BBS7 is a subunit of the BBSome, an eight-protein complex involved in membrane-protein trafficking at cilia. It forms a coiled-coil heterodimer with BBS2 within the BBSome assembly intermediate. BBS7 and BBS2 also support one another's protein stability. BBS7 occurs in cytoplasmic, centrosomal and ciliary compartments, and its loss disrupts BBSome organization and selected ciliary membrane-protein distributions. Biallelic pathogenic variants cause Bardet-Biedl syndrome, which can include retinal degeneration, obesity, polydactyly and reproductive abnormalities.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0008104 intracellular protein localization | IBA GO_REF:0000033 | MODIFY | Summary: BBS7 participates in ciliary protein localization through the BBSome. Reason: Ciliary protein localization is a supported specific instance of the broad inherited process. Human BBS7 depletion disrupts BBSome ciliary entry; Bbs7-null mice show selective receptor-localization defects. The specific term includes maintaining a protein within a cilium and does not assert that BBS7 autonomously recognizes every cargo. Proposed replacements: protein localization to cilium Supporting Evidence: PMID:23572516 BBS7 is involved in specific membrane protein localization to cilia. |
| GO:0016020 membrane | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: BBS7 is associated with membranes through the BBSome. Reason: Retain the broad inherited membrane localization, consistent with the complex at the ciliary membrane. A peripheral complex subunit need not be transmembrane or bind a lipid directly to have this location. |
| GO:0034464 BBSome | IBA GO_REF:0000033 | ACCEPT | Summary: BBS7 is a constituent of the BBSome. Reason: Complex membership is a central feature of BBS7 and agrees with founding purification, subsequent assembly studies and Bbs7-null mouse experiments. Its membership is distinct from the separate BBS6/BBS10/BBS12 chaperonin-assisted assembly machinery. |
| GO:0036064 ciliary basal body | IBA GO_REF:0000033 | ACCEPT | Summary: BBS7 localizes at the ciliary basal body. Reason: Retain the inherited basal-body localization. The UniProt record explicitly transfers basal-body localization from mouse Bbs7; the localization does not imply that BBS7 is an exclusive structural constituent of the basal body. |
| GO:0043005 neuron projection | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: BBS7 has a supported localization in specialized neuronal projections. Reason: Retain the phylogenetically inferred projection localization as non-core context for a ciliary trafficking protein. Bbs7-null mouse neuronal cilia show altered receptor composition; this does not make BBS7 a general neuronal structural protein. |
| GO:0060271 cilium assembly | IBA GO_REF:0000033 | ACCEPT | Summary: BBS7 contributes to cilium assembly and maintenance in the tested biological contexts. Reason: Retain the source process. Zebrafish bbs7 perturbation affects Kupffer-vesicle cilia, and Bbs7-null mice have abnormal sperm flagellar axonemes. These findings support a ciliary role without a claim that BBS7 is required to initiate every primary cilium; receptor-trafficking and BBSome-assembly defects can coexist with persistent cilia. |
| GO:0005930 axoneme | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: BBS7 has an inherited axonemal localization. Reason: Keep the location. Association with the axonemal compartment does not require BBS7 to be an integral microtubule structural protein, and its trafficking function is compatible with this localization. |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: BBS7 has a cytoplasmic pool. Reason: The broad localization is compatible with BBSome assembly and trafficking between cytoplasmic and ciliary compartments. It neither excludes membrane association nor asserts an exclusively cytoplasmic protein. |
| GO:0034451 centriolar satellite | IEA GO_REF:0000044 | ACCEPT | Summary: BBS7 associates with centriolar satellites. Reason: Retain the mapped satellite localization, which agrees with BBSome localization in the founding study. This does not transfer the PCM1–dynactin adaptor mechanism of BBS4 to BBS7. |
