causes a congenital disorder of glycosylation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] ↑ . Mutation of Nogo-B receptor, a subunit of cis-prenyltransferase, causes a congenital disorder of glycosylation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [14] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] ↑ . Mutation of Nogo-B receptor, a subunit of cis-prenyltransferase, causes a congenital disorder of glycosylation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] ↑ . GOA. 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] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] ↑ . 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.
  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] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. 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] ↑ . 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.
  24. [25] ↑ . UniProt. Retrieved . wikidata.org.
  25. [26] ↑ . UniProt. Retrieved . wikidata.org.

Class ancestry

  1. [1] ↑ . Wikidata. wikidata.org.

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