BBS4 is a tetratricopeptide-repeat protein and a subunit of the BBSome, an eight-subunit complex involved in the localization of membrane proteins at cilia. It occurs at centriolar satellites, centrosomes and ciliary structures. BBS4 interacts with PCM1 and the dynactin subunit DCTN1/p150-glued, supporting recruitment or retention of pericentriolar proteins and the organization of centrosomal microtubules. Its cooperation with DISC1 helps position PCM1 and associated proteins such as ninein near centrosomes. Within the BBSome, BBS4 contributes to ciliary trafficking and connects the complex with satellite proteins including CEP131 and CEP290. These functions have different requirements across cargoes and cell types; BBS4 loss does not prevent every form of cilium formation or ciliary protein transport. Biallelic pathogenic variants cause a Bardet-Biedl syndrome ciliopathy with retinal, metabolic and other organ involvement.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0060271 cilium assembly | IBA GO_REF:0000033 | ACCEPT | Summary: BBS4 contributes to cilium assembly through its trafficking and BBSome roles. Reason: Retain the phylogenetic process, consistent with ciliary membrane biogenesis and tissue-specific assembly defects. Bbs4-null mice form many primary and motile cilia but fail to form sperm flagella; the annotation is not a universal claim that BBS4 initiates every axoneme. |
| GO:0036064 ciliary basal body | IBA GO_REF:0000033 | ACCEPT | Summary: BBS4 localizes to the ciliary basal body. Reason: The inherited localization agrees with target experimental annotations and primary basal-body observations. It does not require BBS4 to be an exclusive basal-body structural component. |
| GO:0061512 protein localization to cilium | IBA GO_REF:0000033 | ACCEPT | Summary: BBS4 supports localization of proteins to cilia. Reason: The BBSome and satellite-associated trafficking role supports this central inherited process. Requirements vary by cargo: the separate polycystin-1 study does not show a BBS4 requirement for polycystin-1 ciliary localization. |
| GO:0000226 microtubule cytoskeleton organization | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: BBS4 contributes to microtubule organization in more than one cellular context. Reason: Centrosomal anchoring is directly supported by PMID:15107855, while mouse olfactory neurons in PMID:15322545 show broader dendritic microtubule disorganization. Retain the broad process as non-core rather than narrowing every source to centrosomal anchoring and losing the neuronal scope. The specific centrosomal process is retained separately. |
| GO:0005634 nucleus | IEA GO_REF:0000108 | UNDECIDED | Summary: The electronically inferred nuclear localization remains unresolved. Reason: This source is a GO:0051457-to-location inference. The underlying nuclear-retention assertion is not resolved by the selected original experimental text. Later BBS4-dependent nuclear transport of XBP1/ATF6 concerns the cargoes and does not independently demonstrate BBS4 nuclear residence. Preserve the assertion as undecided rather than declaring BBS4 exclusively cytoplasmic. |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: BBS4 has a cytoplasmic pool. Reason: The broad UniProt localization is compatible with satellite-associated and BBSome pools. It does not mean BBS4 is confined to the cytoplasm or lacks more specific localizations. |
| GO:0005813 centrosome | IEA GO_REF:0000120 | ACCEPT | Summary: BBS4 localizes to the centrosome. Reason: The electronic localization agrees with separately curated target evidence and the protein’s satellite/BBSome trafficking roles. A cellular-component annotation does not require a unique molecular activity dedicated to that location. |
| GO:0005929 cilium | IEA GO_REF:0000044 | ACCEPT | Summary: BBS4 localizes to the cilium. Reason: The electronic localization agrees with separately curated target evidence and the protein’s satellite/BBSome trafficking roles. A cellular-component annotation does not require a unique molecular activity dedicated to that location. |
| GO:0007600 sensory perception | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: BBS4 supports sensory function through specialized cellular trafficking. Reason: Olfactory-cilium and retinal defects in Bbs4 models support a broad sensory-perception context. Retain this electronic process as non-core without making BBS4 a sensory receptor or a neural signal-interpretation enzyme. |
| GO:0031514 motile cilium | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: BBS4 can localize to motile cilia. Reason: The ortholog/electronic location agrees with airway-cilium evidence. Localization and maintenance roles do not imply axonemal motor activity. |
| GO:0034451 centriolar satellite | IEA GO_REF:0000120 | ACCEPT | Summary: BBS4 localizes to the centriolar satellites. Reason: The electronic localization agrees with separately curated target evidence and the protein’s satellite/BBSome trafficking roles. A cellular-component annotation does not require a unique molecular activity dedicated to that location. |
| GO:0035869 ciliary transition zone | IEA GO_REF:0000117 | ACCEPT | Summary: BBS4 localizes to the ciliary transition zone. Reason: The electronic localization agrees with separately curated target evidence and the protein’s satellite/BBSome trafficking roles. A cellular-component annotation does not require a unique molecular activity dedicated to that location. |
