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Literature summary for 2.4.1.141 extracted from

  • Averbeck, N.; Gao, X.D.; Nishimura, S.; Dean, N.
    Alg13p, the catalytic subunit of the endoplasmic reticulum UDP-GlcNAc glycosyltransferase, is a target for proteasomal degradation (2008), Mol. Biol. Cell, 19, 2169-2178.
    View publication on PubMedView publication on EuropePMC

General Stability

General Stability Organism
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

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum cytosolic Alg13p is very short-lived, whereas membrane-associated Alg13 is relatively stable Saccharomyces cerevisiae 5783
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Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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Source Tissue

Source Tissue Comment Organism Textmining

Synonyms

Synonyms Comment Organism
Alg13p the catalytic subunit of the endoplasmic reticulum UDP-GlcNAc glycosyltransferase Saccharomyces cerevisiae