Difference between revisions of "YPR158W"

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'''Description of YPR158W:''' Protein of unknown function involved in destabilization of [URE3] prions; similar in sequence to Btn2p<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
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'''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|S000127914}} PMID 18833194</ref>
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  {{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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  1. 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
  2. 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
  3. 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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