FOG01870
EOG8M37SX
sce:RER2
Genes: 34
SGD DescriptionCis-prenyltransferase involved in dolichol synthesis; major enzyme of polyprenol synthesis in both the endoplasmic reticulum (ER) and in lipid droplets; participates in ER protein sorting
PomBase Descriptioncis-prenyltransferase
AspGD DescriptionProtein with a predicted role in retention of ER membrane proteins; expression enhanced by maltose; expression induced by tunicamycin and DTT
References
Sato M, et al. (1999 Jan). The yeast RER2 gene, identified by endoplasmic reticulum protein localization mutations, encodes cis-prenyltransferase, a key enzyme in dolichol synthesis.
Sato M, et al. (2001 Jun). Yeast Saccharomyces cerevisiae has two cis-prenyltransferases with different properties and localizations. Implication for their distinct physiological roles in dolichol synthesis.
Poznański J, et al. (2007 Jun 5). Precise bacterial polyprenol length control fails in Saccharomyces cerevisiae.
Wendland J, et al. (2011 Dec). Genome evolution in the eremothecium clade of the Saccharomyces complex revealed by comparative genomics.
Park EJ, et al. (2014 Sep 2). Mutation of Nogo-B receptor, a subunit of cis-prenyltransferase, causes a congenital disorder of glycosylation.
FOG01871
EOG8M37SX
sce:SRT1
Genes: 25
SGD DescriptionCis-prenyltransferase; involved in synthesis of long-chain dolichols (19-22 isoprene units; as opposed to Rer2p which synthesizes shorter-chain dolichols); localizes to lipid bodies; transcription is induced during stationary phase
References
Sato M, et al. (1999 Jan). The yeast RER2 gene, identified by endoplasmic reticulum protein localization mutations, encodes cis-prenyltransferase, a key enzyme in dolichol synthesis.
Sato M, et al. (2001 Jun). Yeast Saccharomyces cerevisiae has two cis-prenyltransferases with different properties and localizations. Implication for their distinct physiological roles in dolichol synthesis.
Poznański J, et al. (2007 Jun 5). Precise bacterial polyprenol length control fails in Saccharomyces cerevisiae.
Park EJ, et al. (2014 Sep 2). Mutation of Nogo-B receptor, a subunit of cis-prenyltransferase, causes a congenital disorder of glycosylation.