KIF3B is a kinesin-2 family motor subunit that forms an obligate heterodimer with KIF3A; the KIF3A/KIF3B heterodimer associates with the accessory subunit KAP3 (KIFAP3) to form heterotrimeric kinesin-2 (kinesin II). KIF3B has an N-terminal kinesin motor domain with microtubule-stimulated ATPase activity, a coiled-coil stalk that pairs with KIF3A, and a C-terminal tail that binds KAP3 and IFT-B components such as IFT20. The complex moves processively toward microtubule plus ends and is the principal anterograde intraflagellar transport (IFT) motor, so KIF3B is essential for assembly of nodal, primary and photoreceptor cilia; mouse Kif3b knockouts lack nodal cilia and have randomized left-right asymmetry, and heterozygous human KIF3B variants cause an autosomal-dominant ciliopathy with retinitis pigmentosa, elongated cilia and impaired rhodopsin transport. Outside cilia, KIF3A/KIF3B transports membranous organelles and vesicles anterogradely in axons and dendrites (including NMDA receptor GRIN2A-containing vesicles) and contributes to mitotic spindle organization. KIF3B localizes to cilia (notably the ciliary tip), centrosome, microtubules, cytoplasm and neuronal dendrites.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003777 microtubule motor activity | IBA GO_REF:0000033 | ACCEPT | Summary: microtubule motor activity. Reason: KIF3B is a kinesin-2 motor subunit with intrinsic motor activity; the KIF3A/B complex shows plus-end-directed microtubule sliding. Core molecular activity. Supporting Evidence: PMID:7559760 The recombinant KIF3A/B complex (approximately 50-nm rod with two globular heads and a single globular tail) demonstrated plus end-directed microtubule sliding activity in vitro. PMID:7559760 we showed that KIF3B itself has motor activity in vitro |
| GO:0003777 microtubule motor activity | IEA GO_REF:0000002 | ACCEPT | Summary: microtubule motor activity. Reason: KIF3B is a kinesin-2 motor subunit with intrinsic motor activity; the KIF3A/B complex shows plus-end-directed microtubule sliding. Core molecular activity. Supporting Evidence: PMID:7559760 The recombinant KIF3A/B complex (approximately 50-nm rod with two globular heads and a single globular tail) demonstrated plus end-directed microtubule sliding activity in vitro. PMID:7559760 we showed that KIF3B itself has motor activity in vitro |
| GO:0003777 microtubule motor activity | TAS PMID:9865700 Randomization of left-right asymmetry due to loss of nodal c... | ACCEPT | Summary: microtubule motor activity. Reason: KIF3B is a kinesin-2 motor subunit with intrinsic motor activity; the KIF3A/B complex shows plus-end-directed microtubule sliding. Core molecular activity. Supporting Evidence: PMID:7559760 The recombinant KIF3A/B complex (approximately 50-nm rod with two globular heads and a single globular tail) demonstrated plus end-directed microtubule sliding activity in vitro. PMID:7559760 we showed that KIF3B itself has motor activity in vitro |
| GO:0005515 protein binding | IPI PMID:16298999 Role of the kinesin-2 family protein, KIF3, during mitosis. | REMOVE | Summary: Interaction with KIFAP3/KAP3. Reason: Interaction of KIF3B with the kinesin-2 accessory subunit KIFAP3/KAP3. The interaction is real, but 'protein binding' is uninformative and the heterotrimer is captured by the kinesin II complex part_of annotations. Removal does not mean the interaction is false. Supporting Evidence: PMID:16298999 Kinesin-2 is composed of two microtubule-based motor subunits, KIF3A/3B, and a kinesin-associated protein known as KAP3, which links KIF3A/3B to cargo that is carried to cellular organelles along microtubules in interphase cells. |
| GO:0005515 protein binding | IPI PMID:19635168 Regulation of mitotic spindle formation by the RhoA guanine ... | REMOVE | Summary: Protein binding with UniProtKB:O15013. Reason: Generic protein binding from a high-throughput interaction screen. 'Protein binding' is uninformative and no more specific molecular function is supported by this screen alone. Removal does not mean the interaction is false. |
| GO:0005515 protein binding | IPI PMID:19940036 CLC-5 and KIF3B interact to facilitate CLC-5 plasma membrane... | REMOVE | Summary: Protein binding with UniProtKB:P51795. Reason: Generic protein binding from a high-throughput interaction screen. 'Protein binding' is uninformative and no more specific molecular function is supported by this screen alone. Removal does not mean the interaction is false. |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | REMOVE | Summary: Interaction with KIFAP3/KAP3. Reason: Interaction of KIF3B with the kinesin-2 accessory subunit KIFAP3/KAP3. The interaction is real, but 'protein binding' is uninformative and the heterotrimer is captured by the kinesin II complex part_of annotations. Removal does not mean the interaction is false. Supporting Evidence: PMID:16298999 Kinesin-2 is composed of two microtubule-based motor subunits, KIF3A/3B, and a kinesin-associated protein known as KAP3, which links KIF3A/3B to cargo that is carried to cellular organelles along microtubules in interphase cells. |
