YKL216W - Revision history

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@@ 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=S000001699 YKL216W]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000001699 YKL216W]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''URA1 ''

@@ Line 13: / Line 13: @@
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr XI:25216..26160
+|nowrap| Chr XI:25215..26159
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000001699

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YKL216W:''' Dihydroorotate dehydrogenase, catalyzes the fourth enzymatic step in the de novo biosynthesis of pyrimidines, converting dihydroorotic acid into orotic acid<ref name='S000069514'>Vorisek J, et al. (2002) Enzymatic activities of Ura2 and Ura1 proteins (aspartate carbamoyltransferase and dihydro-orotate dehydrogenase) are present in both isolated membranes and cytoplasm of Saccharomyces cerevisiae. Yeast 19(5):449-57 {{SGDpaper|S000069514}} PMID 11921093</ref><ref name='S000065623'>Lacroute F (1968) Regulation of pyrimidine biosynthesis in Saccharomyces cerevisiae. J Bacteriol 95(3):824-32 {{SGDpaper|S000065623}} PMID 5651325</ref><ref name='S000039339'>Guerry-Kopecko P and Wickner RB (1980) Cloning of the URA1 gene of Saccharomyces cerevisiae. J Bacteriol 143(3):1530-3
+'''Description of YKL216W:''' Dihydroorotate dehydrogenase, catalyzes the fourth enzymatic step in the de novo biosynthesis of pyrimidines, converting dihydroorotic acid into orotic acid<ref name='S000039339'>Guerry-Kopecko P and Wickner RB (1980) Cloning of the URA1 gene of Saccharomyces cerevisiae. J Bacteriol 143(3):1530-3 {{SGDpaper|S000039339}} PMID 6251032</ref><ref name='S000065623'>Lacroute F (1968) Regulation of pyrimidine biosynthesis in Saccharomyces cerevisiae. J Bacteriol 95(3):824-32 {{SGDpaper|S000065623}} PMID 5651325</ref><ref name='S000069514'>Vorisek J, et al. (2002) Enzymatic activities of Ura2 and Ura1 proteins (aspartate carbamoyltransferase and dihydro-orotate dehydrogenase) are present in both isolated membranes and cytoplasm of Saccharomyces cerevisiae. Yeast 19(5):449-57
-  {{SGDpaper|S000039339}} PMID 6251032</ref>
+  {{SGDpaper|S000069514}} PMID 11921093</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YKL216W:''' Dihydroorotate dehydrogenase, catalyzes the fourth enzymatic step in the de novo biosynthesis of pyrimidines, converting dihydroorotic acid into orotic acid<ref name='S000039339'>Guerry-Kopecko P and Wickner RB (1980) Cloning of the URA1 gene of Saccharomyces cerevisiae. J Bacteriol 143(3):1530-3 {{SGDpaper|S000039339}} PMID 6251032</ref><ref name='S000065623'>Lacroute F (1968) Regulation of pyrimidine biosynthesis in Saccharomyces cerevisiae. J Bacteriol 95(3):824-32 {{SGDpaper|S000065623}} PMID 5651325</ref><ref name='S000069514'>Vorisek J, et al. (2002) Enzymatic activities of Ura2 and Ura1 proteins (aspartate carbamoyltransferase and dihydro-orotate dehydrogenase) are present in both isolated membranes and cytoplasm of Saccharomyces cerevisiae. Yeast 19(5):449-57
+'''Description of YKL216W:''' Dihydroorotate dehydrogenase, catalyzes the fourth enzymatic step in the de novo biosynthesis of pyrimidines, converting dihydroorotic acid into orotic acid<ref name='S000069514'>Vorisek J, et al. (2002) Enzymatic activities of Ura2 and Ura1 proteins (aspartate carbamoyltransferase and dihydro-orotate dehydrogenase) are present in both isolated membranes and cytoplasm of Saccharomyces cerevisiae. Yeast 19(5):449-57 {{SGDpaper|S000069514}} PMID 11921093</ref><ref name='S000065623'>Lacroute F (1968) Regulation of pyrimidine biosynthesis in Saccharomyces cerevisiae. J Bacteriol 95(3):824-32 {{SGDpaper|S000065623}} PMID 5651325</ref><ref name='S000039339'>Guerry-Kopecko P and Wickner RB (1980) Cloning of the URA1 gene of Saccharomyces cerevisiae. J Bacteriol 143(3):1530-3
-  {{SGDpaper|S000069514}} PMID 11921093</ref>
+  {{SGDpaper|S000039339}} PMID 6251032</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YKL216W:''' Dihydroorotate dehydrogenase, catalyzes the fourth enzymatic step in the de novo biosynthesis of pyrimidines, converting dihydroorotic acid into orotic acid<ref name='S000069514'>Vorisek J, et al. (2002) Enzymatic activities of Ura2 and Ura1 proteins (aspartate carbamoyltransferase and dihydro-orotate dehydrogenase) are present in both isolated membranes and cytoplasm of Saccharomyces cerevisiae. Yeast 19(5):449-57 {{SGDpaper|S000069514}} PMID 11921093</ref><ref name='S000065623'>Lacroute F (1968) Regulation of pyrimidine biosynthesis in Saccharomyces cerevisiae. J Bacteriol 95(3):824-32 {{SGDpaper|S000065623}} PMID 5651325</ref><ref name='S000039339'>Guerry-Kopecko P and Wickner RB (1980) Cloning of the URA1 gene of Saccharomyces cerevisiae. J Bacteriol 143(3):1530-3
+'''Description of YKL216W:''' Dihydroorotate dehydrogenase, catalyzes the fourth enzymatic step in the de novo biosynthesis of pyrimidines, converting dihydroorotic acid into orotic acid<ref name='S000039339'>Guerry-Kopecko P and Wickner RB (1980) Cloning of the URA1 gene of Saccharomyces cerevisiae. J Bacteriol 143(3):1530-3 {{SGDpaper|S000039339}} PMID 6251032</ref><ref name='S000065623'>Lacroute F (1968) Regulation of pyrimidine biosynthesis in Saccharomyces cerevisiae. J Bacteriol 95(3):824-32 {{SGDpaper|S000065623}} PMID 5651325</ref><ref name='S000069514'>Vorisek J, et al. (2002) Enzymatic activities of Ura2 and Ura1 proteins (aspartate carbamoyltransferase and dihydro-orotate dehydrogenase) are present in both isolated membranes and cytoplasm of Saccharomyces cerevisiae. Yeast 19(5):449-57
-  {{SGDpaper|S000039339}} PMID 6251032</ref>
+  {{SGDpaper|S000069514}} PMID 11921093</ref>
 <br>
 <br>

← 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 -->
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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>
		+	-->

	<protect>		<protect>

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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 |nowrap| Chr XI:25216..26160
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 ==Community Commentary==
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 ==References==
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