Difference between revisions of "YOL088C"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YOL088C YOL088C]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005448 YOL088C]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''MPD2 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''MPD2 ''
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|nowrap| Chr XV:154745..153912
 
|nowrap| Chr XV:154745..153912
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000005448
 
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'''Description of {{PAGENAME}}:''' Member of the protein disulfide isomerase (PDI) family, exhibits chaperone activity; overexpression suppresses the lethality of a pdi1 deletion but does not complement all Pdi1p functions; undergoes oxidation by Ero1p<ref name='S000076703'>Kimura T, et al. (2004) Functional differences between human and yeast protein disulfide isomerase family proteins. Biochem Biophys Res Commun 320(2):359-65 {{SGDpaper|S000076703}} PMID 15219835</ref><ref name='S000053250'>Tachikawa H, et al. (1997) Overproduction of Mpd2p suppresses the lethality of protein disulfide isomerase depletion in a CXXC sequence dependent manner. Biochem Biophys Res Commun 239(3):710-4 {{SGDpaper|S000053250}} PMID 9367834</ref><ref name='S000044010'>Frand AR and Kaiser CA (1999) Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum. Mol Cell 4(4):469-77
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'''Description of YOL088C:''' Member of the protein disulfide isomerase (PDI) family, exhibits chaperone activity; overexpression suppresses the lethality of a pdi1 deletion but does not complement all Pdi1p functions; undergoes oxidation by Ero1p<ref name='S000044010'>Frand AR and Kaiser CA (1999) Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum. Mol Cell 4(4):469-77 {{SGDpaper|S000044010}} PMID 10549279</ref><ref name='S000076703'>Kimura T, et al. (2004) Functional differences between human and yeast protein disulfide isomerase family proteins. Biochem Biophys Res Commun 320(2):359-65 {{SGDpaper|S000076703}} PMID 15219835</ref><ref name='S000053250'>Tachikawa H, et al. (1997) Overproduction of Mpd2p suppresses the lethality of protein disulfide isomerase depletion in a CXXC sequence dependent manner. Biochem Biophys Res Commun 239(3):710-4
{{SGDpaper|S000044010}} PMID 10549279</ref>
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{{SGDpaper|S000053250}} PMID 9367834</ref>
 
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==Community Commentary==
 
==Community Commentary==
 
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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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==References==
 
==References==
 
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Latest revision as of 07:45, 23 January 2012

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Systematic name YOL088C
Gene name MPD2
Aliases
Feature type ORF, Verified
Coordinates Chr XV:154745..153912
Primary SGDID S000005448


Description of YOL088C: Member of the protein disulfide isomerase (PDI) family, exhibits chaperone activity; overexpression suppresses the lethality of a pdi1 deletion but does not complement all Pdi1p functions; undergoes oxidation by Ero1p[1][2][3]




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Community Commentary

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References

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  1. Frand AR and Kaiser CA (1999) Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum. Mol Cell 4(4):469-77 SGD PMID 10549279
  2. Kimura T, et al. (2004) Functional differences between human and yeast protein disulfide isomerase family proteins. Biochem Biophys Res Commun 320(2):359-65 SGD PMID 15219835
  3. Tachikawa H, et al. (1997) Overproduction of Mpd2p suppresses the lethality of protein disulfide isomerase depletion in a CXXC sequence dependent manner. Biochem Biophys Res Commun 239(3):710-4 SGD PMID 9367834

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