General Stability | Organism |
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cytosolic Alg13p is very short-lived, whereas membrane-associated Alg13 is relatively stable. Cytosolic Alg13p is a target for proteasomal degradation, and the failure to degrade excess Alg13p leads to glycosylation defects. Alg13p degradation requires a C-terminal domain whose deletion results in Alg13p stability. Appending this sequence onto normally long-lived beta-galactosidase causes it to undergo rapid degradation, demonstrating that this C-terminal domain represents a novel and autonomous degradation motif. Proteasomal degradation of excess unassembled Alg13p is an important quality control mechanism that ensures proper protein complex assembly and correct N-linked glycosylation | Saccharomyces cerevisiae |
Localization | Comment | Organism | GeneOntology No. | Textmining |
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endoplasmic reticulum | cytosolic Alg13p is very short-lived, whereas membrane-associated Alg13 is relatively stable | Saccharomyces cerevisiae | 5783 | - |
Organism | UniProt | Comment | Textmining |
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Saccharomyces cerevisiae | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
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Synonyms | Comment | Organism |
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Alg13p | the catalytic subunit of the endoplasmic reticulum UDP-GlcNAc glycosyltransferase | Saccharomyces cerevisiae |