Difference between revisions of "YPL144W"

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'''Description of YPL144W:''' 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='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='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 {{SGDpaper|S000125712}} PMID 18278057</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
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'''Description of YPL144W:''' 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='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 {{SGDpaper|S000125712}} PMID 18278057</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
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  {{SGDpaper|S000125713}} PMID 18278055</ref>
 
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Revision as of 14:05, 31 March 2009

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Systematic name YPL144W
Gene name POC4
Aliases DMP1, PBA4
Feature type ORF, Verified
Coordinates Chr XVI:280479..280925
Primary SGDID S000006065


Description of YPL144W: 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]




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References

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  1. 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
  2. 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
  3. 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

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