| GO:0005515 protein binding | IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis... | REMOVE | Summary: Interaction with KIFAP3/KAP3. Reason: Interaction of KIF3B with the kinesin-2 accessory subunit KIFAP3/KAP3. The interaction is real, but 'protein binding' is uninformative and the heterotrimer is captured by the kinesin II complex part_of annotations. Removal does not mean the interaction is false. Supporting Evidence: PMID:16298999 Kinesin-2 is composed of two microtubule-based motor subunits, KIF3A/3B, and a kinesin-associated protein known as KAP3, which links KIF3A/3B to cargo that is carried to cellular organelles along microtubules in interphase cells. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Interaction with KIFAP3/KAP3. Reason: Interaction of KIF3B with the kinesin-2 accessory subunit KIFAP3/KAP3. The interaction is real, but 'protein binding' is uninformative and the heterotrimer is captured by the kinesin II complex part_of annotations. Removal does not mean the interaction is false. Supporting Evidence: PMID:16298999 Kinesin-2 is composed of two microtubule-based motor subunits, KIF3A/3B, and a kinesin-associated protein known as KAP3, which links KIF3A/3B to cargo that is carried to cellular organelles along microtubules in interphase cells. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Interaction with KIFAP3/KAP3. Reason: Interaction of KIF3B with the kinesin-2 accessory subunit KIFAP3/KAP3. The interaction is real, but 'protein binding' is uninformative and the heterotrimer is captured by the kinesin II complex part_of annotations. Removal does not mean the interaction is false. Supporting Evidence: PMID:16298999 Kinesin-2 is composed of two microtubule-based motor subunits, KIF3A/3B, and a kinesin-associated protein known as KAP3, which links KIF3A/3B to cargo that is carried to cellular organelles along microtubules in interphase cells. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: Interaction with KIFAP3/KAP3. Reason: Interaction of KIF3B with the kinesin-2 accessory subunit KIFAP3/KAP3. The interaction is real, but 'protein binding' is uninformative and the heterotrimer is captured by the kinesin II complex part_of annotations. Removal does not mean the interaction is false. Supporting Evidence: PMID:16298999 Kinesin-2 is composed of two microtubule-based motor subunits, KIF3A/3B, and a kinesin-associated protein known as KAP3, which links KIF3A/3B to cargo that is carried to cellular organelles along microtubules in interphase cells. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: Interaction with KIFAP3/KAP3. Reason: Interaction of KIF3B with the kinesin-2 accessory subunit KIFAP3/KAP3. The interaction is real, but 'protein binding' is uninformative and the heterotrimer is captured by the kinesin II complex part_of annotations. Removal does not mean the interaction is false. Supporting Evidence: PMID:16298999 Kinesin-2 is composed of two microtubule-based motor subunits, KIF3A/3B, and a kinesin-associated protein known as KAP3, which links KIF3A/3B to cargo that is carried to cellular organelles along microtubules in interphase cells. |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | ACCEPT | Summary: ATP binding (InterPro). Reason: Kinesin motor domains bind ATP. Electronic annotation consistent with experimental and phylogenetic evidence. Supporting Evidence: file:human/KIF3B/KIF3B-uniprot.txt Uses ATP hydrolysis to generate force to bind and move along the microtubule (By similarity). |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | ACCEPT | Summary: cytoplasm localization. Reason: Kinesin-2 is a cytoplasmic microtubule motor associated with the microtubule cytoskeleton. Supporting Evidence: PMID:16298999 Kinesin-2 is composed of two microtubule-based motor subunits, KIF3A/3B, and a kinesin-associated protein known as KAP3, which links KIF3A/3B to cargo that is carried to cellular organelles along microtubules in interphase cells. |
| GO:0005737 cytoplasm | IEA GO_REF:0000117 | ACCEPT | Summary: cytoplasm localization. Reason: Kinesin-2 is a cytoplasmic microtubule motor associated with the microtubule cytoskeleton. Supporting Evidence: PMID:16298999 Kinesin-2 is composed of two microtubule-based motor subunits, KIF3A/3B, and a kinesin-associated protein known as KAP3, which links KIF3A/3B to cargo that is carried to cellular organelles along microtubules in interphase cells. |
| GO:0005813 centrosome | IEA GO_REF:0000107 | ACCEPT | Summary: Centrosome localization. Reason: Kinesin-2 localizes to centrosomes; HPA detects KIF3B at the flagellar centriole. Supporting Evidence: PMID:16298999 the kinesin-2 complex is localized with components of the mitotic apparatus such as spindle microtubules and centrosomes PMID:41005307 We employed antibody-based spatial proteomics to expand the Human Protein Atlas to primary cilia. |
