Function | Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. Acts as a processive microtubule polymerase. Promotes cytoplasmic microtubule nucleation and elongation. Plays a major role in organizing spindle poles. In spindle formation protects kinetochore microtubules from depolymerization by KIF2C and has an essential role in centrosomal microtubule assembly independently of KIF2C activity. Contributes to centrosome integrity. Acts as a component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge. The TACC3/ch-TOG/clathrin complex is required for the maintenance of kinetochore fiber tension. Enhances the strength of NDC80 complex-mediated kinetochore-tip microtubule attachments. |
Protein Name | Cytoskeleton-Associated Protein 5Colonic And Hepatic Tumor Overexpressed Gene ProteinCh-Tog |
Database Links | Reactome: R-HSA-141444Reactome: R-HSA-2467813Reactome: R-HSA-2500257Reactome: R-HSA-2565942Reactome: R-HSA-380259Reactome: R-HSA-380270Reactome: R-HSA-380284Reactome: R-HSA-380320Reactome: R-HSA-5620912Reactome: R-HSA-5663220Reactome: R-HSA-68877Reactome: R-HSA-8854518Reactome: R-HSA-9648025 |
Cellular Localisation | CytoplasmCytoskeletonMicrotubule Organizing CenterCentrosomeSpindle PoleSpindleChromosomeCentromereKinetochoreDetected On Centrosomes And Kinetochores During Interphase And Mitosis Independently From Tacc3 And ClathrinLocated To Spindle Poles And Microtubules During MitosisIn Complex With Tacc3 Localized To Microtubule Plus-Ends In Mitosis And InterphaseIn Complex With Tacc3 And Clathrin Localized To Inter-Microtubule Bridges In Mitotic SpindlesAccumulation Sites At Microtubule Plus Ends Protruded Approximately 100 Nm From Mapre1/Eb1 Sites In Interphase Cells |
Alternative Protein Names | Cytoskeleton-Associated Protein 5 proteinColonic And Hepatic Tumor Overexpressed Gene Protein proteinCh-Tog proteinCKAP5 proteinKIAA0097 protein |
Information sourced from Uniprot.org