Difference between revisions of "YKR089C"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YKR089C YKR089C]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.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
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|nowrap| Chr XI:608365..605633
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000001797
 
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'''Description of {{PAGENAME}}:''' 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
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'''Description of YKR089C:''' Multifunctional triacylglycerol lipase, steryl ester hydrolase, and Ca2+-independent phospholipase A2; catalyzes acyl-CoA dependent acylation of LPA to PA; required with Tgl3p for timely bud formation; phosphorylated and activated by Cdc28p<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='S000129072'>Kurat CF, et al. (2009) Cdk1/Cdc28-dependent activation of the major triacylglycerol lipase Tgl4 in yeast links lipolysis to cell-cycle progression. Mol Cell 33(1):53-63 {{SGDpaper|S000129072}} PMID 19150427</ref><ref name='S000133526'>Rajakumari S and Daum G (2010) Multiple functions as lipase, steryl ester hydrolase, phospholipase, and acyltransferase of Tgl4p from the yeast Saccharomyces cerevisiae. J Biol Chem 285(21):15769-76 {{SGDpaper|S000133526}} PMID 20332534</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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__TOC__
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==Community Commentary==
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{{CommentaryHelp}}
 
=== Alleles, Strains, and Phenotypes ===
 
=== Alleles, Strains, and Phenotypes ===
 
[[Category:Topic:Alleles, Strains, and Phenotypes]]
 
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==Community Commentary==
 
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=== Alleles, Strains, and Phenotypes ===
 
[[Category:Topic:Alleles, Strains, and Phenotypes]]
 
==== Multiple Knockout Strains ====
 
[[Category:Topic:Alleles, Strains, and Phenotypes:Multiple Knockout Strains]]
 
'''Together with''': TGL3<br>
 
'''Phenotype(s)''': Loss of function (Null) [[Category:Phenotype:Loss of function (Null)]], Recessive [[Category:Phenotype:Recessive]], Viable [[Category:Phenotype:Viable]]
 
  
tgl3 tgl4 double mutants are unable to degrade triglycerides in lag and early log-phases of growth <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 = 'CAset3132-2006-05-22'>submitted by [http://db.yeastgenome.org/cgi-bin/colleague/colleagueSearch?id=3132 Sepp D. Kohlwein] on 2006-05-22</ref>
 
  
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=== Protein Details ===
 
[[Category:Topic:Protein Details]]
 
==== Protein Function/Process ====
 
[[Category:Topic:Protein Details:Protein Function/Process]]
 
'''Together with''': TGL3<br>
 
  
Triglyceride lipase activity; Functional complementation of tgl4 mutants by murine ATGL, Adipose Triglyceride Lipase <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 = 'CAset3132-2006-05-22'>submitted by [http://db.yeastgenome.org/cgi-bin/colleague/colleagueSearch?id=3132 Sepp D. Kohlwein] on 2006-05-22</ref>
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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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==== Protein Modification ====
 
[[Category:Topic:Protein Details:Protein Modification]]
 
'''Modification(s)''': Phosphorylation [[Category:Modification:Phosphorylation]]
 
  
Identified as an efficient substrate of Clb2-Cdk1-as1 in a screen of a proteomic GST-fusion library. <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> <ref name = 'CAset7903-2004-01-29'>submitted by [http://db.yeastgenome.org/cgi-bin/colleague/colleagueSearch?id=7903 Jeff Ubersax] on 2004-01-29</ref>
 
  
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==References==
 
==References==
 
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Latest revision as of 06:45, 23 January 2012

Share your knowledge...Edit this entry! <protect>

Systematic name YKR089C
Gene name TGL4
Aliases STC1
Feature type ORF, Verified
Coordinates Chr XI:608365..605633
Primary SGDID S000001797


Description of YKR089C: Multifunctional triacylglycerol lipase, steryl ester hydrolase, and Ca2+-independent phospholipase A2; catalyzes acyl-CoA dependent acylation of LPA to PA; required with Tgl3p for timely bud formation; phosphorylated and activated by Cdc28p[1][2][3][4]




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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] [5]


Protein Details

Protein Function/Process

Together with: TGL3

Triglyceride lipase activity; Functional complementation of tgl4 mutants by murine ATGL, Adipose Triglyceride Lipase [1] [5]


Protein Modification

Modification(s): Phosphorylation

Identified as an efficient substrate of Clb2-Cdk1-as1 in a screen of a proteomic GST-fusion library. [4] [6]





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References

See Help:References on how to add references

  1. 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
  2. Kurat CF, et al. (2009) Cdk1/Cdc28-dependent activation of the major triacylglycerol lipase Tgl4 in yeast links lipolysis to cell-cycle progression. Mol Cell 33(1):53-63 SGD PMID 19150427
  3. Rajakumari S and Daum G (2010) Multiple functions as lipase, steryl ester hydrolase, phospholipase, and acyltransferase of Tgl4p from the yeast Saccharomyces cerevisiae. J Biol Chem 285(21):15769-76 SGD PMID 20332534
  4. 4.0 4.1 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
  5. 5.0 5.1 submitted by Sepp D. Kohlwein on 2006-05-22
  6. submitted by Jeff Ubersax on 2004-01-29

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