Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
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
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Basal body dysfunction is a likely cause of pleiotropic Bardet-Biedl syndrome.
The Bardet-Biedl protein BBS4 targets cargo to the pericentriolar region and is required for microtubule anchoring and cell cycle progression.
Dissection of epistasis in oligogenic Bardet-Biedl syndrome.
Bardet-Biedl syndrome genes are important in retrograde intracellular trafficking and Kupffer's vesicle cilia function.
A core complex of BBS proteins cooperates with the GTPase Rab8 to promote ciliary membrane biogenesis.
Novel interaction partners of Bardet-Biedl syndrome proteins.
Loss of Bardet-Biedl syndrome proteins alters the morphology and function of motile cilia in airway epithelia.
Recruitment of PCM1 to the centrosome by the cooperative action of DISC1 and BBS4: a candidate for psychiatric illnesses.
CEP290 interacts with the centriolar satellite component PCM-1 and is required for Rab8 localization to the primary cilium.
A BBSome subunit links ciliogenesis, microtubule stability, and acetylation.
BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and mediate BBSome assembly.
A novel protein LZTFL1 regulates ciliary trafficking of the BBSome and Smoothened.
Direct role of Bardet-Biedl syndrome proteins in transcriptional regulation.
Intrinsic protein-protein interaction-mediated and chaperonin-assisted sequential assembly of stable bardet-biedl syndrome protein complex, the BBSome.
BBS mutations modify phenotypic expression of CEP290-related ciliopathies.
The centriolar satellite protein AZI1 interacts with BBS4 and regulates ciliary trafficking of the BBSome.
Bardet-Biedl syndrome proteins 1 and 3 regulate the ciliary trafficking of polycystic kidney disease 1 protein.
A proteome-scale map of the human interactome network.
Nephrocystin proteins NPHP5 and Cep290 regulate BBSome integrity, ciliary trafficking and cargo delivery.
Widespread Expansion of Protein Interaction Capabilities by Alternative Splicing.
An organelle-specific protein landscape identifies novel diseases and molecular mechanisms.
Protein interaction perturbation profiling at amino-acid resolution.
A reference map of the human binary protein interactome.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
Dlec1 is required for spermatogenesis and male fertility in mice.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Multimodal cell maps as a foundation for structural and functional genomics.
ARL6:GTP and the BBSome bind ciliary cargo
ARL6:GTP and the BBSome target cargo to the primary cilium
LZTFL1 binds the BBSome and prevents its traffic to the cilium
Bardet-Biedl syndrome type 4 (BBS4)-null mice implicate Bbs4 in flagella formation but not global cilia assembly.
Loss of BBS proteins causes anosmia in humans and defects in olfactory cilia structure and function in the mouse.
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Bbs1- and Bbs4-deficient mice showed olfactory-cilium abnormalities, dendritic microtubule disorganization and retention of olfactory proteins in dendrites or cell bodies, with respiratory epithelium spared. These are tissue-specific observations.
Disruption of Bardet-Biedl syndrome ciliary proteins perturbs planar cell polarity in vertebrates.
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The study reports BBS/planar-cell-polarity phenotypes and genetic interactions in mouse and zebrafish. The abstract alone does not identify every Bbs4-specific genotype; preserved donor annotation provenance, rather than inferred genotype details, supports the existing non-core transfer.
Phenotypic characterization of Bbs4 null mice reveals age-dependent penetrance and variable expressivity.
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Bbs4-null mice developed age- and sex-dependent obesity, retinal dystrophy, altered lipid and hormone measurements, and behavioral differences. These organismal outcomes do not identify a direct BBS4 lipid enzyme or universal neural mechanism.
Impaired photoreceptor protein transport and synaptic transmission in a mouse model of Bardet-Biedl syndrome.
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BBS4 immunostaining was detected in photoreceptor inner segments and outer plexiform layer, with knockout tissue used as the staining control.
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Opsin mislocalization appeared early, before widespread photoreceptor loss, whereas peripherin/rds and ROM1 localization was retained. Selected light-dependent translocation was also impaired; ciliary microtubule structure could remain grossly normal.
A knockin mouse model of the Bardet-Biedl syndrome 1 M390R mutation has cilia defects, ventriculomegaly, retinopathy, and obesity.
Requirement of Bardet-Biedl syndrome proteins for leptin receptor signaling.
Bardet-Biedl syndrome 3 (Bbs3) knockout mouse model reveals common BBS-associated phenotypes and Bbs3 unique phenotypes.
BBS4 directly affects proliferation and differentiation of adipocytes.
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In mouse 3T3-F442A cells, stable Bbs4 silencing altered proliferation, adipogenic marker expression, lipid droplets and triglyceride accumulation. Selected knockdown and overexpression experiments showed opposing proliferation effects.
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The perturbation evidence supports the existing non-core adipocyte context beyond expression alone; the molecular step remains unresolved, and this does not assign transcription-factor or lipid-catalytic activity to BBS4.
BBS4 is required for intraflagellar transport coordination and basal body number in mammalian olfactory cilia.
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Bbs4-null olfactory sensory neurons had fewer and shorter cilia, fewer basal bodies and altered IFT-A/B transport coordination. Residual cilia retained entry of tested olfactory signaling proteins and BBSome reporters.
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Adenoviral BBS4 expression partly restored ciliary length and olfactory responses in mature neurons, without restoring cilium or basal-body numbers in the reported interval. These limits prevent a universal cargo-entry or complete-rescue claim.
BBS4 Is Essential for Nuclear Transport of Transcription Factors Mediating Neuronal ER Stress Response.