| GO:0060170 ciliary membrane | IEA GO_REF:0000044 | ACCEPT | Summary: BBS4 localizes to the ciliary membrane. Reason: The electronic localization agrees with separately curated target evidence and the protein’s satellite/BBSome trafficking roles. A cellular-component annotation does not require a unique molecular activity dedicated to that location. |
| GO:0061512 protein localization to cilium | IEA GO_REF:0000117 | ACCEPT | Summary: BBS4 contributes to protein localization at cilia. Reason: The electronic process agrees with BBSome-entry and CEP290-associated trafficking experiments. Retain the core process without claiming that BBS4 directly recognizes every receptor cargo. |
| GO:0097730 non-motile cilium | IEA GO_REF:0000117 | ACCEPT | Summary: BBS4 localizes to the non-motile cilia. Reason: The electronic localization agrees with separately curated target evidence and the protein’s satellite/BBSome trafficking roles. A cellular-component annotation does not require a unique molecular activity dedicated to that location. |
| GO:0005515 protein binding | IPI PMID:15107855 The Bardet-Biedl protein BBS4 targets cargo to the pericentr... | MODIFY | Summary: BBS4 binds the dynactin subunit DCTN1/p150-glued. Reason: The partner is a dynactin component. Original Y2H and co-immunoprecipitation evidence in PMID:15107855 independently grounds the more specific dynactin-binding annotation; this does not confer dynein motor activity on BBS4. Proposed replacements: dynactin binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16327777 Dissection of epistasis in oligogenic Bardet-Biedl syndrome. | KEEP AS NON CORE | Summary: BBS4 is reported to associate with CCDC28B (Q9BUN5). Reason: Retain the experimentally curated partner interaction as non-core under the explicit ClinGen project instruction. The inspected evidence does not establish a finer BBS4 molecular function for this pair. The supported association is retained without using generic binding to describe a core mechanism. |
| GO:0005515 protein binding | IPI PMID:17574030 A core complex of BBS proteins cooperates with the GTPase Ra... | KEEP AS NON CORE | Summary: BBS4 has a curated association with PCM1. Reason: Retain this source-specific PCM1 association. The combined PCM1/DCTN1 binding, localization and depletion experiments in PMID:15107855 establish the pericentriolar adaptor mechanism, which is already represented by its own source annotations and the core function. This individual interaction record is not assigned that complete mechanism. The reported association is coherent with the independent PCM1 evidence and is not rejected solely because generic binding is less informative. |
| GO:0005515 protein binding | IPI PMID:18000879 Novel interaction partners of Bardet-Biedl syndrome proteins... | KEEP AS NON CORE | Summary: BBS4 is reported to associate with ALDOB (P05062). Reason: IntAct records EBI-1805866 and EBI-1995150 link BBS4-ALDOB to the PMID:18000879 yeast two-hybrid and co-immunoprecipitation experiments, respectively. The curated pair/source/method linkage was checked; the full article and figure controls were not independently re-read. Retain the supported association as non-core under the explicit project instruction without assigning an additional BBS4 enzymatic activity. |
| GO:0005515 protein binding | IPI PMID:18772192 CEP290 interacts with the centriolar satellite component PCM... | KEEP AS NON CORE | Summary: BBS4 has a curated association with PCM1. Reason: Retain this source-specific PCM1 association. The combined PCM1/DCTN1 binding, localization and depletion experiments in PMID:15107855 establish the pericentriolar adaptor mechanism, which is already represented by its own source annotations and the core function. This individual interaction record is not assigned that complete mechanism. The reported association is coherent with the independent PCM1 evidence and is not rejected solely because generic binding is less informative. |
| GO:0005515 protein binding | IPI PMID:19081074 A BBSome subunit links ciliogenesis, microtubule stability, ... | KEEP AS NON CORE | Summary: BBS4 is reported to associate with BBIP1 (A8MTZ0). Reason: Retain the BBIP1 association in the BBSome/PCM1 recruitment context. The independent assembly study reports BBS4-dependent BBIP1–PCM1 association, but this source interaction alone is not a separate autonomous BBS4 folding or HDAC6 mechanism. BBIP1-specific microtubule phenotypes are not transferred to BBS4. |
| GO:0005515 protein binding | IPI PMID:20080638 BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family c... | KEEP AS NON CORE | Summary: BBS4 is reported to associate with BBS9 (Q3SYG4). Reason: Retain the partner-specific BBSome association. Complex membership does not by itself define a BBS4 heterodimer or an autonomous cargo-recognition activity for this exact pair. |
| GO:0005515 protein binding | IPI PMID:22500027 Intrinsic protein-protein interaction-mediated and chaperoni... | KEEP AS NON CORE | Summary: BBS4 is reported to associate with BBIP1 (A8MTZ0). Reason: Retain the BBIP1 association in the BBSome/PCM1 recruitment context. The independent assembly study reports BBS4-dependent BBIP1–PCM1 association, but this source interaction alone is not a separate autonomous BBS4 folding or HDAC6 mechanism. BBIP1-specific microtubule phenotypes are not transferred to BBS4. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: BBS4 is reported to associate with MYOG (P15173). Reason: Retain the experimentally curated partner interaction as non-core under the explicit ClinGen project instruction. The inspected evidence does not establish a finer BBS4 molecular function for this pair. The supported association is retained without using generic binding to describe a core mechanism. |
