CCT2 encodes the essential beta subunit of the cytosolic CCT/TRiC group II chaperonin, contributing ATP binding, ATP hydrolysis-coupled allostery, and substrate interaction surfaces needed for folding actin, tubulin, and other cytosolic clients.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0006457 protein folding | IBA GO_REF:0000033 | ACCEPT | Summary: protein folding reviewed for CCT2: ACCEPT. Reason: Retain as the core process carried out by the CCT/TRiC chaperonin containing Cct2. Supporting Evidence: file:yeast/CCT2/CCT2-deep-research-falcon.md CCT/TRiC is the eukaryotic **Group II cytosolic chaperonin** and forms an **ATP-dependent protein-folding machine** |
| GO:0005832 chaperonin-containing T-complex | IBA GO_REF:0000033 | ACCEPT | Summary: chaperonin-containing T-complex reviewed for CCT2: ACCEPT. Reason: Retain; Cct2 is a core subunit of the chaperonin-containing T-complex/CCT. Supporting Evidence: file:yeast/CCT2/CCT2-deep-research-falcon.md Cct2p (**CCT2**) is one of the eight essential subunits that assemble into the full CCT/TRiC complex |
| GO:0051082 unfolded protein binding | IBA GO_REF:0000033 | MODIFY | Summary: unfolded protein binding reviewed for CCT2: MODIFY. Reason: Unfolded protein binding is too broad for CCT2; the complex-level function is ATP-dependent protein folding chaperone activity. Because Cct2 is one subunit of the CCT/TRiC complex, any final GOA replacement with GO:0140662 should use the contributes_to qualifier. Proposed replacements: ATP-dependent protein folding chaperone Supporting Evidence: file:yeast/CCT2/CCT2-deep-research-falcon.md CCT/TRiC operates through an **ATP-driven conformational cycle** that couples ATP binding/hydrolysis to **lid closure** and substrate encapsulation |
| GO:0000166 nucleotide binding | IEA GO_REF:0000043 | MODIFY | Summary: nucleotide binding reviewed for CCT2: MODIFY. Reason: Nucleotide binding is too general; Cct2 has a conserved ATP-binding/hydrolysis chaperonin domain. Proposed replacements: ATP binding ATP hydrolysis activity Supporting Evidence: file:yeast/CCT2/CCT2-deep-research-falcon.md CCT/TRiC operates through an **ATP-driven conformational cycle** that couples ATP binding/hydrolysis to **lid closure** and substrate encapsulation |
| GO:0005524 ATP binding | IEA GO_REF:0000120 | ACCEPT | Summary: ATP binding reviewed for CCT2: ACCEPT. Reason: Retain as a direct subunit molecular function supported by conserved CCT ATPase-domain biology. Supporting Evidence: file:yeast/CCT2/CCT2-deep-research-falcon.md Each subunit has a conserved chaperonin fold with **three domains**, including an equatorial domain that contains the ATP-binding site |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: cytoplasm reviewed for CCT2: ACCEPT. Reason: Retain as a broad localization consistent with cytosolic CCT/TRiC function. Supporting Evidence: file:yeast/CCT2/CCT2-deep-research-falcon.md CCT/TRiC is classically considered a **cytosolic chaperonin** central to folding/assembly of cytoskeletal and other complex substrates |
| GO:0005829 cytosol | IEA GO_REF:0000002 | ACCEPT | Summary: cytosol reviewed for CCT2: ACCEPT. Reason: Retain as the more precise core localization for cytosolic CCT/TRiC. Supporting Evidence: file:yeast/CCT2/CCT2-deep-research-falcon.md CCT/TRiC is classically considered a **cytosolic chaperonin** central to folding/assembly of cytoskeletal and other complex substrates |
| GO:0005832 chaperonin-containing T-complex | IEA GO_REF:0000120 | ACCEPT | Summary: chaperonin-containing T-complex reviewed for CCT2: ACCEPT. Reason: Retain; Cct2 is a core subunit of the chaperonin-containing T-complex/CCT. Supporting Evidence: file:yeast/CCT2/CCT2-deep-research-falcon.md Cct2p (**CCT2**) is one of the eight essential subunits that assemble into the full CCT/TRiC complex |