| GO:0005813 centrosome | NAS PMID:16298999 Role of the kinesin-2 family protein, KIF3, during mitosis. | ACCEPT | Summary: Centrosome localization. Reason: Kinesin-2 localizes to centrosomes; HPA detects KIF3B at the flagellar centriole. Supporting Evidence: PMID:16298999 the kinesin-2 complex is localized with components of the mitotic apparatus such as spindle microtubules and centrosomes PMID:41005307 We employed antibody-based spatial proteomics to expand the Human Protein Atlas to primary cilia. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2213248 | ACCEPT | Summary: cytosol localization. Reason: Kinesin-2 is a cytoplasmic microtubule motor associated with the microtubule cytoskeleton. Supporting Evidence: PMID:16298999 Kinesin-2 is composed of two microtubule-based motor subunits, KIF3A/3B, and a kinesin-associated protein known as KAP3, which links KIF3A/3B to cargo that is carried to cellular organelles along microtubules in interphase cells. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6811423 | ACCEPT | Summary: cytosol localization. Reason: Kinesin-2 is a cytoplasmic microtubule motor associated with the microtubule cytoskeleton. Supporting Evidence: PMID:16298999 Kinesin-2 is composed of two microtubule-based motor subunits, KIF3A/3B, and a kinesin-associated protein known as KAP3, which links KIF3A/3B to cargo that is carried to cellular organelles along microtubules in interphase cells. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6811426 | ACCEPT | Summary: cytosol localization. Reason: Kinesin-2 is a cytoplasmic microtubule motor associated with the microtubule cytoskeleton. Supporting Evidence: PMID:16298999 Kinesin-2 is composed of two microtubule-based motor subunits, KIF3A/3B, and a kinesin-associated protein known as KAP3, which links KIF3A/3B to cargo that is carried to cellular organelles along microtubules in interphase cells. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-983259 | ACCEPT | Summary: cytosol localization. Reason: Kinesin-2 is a cytoplasmic microtubule motor associated with the microtubule cytoskeleton. Supporting Evidence: PMID:16298999 Kinesin-2 is composed of two microtubule-based motor subunits, KIF3A/3B, and a kinesin-associated protein known as KAP3, which links KIF3A/3B to cargo that is carried to cellular organelles along microtubules in interphase cells. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-983266 | ACCEPT | Summary: cytosol localization. Reason: Kinesin-2 is a cytoplasmic microtubule motor associated with the microtubule cytoskeleton. Supporting Evidence: PMID:16298999 Kinesin-2 is composed of two microtubule-based motor subunits, KIF3A/3B, and a kinesin-associated protein known as KAP3, which links KIF3A/3B to cargo that is carried to cellular organelles along microtubules in interphase cells. |
| GO:0005856 cytoskeleton | IEA GO_REF:0000044 | ACCEPT | Summary: cytoskeleton localization. Reason: Kinesin-2 is a cytoplasmic microtubule motor associated with the microtubule cytoskeleton. Supporting Evidence: PMID:16298999 Kinesin-2 is composed of two microtubule-based motor subunits, KIF3A/3B, and a kinesin-associated protein known as KAP3, which links KIF3A/3B to cargo that is carried to cellular organelles along microtubules in interphase cells. |
| GO:0005871 kinesin complex | IBA GO_REF:0000033 | ACCEPT | Summary: kinesin complex. Reason: KIF3B is a motor subunit of heterotrimeric kinesin-2 (KIF3A/KIF3B/KAP3). Supporting Evidence: PMID:7559760 Immunoprecipitation assay of the brain revealed that KIF3B forms a complex with KIF3A and three other high molecular weight (approximately 100 kD)-associated polypeptides, called the kinesin superfamily-associated protein 3 (KAP3). PMID:7559760 KIF3A and KIF3B directly bind with each other in the absence of KAP3. |
| GO:0005873 plus-end kinesin complex | TAS PMID:7559760 KIF3A/B: a heterodimeric kinesin superfamily protein that wo... | ACCEPT | Summary: plus-end kinesin complex. Reason: KIF3B is a motor subunit of heterotrimeric kinesin-2 (KIF3A/KIF3B/KAP3). Supporting Evidence: PMID:7559760 Immunoprecipitation assay of the brain revealed that KIF3B forms a complex with KIF3A and three other high molecular weight (approximately 100 kD)-associated polypeptides, called the kinesin superfamily-associated protein 3 (KAP3). PMID:7559760 KIF3A and KIF3B directly bind with each other in the absence of KAP3. |
| GO:0005874 microtubule | IBA GO_REF:0000033 | ACCEPT | Summary: microtubule localization. Reason: Kinesin-2 is a cytoplasmic microtubule motor associated with the microtubule cytoskeleton. Supporting Evidence: PMID:16298999 Kinesin-2 is composed of two microtubule-based motor subunits, KIF3A/3B, and a kinesin-associated protein known as KAP3, which links KIF3A/3B to cargo that is carried to cellular organelles along microtubules in interphase cells. |
| GO:0005876 spindle microtubule | NAS PMID:16298999 Role of the kinesin-2 family protein, KIF3, during mitosis. | KEEP AS NON CORE | Summary: Colocalizes with spindle microtubules (NAS). Reason: Kinesin-2 colocalizes with mitotic spindle microtubules; secondary role. Supporting Evidence: PMID:16298999 the kinesin-2 complex is localized with components of the mitotic apparatus such as spindle microtubules and centrosomes |
| GO:0005929 cilium | IEA GO_REF:0000120 | ACCEPT | Summary: cilium localization. Reason: As the anterograde IFT motor, kinesin-2 travels to the ciliary tip; KIF3B localizes to nodal cilia and HPA detects it at the primary cilium tip (Approved). Supporting Evidence: PMID:32386558 Kinesin-2 enables ciliary assembly and maintenance as an anterograde intraflagellar transport (IFT) motor. PMID:41005307 We employed antibody-based spatial proteomics to expand the Human Protein Atlas to primary cilia. |
