Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Electronic Gene Ontology annotations created by ARBA machine learning models
Functional overlap between retinitis pigmentosa 2 protein and the tubulin-specific chaperone cofactor C.
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Cofactor C, with cofactors D and E, stimulates GTP hydrolysis by native tubulin; a conserved arginine acts as an arginine finger.
"Together with cofactors D and E, cofactor C stimulates the GTPase activity of native tubulin"
Localization in the human retina of the X-linked retinitis pigmentosa protein RP2, its homologue cofactor C and the RP2 interacting protein Arl3.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
Pathway leading to correctly folded beta-tubulin.
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Cofactor C triggers release of native beta-tubulin from the cofactor E/D-tubulin complex.
"Cofactor E binds to the cofactor D-beta-tubulin complex; interaction with cofactor C then causes the release of beta-tubulin polypeptides that are committed to the native state."
Tubulin folding cofactors as GTPase-activating proteins. GTP hydrolysis and the assembly of the alpha/beta-tubulin heterodimer.
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Tubulin cofactors act as GAPs that stimulate beta-tubulin to hydrolyze GTP, the switch for heterodimer release.
"the cofactors behave as GTPase-activating proteins, stimulating the GTP-binding protein beta-tubulin to hydrolyze its GTP"
ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin.
The solution structure of the N-terminal domain of human tubulin binding cofactor C reveals a platform for tubulin interaction.
Tubulin cofactors and Arl2 are cage-like chaperones that regulate the soluble αβ-tubulin pool for microtubule dynamics.
The dual role of fission yeast Tbc1/cofactor C orchestrates microtubule homeostasis in tubulin folding and acts as a GAP for GTPase Alp41/Arl2.
Tubulin binding cofactor C (TBCC) suppresses tumor growth and enhances chemosensitivity in human breast cancer cells.
Silencing of tubulin binding cofactor C modifies microtubule dynamics and cell cycle distribution and enhances sensitivity to gemcitabine in breast cancer cells.
UniProt record for human TBCC (Q15814)