| GO:0005515 protein binding | IPI PMID:25552655 Nephrocystin proteins NPHP5 and Cep290 regulate BBSome integ... | KEEP AS NON CORE | Summary: BBS4 is reported to associate with IQCB1/NPHP5 (Q15051). Reason: Retain the experimentally curated partner interaction as non-core under the explicit ClinGen project instruction. The inspected evidence does not establish a finer BBS4 molecular function for this pair. The supported association is retained without using generic binding to describe a core mechanism. |
| GO:0005515 protein binding | IPI PMID:26871637 Widespread Expansion of Protein Interaction Capabilities by ... | KEEP AS NON CORE | Summary: BBS4 is reported to associate with REL isoform 2 (Q04864-2). Reason: Retain the experimentally curated partner interaction as non-core under the explicit ClinGen project instruction. The inspected evidence does not establish a finer BBS4 molecular function for this pair. The supported association is retained without using generic binding to describe a core mechanism. |
| GO:0005515 protein binding | IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis... | KEEP AS NON CORE | Summary: BBS4 is reported to associate with BBS9 (Q3SYG4). Reason: Retain the partner-specific BBSome association. Complex membership does not by itself define a BBS4 heterodimer or an autonomous cargo-recognition activity for this exact pair. |
| GO:0005515 protein binding | IPI PMID:29039417 Protein interaction perturbation profiling at amino-acid res... | KEEP AS NON CORE | Summary: BBS4 is reported to associate with BBIP1 (A8MTZ0). Reason: Retain the BBIP1 association in the BBSome/PCM1 recruitment context. The independent assembly study reports BBS4-dependent BBIP1–PCM1 association, but this source interaction alone is not a separate autonomous BBS4 folding or HDAC6 mechanism. BBIP1-specific microtubule phenotypes are not transferred to BBS4. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: BBS4 is reported to associate with OAS1 isoform 2 (P00973-2). Reason: Retain the experimentally curated partner interaction as non-core under the explicit ClinGen project instruction. The inspected evidence does not establish a finer BBS4 molecular function for this pair. The supported association is retained without using generic binding to describe a core mechanism. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | KEEP AS NON CORE | Summary: BBS4 is reported to associate with P4HB (P07237). Reason: Retain the experimentally curated partner interaction as non-core under the explicit ClinGen project instruction. The inspected evidence does not establish a finer BBS4 molecular function for this pair. The supported association is retained without using generic binding to describe a core mechanism. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: BBS4 is reported to associate with BBS1 (Q8NFJ9). Reason: Retain the partner-specific BBSome association. Complex membership does not by itself define a BBS4 heterodimer or an autonomous cargo-recognition activity for this exact pair. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | KEEP AS NON CORE | Summary: BBS4 is reported to associate with BBS1 (Q8NFJ9). Reason: Retain the partner-specific BBSome association. Complex membership does not by itself define a BBS4 heterodimer or an autonomous cargo-recognition activity for this exact pair. |
| GO:0001750 photoreceptor outer segment | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Bbs4 localizes to the photoreceptor outer segment in the donor evidence. Reason: Retain the mouse-derived specialized localization. It is compatible with retinal ciliary trafficking and does not require an additional compartment-specific catalytic function. |
| GO:0001917 photoreceptor inner segment | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Bbs4 localizes to the photoreceptor inner segment in the donor evidence. Reason: Retain the mouse-derived specialized localization. It is compatible with retinal ciliary trafficking and does not require an additional compartment-specific catalytic function. |
| GO:0016020 membrane | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: BBS4 can associate with membranes as part of the BBSome. Reason: The mouse-derived location is compatible with peripheral coat association. A membrane annotation does not require a transmembrane segment; retain its broader scope alongside ciliary-membrane localization. |
| GO:0032391 photoreceptor connecting cilium | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Bbs4 localizes to the photoreceptor connecting cilium in the donor evidence. Reason: Retain the mouse-derived specialized localization. It is compatible with retinal ciliary trafficking and does not require an additional compartment-specific catalytic function. |
| GO:0034464 BBSome | IEA GO_REF:0000120 | ACCEPT | Summary: BBS4 is a BBSome subunit. Reason: Retain the complex-membership annotation, supported by founding purification and subsequent assembly work. BBS4 joins relatively late, and its absence can leave much of the remaining complex assembled; membership does not mean it alone stabilizes every subunit. |
| GO:0038108 negative regulation of appetite by leptin-mediated signaling pathway | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Bbs4 supports leptin-dependent appetite control. Reason: The mouse donor has direct leptin-response evidence in PMID:19150989. Retain this physiological consequence as non-core without transferring BBS1’s direct leptin-receptor binding to BBS4 or assuming an identical human appetite assay. |
