Difference between revisions of "YMR274C"
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| − | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl? | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.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 | |nowrap| Chr XIII:815310..814363 | ||
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| + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000004887 | ||
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<br> | <br> | ||
| − | '''Description of | + | '''Description of YMR274C:''' 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 |
{{SGDpaper|S000046992}} PMID 10825201</ref> | {{SGDpaper|S000046992}} PMID 10825201</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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Revision as of 07:46, 27 February 2007
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| Systematic name | YMR274C |
| Gene name | RCE1 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr XIII:815310..814363 |
| 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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Contents
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References
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- ↑ 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
- ↑ Boyartchuk VL, et al. (1997) Modulation of Ras and a-factor function by carboxyl-terminal proteolysis. Science 275(5307):1796-800 SGD PMID 9065405
- ↑ 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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