Difference between revisions of "YOL088C"

From SGD-Wiki
Jump to: navigation, search
(Automated import of articles)
(Automated import of articles)
 
(One intermediate revision by the same user not shown)
Line 4: Line 4:
 
{|{{Prettytable}} align = 'right' width = '200px'
 
{|{{Prettytable}} align = 'right' width = '200px'
 
|-
 
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005448 YOL088C]  
+
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005448 YOL088C]  
 
|-
 
|-
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''MPD2 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''MPD2 ''
Line 18: Line 18:
 
|}
 
|}
 
<br>
 
<br>
'''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='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='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
+
'''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|S000076703}} PMID 15219835</ref>
+
  {{SGDpaper|S000053250}} PMID 9367834</ref>
 
<br>
 
<br>
 
<br>
 
<br>

Latest revision as of 06:45, 23 January 2012

Share your knowledge...Edit this entry! <protect>

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]




</protect>

Community Commentary

About Community Commentary. Please share your knowledge!




<protect>

References

See Help:References on how to add references

  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

See Help:Categories on how to add the wiki page for this gene to a Category </protect>