YDR518W - Revision history

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@@ Line 18: / Line 18: @@
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 <br>
-'''Description of YDR518W:''' Protein disulfide isomerase of the endoplasmic reticulum lumen, function overlaps with that of Pdi1p; may interact with nascent polypeptides in the ER<ref name='S000042569'>Holst B, et al. (1997) Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum. J Cell Biol 138(6):1229-38 {{SGDpaper|S000042569}} PMID 9298979</ref><ref name='S000039536'>Tachibana C and Stevens TH (1992) The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase. Mol Cell Biol 12(10):4601-11
+'''Description of YDR518W:''' Protein disulfide isomerase of the endoplasmic reticulum lumen; EUG1 has a paralog, PDI1, that arose from the whole genome duplication; function overlaps with that of Pdi1p; may interact with nascent polypeptides in the ER<ref name='S000113653'>Byrne KP and Wolfe KH (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61 {{SGDpaper|S000113653}} PMID 16169922</ref><ref name='S000042569'>Holst B, et al. (1997) Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum. J Cell Biol 138(6):1229-38 {{SGDpaper|S000042569}} PMID 9298979</ref><ref name='S000039536'>Tachibana C and Stevens TH (1992) The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase. Mol Cell Biol 12(10):4601-11
   {{SGDpaper|S000039536}} PMID 1406650</ref>
 <br>

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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=S000002926 YDR518W]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002926 YDR518W]
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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''EUG1 ''

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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr IV:1478601..1480154
+|nowrap| Chr IV:1478608..1480161
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000002926

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YDR518W:''' Protein disulfide isomerase of the endoplasmic reticulum lumen, function overlaps with that of Pdi1p; may interact with nascent polypeptides in the ER<ref name='S000039536'>Tachibana C and Stevens TH (1992) The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase. Mol Cell Biol 12(10):4601-11 {{SGDpaper|S000039536}} PMID 1406650</ref><ref name='S000042569'>Holst B, et al. (1997) Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum. J Cell Biol 138(6):1229-38
+'''Description of YDR518W:''' Protein disulfide isomerase of the endoplasmic reticulum lumen, function overlaps with that of Pdi1p; may interact with nascent polypeptides in the ER<ref name='S000042569'>Holst B, et al. (1997) Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum. J Cell Biol 138(6):1229-38 {{SGDpaper|S000042569}} PMID 9298979</ref><ref name='S000039536'>Tachibana C and Stevens TH (1992) The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase. Mol Cell Biol 12(10):4601-11
-  {{SGDpaper|S000042569}} PMID 9298979</ref>
+  {{SGDpaper|S000039536}} PMID 1406650</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YDR518W:''' Protein disulfide isomerase of the endoplasmic reticulum lumen, function overlaps with that of Pdi1p; may interact with nascent polypeptides in the ER<ref name='S000042569'>Holst B, et al. (1997) Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum. J Cell Biol 138(6):1229-38 {{SGDpaper|S000042569}} PMID 9298979</ref><ref name='S000039536'>Tachibana C and Stevens TH (1992) The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase. Mol Cell Biol 12(10):4601-11
+'''Description of YDR518W:''' Protein disulfide isomerase of the endoplasmic reticulum lumen, function overlaps with that of Pdi1p; may interact with nascent polypeptides in the ER<ref name='S000039536'>Tachibana C and Stevens TH (1992) The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase. Mol Cell Biol 12(10):4601-11 {{SGDpaper|S000039536}} PMID 1406650</ref><ref name='S000042569'>Holst B, et al. (1997) Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum. J Cell Biol 138(6):1229-38
- {{SGDpaper|S000039536}} PMID 1406650</ref>
+ {{SGDpaper|S000042569}} PMID 9298979</ref>
 <br>
 <br>

← Older revision		Revision as of 20:02, 21 February 2007
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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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