Difference between revisions of "YPL004C"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005925 YPL004C]  
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|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 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''LSP1 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr XVI:551654..550629
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|nowrap| Chr XVI:551657..550632
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000005925
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000005925
 
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'''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
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'''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>
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  {{SGDpaper|S000145807}} PMID 21685922</ref>
 
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Latest revision as of 06:45, 23 January 2012

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Systematic name YPL004C
Gene name LSP1
Aliases
Feature type ORF, Verified
Coordinates Chr XVI:551657..550632
Primary SGDID S000005925


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[1][2][3]




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Protein Details

Protein Localization

Protein identified in a purified mitochondrial extract. [4] [5]




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References

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  1. Walther TC, et al. (2006) Eisosomes mark static sites of endocytosis. Nature 439(7079):998-1003 SGD PMID 16496001
  2. 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 SGD PMID 15016821
  3. 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 () SGD PMID 21685922
  4. Ohlmeier S, et al. (2004) The yeast mitochondrial proteome, a study of fermentative and respiratory growth. J Biol Chem 279(6):3956-79 SGD PMID 14597615
  5. submitted by Steffen Ohlmeier on 2004-04-08

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