| GO:0005929 cilium | ISS GO_REF:0000024 | ACCEPT | Summary: cilium localization. Reason: As the anterograde IFT motor, kinesin-2 travels to the ciliary tip; KIF3B localizes to nodal cilia and HPA detects it at the primary cilium tip (Approved). Supporting Evidence: PMID:32386558 Kinesin-2 enables ciliary assembly and maintenance as an anterograde intraflagellar transport (IFT) motor. PMID:41005307 We employed antibody-based spatial proteomics to expand the Human Protein Atlas to primary cilia. |
| GO:0005929 cilium | TAS Reactome:R-HSA-5624949 | ACCEPT | Summary: cilium localization. Reason: As the anterograde IFT motor, kinesin-2 travels to the ciliary tip; KIF3B localizes to nodal cilia and HPA detects it at the primary cilium tip (Approved). Supporting Evidence: PMID:32386558 Kinesin-2 enables ciliary assembly and maintenance as an anterograde intraflagellar transport (IFT) motor. PMID:41005307 We employed antibody-based spatial proteomics to expand the Human Protein Atlas to primary cilia. |
| GO:0005929 cilium | TAS Reactome:R-HSA-5625416 | ACCEPT | Summary: cilium localization. Reason: As the anterograde IFT motor, kinesin-2 travels to the ciliary tip; KIF3B localizes to nodal cilia and HPA detects it at the primary cilium tip (Approved). Supporting Evidence: PMID:32386558 Kinesin-2 enables ciliary assembly and maintenance as an anterograde intraflagellar transport (IFT) motor. PMID:41005307 We employed antibody-based spatial proteomics to expand the Human Protein Atlas to primary cilia. |
| GO:0005929 cilium | TAS Reactome:R-HSA-5625424 | ACCEPT | Summary: cilium localization. Reason: As the anterograde IFT motor, kinesin-2 travels to the ciliary tip; KIF3B localizes to nodal cilia and HPA detects it at the primary cilium tip (Approved). Supporting Evidence: PMID:32386558 Kinesin-2 enables ciliary assembly and maintenance as an anterograde intraflagellar transport (IFT) motor. PMID:41005307 We employed antibody-based spatial proteomics to expand the Human Protein Atlas to primary cilia. |
| GO:0005929 cilium | TAS Reactome:R-HSA-5625426 | ACCEPT | Summary: cilium localization. Reason: As the anterograde IFT motor, kinesin-2 travels to the ciliary tip; KIF3B localizes to nodal cilia and HPA detects it at the primary cilium tip (Approved). Supporting Evidence: PMID:32386558 Kinesin-2 enables ciliary assembly and maintenance as an anterograde intraflagellar transport (IFT) motor. PMID:41005307 We employed antibody-based spatial proteomics to expand the Human Protein Atlas to primary cilia. |
| GO:0007018 microtubule-based movement | IBA GO_REF:0000033 | ACCEPT | Summary: microtubule-based movement. Reason: KIF3A/KIF3B kinesin-2 moves membranous organelles, vesicles and protein complexes along microtubules toward plus ends. Supporting Evidence: file:human/KIF3B/KIF3B-uniprot.txt Microtubule-based molecular motor that transport intracellular cargos, such as vesicles, organelles and protein complexes. PMID:7559760 KIF3B forms a heterodimer with KIF3A and functions as a new microtubule-based anterograde translocator for membranous organelles, and that KAP3 may determine functional diversity of the KIF3 complex in various kinds of cells in vivo. |
| GO:0007018 microtubule-based movement | IEA GO_REF:0000002 | ACCEPT | Summary: microtubule-based movement. Reason: KIF3A/KIF3B kinesin-2 moves membranous organelles, vesicles and protein complexes along microtubules toward plus ends. Supporting Evidence: file:human/KIF3B/KIF3B-uniprot.txt Microtubule-based molecular motor that transport intracellular cargos, such as vesicles, organelles and protein complexes. PMID:7559760 KIF3B forms a heterodimer with KIF3A and functions as a new microtubule-based anterograde translocator for membranous organelles, and that KAP3 may determine functional diversity of the KIF3 complex in various kinds of cells in vivo. |
| GO:0007052 mitotic spindle organization | TAS PMID:16298999 Role of the kinesin-2 family protein, KIF3, during mitosis. | KEEP AS NON CORE | Summary: mitotic spindle organization. Reason: A KIF3B mutant unable to bind KAP3 causes abnormal spindles and aneuploidy, and KIF3B knockdown induces multipolar spindles; a reported mitotic role secondary to the ciliary/transport function. Supporting Evidence: PMID:16298999 expression of a mutant KIF3B, which is able to associate with KIF3A but not KAP3 in NIH3T3 cells, caused chromosomal aneuploidy and abnormal spindle formation PMID:19635168 Quantification of multipolar spindle formation in KIF3B-knockdown cells. |
| GO:0007100 mitotic centrosome separation | TAS PMID:16298999 Role of the kinesin-2 family protein, KIF3, during mitosis. | UNDECIDED | Summary: Mitotic centrosome separation (TAS). Reason: The cached abstract reports abnormal spindle formation and aneuploidy but does not mention centrosome separation; the full text could not be checked. Supporting Evidence: PMID:16298999 expression of a mutant KIF3B, which is able to associate with KIF3A but not KAP3 in NIH3T3 cells, caused chromosomal aneuploidy and abnormal spindle formation |