| GO:0034464 BBSome | IEA GO_REF:0000002 | ACCEPT | Summary: BBS7 is a constituent of the BBSome. Reason: Complex membership is a central feature of BBS7 and agrees with founding purification, subsequent assembly studies and Bbs7-null mouse experiments. Its membership is distinct from the separate BBS6/BBS10/BBS12 chaperonin-assisted assembly machinery. |
| GO:0060170 ciliary membrane | IEA GO_REF:0000044 | ACCEPT | Summary: BBS7 associates with the ciliary membrane as a BBSome subunit. Reason: The location is central to the trafficking complex. It does not mean that BBS7 is an integral membrane protein or is sufficient on its own to recruit the complex to a membrane. |
| GO:1905515 non-motile cilium assembly | IEA GO_REF:0000002 | ACCEPT | Summary: BBS7 has a supported conserved role in non-motile ciliary assembly and maintenance. Reason: Retain the family-based electronic process. Independent C. elegans bbs-7 mutations produce structural defects in sensory cilia and compromise the localization and motility of selected IFT proteins. This supplies non-motile sensory-cilium context beyond zebrafish motile Kupffer-vesicle or mouse sperm phenotypes; it is not a claim that human BBS7 is universally required to initiate all primary cilia. |
| GO:0005515 protein binding | IPI PMID:17574030 A core complex of BBS proteins cooperates with the GTPase Ra... | KEEP AS NON CORE | Summary: BBS7 has a source-attributed association with BBS1. Reason: Retain the source-attributed association with BBS1 (Q8NFJ9) as supported non-core context from the founding BBSome study. BBSome co-association alone does not establish a distinct binary heterodimer or a partner-specific catalytic/adaptor activity for this pair. |
| GO:0005515 protein binding | IPI PMID:18000879 Novel interaction partners of Bardet-Biedl syndrome proteins... | KEEP AS NON CORE | Summary: BBS7 has a source-attributed association with ALDOB. Reason: Retain the source-attributed association with ALDOB (P05062) as supported non-core context from the targeted BBS interaction study. A better-supported specific molecular-function replacement for this exact interaction has not been established. |
| GO:0005515 protein binding | IPI PMID:20080638 BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family c... | KEEP AS NON CORE | Summary: BBS7 has a source-attributed association with CCT2. Reason: Retain the source-attributed association with CCT2 (P78371) as supported non-core context from the BBS-chaperonin assembly study. Binding to assembly chaperonin machinery does not establish that BBS7 folds another protein; BBS7 is stabilized during its own assembly. |
| GO:0005515 protein binding | IPI PMID:20195357 A comprehensive resource of interacting protein regions for ... | KEEP AS NON CORE | Summary: BBS7 has a source-attributed association with JUN. Reason: Retain the source-attributed association with JUN (P05412) as supported non-core context from a transcription-factor interaction resource. The interaction resource does not establish that the exact assayed fragment mediates a physiological BBS7 transcription-factor regulatory mechanism. |
| GO:0005515 protein binding | IPI PMID:22500027 Intrinsic protein-protein interaction-mediated and chaperoni... | KEEP AS NON CORE | Summary: BBS7 has a source-attributed association with CCT2. Reason: Retain the source-attributed association with CCT2 (P78371) as supported non-core context from the ordered BBSome assembly study. Binding to assembly chaperonin machinery does not establish that BBS7 folds another protein; BBS7 is stabilized during its own assembly. |
| GO:0005515 protein binding | IPI PMID:25552655 Nephrocystin proteins NPHP5 and Cep290 regulate BBSome integ... | KEEP AS NON CORE | Summary: BBS7 has a source-attributed association with IQCB1/NPHP5. Reason: Retain the source-attributed association with IQCB1/NPHP5 (Q15051) as supported non-core context from the NPHP5/CEP290 BBSome-integrity study. A better-supported specific molecular-function replacement for this exact interaction has not been established. |
