YGL208W - 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?dbid=S000003176 YGL208W]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003176 YGL208W]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''SIP2 ''

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 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr VII:97342..98589
+|nowrap| Chr VII:97338..98585
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000003176

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YGL208W:''' One of three beta subunits of the Snf1 serine/threonine protein kinase complex involved in the response to glucose starvation; null mutants exhibit accelerated aging; N-myristoylprotein localized to the cytoplasm and the plasma membrane<ref name='S000049850'>Ashrafi K, et al. (2000) Sip2p and its partner snf1p kinase affect aging in S. cerevisiae. Genes Dev 14(15):1872-85 {{SGDpaper|S000049850}} PMID 10921902</ref><ref name='S000059161'>Schmidt MC and McCartney RR (2000) beta-subunits of Snf1 kinase are required for kinase function and substrate definition. EMBO J 19(18):4936-43 {{SGDpaper|S000059161}} PMID 10990457</ref><ref name='S000060188'>Vincent O, et al. (2001) Subcellular localization of the Snf1 kinase is regulated by specific beta subunits and a novel glucose signaling mechanism. Genes Dev 15(9):1104-14 {{SGDpaper|S000060188}} PMID 11331606</ref><ref name='S000072977'>Lin SS, et al. (2003) Sip2, an N-myristoylated beta subunit of Snf1 kinase, regulates aging in Saccharomyces cerevisiae by affecting cellular histone kinase activity, recombination at rDNA loci, and silencing. J Biol Chem 278(15):13390-7
+'''Description of YGL208W:''' One of three beta subunits of the Snf1 serine/threonine protein kinase complex involved in the response to glucose starvation; null mutants exhibit accelerated aging; N-myristoylprotein localized to the cytoplasm and the plasma membrane<ref name='S000049850'>Ashrafi K, et al. (2000) Sip2p and its partner snf1p kinase affect aging in S. cerevisiae. Genes Dev 14(15):1872-85 {{SGDpaper|S000049850}} PMID 10921902</ref><ref name='S000072977'>Lin SS, et al. (2003) Sip2, an N-myristoylated beta subunit of Snf1 kinase, regulates aging in Saccharomyces cerevisiae by affecting cellular histone kinase activity, recombination at rDNA loci, and silencing. J Biol Chem 278(15):13390-7 {{SGDpaper|S000072977}} PMID 12562756</ref><ref name='S000059161'>Schmidt MC and McCartney RR (2000) beta-subunits of Snf1 kinase are required for kinase function and substrate definition. EMBO J 19(18):4936-43 {{SGDpaper|S000059161}} PMID 10990457</ref><ref name='S000060188'>Vincent O, et al. (2001) Subcellular localization of the Snf1 kinase is regulated by specific beta subunits and a novel glucose signaling mechanism. Genes Dev 15(9):1104-14
- {{SGDpaper|S000072977}} PMID 12562756</ref>
+ {{SGDpaper|S000060188}} PMID 11331606</ref>
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 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YGL208W:''' One of three beta subunits of the Snf1 serine/threonine protein kinase complex involved in the response to glucose starvation; null mutants exhibit accelerated aging; N-myristoylprotein localized to the cytoplasm and the plasma membrane<ref name='S000072977'>Lin SS, et al. (2003) Sip2, an N-myristoylated beta subunit of Snf1 kinase, regulates aging in Saccharomyces cerevisiae by affecting cellular histone kinase activity, recombination at rDNA loci, and silencing. J Biol Chem 278(15):13390-7 {{SGDpaper|S000072977}} PMID 12562756</ref><ref name='S000060188'>Vincent O, et al. (2001) Subcellular localization of the Snf1 kinase is regulated by specific beta subunits and a novel glucose signaling mechanism. Genes Dev 15(9):1104-14 {{SGDpaper|S000060188}} PMID 11331606</ref><ref name='S000059161'>Schmidt MC and McCartney RR (2000) beta-subunits of Snf1 kinase are required for kinase function and substrate definition. EMBO J 19(18):4936-43 {{SGDpaper|S000059161}} PMID 10990457</ref><ref name='S000049850'>Ashrafi K, et al. (2000) Sip2p and its partner snf1p kinase affect aging in S. cerevisiae. Genes Dev 14(15):1872-85
