Difference between revisions of "YIL097W"

From SGD-Wiki
Jump to: navigation, search
(Automated import of articles)
(Automated import of articles)
 
(9 intermediate revisions by the same user not shown)
Line 4: Line 4:
 
{|{{Prettytable}} align = 'right' width = '200px'
 
{|{{Prettytable}} align = 'right' width = '200px'
 
|-
 
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YIL097W YIL097W]  
+
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000001359 YIL097W]  
 
|-
 
|-
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''FYV10 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''FYV10 ''
Line 13: Line 13:
 
|-
 
|-
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr IX:180424..181974
+
|nowrap| Chr IX:180427..181977
 +
|-
 +
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000001359
 
|}
 
|}
 
<br>
 
<br>
'''Description of {{PAGENAME}}:''' Protein of unknown function, required for survival upon exposure to K1 killer toxin; involved in proteasome-dependent catabolite inactivation of fructose-1,6-bisphosphatase; contains CTLH domain<ref name='S000072994'>Page N, et al. (2003) A Saccharomyces cerevisiae genome-wide mutant screen for altered sensitivity to K1 killer toxin. Genetics 163(3):875-94 {{SGDpaper|S000072994}} PMID 12663529</ref><ref name='S000072993'>Regelmann J, et al. (2003) Catabolite degradation of fructose-1,6-bisphosphatase in the yeast Saccharomyces cerevisiae: a genome-wide screen identifies eight novel GID genes and indicates the existence of two degradation pathways. Mol Biol Cell 14(4):1652-63
+
'''Description of YIL097W:''' Subunit of GID complex; involved in proteasome-dependent catabolite inactivation of gluconeogenic enzymes FBPase, PEPCK, and c-MDH; forms dimer with Rmd5p that is then recruited to GID Complex by Gid8p; contains a degenerate RING finger motif needed for GID complex ubiquitin ligase activity in vivo, as well as CTLH and CRA domains; plays role in anti-apoptosis; required for survival upon exposure to K1 killer toxin<ref name='S000147292'>Braun B, et al. (2011) Gid9, a second RING finger protein contributes to the ubiquitin ligase activity of the Gid complex required for catabolite degradation. FEBS Lett () {{SGDpaper|S000147292}} PMID 22044534</ref><ref name='S000125883'>Khoury CM, et al. (2008) A TSC22-like motif defines a novel antiapoptotic protein family. FEMS Yeast Res 8(4):540-63 {{SGDpaper|S000125883}} PMID 18355271</ref><ref name='S000149618'>Menssen R, et al. (2012) Exploring the topology of the Gid complex, the E3 ubiquitin ligase involved in catabolite induced degradation of gluconeogenic enzymes. J Biol Chem () {{SGDpaper|S000149618}} PMID 22645139</ref><ref name='S000072994'>Page N, et al. (2003) A Saccharomyces cerevisiae genome-wide mutant screen for altered sensitivity to K1 killer toxin. Genetics 163(3):875-94 {{SGDpaper|S000072994}} PMID 12663529</ref><ref name='S000072993'>Regelmann J, et al. (2003) Catabolite degradation of fructose-1,6-bisphosphatase in the yeast Saccharomyces cerevisiae: a genome-wide screen identifies eight novel GID genes and indicates the existence of two degradation pathways. Mol Biol Cell 14(4):1652-63
 
  {{SGDpaper|S000072993}} PMID 12686616</ref>
 
  {{SGDpaper|S000072993}} PMID 12686616</ref>
 
<br>
 
<br>
Line 37: Line 39:
 
J Biol Chem 278(5):3265-74</ref>
 
J Biol Chem 278(5):3265-74</ref>
 
-->
 
-->
 +
 +
  
 
<protect>
 
<protect>

Latest revision as of 13:05, 27 August 2012

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

Systematic name YIL097W
Gene name FYV10
Aliases GID9
Feature type ORF, Verified
Coordinates Chr IX:180427..181977
Primary SGDID S000001359


Description of YIL097W: Subunit of GID complex; involved in proteasome-dependent catabolite inactivation of gluconeogenic enzymes FBPase, PEPCK, and c-MDH; forms dimer with Rmd5p that is then recruited to GID Complex by Gid8p; contains a degenerate RING finger motif needed for GID complex ubiquitin ligase activity in vivo, as well as CTLH and CRA domains; plays role in anti-apoptosis; required for survival upon exposure to K1 killer toxin[1][2][3][4][5]




</protect>

Community Commentary

About Community Commentary. Please share your knowledge!




<protect>

References

See Help:References on how to add references

  1. Braun B, et al. (2011) Gid9, a second RING finger protein contributes to the ubiquitin ligase activity of the Gid complex required for catabolite degradation. FEBS Lett () SGD PMID 22044534
  2. Khoury CM, et al. (2008) A TSC22-like motif defines a novel antiapoptotic protein family. FEMS Yeast Res 8(4):540-63 SGD PMID 18355271
  3. Menssen R, et al. (2012) Exploring the topology of the Gid complex, the E3 ubiquitin ligase involved in catabolite induced degradation of gluconeogenic enzymes. J Biol Chem () SGD PMID 22645139
  4. Page N, et al. (2003) A Saccharomyces cerevisiae genome-wide mutant screen for altered sensitivity to K1 killer toxin. Genetics 163(3):875-94 SGD PMID 12663529
  5. Regelmann J, et al. (2003) Catabolite degradation of fructose-1,6-bisphosphatase in the yeast Saccharomyces cerevisiae: a genome-wide screen identifies eight novel GID genes and indicates the existence of two degradation pathways. Mol Biol Cell 14(4):1652-63 SGD PMID 12686616

See Help:Categories on how to add the wiki page for this gene to a Category </protect>