Difference between revisions of "YPR158W"
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| − | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http:// | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000006362 YPR158W] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''CUR1 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''CUR1 '' | ||
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| − | '''Description of YPR158W:''' | + | '''Description of YPR158W:''' Sorting factor, central regulator of spatial protein quality control; physically and functionally interacts with chaperones to promote sorting and deposition of misfolded proteins into cytosolic compartments; involved in destabilization of [URE3] prions; CUR1 has a paralog, BTN2, that arose from the whole genome duplication<ref name='S000113653'>Byrne KP and Wolfe KH (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61 {{SGDpaper|S000113653}} PMID 16169922</ref><ref name='S000127914'>Kryndushkin DS, et al. (2008) Curing of the [URE3] prion by Btn2p, a Batten disease-related protein. EMBO J 27(20):2725-35 {{SGDpaper|S000127914}} PMID 18833194</ref><ref name='S000149864'>Malinovska L, et al. (2012) Molecular chaperones and stress-inducible protein sorting factors coordinate the spatio-temporal distribution of protein aggregates. Mol Biol Cell () |
| − | {{SGDpaper| | + | {{SGDpaper|S000149864}} PMID 22718905</ref> |
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Latest revision as of 13:05, 20 October 2012
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| Systematic name | YPR158W |
| Gene name | CUR1 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr XVI:843262..844020 |
| Primary SGDID | S000006362 |
Description of YPR158W: Sorting factor, central regulator of spatial protein quality control; physically and functionally interacts with chaperones to promote sorting and deposition of misfolded proteins into cytosolic compartments; involved in destabilization of [URE3] prions; CUR1 has a paralog, BTN2, that arose from the whole genome duplication[1][2][3]
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References
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- ↑ Byrne KP and Wolfe KH (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61 SGD PMID 16169922
- ↑ Kryndushkin DS, et al. (2008) Curing of the [URE3] prion by Btn2p, a Batten disease-related protein. EMBO J 27(20):2725-35 SGD PMID 18833194
- ↑ Malinovska L, et al. (2012) Molecular chaperones and stress-inducible protein sorting factors coordinate the spatio-temporal distribution of protein aggregates. Mol Biol Cell () SGD PMID 22718905
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