Difference between revisions of "YJR131W"
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| − | '''Description of YJR131W:''' Alpha-1,2-mannosidase involved in ER | + | '''Description of YJR131W:''' Alpha-1,2-mannosidase involved in ER-associated protein degradation (ERAD); catalyzes the removal of one mannose residue from a glycosylated protein, converting the modification from Man9GlcNAc to Man8GlcNAc; catalyzes the last step in glycoprotein maturation in the ER and is critical for ER protein degradation<ref name='S000048905'>Burke J, et al. (1996) The Saccharomyces cerevisiae processing alpha 1,2-mannosidase is localized in the endoplasmic reticulum, independently of known retrieval motifs. Eur J Cell Biol 70(4):298-305 {{SGDpaper|S000048905}} PMID 8864657</ref><ref name='S000054810'>Camirand A, et al. (1991) Glycoprotein biosynthesis in Saccharomyces cerevisiae. Isolation and characterization of the gene encoding a specific processing alpha-mannosidase. J Biol Chem 266(23):15120-7 {{SGDpaper|S000054810}} PMID 1714453</ref><ref name='S000061582'>Jakob CA, et al. (1998) Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure. J Cell Biol 142(5):1223-33 {{SGDpaper|S000061582}} PMID 9732283</ref><ref name='S000055216'>Knop M, et al. (1996) N-Glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase yscY in yeast. Yeast 12(12):1229-38 |
{{SGDpaper|S000055216}} PMID 8905927</ref> | {{SGDpaper|S000055216}} PMID 8905927</ref> | ||
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Latest revision as of 14:05, 13 June 2012
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| Systematic name | YJR131W |
| Gene name | MNS1 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr X:667644..669293 |
| Primary SGDID | S000003892 |
Description of YJR131W: Alpha-1,2-mannosidase involved in ER-associated protein degradation (ERAD); catalyzes the removal of one mannose residue from a glycosylated protein, converting the modification from Man9GlcNAc to Man8GlcNAc; catalyzes the last step in glycoprotein maturation in the ER and is critical for ER protein degradation[1][2][3][4]
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References
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- ↑ Burke J, et al. (1996) The Saccharomyces cerevisiae processing alpha 1,2-mannosidase is localized in the endoplasmic reticulum, independently of known retrieval motifs. Eur J Cell Biol 70(4):298-305 SGD PMID 8864657
- ↑ Camirand A, et al. (1991) Glycoprotein biosynthesis in Saccharomyces cerevisiae. Isolation and characterization of the gene encoding a specific processing alpha-mannosidase. J Biol Chem 266(23):15120-7 SGD PMID 1714453
- ↑ Jakob CA, et al. (1998) Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure. J Cell Biol 142(5):1223-33 SGD PMID 9732283
- ↑ Knop M, et al. (1996) N-Glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase yscY in yeast. Yeast 12(12):1229-38 SGD PMID 8905927
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