| GO:0007368 determination of left/right symmetry | TAS PMID:9865700 Randomization of left-right asymmetry due to loss of nodal c... | KEEP AS NON CORE | Summary: Determination of left/right symmetry (TAS). Reason: Kif3b-null mice lack nodal cilia and show randomized left-right asymmetry; a developmental consequence of loss of nodal ciliogenesis. Supporting Evidence: PMID:9865700 the left-right asymmetry was randomized in the heart loop and the direction of embryonic turning PMID:9865700 the node lacked monocilia while the basal bodies were present |
| GO:0008017 microtubule binding | IBA GO_REF:0000033 | ACCEPT | Summary: Microtubule binding. Reason: Intrinsic to kinesin motor function. Electronic annotation consistent with experimental and phylogenetic evidence. Supporting Evidence: file:human/KIF3B/KIF3B-uniprot.txt Uses ATP hydrolysis to generate force to bind and move along the microtubule (By similarity). |
| GO:0008017 microtubule binding | IEA GO_REF:0000002 | ACCEPT | Summary: Microtubule binding. Reason: Intrinsic to kinesin motor function. Electronic annotation consistent with experimental and phylogenetic evidence. Supporting Evidence: file:human/KIF3B/KIF3B-uniprot.txt Uses ATP hydrolysis to generate force to bind and move along the microtubule (By similarity). |
| GO:0008088 axo-dendritic transport | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: axo-dendritic transport. Reason: KIF3B accumulates with anterogradely moving membranous organelles in ligated axons. Neuronal (axonal/dendritic/synaptic) role of KIF3 kinesin-2, mostly transferred from mouse Kif3b, which transports membranous organelles and NMDA receptor (GRIN2A) vesicles. A real non-ciliary transport context of the motor, kept as non-core. Supporting Evidence: PMID:7559760 accumulates with anterogradely moving membranous organelles after ligation of nerve axons file:human/KIF3B/KIF3B-uniprot.txt Transports vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit GRIN2A into neuronal dendrites (By similarity). |
| GO:0008089 anterograde axonal transport | TAS PMID:7559760 KIF3A/B: a heterodimeric kinesin superfamily protein that wo... | KEEP AS NON CORE | Summary: anterograde axonal transport. Reason: KIF3B accumulates with anterogradely moving membranous organelles in ligated axons. Neuronal (axonal/dendritic/synaptic) role of KIF3 kinesin-2, mostly transferred from mouse Kif3b, which transports membranous organelles and NMDA receptor (GRIN2A) vesicles. A real non-ciliary transport context of the motor, kept as non-core. Supporting Evidence: PMID:7559760 accumulates with anterogradely moving membranous organelles after ligation of nerve axons file:human/KIF3B/KIF3B-uniprot.txt Transports vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit GRIN2A into neuronal dendrites (By similarity). |
| GO:0008574 plus-end-directed microtubule motor activity | TAS PMID:7559760 KIF3A/B: a heterodimeric kinesin superfamily protein that wo... | ACCEPT | Summary: plus-end-directed microtubule motor activity. Reason: KIF3B is a kinesin-2 motor subunit with intrinsic motor activity; the KIF3A/B complex shows plus-end-directed microtubule sliding. Core molecular activity. Supporting Evidence: PMID:7559760 The recombinant KIF3A/B complex (approximately 50-nm rod with two globular heads and a single globular tail) demonstrated plus end-directed microtubule sliding activity in vitro. PMID:7559760 we showed that KIF3B itself has motor activity in vitro |
| GO:0015630 microtubule cytoskeleton | IDA PMID:16298999 Role of the kinesin-2 family protein, KIF3, during mitosis. | ACCEPT | Summary: microtubule cytoskeleton localization. Reason: Kinesin-2 is a cytoplasmic microtubule motor associated with the microtubule cytoskeleton. Supporting Evidence: PMID:16298999 the kinesin-2 complex is localized with components of the mitotic apparatus such as spindle microtubules and centrosomes |
| GO:0016020 membrane | HDA PMID:19946888 Defining the membrane proteome of NK cells. | KEEP AS NON CORE | Summary: Membrane (NK-cell membrane proteome, HDA). Reason: Native KIF3 is associated with membranous organelle fractions; membrane association reflects cargo binding. Supporting Evidence: PMID:7559760 KIF3 is associated with membranous organelles |
| GO:0016192 vesicle-mediated transport | IEA GO_REF:0000107 | ACCEPT | Summary: vesicle-mediated transport. Reason: KIF3A/KIF3B kinesin-2 moves membranous organelles, vesicles and protein complexes along microtubules toward plus ends. Supporting Evidence: file:human/KIF3B/KIF3B-uniprot.txt Microtubule-based molecular motor that transport intracellular cargos, such as vesicles, organelles and protein complexes. PMID:7559760 KIF3B forms a heterodimer with KIF3A and functions as a new microtubule-based anterograde translocator for membranous organelles, and that KAP3 may determine functional diversity of the KIF3 complex in various kinds of cells in vivo. |
| GO:0016887 ATP hydrolysis activity | IBA GO_REF:0000033 | ACCEPT | Summary: ATP hydrolysis activity (IBA). Reason: Kinesin motor ATPase powers movement. Supporting Evidence: file:human/KIF3B/KIF3B-uniprot.txt Uses ATP hydrolysis to generate force to bind and move along the microtubule (By similarity). |
| GO:0016939 kinesin II complex | IDA PMID:16298999 Role of the kinesin-2 family protein, KIF3, during mitosis. | ACCEPT | Summary: kinesin II complex. Reason: KIF3B is a motor subunit of heterotrimeric kinesin-2 (KIF3A/KIF3B/KAP3). Supporting Evidence: PMID:7559760 Immunoprecipitation assay of the brain revealed that KIF3B forms a complex with KIF3A and three other high molecular weight (approximately 100 kD)-associated polypeptides, called the kinesin superfamily-associated protein 3 (KAP3). PMID:7559760 KIF3A and KIF3B directly bind with each other in the absence of KAP3. |
