BBS9 is an integral subunit of the BBSome, an eight-protein complex that contributes to membrane-protein trafficking at cilia. It provides multiple contacts with other BBSome subunits and helps organize assembly of the complex. Its N-terminal region forms a beta-propeller, while other regions participate in subunit association. BBS9 occurs in cytoplasmic and ciliary compartments, including the ciliary base and centriolar satellites. Loss of BBS9 can disrupt BBSome organization and ciliary assembly or trafficking in a manner that depends on the cell and organism studied. Biallelic pathogenic variants cause Bardet-Biedl syndrome, with features that can include retinal degeneration, obesity, polydactyly and renal abnormalities.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0016020 membrane | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: BBS9 has a supported membrane-associated location. Reason: Retain the broad localization. BBS9 is an integral component of the peripheral BBSome, which associates with the ciliary membrane; the location neither requires a transmembrane segment nor claims autonomous lipid binding. A broad true location need not be relabeled as a different source assertion. |
| GO:0034464 BBSome | IBA GO_REF:0000033 | ACCEPT | Summary: BBS9 is a constituent of the BBSome. Reason: Membership in the stable BBSome is a defining role of BBS9, supported by complex purification, subunit association and assembly perturbation experiments. This complex membership does not assign the enzymatic activities of associated ARL6, Rabin8 or chaperonins to BBS9. |
| GO:0060271 cilium assembly | IBA GO_REF:0000033 | ACCEPT | Summary: BBS9 contributes to cilium assembly in the tested biological contexts. Reason: Retain the existing cilium-assembly process. PMID:22479622 reports that Bbs9 shRNA in mouse IMCD3 cells increases the number of unciliated cells and shortens residual cilia, while zebrafish bbs9 morpholino perturbation reduces Kupffer-vesicle cilia number and length. The paper discusses a weaker effect in earlier RPE-cell assays, so these results support a conserved, context-dependent contribution without establishing universal necessity for initiation of every primary cilium. Human wild-type mRNA rescues the measured zebrafish eye phenotype; this is not a direct human-cell ciliogenesis assay. |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: BBS9 has a cytoplasmic pool. Reason: The broad cytoplasmic location is compatible with assembly and trafficking of the BBSome between cytoplasmic, centrosomal and ciliary compartments. It does not imply an exclusively cytoplasmic protein. |
| GO:0005813 centrosome | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: BBS9 localizes in the centrosomal region. Reason: Retain the broad centrosomal location. It is compatible with centriolar-satellite and pericentriolar pools of BBS9; it does not assert a structural role in centriole formation. |
| GO:0034451 centriolar satellite | IEA GO_REF:0000044 | ACCEPT | Summary: BBS9 localizes to centriolar satellites. Reason: This is a supported localization of the BBSome. In the CEP290 study, the Results explicitly report a BBS9 localization pattern similar to BBS4 in hTERT-RPE1 cells, including centriolar satellites. The PCM1/dynactin adaptor mechanism of BBS4 is not assigned to BBS9. |
| GO:0034464 BBSome | IEA GO_REF:0000120 | ACCEPT | Summary: BBS9 is a constituent of the BBSome. Reason: Membership in the stable BBSome is a defining role of BBS9, supported by complex purification, subunit association and assembly perturbation experiments. This complex membership does not assign the enzymatic activities of associated ARL6, Rabin8 or chaperonins to BBS9. |
| GO:0060170 ciliary membrane | IEA GO_REF:0000044 | ACCEPT | Summary: BBS9 associates with the ciliary membrane as part of the BBSome. Reason: The source location describes the membrane-associated trafficking complex and is consistent with the founding BBSome study. It does not identify BBS9 as a transmembrane protein or an autonomous membrane receptor. |
| GO:0005515 protein binding | IPI PMID:17574030 A core complex of BBS proteins cooperates with the GTPase Ra... | MODIFY | Summary: The BBS9–BBS5 association supports its BBSome scaffold role. Reason: The founding BBSome purification study attributes an association with BBS5. Independent assembly experiments in PMID:22500027 identify BBS9 contacts with BBS1, BBS2, BBS5 and BBS8 and show loss of downstream complex incorporation after BBS9 depletion. These contacts implement BBS9's integral scaffold role, a more informative function than generic binding. This refinement uses the independent mechanistic evidence rather than claiming that the original screening experiment alone proves scaffolding or direct endogenous affinity. Proposed replacements: protein complex scaffold activity |
