YLL024C
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| 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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