| GO:0045444 fat cell differentiation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Bbs4 perturbation affects adipocyte differentiation. Reason: The inherited mouse donor includes expression evidence, while independent PMID:24500759 explicitly silences Bbs4 in 3T3F442A preadipocytes and measures altered differentiation, adipogenic markers and lipid accumulation. This supports the existing context as non-core without claiming that BBS4 is an adipogenic transcription factor or that the molecular step is resolved. |
| GO:0060271 cilium assembly | IEA GO_REF:0000107 | ACCEPT | Summary: BBS4 contributes to context-dependent cilium assembly and maintenance. Reason: Retain the process in agreement with BBSome-dependent ciliary entry and olfactory/flagellar defects. Primary and motile cilia can form in Bbs4-null mice, so this annotation is not a universal requirement for initial axoneme formation. |
| GO:0060296 regulation of cilium beat frequency involved in ciliary motility | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Bbs4 deficiency affects ciliary beat frequency in airway models. Reason: Retain the transferred regulation process as a tissue-specific consequence. The annotation does not require BBS4 to generate force directly; altered ciliary structure or maintenance can mediate the measured beat-frequency phenotype. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5617815 | KEEP AS NON CORE | Summary: BBS4 occurs in a cytosolic BBSome pool in this Reactome event. Reason: Retain the event-specific cytosol annotation. The event includes complex assembly or recruitment participants, so it does not assign RAB3IP exchange activity, ARL6 GTPase activity or another participant’s chemistry to BBS4. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5624125 | KEEP AS NON CORE | Summary: BBS4 occurs in a cytosolic BBSome pool in this Reactome event. Reason: Retain the event-specific cytosol annotation. The event includes complex assembly or recruitment participants, so it does not assign RAB3IP exchange activity, ARL6 GTPase activity or another participant’s chemistry to BBS4. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5624126 | KEEP AS NON CORE | Summary: BBS4 occurs in a cytosolic BBSome pool in this Reactome event. Reason: Retain the event-specific cytosol annotation. The event includes complex assembly or recruitment participants, so it does not assign RAB3IP exchange activity, ARL6 GTPase activity or another participant’s chemistry to BBS4. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5624127 | KEEP AS NON CORE | Summary: BBS4 occurs in a cytosolic BBSome pool in this Reactome event. Reason: Retain the event-specific cytosol annotation. The event includes complex assembly or recruitment participants, so it does not assign RAB3IP exchange activity, ARL6 GTPase activity or another participant’s chemistry to BBS4. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5624129 | KEEP AS NON CORE | Summary: BBS4 occurs in a cytosolic BBSome pool in this Reactome event. Reason: Retain the event-specific cytosol annotation. The event includes complex assembly or recruitment participants, so it does not assign RAB3IP exchange activity, ARL6 GTPase activity or another participant’s chemistry to BBS4. |
| GO:0034464 BBSome | IPI PMID:19081074 A BBSome subunit links ciliogenesis, microtubule stability, ... | ACCEPT | Summary: BBS4 is a BBSome subunit. Reason: Retain the complex-membership annotation, supported by founding purification and subsequent assembly work. BBS4 joins relatively late, and its absence can leave much of the remaining complex assembled; membership does not mean it alone stabilizes every subunit. |
| GO:0060170 ciliary membrane | IDA PMID:19081074 A BBSome subunit links ciliogenesis, microtubule stability, ... | ACCEPT | Summary: BBS4 localizes with the BBSome at the ciliary membrane. Reason: Retain the direct experimental location. The BBIP1-focused source does not invalidate its BBS4 localization measurements or transfer BBIP1-specific enzymatic regulation to BBS4. |
| GO:0060271 cilium assembly | NAS PMID:19081074 A BBSome subunit links ciliogenesis, microtubule stability, ... | ACCEPT | Summary: BBS4 contributes to context-dependent cilium assembly and maintenance. Reason: Retain the process in agreement with BBSome-dependent ciliary entry and olfactory/flagellar defects. Primary and motile cilia can form in Bbs4-null mice, so this annotation is not a universal requirement for initial axoneme formation. |
| GO:0001947 heart looping | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Bbs4 contributes to normal heart looping in zebrafish. Reason: The source donor E7EXH4 is zebrafish Bbs4. PMID:16399798 explicitly studies bbs4 knockdown with left-right/ciliary and retrograde melanosome-transport phenotypes. Retain this non-core transferred process without claiming a direct human developmental or pigment-cell experiment. |
| GO:0032402 melanosome transport | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Bbs4 contributes to normal melanosome transport in zebrafish. Reason: The source donor E7EXH4 is zebrafish Bbs4. PMID:16399798 explicitly studies bbs4 knockdown with left-right/ciliary and retrograde melanosome-transport phenotypes. Retain this non-core transferred process without claiming a direct human developmental or pigment-cell experiment. |
