BBS1 is a subunit of the BBSome, a membrane-trafficking coat composed of BBS1, BBS2, BBS4, BBS5, BBS7, TTC8/BBS8, BBS9 and BBIP1. Its N-terminal beta-propeller binds GTP-loaded ARL6, helping recruit the complex to membranes. BBS1 also associates with cytoplasmic regions of signaling receptors, including Smoothened, Patched1 and the leptin receptor. These contacts contribute to cargo recognition and the regulated composition of ciliary membranes. BBS1 has cytoplasmic, centrosomal and ciliary pools and supports ciliary trafficking in sensory and other ciliated cells. Loss of BBS1 disrupts receptor trafficking and cilium function and causes BardetβBiedl syndrome.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0034464 BBSome | IBA GO_REF:0000033 | ACCEPT | Summary: BBS1 is an established component of the BBSome trafficking complex. Reason: Retain this source-specific complex-membership assertion. Biochemical identification and assembly studies converge on BBS1 membership; this does not assign every other subunit's autonomous activity to BBS1. The PAINT placement is not challenged; self-derived evidence or donor count is not a defect. |
| GO:0005813 centrosome | IBA GO_REF:0000033 | ACCEPT | Summary: BBS1 has a centrosomal/basal-body-associated pool relevant to ciliary recruitment. Reason: Retain the curator-supported localization alongside ciliary localization. PMID:18762586 highlights DISC1/BBS4 in its abstract; that focus does not disprove its BBS1 IDA annotation. The complete BBS1 imaging experiment in that paper was not independently re-read here. |
| GO:0061512 protein localization to cilium | IBA GO_REF:0000033 | ACCEPT | Summary: BBS1 contributes to localization of membrane cargo and the BBSome to cilia. Reason: Cargo localization is central to BBSome function. Preserve the existing IBA/IMP assertion with its own source; the BBS4-centered CEP290 abstract does not refute the BBS1 annotation. Separate BBS1 depletion experiments support altered PC1 ciliary targeting without a general plasma-membrane delivery defect. |
| GO:1905515 non-motile cilium assembly | IBA GO_REF:0000033 | ACCEPT | Summary: BBS1 contributes to cilium assembly in the experimentally annotated contexts. Reason: Retain the established ciliogenesis annotation without asserting an absolute requirement in every cell type: ciliary cargo defects can occur with preserved cilium length. BBSome-dependent membrane biogenesis supports the process; the existing source/evidence remains distinct from other subunits' specific tubulin effects. |
| GO:0005113 patched binding | IBA GO_REF:0000033 | ACCEPT | Summary: BBS1 associates with the ciliary signaling receptor PTCH1. Reason: PMID:22228099 includes human BBS1 constructs in reciprocal immunoprecipitation and receptor-tail mapping experiments in 293T cells. These support the specific receptor-binding function, separately from the mouse genetic and ciliary-accumulation results. Cell-lysate association is not represented as a purified binary-affinity measurement. Retain PAINT inheritance; no contrary phylogenetic placement evidence was established. |
| GO:0005119 smoothened binding | IBA GO_REF:0000033 | ACCEPT | Summary: BBS1 associates with the ciliary signaling receptor SMO. Reason: PMID:22228099 includes human BBS1 constructs in reciprocal immunoprecipitation and receptor-tail mapping experiments in 293T cells. These support the specific receptor-binding function, separately from the mouse genetic and ciliary-accumulation results. Cell-lysate association is not represented as a purified binary-affinity measurement. Retain PAINT inheritance; no contrary phylogenetic placement evidence was established. |
| GO:0005930 axoneme | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: An axonemal/ciliary-shaft-associated pool is compatible with BBSome transport. Reason: Retain the IBA location without equating a moving membrane-associated coat with a structural axonemal polymer. No target-specific loss or contrary PAINT node placement was established. |
| GO:0001895 retina homeostasis | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: BBS1 supports retinal homeostasis through photoreceptor ciliary function. Reason: Retinal degeneration is an established physiological consequence of BBS1 dysfunction, retained as tissue context rather than a distinct molecular activity. |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: BBS1 has a cytoplasmic pool before and during BBSome recruitment. Reason: The broad location is compatible with cytosolic complex assembly and ciliary recruitment; it is not an exclusive localization. |
