Difference between revisions of "YLR021W"

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{|{{Prettytable}} align = 'right' width = '200px'
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YLR021W YLR021W]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004011 YLR021W]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''IRC25 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''IRC25 ''
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases'''          ||'' ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases'''          ||''DMP2, PBA3, POC3''
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type'''          || ORF, Uncharacterized[[Category:ORF]][[Category:ORF, Uncharacterized]]
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type'''          || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]]
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
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|nowrap| Chr XII:183622..184161
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|nowrap| Chr XII:183623..184162
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000004011
 
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'''Description of {{PAGENAME}}:''' Putative protein of unknown function; mutant accumulates unusually high amounts of dityrosine in the soluble fraction though spores appear wild-type; YLR021W is not an essential gene; null mutant displays increased levels of spontaneous Rad52 foci<ref name='S000117038'>Alvaro D (2006)   () {{SGDpaper|S000117038}} PMID </ref><ref name='S000074332'>Briza P, et al. (2002) Systematic analysis of sporulation phenotypes in 624 non-lethal homozygous deletion strains of Saccharomyces cerevisiae. Yeast 19(5):403-22 {{SGDpaper|S000074332}} PMID 11921089</ref><ref name='S000071347'>Giaever G, et al. (2002) Functional profiling of the Saccharomyces cerevisiae genome. Nature 418(6896):387-91
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'''Description of YLR021W:''' Component of a heterodimeric Poc4p-Irc25p chaperone involved in assembly of alpha subunits into the 20S proteasome; may regulate formation of proteasome isoforms with alternative subunits under different conditions<ref name='S000125059'>Alvaro D, et al. (2007) Genome-wide analysis of Rad52 foci reveals diverse mechanisms impacting recombination. PLoS Genet 3(12):e228 {{SGDpaper|S000125059}} PMID 18085829</ref><ref name='S000125713'>Kusmierczyk AR, et al. (2008) A multimeric assembly factor controls the formation of alternative 20S proteasomes. Nat Struct Mol Biol 15(3):237-44 {{SGDpaper|S000125713}} PMID 18278055</ref><ref name='S000123910'>Le Tallec B, et al. (2007) 20S proteasome assembly is orchestrated by two distinct pairs of chaperones in yeast and in mammals. Mol Cell 27(4):660-74 {{SGDpaper|S000123910}} PMID 17707236</ref><ref name='S000125712'>Yashiroda H, et al. (2008) Crystal structure of a chaperone complex that contributes to the assembly of yeast 20S proteasomes. Nat Struct Mol Biol 15(3):228-36
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  {{SGDpaper|S000071347}} PMID 12140549</ref>
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  {{SGDpaper|S000125712}} PMID 18278057</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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Latest revision as of 07:45, 23 January 2012

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Systematic name YLR021W
Gene name IRC25
Aliases DMP2, PBA3, POC3
Feature type ORF, Verified
Coordinates Chr XII:183623..184162
Primary SGDID S000004011


Description of YLR021W: Component of a heterodimeric Poc4p-Irc25p chaperone involved in assembly of alpha subunits into the 20S proteasome; may regulate formation of proteasome isoforms with alternative subunits under different conditions[1][2][3][4]




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References

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  1. ↑ Alvaro D, et al. (2007) Genome-wide analysis of Rad52 foci reveals diverse mechanisms impacting recombination. PLoS Genet 3(12):e228 SGD PMID 18085829
  2. ↑ Kusmierczyk AR, et al. (2008) A multimeric assembly factor controls the formation of alternative 20S proteasomes. Nat Struct Mol Biol 15(3):237-44 SGD PMID 18278055
  3. ↑ Le Tallec B, et al. (2007) 20S proteasome assembly is orchestrated by two distinct pairs of chaperones in yeast and in mammals. Mol Cell 27(4):660-74 SGD PMID 17707236
  4. ↑ Yashiroda H, et al. (2008) Crystal structure of a chaperone complex that contributes to the assembly of yeast 20S proteasomes. Nat Struct Mol Biol 15(3):228-36 SGD PMID 18278057

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