Difference between revisions of "YNL025C"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YNL025C YNL025C]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004970 YNL025C]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''SSN8 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''SSN8 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|nowrap| Chr XIV:585292..584321
 
|nowrap| Chr XIV:585292..584321
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000004970
 
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'''Description of {{PAGENAME}}:''' Cyclin-like component of the RNA polymerase II holoenzyme, involved in phosphorylation of the RNA polymerase II C-terminal domain; involved in glucose repression and telomere maintenance<ref name='S000114270'>Askree SH, et al. (2004) A genome-wide screen for Saccharomyces cerevisiae deletion mutants that affect telomere length. Proc Natl Acad Sci U S A 101(23):8658-63 {{SGDpaper|S000114270}} PMID 15161972</ref><ref name='S000053165'>Kuchin S, et al. (1995) Cyclin-dependent protein kinase and cyclin homologs SSN3 and SSN8 contribute to transcriptional control in yeast. Proc Natl Acad Sci U S A 92(9):4006-10 {{SGDpaper|S000053165}} PMID 7732022</ref><ref name='S000050148'>Balciunas D and Ronne H (1995) Three subunits of the RNA polymerase II mediator complex are involved in glucose repression. Nucleic Acids Res 23(21):4421-5 {{SGDpaper|S000050148}} PMID 7501465</ref><ref name='S000049118'>Liao SM, et al. (1995) A kinase-cyclin pair in the RNA polymerase II holoenzyme. Nature 374(6518):193-6
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'''Description of YNL025C:''' Cyclin-like component of the RNA polymerase II holoenzyme, involved in phosphorylation of the RNA polymerase II C-terminal domain; involved in glucose repression and telomere maintenance<ref name='S000114270'>Askree SH, et al. (2004) A genome-wide screen for Saccharomyces cerevisiae deletion mutants that affect telomere length. Proc Natl Acad Sci U S A 101(23):8658-63 {{SGDpaper|S000114270}} PMID 15161972</ref><ref name='S000053165'>Kuchin S, et al. (1995) Cyclin-dependent protein kinase and cyclin homologs SSN3 and SSN8 contribute to transcriptional control in yeast. Proc Natl Acad Sci U S A 92(9):4006-10 {{SGDpaper|S000053165}} PMID 7732022</ref><ref name='S000050148'>Balciunas D and Ronne H (1995) Three subunits of the RNA polymerase II mediator complex are involved in glucose repression. Nucleic Acids Res 23(21):4421-5 {{SGDpaper|S000050148}} PMID 7501465</ref><ref name='S000049118'>Liao SM, et al. (1995) A kinase-cyclin pair in the RNA polymerase II holoenzyme. Nature 374(6518):193-6
 
  {{SGDpaper|S000049118}} PMID 7877695</ref>
 
  {{SGDpaper|S000049118}} PMID 7877695</ref>
 
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J Biol Chem 278(5):3265-74</ref>
 
J Biol Chem 278(5):3265-74</ref>
 
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Revision as of 07:46, 27 February 2007

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Systematic name YNL025C
Gene name SSN8
Aliases CycC, GIG3, NUT9, RYE2, SRB11, UME3
Feature type ORF, Verified
Coordinates Chr XIV:585292..584321
Primary SGDID S000004970


Description of YNL025C: Cyclin-like component of the RNA polymerase II holoenzyme, involved in phosphorylation of the RNA polymerase II C-terminal domain; involved in glucose repression and telomere maintenance[1][2][3][4]




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References

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  1. Askree SH, et al. (2004) A genome-wide screen for Saccharomyces cerevisiae deletion mutants that affect telomere length. Proc Natl Acad Sci U S A 101(23):8658-63 SGD PMID 15161972
  2. Kuchin S, et al. (1995) Cyclin-dependent protein kinase and cyclin homologs SSN3 and SSN8 contribute to transcriptional control in yeast. Proc Natl Acad Sci U S A 92(9):4006-10 SGD PMID 7732022
  3. Balciunas D and Ronne H (1995) Three subunits of the RNA polymerase II mediator complex are involved in glucose repression. Nucleic Acids Res 23(21):4421-5 SGD PMID 7501465
  4. Liao SM, et al. (1995) A kinase-cyclin pair in the RNA polymerase II holoenzyme. Nature 374(6518):193-6 SGD PMID 7877695

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