| GO:0005515 protein binding | IPI PMID:19081074 A BBSome subunit links ciliogenesis, microtubule stability, ... | KEEP AS NON CORE | Summary: BBS9 has a source-attributed association with BBS4. Reason: Retain the source-attributed association with BBS4 in the BBIP1/BBSome study. This co-complex association is coherent with BBSome assembly. The selected ordered-assembly evidence does not independently establish that this exact BBS4 association is a direct scaffold interface; no specific replacement is imposed. |
| GO:0005515 protein binding | IPI PMID:20080638 BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family c... | KEEP AS NON CORE | Summary: BBS9 has a source-attributed association with BBS12. Reason: Retain the source-attributed association with BBS12 in the chaperonin-assisted BBSome assembly study. Association with the BBSome assembly machinery does not establish that BBS9 itself folds a client protein or hydrolyzes ATP. |
| GO:0005515 protein binding | IPI PMID:22072986 A novel protein LZTFL1 regulates ciliary trafficking of the ... | KEEP AS NON CORE | Summary: BBS9 has a source-attributed association with LZTFL1. Reason: Retain the source-attributed association with LZTFL1 in the LZTFL1 trafficking study. LZTFL1 regulates BBSome trafficking through BBS9 association, but that does not by itself identify a separate molecular activity of BBS9 beyond the supported interaction context. |
| GO:0005515 protein binding | IPI PMID:22139371 Bardet-Biedl syndrome 3 (Bbs3) knockout mouse model reveals ... | MODIFY | Summary: The BBS9–BBS2 association supports its BBSome scaffold role. Reason: The Bbs3-associated BBSome study attributes an association with BBS2. Independent assembly experiments in PMID:22500027 identify BBS9 contacts with BBS1, BBS2, BBS5 and BBS8 and show loss of downstream complex incorporation after BBS9 depletion. These contacts implement BBS9's integral scaffold role, a more informative function than generic binding. This refinement uses the independent mechanistic evidence rather than claiming that the original screening experiment alone proves scaffolding or direct endogenous affinity. Proposed replacements: protein complex scaffold activity |
| GO:0005515 protein binding | IPI PMID:22500027 Intrinsic protein-protein interaction-mediated and chaperoni... | MODIFY | Summary: The BBS9–BBS5 association supports its BBSome scaffold role. Reason: The original PMID:22500027 itself supports the BBS9-BBS5 association in the ordered-assembly study. Its BBS9 depletion and subunit-incorporation experiments support an integral scaffold role. This is the mechanistic source behind the refinement, not a separate independent experiment; GO:0140378 states that role more specifically than generic binding. Proposed replacements: protein complex scaffold activity |
| GO:0005515 protein binding | IPI PMID:25552655 Nephrocystin proteins NPHP5 and Cep290 regulate BBSome integ... | KEEP AS NON CORE | Summary: BBS9 has a source-attributed association with IQCB1/NPHP5. Reason: Retain the source-attributed association with IQCB1/NPHP5 in the NPHP5/CEP290 BBSome-integrity study. NPHP5 controls BBSome integrity, but this association does not make BBS9 the autonomous transition-zone gatekeeper or transfer NPHP5 binding-site functions to it. |
| GO:0005515 protein binding | IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis... | KEEP AS NON CORE | Summary: The source attributes a BBS9-BBS5 association compatible with BBSome co-complex membership. Reason: Retain the curator-attributed interaction with BBS5 (Q8N3I7). The paper maps ciliary protein complexes using tandem affinity purification and mass spectrometry of tagged proteins in HEK293T cells. Its Methods establish the assay class, but the exact BBS9 supplementary bait/prey record was not independently re-examined. Co-complex recovery is compatible with this source assertion without demonstrating a binary contact or the organizing activity of BBS9 in that experiment. Targeted assembly studies support the separate scaffold core; they do not turn this screening record into a mechanistic scaffold assay. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | KEEP AS NON CORE | Summary: BBS9 has a source-attributed association with LZTFL1. Reason: Retain the source-attributed association with LZTFL1 in the BioPlex interaction map. LZTFL1 regulates BBSome trafficking through BBS9 association, but that does not by itself identify a separate molecular activity of BBS9 beyond the supported interaction context. |