| GO:0008104 intracellular protein localization | IEA GO_REF:0000117 | MODIFY | Summary: The localization role is more precisely described as protein localization to cilium. Reason: BBS1 participates in BBSome-dependent delivery of cargo to cilia. BBS1 depletion or mutation impairs polycystin-1 ciliary targeting without disrupting its general plasma-membrane delivery, supporting refinement of intracellular localization to the ciliary process. Proposed replacements: protein localization to cilium |
| GO:0034451 centriolar satellite | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: BBS1/BBSome associates with centriolar satellites. Reason: This supported assembly/recruitment pool is retained as non-core location context; localization does not imply BBS1 performs all centriolar-satellite functions. |
| GO:0034464 BBSome | IEA GO_REF:0000120 | ACCEPT | Summary: BBS1 is an established component of the BBSome trafficking complex. Reason: Retain this source-specific complex-membership assertion. Biochemical identification and assembly studies converge on BBS1 membership; this does not assign every other subunit's autonomous activity to BBS1. The current evidence code and original reference remain unchanged. |
| GO:0060170 ciliary membrane | IEA GO_REF:0000044 | ACCEPT | Summary: BBS1 acts with the BBSome at ciliary membranes. Reason: Membrane-associated BBSome cargo sorting supports this core localization. The BBIP1-focused paper does not transfer BBIP1-specific cytoplasmic tubulin activities to BBS1. |
| GO:1905515 non-motile cilium assembly | IEA GO_REF:0000120 | ACCEPT | Summary: BBS1 contributes to cilium assembly in the experimentally annotated contexts. Reason: Retain the established ciliogenesis annotation without asserting an absolute requirement in every cell type: ciliary cargo defects can occur with preserved cilium length. BBSome-dependent membrane biogenesis supports the process; the existing source/evidence remains distinct from other subunits' specific tubulin effects. |
| GO:0005515 protein binding | IPI PMID:17574030 A core complex of BBS proteins cooperates with the GTPase Ra... | KEEP AS NON CORE | Summary: BBS1 association with PCM1 is retained as non-core interaction context. Reason: The association is consistent with the original BBSome complex and recruitment study. It supports an interaction context without establishing an additional autonomous BBS1 activity. |
| GO:0005515 protein binding | IPI PMID:18000879 Novel interaction partners of Bardet-Biedl syndrome proteins... | KEEP AS NON CORE | Summary: BBS1 association with ALDOB is retained as non-core interaction context. Reason: The interaction screen supports this curator-attributed association. The association alone does not establish a distinct BBS1 molecular activity; pair-specific follow-up assays are not assumed. |
| GO:0005515 protein binding | IPI PMID:19081074 A BBSome subunit links ciliogenesis, microtubule stability, ... | KEEP AS NON CORE | Summary: BBS1 association with BBS4 is retained as non-core interaction context. Reason: Association with another BBSome subunit supports complex organization. It does not transfer BBIP1-specific tubulin regulation to BBS1. |
| GO:0005515 protein binding | IPI PMID:19150989 Requirement of Bardet-Biedl syndrome proteins for leptin rec... | MODIFY | Summary: BBS1 associates with the signaling receptor LEPR. Reason: BBS1 associates with LEPR, a signaling receptor, and BBS protein loss perturbs receptor trafficking. Signaling receptor binding therefore describes this interaction more precisely than protein binding. This does not assign BBS1 leptin-like ligand activity or direct receptor activation. Proposed replacements: signaling receptor binding Supporting Evidence: PMID:19150989 BBS1 protein physically interacts with the LepR |
| GO:0005515 protein binding | IPI PMID:20080638 BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family c... | KEEP AS NON CORE | Summary: BBS1 association with BBS9 is retained as non-core interaction context. Reason: The association is consistent with chaperonin-assisted BBSome assembly. It does not establish intrinsic BBS1 chaperonin or protein-folding activity. |
| GO:0005515 protein binding | IPI PMID:20603001 The conserved Bardet-Biedl syndrome proteins assemble a coat... | MODIFY | Summary: BBS1 binds the small GTPase ARL6, a BBSome recruitment factor. Reason: ARL6 is the source partner, so small GTPase binding gives an informative refinement. BBS1 is an effector/binding component, not itself a GTPase. The current IPI assertion is retained and refined; individual sources need not independently reproduce every structural detail. Proposed replacements: small GTPase binding |
| GO:0005515 protein binding | IPI PMID:22139371 Bardet-Biedl syndrome 3 (Bbs3) knockout mouse model reveals ... | MODIFY | Summary: BBS1 binds the small GTPase ARL6, a BBSome recruitment factor. Reason: ARL6 is the source partner, so small GTPase binding gives an informative refinement. BBS1 is an effector/binding component, not itself a GTPase. The current IPI assertion is retained and refined; individual sources need not independently reproduce every structural detail. Proposed replacements: small GTPase binding |