| GO:0060271 cilium assembly | ISS PMID:16399798 Bardet-Biedl syndrome genes are important in retrograde intr... | ACCEPT | Summary: Zebrafish Bbs4 supports ciliary assembly in the Kupffer’s vesicle context. Reason: The original PMID:16399798 examines bbs4 depletion and ciliary phenotypes in zebrafish. Retain this existing ciliary role, with its organism and tissue scope rather than generalizing to every human cilium. |
| GO:0005515 protein binding | IPI PMID:33144677 Dlec1 is required for spermatogenesis and male fertility in ... | KEEP AS NON CORE | Summary: BBS4 is reported to associate with DLEC1 (Q9Y238). Reason: Selected primary Results directly include human BBS4 in tagged DLEC1 co-immunoprecipitation. Retain this association as non-core; co-IP is not purified binary affinity and the mouse Dlec1 knockout phenotype is not a BBS4 perturbation. |
| GO:0030674 protein-macromolecule adaptor activity | IMP PMID:15107855 The Bardet-Biedl protein BBS4 targets cargo to the pericentr... | ACCEPT | Summary: BBS4 acts as a protein-macromolecule adaptor in pericentriolar recruitment. Reason: Primary interaction and depletion experiments connect BBS4 with PCM1 and DCTN1/p150-glued. They support dynein-associated recruitment or retention of PCM1 and centrosomal microtubule anchoring, without establishing BBS4 as a motor. |
| GO:0005515 protein binding | IPI PMID:18762586 Recruitment of PCM1 to the centrosome by the cooperative act... | KEEP AS NON CORE | Summary: BBS4 is reported to associate with DISC1 (Q9NRI5). Reason: The primary abstract explicitly places DISC1, BBS4 and PCM1 in a complex that cooperates in centrosomal PCM1/ninein localization. Retain the interaction as non-core; this pair alone does not establish a distinct autonomous BBS4 transcriptional or neuronal differentiation activity. |
| GO:0005813 centrosome | IDA PMID:18762586 Recruitment of PCM1 to the centrosome by the cooperative act... | ACCEPT | Summary: BBS4 localizes to the centrosome. Reason: Retain the experimentally curated localization, consistent with BBS4’s satellite-associated recruitment and BBSome trafficking roles. A cellular-component annotation need not imply a separate dedicated molecular function. |
| GO:0005515 protein binding | IPI PMID:23943788 BBS mutations modify phenotypic expression of CEP290-related... | KEEP AS NON CORE | Summary: BBS4 is reported to associate with CEP290 (O15078). Reason: CEP290 links BBS4/BBSome association to satellite and ciliary trafficking. Retain the reported interaction as non-core without assigning CEP290 catalytic activity or an independently demonstrated binary affinity to BBS4. |
| GO:0005929 cilium | IDA PMID:23943788 BBS mutations modify phenotypic expression of CEP290-related... | ACCEPT | Summary: BBS4 localizes to the cilium. Reason: Retain the experimentally curated localization, consistent with BBS4’s satellite-associated recruitment and BBSome trafficking roles. A cellular-component annotation need not imply a separate dedicated molecular function. Supporting Evidence: PMID:23943788 through BBS4 and co-localizes with CEP290 to the transition zone (TZ) of primary cilia and centriolar satellites in ciliated cells |
| GO:0034451 centriolar satellite | IDA PMID:23943788 BBS mutations modify phenotypic expression of CEP290-related... | ACCEPT | Summary: BBS4 localizes to the centriolar satellites. Reason: Retain the experimentally curated localization, consistent with BBS4’s satellite-associated recruitment and BBSome trafficking roles. A cellular-component annotation need not imply a separate dedicated molecular function. Supporting Evidence: |
| GO:0035869 ciliary transition zone | IDA PMID:23943788 BBS mutations modify phenotypic expression of CEP290-related... | ACCEPT | Summary: BBS4 localizes to the ciliary transition zone. Reason: Retain the experimentally curated localization, consistent with BBS4’s satellite-associated recruitment and BBSome trafficking roles. A cellular-component annotation need not imply a separate dedicated molecular function. Supporting Evidence: |
| GO:0061512 protein localization to cilium | IMP PMID:23943788 BBS mutations modify phenotypic expression of CEP290-related... | ACCEPT | Summary: BBS4 supports ciliary protein localization in the CEP290-associated pathway. Reason: The BBS4–CEP290 connection and perturbation evidence support this core trafficking process. Cargo and cellular context matter, and the separate PC1 study shows that BBS4 dependence cannot be assumed for every receptor. |
| GO:0005515 protein binding | IPI PMID:24939912 Bardet-Biedl syndrome proteins 1 and 3 regulate the ciliary ... | KEEP AS NON CORE | Summary: BBS4 is reported to associate with TTC8/BBS8 (Q8TAM2). Reason: Retain the partner-specific BBSome association as non-core binding context. Co-complex membership alone does not establish an autonomous cargo-recognition activity or a particular BBS4 heterodimer function. In the PC1 study, the Q8TAM2 source partner is TTC8/BBS8, not PC1; BBS1-dependent PC1 trafficking is not assigned to BBS4. |
| GO:0034464 BBSome | IDA PMID:24550735 The centriolar satellite protein AZI1 interacts with BBS4 an... | ACCEPT | Summary: BBS4 is a BBSome subunit. Reason: Retain the complex-membership annotation, supported by founding purification and subsequent assembly work. BBS4 joins relatively late, and its absence can leave much of the remaining complex assembled; membership does not mean it alone stabilizes every subunit. |
| GO:0005515 protein binding | IPI PMID:24550735 The centriolar satellite protein AZI1 interacts with BBS4 an... | KEEP AS NON CORE | Summary: BBS4 is reported to associate with CEP131/AZI1 (Q9UPN4). Reason: The source supports a CEP131/AZI1-associated BBSome trafficking context. Retain the BBS4 interaction without converting the phenotype of CEP131 perturbation into a new BBS4 catalytic or motor activity. |