| GO:0005515 protein binding | IPI PMID:29039417 Protein interaction perturbation profiling at amino-acid res... | MODIFY | Summary: The source-attributed BBS9-TTC8 interface contributes to the BBSome scaffold. Reason: The original interaction-perturbation study specifically maps a BBS8 region required for BBS9 binding. Its curated TTC8 partner remains A0A0C4DGX9. Together with the BBS9-dependent assembly and subunit-contact evidence in PMID:22500027, this supports the specific scaffold function. HPA maps A0A0C4DGX9 to a 531-amino-acid TTC8 transcript; neither identity with Q8TAM2 nor equivalence of every isoform or assay construct is assumed. The refinement concerns BBS9 organizing the complex, not an assertion that the yeast assay alone demonstrates endogenous assembly. Proposed replacements: protein complex scaffold activity |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: The source attributes a BBS9-BBS5 association compatible with BBSome co-complex membership. Reason: Retain the curator-attributed interaction with BBS5 (Q8N3I7). The paper uses affinity-purification mass spectrometry to map 293T and HCT116 interactomes. The available extraction contains the abstract, Introduction and Discussion; the pair-specific supplement and its cell-line assignment were not independently inspected. Co-complex recovery is compatible with this source assertion without demonstrating a binary contact or the organizing activity of BBS9 in that experiment. Targeted assembly studies support the separate scaffold core; they do not turn this screening record into a mechanistic scaffold assay. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | KEEP AS NON CORE | Summary: The source attributes a BBS9-BBS1 association compatible with BBSome co-complex membership. Reason: Retain the curator-attributed interaction with BBS1 (Q8NFJ9). The paper integrates U2OS affinity-purification mass spectrometry and immunofluorescence into cell maps. The selected AP-MS Methods describe recovery of associated complexes, but the exact BBS9-BBS1 supplemental record and its modality were not independently reconstructed. Co-complex recovery is compatible with this source assertion without demonstrating a binary contact or the organizing activity of BBS9 in that experiment. Targeted assembly studies support the separate scaffold core; they do not turn this screening record into a mechanistic scaffold assay. Supporting Evidence: |
| GO:0016020 membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: BBS9 has a supported membrane-associated location. Reason: Retain the broad localization. BBS9 is an integral component of the peripheral BBSome, which associates with the ciliary membrane; the location neither requires a transmembrane segment nor claims autonomous lipid binding. A broad true location need not be relabeled as a different source assertion. |
| GO:0045444 fat cell differentiation | IEA GO_REF:0000107 | UNDECIDED | Summary: The transferred fat-cell differentiation role remains unresolved. Reason: The source Q811G0 is mouse Bbs9. The official donor table traces this process to IEP evidence in PMID:17379567, whose normal abstract reports Bbs9 transcript changes during 3T3-F442A adipogenesis. Expression changes do not establish a differentiation mechanism or perturbation phenotype. Preserve the source assertion while the complete donor experiment remains unresolved; obesity alone cannot supply the missing functional evidence. |
| GO:0060271 cilium assembly | IEA GO_REF:0000107 | ACCEPT | Summary: BBS9 contributes to cilium assembly in the tested biological contexts. Reason: Retain the existing cilium-assembly process. PMID:22479622 reports that Bbs9 shRNA in mouse IMCD3 cells increases the number of unciliated cells and shortens residual cilia, while zebrafish bbs9 morpholino perturbation reduces Kupffer-vesicle cilia number and length. The paper discusses a weaker effect in earlier RPE-cell assays, so these results support a conserved, context-dependent contribution without establishing universal necessity for initiation of every primary cilium. Human wild-type mRNA rescues the measured zebrafish eye phenotype; this is not a direct human-cell ciliogenesis assay. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5617815 | KEEP AS NON CORE | Summary: BBS9 is present in a cytosolic BBSome pool in the curated pathway. Reason: Retain the cytosolic location for the BBSome-containing event. Membership in an event involving RAB3IP, ARL6 or cargo does not confer their nucleotide-exchange, GTPase or cargo-binding activities on isolated BBS9. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5624125 | KEEP AS NON CORE | Summary: BBS9 is present in a cytosolic BBSome pool in the curated pathway. Reason: Retain the cytosolic location for the BBSome-containing event. Membership in an event involving RAB3IP, ARL6 or cargo does not confer their nucleotide-exchange, GTPase or cargo-binding activities on isolated BBS9. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5624126 | KEEP AS NON CORE | Summary: BBS9 is present in a cytosolic BBSome pool in the curated pathway. Reason: Retain the cytosolic location for the BBSome-containing event. Membership in an event involving RAB3IP, ARL6 or cargo does not confer their nucleotide-exchange, GTPase or cargo-binding activities on isolated BBS9. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5624127 | KEEP AS NON CORE | Summary: BBS9 is present in a cytosolic BBSome pool in the curated pathway. Reason: Retain the cytosolic location for the BBSome-containing event. Membership in an event involving RAB3IP, ARL6 or cargo does not confer their nucleotide-exchange, GTPase or cargo-binding activities on isolated BBS9. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5624129 | KEEP AS NON CORE | Summary: BBS9 is present in a cytosolic BBSome pool in the curated pathway. Reason: Retain the cytosolic location for the BBSome-containing event. Membership in an event involving RAB3IP, ARL6 or cargo does not confer their nucleotide-exchange, GTPase or cargo-binding activities on isolated BBS9. |