| GO:0005515 protein binding | IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis... | KEEP AS NON CORE | Summary: BBS7 has a source-attributed association with BBS1. Reason: Retain the source-attributed association with BBS1 (Q8NFJ9) as supported non-core context from a ciliary protein interaction landscape. BBSome co-association alone does not establish a distinct binary heterodimer or a partner-specific catalytic/adaptor activity for this pair. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | KEEP AS NON CORE | Summary: BBS7 has a source-attributed association with BBS12. Reason: Retain the source-attributed association with BBS12 (Q6ZW61) as supported non-core context from the BioPlex interaction map. Binding to assembly chaperonin machinery does not establish that BBS7 folds another protein; BBS7 is stabilized during its own assembly. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: BBS7 has a source-attributed association with BBS12. Reason: Retain the source-attributed association with BBS12 (Q6ZW61) as supported non-core context from the comparative human interactome study. Binding to assembly chaperonin machinery does not establish that BBS7 folds another protein; BBS7 is stabilized during its own assembly. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | KEEP AS NON CORE | Summary: BBS7 has a source-attributed association with BBS1. Reason: Retain the source-attributed association with BBS1 (Q8NFJ9) as supported non-core context from the multimodal human cell-map study. BBSome co-association alone does not establish a distinct binary heterodimer or a partner-specific catalytic/adaptor activity for this pair. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5617815 | KEEP AS NON CORE | Summary: BBS7 participates in a cytosolic BBSome pool in the curated pathway. Reason: Retain the location recorded for the BBSome-containing event. Complex membership in this cytosolic event does not assign the event’s ARL6 nucleotide activity, RAB3IP exchange activity or cargo recognition to isolated BBS7. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5624125 | KEEP AS NON CORE | Summary: BBS7 participates in a cytosolic BBSome pool in the curated pathway. Reason: Retain the location recorded for the BBSome-containing event. Complex membership in this cytosolic event does not assign the event’s ARL6 nucleotide activity, RAB3IP exchange activity or cargo recognition to isolated BBS7. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5624126 | KEEP AS NON CORE | Summary: BBS7 participates in a cytosolic BBSome pool in the curated pathway. Reason: Retain the location recorded for the BBSome-containing event. Complex membership in this cytosolic event does not assign the event’s ARL6 nucleotide activity, RAB3IP exchange activity or cargo recognition to isolated BBS7. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5624127 | KEEP AS NON CORE | Summary: BBS7 participates in a cytosolic BBSome pool in the curated pathway. Reason: Retain the location recorded for the BBSome-containing event. Complex membership in this cytosolic event does not assign the event’s ARL6 nucleotide activity, RAB3IP exchange activity or cargo recognition to isolated BBS7. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5624129 | KEEP AS NON CORE | Summary: BBS7 participates in a cytosolic BBSome pool in the curated pathway. Reason: Retain the location recorded for the BBSome-containing event. Complex membership in this cytosolic event does not assign the event’s ARL6 nucleotide activity, RAB3IP exchange activity or cargo recognition to isolated BBS7. |
| GO:0005737 cytoplasm | EXP PMID:22072986 A novel protein LZTFL1 regulates ciliary trafficking of the ... | KEEP AS NON CORE | Summary: BBS7 has a cytoplasmic pool. Reason: The broad localization is compatible with BBSome assembly and trafficking between cytoplasmic and ciliary compartments. It neither excludes membrane association nor asserts an exclusively cytoplasmic protein. |
| GO:0034464 BBSome | IPI PMID:19081074 A BBSome subunit links ciliogenesis, microtubule stability, ... | ACCEPT | Summary: BBS7 is a constituent of the BBSome. Reason: Complex membership is a central feature of BBS7 and agrees with founding purification, subsequent assembly studies and Bbs7-null mouse experiments. Its membership is distinct from the separate BBS6/BBS10/BBS12 chaperonin-assisted assembly machinery. |
| GO:0060170 ciliary membrane | IDA PMID:19081074 A BBSome subunit links ciliogenesis, microtubule stability, ... | ACCEPT | Summary: BBS7 associates with the ciliary membrane as a BBSome subunit. Reason: The location is central to the trafficking complex. It does not mean that BBS7 is an integral membrane protein or is sufficient on its own to recruit the complex to a membrane. |
