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Chaperonin containing TCP1, subunit 5

CCT5, CCTepsilon, Ccte
The protein encoded by this gene is a molecular chaperone that is a member of the chaperonin containing TCP1 complex (CCT), also known as the TCP1 ring complex (TRiC). This complex consists of two identical stacked rings, each containing eight different proteins. Unfolded polypeptides enter the central cavity of the complex and are folded in an ATP-dependent manner. The complex folds various proteins, including actin and tubulin. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized. In addition, three pseudogenes of this gene have been identified. [provided by RefSeq, Jun 2010] (from NCBI)
Papers on CCT5
A novel function of the human chaperonin CCT epsilon subunit in yeast.
Kimura et al., Iizuka, Japan. In Biosci Biotechnol Biochem, 2011
introduction of the truncated human CCT epsilon subunit into yeast cells
Possible involvement of CCT5, RGS3, and YKT6 genes up-regulated in p53-mutated tumors in resistance to docetaxel in human breast cancers.
Noguchi et al., Suita, Japan. In Breast Cancer Res Treat, 2007
mRNA expression of CCT5, RGS3, and YKT6 was significantly up-regulated in p53-mutated tumors and associated with a low response rate to docetaxel.
Mutation in the epsilon subunit of the cytosolic chaperonin-containing t-complex peptide-1 (Cct5) gene causes autosomal recessive mutilating sensory neuropathy with spastic paraplegia.
Yahyaoui et al., Rabat, Morocco. In J Med Genet, 2006
A missense mutation within the CCT5 gene is associated with autosomal recessive mutilating sensory neuropathy with spastic paraplegia.
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