Difference between revisions of "YJR131W"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YJR131W YJR131W]  
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|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'''
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|nowrap| Chr X:667638..669287
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|nowrap| Chr X:667644..669293
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000003892
 
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'''Description of {{PAGENAME}}:''' Alpha-1,2-mannosidase involved in ER quality control; catalyzes the removal of one mannose residue from Man9GlcNAc to produce a single isomer of Man8GlcNAc in N-linked oligosaccharide biosynthesis; integral to ER membrane<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><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='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
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'''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
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  {{SGDpaper|S000048905}} PMID 8864657</ref>
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  {{SGDpaper|S000055216}} PMID 8905927</ref>
 
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==Community Commentary==
 
==Community Commentary==
 
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<!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation -->
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Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
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<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.
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J Biol Chem 278(5):3265-74</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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Community Commentary

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References

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  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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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