Difference between revisions of "YAL030W"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YAL030W YAL030W]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000000028 YAL030W]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''SNC1 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''SNC1 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr I:87287..87753
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|nowrap| Chr I:87286..87752
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000000028
 
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'''Description of {{PAGENAME}}:''' Vesicle membrane receptor protein (v-SNARE) involved in the fusion between Golgi-derived secretory vesicles with the plasma membrane; proposed to be involved in endocytosis; member of the synaptobrevin/VAMP family of R-type v-SNARE proteins<ref name='S000059602'>Gurunathan S, et al. (2000) Yeast exocytic v-SNAREs confer endocytosis. Mol Biol Cell 11(10):3629-43 {{SGDpaper|S000059602}} PMID 11029060</ref><ref name='S000043829'>Protopopov V, et al. (1993) Homologs of the synaptobrevin/VAMP family of synaptic vesicle proteins function on the late secretory pathway in S. cerevisiae. Cell 74(5):855-61 {{SGDpaper|S000043829}} PMID 8374953</ref><ref name='S000043234'>David D, et al. (1998) Involvement of long chain fatty acid elongation in the trafficking of secretory vesicles in yeast. J Cell Biol 143(5):1167-82
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'''Description of YAL030W:''' Vesicle membrane receptor protein (v-SNARE); involved in the fusion between Golgi-derived secretory vesicles with the plasma membrane; proposed to be involved in endocytosis; member of the synaptobrevin/VAMP family of R-type v-SNARE proteins; SNC1 has a paralog, SNC2, that arose from the whole genome duplication<ref name='S000113653'>Byrne KP and Wolfe KH (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61 {{SGDpaper|S000113653}} PMID 16169922</ref><ref name='S000043234'>David D, et al. (1998) Involvement of long chain fatty acid elongation in the trafficking of secretory vesicles in yeast. J Cell Biol 143(5):1167-82 {{SGDpaper|S000043234}} PMID 9832547</ref><ref name='S000059602'>Gurunathan S, et al. (2000) Yeast exocytic v-SNAREs confer endocytosis. Mol Biol Cell 11(10):3629-43 {{SGDpaper|S000059602}} PMID 11029060</ref><ref name='S000043829'>Protopopov V, et al. (1993) Homologs of the synaptobrevin/VAMP family of synaptic vesicle proteins function on the late secretory pathway in S. cerevisiae. Cell 74(5):855-61
{{SGDpaper|S000043234}} PMID 9832547</ref>
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{{SGDpaper|S000043829}} PMID 8374953</ref>
 
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==Community Commentary==
 
==Community Commentary==
 
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Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
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<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.
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J Biol Chem 278(5):3265-74</ref>
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==References==
 
==References==
 
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Latest revision as of 13:05, 21 August 2012

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Systematic name YAL030W
Gene name SNC1
Aliases
Feature type ORF, Verified
Coordinates Chr I:87286..87752
Primary SGDID S000000028


Description of YAL030W: Vesicle membrane receptor protein (v-SNARE); involved in the fusion between Golgi-derived secretory vesicles with the plasma membrane; proposed to be involved in endocytosis; member of the synaptobrevin/VAMP family of R-type v-SNARE proteins; SNC1 has a paralog, SNC2, that arose from the whole genome duplication[1][2][3][4]




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Community Commentary

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References

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  1. Byrne KP and Wolfe KH (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61 SGD PMID 16169922
  2. David D, et al. (1998) Involvement of long chain fatty acid elongation in the trafficking of secretory vesicles in yeast. J Cell Biol 143(5):1167-82 SGD PMID 9832547
  3. Gurunathan S, et al. (2000) Yeast exocytic v-SNAREs confer endocytosis. Mol Biol Cell 11(10):3629-43 SGD PMID 11029060
  4. Protopopov V, et al. (1993) Homologs of the synaptobrevin/VAMP family of synaptic vesicle proteins function on the late secretory pathway in S. cerevisiae. Cell 74(5):855-61 SGD PMID 8374953

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