| GO:0005829 cytosol | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: BBS9 has a supported cytosolic localization. Reason: Retain the experimental cytosolic pool. The current HPA annotation rates cytosol as supported, alongside supported ciliary compartments, consistent with a mobile BBSome subunit. |
| GO:0005929 cilium | IDA GO_REF:0000052 | ACCEPT | Summary: BBS9 localizes to the cilium. Reason: Retain the immunofluorescence-derived location. The current Human Protein Atlas lists this ciliary compartment as supported. Presence at the location does not imply that BBS9 is a motor, a diffusion-barrier enzyme, or an exclusive resident there. |
| GO:0035869 ciliary transition zone | IDA GO_REF:0000052 | ACCEPT | Summary: BBS9 localizes to the ciliary transition zone. Reason: Retain the immunofluorescence-derived location. The current Human Protein Atlas lists this ciliary compartment as supported. Presence at the location does not imply that BBS9 is a motor, a diffusion-barrier enzyme, or an exclusive resident there. |
| GO:0097542 ciliary tip | IDA GO_REF:0000052 | ACCEPT | Summary: BBS9 localizes to the ciliary tip. Reason: Retain the immunofluorescence-derived location. The current Human Protein Atlas lists this ciliary compartment as supported. Presence at the location does not imply that BBS9 is a motor, a diffusion-barrier enzyme, or an exclusive resident there. |
| GO:0034464 BBSome | IPI PMID:19081074 A BBSome subunit links ciliogenesis, microtubule stability, ... | ACCEPT | Summary: BBS9 is a constituent of the BBSome. Reason: Membership in the stable BBSome is a defining role of BBS9, supported by complex purification, subunit association and assembly perturbation experiments. This complex membership does not assign the enzymatic activities of associated ARL6, Rabin8 or chaperonins to BBS9. |
| GO:0060170 ciliary membrane | IDA PMID:19081074 A BBSome subunit links ciliogenesis, microtubule stability, ... | ACCEPT | Summary: BBS9 associates with the ciliary membrane as part of the BBSome. Reason: The source location describes the membrane-associated trafficking complex and is consistent with the founding BBSome study. It does not identify BBS9 as a transmembrane protein or an autonomous membrane receptor. |
| GO:0060271 cilium assembly | NAS PMID:19081074 A BBSome subunit links ciliogenesis, microtubule stability, ... | ACCEPT | Summary: BBS9 contributes to cilium assembly in the tested biological contexts. Reason: Retain the existing cilium-assembly process. PMID:22479622 reports that Bbs9 shRNA in mouse IMCD3 cells increases the number of unciliated cells and shortens residual cilia, while zebrafish bbs9 morpholino perturbation reduces Kupffer-vesicle cilia number and length. The paper discusses a weaker effect in earlier RPE-cell assays, so these results support a conserved, context-dependent contribution without establishing universal necessity for initiation of every primary cilium. Human wild-type mRNA rescues the measured zebrafish eye phenotype; this is not a direct human-cell ciliogenesis assay. |
| GO:0061512 protein localization to cilium | IMP PMID:23943788 BBS mutations modify phenotypic expression of CEP290-related... | ACCEPT | Summary: BBS9 participates in ciliary protein localization through the BBSome. Reason: The BBS9 role in maintaining an assembled trafficking complex supports this process. In PMID:23943788, BBS9 depletion perturbs CEP290 centriolar-satellite localization; the source must not be paraphrased as abolishing CEP290 transition-zone localization. Independent human-cell BBS9 depletion in PMID:22072986 disrupts BBSome assembly and ciliary entry, providing additional process support without autonomous cargo-recognition claims. |
| GO:0005929 cilium | IDA PMID:23943788 BBS mutations modify phenotypic expression of CEP290-related... | ACCEPT | Summary: BBS9 localizes to the cilium. Reason: Retain the experimental location. The original Results explicitly describe BBS9 in hTERT-RPE1 cells with a localization pattern similar to BBS4, spanning cilium, transition zone and satellites. This is not inferred from mouse Bbs4 genetics alone. |
| GO:0034451 centriolar satellite | IDA PMID:23943788 BBS mutations modify phenotypic expression of CEP290-related... | ACCEPT | Summary: BBS9 localizes to centriolar satellites. Reason: This is a supported localization of the BBSome. In the CEP290 study, the Results explicitly report a BBS9 localization pattern similar to BBS4 in hTERT-RPE1 cells, including centriolar satellites. The PCM1/dynactin adaptor mechanism of BBS4 is not assigned to BBS9. |
