YMR215W - 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=YMR215W YMR215W]
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''GAS3 ''
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases''' ||'' ''
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type''' || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]]
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr XIII:696795..698369
|-
|colspan = '3'|{{Don'tEditThisBox}}
|}
 
'''Description of {{PAGENAME}}:''' Putative 1,3-beta-glucanosyltransferase, has similarity to Gas1p; localizes to the cell wall<ref name='S000063190'>Mouyna I, et al. (2000) Identification of the catalytic residues of the first family of beta(1-3)glucanosyltransferases identified in fungi. Biochem J 347 Pt 3():741-7 {{SGDpaper|S000063190}} PMID 10769178</ref><ref name='S000040179'>Hamada K, et al. (1999) Amino acid residues in the omega-minus region participate in cellular localization of yeast glycosylphosphatidylinositol-attached proteins. J Bacteriol 181(13):3886-9
{{SGDpaper|S000040179}} PMID 10383953</ref>
 
 
 
 

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==Community Commentary==
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==References==

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 <br>
-'''Description of YMR215W:''' Putative 1,3-beta-glucanosyltransferase, has similarity to Gas1p; localizes to the cell wall<ref name='S000040179'>Hamada K, et al. (1999) Amino acid residues in the omega-minus region participate in cellular localization of yeast glycosylphosphatidylinositol-attached proteins. J Bacteriol 181(13):3886-9 {{SGDpaper|S000040179}} PMID 10383953</ref><ref name='S000063190'>Mouyna I, et al. (2000) Identification of the catalytic residues of the first family of beta(1-3)glucanosyltransferases identified in fungi. Biochem J 347 Pt 3():741-7
+'''Description of YMR215W:''' Low abundance, possibly inactive member of the GAS family of GPI-containing proteins; putative 1,3-beta-glucanosyltransferase with similarity to other GAS family members; localizes to the cell wall; mRNA induced during sporulation<ref name='S000040179'>Hamada K, et al. (1999) Amino acid residues in the omega-minus region participate in cellular localization of yeast glycosylphosphatidylinositol-attached proteins. J Bacteriol 181(13):3886-9 {{SGDpaper|S000040179}} PMID 10383953</ref><ref name='S000063190'>Mouyna I, et al. (2000) Identification of the catalytic residues of the first family of beta(1-3)glucanosyltransferases identified in fungi. Biochem J 347 Pt 3():741-7 {{SGDpaper|S000063190}} PMID 10769178</ref><ref name='S000051006'>Popolo L and Vai M (1999) The Gas1 glycoprotein, a putative wall polymer cross-linker. Biochim Biophys Acta 1426(2):385-400 {{SGDpaper|S000051006}} PMID 9878845</ref><ref name='S000135055'>Rolli E, et al. (2010) GAS3, a developmentally regulated gene, encodes a highly mannosylated and inactive protein of the Gas family of Saccharomyces cerevisiae. Yeast 27(8):597-610
-  {{SGDpaper|S000063190}} PMID 10769178</ref>
+  {{SGDpaper|S000135055}} PMID 20641027</ref>
 <br>
 <br>

@@ Line 13: / Line 13: @@
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr XIII:696795..698369
+|nowrap| Chr XIII:696796..698370
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000004828

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YMR215W:''' Putative 1,3-beta-glucanosyltransferase, has similarity to Gas1p; localizes to the cell wall<ref name='S000040179'>Hamada K, et al. (1999) Amino acid residues in the omega-minus region participate in cellular localization of yeast glycosylphosphatidylinositol-attached proteins. J Bacteriol 181(13):3886-9 {{SGDpaper|S000040179}} PMID 10383953</ref><ref name='S000063190'>Mouyna I, et al. (2000) Identification of the catalytic residues of the first family of beta(1-3)glucanosyltransferases identified in fungi. Biochem J 347 Pt 3:741-7
+'''Description of YMR215W:''' Putative 1,3-beta-glucanosyltransferase, has similarity to Gas1p; localizes to the cell wall<ref name='S000040179'>Hamada K, et al. (1999) Amino acid residues in the omega-minus region participate in cellular localization of yeast glycosylphosphatidylinositol-attached proteins. J Bacteriol 181(13):3886-9 {{SGDpaper|S000040179}} PMID 10383953</ref><ref name='S000063190'>Mouyna I, et al. (2000) Identification of the catalytic residues of the first family of beta(1-3)glucanosyltransferases identified in fungi. Biochem J 347 Pt 3():741-7
   {{SGDpaper|S000063190}} PMID 10769178</ref>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YMR215W:''' Putative 1,3-beta-glucanosyltransferase, has similarity to Gas1p; localizes to the cell wall<ref name='S000063190'>Mouyna I, et al. (2000) Identification of the catalytic residues of the first family of beta(1-3)glucanosyltransferases identified in fungi. Biochem J 347 Pt 3:741-7 {{SGDpaper|S000063190}} PMID 10769178</ref><ref name='S000040179'>Hamada K, et al. (1999) Amino acid residues in the omega-minus region participate in cellular localization of yeast glycosylphosphatidylinositol-attached proteins. J Bacteriol 181(13):3886-9
+'''Description of YMR215W:''' Putative 1,3-beta-glucanosyltransferase, has similarity to Gas1p; localizes to the cell wall<ref name='S000040179'>Hamada K, et al. (1999) Amino acid residues in the omega-minus region participate in cellular localization of yeast glycosylphosphatidylinositol-attached proteins. J Bacteriol 181(13):3886-9 {{SGDpaper|S000040179}} PMID 10383953</ref><ref name='S000063190'>Mouyna I, et al. (2000) Identification of the catalytic residues of the first family of beta(1-3)glucanosyltransferases identified in fungi. Biochem J 347 Pt 3:741-7
-  {{SGDpaper|S000040179}} PMID 10383953</ref>
+  {{SGDpaper|S000063190}} PMID 10769178</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YMR215W:''' Putative 1,3-beta-glucanosyltransferase, has similarity to Gas1p; localizes to the cell wall<ref name='S000063190'>Mouyna I, et al. (2000) Identification of the catalytic residues of the first family of beta(1-3)glucanosyltransferases identified in fungi. Biochem J 347 Pt 3():741-7 {{SGDpaper|S000063190}} PMID 10769178</ref><ref name='S000040179'>Hamada K, et al. (1999) Amino acid residues in the omega-minus region participate in cellular localization of yeast glycosylphosphatidylinositol-attached proteins. J Bacteriol 181(13):3886-9
+'''Description of YMR215W:''' Putative 1,3-beta-glucanosyltransferase, has similarity to Gas1p; localizes to the cell wall<ref name='S000063190'>Mouyna I, et al. (2000) Identification of the catalytic residues of the first family of beta(1-3)glucanosyltransferases identified in fungi. Biochem J 347 Pt 3:741-7 {{SGDpaper|S000063190}} PMID 10769178</ref><ref name='S000040179'>Hamada K, et al. (1999) Amino acid residues in the omega-minus region participate in cellular localization of yeast glycosylphosphatidylinositol-attached proteins. J Bacteriol 181(13):3886-9
   {{SGDpaper|S000040179}} PMID 10383953</ref>
 <br>

@@ Line 4: / Line 4: @@
 {|{{Prettytable}} align = 'right' width = '200px'
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004828 YMR215W]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004828 YMR215W]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''GAS3 ''

← Older revision		Revision as of 20:02, 21 February 2007
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		+	<!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation -->
		+	<!--
		+	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>
		+	-->

	<protect>		<protect>

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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 |nowrap| Chr XIII:696795..698369
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 ==Community Commentary==
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 ==References==
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