Difference between revisions of "YDR385W"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YDR385W YDR385W]  
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|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:1243222..1245750
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|nowrap| Chr IV:1243230..1245758
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000002793
 
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'''Description of {{PAGENAME}}:''' 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='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|S000055796}} PMID 1730643</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
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'''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|S000044567}} PMID 9452424</ref>
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  {{SGDpaper|S000055796}} PMID 1730643</ref>
 
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==Community Commentary==
 
==Community Commentary==
 
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<!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation -->
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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 06:45, 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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  1. Dunlop PC and Bodley JW (1983) Biosynthetic labeling of diphthamide in Saccharomyces cerevisiae. J Biol Chem 258(8):4754-8 SGD PMID 6339504
  2. 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
  3. 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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