| GO:0060271 cilium assembly | NAS PMID:19081074 A BBSome subunit links ciliogenesis, microtubule stability, ... | ACCEPT | Summary: BBS7 contributes to cilium assembly and maintenance in the tested biological contexts. Reason: Retain the source process. Zebrafish bbs7 perturbation affects Kupffer-vesicle cilia, and Bbs7-null mice have abnormal sperm flagellar axonemes. These findings support a ciliary role without a claim that BBS7 is required to initiate every primary cilium; receptor-trafficking and BBSome-assembly defects can coexist with persistent cilia. |
| GO:0060271 cilium assembly | ISS GO_REF:0000024 | ACCEPT | Summary: BBS7 contributes to cilium assembly and maintenance in the tested biological contexts. Reason: Retain the source process. Zebrafish bbs7 perturbation affects Kupffer-vesicle cilia, and Bbs7-null mice have abnormal sperm flagellar axonemes. These findings support a ciliary role without a claim that BBS7 is required to initiate every primary cilium; receptor-trafficking and BBSome-assembly defects can coexist with persistent cilia. |
| GO:0005515 protein binding | IPI PMID:18762586 Recruitment of PCM1 to the centrosome by the cooperative act... | KEEP AS NON CORE | Summary: BBS7 has a source-attributed association with DISC1. Reason: Retain the source-attributed association with DISC1 (Q9NRI5) as supported non-core context from the DISC1/centrosomal interaction study. The exact partner is DISC1, not PCM1; the paper’s PCM1-recruitment mechanism concerns DISC1 and BBS4 and is not transferred to BBS7. |
| GO:0005515 protein binding | IPI PMID:24550735 The centriolar satellite protein AZI1 interacts with BBS4 an... | KEEP AS NON CORE | Summary: BBS7 has a source-attributed association with AZI1/CEP131. Reason: Retain the source-attributed association with AZI1/CEP131 (Q9UPN4) as supported non-core context from the AZI1/BBSome study. Co-complex association with AZI1 is compatible with its reported BBS4-mediated interaction and does not show that BBS7 is the autonomous AZI1 receptor. |
| GO:0034464 BBSome | IDA PMID:24550735 The centriolar satellite protein AZI1 interacts with BBS4 an... | ACCEPT | Summary: BBS7 is a constituent of the BBSome. Reason: Complex membership is a central feature of BBS7 and agrees with founding purification, subsequent assembly studies and Bbs7-null mouse experiments. Its membership is distinct from the separate BBS6/BBS10/BBS12 chaperonin-assisted assembly machinery. |
| GO:0006357 regulation of transcription by RNA polymerase II | IPI PMID:22302990 Direct role of Bardet-Biedl syndrome proteins in transcripti... | KEEP AS NON CORE | Summary: BBS7 influences transcription in an RNF2-associated cellular context. Reason: Human-cell BBS7 depletion changes RNF2 abundance and target-gene expression; zebrafish double-knockdown supports RNF2-dependent context. Retain the existing regulatory process as secondary to BBSome trafficking. This does not establish BBS7 sequence-specific DNA binding or direct promoter occupancy. |
| GO:0032436 positive regulation of proteasomal ubiquitin-dependent protein catabolic process | IPI PMID:22302990 Direct role of Bardet-Biedl syndrome proteins in transcripti... | KEEP AS NON CORE | Summary: BBS7 supports proteasomal protein clearance in the tested cellular context. Reason: BBS7 depletion increases the HEK293 proteasome-sensor signal and RNF2 protein despite reduced RNF2 RNA. These results support a positive influence on proteasomal clearance. RNF2-specific degradation remains the authors’ interpretation, rather than a measured isolated degradation reaction; do not describe BBS7 as a protease or ubiquitin ligase. |
| 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: BBS7 binds the ubiquitin ligase RNF2. Reason: The exact partner Q99496 is RNF2/RING1B, a PRC1 E3 ligase. Human BBS7 bait–prey testing, tagged HEK293 co-IP and endogenous HeLa co-IP support the interaction. RNF2’s transcriptional role does not establish the sequence-specific DNA-binding factor class required by GO:0061629. Proposed replacements: ubiquitin protein ligase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16327777 Dissection of epistasis in oligogenic Bardet-Biedl syndrome. | KEEP AS NON CORE | Summary: BBS7 has a source-attributed association with CCDC28B. Reason: Retain the source-attributed association with CCDC28B (Q9BUN5) as supported non-core context from the BBS genetic-modifier study. A better-supported specific molecular-function replacement for this exact interaction has not been established. |
