Difference between revisions of "YPL004C"
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| − | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http:// | + | |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: | + | |nowrap| Chr XVI:551657..550632 |
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| + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000005925 | ||
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| − | '''Description of | + | '''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| | + | {{SGDpaper|S000145807}} PMID 21685922</ref> |
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J Biol Chem 278(5):3265-74</ref> | J Biol Chem 278(5):3265-74</ref> | ||
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Latest revision as of 06:45, 23 January 2012
Share your knowledge...Edit this entry! <protect>
| 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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- ↑ Walther TC, et al. (2006) Eisosomes mark static sites of endocytosis. Nature 439(7079):998-1003 SGD PMID 16496001
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ submitted by Steffen Ohlmeier on 2004-04-08
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