| GO:0005813 centrosome | IDA PMID:24550735 The centriolar satellite protein AZI1 interacts with BBS4 an... | ACCEPT | Summary: BBS4 localizes to the centrosome. Reason: Retain the experimentally curated localization, consistent with BBS4’s satellite-associated recruitment and BBSome trafficking roles. A cellular-component annotation need not imply a separate dedicated molecular function. |
| GO:0005929 cilium | IDA PMID:24550735 The centriolar satellite protein AZI1 interacts with BBS4 an... | ACCEPT | Summary: BBS4 localizes to the cilium. Reason: Retain the experimentally curated localization, consistent with BBS4’s satellite-associated recruitment and BBSome trafficking roles. A cellular-component annotation need not imply a separate dedicated molecular function. |
| GO:0034451 centriolar satellite | IDA PMID:24550735 The centriolar satellite protein AZI1 interacts with BBS4 an... | ACCEPT | Summary: BBS4 localizes to the centriolar satellites. Reason: Retain the experimentally curated localization, consistent with BBS4’s satellite-associated recruitment and BBSome trafficking roles. A cellular-component annotation need not imply a separate dedicated molecular function. |
| GO:0000281 mitotic cytokinesis | IMP PMID:15107855 The Bardet-Biedl protein BBS4 targets cargo to the pericentr... | KEEP AS NON CORE | Summary: BBS4 depletion produces a mitotic cytokinesis phenotype. Reason: The original Results document multinucleated HeLa/COS7 cells after BBS4 depletion, together with cell-cycle abnormalities. Retain this experimentally supported process as non-core. The data do not prove a dedicated cytokinetic enzyme, but neither do they establish that every division defect is secondary. |
| GO:0071539 protein localization to centrosome | IMP PMID:15107855 The Bardet-Biedl protein BBS4 targets cargo to the pericentr... | ACCEPT | Summary: BBS4 supports protein localization to the centrosome. Reason: BBS4 depletion or interaction-disrupting constructs disperse PCM1 from the pericentriolar region. This directly supports the process, with recruitment and retention remaining possible components of the mechanism. |
| 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: BBS4 associates with the E3 ubiquitin ligase RNF2. Reason: The source partner Q99496/RNF2 is a PRC1 RING E3 ubiquitin ligase, whereas GO:0061629 requires a sequence-specific RNA-polymerase-II DNA-binding transcription factor. Refine to ubiquitin protein ligase binding. Separately accessed original Results and the Fig.3C caption at https://pmc.ncbi.nlm.nih.gov/articles/PMC3283873/ report tagged BBS4–RNF2 co-immunoprecipitation. The local normal cache is abstract-only; the external text, not cached full text or figure pixels, supplies that assay detail. The endogenous co-IP and yeast-screen experiments concern BBS7. Proposed replacements: ubiquitin protein ligase binding Supporting Evidence: |
| GO:0005813 centrosome | IDA PMID:22500027 Intrinsic protein-protein interaction-mediated and chaperoni... | ACCEPT | Summary: BBS4 localizes to the centrosome. Reason: Retain the experimentally curated localization, consistent with BBS4’s satellite-associated recruitment and BBSome trafficking roles. A cellular-component annotation need not imply a separate dedicated molecular function. |
| GO:0038108 negative regulation of appetite by leptin-mediated signaling pathway | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Bbs4 supports leptin-dependent appetite control. Reason: The mouse donor has direct leptin-response evidence in PMID:19150989. Retain this physiological consequence as non-core without transferring BBS1’s direct leptin-receptor binding to BBS4 or assuming an identical human appetite assay. |
| GO:0034464 BBSome | IDA PMID:20080638 BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family c... | ACCEPT | Summary: BBS4 is a BBSome subunit. Reason: Retain the complex-membership annotation, supported by founding purification and subsequent assembly work. BBS4 joins relatively late, and its absence can leave much of the remaining complex assembled; membership does not mean it alone stabilizes every subunit. |
| GO:0000226 microtubule cytoskeleton organization | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: BBS4 contributes to microtubule organization in more than one cellular context. Reason: Centrosomal anchoring is directly supported by PMID:15107855, while mouse olfactory neurons in PMID:15322545 show broader dendritic microtubule disorganization. Retain the broad process as non-core rather than narrowing every source to centrosomal anchoring and losing the neuronal scope. The specific centrosomal process is retained separately. |
| GO:0001843 neural tube closure | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Mouse Bbs4 has a neural-tube-closure phenotype. Reason: The official donor record assigns this process from PMID:16170314, whose primary abstract addresses BBS/planar-cell-polarity interactions. Retain the existing tissue-level transfer as non-core; the available abstract does not independently resolve every Bbs4 genotype or mechanistic interaction. |
| GO:0001895 retina homeostasis | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Bbs4 supports retinal homeostasis. Reason: Bbs4-null mice develop retinal degeneration, and later trafficking work shows photoreceptor transport defects before cell loss. Retain this existing tissue-maintenance context without assigning a phototransduction catalytic activity. |