| GO:0035869 ciliary transition zone | IDA PMID:23943788 BBS mutations modify phenotypic expression of CEP290-related... | ACCEPT | Summary: BBS9 localizes to the ciliary transition zone. Reason: Retain the experimental location. The original Results explicitly describe BBS9 in hTERT-RPE1 cells with a localization pattern similar to BBS4, spanning cilium, transition zone and satellites. This is not inferred from mouse Bbs4 genetics alone. |
| GO:0000242 pericentriolar material | IDA PMID:22139371 Bardet-Biedl syndrome 3 (Bbs3) knockout mouse model reveals ... | ACCEPT | Summary: BBS9 has a supported pericentriolar material localization. Reason: Retain the source experimental localization, which is coherent with the human BBSome localization evidence. The Bbs3-focused mouse-paper title is not grounds to reject a curated BBS9 assay or to assume that every experiment used mouse material. |
| GO:0005929 cilium | IDA PMID:22139371 Bardet-Biedl syndrome 3 (Bbs3) knockout mouse model reveals ... | ACCEPT | Summary: BBS9 has a supported cilium localization. Reason: Retain the source experimental localization, which is coherent with the human BBSome localization evidence. The Bbs3-focused mouse-paper title is not grounds to reject a curated BBS9 assay or to assume that every experiment used mouse material. |
| GO:0005515 protein binding | IPI PMID:24550735 The centriolar satellite protein AZI1 interacts with BBS4 an... | KEEP AS NON CORE | Summary: BBS9 has a source-attributed association with AZI1/CEP131. Reason: Retain the source-attributed association with AZI1/CEP131 in the AZI1 trafficking study. The paper reports BBS4-mediated association of AZI1 with the BBSome, so a source-attributed BBS9 co-complex association is not evidence that BBS9 is the direct AZI1 receptor. |
| GO:0005929 cilium | IDA PMID:24550735 The centriolar satellite protein AZI1 interacts with BBS4 an... | ACCEPT | Summary: BBS9 localizes to cilia in the BBSome-trafficking study. Reason: Retain the experimental location. The AZI1 study examines BBSome entry into cilia, with BBS9 used as a complex-localization readout. AZI1 regulation does not imply that BBS9 itself is the regulator or that its ciliary presence is constant in every condition. |
| GO:0034464 BBSome | IDA PMID:24550735 The centriolar satellite protein AZI1 interacts with BBS4 an... | ACCEPT | Summary: BBS9 is a constituent of the BBSome. Reason: Membership in the stable BBSome is a defining role of BBS9, supported by complex purification, subunit association and assembly perturbation experiments. This complex membership does not assign the enzymatic activities of associated ARL6, Rabin8 or chaperonins to BBS9. |
| GO:0034464 BBSome | IDA PMID:20080638 BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family c... | ACCEPT | Summary: BBS9 is a constituent of the BBSome. Reason: Membership in the stable BBSome is a defining role of BBS9, supported by complex purification, subunit association and assembly perturbation experiments. This complex membership does not assign the enzymatic activities of associated ARL6, Rabin8 or chaperonins to BBS9. |
| GO:0003674 molecular_function | ND GO_REF:0000015 | MODIFY | Summary: BBS9 provides an integral scaffold within the BBSome. Reason: An uncharacterized molecular-function root is no longer the best description. PMID:22500027 identifies BBS9 as a central scaffold through multiple subunit contacts, and BBS9 knockdown reduces incorporation of BBS1, BBS4 and BBS8 into the BBS2-containing complex. PMID:22072986 independently shows BBSome disintegration after BBS9 depletion. The specific scaffold term describes an integral complex component that holds the complex together; molecular function is not restricted to catalysis. Proposed replacements: protein complex scaffold activity |
| GO:0045444 fat cell differentiation | ISS GO_REF:0000024 | UNDECIDED | Summary: The transferred fat-cell differentiation role remains unresolved. Reason: The source Q811G0 is mouse Bbs9. The official donor table traces this process to IEP evidence in PMID:17379567, whose normal abstract reports Bbs9 transcript changes during 3T3-F442A adipogenesis. Expression changes do not establish a differentiation mechanism or perturbation phenotype. Preserve the source assertion while the complete donor experiment remains unresolved; obesity alone cannot supply the missing functional evidence. |
| GO:0034464 BBSome | IDA PMID:17574030 A core complex of BBS proteins cooperates with the GTPase Ra... | ACCEPT | Summary: BBS9 is a constituent of the BBSome. Reason: Membership in the stable BBSome is a defining role of BBS9, supported by complex purification, subunit association and assembly perturbation experiments. This complex membership does not assign the enzymatic activities of associated ARL6, Rabin8 or chaperonins to BBS9. |
