Difference between revisions of "YPR031W"
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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=S000006235 YPR031W] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''NTO1 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''NTO1 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr XVI: | + | |nowrap| Chr XVI:631515..633761 |
|- | |- | ||
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000006235 | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000006235 | ||
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<br> | <br> | ||
| − | '''Description of YPR031W:''' Subunit of the NuA3 histone acetyltransferase complex that acetylates histone H3; contains PHD finger domain that interacts with methylated histone H3 | + | '''Description of YPR031W:''' Subunit of the NuA3 histone acetyltransferase complex that acetylates histone H3; contains PHD finger domain that interacts with methylated histone H3<ref name='S000119974'>Shi X, et al. (2007) Proteome-wide Analysis in Saccharomyces cerevisiae Identifies Several PHD Fingers as Novel Direct and Selective Binding Modules of Histone H3 Methylated at Either Lysine 4 or Lysine 36. J Biol Chem 282(4):2450-5 {{SGDpaper|S000119974}} PMID 17142463</ref><ref name='S000121976'>Taverna SD, et al. (2006) Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT activity at K14 of H3 and transcription at a subset of targeted ORFs. Mol Cell 24(5):785-96 |
| − | {{SGDpaper| | + | {{SGDpaper|S000121976}} PMID 17157260</ref> |
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<br> | <br> | ||
Latest revision as of 07:45, 23 January 2012
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| Systematic name | YPR031W |
| Gene name | NTO1 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr XVI:631515..633761 |
| Primary SGDID | S000006235 |
Description of YPR031W: Subunit of the NuA3 histone acetyltransferase complex that acetylates histone H3; contains PHD finger domain that interacts with methylated histone H3[1][2]
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References
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- ↑ Shi X, et al. (2007) Proteome-wide Analysis in Saccharomyces cerevisiae Identifies Several PHD Fingers as Novel Direct and Selective Binding Modules of Histone H3 Methylated at Either Lysine 4 or Lysine 36. J Biol Chem 282(4):2450-5 SGD PMID 17142463
- ↑ Taverna SD, et al. (2006) Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT activity at K14 of H3 and transcription at a subset of targeted ORFs. Mol Cell 24(5):785-96 SGD PMID 17157260
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