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='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 | + | '''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='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> | |
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Revision as of 14:05, 25 February 2010
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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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- ↑ 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
- ↑ 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
- ↑ 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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