Difference between revisions of "YKL191W"
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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=' | + | '''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='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><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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Revision as of 04:40, 18 December 2008
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| Systematic name | YKL191W |
| Gene name | DPH2 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr XI:81040..82644 |
| 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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References
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- ↑ Mattheakis LC, et al. (1993) Diphthamide synthesis in Saccharomyces cerevisiae: structure of the DPH2 gene. Gene 132(1):149-54 SGD PMID 8406038
- ↑ 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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