| GO:0034464 BBSome | IDA PMID:20080638 BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family c... | ACCEPT | Summary: BBS7 is a constituent of the BBSome. Reason: Complex membership is a central feature of BBS7 and agrees with founding purification, subsequent assembly studies and Bbs7-null mouse experiments. Its membership is distinct from the separate BBS6/BBS10/BBS12 chaperonin-assisted assembly machinery. |
| GO:0005813 centrosome | IDA PMID:21399614 Novel asymmetrically localizing components of human centroso... | ACCEPT | Summary: BBS7 is localized to the centrosome. Reason: Keep the human experimental cellular-component annotation. The study used complementary centrosome proteomics and localization assays; its title does not establish that every identified protein, including BBS7, has a particular mother-versus-daughter asymmetry. |
| GO:0001947 heart looping | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: BBS7 has a transferred developmental association with heart looping. Reason: The source ortholog Q08C18 is zebrafish Bbs7. Its knockdown affects Kupffer-vesicle cilia and organ laterality, providing positive developmental support. Retain this as organismal context rather than a direct heart-patterning molecular activity of human BBS7. |
| GO:0007368 determination of left/right symmetry | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: BBS7 has a transferred developmental association with left/right symmetry specification. Reason: The source ortholog Q08C18 is zebrafish Bbs7. Its knockdown affects Kupffer-vesicle cilia and organ laterality, providing positive developmental support. Retain this as organismal context rather than a direct heart-patterning molecular activity of human BBS7. |
| GO:0032402 melanosome transport | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: BBS7 has a transferred role in melanosome transport. Reason: Zebrafish bbs7 knockdown delays retrograde melanosome transport. Retain the positive ortholog phenotype as a non-core transport context. BBS7 is not thereby established as a motor or as a general controller of both retrograde and anterograde transport. Supporting Evidence: PMID:24938409 bbs7 knockdown leads to a statistically significant delay |
| GO:0045444 fat cell differentiation | ISS GO_REF:0000024 | UNDECIDED | Summary: The fat-cell differentiation transfer remains unresolved. Reason: The stated source Q8K2G4 is mouse Bbs7. The official donor table traces this process to IEP evidence in PMID:17379567, whose available abstract reports expression changes during differentiation of mouse 3T3-F442A cells. That does not establish a Bbs7 perturbation effect; the complete primary body and a stronger donor assay have not been inspected. Preserve the source assertion pending resolution. |
| GO:0048546 digestive tract morphogenesis | ISS GO_REF:0000024 | UNDECIDED | Summary: The digestive-tract morphogenesis transfer is not yet resolved. Reason: The source is zebrafish Bbs7, but the available primary laterality and Kupffer-vesicle observations do not identify the specific digestive-tract morphogenesis assay behind this transfer. GO:0048546 concerns formation and organization of digestive-tract anatomy. Preserve the assertion while its experimental donor context remains unresolved. |
| GO:0051877 pigment granule aggregation in cell center | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: BBS7 has a transferred role in pigment granule aggregation toward the cell center. Reason: Zebrafish bbs7 knockdown delays retrograde melanosome transport. Retain the positive ortholog phenotype as a non-core transport context. BBS7 is not thereby established as a motor or as a general controller of both retrograde and anterograde transport. |
| GO:0034464 BBSome | IDA PMID:17574030 A core complex of BBS proteins cooperates with the GTPase Ra... | ACCEPT | Summary: BBS7 is a constituent of the BBSome. Reason: Complex membership is a central feature of BBS7 and agrees with founding purification, subsequent assembly studies and Bbs7-null mouse experiments. Its membership is distinct from the separate BBS6/BBS10/BBS12 chaperonin-assisted assembly machinery. |