| GO:0006457 protein folding | IEA GO_REF:0000120 | ACCEPT | Summary: protein folding reviewed for CCT2: ACCEPT. Reason: Retain as the core process carried out by the CCT/TRiC chaperonin containing Cct2. Supporting Evidence: file:yeast/CCT2/CCT2-deep-research-falcon.md CCT/TRiC is the eukaryotic **Group II cytosolic chaperonin** and forms an **ATP-dependent protein-folding machine** |
| GO:0016887 ATP hydrolysis activity | IEA GO_REF:0000002 | ACCEPT | Summary: ATP hydrolysis activity reviewed for CCT2: ACCEPT. Reason: Retain as the ATPase activity coupled to the CCT/TRiC folding cycle. Supporting Evidence: file:yeast/CCT2/CCT2-deep-research-falcon.md CCT/TRiC operates through an **ATP-driven conformational cycle** that couples ATP binding/hydrolysis to **lid closure** and substrate encapsulation |
| GO:0051082 unfolded protein binding | IEA GO_REF:0000120 | MODIFY | Summary: unfolded protein binding reviewed for CCT2: MODIFY. Reason: Unfolded protein binding is too broad for CCT2; the complex-level function is ATP-dependent protein folding chaperone activity. Because Cct2 is one subunit of the CCT/TRiC complex, any final GOA replacement with GO:0140662 should use the contributes_to qualifier. Proposed replacements: ATP-dependent protein folding chaperone Supporting Evidence: file:yeast/CCT2/CCT2-deep-research-falcon.md CCT/TRiC operates through an **ATP-driven conformational cycle** that couples ATP binding/hydrolysis to **lid closure** and substrate encapsulation |
| GO:0140662 ATP-dependent protein folding chaperone | IEA GO_REF:0000002 | ACCEPT | Summary: ATP-dependent protein folding chaperone reviewed for CCT2: ACCEPT. Reason: Retain as the best complex-level molecular-function annotation for Cct2-containing CCT/TRiC. Supporting Evidence: file:yeast/CCT2/CCT2-deep-research-falcon.md CCT/TRiC is the eukaryotic **Group II cytosolic chaperonin** and forms an **ATP-dependent protein-folding machine** |
| GO:0005515 protein binding | IPI PMID:16554755 Global landscape of protein complexes in the yeast Saccharom... | MARK AS OVER ANNOTATED | Summary: protein binding reviewed for CCT2: MARK_AS_OVER_ANNOTATED. Reason: Protein binding is generic and less informative than CCT complex membership and ATP-dependent chaperonin activity. Supporting Evidence: file:yeast/CCT2/CCT2-deep-research-falcon.md Cct2p is robustly detected in purified CCT complexes; the same purifications identify known substrates/partners, including **actin** and **beta-tubulin** |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: protein binding reviewed for CCT2: MARK_AS_OVER_ANNOTATED. Reason: Protein binding is generic and less informative than CCT complex membership and ATP-dependent chaperonin activity. Supporting Evidence: file:yeast/CCT2/CCT2-deep-research-falcon.md Cct2p is robustly detected in purified CCT complexes; the same purifications identify known substrates/partners, including **actin** and **beta-tubulin** |
| GO:0005515 protein binding | IPI PMID:37968396 The social and structural architecture of the yeast protein ... | MARK AS OVER ANNOTATED | Summary: protein binding reviewed for CCT2: MARK_AS_OVER_ANNOTATED. Reason: Protein binding is generic and less informative than CCT complex membership and ATP-dependent chaperonin activity. Supporting Evidence: file:yeast/CCT2/CCT2-deep-research-falcon.md Cct2p is robustly detected in purified CCT complexes; the same purifications identify known substrates/partners, including **actin** and **beta-tubulin** |