| GO:0005515 protein binding | IPI PMID:17574030 A core complex of BBS proteins cooperates with the GTPase Ra... | MODIFY | Summary: The BBS9–BBS1 association supports its BBSome scaffold role. Reason: The founding BBSome purification study attributes an association with BBS1. Independent assembly experiments in PMID:22500027 identify BBS9 contacts with BBS1, BBS2, BBS5 and BBS8 and show loss of downstream complex incorporation after BBS9 depletion. These contacts implement BBS9's integral scaffold role, a more informative function than generic binding. This refinement uses the independent mechanistic evidence rather than claiming that the original screening experiment alone proves scaffolding or direct endogenous affinity. Proposed replacements: protein complex scaffold activity |
| GO:0005515 protein binding | IPI PMID:17574030 A core complex of BBS proteins cooperates with the GTPase Ra... | MODIFY | Summary: The BBS9–TTC8/BBS8 association supports its BBSome scaffold role. Reason: The founding BBSome purification study attributes an association with TTC8/BBS8. Independent assembly experiments in PMID:22500027 identify BBS9 contacts with BBS1, BBS2, BBS5 and BBS8 and show loss of downstream complex incorporation after BBS9 depletion. These contacts implement BBS9's integral scaffold role, a more informative function than generic binding. This refinement uses the independent mechanistic evidence rather than claiming that the original screening experiment alone proves scaffolding or direct endogenous affinity. Proposed replacements: protein complex scaffold activity |
| GO:0005515 protein binding | IPI PMID:17574030 A core complex of BBS proteins cooperates with the GTPase Ra... | KEEP AS NON CORE | Summary: BBS9 has a source-attributed association with BBS4. Reason: Retain the source-attributed association with BBS4 in the founding BBSome purification study. This co-complex association is coherent with BBSome assembly. The selected ordered-assembly evidence does not independently establish that this exact BBS4 association is a direct scaffold interface; no specific replacement is imposed. |
| GO:0005515 protein binding | IPI PMID:17574030 A core complex of BBS proteins cooperates with the GTPase Ra... | MODIFY | Summary: The BBS9–BBS2 association supports its BBSome scaffold role. Reason: The founding BBSome purification study attributes an association with BBS2. Independent assembly experiments in PMID:22500027 identify BBS9 contacts with BBS1, BBS2, BBS5 and BBS8 and show loss of downstream complex incorporation after BBS9 depletion. These contacts implement BBS9's integral scaffold role, a more informative function than generic binding. This refinement uses the independent mechanistic evidence rather than claiming that the original screening experiment alone proves scaffolding or direct endogenous affinity. Proposed replacements: protein complex scaffold activity |
| GO:0005515 protein binding | IPI PMID:20080638 BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family c... | MODIFY | Summary: The BBS9–BBS5 association supports its BBSome scaffold role. Reason: The chaperonin-assisted BBSome assembly study attributes an association with BBS5. Independent assembly experiments in PMID:22500027 identify BBS9 contacts with BBS1, BBS2, BBS5 and BBS8 and show loss of downstream complex incorporation after BBS9 depletion. These contacts implement BBS9's integral scaffold role, a more informative function than generic binding. This refinement uses the independent mechanistic evidence rather than claiming that the original screening experiment alone proves scaffolding or direct endogenous affinity. Proposed replacements: protein complex scaffold activity |
| GO:0005515 protein binding | IPI PMID:20080638 BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family c... | MODIFY | Summary: The BBS9–BBS1 association supports its BBSome scaffold role. Reason: The chaperonin-assisted BBSome assembly study attributes an association with BBS1. Independent assembly experiments in PMID:22500027 identify BBS9 contacts with BBS1, BBS2, BBS5 and BBS8 and show loss of downstream complex incorporation after BBS9 depletion. These contacts implement BBS9's integral scaffold role, a more informative function than generic binding. This refinement uses the independent mechanistic evidence rather than claiming that the original screening experiment alone proves scaffolding or direct endogenous affinity. Proposed replacements: protein complex scaffold activity |
| GO:0005515 protein binding | IPI PMID:20080638 BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family c... | KEEP AS NON CORE | Summary: BBS9 has a source-attributed association with BBS10. Reason: Retain the source-attributed association with BBS10 in the chaperonin-assisted BBSome assembly study. Association with the BBSome assembly machinery does not establish that BBS9 itself folds a client protein or hydrolyzes ATP. |
| GO:0005515 protein binding | IPI PMID:20080638 BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family c... | KEEP AS NON CORE | Summary: BBS9 has a source-attributed association with BBS4. Reason: Retain the source-attributed association with BBS4 in the chaperonin-assisted BBSome assembly study. This co-complex association is coherent with BBSome assembly. The selected ordered-assembly evidence does not independently establish that this exact BBS4 association is a direct scaffold interface; no specific replacement is imposed. |
