Difference between revisions of "YLR195C"
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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=S000004185 YLR195C] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''NMT1 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''NMT1 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr XII: | + | |nowrap| Chr XII:543304..541937 |
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| − | | | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000004185 |
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| − | '''Description of | + | '''Description of YLR195C:''' N-myristoyl transferase, catalyzes the cotranslational, covalent attachment of myristic acid to the N-terminal glycine residue of several proteins involved in cellular growth and signal transduction<ref name='S000051384'>Duronio RJ, et al. (1989) Disruption of the yeast N-myristoyl transferase gene causes recessive lethality. Science 243(4892):796-800 {{SGDpaper|S000051384}} PMID 2644694</ref><ref name='S000039761'>Knoll LJ, et al. (1992) Analysis of the compartmentalization of myristoyl-CoA:protein N-myristoyltransferase in Saccharomyces cerevisiae. J Biol Chem 267(8):5366-73 {{SGDpaper|S000039761}} PMID 1544917</ref><ref name='S000044070'>Stone DE, et al. (1991) N-myristoylation is required for function of the pheromone-responsive G alpha protein of yeast: conditional activation of the pheromone response by a temperature-sensitive N-myristoyl transferase. Genes Dev 5(11):1969-81 {{SGDpaper|S000044070}} PMID 1936988</ref><ref name='S000061574'>Towler DA, et al. (1987) Amino-terminal processing of proteins by N-myristoylation. Substrate specificity of N-myristoyl transferase. J Biol Chem 262(3):1030-6 |
| − | {{SGDpaper| | + | {{SGDpaper|S000061574}} PMID 3100524</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
Share your knowledge...Edit this entry! <protect>
| Systematic name | YLR195C |
| Gene name | NMT1 |
| Aliases | CDC72 |
| Feature type | ORF, Verified |
| Coordinates | Chr XII:543304..541937 |
| Primary SGDID | S000004185 |
Description of YLR195C: N-myristoyl transferase, catalyzes the cotranslational, covalent attachment of myristic acid to the N-terminal glycine residue of several proteins involved in cellular growth and signal transduction[1][2][3][4]
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Community Commentary
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References
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- ↑ Duronio RJ, et al. (1989) Disruption of the yeast N-myristoyl transferase gene causes recessive lethality. Science 243(4892):796-800 SGD PMID 2644694
- ↑ Knoll LJ, et al. (1992) Analysis of the compartmentalization of myristoyl-CoA:protein N-myristoyltransferase in Saccharomyces cerevisiae. J Biol Chem 267(8):5366-73 SGD PMID 1544917
- ↑ Stone DE, et al. (1991) N-myristoylation is required for function of the pheromone-responsive G alpha protein of yeast: conditional activation of the pheromone response by a temperature-sensitive N-myristoyl transferase. Genes Dev 5(11):1969-81 SGD PMID 1936988
- ↑ Towler DA, et al. (1987) Amino-terminal processing of proteins by N-myristoylation. Substrate specificity of N-myristoyl transferase. J Biol Chem 262(3):1030-6 SGD PMID 3100524
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