Difference between revisions of "YIL103W"
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{|{{Prettytable}} align = 'right' width = '200px' | {|{{Prettytable}} align = 'right' width = '200px' | ||
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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=S000001365 YIL103W] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''DPH1 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''DPH1 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
− | |nowrap| Chr IX: | + | |nowrap| Chr IX:171751..173028 |
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+ | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000001365 | ||
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− | '''Description of | + | '''Description of YIL103W:''' Protein required, along with Dph2p, 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 Dph2p 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| | + | {{SGDpaper|S000079857}} PMID 15485916</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 06:45, 23 January 2012
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Systematic name | YIL103W |
Gene name | DPH1 |
Aliases | KIF48 |
Feature type | ORF, Verified |
Coordinates | Chr IX:171751..173028 |
Primary SGDID | S000001365 |
Description of YIL103W: Protein required, along with Dph2p, 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 Dph2p and Kti11p[1][2]
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References
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- ↑ 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
- ↑ 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
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