| GO:0005515 protein binding | IPI PMID:20080638 BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family c... | MODIFY | Summary: The BBS9–BBS2 association supports its BBSome scaffold role. Reason: The chaperonin-assisted BBSome assembly study attributes an association with BBS2. Independent assembly experiments in PMID:22500027 identify BBS9 contacts with BBS1, BBS2, BBS5 and BBS8 and show loss of downstream complex incorporation after BBS9 depletion. These contacts implement BBS9's integral scaffold role, a more informative function than generic binding. This refinement uses the independent mechanistic evidence rather than claiming that the original screening experiment alone proves scaffolding or direct endogenous affinity. Proposed replacements: protein complex scaffold activity |
| GO:0005515 protein binding | IPI PMID:22500027 Intrinsic protein-protein interaction-mediated and chaperoni... | MODIFY | Summary: The BBS9–BBS1 association supports its BBSome scaffold role. Reason: The original PMID:22500027 itself supports the BBS9-BBS1 association in the ordered-assembly study. Its BBS9 depletion and subunit-incorporation experiments support an integral scaffold role. This is the mechanistic source behind the refinement, not a separate independent experiment; GO:0140378 states that role more specifically than generic binding. Proposed replacements: protein complex scaffold activity |
| GO:0005515 protein binding | IPI PMID:22500027 Intrinsic protein-protein interaction-mediated and chaperoni... | MODIFY | Summary: The BBS9–BBS2 association supports its BBSome scaffold role. Reason: The original PMID:22500027 itself supports the BBS9-BBS2 association in the ordered-assembly study. Its BBS9 depletion and subunit-incorporation experiments support an integral scaffold role. This is the mechanistic source behind the refinement, not a separate independent experiment; GO:0140378 states that role more specifically than generic binding. Proposed replacements: protein complex scaffold activity |
| GO:0005515 protein binding | IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis... | KEEP AS NON CORE | Summary: The source attributes a BBS9-BBS1 association compatible with BBSome co-complex membership. Reason: Retain the curator-attributed interaction with BBS1 (Q8NFJ9). The paper maps ciliary protein complexes using tandem affinity purification and mass spectrometry of tagged proteins in HEK293T cells. Its Methods establish the assay class, but the exact BBS9 supplementary bait/prey record was not independently re-examined. Co-complex recovery is compatible with this source assertion without demonstrating a binary contact or the organizing activity of BBS9 in that experiment. Targeted assembly studies support the separate scaffold core; they do not turn this screening record into a mechanistic scaffold assay. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis... | KEEP AS NON CORE | Summary: BBS9 has a source-attributed association with BBS4. Reason: Retain the source-attributed association with BBS4 in the ciliary affinity-proteomics study. This co-complex association is coherent with BBSome assembly. The selected ordered-assembly evidence does not independently establish that this exact BBS4 association is a direct scaffold interface; no specific replacement is imposed. |
| GO:0005515 protein binding | IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis... | KEEP AS NON CORE | Summary: The source attributes a BBS9-BBS2 association compatible with BBSome co-complex membership. Reason: Retain the curator-attributed interaction with BBS2 (Q9BXC9). The paper maps ciliary protein complexes using tandem affinity purification and mass spectrometry of tagged proteins in HEK293T cells. Its Methods establish the assay class, but the exact BBS9 supplementary bait/prey record was not independently re-examined. Co-complex recovery is compatible with this source assertion without demonstrating a binary contact or the organizing activity of BBS9 in that experiment. Targeted assembly studies support the separate scaffold core; they do not turn this screening record into a mechanistic scaffold assay. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis... | KEEP AS NON CORE | Summary: BBS9 has a source-attributed association with LZTFL1. Reason: Retain the source-attributed association with LZTFL1 in the ciliary affinity-proteomics study. LZTFL1 regulates BBSome trafficking through BBS9 association, but that does not by itself identify a separate molecular activity of BBS9 beyond the supported interaction context. |
