Difference between revisions of "YDR212W"

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'''Description of YDR212W:''' Alpha subunit of chaperonin-containing T-complex, which mediates protein folding in the cytosol; involved in maintenance of actin cytoskeleton; homolog to Drosophila melanogaster and mouse tailless complex polypeptide<ref name='S000042926'>Ursic D and Culbertson MR (1991) The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes. Mol Cell Biol 11(5):2629-40 {{SGDpaper|S000042926}} PMID 1901944</ref><ref name='S000043581'>Ursic D, et al. (1994) The essential yeast Tcp1 protein affects actin and microtubules. Mol Biol Cell 5(10):1065-80 {{SGDpaper|S000043581}} PMID 7865875</ref><ref name='S000061049'>Siegers K, et al. (1999) Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system. EMBO J 18(1):75-84 {{SGDpaper|S000061049}} PMID 9878052</ref><ref name='S000075049'>Siegers K, et al. (2003) TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes. EMBO J 22(19):5230-40
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'''Description of YDR212W:''' Alpha subunit of chaperonin-containing T-complex, which mediates protein folding in the cytosol; involved in maintenance of actin cytoskeleton; homolog to Drosophila melanogaster and mouse tailless complex polypeptide<ref name='S000075049'>Siegers K, et al. (2003) TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes. EMBO J 22(19):5230-40 {{SGDpaper|S000075049}} PMID 14517260</ref><ref name='S000061049'>Siegers K, et al. (1999) Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system. EMBO J 18(1):75-84 {{SGDpaper|S000061049}} PMID 9878052</ref><ref name='S000043581'>Ursic D, et al. (1994) The essential yeast Tcp1 protein affects actin and microtubules. Mol Biol Cell 5(10):1065-80 {{SGDpaper|S000043581}} PMID 7865875</ref><ref name='S000042926'>Ursic D and Culbertson MR (1991) The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes. Mol Cell Biol 11(5):2629-40
  {{SGDpaper|S000075049}} PMID 14517260</ref>
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  {{SGDpaper|S000042926}} PMID 1901944</ref>
 
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Revision as of 14:05, 16 January 2009

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Systematic name YDR212W
Gene name TCP1
Aliases CCT1
Feature type ORF, Verified
Coordinates Chr IV:887230..888909
Primary SGDID S000002620


Description of YDR212W: Alpha subunit of chaperonin-containing T-complex, which mediates protein folding in the cytosol; involved in maintenance of actin cytoskeleton; homolog to Drosophila melanogaster and mouse tailless complex polypeptide[1][2][3][4]




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References

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  1. Siegers K, et al. (2003) TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes. EMBO J 22(19):5230-40 SGD PMID 14517260
  2. Siegers K, et al. (1999) Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system. EMBO J 18(1):75-84 SGD PMID 9878052
  3. Ursic D, et al. (1994) The essential yeast Tcp1 protein affects actin and microtubules. Mol Biol Cell 5(10):1065-80 SGD PMID 7865875
  4. Ursic D and Culbertson MR (1991) The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes. Mol Cell Biol 11(5):2629-40 SGD PMID 1901944

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