Difference between revisions of "YDR385W"
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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=S000002793 YDR385W] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''EFT2 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''EFT2 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr IV: | + | |nowrap| Chr IV:1243230..1245758 |
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| + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000002793 | ||
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| − | '''Description of | + | '''Description of YDR385W:''' Elongation factor 2 (EF-2), also encoded by EFT1; catalyzes ribosomal translocation during protein synthesis; contains diphthamide, the unique posttranslationally modified histidine residue specifically ADP-ribosylated by diphtheria toxin<ref name='S000062786'>Dunlop PC and Bodley JW (1983) Biosynthetic labeling of diphthamide in Saccharomyces cerevisiae. J Biol Chem 258(8):4754-8 {{SGDpaper|S000062786}} PMID 6339504</ref><ref name='S000044567'>Justice MC, et al. (1998) Elongation factor 2 as a novel target for selective inhibition of fungal protein synthesis. J Biol Chem 273(6):3148-51 {{SGDpaper|S000044567}} PMID 9452424</ref><ref name='S000055796'>Perentesis JP, et al. (1992) Saccharomyces cerevisiae elongation factor 2. Genetic cloning, characterization of expression, and G-domain modeling. J Biol Chem 267(2):1190-7 |
| − | {{SGDpaper| | + | {{SGDpaper|S000055796}} PMID 1730643</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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Latest revision as of 07:45, 23 January 2012
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| Systematic name | YDR385W |
| Gene name | EFT2 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr IV:1243230..1245758 |
| Primary SGDID | S000002793 |
Description of YDR385W: Elongation factor 2 (EF-2), also encoded by EFT1; catalyzes ribosomal translocation during protein synthesis; contains diphthamide, the unique posttranslationally modified histidine residue specifically ADP-ribosylated by diphtheria toxin[1][2][3]
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References
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- ↑ Dunlop PC and Bodley JW (1983) Biosynthetic labeling of diphthamide in Saccharomyces cerevisiae. J Biol Chem 258(8):4754-8 SGD PMID 6339504
- ↑ Justice MC, et al. (1998) Elongation factor 2 as a novel target for selective inhibition of fungal protein synthesis. J Biol Chem 273(6):3148-51 SGD PMID 9452424
- ↑ Perentesis JP, et al. (1992) Saccharomyces cerevisiae elongation factor 2. Genetic cloning, characterization of expression, and G-domain modeling. J Biol Chem 267(2):1190-7 SGD PMID 1730643
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