Difference between revisions of "YDL213C"
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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://db.yeastgenome.org/cgi-bin/locus.pl? | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002372 YDL213C] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''NOP6 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''NOP6 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
|nowrap| Chr IV:77967..77290 | |nowrap| Chr IV:77967..77290 | ||
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| + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000002372 | ||
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<br> | <br> | ||
| − | '''Description of | + | '''Description of YDL213C:''' Protein with similarity to hydrophilins, which are involved in the adaptive response to hyperosmotic conditions; computational analysis of large-scale protein-protein interaction data suggests a possible role in rRNA processing<ref name='S000074191'>Samanta MP and Liang S (2003) Predicting protein functions from redundancies in large-scale protein interaction networks. Proc Natl Acad Sci U S A 100(22):12579-83 {{SGDpaper|S000074191}} PMID 14566057</ref><ref name='S000063137'>Garay-Arroyo A, et al. (2000) Highly hydrophilic proteins in prokaryotes and eukaryotes are common during conditions of water deficit. J Biol Chem 275(8):5668-74 |
{{SGDpaper|S000063137}} PMID 10681550</ref> | {{SGDpaper|S000063137}} PMID 10681550</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 08:46, 27 February 2007
Share your knowledge...Edit this entry! <protect>
| Systematic name | YDL213C |
| Gene name | NOP6 |
| Aliases | |
| Feature type | ORF, Uncharacterized |
| Coordinates | Chr IV:77967..77290 |
| Primary SGDID | S000002372 |
Description of YDL213C: Protein with similarity to hydrophilins, which are involved in the adaptive response to hyperosmotic conditions; computational analysis of large-scale protein-protein interaction data suggests a possible role in rRNA processing[1][2]
</protect>
Contents
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References
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- ↑ Samanta MP and Liang S (2003) Predicting protein functions from redundancies in large-scale protein interaction networks. Proc Natl Acad Sci U S A 100(22):12579-83 SGD PMID 14566057
- ↑ Garay-Arroyo A, et al. (2000) Highly hydrophilic proteins in prokaryotes and eukaryotes are common during conditions of water deficit. J Biol Chem 275(8):5668-74 SGD PMID 10681550
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