Difference between revisions of "YGL240W"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YGL240W YGL240W]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000003209 YGL240W]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''DOC1 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''DOC1 ''
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|nowrap| Chr VII:48613..49365
 
|nowrap| Chr VII:48613..49365
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000003209
 
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'''Description of {{PAGENAME}}:''' Processivity factor required for the ubiquitination activity of the anaphase promoting complex (APC), mediates the activity of the APC by contributing to substrate recognition; involved in cyclin proteolysis<ref name='S000072817'>Passmore LA, et al. (2003) Doc1 mediates the activity of the anaphase-promoting complex by contributing to substrate recognition. EMBO J 22(4):786-96 {{SGDpaper|S000072817}} PMID 12574115</ref><ref name='S000071780'>Carroll CW and Morgan DO (2002) The Doc1 subunit is a processivity factor for the anaphase-promoting complex. Nat Cell Biol 4(11):880-7 {{SGDpaper|S000071780}} PMID 12402045</ref><ref name='S000069423'>Au SW, et al. (2002) Implications for the ubiquitination reaction of the anaphase-promoting complex from the crystal structure of the Doc1/Apc10 subunit. J Mol Biol 316(4):955-68 {{SGDpaper|S000069423}} PMID 11884135</ref><ref name='S000061630'>Grossberger R, et al. (1999) Characterization of the DOC1/APC10 subunit of the yeast and the human anaphase-promoting complex. J Biol Chem 274(20):14500-7 {{SGDpaper|S000061630}} PMID 10318877</ref><ref name='S000046390'>Hwang LH and Murray AW (1997) A novel yeast screen for mitotic arrest mutants identifies DOC1, a new gene involved in cyclin proteolysis. Mol Biol Cell 8(10):1877-87
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'''Description of YGL240W:''' Processivity factor required for the ubiquitination activity of the anaphase promoting complex (APC), mediates the activity of the APC by contributing to substrate recognition; involved in cyclin proteolysis; contains a conserved DOC1 homology domain<ref name='S000069423'>Au SW, et al. (2002) Implications for the ubiquitination reaction of the anaphase-promoting complex from the crystal structure of the Doc1/Apc10 subunit. J Mol Biol 316(4):955-68 {{SGDpaper|S000069423}} PMID 11884135</ref><ref name='S000071780'>Carroll CW and Morgan DO (2002) The Doc1 subunit is a processivity factor for the anaphase-promoting complex. Nat Cell Biol 4(11):880-7 {{SGDpaper|S000071780}} PMID 12402045</ref><ref name='S000061630'>Grossberger R, et al. (1999) Characterization of the DOC1/APC10 subunit of the yeast and the human anaphase-promoting complex. J Biol Chem 274(20):14500-7 {{SGDpaper|S000061630}} PMID 10318877</ref><ref name='S000046390'>Hwang LH and Murray AW (1997) A novel yeast screen for mitotic arrest mutants identifies DOC1, a new gene involved in cyclin proteolysis. Mol Biol Cell 8(10):1877-87 {{SGDpaper|S000046390}} PMID 9348530</ref><ref name='S000072817'>Passmore LA, et al. (2003) Doc1 mediates the activity of the anaphase-promoting complex by contributing to substrate recognition. EMBO J 22(4):786-96
  {{SGDpaper|S000046390}} PMID 9348530</ref>
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  {{SGDpaper|S000072817}} PMID 12574115</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 07:45, 23 January 2012

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Systematic name YGL240W
Gene name DOC1
Aliases APC10
Feature type ORF, Verified
Coordinates Chr VII:48613..49365
Primary SGDID S000003209


Description of YGL240W: Processivity factor required for the ubiquitination activity of the anaphase promoting complex (APC), mediates the activity of the APC by contributing to substrate recognition; involved in cyclin proteolysis; contains a conserved DOC1 homology domain[1][2][3][4][5]




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References

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  1. Au SW, et al. (2002) Implications for the ubiquitination reaction of the anaphase-promoting complex from the crystal structure of the Doc1/Apc10 subunit. J Mol Biol 316(4):955-68 SGD PMID 11884135
  2. Carroll CW and Morgan DO (2002) The Doc1 subunit is a processivity factor for the anaphase-promoting complex. Nat Cell Biol 4(11):880-7 SGD PMID 12402045
  3. Grossberger R, et al. (1999) Characterization of the DOC1/APC10 subunit of the yeast and the human anaphase-promoting complex. J Biol Chem 274(20):14500-7 SGD PMID 10318877
  4. Hwang LH and Murray AW (1997) A novel yeast screen for mitotic arrest mutants identifies DOC1, a new gene involved in cyclin proteolysis. Mol Biol Cell 8(10):1877-87 SGD PMID 9348530
  5. Passmore LA, et al. (2003) Doc1 mediates the activity of the anaphase-promoting complex by contributing to substrate recognition. EMBO J 22(4):786-96 SGD PMID 12574115

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