Difference between revisions of "YDR016C"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002423 YDR016C]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002423 YDR016C]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''DAD1 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''DAD1 ''
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr IV:478756..478472
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|nowrap| Chr IV:478758..478474
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000002423
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000002423
 
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'''Description of YDR016C:''' Essential subunit of the Dam1 complex (aka DASH complex), couples kinetochores to the force produced by MT depolymerization thereby aiding in chromosome segregation; is transferred to the kinetochore prior to mitosis<ref name='S000114260'>Westermann S, et al. (2006) The Dam1 kinetochore ring complex moves processively on depolymerizing microtubule ends. Nature 440(7083):565-9 {{SGDpaper|S000114260}} PMID 16415853</ref><ref name='S000080444'>Miranda JJ, et al. (2005) The yeast DASH complex forms closed rings on microtubules. Nat Struct Mol Biol 12(2):138-43 {{SGDpaper|S000080444}} PMID 15640796</ref><ref name='S000080667'>Westermann S, et al. (2005) Formation of a dynamic kinetochore- microtubule interface through assembly of the Dam1 ring complex. Mol Cell 17(2):277-90 {{SGDpaper|S000080667}} PMID 15664196</ref><ref name='S000065964'>Enquist-Newman M, et al. (2001) Dad1p, third component of the Duo1p/Dam1p complex involved in kinetochore function and mitotic spindle integrity. Mol Biol Cell 12(9):2601-13
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'''Description of YDR016C:''' Essential subunit of the Dam1 complex (aka DASH complex), couples kinetochores to the force produced by MT depolymerization thereby aiding in chromosome segregation; is transferred to the kinetochore prior to mitosis<ref name='S000065964'>Enquist-Newman M, et al. (2001) Dad1p, third component of the Duo1p/Dam1p complex involved in kinetochore function and mitotic spindle integrity. Mol Biol Cell 12(9):2601-13 {{SGDpaper|S000065964}} PMID 11553702</ref><ref name='S000080444'>Miranda JJ, et al. (2005) The yeast DASH complex forms closed rings on microtubules. Nat Struct Mol Biol 12(2):138-43 {{SGDpaper|S000080444}} PMID 15640796</ref><ref name='S000080667'>Westermann S, et al. (2005) Formation of a dynamic kinetochore- microtubule interface through assembly of the Dam1 ring complex. Mol Cell 17(2):277-90 {{SGDpaper|S000080667}} PMID 15664196</ref><ref name='S000114260'>Westermann S, et al. (2006) The Dam1 kinetochore ring complex moves processively on depolymerizing microtubule ends. Nature 440(7083):565-9
  {{SGDpaper|S000065964}} PMID 11553702</ref>
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  {{SGDpaper|S000114260}} PMID 16415853</ref>
 
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Latest revision as of 07:45, 23 January 2012

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Systematic name YDR016C
Gene name DAD1
Aliases
Feature type ORF, Verified
Coordinates Chr IV:478758..478474
Primary SGDID S000002423


Description of YDR016C: Essential subunit of the Dam1 complex (aka DASH complex), couples kinetochores to the force produced by MT depolymerization thereby aiding in chromosome segregation; is transferred to the kinetochore prior to mitosis[1][2][3][4]




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References

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  1. Enquist-Newman M, et al. (2001) Dad1p, third component of the Duo1p/Dam1p complex involved in kinetochore function and mitotic spindle integrity. Mol Biol Cell 12(9):2601-13 SGD PMID 11553702
  2. Miranda JJ, et al. (2005) The yeast DASH complex forms closed rings on microtubules. Nat Struct Mol Biol 12(2):138-43 SGD PMID 15640796
  3. Westermann S, et al. (2005) Formation of a dynamic kinetochore- microtubule interface through assembly of the Dam1 ring complex. Mol Cell 17(2):277-90 SGD PMID 15664196
  4. Westermann S, et al. (2006) The Dam1 kinetochore ring complex moves processively on depolymerizing microtubule ends. Nature 440(7083):565-9 SGD PMID 16415853

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