| GO:0016939 kinesin II complex | IEA GO_REF:0000120 | ACCEPT | Summary: kinesin II complex. Reason: KIF3B is a motor subunit of heterotrimeric kinesin-2 (KIF3A/KIF3B/KAP3). Supporting Evidence: PMID:7559760 Immunoprecipitation assay of the brain revealed that KIF3B forms a complex with KIF3A and three other high molecular weight (approximately 100 kD)-associated polypeptides, called the kinesin superfamily-associated protein 3 (KAP3). PMID:7559760 KIF3A and KIF3B directly bind with each other in the absence of KAP3. |
| GO:0030425 dendrite | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: dendrite. Reason: Neuronal (axonal/dendritic/synaptic) role of KIF3 kinesin-2, mostly transferred from mouse Kif3b, which transports membranous organelles and NMDA receptor (GRIN2A) vesicles. A real non-ciliary transport context of the motor, kept as non-core. Supporting Evidence: file:human/KIF3B/KIF3B-uniprot.txt Transports vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit GRIN2A into neuronal dendrites (By similarity). |
| GO:0030425 dendrite | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: dendrite. Reason: Neuronal (axonal/dendritic/synaptic) role of KIF3 kinesin-2, mostly transferred from mouse Kif3b, which transports membranous organelles and NMDA receptor (GRIN2A) vesicles. A real non-ciliary transport context of the motor, kept as non-core. Supporting Evidence: file:human/KIF3B/KIF3B-uniprot.txt Transports vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit GRIN2A into neuronal dendrites (By similarity). |
| GO:0030705 cytoskeleton-dependent intracellular transport | IBA GO_REF:0000033 | ACCEPT | Summary: cytoskeleton-dependent intracellular transport. Reason: KIF3A/KIF3B kinesin-2 moves membranous organelles, vesicles and protein complexes along microtubules toward plus ends. Supporting Evidence: file:human/KIF3B/KIF3B-uniprot.txt Microtubule-based molecular motor that transport intracellular cargos, such as vesicles, organelles and protein complexes. PMID:7559760 KIF3B forms a heterodimer with KIF3A and functions as a new microtubule-based anterograde translocator for membranous organelles, and that KAP3 may determine functional diversity of the KIF3 complex in various kinds of cells in vivo. |
| GO:0031267 small GTPase binding | IPI PMID:19635168 Regulation of mitotic spindle formation by the RhoA guanine ... | REMOVE | Summary: Small GTPase binding, IPI with ARHGEF10 (O15013). Reason: The interacting partner recorded for this annotation, ARHGEF10, is a Dbl-family guanine nucleotide exchange factor for RhoA, not a small GTPase. The yeast two-hybrid/co-IP interaction of KIF3B with ARHGEF10 is real, but the term misdescribes it; no GO term exists for GEF binding and generic protein binding would be uninformative. Supporting Evidence: PMID:19635168 Yeast two-hybrid interaction of KIF3B with ARHGEF10. PMID:19635168 Here we show that RhoA is a substrate for ARHGEF10. |
| GO:0032839 dendrite cytoplasm | IEA GO_REF:0000108 | KEEP AS NON CORE | Summary: dendrite cytoplasm. Reason: Neuronal (axonal/dendritic/synaptic) role of KIF3 kinesin-2, mostly transferred from mouse Kif3b, which transports membranous organelles and NMDA receptor (GRIN2A) vesicles. A real non-ciliary transport context of the motor, kept as non-core. Supporting Evidence: file:human/KIF3B/KIF3B-uniprot.txt Transports vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit GRIN2A into neuronal dendrites (By similarity). |
| GO:0036372 opsin transport | IMP PMID:32386558 Mutations in the Kinesin-2 Motor KIF3B Cause an Autosomal-Do... | KEEP AS NON CORE | Summary: Opsin transport (IMP). Reason: KIF3B variants sequester rhodopsin in the rod inner segment; opsin delivery through the connecting cilium is a photoreceptor-specific cargo of kinesin-2-driven ciliary transport. Supporting Evidence: PMID:32386558 rhodopsin was sequestered to the photoreceptor rod inner segment layer with a concomitant increase in photoreceptor cilia length file:human/KIF3B/KIF3B-uniprot.txt Involved in photoreceptor integrity and opsin trafficking in rod photoreceptors |
| GO:0042073 intraciliary transport | IMP PMID:32386558 Mutations in the Kinesin-2 Motor KIF3B Cause an Autosomal-Do... | ACCEPT | Summary: Intraciliary transport (IMP). Reason: Kinesin-2 is the anterograde IFT motor; KIF3B variants impair kinesin-driven ciliary transport. Supporting Evidence: PMID:32386558 Kinesin-2 enables ciliary assembly and maintenance as an anterograde intraflagellar transport (IFT) motor. PMID:32386558 suggest that multiple KIF3B pathomechanisms can impair kinesin-driven ciliary transport in the photoreceptor |
| GO:0043197 dendritic spine | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: dendritic spine. Reason: Neuronal (axonal/dendritic/synaptic) role of KIF3 kinesin-2, mostly transferred from mouse Kif3b, which transports membranous organelles and NMDA receptor (GRIN2A) vesicles. A real non-ciliary transport context of the motor, kept as non-core. Supporting Evidence: file:human/KIF3B/KIF3B-uniprot.txt Cell projection, dendritic spine file:human/KIF3B/KIF3B-uniprot.txt Transports vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit GRIN2A into neuronal dendrites (By similarity). |
