Difference between revisions of "YKL191W"

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{|{{Prettytable}} align = 'right' width = '200px'
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YKL191W YKL191W]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000001674 YKL191W]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''DPH2 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''DPH2 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr XI:81040..82644
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|nowrap| Chr XI:81035..82639
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000001674
 
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'''Description of {{PAGENAME}}:''' Protein required, along with Dph1p, Kti11p, Jjj3p, and Dph5p, for synthesis of diphthamide, which is a modified histidine residue of translation elongation factor 2 (Eft1p or Eft2p); may act in a complex with Dph1p and Kti11p<ref name='S000079857'>Liu S, et al. (2004) Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2. Mol Cell Biol 24(21):9487-97 {{SGDpaper|S000079857}} PMID 15485916</ref><ref name='S000074040'>Fichtner L, et al. (2003) Elongator's toxin-target (TOT) function is nuclear localization sequence dependent and suppressed by post-translational modification. Mol Microbiol 49(5):1297-307 {{SGDpaper|S000074040}} PMID 12940988</ref><ref name='S000041529'>Mattheakis LC, et al. (1993) Diphthamide synthesis in Saccharomyces cerevisiae: structure of the DPH2 gene. Gene 132(1):149-54
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'''Description of YKL191W:''' Protein required, along with Dph1p, Kti11p, Jjj3p, and Dph5p, for synthesis of diphthamide, which is a modified histidine residue of translation elongation factor 2 (Eft1p or Eft2p); may act in a complex with Dph1p and Kti11p<ref name='S000074040'>Fichtner L, et al. (2003) Elongator's toxin-target (TOT) function is nuclear localization sequence dependent and suppressed by post-translational modification. Mol Microbiol 49(5):1297-307 {{SGDpaper|S000074040}} PMID 12940988</ref><ref name='S000079857'>Liu S, et al. (2004) Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2. Mol Cell Biol 24(21):9487-97 {{SGDpaper|S000079857}} PMID 15485916</ref><ref name='S000041529'>Mattheakis LC, et al. (1993) Diphthamide synthesis in Saccharomyces cerevisiae: structure of the DPH2 gene. Gene 132(1):149-54
 
  {{SGDpaper|S000041529}} PMID 8406038</ref>
 
  {{SGDpaper|S000041529}} PMID 8406038</ref>
 
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==Community Commentary==
 
==Community Commentary==
 
{{CommentaryHelp}}
 
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<!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation -->
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<!--
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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 YKL191W
Gene name DPH2
Aliases
Feature type ORF, Verified
Coordinates Chr XI:81035..82639
Primary SGDID S000001674


Description of YKL191W: Protein required, along with Dph1p, Kti11p, Jjj3p, and Dph5p, for synthesis of diphthamide, which is a modified histidine residue of translation elongation factor 2 (Eft1p or Eft2p); may act in a complex with Dph1p and Kti11p[1][2][3]




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Community Commentary

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References

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  1. Fichtner L, et al. (2003) Elongator's toxin-target (TOT) function is nuclear localization sequence dependent and suppressed by post-translational modification. Mol Microbiol 49(5):1297-307 SGD PMID 12940988
  2. Liu S, et al. (2004) Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2. Mol Cell Biol 24(21):9487-97 SGD PMID 15485916
  3. Mattheakis LC, et al. (1993) Diphthamide synthesis in Saccharomyces cerevisiae: structure of the DPH2 gene. Gene 132(1):149-54 SGD PMID 8406038

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