Difference between revisions of "YDL139C"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002298 YDL139C]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002298 YDL139C]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''SCM3 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''SCM3 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr IV:212047..211376
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|nowrap| Chr IV:212046..211375
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000002298
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000002298
 
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'''Description of YDL139C:''' Nonhistone component of centromeric chromatin that binds stoichiometrically to CenH3-H4 histones, required for kinetochore assembly; contains nuclear export signal (NES); required for G2/M progression and localization of Cse4p<ref name='S000123881'>Aravind L, et al. (2007) Domain Architectures of the Scm3p Protein Provide Insights into Centromere Function and Evolution. Cell Cycle 6(20) {{SGDpaper|S000123881}} PMID 17704645</ref><ref name='S000122928'>Stoler S, et al. (2007) Scm3, an essential Saccharomyces cerevisiae centromere protein required for G2/M progression and Cse4 localization. Proc Natl Acad Sci U S A 104(25):10571-6 {{SGDpaper|S000122928}} PMID 17548816</ref><ref name='S000052739'>Chen Y, et al. (2000) The N terminus of the centromere H3-like protein Cse4p performs an essential function distinct from that of the histone fold domain. Mol Cell Biol 20(18):7037-48
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'''Description of YDL139C:''' Nonhistone component of centromeric chromatin that binds stoichiometrically to CenH3-H4 histones, required for kinetochore assembly; required for G2/M progression and localization of Cse4p; may protect Cse4p from ubiquitylation<ref name='S000123881'>Aravind L, et al. (2007) Domain architectures of the Scm3p protein provide insights into centromere function and evolution. Cell Cycle 6(20):2511-5 {{SGDpaper|S000123881}} PMID 17704645</ref><ref name='S000052739'>Chen Y, et al. (2000) The N terminus of the centromere H3-like protein Cse4p performs an essential function distinct from that of the histone fold domain. Mol Cell Biol 20(18):7037-48 {{SGDpaper|S000052739}} PMID 10958698</ref><ref name='S000140160'>Hewawasam G, et al. (2010) Psh1 Is an E3 Ubiquitin Ligase that Targets the Centromeric Histone Variant Cse4. Mol Cell 40(3):444-54 {{SGDpaper|S000140160}} PMID 21070970</ref><ref name='S000122928'>Stoler S, et al. (2007) Scm3, an essential Saccharomyces cerevisiae centromere protein required for G2/M progression and Cse4 localization. Proc Natl Acad Sci U S A 104(25):10571-6
  {{SGDpaper|S000052739}} PMID 10958698</ref>
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  {{SGDpaper|S000122928}} PMID 17548816</ref>
 
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Latest revision as of 06:45, 23 January 2012

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Systematic name YDL139C
Gene name SCM3
Aliases
Feature type ORF, Verified
Coordinates Chr IV:212046..211375
Primary SGDID S000002298


Description of YDL139C: Nonhistone component of centromeric chromatin that binds stoichiometrically to CenH3-H4 histones, required for kinetochore assembly; required for G2/M progression and localization of Cse4p; may protect Cse4p from ubiquitylation[1][2][3][4]




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References

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  1. Aravind L, et al. (2007) Domain architectures of the Scm3p protein provide insights into centromere function and evolution. Cell Cycle 6(20):2511-5 SGD PMID 17704645
  2. Chen Y, et al. (2000) The N terminus of the centromere H3-like protein Cse4p performs an essential function distinct from that of the histone fold domain. Mol Cell Biol 20(18):7037-48 SGD PMID 10958698
  3. Hewawasam G, et al. (2010) Psh1 Is an E3 Ubiquitin Ligase that Targets the Centromeric Histone Variant Cse4. Mol Cell 40(3):444-54 SGD PMID 21070970
  4. Stoler S, et al. (2007) Scm3, an essential Saccharomyces cerevisiae centromere protein required for G2/M progression and Cse4 localization. Proc Natl Acad Sci U S A 104(25):10571-6 SGD PMID 17548816

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