Difference between revisions of "YMR272C"
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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=S000004885 YMR272C] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''SCS7 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''SCS7 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
− | |nowrap| Chr XIII: | + | |nowrap| Chr XIII:810777..809623 |
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− | | | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000004885 |
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− | '''Description of | + | '''Description of YMR272C:''' Sphingolipid alpha-hydroxylase, functions in the alpha-hydroxylation of sphingolipid-associated very long chain fatty acids, has both cytochrome b5-like and hydroxylase/desaturase domains, not essential for growth<ref name='S000050220'>Haak D, et al. (1997) Hydroxylation of Saccharomyces cerevisiae ceramides requires Sur2p and Scs7p. J Biol Chem 272(47):29704-10 {{SGDpaper|S000050220}} PMID 9368039</ref><ref name='S000048699'>Hama H, et al. (2000) Requirement of sphingolipid alpha-hydroxylation for fungicidal action of syringomycin E. FEBS Lett 478(1-2):26-8 {{SGDpaper|S000048699}} PMID 10922463</ref><ref name='S000039246'>Mitchell AG and Martin CE (1997) Fah1p, a Saccharomyces cerevisiae cytochrome b5 fusion protein, and its Arabidopsis thaliana homolog that lacks the cytochrome b5 domain both function in the alpha-hydroxylation of sphingolipid-associated very long chain fatty acids. J Biol Chem 272(45):28281-8 |
{{SGDpaper|S000039246}} PMID 9353282</ref> | {{SGDpaper|S000039246}} PMID 9353282</ref> | ||
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==Community Commentary== | ==Community Commentary== | ||
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+ | Specifically higher expression in carbon limited chemostat cultures versus carbon excess. | ||
+ | <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. | ||
+ | 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
Share your knowledge...Edit this entry! <protect>
Systematic name | YMR272C |
Gene name | SCS7 |
Aliases | FAH1 |
Feature type | ORF, Verified |
Coordinates | Chr XIII:810777..809623 |
Primary SGDID | S000004885 |
Description of YMR272C: Sphingolipid alpha-hydroxylase, functions in the alpha-hydroxylation of sphingolipid-associated very long chain fatty acids, has both cytochrome b5-like and hydroxylase/desaturase domains, not essential for growth[1][2][3]
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Contents
Community Commentary
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References
See Help:References on how to add references
- ↑ Haak D, et al. (1997) Hydroxylation of Saccharomyces cerevisiae ceramides requires Sur2p and Scs7p. J Biol Chem 272(47):29704-10 SGD PMID 9368039
- ↑ Hama H, et al. (2000) Requirement of sphingolipid alpha-hydroxylation for fungicidal action of syringomycin E. FEBS Lett 478(1-2):26-8 SGD PMID 10922463
- ↑ Mitchell AG and Martin CE (1997) Fah1p, a Saccharomyces cerevisiae cytochrome b5 fusion protein, and its Arabidopsis thaliana homolog that lacks the cytochrome b5 domain both function in the alpha-hydroxylation of sphingolipid-associated very long chain fatty acids. J Biol Chem 272(45):28281-8 SGD PMID 9353282
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