Difference between revisions of "YHR176W"
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| − | '''Description of YHR176W:''' Flavin-containing monooxygenase, localized to the cytoplasmic face of the ER membrane; catalyzes oxidation of biological thiols to maintain the ER redox buffer ratio for correct folding of disulfide-bonded proteins<ref name='S000065744'>Suh JK, et al. (1999) Yeast flavin-containing monooxygenase generates oxidizing equivalents that control protein folding in the endoplasmic reticulum. Proc Natl Acad Sci U S A 96(6):2687-91 {{SGDpaper|S000065744}} PMID 10077572 | + | '''Description of YHR176W:''' Flavin-containing monooxygenase, localized to the cytoplasmic face of the ER membrane; catalyzes oxidation of biological thiols to maintain the ER redox buffer ratio for correct folding of disulfide-bonded proteins<ref name='S000071709'>Zhang M and Robertus JD (2002) Molecular cloning and characterization of a full-length flavin-dependent monooxygenase from yeast. Arch Biochem Biophys 403(2):277-83 {{SGDpaper|S000071709}} PMID 12139977</ref><ref name='S000065744'>Suh JK, et al. (1999) Yeast flavin-containing monooxygenase generates oxidizing equivalents that control protein folding in the endoplasmic reticulum. Proc Natl Acad Sci U S A 96(6):2687-91 |
| − | + | {{SGDpaper|S000065744}} PMID 10077572</ref> | |
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Revision as of 14:05, 16 January 2009
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| Systematic name | YHR176W |
| Gene name | FMO1 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr VIII:454229..455527 |
| Primary SGDID | S000001219 |
Description of YHR176W: Flavin-containing monooxygenase, localized to the cytoplasmic face of the ER membrane; catalyzes oxidation of biological thiols to maintain the ER redox buffer ratio for correct folding of disulfide-bonded proteins[1][2]
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Contents
Community Commentary
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DNA and RNA Details
Other DNA and RNA Details
Other Topic: expression
Specifically higher expression in sulfur limited chemostat cultures versus sulfur excess. [3] [4]
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References
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- ↑ Zhang M and Robertus JD (2002) Molecular cloning and characterization of a full-length flavin-dependent monooxygenase from yeast. Arch Biochem Biophys 403(2):277-83 SGD PMID 12139977
- ↑ Suh JK, et al. (1999) Yeast flavin-containing monooxygenase generates oxidizing equivalents that control protein folding in the endoplasmic reticulum. Proc Natl Acad Sci U S A 96(6):2687-91 SGD PMID 10077572
- ↑ 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 SGD PMID 12414795
- ↑ submitted by Viktor Boer on 2003-07-25
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