| Standard Name | SEC59 1, 2 |
|---|---|
| Systematic Name | YMR013C |
| Feature Type | ORF, Verified |
| Description | Dolichol kinase, catalyzes the terminal step in dolichyl monophosphate (Dol-P) biosynthesis; required for viability and for normal rates of lipid intermediate synthesis and protein N-glycosylation (1, 3 and see Summary Paragraph) |
| Name Description | SECretory 1 |
| Chromosomal Location | |
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| Note: this feature is encoded on the Crick strand. | |
| Genetic position: 3 cM |
| View Computational GO annotations for SEC59 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated | |
| High-throughput |
| Classical genetics | |
|---|---|
| conditional |
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| reduction of function | |
| Large-scale survey | |
| null | |
| reduction of function | |
| Resources |
| 22 total interaction(s) for 19 unique genes/features. | |
| Physical Interactions |
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| Genetic Interactions |
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| Resources |
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| Resources |
| Localization | |
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| Phosphorylation | PhosphoGRID | PhosphoPep Database |
| Structure | |
| Homologs |
| Note: this feature is encoded on the Crick strand. | |||||||||||||
| This feature contains embedded feature(s): YMR013C-A | |||||||||||||
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| Genetic position: 3 cM | |||||||||||||
| Last Update | Coordinates: 2011-02-03 | Sequence: 1996-07-31 | ||||||||||||
| Subfeature details |
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| S288C only | |
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| S288C vs. other species | |
| S288C vs. other strains |
| External Links | All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB |
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| Primary SGDID | S000004615 |
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Dolichols are a class of polyisoprenoid alcohols with five or more isoprene units in which the C2-C3 bond is saturated. In yeast, dolichols with 14-18 isoprene units are the carrier molecules on which many of the steps in N-linked glycosylation, O-linked glycosylation, and GPI anchor synthesis occur on the membrane of the endoplasmic reticulum (ER) (reviewed in 4). In mammals, dolichols with 19-22 isoprene units are the carrier molecules on which these steps occur.
SEC59 encodes dolichol kinase (3), which synthesizes dolichyl-phosphate (Dol-P), the substrate on which oligosaccharide cores are assembled on the ER membrane. Mutants lacking Sec59p produce poorly N-glycosylated proteins that accumulate in the ER, hence the secretory phenotype (5). Dol-P is also used to shuttle mannose (and glucose) into the ER, so sec59 mutants are also deficient in O-linked glycosylation and GPI anchor synthesis (6, 7). (Refer to the entries for DPM1 and ALG5 for information on shuttling mannose and glucose, respectively, into the ER.) A putative human dolichol kinase cDNA complements the sec59-1 mutation (8).
| 1) | Bernstein M, et al. (1989) Sec59 encodes a membrane protein required for core glycosylation in Saccharomyces cerevisiae. Mol Cell Biol 9(3):1191-9 |
| 2) | Fields, C. and Schekman, R. (1985) Personal Communication, Mortimer Map Edition 9 |
| 3) | Heller L, et al. (1992) Saccharomyces cerevisiae sec59 cells are deficient in dolichol kinase activity. Proc Natl Acad Sci U S A 89(15):7013-6 |
| 4) | Grabinska K and Palamarczyk G (2002) Dolichol biosynthesis in the yeast Saccharomyces cerevisiae: an insight into the regulatory role of farnesyl diphosphate synthase. FEMS Yeast Res 2(3):259-65 |
| 5) | Ferro-Novick S, et al. (1984) Yeast secretory mutants that block the formation of active cell surface enzymes. J Cell Biol 98(1):35-43 |
| 6) | Orlean P (1990) Dolichol phosphate mannose synthase is required in vivo for glycosyl phosphatidylinositol membrane anchoring, O mannosylation, and N glycosylation of protein in Saccharomyces cerevisiae. Mol Cell Biol 10(11):5796-805 |
| 7) | Orlean P (1992) Enzymes that recognize dolichols participate in three glycosylation pathways and are required for protein secretion. Biochem Cell Biol 70(6):438-47 |
| 8) | Fernandez F, et al. (2002) Expression and characterization of a human cDNA that complements the temperature-sensitive defect in dolichol kinase activity in the yeast sec59-1 mutant: the enzymatic phosphorylation of dolichol and diacylglycerol are catalyzed by separate CTP-mediated kinase activities in Saccharomyces cerevisiae. Glycobiology 12(9):555-62 |