| GO:0007286 spermatid development | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Bbs4 supports normal spermatid and sperm flagellum development. Reason: The Bbs4-null mouse study reports male infertility and failure of sperm flagellum formation. Retain this tissue-specific process without equating it to a universal requirement for formation of all cilia. |
| GO:0007608 sensory perception of smell | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Bbs4 supports olfactory function through olfactory-cilium integrity. Reason: Mouse Bbs4 loss disrupts olfactory cilia, and later BBS4 gene delivery restores olfactory function with differential rescue of ciliary properties. Retain the sensory outcome as non-core without classifying BBS4 itself as an odorant receptor. |
| GO:0016358 dendrite development | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Mouse Bbs4 supports normal olfactory-neuron dendritic organization. Reason: The traced donor PMID:15322545 reports disorganized dendritic microtubules and retained proteins in Bbs4-deficient olfactory neurons. Retain the developmental context without claiming a general autonomous neurite-growth activity. |
| GO:0019216 regulation of lipid metabolic process | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Bbs4 perturbation alters lipid metabolism in metabolic models. Reason: Bbs4-null mice show altered lipid/metabolic profiles, and Bbs4-silenced preadipocytes show abnormal lipid accumulation and composition. Retain the existing regulatory process as a physiological context, not a claim that BBS4 catalyzes lipid chemistry. |
| GO:0021756 striatum development | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Bbs4-null mice show abnormal striatum morphology. Reason: PMID:18032602 includes Bbs4-null mice in its neuroanatomical observations despite a Bbs1-focused title. Retain the mouse-derived developmental process as non-core without claiming that an autonomous BBS4 morphogenetic signal or the causal route has been established. |
| GO:0021766 hippocampus development | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Bbs4-null mice show abnormal hippocampus morphology. Reason: PMID:18032602 includes Bbs4-null mice in its neuroanatomical observations despite a Bbs1-focused title. Retain the mouse-derived developmental process as non-core without claiming that an autonomous BBS4 morphogenetic signal or the causal route has been established. |
| GO:0021987 cerebral cortex development | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Bbs4-null mice show abnormal cerebral cortex morphology. Reason: PMID:18032602 includes Bbs4-null mice in its neuroanatomical observations despite a Bbs1-focused title. Retain the mouse-derived developmental process as non-core without claiming that an autonomous BBS4 morphogenetic signal or the causal route has been established. |
| GO:0030534 adult behavior | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Mouse Bbs4 loss alters adult behavior. Reason: The existing donor and the independent Bbs4-null characterization include social-dominance or anxiety-related behavioral abnormalities. Retain this organismal outcome as non-core without equating it to an intrinsic neural signaling activity or a demonstrated human behavior mechanism. |
| GO:0045444 fat cell differentiation | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Bbs4 perturbation affects adipocyte differentiation. Reason: The inherited mouse donor includes expression evidence, while independent PMID:24500759 explicitly silences Bbs4 in 3T3F442A preadipocytes and measures altered differentiation, adipogenic markers and lipid accumulation. This supports the existing context as non-core without claiming that BBS4 is an adipogenic transcription factor or that the molecular step is resolved. |
| GO:0045494 photoreceptor cell maintenance | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Bbs4 supports photoreceptor-cell maintenance. Reason: Retinal degeneration, altered photoreceptor transport and Bbs4/Cep290 genetic interactions support this tissue-specific maintenance process. Retain it as non-core rather than inferring a separate catalytic or structural photoreceptor activity. |
| GO:0045724 positive regulation of cilium assembly | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Bbs4 supports cilium assembly in specific developmental contexts. Reason: The transferred positive-regulation process is supported by Bbs4-loss ciliary phenotypes, especially sperm flagella and specialized sensory structures. Retain it as non-core without asserting universal ciliogenesis necessity or a resolved direct regulatory step. |
| GO:0046548 retinal rod cell development | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Bbs4 is associated with normal retinal rod development and survival. Reason: Retain the existing mouse-derived developmental annotation with curator deference. The available primary evidence documents progressive retinal defects; it does not by itself distinguish every initial differentiation defect from later maintenance failure, so no new rod-specification mechanism is asserted. |
| GO:0048854 brain morphogenesis | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Bbs4-null mice show abnormal brain morphology. Reason: PMID:18032602 includes Bbs4-null mice in its neuroanatomical observations despite a Bbs1-focused title. Retain the mouse-derived developmental process as non-core without claiming that an autonomous BBS4 morphogenetic signal or the causal route has been established. |