| GO:0005515 protein binding | IPI PMID:17574030 A core complex of BBS proteins cooperates with the GTPase Ra... | KEEP AS NON CORE | Summary: BBS7 has a curated association with BBS2. Reason: The founding BBSome study establishes complex membership and the ciliary context. The locally cached abstract does not resolve a purified binary BBS2-BBS7 assay. Retain the supported interaction. The direct pairwise evidence in PMID:22500027 and human structural evidence in PMID:31530639 ground the heterodimer mechanism separately; that mechanism is not attributed to this source assay. |
| GO:0005515 protein binding | IPI PMID:20080638 BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family c... | KEEP AS NON CORE | Summary: BBS7 has a source-attributed association with BBS12. Reason: Retain the source-attributed association with BBS12 (Q6ZW61) as supported non-core context from the BBS-chaperonin assembly study. Binding to assembly chaperonin machinery does not establish that BBS7 folds another protein; BBS7 is stabilized during its own assembly. |
| GO:0005515 protein binding | IPI PMID:20080638 BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family c... | KEEP AS NON CORE | Summary: BBS7 has a source-attributed association with BBS1. Reason: Retain the source-attributed association with BBS1 (Q8NFJ9) as supported non-core context from the BBS-chaperonin assembly study. BBSome co-association alone does not establish a distinct binary heterodimer or a partner-specific catalytic/adaptor activity for this pair. |
| GO:0005515 protein binding | IPI PMID:20080638 BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family c... | KEEP AS NON CORE | Summary: BBS7 has a source-attributed association with BBS10. Reason: Retain the source-attributed association with BBS10 (Q8TAM1) as supported non-core context from the BBS-chaperonin assembly study. Binding to assembly chaperonin machinery does not establish that BBS7 folds another protein; BBS7 is stabilized during its own assembly. |
| GO:0005515 protein binding | IPI PMID:20080638 BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family c... | KEEP AS NON CORE | Summary: BBS7 has a curated association with BBS2. Reason: The chaperonin-assisted assembly study places BBS7 in the assembly pathway. The locally cached abstract does not by itself establish the geometry or stoichiometry of the BBS2-BBS7 interface. Retain the supported interaction. The direct pairwise evidence in PMID:22500027 and human structural evidence in PMID:31530639 ground the heterodimer mechanism separately; that mechanism is not attributed to this source assay. |
| GO:0005515 protein binding | IPI PMID:22500027 Intrinsic protein-protein interaction-mediated and chaperoni... | KEEP AS NON CORE | Summary: BBS7 has a source-attributed association with BBS12. Reason: Retain the source-attributed association with BBS12 (Q6ZW61) as supported non-core context from the ordered BBSome assembly study. Binding to assembly chaperonin machinery does not establish that BBS7 folds another protein; BBS7 is stabilized during its own assembly. |
| GO:0005515 protein binding | IPI PMID:22500027 Intrinsic protein-protein interaction-mediated and chaperoni... | KEEP AS NON CORE | Summary: BBS7 has a source-attributed association with BBS1. Reason: Retain the source-attributed association with BBS1 (Q8NFJ9) as supported non-core context from the ordered BBSome assembly study. BBSome co-association alone does not establish a distinct binary heterodimer or a partner-specific catalytic/adaptor activity for this pair. |
| GO:0005515 protein binding | IPI PMID:22500027 Intrinsic protein-protein interaction-mediated and chaperoni... | MODIFY | Summary: BBS7 forms a heterodimeric interface with BBS2. Reason: The original Results explicitly report pairwise BBS2-BBS7 interaction, distinguished from the indirect BBS7-BBS9 association that requires BBS2 (supplemental Fig.S2B is described in the Results but its image was not independently inspected). Thus this source supports the binary interaction itself. Human recombinant structural analysis in PMID:31530639 establishes the coiled-coil heterodimer geometry. Refine this directly supported pair to heterodimerization; other co-complex screens retain their own association claims. Proposed replacements: protein heterodimerization activity |
