Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Global landscape of protein complexes in the yeast Saccharomyces cerevisiae.
Quantitative actin folding reactions using yeast CCT purified via an internal tag in the CCT3/gamma subunit.
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Purified yeast CCT, tagged through CCT3, catalyzes ATP-dependent actin folding; this supports protein-folding and chaperonin activity annotations for CCT6 as a TRiC/CCT subunit.
"The eukaryotic cytosolic chaperonin CCT is an essential ATP-dependent protein folding machine whose action is required for folding the cytoskeletal proteins actin and tubulin"
Physiological effects of unassembled chaperonin Cct subunits in the yeast Saccharomyces cerevisiae.
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Yeast CCT is a double-ring complex with a stoichiometric set of eight distinct Cct subunits.
"Eukaryotic chaperonins, the Cct complexes, are assembled into two rings, each of which is composed of a stoichiometric array of eight different subunits"
An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell.
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The chaperone interactome study is useful context for CCT contacts but reports indirect TAP-tag interactions rather than a specific molecular activity.
"It should be emphasized that the interactions presented are indirect TAP-tag based interactions and not direct binary interactions."
The social and structural architecture of the yeast protein interactome.
Falcon deep research report for CCT6
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The Falcon report was reviewed and synthesized into the CCT6 curation, including core-function framing, family/PANTHER context, and evidence limitations.