| GO:0006457 protein folding | IDA PMID:16762366 Quantitative actin folding reactions using yeast CCT purifie... | ACCEPT | Summary: protein folding reviewed for CCT2: ACCEPT. Reason: Retain as the core process carried out by the CCT/TRiC chaperonin containing Cct2. Supporting Evidence: file:yeast/CCT2/CCT2-deep-research-falcon.md Best-supported client classes include actin and tubulin, which are repeatedly emphasized as major/obligate substrates of TRiC/CCT |
| GO:0005515 protein binding | IPI PMID:17429077 Functional interaction between phosducin-like protein 2 and ... | MARK AS OVER ANNOTATED | Summary: protein binding reviewed for CCT2: MARK_AS_OVER_ANNOTATED. Reason: Protein binding is generic and less informative than CCT complex membership and ATP-dependent chaperonin activity. Supporting Evidence: file:yeast/CCT2/CCT2-deep-research-falcon.md Cct2p is robustly detected in purified CCT complexes; the same purifications identify known substrates/partners, including **actin** and **beta-tubulin** |
| GO:0005737 cytoplasm | HDA PMID:11914276 Subcellular localization of the yeast proteome. | ACCEPT | Summary: cytoplasm reviewed for CCT2: ACCEPT. Reason: Retain as a broad localization consistent with cytosolic CCT/TRiC function. Supporting Evidence: file:yeast/CCT2/CCT2-deep-research-falcon.md CCT/TRiC is classically considered a **cytosolic chaperonin** central to folding/assembly of cytoskeletal and other complex substrates |
| GO:0005832 chaperonin-containing T-complex | IPI PMID:15704212 Physiological effects of unassembled chaperonin Cct subunits... | ACCEPT | Summary: chaperonin-containing T-complex reviewed for CCT2: ACCEPT. Reason: Retain; Cct2 is a core subunit of the chaperonin-containing T-complex/CCT. Supporting Evidence: file:yeast/CCT2/CCT2-deep-research-falcon.md Cct2p (**CCT2**) is one of the eight essential subunits that assemble into the full CCT/TRiC complex |
| GO:0005832 chaperonin-containing T-complex | IDA PMID:16762366 Quantitative actin folding reactions using yeast CCT purifie... | ACCEPT | Summary: chaperonin-containing T-complex reviewed for CCT2: ACCEPT. Reason: Retain; Cct2 is a core subunit of the chaperonin-containing T-complex/CCT. Supporting Evidence: file:yeast/CCT2/CCT2-deep-research-falcon.md Cct2p (**CCT2**) is one of the eight essential subunits that assemble into the full CCT/TRiC complex |
| GO:0051082 unfolded protein binding | IDA PMID:16762366 Quantitative actin folding reactions using yeast CCT purifie... | MODIFY | Summary: unfolded protein binding reviewed for CCT2: MODIFY. Reason: Unfolded protein binding is too broad for CCT2; the complex-level function is ATP-dependent protein folding chaperone activity. Because Cct2 is one subunit of the CCT/TRiC complex, any final GOA replacement with GO:0140662 should use the contributes_to qualifier. Proposed replacements: ATP-dependent protein folding chaperone Supporting Evidence: file:yeast/CCT2/CCT2-deep-research-falcon.md CCT/TRiC operates through an **ATP-driven conformational cycle** that couples ATP binding/hydrolysis to **lid closure** and substrate encapsulation |
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Download this section (compressed HTML)Q: Which Cct2-specific ATPase and apical-domain features determine actin-side substrate engagement in the asymmetric CCT/TRiC cycle?
Q: How much of the reported nuclear TRiC/CCT function requires Cct2-specific surfaces versus intact holo-complex abundance?
Experiment: Introduce endogenous CCT2 ATP-site and apical-domain mutants and assay holo-complex assembly, ATPase cycling, actin/tubulin folding, cytoskeletal organization, and nuclear TRiC localization/function.
Hypothesis: Cct2 ATP-site and apical-domain residues make separable contributions to chaperonin allostery and client recognition.
Type: structure-guided mutagenesis
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