Difference between revisions of "YDR533C"
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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=S000002941 YDR533C] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''HSP31 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''HSP31 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
− | |nowrap| Chr IV: | + | |nowrap| Chr IV:1502160..1501447 |
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− | | | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000002941 |
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− | '''Description of | + | '''Description of YDR533C:''' Possible chaperone and cysteine protease with similarity to E. coli Hsp31; member of the DJ-1/ThiJ/PfpI superfamily, which includes human DJ-1 involved in Parkinson's disease; exists as a dimer and contains a putative metal-binding site<ref name='S000124090'>Goyal K and Mande SC (2008) Exploiting 3D structural templates for detection of metal-binding sites in protein structures. Proteins 70(4):1206-18 {{SGDpaper|S000124090}} PMID 17847089</ref><ref name='S000074850'>Wilson MA, et al. (2004) The 1.8-A resolution crystal structure of YDR533Cp from Saccharomyces cerevisiae: A member of the DJ-1/ThiJ/PfpI superfamily. Proc Natl Acad Sci U S A 101(6):1531-6 |
{{SGDpaper|S000074850}} PMID 14745011</ref> | {{SGDpaper|S000074850}} PMID 14745011</ref> | ||
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==Community Commentary== | ==Community Commentary== | ||
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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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==References== | ==References== | ||
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Latest revision as of 07:45, 23 January 2012
Share your knowledge...Edit this entry! <protect>
Systematic name | YDR533C |
Gene name | HSP31 |
Aliases | |
Feature type | ORF, Verified |
Coordinates | Chr IV:1502160..1501447 |
Primary SGDID | S000002941 |
Description of YDR533C: Possible chaperone and cysteine protease with similarity to E. coli Hsp31; member of the DJ-1/ThiJ/PfpI superfamily, which includes human DJ-1 involved in Parkinson's disease; exists as a dimer and contains a putative metal-binding site[1][2]
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Contents
Community Commentary
About Community Commentary. Please share your knowledge!
DNA and RNA Details
Other DNA and RNA Details
Other Topic: expression
Specifically lower expression in carbon limited chemostat cultures versus carbon excess. [3] [4]
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References
See Help:References on how to add references
- ↑ Goyal K and Mande SC (2008) Exploiting 3D structural templates for detection of metal-binding sites in protein structures. Proteins 70(4):1206-18 SGD PMID 17847089
- ↑ Wilson MA, et al. (2004) The 1.8-A resolution crystal structure of YDR533Cp from Saccharomyces cerevisiae: A member of the DJ-1/ThiJ/PfpI superfamily. Proc Natl Acad Sci U S A 101(6):1531-6 SGD PMID 14745011
- ↑ 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 SGD PMID 12414795
- ↑ submitted by Viktor Boer on 2003-07-25
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