YMR200W - Revision history

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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 for 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
+'''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|S000126534}} PMID 18508919</ref>
 <br>

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 |}
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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<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='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
+'''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 for 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|S000126534}} PMID 18508919</ref>
 <br>

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 {|{{Prettytable}} align = 'right' width = '200px'
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-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004813 YMR200W]
+|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 ''

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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr XIII:664751..665521
+|nowrap| Chr XIII:664752..665522
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000004813

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 |}
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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<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='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='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='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
+'''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<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='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|S000126534}} PMID 18508919</ref>
 <br>

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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.
		+	<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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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 |nowrap| Chr XIII:664751..665521
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 ==Community Commentary==
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