Difference between revisions of "YGR123C"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YGR123C YGR123C]  
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|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:738208..736667
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|nowrap| Chr VII:738203..736662
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000003355
 
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'''Description of {{PAGENAME}}:''' Protein serine/threonine phosphatase with similarity to human phosphatase PP5; present in both the nucleus and cytoplasm; expressed during logarithmic growth<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='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
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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|S000049716}} PMID 7925273</ref>
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  {{SGDpaper|S000114194}} PMID 16407978</ref>
 
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==Community Commentary==
 
==Community Commentary==
 
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Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
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<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.
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J Biol Chem 278(5):3265-74</ref>
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==References==
 
==References==
 
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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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