Difference between revisions of "YMR200W"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YMR200W YMR200W]  
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|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'''
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|nowrap| Chr XIII:664751..665521
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|nowrap| Chr XIII:664752..665522
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000004813
 
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'''Description of {{PAGENAME}}:''' Essential ER membrane protein; may be involved in protein folding; 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<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 (Tokyo) 139(3):597-605 {{SGDpaper|S000114705}} PMID 16567426</ref><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
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'''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
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  {{SGDpaper|S000050727}} PMID 9545237</ref>
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  {{SGDpaper|S000126534}} PMID 18508919</ref>
 
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==Community Commentary==
 
==Community Commentary==
 
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<!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation -->
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Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
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<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.
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J Biol Chem 278(5):3265-74</ref>
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Latest revision as of 14:05, 26 April 2012

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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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Community Commentary

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References

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  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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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