YPL004C - 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=S000005925 YPL004C]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005925 YPL004C]
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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''LSP1 ''

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 |}
 <br>
-'''Description of YPL004C:''' Primary component of eisosomes, which are large immobile patch structures at the cell cortex associated with endocytosis, along with Pil1p and Sur7p; null mutants show activation of Pkc1p/Ypk1p stress resistance pathways<ref name='S000114479'>Walther TC, et al. (2006) Eisosomes mark static sites of endocytosis. Nature 439(7079):998-1003 {{SGDpaper|S000114479}} PMID 16496001</ref><ref name='S000076362'>Zhang X, et al. (2004) Pil1p and Lsp1p negatively regulate the 3-phosphoinositide-dependent protein kinase-like kinase Pkh1p and downstream signaling pathways Pkc1p and Ypk1p. J Biol Chem 279(21):22030-8
+'''Description of YPL004C:''' Primary component of eisosomes, which are large immobile patch structures at the cell cortex associated with endocytosis, along with Pil1p and Sur7p; null mutants show activation of Pkc1p/Ypk1p stress resistance pathways; member of the BAR domain family<ref name='S000114479'>Walther TC, et al. (2006) Eisosomes mark static sites of endocytosis. Nature 439(7079):998-1003 {{SGDpaper|S000114479}} PMID 16496001</ref><ref name='S000076362'>Zhang X, et al. (2004) Pil1p and Lsp1p negatively regulate the 3-phosphoinositide-dependent protein kinase-like kinase Pkh1p and downstream signaling pathways Pkc1p and Ypk1p. J Biol Chem 279(21):22030-8 {{SGDpaper|S000076362}} PMID 15016821</ref><ref name='S000145807'>Ziolkowska NE, et al. (2011) Eisosome-driven plasma membrane organization is mediated by BAR domains.LID - 10.1038/nsmb.2080 [doi] Nat Struct Mol Biol ()
-  {{SGDpaper|S000076362}} PMID 15016821</ref>
+  {{SGDpaper|S000145807}} PMID 21685922</ref>
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 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr XVI:551654..550629
+|nowrap| Chr XVI:551657..550632
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000005925

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YPL004C:''' Primary component of eisosomes, which are large immobile patch structures at the cell cortex associated with endocytosis, along with Pil1p and Sur7p; null mutants show activation of Pkc1p/Ypk1p stress resistance pathways<ref name='S000076362'>Zhang X, et al. (2004) Pil1p and Lsp1p negatively regulate the 3-phosphoinositide-dependent protein kinase-like kinase Pkh1p and downstream signaling pathways Pkc1p and Ypk1p. J Biol Chem 279(21):22030-8 {{SGDpaper|S000076362}} PMID 15016821</ref><ref name='S000114479'>Walther TC, et al. (2006) Eisosomes mark static sites of endocytosis. Nature 439(7079):998-1003
+'''Description of YPL004C:''' Primary component of eisosomes, which are large immobile patch structures at the cell cortex associated with endocytosis, along with Pil1p and Sur7p; null mutants show activation of Pkc1p/Ypk1p stress resistance pathways<ref name='S000114479'>Walther TC, et al. (2006) Eisosomes mark static sites of endocytosis. Nature 439(7079):998-1003 {{SGDpaper|S000114479}} PMID 16496001</ref><ref name='S000076362'>Zhang X, et al. (2004) Pil1p and Lsp1p negatively regulate the 3-phosphoinositide-dependent protein kinase-like kinase Pkh1p and downstream signaling pathways Pkc1p and Ypk1p. J Biol Chem 279(21):22030-8
- {{SGDpaper|S000114479}} PMID 16496001</ref>
+ {{SGDpaper|S000076362}} PMID 15016821</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YPL004C:''' Primary component of eisosomes, which are large immobile patch structures at the cell cortex associated with endocytosis, along with Pil1p and Sur7p; null mutants show activation of Pkc1p/Ypk1p stress resistance pathways<ref name='S000114479'>Walther TC, et al. (2006) Eisosomes mark static sites of endocytosis. Nature 439(7079):998-1003 {{SGDpaper|S000114479}} PMID 16496001</ref><ref name='S000076362'>Zhang X, et al. (2004) Pil1p and Lsp1p negatively regulate the 3-phosphoinositide-dependent protein kinase-like kinase Pkh1p and downstream signaling pathways Pkc1p and Ypk1p. J Biol Chem 279(21):22030-8
+'''Description of YPL004C:''' Primary component of eisosomes, which are large immobile patch structures at the cell cortex associated with endocytosis, along with Pil1p and Sur7p; null mutants show activation of Pkc1p/Ypk1p stress resistance pathways<ref name='S000076362'>Zhang X, et al. (2004) Pil1p and Lsp1p negatively regulate the 3-phosphoinositide-dependent protein kinase-like kinase Pkh1p and downstream signaling pathways Pkc1p and Ypk1p. J Biol Chem 279(21):22030-8 {{SGDpaper|S000076362}} PMID 15016821</ref><ref name='S000114479'>Walther TC, et al. (2006) Eisosomes mark static sites of endocytosis. Nature 439(7079):998-1003
-  {{SGDpaper|S000076362}} PMID 15016821</ref>
+  {{SGDpaper|S000114479}} PMID 16496001</ref>
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 <br>

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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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