Difference between revisions of "YGR123C"
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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=S000003355 YGR123C] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''PPT1 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''PPT1 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr VII: | + | |nowrap| Chr VII:738203..736662 |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000003355 | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000003355 | ||
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| − | '''Description of YGR123C:''' Protein serine/threonine phosphatase | + | '''Description of YGR123C:''' Protein serine/threonine phosphatase, regulates Hsp90 chaperone by affecting its ATPase and cochaperone binding activities; has similarity to human phosphatase PP5; present in both the nucleus and cytoplasm; expressed during logarithmic growth<ref name='S000049716'>Chen MX, et al. (1994) A novel human protein serine/threonine phosphatase, which possesses four tetratricopeptide repeat motifs and localizes to the nucleus. EMBO J 13(18):4278-90 {{SGDpaper|S000049716}} PMID 7925273</ref><ref name='S000072959'>Jeong JY, et al. (2003) Characterization of Saccharomyces cerevisiae protein Ser/Thr phosphatase T1 and comparison to its mammalian homolog PP5. BMC Cell Biol 4():3 {{SGDpaper|S000072959}} PMID 12694636</ref><ref name='S000148585'>Soroka J, et al. (2012) Conformational Switching of the Molecular Chaperone Hsp90 via Regulated Phosphorylation. Mol Cell 45(4):517-28 {{SGDpaper|S000148585}} PMID 22365831</ref><ref name='S000128042'>Vaughan CK, et al. (2008) Hsp90-dependent activation of protein kinases is regulated by chaperone-targeted dephosphorylation of Cdc37. Mol Cell 31(6):886-95 {{SGDpaper|S000128042}} PMID 18922470</ref><ref name='S000114194'>Wandinger SK, et al. (2006) The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90. EMBO J 25(2):367-76 |
| − | {{SGDpaper| | + | {{SGDpaper|S000114194}} PMID 16407978</ref> |
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Latest revision as of 14:05, 15 March 2012
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| Systematic name | YGR123C |
| Gene name | PPT1 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr VII:738203..736662 |
| Primary SGDID | S000003355 |
Description of YGR123C: Protein serine/threonine phosphatase, regulates Hsp90 chaperone by affecting its ATPase and cochaperone binding activities; has similarity to human phosphatase PP5; present in both the nucleus and cytoplasm; expressed during logarithmic growth[1][2][3][4][5]
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References
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- ↑ Chen MX, et al. (1994) A novel human protein serine/threonine phosphatase, which possesses four tetratricopeptide repeat motifs and localizes to the nucleus. EMBO J 13(18):4278-90 SGD PMID 7925273
- ↑ Jeong JY, et al. (2003) Characterization of Saccharomyces cerevisiae protein Ser/Thr phosphatase T1 and comparison to its mammalian homolog PP5. BMC Cell Biol 4():3 SGD PMID 12694636
- ↑ Soroka J, et al. (2012) Conformational Switching of the Molecular Chaperone Hsp90 via Regulated Phosphorylation. Mol Cell 45(4):517-28 SGD PMID 22365831
- ↑ Vaughan CK, et al. (2008) Hsp90-dependent activation of protein kinases is regulated by chaperone-targeted dephosphorylation of Cdc37. Mol Cell 31(6):886-95 SGD PMID 18922470
- ↑ Wandinger SK, et al. (2006) The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90. EMBO J 25(2):367-76 SGD PMID 16407978
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