| GO:0005515 protein binding | IPI PMID:29039417 Protein interaction perturbation profiling at amino-acid res... | MODIFY | Summary: The BBS9–BBS5 association supports its BBSome scaffold role. Reason: The yeast two-hybrid interaction-perturbation study attributes an association with BBS5. Independent assembly experiments in PMID:22500027 identify BBS9 contacts with BBS1, BBS2, BBS5 and BBS8 and show loss of downstream complex incorporation after BBS9 depletion. These contacts implement BBS9's integral scaffold role, a more informative function than generic binding. This refinement uses the independent mechanistic evidence rather than claiming that the original screening experiment alone proves scaffolding or direct endogenous affinity. Proposed replacements: protein complex scaffold activity |
| GO:0005515 protein binding | IPI PMID:29039417 Protein interaction perturbation profiling at amino-acid res... | MODIFY | Summary: The BBS9–BBS1 association supports its BBSome scaffold role. Reason: The yeast two-hybrid interaction-perturbation study attributes an association with BBS1. Independent assembly experiments in PMID:22500027 identify BBS9 contacts with BBS1, BBS2, BBS5 and BBS8 and show loss of downstream complex incorporation after BBS9 depletion. These contacts implement BBS9's integral scaffold role, a more informative function than generic binding. This refinement uses the independent mechanistic evidence rather than claiming that the original screening experiment alone proves scaffolding or direct endogenous affinity. Proposed replacements: protein complex scaffold activity |
| GO:0005515 protein binding | IPI PMID:29039417 Protein interaction perturbation profiling at amino-acid res... | KEEP AS NON CORE | Summary: BBS9 has a source-attributed association with BBS4. Reason: The original yeast two-hybrid interaction-perturbation study maps BBS4-associated contacts to the C-terminal region of BBS9. This supports the curator-attributed binary association. The selected assembly experiments do not isolate the organizing contribution of that BBS4 interface, so the association remains non-core without assigning a more specific molecular function. No endogenous-affinity measurement is inferred from the yeast assay. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:29039417 Protein interaction perturbation profiling at amino-acid res... | MODIFY | Summary: The BBS9–BBS2 association supports its BBSome scaffold role. Reason: The yeast two-hybrid interaction-perturbation study attributes an association with BBS2. Independent assembly experiments in PMID:22500027 identify BBS9 contacts with BBS1, BBS2, BBS5 and BBS8 and show loss of downstream complex incorporation after BBS9 depletion. These contacts implement BBS9's integral scaffold role, a more informative function than generic binding. This refinement uses the independent mechanistic evidence rather than claiming that the original screening experiment alone proves scaffolding or direct endogenous affinity. Proposed replacements: protein complex scaffold activity |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: The source attributes a BBS9-BBS1 association compatible with BBSome co-complex membership. Reason: Retain the curator-attributed interaction with BBS1 (Q8NFJ9). The paper uses affinity-purification mass spectrometry to map 293T and HCT116 interactomes. The available extraction contains the abstract, Introduction and Discussion; the pair-specific supplement and its cell-line assignment were not independently inspected. Co-complex recovery is compatible with this source assertion without demonstrating a binary contact or the organizing activity of BBS9 in that experiment. Targeted assembly studies support the separate scaffold core; they do not turn this screening record into a mechanistic scaffold assay. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: BBS9 has a source-attributed association with LZTFL1. Reason: Retain the source-attributed association with LZTFL1 in the comparative human interactome study. LZTFL1 regulates BBSome trafficking through BBS9 association, but that does not by itself identify a separate molecular activity of BBS9 beyond the supported interaction context. |
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Download this section (compressed HTML)Q: Which BBS9 interfaces control stable BBSome assembly, and which can affect cargo transport while preserving complex integrity?
Q: How does BBS9 influence the centriolar-satellite pool of CEP290 while its transition-zone localization remains detectable in the tested cells?
Q: Do the alternative BBS9 products have distinct subunit contacts or ciliary distributions under physiological expression conditions?
Q: What experimental donor evidence, beyond an adipogenic expression timecourse, supports a role for Bbs9 in adipocyte differentiation?
Experiment: Compare BBS9 interface variants at matched expression levels, measuring pairwise subunit association, complete BBSome assembly, ciliary entry and individual cargo distributions separately. Include variants that preserve overall folding to distinguish interface defects from loss of protein stability.
Hypothesis: Different BBS9 interfaces make separable contributions to assembly and transport, while destabilizing variants affect both.
Type: controlled biochemical and cell-based structure-function analysis
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