Difference between revisions of "YNL281W"
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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=S000005225 YNL281W] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''HCH1 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''HCH1 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
|nowrap| Chr XIV:108467..108928 | |nowrap| Chr XIV:108467..108928 | ||
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+ | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000005225 | ||
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− | '''Description of | + | '''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='S000074185'>Huh WK, et al. (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91 {{SGDpaper|S000074185}} PMID 14562095</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='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| | + | {{SGDpaper|S000072028}} PMID 12504007</ref> |
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==Community Commentary== | ==Community Commentary== | ||
{{CommentaryHelp}} | {{CommentaryHelp}} | ||
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+ | <!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation --> | ||
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+ | Specifically higher expression in carbon limited chemostat cultures versus carbon excess. | ||
+ | <ref>Boer VM, et al. (2003) The genome-wide transcriptional responses of Saccharomyces cerevisiae grown on glucose in aerobic chemostat cultures limited for carbon, nitrogen, phosphorus, or sulfur. | ||
+ | J Biol Chem 278(5):3265-74</ref> | ||
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Latest revision as of 07:45, 23 January 2012
Share your knowledge...Edit this entry! <protect>
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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Contents
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References
See Help:References on how to add references
- Jump up ↑ Huh WK, et al. (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91 SGD PMID 14562095
- 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 ↑ 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
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