| GO:0060271 cilium assembly | IBA GO_REF:0000033 | ACCEPT | Summary: Cilium assembly. Reason: Kif3b-null nodes lack monocilia; KIF3B variants alter cilia length. Phylogenetically supported. Supporting Evidence: PMID:9865700 the node lacked monocilia while the basal bodies were present file:human/KIF3B/KIF3B-uniprot.txt Plays a role in cilia formation (PubMed:32386558). PMID:32386558 We observed a significant increase in primary cilia length in vitro in the context of either of the two mutations |
| GO:0060271 cilium assembly | IEA GO_REF:0000120 | ACCEPT | Summary: Cilium assembly. Reason: Kif3b-null nodes lack monocilia; KIF3B variants alter cilia length. Phylogenetically supported. Supporting Evidence: PMID:9865700 the node lacked monocilia while the basal bodies were present file:human/KIF3B/KIF3B-uniprot.txt Plays a role in cilia formation (PubMed:32386558). PMID:32386558 We observed a significant increase in primary cilia length in vitro in the context of either of the two mutations |
| GO:0060271 cilium assembly | IMP PMID:32386558 Mutations in the Kinesin-2 Motor KIF3B Cause an Autosomal-Do... | ACCEPT | Summary: Cilium assembly. Reason: Kif3b-null nodes lack monocilia; KIF3B variants alter cilia length. Phylogenetically supported. Supporting Evidence: PMID:9865700 the node lacked monocilia while the basal bodies were present file:human/KIF3B/KIF3B-uniprot.txt Plays a role in cilia formation (PubMed:32386558). PMID:32386558 We observed a significant increase in primary cilia length in vitro in the context of either of the two mutations |
| GO:0070062 extracellular exosome | HDA PMID:19056867 Large-scale proteomics and phosphoproteomics of urinary exos... | MARK AS OVER ANNOTATED | Summary: Extracellular exosome (urinary exosome proteomics, HDA). Reason: Detection in a urinary exosome proteome does not indicate a functional exosomal location for a cytoplasmic motor. |
| GO:0072383 plus-end-directed vesicle transport along microtubule | TAS PMID:16298999 Role of the kinesin-2 family protein, KIF3, during mitosis. | ACCEPT | Summary: plus-end-directed vesicle transport along microtubule. Reason: KIF3A/KIF3B kinesin-2 moves membranous organelles, vesicles and protein complexes along microtubules toward plus ends. Supporting Evidence: file:human/KIF3B/KIF3B-uniprot.txt Microtubule-based molecular motor that transport intracellular cargos, such as vesicles, organelles and protein complexes. PMID:7559760 KIF3B forms a heterodimer with KIF3A and functions as a new microtubule-based anterograde translocator for membranous organelles, and that KAP3 may determine functional diversity of the KIF3 complex in various kinds of cells in vivo. |
| GO:0090307 mitotic spindle assembly | IMP PMID:19635168 Regulation of mitotic spindle formation by the RhoA guanine ... | KEEP AS NON CORE | Summary: mitotic spindle assembly. Reason: A KIF3B mutant unable to bind KAP3 causes abnormal spindles and aneuploidy, and KIF3B knockdown induces multipolar spindles; a reported mitotic role secondary to the ciliary/transport function. Supporting Evidence: PMID:16298999 expression of a mutant KIF3B, which is able to associate with KIF3A but not KAP3 in NIH3T3 cells, caused chromosomal aneuploidy and abnormal spindle formation PMID:19635168 Quantification of multipolar spindle formation in KIF3B-knockdown cells. |
| GO:0097542 ciliary tip | TAS Reactome:R-HSA-5624952 | ACCEPT | Summary: ciliary tip localization. Reason: As the anterograde IFT motor, kinesin-2 travels to the ciliary tip; KIF3B localizes to nodal cilia and HPA detects it at the primary cilium tip (Approved). Supporting Evidence: PMID:32386558 Kinesin-2 enables ciliary assembly and maintenance as an anterograde intraflagellar transport (IFT) motor. PMID:41005307 We employed antibody-based spatial proteomics to expand the Human Protein Atlas to primary cilia. |
| GO:0097542 ciliary tip | TAS Reactome:R-HSA-5625416 | ACCEPT | Summary: ciliary tip localization. Reason: As the anterograde IFT motor, kinesin-2 travels to the ciliary tip; KIF3B localizes to nodal cilia and HPA detects it at the primary cilium tip (Approved). Supporting Evidence: PMID:32386558 Kinesin-2 enables ciliary assembly and maintenance as an anterograde intraflagellar transport (IFT) motor. PMID:41005307 We employed antibody-based spatial proteomics to expand the Human Protein Atlas to primary cilia. |
| GO:0097542 ciliary tip | TAS Reactome:R-HSA-5625421 | ACCEPT | Summary: ciliary tip localization. Reason: As the anterograde IFT motor, kinesin-2 travels to the ciliary tip; KIF3B localizes to nodal cilia and HPA detects it at the primary cilium tip (Approved). Supporting Evidence: PMID:32386558 Kinesin-2 enables ciliary assembly and maintenance as an anterograde intraflagellar transport (IFT) motor. PMID:41005307 We employed antibody-based spatial proteomics to expand the Human Protein Atlas to primary cilia. |
