CCT6A
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. The TRiC complex plays a role in the folding of actin and tubulin. Belongs to the TCP-1 chaperonin family. 2 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
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Protein type: Chaperone |
Chromosomal Location of mouse Ortholog: 5|5 G1.3 |
Cellular Component:
acrosomal vesicle; cell body; chaperonin-containing T-complex; cytoplasm; cytosol; microtubule; zona pellucida receptor complex
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Molecular Function:
ATP binding; ATP hydrolysis activity; ATP-dependent protein folding chaperone; nucleotide binding; protein binding; protein folding chaperone; unfolded protein binding; WD40-repeat domain binding
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Biological Process:
binding of sperm to zona pellucida; chaperone-mediated protein folding; positive regulation of establishment of protein localization to telomere; positive regulation of telomere maintenance via telomerase; protein folding; protein stabilization
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Reference #:
P80317
(UniProtKB)
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Alt. Names/Synonyms: CCT-zeta; CCT-zeta-1; Cct6; Cct6a; Cctz; Cctz-1; Cctz1; chaperonin containing TCP-1; chaperonin containing Tcp1, subunit 6a (zeta); chaperonin subunit 6a (zeta); T-complex protein 1 subunit zeta; TCP-1-zeta; TCPZ
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Gene Symbols: Cct6a
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Molecular weight:
58,004 Da
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Basal Isoelectric point:
6.63
Predict pI for various phosphorylation states
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