TCP1 (CCT1) notes

Deep research: skipped because the providers are unavailable here. The review is based on UniProt P17987 and cached publications.

Key findings

• TCP1 acts as a cytosolic chaperone for tubulin, and ATP hydrolysis is required PMID:1630491.
• Human TRiC contains all eight subunits PMID:23011926.
• CCT1 is a higher-affinity ATP-binding subunit PMID:23041314.
• TRiC folds TCAB1 PMID:25467444. The telomere and Cajal-body process rows are client-specific consequences and were kept as non-core.
• CCT works with BBS6/10/12 in BBSome assembly at the centrosome PMID:20080638.

Decisions

• The core MF is ATP binding, and the subunit contributes to GO:0140662 ATP-dependent protein folding chaperone. This matches the worm cct-1 review.
• Protein folding chaperone (GO:0044183) rows were modified to GO:0140662.
• Protein-binding rows were removed: CCT subunit-subunit rows as redundant with complex membership, and client rows as uninformative.
• The microtubule IDA (PMID:21525035, a PEX14 paper, abstract only) was left UNDECIDED.