| GO:0005515 protein binding | IPI PMID:22500027 Intrinsic protein-protein interaction-mediated and chaperoni... | KEEP AS NON CORE | Summary: BBS1 association with BBS9 is retained as non-core interaction context. Reason: The association supports sequential BBSome assembly and intermediate stability. Co-immunoprecipitation does not by itself establish a purified binary interface or an additional BBS1 activity. |
| GO:0005515 protein binding | IPI PMID:25402481 Structural basis for membrane targeting of the BBSome by ARL... | MODIFY | Summary: BBS1 binds the small GTPase ARL6, a BBSome recruitment factor. Reason: ARL6 is the source partner, so small GTPase binding gives an informative refinement. BBS1 is an effector/binding component, not itself a GTPase. The crystal complex is Chlamydomonas; separate purified human N-terminal-domain binding and mutant assays support the human interaction. The construct endpoint discrepancy does not define a natural isoform. Proposed replacements: small GTPase binding |
| GO:0005515 protein binding | IPI PMID:25552655 Nephrocystin proteins NPHP5 and Cep290 regulate BBSome integ... | KEEP AS NON CORE | Summary: BBS1 association with IQCB1/NPHP5 is retained as non-core interaction context. Reason: The association places BBS1 in the NPHP5/CEP290 context that regulates BBSome integrity and cargo delivery. A separate autonomous molecular activity is not established. |
| GO:0005515 protein binding | IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis... | KEEP AS NON CORE | Summary: BBS1 association with BBS9 is retained as non-core interaction context. Reason: The ciliary affinity-proteomics association supports a complex interaction context. It is not evidence for an additional autonomous BBS1 activity or purified direct binding. |
| GO:0005515 protein binding | IPI PMID:29039417 Protein interaction perturbation profiling at amino-acid res... | KEEP AS NON CORE | Summary: BBS1 association with BBS9 is retained as non-core interaction context. Reason: Interaction-perturbation profiling supports the BBSome partner association. This interaction does not establish a separate BBS1 molecular activity. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | KEEP AS NON CORE | Summary: BBS1 association with DCTN1 isoform 5 is retained as non-core interaction context. Reason: The source-attributed interaction is retained as non-core context. The neurodegeneration-focused interaction network does not assign BBS1 an aggregation mechanism from this association alone. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: BBS1 association with BBS9 is retained as non-core interaction context. Reason: The affinity-purification association supports BBSome complex context. It does not establish a separate BBS1 molecular activity, direct contact, or validation in both sampled cell lines. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | KEEP AS NON CORE | Summary: BBS1 association with BBS9 is retained as non-core interaction context. Reason: The U2OS interaction map supports BBSome complex context. It does not establish a separate BBS1 molecular activity or a direct binding interface. |
| GO:0005102 signaling receptor binding | IEA GO_REF:0000120 | ACCEPT | Summary: BBS1 binds multiple signaling-receptor cargoes of the BBSome. Reason: The parent receptor-binding term captures a common cargo-recognition activity supported by the specific PTCH1 and SMO interactions. It is not limited to agonist binding. Retain it alongside the specific child annotations without multiplying cargo cores. |
| GO:0005813 centrosome | IEA GO_REF:0000120 | ACCEPT | Summary: BBS1 has a centrosomal/basal-body-associated pool relevant to ciliary recruitment. Reason: Retain the curator-supported localization alongside ciliary localization. PMID:18762586 highlights DISC1/BBS4 in its abstract; that focus does not disprove its BBS1 IDA annotation. The complete BBS1 imaging experiment in that paper was not independently re-read here. |
| GO:0005929 cilium | IEA GO_REF:0000107 | ACCEPT | Summary: BBS1 localizes to cilia as part of the BBSome. Reason: Retain the orthology-based broad ciliary location, corroborated by human ciliary membrane/complex studies. This is compatible with additional cytoplasmic and centrosomal pools. |
| GO:0031514 motile cilium | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Retain motile-cilium association as orthology-supported non-core context. Reason: The actual mouse donor has an MGI IMP motile-cilium annotation from PMID:18299575, which tests Bbs1-mutant airway cilia. The primary-cilium role does not invalidate that context. This does not claim direct human BBS1 motile-cilium imaging or transfer BBS2/BBS4 antibody localization to BBS1. Supporting Evidence: PMID:18299575 airway cilia from Bbs1, Bbs2, Bbs4, and Bbs6 mutant mice. |
