Difference between revisions of "YML130C"
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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=S000004599 YML130C] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''ERO1 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''ERO1 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr XIII: | + | |nowrap| Chr XIII:13174..11483 |
|- | |- | ||
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000004599 | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000004599 | ||
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| − | '''Description of YML130C:''' Thiol oxidase required for oxidative protein folding in the | + | '''Description of YML130C:''' Thiol oxidase required for oxidative protein folding in the ER; essential for maintaining proper redox balance in ER; feedback regulation of Ero1p occurs via reduction and oxidation of Ero1p regulatory bonds; reduced Pdi1p activates Ero1p by direct reduction of Ero1p regulatory bonds; depletion of thiol substrates and accumulation of oxidized Pdi1p results in inactivation of Ero1p by both Pdi1p-mediated oxidation and autonomous oxidation of Ero1p regulatory bonds<ref name='S000053009'>Frand AR and Kaiser CA (1998) The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Mol Cell 1(2):161-70 {{SGDpaper|S000053009}} PMID 9659913</ref><ref name='S000114189'>Gross E, et al. (2006) Generating disulfides enzymatically: reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p. Proc Natl Acad Sci U S A 103(2):299-304 {{SGDpaper|S000114189}} PMID 16407158</ref><ref name='S000150261'>Kim S, et al. (2012) Balanced Ero1 activation and inactivation establishes ER redox homeostasis. J Cell Biol 196(6):713-25 {{SGDpaper|S000150261}} PMID 22412017</ref><ref name='S000053010'>Pollard MG, et al. (1998) Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum. Mol Cell 1(2):171-82 |
{{SGDpaper|S000053010}} PMID 9659914</ref> | {{SGDpaper|S000053010}} PMID 9659914</ref> | ||
<br> | <br> | ||
Latest revision as of 13:05, 13 August 2012
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| Systematic name | YML130C |
| Gene name | ERO1 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr XIII:13174..11483 |
| Primary SGDID | S000004599 |
Description of YML130C: Thiol oxidase required for oxidative protein folding in the ER; essential for maintaining proper redox balance in ER; feedback regulation of Ero1p occurs via reduction and oxidation of Ero1p regulatory bonds; reduced Pdi1p activates Ero1p by direct reduction of Ero1p regulatory bonds; depletion of thiol substrates and accumulation of oxidized Pdi1p results in inactivation of Ero1p by both Pdi1p-mediated oxidation and autonomous oxidation of Ero1p regulatory bonds[1][2][3][4]
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References
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- ↑ Frand AR and Kaiser CA (1998) The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Mol Cell 1(2):161-70 SGD PMID 9659913
- ↑ Gross E, et al. (2006) Generating disulfides enzymatically: reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p. Proc Natl Acad Sci U S A 103(2):299-304 SGD PMID 16407158
- ↑ Kim S, et al. (2012) Balanced Ero1 activation and inactivation establishes ER redox homeostasis. J Cell Biol 196(6):713-25 SGD PMID 22412017
- ↑ Pollard MG, et al. (1998) Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum. Mol Cell 1(2):171-82 SGD PMID 9659914
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