Difference between revisions of "YKR089C"
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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=S000001797 YKR089C] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''TGL4 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''TGL4 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
|nowrap| Chr XI:608007..605275 | |nowrap| Chr XI:608007..605275 | ||
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+ | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000001797 | ||
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<br> | <br> | ||
− | '''Description of | + | '''Description of YKR089C:''' Triacylglycerol lipase involved in triacylglycerol mobilization and degradation; found in lipid particles; potential Cdc28p substrate<ref name='S000087074'>Kurat CF, et al. (2006) Obese yeast: triglyceride lipolysis is functionally conserved from mammals to yeast. J Biol Chem 281(1):491-500 {{SGDpaper|S000087074}} PMID 16267052</ref><ref name='S000086466'>Athenstaedt K and Daum G (2005) Tgl4p and Tgl5p, two triacylglycerol lipases of the yeast Saccharomyces cerevisiae are localized to lipid particles. J Biol Chem 280(45):37301-9 {{SGDpaper|S000086466}} PMID 16135509</ref><ref name='S000074306'>Ubersax JA, et al. (2003) Targets of the cyclin-dependent kinase Cdk1. Nature 425(6960):859-64 |
{{SGDpaper|S000074306}} PMID 14574415</ref> | {{SGDpaper|S000074306}} PMID 14574415</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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<protect> | <protect> |
Revision as of 07:46, 27 February 2007
Share your knowledge...Edit this entry! <protect>
Systematic name | YKR089C |
Gene name | TGL4 |
Aliases | STC1 |
Feature type | ORF, Verified |
Coordinates | Chr XI:608007..605275 |
Primary SGDID | S000001797 |
Description of YKR089C: Triacylglycerol lipase involved in triacylglycerol mobilization and degradation; found in lipid particles; potential Cdc28p substrate[1][2][3]
</protect>
Contents
Community Commentary
About Community Commentary. Please share your knowledge!
Alleles, Strains, and Phenotypes
Multiple Knockout Strains
Together with: TGL3
Phenotype(s): Loss of function (Null), Recessive, Viable
tgl3 tgl4 double mutants are unable to degrade triglycerides in lag and early log-phases of growth [1] [4]
Protein Details
Protein Function/Process
Together with: TGL3
Triglyceride lipase activity; Functional complementation of tgl4 mutants by murine ATGL, Adipose Triglyceride Lipase [1] [4]
Protein Modification
Modification(s): Phosphorylation
Identified as an efficient substrate of Clb2-Cdk1-as1 in a screen of a proteomic GST-fusion library. [3] [5]
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References
See Help:References on how to add references
- ↑ 1.0 1.1 1.2 Kurat CF, et al. (2006) Obese yeast: triglyceride lipolysis is functionally conserved from mammals to yeast. J Biol Chem 281(1):491-500 SGD PMID 16267052
- ↑ Athenstaedt K and Daum G (2005) Tgl4p and Tgl5p, two triacylglycerol lipases of the yeast Saccharomyces cerevisiae are localized to lipid particles. J Biol Chem 280(45):37301-9 SGD PMID 16135509
- ↑ 3.0 3.1 Ubersax JA, et al. (2003) Targets of the cyclin-dependent kinase Cdk1. Nature 425(6960):859-64
SGD PMID 14574415 Cite error: Invalid
<ref>
tag; name "S000074306" defined multiple times with different content - ↑ 4.0 4.1 submitted by Sepp D. Kohlwein on 2006-05-22
- ↑ submitted by Jeff Ubersax on 2004-01-29
See Help:Categories on how to add the wiki page for this gene to a Category </protect>
- Pages with reference errors
- ORF
- ORF, Verified
- Topic:Alleles, Strains, and Phenotypes
- Topic:Alleles, Strains, and Phenotypes:Multiple Knockout Strains
- Phenotype:Loss of function (Null)
- Phenotype:Recessive
- Phenotype:Viable
- Topic:Protein Details
- Topic:Protein Details:Protein Function/Process
- Topic:Protein Details:Protein Modification
- Modification:Phosphorylation