| GO:0045444 fat cell differentiation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Retain fat-cell differentiation as physiological orthology context. Reason: Adipogenic effects are distinct from the defining BBSome cargo-recognition activity. The electronic source is preserved without turning the obesity phenotype into a new autonomous differentiation mechanism. |
| GO:0051219 phosphoprotein binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: DISC1 phosphorylation-sensitive BBS1 association supports contextual phosphoprotein binding. Reason: Mouse DISC1 S710 mutant comparisons in HT22 cells alter BBS1 co-immunoprecipitation. The homologous human DISC1 site is S713; those site assays are distinct from the mouse BBS1 association experiment. Retain the mouse-to-human electronic assertion with these limits, not a purified phosphopeptide-affinity claim. Supporting Evidence: PMID:21471969 Enhanced binding of DISC1 with BBS1 was also observed by a phospho-mimic E710-DISC1 |
| GO:0060271 cilium assembly | IEA GO_REF:0000107 | ACCEPT | Summary: BBS1 contributes to cilium assembly in the experimentally annotated contexts. Reason: Retain the established ciliogenesis annotation without asserting an absolute requirement in every cell type: ciliary cargo defects can occur with preserved cilium length. BBSome-dependent membrane biogenesis supports the process; the existing source/evidence remains distinct from other subunits' specific tubulin effects. |
| GO:0060296 regulation of cilium beat frequency involved in ciliary motility | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Bbs1-mutant airway cilia have altered beating, supporting a non-core motile-cilium role. Reason: The mouse MGI IMP donor annotation links the beat-frequency phenotype to PMID:18299575. Retain the electronic transfer as physiological context; BBS1 is not thereby a dynein motor or a universal ciliogenesis factor. Supporting Evidence: PMID:18299575 ciliary beat frequency was reduced in Bbs mutant mice. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5617815 | ACCEPT | Summary: Reactome places the BBSome in a cytosolic pool during RAB3IP association. Reason: Retain the source-specific cytosolic localization of the complex. The complete normal human event summary was read; this does not make BBS1 the catalytic GEF, GTPase, or trafficking regulator named as a separate partner. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5624125 | ACCEPT | Summary: Reactome places the BBSome in a cytosolic pool during BBSome formation. Reason: Retain the source-specific cytosolic localization of the complex. The complete normal human event summary was read; this does not make BBS1 the catalytic GEF, GTPase, or trafficking regulator named as a separate partner. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5624126 | ACCEPT | Summary: Reactome places the BBSome in a cytosolic pool during ARL6/cargo association. Reason: Retain the source-specific cytosolic localization of the complex. The complete normal human event summary was read; this does not make BBS1 the catalytic GEF, GTPase, or trafficking regulator named as a separate partner. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5624127 | ACCEPT | Summary: Reactome places the BBSome in a cytosolic pool during ciliary cargo targeting. Reason: Retain the source-specific cytosolic localization of the complex. The complete normal human event summary was read; this does not make BBS1 the catalytic GEF, GTPase, or trafficking regulator named as a separate partner. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5624129 | ACCEPT | Summary: Reactome places the BBSome in a cytosolic pool during LZTFL1 regulation. Reason: Retain the source-specific cytosolic localization of the complex. The complete normal human event summary was read; this does not make BBS1 the catalytic GEF, GTPase, or trafficking regulator named as a separate partner. |
| GO:0034464 BBSome | IPI PMID:19081074 A BBSome subunit links ciliogenesis, microtubule stability, ... | ACCEPT | Summary: BBS1 is an established component of the BBSome trafficking complex. Reason: Retain this source-specific complex-membership assertion. Biochemical identification and assembly studies converge on BBS1 membership; this does not assign every other subunit's autonomous activity to BBS1. The current evidence code and original reference remain unchanged. |
| GO:0060170 ciliary membrane | IDA PMID:19081074 A BBSome subunit links ciliogenesis, microtubule stability, ... | ACCEPT | Summary: BBS1 acts with the BBSome at ciliary membranes. Reason: Membrane-associated BBSome cargo sorting supports this core localization. The BBIP1-focused paper does not transfer BBIP1-specific cytoplasmic tubulin activities to BBS1. |
