Difference between revisions of "YDR212W"
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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=S000002620 YDR212W] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''TCP1 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''TCP1 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr IV: | + | |nowrap| Chr IV:887232..888911 |
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| + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000002620 | ||
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| − | '''Description of | + | '''Description of YDR212W:''' Alpha subunit of chaperonin-containing T-complex, which mediates protein folding in the cytosol; involved in actin cytoskeleton maintenance; overexpression in neurons suppresses formation of pathogenic conformations of huntingtin protein<ref name='S000061049'>Siegers K, et al. (1999) Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system. EMBO J 18(1):75-84 {{SGDpaper|S000061049}} PMID 9878052</ref><ref name='S000075049'>Siegers K, et al. (2003) TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes. EMBO J 22(19):5230-40 {{SGDpaper|S000075049}} PMID 14517260</ref><ref name='S000118957'>Tam S, et al. (2006) The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions. Nat Cell Biol 8(10):1155-62 {{SGDpaper|S000118957}} PMID 16980959</ref><ref name='S000042926'>Ursic D and Culbertson MR (1991) The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes. Mol Cell Biol 11(5):2629-40 {{SGDpaper|S000042926}} PMID 1901944</ref><ref name='S000043581'>Ursic D, et al. (1994) The essential yeast Tcp1 protein affects actin and microtubules. Mol Biol Cell 5(10):1065-80 |
| − | {{SGDpaper| | + | {{SGDpaper|S000043581}} PMID 7865875</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 | YDR212W |
| Gene name | TCP1 |
| Aliases | CCT1 |
| Feature type | ORF, Verified |
| Coordinates | Chr IV:887232..888911 |
| Primary SGDID | S000002620 |
Description of YDR212W: Alpha subunit of chaperonin-containing T-complex, which mediates protein folding in the cytosol; involved in actin cytoskeleton maintenance; overexpression in neurons suppresses formation of pathogenic conformations of huntingtin protein[1][2][3][4][5]
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Contents
Community Commentary
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References
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- ↑ Siegers K, et al. (1999) Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system. EMBO J 18(1):75-84 SGD PMID 9878052
- ↑ Siegers K, et al. (2003) TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes. EMBO J 22(19):5230-40 SGD PMID 14517260
- ↑ Tam S, et al. (2006) The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions. Nat Cell Biol 8(10):1155-62 SGD PMID 16980959
- ↑ Ursic D and Culbertson MR (1991) The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes. Mol Cell Biol 11(5):2629-40 SGD PMID 1901944
- ↑ Ursic D, et al. (1994) The essential yeast Tcp1 protein affects actin and microtubules. Mol Biol Cell 5(10):1065-80 SGD PMID 7865875
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