Difference between revisions of "YDR188W"

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'''Description of YDR188W:''' Subunit of the cytosolic chaperonin Cct ring complex, related to Tcp1p, essential protein that is required for the assembly of actin and tubulins in vivo; contains an ATP-binding motif<ref name='S000080727'>Kabir MA, et al. (2005) Physiological effects of unassembled chaperonin Cct subunits in the yeast Saccharomyces cerevisiae. Yeast 22(3):219-39 {{SGDpaper|S000080727}} PMID 15704212</ref><ref name='S000062058'>Kim S, et al. (1994) Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains. Trends Biochem Sci 19(12):543-8 {{SGDpaper|S000062058}} PMID 7846767</ref><ref name='S000042209'>Stoldt V, et al. (1996) Review: the Cct eukaryotic chaperonin subunits of Saccharomyces cerevisiae and other yeasts. Yeast 12(6):523-9
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'''Description of YDR188W:''' Subunit of the cytosolic chaperonin Cct ring complex, related to Tcp1p, essential protein that is required for the assembly of actin and tubulins in vivo; contains an ATP-binding motif<ref name='S000042209'>Stoldt V, et al. (1996) Review: the Cct eukaryotic chaperonin subunits of Saccharomyces cerevisiae and other yeasts. Yeast 12(6):523-9 {{SGDpaper|S000042209}} PMID 8771707</ref><ref name='S000062058'>Kim S, et al. (1994) Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains. Trends Biochem Sci 19(12):543-8 {{SGDpaper|S000062058}} PMID 7846767</ref><ref name='S000080727'>Kabir MA, et al. (2005) Physiological effects of unassembled chaperonin Cct subunits in the yeast Saccharomyces cerevisiae. Yeast 22(3):219-39
  {{SGDpaper|S000042209}} PMID 8771707</ref>
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  {{SGDpaper|S000080727}} PMID 15704212</ref>
 
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Revision as of 04:15, 19 December 2008

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Systematic name YDR188W
Gene name CCT6
Aliases HTR3, TCP20, TCP6
Feature type ORF, Verified
Coordinates Chr IV:836419..838059
Primary SGDID S000002596


Description of YDR188W: Subunit of the cytosolic chaperonin Cct ring complex, related to Tcp1p, essential protein that is required for the assembly of actin and tubulins in vivo; contains an ATP-binding motif[1][2][3]




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References

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  1. Stoldt V, et al. (1996) Review: the Cct eukaryotic chaperonin subunits of Saccharomyces cerevisiae and other yeasts. Yeast 12(6):523-9 SGD PMID 8771707
  2. Kim S, et al. (1994) Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains. Trends Biochem Sci 19(12):543-8 SGD PMID 7846767
  3. Kabir MA, et al. (2005) Physiological effects of unassembled chaperonin Cct subunits in the yeast Saccharomyces cerevisiae. Yeast 22(3):219-39 SGD PMID 15704212

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