| GO:0060271 cilium assembly | NAS PMID:19081074 A BBSome subunit links ciliogenesis, microtubule stability, ... | ACCEPT | Summary: BBS1 contributes to cilium assembly in the experimentally annotated contexts. Reason: Retain the established ciliogenesis annotation without asserting an absolute requirement in every cell type: ciliary cargo defects can occur with preserved cilium length. BBSome-dependent membrane biogenesis supports the process; the existing source/evidence remains distinct from other subunits' specific tubulin effects. |
| GO:0005515 protein binding | IPI PMID:18762586 Recruitment of PCM1 to the centrosome by the cooperative act... | KEEP AS NON CORE | Summary: BBS1 association with DISC1 is retained as non-core interaction context. Reason: The DISC1 association is retained as centrosomal recruitment context. It does not establish a separate core molecular activity; the source-specific interaction remains curator-attributed. |
| GO:0005813 centrosome | IDA PMID:18762586 Recruitment of PCM1 to the centrosome by the cooperative act... | ACCEPT | Summary: BBS1 has a centrosomal/basal-body-associated pool relevant to ciliary recruitment. Reason: Retain the curator-supported localization alongside ciliary localization. PMID:18762586 highlights DISC1/BBS4 in its abstract; that focus does not disprove its BBS1 IDA annotation. The complete BBS1 imaging experiment in that paper was not independently re-read here. |
| GO:0061512 protein localization to cilium | IMP PMID:23943788 BBS mutations modify phenotypic expression of CEP290-related... | ACCEPT | Summary: BBS1 contributes to localization of membrane cargo and the BBSome to cilia. Reason: Ciliary cargo localization is central to BBSome function. The original PMID:23943788 IMP attribution is retained with curator deference: its available cached text emphasizes BBS4 and CEP290, omits Results and Methods, and does not expose the BBS1-specific experiment. Independent PMID:24939912 evidence directly supports BBS1-dependent polycystin-1 ciliary targeting, with general plasma-membrane delivery preserved. The quotation is corroboration from that separate paper, not verification of the uninspected experiment in the original source. Supporting Evidence: PMID:24939912 depletion or mutation of BBS1, but not depletion of BBS5 and BBS8, or knockout of BBS4, impairs ciliary trafficking of PC1 |
| GO:0005515 protein binding | IPI PMID:24939912 Bardet-Biedl syndrome proteins 1 and 3 regulate the ciliary ... | KEEP AS NON CORE | Summary: BBS1 association with TTC8/BBS8 is retained as non-core interaction context. Reason: The source partner is TTC8/BBS8, a BBSome subunit. Retain the curator-attributed BBS1βTTC8 association as non-core complex context. The same paper separately studies polycystin-1 cargo trafficking; those experiments do not rename the recorded partner or establish a new molecular activity for this interaction. |
| GO:0034464 BBSome | IDA PMID:24550735 The centriolar satellite protein AZI1 interacts with BBS4 an... | ACCEPT | Summary: BBS1 is an established component of the BBSome trafficking complex. Reason: Retain this source-specific complex-membership assertion. Biochemical identification and assembly studies converge on BBS1 membership; this does not assign every other subunit's autonomous activity to BBS1. The current evidence code and original reference remain unchanged. |
| GO:0061629 RNA polymerase II-specific DNA-binding transcription factor binding | IPI PMID:22302990 Direct role of Bardet-Biedl syndrome proteins in transcripti... | MODIFY | Summary: BBS1 associates with RNF2, a ubiquitin protein ligase. Reason: The original partner is RNF2/Q99496. Primary Figure 3C and corresponding Results explicitly include tagged BBS1-RNF2 co-immunoprecipitation; the BBS7-focused abstract does not negate it. RNF2 is a PRC1 ubiquitin ligase rather than the sequence-specific DNA-binding transcription factor required by the original term. Refine the partner class without asserting BBS1 ligase activity, a purified binary interaction, or BBS7-specific yeast/endogenous assays. Proposed replacements: ubiquitin protein ligase binding |
| GO:0005113 patched binding | IPI PMID:22228099 BBS proteins interact genetically with the IFT pathway to in... | ACCEPT | Summary: BBS1 associates with the ciliary signaling receptor PTCH1. Reason: PMID:22228099 includes human BBS1 constructs in reciprocal immunoprecipitation and receptor-tail mapping experiments in 293T cells. These support the specific receptor-binding function, separately from the mouse genetic and ciliary-accumulation results. Cell-lysate association is not represented as a purified binary-affinity measurement. The original IPI source is therefore retained as core cargo recognition. Supporting Evidence: PMID:22228099 Ptch1 interacts with the BBSome through the BBS1 subunit. |