| GO:0005515 protein binding | IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis... | KEEP AS NON CORE | Summary: BBS7 has a curated association with BBS2. Reason: The ciliary interaction landscape supports an association in its interaction map. Co-purification does not distinguish a direct binary interface from association through other BBSome subunits. Retain the supported interaction. The direct pairwise evidence in PMID:22500027 and human structural evidence in PMID:31530639 ground the heterodimer mechanism separately; that mechanism is not attributed to this source assay. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | KEEP AS NON CORE | Summary: BBS7 has a source-attributed association with BBS10. Reason: Retain the source-attributed association with BBS10 (Q8TAM1) as supported non-core context from the BioPlex interaction map. Binding to assembly chaperonin machinery does not establish that BBS7 folds another protein; BBS7 is stabilized during its own assembly. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | KEEP AS NON CORE | Summary: BBS7 has a curated association with BBS2. Reason: The BioPlex interaction map supports co-complex association. It does not independently establish a two-subunit dimer. Retain the supported interaction. The direct pairwise evidence in PMID:22500027 and human structural evidence in PMID:31530639 ground the heterodimer mechanism separately; that mechanism is not attributed to this source assay. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: BBS7 has a source-attributed association with BBS1. Reason: Retain the source-attributed association with BBS1 (Q8NFJ9) as supported non-core context from the comparative human interactome study. BBSome co-association alone does not establish a distinct binary heterodimer or a partner-specific catalytic/adaptor activity for this pair. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: BBS7 has a source-attributed association with BBS10. Reason: Retain the source-attributed association with BBS10 (Q8TAM1) as supported non-core context from the comparative human interactome study. Binding to assembly chaperonin machinery does not establish that BBS7 folds another protein; BBS7 is stabilized during its own assembly. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: BBS7 has a curated association with BBS2. Reason: The comparative human interactome supplies an association record. Its exact supplementary BBS2-BBS7 pair was not independently reconstructed, and the source annotation is retained without replacing it with a dimer mechanism. Retain the supported interaction. The direct pairwise evidence in PMID:22500027 and human structural evidence in PMID:31530639 ground the heterodimer mechanism separately; that mechanism is not attributed to this source assay. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | KEEP AS NON CORE | Summary: BBS7 has a curated association with BBS2. Reason: The multimodal human cell map supplies an association record. Its exact supplementary pair and construct were not independently reconstructed; the specific dimer geometry comes from a separate structural study. Retain the supported interaction. The direct pairwise evidence in PMID:22500027 and human structural evidence in PMID:31530639 ground the heterodimer mechanism separately; that mechanism is not attributed to this source assay. |
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Download this section (compressed HTML)Q: Which BBS7 surfaces contribute to cargo handling independently of maintaining BBS2 abundance and BBSome organization?
Q: Why does Bbs7 loss alter neuronal ciliary dopamine D1 receptor abundance while preserving polycystin-1 and polycystin-2 localization in the tested mouse kidney cells?
Q: Which experimental donor observations support the transferred adipocyte differentiation and digestive tract morphogenesis annotations?
Experiment: Compare BBS7 interface variants at matched expression levels, measuring BBS2 abundance, heterodimer formation and incorporation into the complete BBSome separately. Use variants that preserve complex integrity to test cargo association and ciliary transport.
Hypothesis: Some BBS7 variants change cargo handling through loss of complex organization, whereas others may affect a separable interaction.
Type: controlled biochemical and cell-based structure-function analysis
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