Difference between revisions of "YJR131W"
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− | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http:// | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003892 YJR131W] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''MNS1 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''MNS1 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
− | |nowrap| Chr X: | + | |nowrap| Chr X:667644..669293 |
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− | | | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000003892 |
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− | '''Description of | + | '''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| | + | {{SGDpaper|S000055216}} PMID 8905927</ref> |
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==Community Commentary== | ==Community Commentary== | ||
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+ | Specifically higher expression in carbon limited chemostat cultures versus carbon excess. | ||
+ | <ref>Boer VM, et al. (2003) The genome-wide transcriptional responses of Saccharomyces cerevisiae grown on glucose in aerobic chemostat cultures limited for carbon, nitrogen, phosphorus, or sulfur. | ||
+ | J Biol Chem 278(5):3265-74</ref> | ||
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==References== | ==References== | ||
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Latest revision as of 14:05, 13 June 2012
Share your knowledge...Edit this entry! <protect>
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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Contents
Community Commentary
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References
See Help:References on how to add references
- ↑ 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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