| GO:0005119 smoothened binding | IPI PMID:22228099 BBS proteins interact genetically with the IFT pathway to in... | ACCEPT | Summary: BBS1 associates with the ciliary signaling receptor SMO. Reason: PMID:22228099 includes human BBS1 constructs in reciprocal immunoprecipitation and receptor-tail mapping experiments in 293T cells. These support the specific receptor-binding function, separately from the mouse genetic and ciliary-accumulation results. Cell-lysate association is not represented as a purified binary-affinity measurement. The original IPI source is therefore retained as core cargo recognition. Supporting Evidence: PMID:22228099 HA-BBS1 interacts with the Flag-tagged Smo C-terminal tail |
| GO:0005515 protein binding | IPI PMID:16327777 Dissection of epistasis in oligogenic Bardet-Biedl syndrome. | KEEP AS NON CORE | Summary: BBS1 association with CCDC28B is retained as non-core interaction context. Reason: The CCDC28B association provides oligogenic disease-modifier context. An autonomous BBS1 biochemical activity is not established by this interaction. |
| GO:0034464 BBSome | IDA PMID:20080638 BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family c... | ACCEPT | Summary: BBS1 is an established component of the BBSome trafficking complex. Reason: Retain this source-specific complex-membership assertion. Biochemical identification and assembly studies converge on BBS1 membership; this does not assign every other subunit's autonomous activity to BBS1. The current evidence code and original reference remain unchanged. |
| GO:0043001 Golgi to plasma membrane protein transport | IMP PMID:19150989 Requirement of Bardet-Biedl syndrome proteins for leptin rec... | KEEP AS NON CORE | Summary: BBS proteins influence leptin-receptor trafficking and signaling. Reason: Retain the existing IMP transport assertion as receptor-specific physiological context. The source reports BBS1 receptor association and altered trafficking, while the mouse whole-animal signaling experiments use Bbs2/Bbs4/Bbs6 knockouts; do not relabel them Bbs1-null experiments. |
| GO:0034464 BBSome | IDA PMID:17574030 A core complex of BBS proteins cooperates with the GTPase Ra... | ACCEPT | Summary: BBS1 is an established component of the BBSome trafficking complex. Reason: Retain this source-specific complex-membership assertion. Biochemical identification and assembly studies converge on BBS1 membership; this does not assign every other subunit's autonomous activity to BBS1. The current evidence code and original reference remain unchanged. Supporting Evidence: PMID:17574030 Here we identify a complex composed of seven highly conserved BBS proteins. |
| GO:0060271 cilium assembly | IMP PMID:17574030 A core complex of BBS proteins cooperates with the GTPase Ra... | ACCEPT | Summary: BBS1 contributes to cilium assembly in the experimentally annotated contexts. Reason: Retain the established ciliogenesis annotation without asserting an absolute requirement in every cell type: ciliary cargo defects can occur with preserved cilium length. BBSome-dependent membrane biogenesis supports the process; the existing source/evidence remains distinct from other subunits' specific tubulin effects. |
| GO:0045494 photoreceptor cell maintenance | IMP PMID:17980398 Retinal morphology in patients with BBS1 and BBS10 related B... | KEEP AS NON CORE | Summary: Human BBS1 patients exhibit disrupted photoreceptor integrity. Reason: The study examined four BBS1 and four BBS10 patients by retinal OCT. Preserve the maintenance annotation as tissue context without presenting it as a mouse experiment or a direct biochemical maintenance assay. |
| GO:1905515 non-motile cilium assembly | IMP PMID:17980398 Retinal morphology in patients with BBS1 and BBS10 related B... | ACCEPT | Summary: BBS1 contributes to cilium assembly in the experimentally annotated contexts. Reason: Retain the established ciliogenesis annotation without asserting an absolute requirement in every cell type: ciliary cargo defects can occur with preserved cilium length. This human BBS1/BBS10 patient OCT study reports disrupted photoreceptor architecture and poorly identifiable connecting cilia; the available cache lacks Methods and does not directly resolve an assembly step. Retention defers to the existing IMP interpretation and the broader experimental ciliogenesis literature, not a new mechanistic claim from imaging. |
| GO:0005515 protein binding | IPI PMID:17574030 A core complex of BBS proteins cooperates with the GTPase Ra... | KEEP AS NON CORE | Summary: BBS1 association with BBS9 is retained as non-core interaction context. Reason: The association is consistent with the original BBSome complex and recruitment study. It supports an interaction context without establishing an additional autonomous BBS1 activity. |
