Difference between revisions of "YMR274C"

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{|{{Prettytable}} align = 'right' width = '200px'
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YMR274C YMR274C]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004887 YMR274C]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''RCE1 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''RCE1 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr XIII:815310..814363
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|nowrap| Chr XIII:815311..814364
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000004887
 
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'''Description of {{PAGENAME}}:''' Type II CAAX prenyl protease involved in the proteolysis and maturation of Ras and the a-factor mating pheromone<ref name='S000078321'>Pei J and Grishin NV (2001) Type II CAAX prenyl endopeptidases belong to a novel superfamily of putative membrane-bound metalloproteases. Trends Biochem Sci 26(5):275-7 {{SGDpaper|S000078321}} PMID 11343912</ref><ref name='S000048235'>Boyartchuk VL, et al. (1997) Modulation of Ras and a-factor function by carboxyl-terminal proteolysis. Science 275(5307):1796-800 {{SGDpaper|S000048235}} PMID 9065405</ref><ref name='S000046992'>Trueblood CE, et al. (2000) The CaaX proteases, Afc1p and Rce1p, have overlapping but distinct substrate specificities. Mol Cell Biol 20(12):4381-92
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'''Description of YMR274C:''' Type II CAAX prenyl protease involved in the proteolysis and maturation of Ras and the a-factor mating pheromone<ref name='S000048235'>Boyartchuk VL, et al. (1997) Modulation of Ras and a-factor function by carboxyl-terminal proteolysis. Science 275(5307):1796-800 {{SGDpaper|S000048235}} PMID 9065405</ref><ref name='S000078321'>Pei J and Grishin NV (2001) Type II CAAX prenyl endopeptidases belong to a novel superfamily of putative membrane-bound metalloproteases. Trends Biochem Sci 26(5):275-7 {{SGDpaper|S000078321}} PMID 11343912</ref><ref name='S000046992'>Trueblood CE, et al. (2000) The CaaX proteases, Afc1p and Rce1p, have overlapping but distinct substrate specificities. Mol Cell Biol 20(12):4381-92
 
  {{SGDpaper|S000046992}} PMID 10825201</ref>
 
  {{SGDpaper|S000046992}} PMID 10825201</ref>
 
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==Community Commentary==
 
==Community Commentary==
 
{{CommentaryHelp}}
 
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<!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation -->
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<!--
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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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Latest revision as of 07:45, 23 January 2012

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Systematic name YMR274C
Gene name RCE1
Aliases
Feature type ORF, Verified
Coordinates Chr XIII:815311..814364
Primary SGDID S000004887


Description of YMR274C: Type II CAAX prenyl protease involved in the proteolysis and maturation of Ras and the a-factor mating pheromone[1][2][3]




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Community Commentary

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References

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  1. Boyartchuk VL, et al. (1997) Modulation of Ras and a-factor function by carboxyl-terminal proteolysis. Science 275(5307):1796-800 SGD PMID 9065405
  2. Pei J and Grishin NV (2001) Type II CAAX prenyl endopeptidases belong to a novel superfamily of putative membrane-bound metalloproteases. Trends Biochem Sci 26(5):275-7 SGD PMID 11343912
  3. Trueblood CE, et al. (2000) The CaaX proteases, Afc1p and Rce1p, have overlapping but distinct substrate specificities. Mol Cell Biol 20(12):4381-92 SGD PMID 10825201

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