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://db.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:667638..669287
 
|nowrap| Chr X:667638..669287
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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 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
 
  {{SGDpaper|S000048905}} PMID 8864657</ref>
 
  {{SGDpaper|S000048905}} PMID 8864657</ref>
 
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J Biol Chem 278(5):3265-74</ref>
 
J Biol Chem 278(5):3265-74</ref>
 
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Revision as of 08:46, 27 February 2007

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Systematic name YJR131W
Gene name MNS1
Aliases
Feature type ORF, Verified
Coordinates Chr X:667638..669287
Primary SGDID S000003892


Description of YJR131W: 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[1][2][3]




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References

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  1. 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
  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. 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

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