YNR030W - Revision history

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{|{{Prettytable}} align = 'right' width = '200px'
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YNR030W YNR030W]
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''ALG12 ''
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases''' ||''ECM39''
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type''' || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]]
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr XIV:678801..680456
|-
|colspan = '3'|{{Don'tEditThisBox}}
|}
 
'''Description of {{PAGENAME}}:''' Alpha-1,6-mannosyltransferase localized to the ER; responsible for the addition of the alpha-1,6 mannose to dolichol-linked Man7GlcNAc2, acts in the dolichol pathway for N-glycosylation<ref name='S000070115'>Burda P, et al. (1999) Ordered assembly of the asymmetrically branched lipid-linked oligosaccharide in the endoplasmic reticulum is ensured by the substrate specificity of the individual glycosyltransferases. Glycobiology 9(6):617-25 {{SGDpaper|S000070115}} PMID 10336995</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='S000060996'>Grimme SJ, et al. (2001) The essential Smp3 protein is required for addition of the side-branching fourth mannose during assembly of yeast glycosylphosphatidylinositols. J Biol Chem 276(29):27731-9
{{SGDpaper|S000060996}} PMID 11356840</ref>
 
 
 
 

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==Community Commentary==
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==References==

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 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr XIV:678802..680457
+|nowrap| Chr XIV:678799..680454
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000005313

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YNR030W:''' Alpha-1,6-mannosyltransferase localized to the ER; responsible for the addition of the alpha-1,6 mannose to dolichol-linked Man7GlcNAc2, acts in the dolichol pathway for N-glycosylation<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='S000060996'>Grimme SJ, et al. (2001) The essential Smp3 protein is required for addition of the side-branching fourth mannose during assembly of yeast glycosylphosphatidylinositols. J Biol Chem 276(29):27731-9 {{SGDpaper|S000060996}} PMID 11356840</ref><ref name='S000070115'>Burda P, et al. (1999) Ordered assembly of the asymmetrically branched lipid-linked oligosaccharide in the endoplasmic reticulum is ensured by the substrate specificity of the individual glycosyltransferases. Glycobiology 9(6):617-25
+'''Description of YNR030W:''' Alpha-1,6-mannosyltransferase localized to the ER; responsible for the addition of the alpha-1,6 mannose to dolichol-linked Man7GlcNAc2, acts in the dolichol pathway for N-glycosylation<ref name='S000070115'>Burda P, et al. (1999) Ordered assembly of the asymmetrically branched lipid-linked oligosaccharide in the endoplasmic reticulum is ensured by the substrate specificity of the individual glycosyltransferases. Glycobiology 9(6):617-25 {{SGDpaper|S000070115}} PMID 10336995</ref><ref name='S000060996'>Grimme SJ, et al. (2001) The essential Smp3 protein is required for addition of the side-branching fourth mannose during assembly of yeast glycosylphosphatidylinositols. J Biol Chem 276(29):27731-9 {{SGDpaper|S000060996}} PMID 11356840</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|S000070115}} PMID 10336995</ref>
+  {{SGDpaper|S000061582}} PMID 9732283</ref>
 <br>
 <br>

@@ Line 13: / Line 13: @@
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr XIV:678801..680456
+|nowrap| Chr XIV:678802..680457
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000005313

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YNR030W:''' Alpha-1,6-mannosyltransferase localized to the ER; responsible for the addition of the alpha-1,6 mannose to dolichol-linked Man7GlcNAc2, acts in the dolichol pathway for N-glycosylation<ref name='S000070115'>Burda P, et al. (1999) Ordered assembly of the asymmetrically branched lipid-linked oligosaccharide in the endoplasmic reticulum is ensured by the substrate specificity of the individual glycosyltransferases. Glycobiology 9(6):617-25 {{SGDpaper|S000070115}} PMID 10336995</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='S000060996'>Grimme SJ, et al. (2001) The essential Smp3 protein is required for addition of the side-branching fourth mannose during assembly of yeast glycosylphosphatidylinositols. J Biol Chem 276(29):27731-9
+'''Description of YNR030W:''' Alpha-1,6-mannosyltransferase localized to the ER; responsible for the addition of the alpha-1,6 mannose to dolichol-linked Man7GlcNAc2, acts in the dolichol pathway for N-glycosylation<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='S000060996'>Grimme SJ, et al. (2001) The essential Smp3 protein is required for addition of the side-branching fourth mannose during assembly of yeast glycosylphosphatidylinositols. J Biol Chem 276(29):27731-9 {{SGDpaper|S000060996}} PMID 11356840</ref><ref name='S000070115'>Burda P, et al. (1999) Ordered assembly of the asymmetrically branched lipid-linked oligosaccharide in the endoplasmic reticulum is ensured by the substrate specificity of the individual glycosyltransferases. Glycobiology 9(6):617-25
-  {{SGDpaper|S000060996}} PMID 11356840</ref>
+  {{SGDpaper|S000070115}} PMID 10336995</ref>
 <br>
 <br>

← Older revision		Revision as of 20:02, 21 February 2007
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		+
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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.
		+	<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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 {|{{Prettytable}} align = 'right' width = '200px'
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005313 YNR030W]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005313 YNR030W]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''ALG12 ''

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 |nowrap| Chr XIV:678801..680456
 |}
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 ==Community Commentary==
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 ==References==
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