| GO:0097542 ciliary tip | TAS Reactome:R-HSA-5625426 | ACCEPT | Summary: ciliary tip localization. Reason: As the anterograde IFT motor, kinesin-2 travels to the ciliary tip; KIF3B localizes to nodal cilia and HPA detects it at the primary cilium tip (Approved). Supporting Evidence: PMID:32386558 Kinesin-2 enables ciliary assembly and maintenance as an anterograde intraflagellar transport (IFT) motor. PMID:41005307 We employed antibody-based spatial proteomics to expand the Human Protein Atlas to primary cilia. |
| GO:0098794 postsynapse | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: postsynapse. Reason: Neuronal (axonal/dendritic/synaptic) role of KIF3 kinesin-2, mostly transferred from mouse Kif3b, which transports membranous organelles and NMDA receptor (GRIN2A) vesicles. A real non-ciliary transport context of the motor, kept as non-core. Supporting Evidence: file:human/KIF3B/KIF3B-uniprot.txt Transports vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit GRIN2A into neuronal dendrites (By similarity). |
| GO:0098971 anterograde dendritic transport of neurotransmitter receptor complex | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: anterograde dendritic transport of neurotransmitter receptor complex. Reason: Neuronal (axonal/dendritic/synaptic) role of KIF3 kinesin-2, mostly transferred from mouse Kif3b, which transports membranous organelles and NMDA receptor (GRIN2A) vesicles. A real non-ciliary transport context of the motor, kept as non-core. Supporting Evidence: file:human/KIF3B/KIF3B-uniprot.txt Transports vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit GRIN2A into neuronal dendrites (By similarity). |
| GO:0098971 anterograde dendritic transport of neurotransmitter receptor complex | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: anterograde dendritic transport of neurotransmitter receptor complex. Reason: Neuronal (axonal/dendritic/synaptic) role of KIF3 kinesin-2, mostly transferred from mouse Kif3b, which transports membranous organelles and NMDA receptor (GRIN2A) vesicles. A real non-ciliary transport context of the motor, kept as non-core. Supporting Evidence: file:human/KIF3B/KIF3B-uniprot.txt Transports vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit GRIN2A into neuronal dendrites (By similarity). |
| GO:0098978 glutamatergic synapse | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: glutamatergic synapse. Reason: Neuronal (axonal/dendritic/synaptic) role of KIF3 kinesin-2, mostly transferred from mouse Kif3b, which transports membranous organelles and NMDA receptor (GRIN2A) vesicles. A real non-ciliary transport context of the motor, kept as non-core. Supporting Evidence: file:human/KIF3B/KIF3B-uniprot.txt Transports vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit GRIN2A into neuronal dendrites (By similarity). |
| GO:0120170 intraciliary transport particle B binding | IEA GO_REF:0000107 | ACCEPT | Summary: Intraciliary transport particle B binding (from mouse). Reason: KIF3B interacts directly with the IFT-B subunit IFT20, linking the motor to anterograde IFT trains. Supporting Evidence: file:human/KIF3B/KIF3B-uniprot.txt Interacts directly with IFT20 (By similarity). PMID:32386558 Kinesin-2 enables ciliary assembly and maintenance as an anterograde intraflagellar transport (IFT) motor. |
| GO:1904115 axon cytoplasm | IEA GO_REF:0000108 | KEEP AS NON CORE | Summary: axon cytoplasm. Reason: Neuronal (axonal/dendritic/synaptic) role of KIF3 kinesin-2, mostly transferred from mouse Kif3b, which transports membranous organelles and NMDA receptor (GRIN2A) vesicles. A real non-ciliary transport context of the motor, kept as non-core. Supporting Evidence: file:human/KIF3B/KIF3B-uniprot.txt Transports vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit GRIN2A into neuronal dendrites (By similarity). |
| GO:0035720 intraciliary anterograde transport | TAS PMID:32386558 Mutations in the Kinesin-2 Motor KIF3B Cause an Autosomal-Do... | NEW | Summary: Proposed: KIF3B, as a motor subunit of heterotrimeric kinesin-2, drives anterograde IFT. Reason: Kinesin-2 is the anterograde IFT motor and itself performs the transport step, so the participation test is met. KIF3B already carries the parent intraciliary transport (IMP); C. elegans KLP-11 carries the anterograde term. This refines rather than adds coverage. Supporting Evidence: PMID:32386558 Kinesin-2 enables ciliary assembly and maintenance as an anterograde intraflagellar transport (IFT) motor. PMID:32386558 suggest that multiple KIF3B pathomechanisms can impair kinesin-driven ciliary transport in the photoreceptor |
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Download this section (compressed HTML)Q: How do dominant KIF3B motor-domain (E250Q) and stalk (L523P) variants lengthen cilia: by altering kinesin-2 processivity, IFT train size, or tip turnover?
Suggested experts: Davis EE, Katsanis N
Q: Is the reported role of KIF3B in mitotic spindle organization direct (motor activity on spindle microtubules) or secondary to centrosome/cilium cycle defects?
Experiment: Single-molecule TIRF motility assays of purified KIF3A/KIF3B(E250Q or L523P)/KAP3 complexes, combined with IFT train imaging in patient-variant knock-in RPE1 cells.
Hypothesis: Dominant KIF3B ciliopathy variants alter single-molecule motility of KIF3A/KIF3B heterodimers.
Type: single-molecule biophysics
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