Difference between revisions of "YLL024C"
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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=S000003947 YLL024C] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''SSA2 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''SSA2 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr XII: | + | |nowrap| Chr XII:97485..95566 |
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| + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000003947 | ||
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| − | '''Description of | + | '''Description of YLL024C:''' ATP binding protein involved in protein folding and vacuolar import of proteins; member of heat shock protein 70 (HSP70) family; associated with the chaperonin-containing T-complex; present in the cytoplasm, vacuolar membrane and cell wall; 98% identical with Ssa1p, but subtle differences between the two proteins provide functional specificity with respect to propagation of yeast [URE3] prions and vacuolar-mediated degradations of gluconeogenesis enzymes<ref name='S000049670'>Brown CR, et al. (2000) The heat shock protein Ssa2p is required for import of fructose-1, 6-bisphosphatase into Vid vesicles. J Cell Biol 150(1):65-76 {{SGDpaper|S000049670}} PMID 10893257</ref><ref name='S000080727'>Kabir MA, et al. (2005) Physiological effects of unassembled chaperonin Cct subunits in the yeast Saccharomyces cerevisiae. Yeast 22(3):219-39 {{SGDpaper|S000080727}} PMID 15704212</ref><ref name='S000043439'>Lopez-Ribot JL and Chaffin WL (1996) Members of the Hsp70 family of proteins in the cell wall of Saccharomyces cerevisiae. J Bacteriol 178(15):4724-6 {{SGDpaper|S000043439}} PMID 8755907</ref><ref name='S000047102'>Satyanarayana C, et al. (2000) Cytosolic Hsp70s are involved in the transport of aminopeptidase 1 from the cytoplasm into the vacuole. FEBS Lett 470(3):232-8 {{SGDpaper|S000047102}} PMID 10745074</ref><ref name='S000146266'>Sharma D and Masison DC (2011) Single methyl group determines prion propagation and protein degradation activities of yeast heat shock protein (Hsp)-70 chaperones Ssa1p and Ssa2p. Proc Natl Acad Sci U S A () {{SGDpaper|S000146266}} PMID 21808014</ref><ref name='S000049179'>Unno K, et al. (1997) Role of Hsp70 subfamily, Ssa, in protein folding in yeast cells, seen in luciferase-transformed ssa mutants. Biol Pharm Bull 20(12):1240-4 |
| − | {{SGDpaper| | + | {{SGDpaper|S000049179}} PMID 9448096</ref> |
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J Biol Chem 278(5):3265-74</ref> | J Biol Chem 278(5):3265-74</ref> | ||
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Latest revision as of 06:45, 23 January 2012
Share your knowledge...Edit this entry! <protect>
| Systematic name | YLL024C |
| Gene name | SSA2 |
| Aliases | YG102 |
| Feature type | ORF, Verified |
| Coordinates | Chr XII:97485..95566 |
| Primary SGDID | S000003947 |
Description of YLL024C: ATP binding protein involved in protein folding and vacuolar import of proteins; member of heat shock protein 70 (HSP70) family; associated with the chaperonin-containing T-complex; present in the cytoplasm, vacuolar membrane and cell wall; 98% identical with Ssa1p, but subtle differences between the two proteins provide functional specificity with respect to propagation of yeast [URE3] prions and vacuolar-mediated degradations of gluconeogenesis enzymes[1][2][3][4][5][6]
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References
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- ↑ Brown CR, et al. (2000) The heat shock protein Ssa2p is required for import of fructose-1, 6-bisphosphatase into Vid vesicles. J Cell Biol 150(1):65-76 SGD PMID 10893257
- ↑ Kabir MA, et al. (2005) Physiological effects of unassembled chaperonin Cct subunits in the yeast Saccharomyces cerevisiae. Yeast 22(3):219-39 SGD PMID 15704212
- ↑ Lopez-Ribot JL and Chaffin WL (1996) Members of the Hsp70 family of proteins in the cell wall of Saccharomyces cerevisiae. J Bacteriol 178(15):4724-6 SGD PMID 8755907
- ↑ Satyanarayana C, et al. (2000) Cytosolic Hsp70s are involved in the transport of aminopeptidase 1 from the cytoplasm into the vacuole. FEBS Lett 470(3):232-8 SGD PMID 10745074
- ↑ Sharma D and Masison DC (2011) Single methyl group determines prion propagation and protein degradation activities of yeast heat shock protein (Hsp)-70 chaperones Ssa1p and Ssa2p. Proc Natl Acad Sci U S A () SGD PMID 21808014
- ↑ Unno K, et al. (1997) Role of Hsp70 subfamily, Ssa, in protein folding in yeast cells, seen in luciferase-transformed ssa mutants. Biol Pharm Bull 20(12):1240-4 SGD PMID 9448096
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