Difference between revisions of "YDL090C"
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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=S000002248 YDL090C] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''RAM1 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''RAM1 '' | ||
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|nowrap| Chr IV:296329..295034 | |nowrap| Chr IV:296329..295034 | ||
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− | | | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000002248 |
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− | '''Description of | + | '''Description of YDL090C:''' Beta subunit of the CAAX farnesyltransferase (FTase) that prenylates the a-factor mating pheromone and Ras proteins; required for the membrane localization of Ras proteins and a-factor; homolog of the mammalian FTase beta subunit<ref name='S000048882'>Gomez R, et al. (1993) Purified yeast protein farnesyltransferase is structurally and functionally similar to its mammalian counterpart. Biochem J 289 ( Pt 1)():25-31 {{SGDpaper|S000048882}} PMID 8424764</ref><ref name='S000050062'>He B, et al. (1991) RAM2, an essential gene of yeast, and RAM1 encode the two polypeptide components of the farnesyltransferase that prenylates a-factor and Ras proteins. Proc Natl Acad Sci U S A 88(24):11373-7 {{SGDpaper|S000050062}} PMID 1763050</ref><ref name='S000052892'>Kohl NE, et al. (1991) Structural homology among mammalian and Saccharomyces cerevisiae isoprenyl-protein transferases. J Biol Chem 266(28):18884-8 {{SGDpaper|S000052892}} PMID 1918005</ref><ref name='S000058250'>Kurth DD, et al. (1997) Functional consequence of mutating conserved residues of the yeast farnesyl-protein transferase beta-subunit Ram1(Dpr1). Biochemistry 36(50):15932-9 {{SGDpaper|S000058250}} PMID 9398327</ref><ref name='S000047476'>Trueblood CE, et al. (1997) Substrate specificity determinants in the farnesyltransferase beta-subunit. Proc Natl Acad Sci U S A 94(20):10774-9 |
{{SGDpaper|S000047476}} PMID 9380709</ref> | {{SGDpaper|S000047476}} PMID 9380709</ref> | ||
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==Community Commentary== | ==Community Commentary== | ||
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+ | Specifically higher expression in carbon limited chemostat cultures versus carbon excess. | ||
+ | <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. | ||
+ | J Biol Chem 278(5):3265-74</ref> | ||
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==References== | ==References== | ||
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Latest revision as of 07:45, 23 January 2012
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Systematic name | YDL090C |
Gene name | RAM1 |
Aliases | DPR1, FUS8, SCG2, SGP2, STE16 |
Feature type | ORF, Verified |
Coordinates | Chr IV:296329..295034 |
Primary SGDID | S000002248 |
Description of YDL090C: Beta subunit of the CAAX farnesyltransferase (FTase) that prenylates the a-factor mating pheromone and Ras proteins; required for the membrane localization of Ras proteins and a-factor; homolog of the mammalian FTase beta subunit[1][2][3][4][5]
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Contents
Community Commentary
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References
See Help:References on how to add references
- ↑ Gomez R, et al. (1993) Purified yeast protein farnesyltransferase is structurally and functionally similar to its mammalian counterpart. Biochem J 289 ( Pt 1)():25-31 SGD PMID 8424764
- ↑ He B, et al. (1991) RAM2, an essential gene of yeast, and RAM1 encode the two polypeptide components of the farnesyltransferase that prenylates a-factor and Ras proteins. Proc Natl Acad Sci U S A 88(24):11373-7 SGD PMID 1763050
- ↑ Kohl NE, et al. (1991) Structural homology among mammalian and Saccharomyces cerevisiae isoprenyl-protein transferases. J Biol Chem 266(28):18884-8 SGD PMID 1918005
- ↑ Kurth DD, et al. (1997) Functional consequence of mutating conserved residues of the yeast farnesyl-protein transferase beta-subunit Ram1(Dpr1). Biochemistry 36(50):15932-9 SGD PMID 9398327
- ↑ Trueblood CE, et al. (1997) Substrate specificity determinants in the farnesyltransferase beta-subunit. Proc Natl Acad Sci U S A 94(20):10774-9 SGD PMID 9380709
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