The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

SEC59  -  Sec59p

Saccharomyces cerevisiae S288c

Synonyms: Dolichol kinase, YM8270.17C, YMR013C
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

High impact information on SEC59

  • In mutants affecting translocation into (sec59) and passage from (sec 18) the endoplasmic reticulum, a glycosylated form of the precursor containing three N-linked core oligosaccharides accumulates; however, it appears that the signal peptide is not removed [1].
  • A portion of the invertase polypeptide accumulated at 37 degrees C is preserved when membranes from sec53 and sec59 are treated with trypsin [2].
  • DK1 is responsible for the final step of the de novo biosynthesis of dolichol phosphate [3].
  • The mutated alleles failed to complement the temperature-sensitive phenotype of DK1-deficient yeast cells, whereas the wild-type allele restored the normal growth phenotype [3].
  • Among the mutants identified by this screen were sec59 (which encodes dolichol kinase) and a mutant that affects the activity of the ALG1-encoded mannosyltransferase that forms dolichol-PP-(GlcNAc)2Man1 [4].

Biological context of SEC59

  • Molecular cloning and DNA sequence analysis of the SEC59 gene predicted an extremely hydrophobic protein product of 59 kilodaltons [5].
  • The CTP-mediated phosphorylation of diacylglycerol (DAG) is unaffected by either the temperature-sensitive mutation in the sec59-1 strain, overexpression of the SEC59 gene, or the mammalian homolog hDK1 under conditions that produced a loss or elevation in the level of DK activity [6].
  • Genetic mapping experiments revealed that ERG6 is located on chromosome XIII, tightly linked to sec59 [7].
  • When sec59 cells were transformed with a plasmid that overexpresses the wild-type gene, dolichol kinase activity increased 10-fold over wild-type levels [8].
  • Sec59 encodes a membrane protein required for core glycosylation in Saccharomyces cerevisiae [5].

Anatomical context of SEC59


Associations of SEC59 with chemical compounds

  • Yeast secretory mutants sec53 and sec59 define a posttranslational stage in the penetration of glycoprotein precursors into the endoplasmic reticulum (ER) [2].
  • Quantitative measurements of dolichyl phosphate in sec59 cells showed that the levels were decreased to 48% of wild type at the permissive temperature and to less than 10% at the restrictive temperature [8].
  • These results were consistent with a role for the Sec59 protein in the transfer of mannose to dolichol-linked oligosaccharide [5].

Other interactions of SEC59

  • The secretion mutant sec59 has a similar phenotype to dpm1, and the presence of a dolichol recognition sequence in the SEC59 protein gave a clue to its defect, which is in dolichol kinase [9].


  1. Glycosylation and processing of prepro-alpha-factor through the yeast secretory pathway. Julius, D., Schekman, R., Thorner, J. Cell (1984) [Pubmed]
  2. Genes required for completion of import of proteins into the endoplasmic reticulum in yeast. Ferro-Novick, S., Hansen, W., Schauer, I., Schekman, R. J. Cell Biol. (1984) [Pubmed]
  3. A defect in dolichol phosphate biosynthesis causes a new inherited disorder with death in early infancy. Kranz, C., Jungeblut, C., Denecke, J., Erlekotte, A., Sohlbach, C., Debus, V., Kehl, H.G., Harms, E., Reith, A., Reichel, S., Grobe, H., Hammersen, G., Schwarzer, U., Marquardt, T. Am. J. Hum. Genet. (2007) [Pubmed]
  4. A screen for yeast mutants with defects in the dolichol-mediated pathway for N-glycosylation. Roos, J., Sternglanz, R., Lennarz, W.J. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  5. Sec59 encodes a membrane protein required for core glycosylation in Saccharomyces cerevisiae. Bernstein, M., Kepes, F., Schekman, R. Mol. Cell. Biol. (1989) [Pubmed]
  6. 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. Fernandez, F., Shridas, P., Jiang, S., Aebi, M., Waechter, C.J. Glycobiology (2002) [Pubmed]
  7. The yeast gene ERG6 is required for normal membrane function but is not essential for biosynthesis of the cell-cycle-sparking sterol. Gaber, R.F., Copple, D.M., Kennedy, B.K., Vidal, M., Bard, M. Mol. Cell. Biol. (1989) [Pubmed]
  8. Saccharomyces cerevisiae sec59 cells are deficient in dolichol kinase activity. Heller, L., Orlean, P., Adair, W.L. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  9. Enzymes that recognize dolichols participate in three glycosylation pathways and are required for protein secretion. Orlean, P. Biochem. Cell Biol. (1992) [Pubmed]
WikiGenes - Universities