Difference between revisions of "YMR200W"
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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=S000004813 YMR200W] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''ROT1 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''ROT1 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr XIII: | + | |nowrap| Chr XIII:664752..665522 |
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| − | | | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000004813 |
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| − | '''Description of | + | '''Description of YMR200W:''' Molecular chaperone involved in protein folding in the ER; mutation causes defects in cell wall synthesis and in lysis of autophagic bodies, suppresses tor2 mutations, and is synthetically lethal with kar2-1 and with rot2 mutations; involved in N-linked glycosylation and O-mannosylation<ref name='S000050727'>Bickle M, et al. (1998) Cell wall integrity modulates RHO1 activity via the exchange factor ROM2. EMBO J 17(8):2235-45 {{SGDpaper|S000050727}} PMID 9545237</ref><ref name='S000149082'>Pasikowska M, et al. (2012) The essential endoplasmic reticulum chaperone Rot1 is required for protein N- and O-glycosylation in yeast. Glycobiology () {{SGDpaper|S000149082}} PMID 22492205</ref><ref name='S000117379'>Takeuchi M, et al. (2006) Causal links between protein folding in the ER and events along the secretory pathway. Autophagy 2(4):323-4 {{SGDpaper|S000117379}} PMID 16874095</ref><ref name='S000114705'>Takeuchi M, et al. (2006) Saccharomyces cerevisiae Rot1p is an ER-localized membrane protein that may function with BiP/Kar2p in protein folding. J Biochem 139(3):597-605 {{SGDpaper|S000114705}} PMID 16567426</ref><ref name='S000126534'>Takeuchi M, et al. (2008) Saccharomyces cerevisiae Rot1 Is an Essential Molecular Chaperone in the Endoplasmic Reticulum. Mol Biol Cell 19(8):3514-25 |
| − | {{SGDpaper| | + | {{SGDpaper|S000126534}} PMID 18508919</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 13:05, 26 April 2012
Share your knowledge...Edit this entry! <protect>
| Systematic name | YMR200W |
| Gene name | ROT1 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr XIII:664752..665522 |
| Primary SGDID | S000004813 |
Description of YMR200W: Molecular chaperone involved in protein folding in the ER; mutation causes defects in cell wall synthesis and in lysis of autophagic bodies, suppresses tor2 mutations, and is synthetically lethal with kar2-1 and with rot2 mutations; involved in N-linked glycosylation and O-mannosylation[1][2][3][4][5]
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Contents
Community Commentary
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References
See Help:References on how to add references
- ↑ Bickle M, et al. (1998) Cell wall integrity modulates RHO1 activity via the exchange factor ROM2. EMBO J 17(8):2235-45 SGD PMID 9545237
- ↑ Pasikowska M, et al. (2012) The essential endoplasmic reticulum chaperone Rot1 is required for protein N- and O-glycosylation in yeast. Glycobiology () SGD PMID 22492205
- ↑ Takeuchi M, et al. (2006) Causal links between protein folding in the ER and events along the secretory pathway. Autophagy 2(4):323-4 SGD PMID 16874095
- ↑ Takeuchi M, et al. (2006) Saccharomyces cerevisiae Rot1p is an ER-localized membrane protein that may function with BiP/Kar2p in protein folding. J Biochem 139(3):597-605 SGD PMID 16567426
- ↑ Takeuchi M, et al. (2008) Saccharomyces cerevisiae Rot1 Is an Essential Molecular Chaperone in the Endoplasmic Reticulum. Mol Biol Cell 19(8):3514-25 SGD PMID 18508919
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