Difference between revisions of "YGR123C"

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'''Description of YGR123C:''' Protein serine/threonine phosphatase with similarity to human phosphatase PP5; present in both the nucleus and cytoplasm; expressed during logarithmic growth; computational analyses suggest roles in phosphate metabolism and rRNA processing<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='S000086472'>Segal E, et al. (2003) Module networks: identifying regulatory modules and their condition-specific regulators from gene expression data. Nat Genet 34(2):166-76
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'''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|S000086472}} PMID 12740579</ref>
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  {{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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  1. 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
  2. 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
  3. Soroka J, et al. (2012) Conformational Switching of the Molecular Chaperone Hsp90 via Regulated Phosphorylation. Mol Cell 45(4):517-28 SGD PMID 22365831
  4. 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
  5. 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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