Difference between revisions of "YNL281W"
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| − | '''Description of YNL281W:''' Heat shock protein regulator that binds to Hsp90p and may stimulate ATPase activity; originally identified as a high-copy number suppressor of a HSP90 loss-of-function mutation; GFP-fusion protein localizes to the cytoplasm and nucleus<ref name=' | + | '''Description of YNL281W:''' Heat shock protein regulator that binds to Hsp90p and may stimulate ATPase activity; originally identified as a high-copy number suppressor of a HSP90 loss-of-function mutation; GFP-fusion protein localizes to the cytoplasm and nucleus<ref name='S000044986'>Nathan DF, et al. (1999) Identification of SSF1, CNS1, and HCH1 as multicopy suppressors of a Saccharomyces cerevisiae Hsp90 loss-of-function mutation. Proc Natl Acad Sci U S A 96(4):1409-14 {{SGDpaper|S000044986}} PMID 9990037</ref><ref name='S000072028'>Panaretou B, et al. (2002) Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1. Mol Cell 10(6):1307-18 {{SGDpaper|S000072028}} PMID 12504007</ref><ref name='S000073164'>Lotz GP, et al. (2003) Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone. J Biol Chem 278(19):17228-35 {{SGDpaper|S000073164}} PMID 12604615</ref><ref name='S000074185'>Huh WK, et al. (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91 |
| − | {{SGDpaper| | + | {{SGDpaper|S000074185}} PMID 14562095</ref> |
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Revision as of 14:05, 31 March 2009
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| Systematic name | YNL281W |
| Gene name | HCH1 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr XIV:108467..108928 |
| Primary SGDID | S000005225 |
Description of YNL281W: Heat shock protein regulator that binds to Hsp90p and may stimulate ATPase activity; originally identified as a high-copy number suppressor of a HSP90 loss-of-function mutation; GFP-fusion protein localizes to the cytoplasm and nucleus[1][2][3][4]
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References
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- Jump up ↑ Nathan DF, et al. (1999) Identification of SSF1, CNS1, and HCH1 as multicopy suppressors of a Saccharomyces cerevisiae Hsp90 loss-of-function mutation. Proc Natl Acad Sci U S A 96(4):1409-14 SGD PMID 9990037
- Jump up ↑ Panaretou B, et al. (2002) Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1. Mol Cell 10(6):1307-18 SGD PMID 12504007
- Jump up ↑ Lotz GP, et al. (2003) Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone. J Biol Chem 278(19):17228-35 SGD PMID 12604615
- Jump up ↑ Huh WK, et al. (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91 SGD PMID 14562095
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