Difference between revisions of "YML055W"
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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=S000004519 YML055W] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''SPC2 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''SPC2 '' | ||
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|nowrap| Chr XIII:164790..165326 | |nowrap| Chr XIII:164790..165326 | ||
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| − | | | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000004519 |
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| − | '''Description of | + | '''Description of YML055W:''' Subunit of signal peptidase complex (Spc1p, Spc2p, Spc3p, Sec11p), which catalyzes cleavage of N-terminal signal sequences of proteins targeted to the secretory pathway; homologous to mammalian SPC25<ref name='S000058467'>Antonin W, et al. (2000) Interactions between Spc2p and other components of the endoplasmic reticulum translocation sites of the yeast Saccharomyces cerevisiae. J Biol Chem 275(44):34068-72 {{SGDpaper|S000058467}} PMID 10921929</ref><ref name='S000055094'>Fang H, et al. (1997) In addition to SEC11, a newly identified gene, SPC3, is essential for signal peptidase activity in the yeast endoplasmic reticulum. J Biol Chem 272(20):13152-8 {{SGDpaper|S000055094}} PMID 9148930</ref><ref name='S000055096'>Meyer HA and Hartmann E (1997) The yeast SPC22/23 homolog Spc3p is essential for signal peptidase activity. J Biol Chem 272(20):13159-64 {{SGDpaper|S000055096}} PMID 9148931</ref><ref name='S000047958'>Mullins C, et al. (1996) Structurally related Spc1p and Spc2p of yeast signal peptidase complex are functionally distinct. J Biol Chem 271(46):29094-9 |
{{SGDpaper|S000047958}} PMID 8910564</ref> | {{SGDpaper|S000047958}} PMID 8910564</ref> | ||
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==Community Commentary== | ==Community Commentary== | ||
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| + | 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> | ||
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==References== | ==References== | ||
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Latest revision as of 06:45, 23 January 2012
Share your knowledge...Edit this entry! <protect>
| Systematic name | YML055W |
| Gene name | SPC2 |
| Aliases | SPY1 |
| Feature type | ORF, Verified |
| Coordinates | Chr XIII:164790..165326 |
| Primary SGDID | S000004519 |
Description of YML055W: Subunit of signal peptidase complex (Spc1p, Spc2p, Spc3p, Sec11p), which catalyzes cleavage of N-terminal signal sequences of proteins targeted to the secretory pathway; homologous to mammalian SPC25[1][2][3][4]
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Contents
Community Commentary
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References
See Help:References on how to add references
- ↑ Antonin W, et al. (2000) Interactions between Spc2p and other components of the endoplasmic reticulum translocation sites of the yeast Saccharomyces cerevisiae. J Biol Chem 275(44):34068-72 SGD PMID 10921929
- ↑ Fang H, et al. (1997) In addition to SEC11, a newly identified gene, SPC3, is essential for signal peptidase activity in the yeast endoplasmic reticulum. J Biol Chem 272(20):13152-8 SGD PMID 9148930
- ↑ Meyer HA and Hartmann E (1997) The yeast SPC22/23 homolog Spc3p is essential for signal peptidase activity. J Biol Chem 272(20):13159-64 SGD PMID 9148931
- ↑ Mullins C, et al. (1996) Structurally related Spc1p and Spc2p of yeast signal peptidase complex are functionally distinct. J Biol Chem 271(46):29094-9 SGD PMID 8910564
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