Difference between revisions of "YIL103W"
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| − | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl? | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.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:171748..173025 | |nowrap| Chr IX:171748..173025 | ||
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| + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000001365 | ||
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<br> | <br> | ||
| − | '''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='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> | {{SGDpaper|S000074040}} PMID 12940988</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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Revision as of 07:46, 27 February 2007
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| Systematic name | YIL103W |
| Gene name | DPH1 |
| Aliases | KIF48 |
| Feature type | ORF, Verified |
| Coordinates | Chr IX:171748..173025 |
| 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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- ↑ 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
- ↑ 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
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