Difference between revisions of "YKL150W"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YKL150W YKL150W]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.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
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|nowrap| Chr XI:166544..167452
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000001633
 
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'''Description of {{PAGENAME}}:''' 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
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'''Description of YKL150W:''' Mitochondrial NADH-cytochrome b5 reductase, involved in ergosterol biosynthesis<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><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|S000046304}} PMID 8001120</ref>
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  {{SGDpaper|S000062024}} PMID 10622712</ref>
 
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=== Protein Details ===
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[[Category:Topic:Protein Details]]
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==== Other Protein Details ====
 
[[Category:Topic:Protein Details:Other Protein Details]]
 
'''Other Topic''': Regulated by the diauxic shift (glycerol) [[Category: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. <ref name='S000074509'>Ohlmeier S, et al. (2004) The yeast mitochondrial proteome, a study of fermentative and respiratory growth. J Biol Chem 279(6):3956-79 {{SGDpaper|S000074509}} PMID 14597615</ref> <ref name = 'CAset9949-2004-04-08'>submitted by [http://db.yeastgenome.org/cgi-bin/colleague/colleagueSearch?id=9949 Steffen Ohlmeier] on 2004-04-08</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 YKL150W
Gene name MCR1
Aliases
Feature type ORF, Verified
Coordinates Chr XI:166544..167452
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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  1. 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
  2. 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
  3. 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
  4. submitted by Steffen Ohlmeier on 2004-04-08

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