| GO:0005515 protein binding | IPI PMID:17574030 A core complex of BBS proteins cooperates with the GTPase Ra... | KEEP AS NON CORE | Summary: BBS1 association with BBS7 is retained as non-core interaction context. Reason: The association is consistent with the original BBSome complex and recruitment study. It supports an interaction context without establishing an additional autonomous BBS1 activity. |
| GO:0005515 protein binding | IPI PMID:17574030 A core complex of BBS proteins cooperates with the GTPase Ra... | KEEP AS NON CORE | Summary: BBS1 association with RAB3IP isoform 1 is retained as non-core interaction context. Reason: The association is consistent with the original BBSome complex and recruitment study. It supports an interaction context without establishing an additional autonomous BBS1 activity. RAB3IP is a nucleotide-exchange factor, not a small GTPase; the partner isoform does not identify a BBS1 isoform. |
| GO:0005515 protein binding | IPI PMID:17574030 A core complex of BBS proteins cooperates with the GTPase Ra... | KEEP AS NON CORE | Summary: BBS1 association with RAB3IP isoform 2 is retained as non-core interaction context. Reason: The association is consistent with the original BBSome complex and recruitment study. It supports an interaction context without establishing an additional autonomous BBS1 activity. RAB3IP is a nucleotide-exchange factor, not a small GTPase; the partner isoform does not identify a BBS1 isoform. |
| GO:0005515 protein binding | IPI PMID:17574030 A core complex of BBS proteins cooperates with the GTPase Ra... | KEEP AS NON CORE | Summary: BBS1 association with BBS4 is retained as non-core interaction context. Reason: The association is consistent with the original BBSome complex and recruitment study. It supports an interaction context without establishing an additional autonomous BBS1 activity. |
| GO:0005515 protein binding | IPI PMID:17574030 A core complex of BBS proteins cooperates with the GTPase Ra... | KEEP AS NON CORE | Summary: BBS1 association with BBS2 is retained as non-core interaction context. Reason: The association is consistent with the original BBSome complex and recruitment study. It supports an interaction context without establishing an additional autonomous BBS1 activity. |
| GO:0005515 protein binding | IPI PMID:18000879 Novel interaction partners of Bardet-Biedl syndrome proteins... | KEEP AS NON CORE | Summary: BBS1 association with EEF1A1 is retained as non-core interaction context. Reason: The interaction screen supports this curator-attributed association. The association alone does not establish a distinct BBS1 molecular activity; pair-specific follow-up assays are not assumed. |
| GO:0005515 protein binding | IPI PMID:18000879 Novel interaction partners of Bardet-Biedl syndrome proteins... | KEEP AS NON CORE | Summary: BBS1 association with PCM1 is retained as non-core interaction context. Reason: The interaction screen supports this curator-attributed association. The association alone does not establish a distinct BBS1 molecular activity; pair-specific follow-up assays are not assumed. |
| GO:0005515 protein binding | IPI PMID:18000879 Novel interaction partners of Bardet-Biedl syndrome proteins... | KEEP AS NON CORE | Summary: BBS1 association with PARK7 is retained as non-core interaction context. Reason: The interaction screen supports this curator-attributed association. The association alone does not establish a distinct BBS1 molecular activity; pair-specific follow-up assays are not assumed. |
| GO:0005515 protein binding | IPI PMID:20080638 BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family c... | KEEP AS NON CORE | Summary: BBS1 association with BBS7 is retained as non-core interaction context. Reason: The association is consistent with chaperonin-assisted BBSome assembly. It does not establish intrinsic BBS1 chaperonin or protein-folding activity. |
| GO:0005515 protein binding | IPI PMID:22500027 Intrinsic protein-protein interaction-mediated and chaperoni... | KEEP AS NON CORE | Summary: BBS1 association with BBS7 is retained as non-core interaction context. Reason: The association supports sequential BBSome assembly and intermediate stability. Co-immunoprecipitation does not by itself establish a purified binary interface or an additional BBS1 activity. |
| GO:0005515 protein binding | IPI PMID:22500027 Intrinsic protein-protein interaction-mediated and chaperoni... | KEEP AS NON CORE | Summary: BBS1 association with BBS4 is retained as non-core interaction context. Reason: The association supports sequential BBSome assembly and intermediate stability. Co-immunoprecipitation does not by itself establish a purified binary interface or an additional BBS1 activity. |
