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Literature summary for 2.4.1.256 extracted from
- SWATH-MS glycoproteomics reveals consequences of defects in the glycosylation machinery (2016), Mol. Cell. Proteomics, 15, 2435-2447.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | P50076 | - |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ALG10 | - |
Saccharomyces cerevisiae |
| Die2 | - |
Saccharomyces cerevisiae |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | Alg10 gene deletion mutants, as well as endoplasmic reticulum lumenal mannosyltransferases (Alg3, Alg9, and Alg12), glucosyltransferases (Alg6, Alg8), or oligosaccharyltransferase subunits (Ost3, Ost5, and Ost6) deletion mutants, show decreased glycan occupancy and altered cell wall proteomes. Mutations in earlier mannosyltransferase or glucosyltransferase steps of glycan biosynthesis have stronger hypoglycosylation phenotypes, but glucosyltransferase defects are more severe | Saccharomyces cerevisiae |
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Release 2023.1 (January 2023)
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