Difference between revisions of "YKL150W"
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| − | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl? | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000001633 YKL150W] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''MCR1 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''MCR1 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
|nowrap| Chr XI:166549..167457 | |nowrap| Chr XI:166549..167457 | ||
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| + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000001633 | ||
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| − | '''Description of | + | '''Description of YKL150W:''' Mitochondrial NADH-cytochrome b5 reductase, involved in ergosterol biosynthesis<ref name='S000062024'>Lamb DC, et al. (1999) Biodiversity of the P450 catalytic cycle: yeast cytochrome b5/NADH cytochrome b5 reductase complex efficiently drives the entire sterol 14-demethylation (CYP51) reaction. FEBS Lett 462(3):283-8 {{SGDpaper|S000062024}} PMID 10622712</ref><ref name='S000046304'>Hahne K, et al. (1994) Incomplete arrest in the outer membrane sorts NADH-cytochrome b5 reductase to two different submitochondrial compartments. Cell 79(5):829-39 |
{{SGDpaper|S000046304}} PMID 8001120</ref> | {{SGDpaper|S000046304}} PMID 8001120</ref> | ||
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J Biol Chem 278(5):3265-74</ref> | J Biol Chem 278(5):3265-74</ref> | ||
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Revision as of 08:46, 27 February 2007
Share your knowledge...Edit this entry! <protect>
| Systematic name | YKL150W |
| Gene name | MCR1 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr XI:166549..167457 |
| Primary SGDID | S000001633 |
Description of YKL150W: Mitochondrial NADH-cytochrome b5 reductase, involved in ergosterol biosynthesis[1][2]
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Community Commentary
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Protein Details
Other Protein Details
Other Topic: Regulated by the diauxic shift (glycerol)
Apart form the overall increase in mitochondrial protein mass after the diauxic shift this protein remains unchanged after the diauxic shift. [3] [4]
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References
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- ↑ Lamb DC, et al. (1999) Biodiversity of the P450 catalytic cycle: yeast cytochrome b5/NADH cytochrome b5 reductase complex efficiently drives the entire sterol 14-demethylation (CYP51) reaction. FEBS Lett 462(3):283-8 SGD PMID 10622712
- ↑ Hahne K, et al. (1994) Incomplete arrest in the outer membrane sorts NADH-cytochrome b5 reductase to two different submitochondrial compartments. Cell 79(5):829-39 SGD PMID 8001120
- ↑ Ohlmeier S, et al. (2004) The yeast mitochondrial proteome, a study of fermentative and respiratory growth. J Biol Chem 279(6):3956-79 SGD PMID 14597615
- ↑ submitted by Steffen Ohlmeier on 2004-04-08
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