| GO:0005515 protein binding | IPI PMID:22500027 Intrinsic protein-protein interaction-mediated and chaperoni... | KEEP AS NON CORE | Summary: BBS1 association with BBS2 is retained as non-core interaction context. Reason: The association supports sequential BBSome assembly and intermediate stability. Co-immunoprecipitation does not by itself establish a purified binary interface or an additional BBS1 activity. |
| GO:0005515 protein binding | IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis... | KEEP AS NON CORE | Summary: BBS1 association with BBS7 is retained as non-core interaction context. Reason: The ciliary affinity-proteomics association supports a complex interaction context. It is not evidence for an additional autonomous BBS1 activity or purified direct binding. |
| GO:0005515 protein binding | IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis... | KEEP AS NON CORE | Summary: BBS1 association with BBS4 is retained as non-core interaction context. Reason: The ciliary affinity-proteomics association supports a complex interaction context. It is not evidence for an additional autonomous BBS1 activity or purified direct binding. |
| GO:0005515 protein binding | IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis... | KEEP AS NON CORE | Summary: BBS1 association with BBS2 is retained as non-core interaction context. Reason: The ciliary affinity-proteomics association supports a complex interaction context. It is not evidence for an additional autonomous BBS1 activity or purified direct binding. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | KEEP AS NON CORE | Summary: BBS1 association with PARK7 is retained as non-core interaction context. Reason: The source-attributed interaction is retained as non-core context. The neurodegeneration-focused interaction network does not assign BBS1 an aggregation mechanism from this association alone. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: BBS1 association with BBS7 is retained as non-core interaction context. Reason: The affinity-purification association supports BBSome complex context. It does not establish a separate BBS1 molecular activity, direct contact, or validation in both sampled cell lines. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: BBS1 association with BBS4 is retained as non-core interaction context. Reason: The affinity-purification association supports BBSome complex context. It does not establish a separate BBS1 molecular activity, direct contact, or validation in both sampled cell lines. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: BBS1 association with BBS2 is retained as non-core interaction context. Reason: The affinity-purification association supports BBSome complex context. It does not establish a separate BBS1 molecular activity, direct contact, or validation in both sampled cell lines. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | KEEP AS NON CORE | Summary: BBS1 association with BBS7 is retained as non-core interaction context. Reason: The U2OS interaction map supports BBSome complex context. It does not establish a separate BBS1 molecular activity or a direct binding interface. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | KEEP AS NON CORE | Summary: BBS1 association with BBS4 is retained as non-core interaction context. Reason: The U2OS interaction map supports BBSome complex context. It does not establish a separate BBS1 molecular activity or a direct binding interface. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | KEEP AS NON CORE | Summary: BBS1 association with BBS2 is retained as non-core interaction context. Reason: The U2OS interaction map supports BBSome complex context. It does not establish a separate BBS1 molecular activity or a direct binding interface. |
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Download this section (compressed HTML)Q: Which receptor-tail contacts with BBS1 are direct in a purified human BBSome, and how does cargo binding alter its interaction with ARL6?
Q: How do BBS1-dependent cargo transport and cilium maintenance contribute separately to motile-cilium phenotypes across mammalian tissues?
Experiment: Test structure-guided variants in purified human BBSome receptor-tail binding and ARL6-binding assays, followed by matched cellular measurements of receptor trafficking, cilium abundance and length. Compare these readouts rather than inferring universal ciliogenesis failure from altered cargo distribution.
Hypothesis: Receptor-tail recognition and ARL6-dependent membrane recruitment can be separated by BBS1 mutations.
Type: binding biochemistry and ciliary cargo transport
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