Difference between revisions of "YLR249W"
SGDwikiBot (talk | contribs) (Automated import of articles) |
SGDwikiBot (talk | contribs) (Automated import of articles) |
||
| (7 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
<!-- PLEASE DO NOT EDIT HERE. USE THE SECTION EDIT LINKS ON THE RIGHT MARGIN--> | <!-- PLEASE DO NOT EDIT HERE. USE THE SECTION EDIT LINKS ON THE RIGHT MARGIN--> | ||
{{PageTop}} | {{PageTop}} | ||
| + | <protect> | ||
{|{{Prettytable}} align = 'right' width = '200px' | {|{{Prettytable}} align = 'right' width = '200px' | ||
|- | |- | ||
| − | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http:// | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004239 YLR249W] |
|- | |- | ||
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''YEF3 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''YEF3 '' | ||
| Line 12: | Line 13: | ||
|- | |- | ||
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr XII: | + | |nowrap| Chr XII:636780..639914 |
|- | |- | ||
| − | | | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000004239 |
|} | |} | ||
<br> | <br> | ||
| − | '''Description of | + | '''Description of YLR249W:''' Gamma subunit of translational elongation factor eEF1B, stimulates the binding of aminoacyl-tRNA (AA-tRNA) to ribosomes by releasing eEF1A (Tef1p/Tef2p) from the ribosomal complex; contains two ABC cassettes; binds and hydrolyzes ATP<ref name='S000074362'>Jeppesen MG, et al. (2003) The crystal structure of the glutathione S-transferase-like domain of elongation factor 1Bgamma from Saccharomyces cerevisiae. J Biol Chem 278(47):47190-8 {{SGDpaper|S000074362}} PMID 12972429</ref><ref name='S000056903'>Kamath A and Chakraburtty K (1989) Role of yeast elongation factor 3 in the elongation cycle. J Biol Chem 264(26):15423-8 {{SGDpaper|S000056903}} PMID 2670939</ref><ref name='S000075912'>Miyazaki M, et al. (1986) Intrinsic ATPase activity of yeast peptide chain elongation factor 3(EF-3) and its direct interaction with various nucleotides. Nucleic Acids Symp Ser(17):171-4 {{SGDpaper|S000075912}} PMID 2951656</ref><ref name='S000075900'>Qin SL, et al. (1987) Isolation of the yeast gene encoding elongation factor 3 for protein synthesis. J Biol Chem 262(16):7802-7 |
| − | + | {{SGDpaper|S000075900}} PMID 3034906</ref> | |
<br> | <br> | ||
<br> | <br> | ||
<br> | <br> | ||
<br> | <br> | ||
| − | + | <br> | |
| + | </protect> | ||
__TOC__ | __TOC__ | ||
==Community Commentary== | ==Community Commentary== | ||
{{CommentaryHelp}} | {{CommentaryHelp}} | ||
| + | |||
| + | |||
| + | |||
| + | <!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation --> | ||
| + | <!-- | ||
| + | Specifically higher expression in carbon limited chemostat cultures versus carbon excess. | ||
| + | <ref>Boer VM, et al. (2003) The genome-wide transcriptional responses of Saccharomyces cerevisiae grown on glucose in aerobic chemostat cultures limited for carbon, nitrogen, phosphorus, or sulfur. | ||
| + | J Biol Chem 278(5):3265-74</ref> | ||
| + | --> | ||
| + | |||
| + | |||
| + | |||
| + | <protect> | ||
==References== | ==References== | ||
<!-- REFERENCES ARE AUTOMATICALLY GENERATED. PLEASE DON'T EDIT THIS SECTION--> | <!-- REFERENCES ARE AUTOMATICALLY GENERATED. PLEASE DON'T EDIT THIS SECTION--> | ||
{{RefHelp}} | {{RefHelp}} | ||
| + | </protect> | ||
Latest revision as of 07:45, 23 January 2012
Share your knowledge...Edit this entry! <protect>
| Systematic name | YLR249W |
| Gene name | YEF3 |
| Aliases | TEF3 |
| Feature type | ORF, Verified |
| Coordinates | Chr XII:636780..639914 |
| Primary SGDID | S000004239 |
Description of YLR249W: Gamma subunit of translational elongation factor eEF1B, stimulates the binding of aminoacyl-tRNA (AA-tRNA) to ribosomes by releasing eEF1A (Tef1p/Tef2p) from the ribosomal complex; contains two ABC cassettes; binds and hydrolyzes ATP[1][2][3][4]
</protect>
Contents
Community Commentary
About Community Commentary. Please share your knowledge!
<protect>
References
See Help:References on how to add references
- ↑ Jeppesen MG, et al. (2003) The crystal structure of the glutathione S-transferase-like domain of elongation factor 1Bgamma from Saccharomyces cerevisiae. J Biol Chem 278(47):47190-8 SGD PMID 12972429
- ↑ Kamath A and Chakraburtty K (1989) Role of yeast elongation factor 3 in the elongation cycle. J Biol Chem 264(26):15423-8 SGD PMID 2670939
- ↑ Miyazaki M, et al. (1986) Intrinsic ATPase activity of yeast peptide chain elongation factor 3(EF-3) and its direct interaction with various nucleotides. Nucleic Acids Symp Ser(17):171-4 SGD PMID 2951656
- ↑ Qin SL, et al. (1987) Isolation of the yeast gene encoding elongation factor 3 for protein synthesis. J Biol Chem 262(16):7802-7 SGD PMID 3034906
See Help:Categories on how to add the wiki page for this gene to a Category </protect>
