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
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
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.
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Cloned BBS8/TTC8; protein localizes to centrosomes, basal bodies and ciliated structures including the retinal connecting cilium, interacts with PCM1, and a null mutation causes left-right asymmetry randomization (nodal cilium defect).
"BBS8 localizes specifically to ciliated structures, such as the connecting cilium of the retina and columnar epithelial cells in the lung. In cells, BBS8 localizes to centrosomes and basal bodies and interacts with PCM1."
Dissection of epistasis in oligogenic Bardet-Biedl syndrome.
A core complex of BBS proteins cooperates with the GTPase Rab8 to promote ciliary membrane biogenesis.
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Identified the BBSome (seven conserved BBS proteins, including BBS8) by mass spectrometry; localizes to centriolar satellites and the ciliary membrane; required for ciliogenesis; cooperates with the Rab8 GEF Rabin8 for ciliary membrane biogenesis.
"Here we identify a complex composed of seven highly conserved BBS proteins. This complex, the BBSome, localizes to nonmembranous centriolar satellites in the cytoplasm but also to the membrane of the cilium."
Recruitment of PCM1 to the centrosome by the cooperative action of DISC1 and BBS4: a candidate for psychiatric illnesses.
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Centered on PCM1 recruitment to the centrosome by DISC1 and BBS4; the TTC8 annotation reflects a BBS8-PCM1 interaction consistent with PMID:14520415.
"Recruitment of PCM1 to the centrosome by the cooperative action of DISC1 and BBS4."
A BBSome subunit links ciliogenesis, microtubule stability, and acetylation.
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The BBSome is a stable complex functioning in membrane trafficking to and inside the primary cilium; identified BBIP10 as an eighth subunit.
"seven highly conserved BBS proteins form a stable complex, the BBSome, that functions in membrane trafficking to and inside the primary cilium."
BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and mediate BBSome assembly.
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BBS chaperonins mediate BBSome assembly; TTC8 is a BBSome component.
"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.
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LZTFL1 regulates ciliary trafficking of the BBSome (including TTC8) and Smoothened; the BBSome traffics into the cilium, contributing to SHH-pathway regulation.
"A novel protein LZTFL1 regulates ciliary trafficking of the BBSome and Smoothened."
Direct role of Bardet-Biedl syndrome proteins in transcriptional regulation.
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BBS7 binds the polycomb member RNF2 and a nuclear/transcriptional role is proposed for BBS proteins; basis of the peripheral TTC8 RNA Pol II TF-binding IPI.
"BBS7 protein (localized in the centrosomes, basal bodies and cilia) probably has a nuclear role."
The centriolar satellite protein AZI1 interacts with BBS4 and regulates ciliary trafficking of the BBSome.
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AZI1/CEP131 interacts with BBS4 and regulates BBSome ciliary trafficking; TTC8 is a BBSome component and interacts with CEP131 (Q9UPN4).
"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.
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BBS1 and BBS3 regulate ciliary trafficking of polycystin-1 (PKD1); TTC8 IPI annotations link it to PKD1 and related cargo.
"Bardet-Biedl syndrome proteins 1 and 3 regulate the ciliary trafficking of polycystic kidney disease 1 protein."
Nephrocystin proteins NPHP5 and Cep290 regulate BBSome integrity, ciliary trafficking and cargo delivery.
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NPHP5 and Cep290 regulate BBSome integrity and ciliary trafficking; Cep290 depletion causes dissociation and loss of ciliary BBS8.
"Depletion of Cep290, another transition zone protein that directly binds to NPHP5, causes additional dissociation of BBS8 and loss of ciliary BBS8."
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
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High-throughput mitochondrial proteome study; TTC8 appears as a single HTP hit, most plausibly a co-purification/contaminant given its established cytoplasmic/ciliary biology.
"Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context."
Falcon deep research report for TTC8
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TTC8/BBS8 is a structural/adaptor (non-catalytic) core BBSome subunit with 12 TPR repeats folded into an alpha-solenoid; loss of the single subunit destabilizes the whole complex. Cargo (e.g. GPCR) recognition by the holo-BBSome is attributed in the report mainly to BBS1, with TTC8 contributing indirectly via structural integrity. A photoreceptor-specific splice mutation (IVS1-2A>G) ablates BBS8 in photoreceptors and causes non-syndromic retinitis pigmentosa.
"Unlike catalytic proteins, TTC8/BBS8 participates in protein-protein interactions to mediate membrane trafficking within primary cilia."
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