Difference between revisions of "YHR034C"

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{|{{Prettytable}} align = 'right' width = '200px'
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YHR034C YHR034C]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000001076 YHR034C]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''PIH1 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''PIH1 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr VIII:177992..176958
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|nowrap| Chr VIII:177999..176965
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000001076
 
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'''Description of {{PAGENAME}}:''' Protein of unresolved function; may function in protein folding and/or rRNA processing, interacts with a chaperone (Hsp82p), two chromatin remodeling factors (Rvb1p, Rvb2p) and two rRNA processing factors (Rrp43p, Nop58p)<ref name='S000079913'>Jonsson ZO, et al. (2004) Rvb1p/Rvb2p recruit Arp5p and assemble a functional Ino80 chromatin remodeling complex. Mol Cell 16(3):465-77 {{SGDpaper|S000079913}} PMID 15525518</ref><ref name='S000081009'>Zhao R, et al. (2005) Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone. Cell 120(5):715-27 {{SGDpaper|S000081009}} PMID 15766533</ref><ref name='S000080660'>Gonzales FA, et al. (2005) Characterization of Saccharomyces cerevisiae Nop17p, a novel Nop58p-interacting protein that is involved in Pre-rRNA processing. J Mol Biol 346(2):437-55
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'''Description of YHR034C:''' Component of the conserved R2TP complex (Rvb1-Rvb2-Tah1-Pih1); R2TP complex interacts with Hsp90 (Hsp82p and Hsc82p) to mediate assembly large protein complexes such as box C/D snoRNPs and RNA polymerase II<ref name='S000135237'>Eckert K, et al. (2010) The Pih1-Tah1 cochaperone complex inhibits Hsp90 molecular chaperone ATPase activity. J Biol Chem 285(41):31304-12 {{SGDpaper|S000135237}} PMID 20663878</ref><ref name='S000080660'>Gonzales FA, et al. (2005) Characterization of Saccharomyces cerevisiae Nop17p, a novel Nop58p-interacting protein that is involved in Pre-rRNA processing. J Mol Biol 346(2):437-55 {{SGDpaper|S000080660}} PMID 15670595</ref><ref name='S000147848'>Jimenez B, et al. (2011) The structure of the minimal tetratricopeptide repeat domain protein Tah1 reveals the mechanism of its interaction with Pih1 and Hsp90. J Biol Chem () {{SGDpaper|S000147848}} PMID 22179618</ref><ref name='S000079913'>Jonsson ZO, et al. (2004) Rvb1p/Rvb2p recruit Arp5p and assemble a functional Ino80 chromatin remodeling complex. Mol Cell 16(3):465-77 {{SGDpaper|S000079913}} PMID 15525518</ref><ref name='S000081009'>Zhao R, et al. (2005) Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone. Cell 120(5):715-27 {{SGDpaper|S000081009}} PMID 15766533</ref><ref name='S000136091'>Zhao R, et al. (2008) Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation. J Cell Biol 180(3):563-78
  {{SGDpaper|S000080660}} PMID 15670595</ref>
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  {{SGDpaper|S000136091}} PMID 18268103</ref>
 
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==Community Commentary==
 
==Community Commentary==
 
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<!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation -->
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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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Latest revision as of 13:05, 6 March 2012

Share your knowledge...Edit this entry! <protect>

Systematic name YHR034C
Gene name PIH1
Aliases NOP17
Feature type ORF, Verified
Coordinates Chr VIII:177999..176965
Primary SGDID S000001076


Description of YHR034C: Component of the conserved R2TP complex (Rvb1-Rvb2-Tah1-Pih1); R2TP complex interacts with Hsp90 (Hsp82p and Hsc82p) to mediate assembly large protein complexes such as box C/D snoRNPs and RNA polymerase II[1][2][3][4][5][6]




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Community Commentary

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References

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  1. Eckert K, et al. (2010) The Pih1-Tah1 cochaperone complex inhibits Hsp90 molecular chaperone ATPase activity. J Biol Chem 285(41):31304-12 SGD PMID 20663878
  2. Gonzales FA, et al. (2005) Characterization of Saccharomyces cerevisiae Nop17p, a novel Nop58p-interacting protein that is involved in Pre-rRNA processing. J Mol Biol 346(2):437-55 SGD PMID 15670595
  3. Jimenez B, et al. (2011) The structure of the minimal tetratricopeptide repeat domain protein Tah1 reveals the mechanism of its interaction with Pih1 and Hsp90. J Biol Chem () SGD PMID 22179618
  4. Jonsson ZO, et al. (2004) Rvb1p/Rvb2p recruit Arp5p and assemble a functional Ino80 chromatin remodeling complex. Mol Cell 16(3):465-77 SGD PMID 15525518
  5. Zhao R, et al. (2005) Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone. Cell 120(5):715-27 SGD PMID 15766533
  6. Zhao R, et al. (2008) Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation. J Cell Biol 180(3):563-78 SGD PMID 18268103

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