+'''Description of YGL208W:''' One of three beta subunits of the Snf1 serine/threonine protein kinase complex involved in the response to glucose starvation; null mutants exhibit accelerated aging; N-myristoylprotein localized to the cytoplasm and the plasma membrane<ref name='S000049850'>Ashrafi K, et al. (2000) Sip2p and its partner snf1p kinase affect aging in S. cerevisiae. Genes Dev 14(15):1872-85 {{SGDpaper|S000049850}} PMID 10921902</ref><ref name='S000059161'>Schmidt MC and McCartney RR (2000) beta-subunits of Snf1 kinase are required for kinase function and substrate definition. EMBO J 19(18):4936-43 {{SGDpaper|S000059161}} PMID 10990457</ref><ref name='S000060188'>Vincent O, et al. (2001) Subcellular localization of the Snf1 kinase is regulated by specific beta subunits and a novel glucose signaling mechanism. Genes Dev 15(9):1104-14 {{SGDpaper|S000060188}} PMID 11331606</ref><ref name='S000072977'>Lin SS, et al. (2003) Sip2, an N-myristoylated beta subunit of Snf1 kinase, regulates aging in Saccharomyces cerevisiae by affecting cellular histone kinase activity, recombination at rDNA loci, and silencing. J Biol Chem 278(15):13390-7
-  {{SGDpaper|S000049850}} PMID 10921902</ref>
+  {{SGDpaper|S000072977}} PMID 12562756</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YGL208W:''' One of three beta subunits of the Snf1 serine/threonine protein kinase complex involved in the response to glucose starvation; null mutants exhibit accelerated aging; N-myristoylprotein localized to the cytoplasm and the plasma membrane<ref name='S000049850'>Ashrafi K, et al. (2000) Sip2p and its partner snf1p kinase affect aging in S. cerevisiae. Genes Dev 14(15):1872-85 {{SGDpaper|S000049850}} PMID 10921902</ref><ref name='S000059161'>Schmidt MC and McCartney RR (2000) beta-subunits of Snf1 kinase are required for kinase function and substrate definition. EMBO J 19(18):4936-43 {{SGDpaper|S000059161}} PMID 10990457</ref><ref name='S000060188'>Vincent O, et al. (2001) Subcellular localization of the Snf1 kinase is regulated by specific beta subunits and a novel glucose signaling mechanism. Genes Dev 15(9):1104-14 {{SGDpaper|S000060188}} PMID 11331606</ref><ref name='S000072977'>Lin SS, et al. (2003) Sip2, an N-myristoylated beta subunit of Snf1 kinase, regulates aging in Saccharomyces cerevisiae by affecting cellular histone kinase activity, recombination at rDNA loci, and silencing. J Biol Chem 278(15):13390-7
+'''Description of YGL208W:''' One of three beta subunits of the Snf1 serine/threonine protein kinase complex involved in the response to glucose starvation; null mutants exhibit accelerated aging; N-myristoylprotein localized to the cytoplasm and the plasma membrane<ref name='S000072977'>Lin SS, et al. (2003) Sip2, an N-myristoylated beta subunit of Snf1 kinase, regulates aging in Saccharomyces cerevisiae by affecting cellular histone kinase activity, recombination at rDNA loci, and silencing. J Biol Chem 278(15):13390-7 {{SGDpaper|S000072977}} PMID 12562756</ref><ref name='S000060188'>Vincent O, et al. (2001) Subcellular localization of the Snf1 kinase is regulated by specific beta subunits and a novel glucose signaling mechanism. Genes Dev 15(9):1104-14 {{SGDpaper|S000060188}} PMID 11331606</ref><ref name='S000059161'>Schmidt MC and McCartney RR (2000) beta-subunits of Snf1 kinase are required for kinase function and substrate definition. EMBO J 19(18):4936-43 {{SGDpaper|S000059161}} PMID 10990457</ref><ref name='S000049850'>Ashrafi K, et al. (2000) Sip2p and its partner snf1p kinase affect aging in S. cerevisiae. Genes Dev 14(15):1872-85
-  {{SGDpaper|S000072977}} PMID 12562756</ref>
+  {{SGDpaper|S000049850}} PMID 10921902</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>
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	<protect>		<protect>

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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 |nowrap| Chr VII:97342..98589
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