| GO:0060271 cilium assembly | ISS GO_REF:0000024 | ACCEPT | Summary: BBS4 contributes to context-dependent cilium assembly and maintenance. Reason: Retain the process in agreement with BBSome-dependent ciliary entry and olfactory/flagellar defects. Primary and motile cilia can form in Bbs4-null mice, so this annotation is not a universal requirement for initial axoneme formation. |
| GO:0060296 regulation of cilium beat frequency involved in ciliary motility | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Bbs4 deficiency affects ciliary beat frequency in airway models. Reason: Retain the transferred regulation process as a tissue-specific consequence. The annotation does not require BBS4 to generate force directly; altered ciliary structure or maintenance can mediate the measured beat-frequency phenotype. |
| GO:1905515 non-motile cilium assembly | ISS GO_REF:0000024 | ACCEPT | Summary: BBS4 contributes to context-dependent cilium assembly and maintenance. Reason: Retain the process in agreement with BBSome-dependent ciliary entry and olfactory/flagellar defects. Primary and motile cilia can form in Bbs4-null mice, so this annotation is not a universal requirement for initial axoneme formation. |
| GO:0034451 centriolar satellite | IDA PMID:15107855 The Bardet-Biedl protein BBS4 targets cargo to the pericentr... | ACCEPT | Summary: BBS4 localizes to the centriolar satellites. Reason: Retain the original localization, consistent with the primary endogenous staining and pericentriolar recruitment experiments. This does not mean BBS4 is exclusive to that site. Supporting Evidence: PMID:15107855 localizes to the centriolar satellites |
| GO:0034452 dynactin binding | IDA PMID:15107855 The Bardet-Biedl protein BBS4 targets cargo to the pericentr... | ACCEPT | Summary: BBS4 binds dynactin through DCTN1/p150-glued. Reason: The primary interaction mapping and co-immunoprecipitation support this specific molecular function within the pericentriolar adaptor mechanism; BBS4 is not itself a dynein motor. Supporting Evidence: PMID:15107855 adaptor of the p150(glued) subunit |
| GO:0034454 microtubule anchoring at centrosome | IMP PMID:15107855 The Bardet-Biedl protein BBS4 targets cargo to the pericentr... | ACCEPT | Summary: BBS4 supports microtubule anchoring at the centrosome. Reason: After BBS4 depletion, microtubules become disorganized and detached from centrosomes while nucleation/regrowth remains detectable. This supports anchoring rather than assigning microtubule nucleation or polymerase activity to BBS4. Supporting Evidence: PMID:15107855 concomitant deanchoring of centrosomal microtubules |
| GO:0034464 BBSome | IDA PMID:17574030 A core complex of BBS proteins cooperates with the GTPase Ra... | ACCEPT | Summary: BBS4 is a BBSome subunit. Reason: Retain the complex-membership annotation, supported by founding purification and subsequent assembly work. BBS4 joins relatively late, and its absence can leave much of the remaining complex assembled; membership does not mean it alone stabilizes every subunit. Supporting Evidence: PMID:17574030 seven highly conserved BBS proteins |
| GO:0000242 pericentriolar material | IDA PMID:15107855 The Bardet-Biedl protein BBS4 targets cargo to the pericentr... | ACCEPT | Summary: BBS4 localizes to the pericentriolar material. Reason: Retain the original localization, consistent with the primary endogenous staining and pericentriolar recruitment experiments. This does not mean BBS4 is exclusive to that site. |
| GO:0005814 centriole | IDA PMID:15107855 The Bardet-Biedl protein BBS4 targets cargo to the pericentr... | ACCEPT | Summary: BBS4 localizes to the centriole. Reason: Retain the original localization, consistent with the primary endogenous staining and pericentriolar recruitment experiments. This does not mean BBS4 is exclusive to that site. |
| GO:0031514 motile cilium | IDA PMID:18299575 Loss of Bardet-Biedl syndrome proteins alters the morphology... | KEEP AS NON CORE | Summary: BBS4 localizes to motile cilia in the airway context. Reason: Retain the direct cellular-component annotation. A motile-cilium location does not require a dedicated beat-generating role. |
| GO:0032465 regulation of cytokinesis | IMP PMID:15107855 The Bardet-Biedl protein BBS4 targets cargo to the pericentr... | KEEP AS NON CORE | Summary: BBS4 perturbation affects regulation of cytokinesis. Reason: Multinucleation and cell-cycle changes after BBS4 depletion support the existing process. Retain it as non-core without requiring an exclusive cytokinesis function or declaring the observed phenotype definitively secondary. |
| GO:0036064 ciliary basal body | IDA PMID:15107855 The Bardet-Biedl protein BBS4 targets cargo to the pericentr... | ACCEPT | Summary: BBS4 localizes to the ciliary basal body. Reason: Retain the original localization, consistent with the primary endogenous staining and pericentriolar recruitment experiments. This does not mean BBS4 is exclusive to that site. |
| GO:0036064 ciliary basal body | IDA PMID:18299575 Loss of Bardet-Biedl syndrome proteins alters the morphology... | ACCEPT | Summary: BBS4 localizes to the ciliary basal body in the airway study. Reason: Retain the experimental site, consistent with independent BBS4 basal-body observations and trafficking functions. |
| GO:0043014 alpha-tubulin binding | IDA PMID:17574030 A core complex of BBS proteins cooperates with the GTPase Ra... | KEEP AS NON CORE | Summary: BBS4 has a curated alpha-tubulin-binding annotation. Reason: Retain the experimentally curated binding as a contextual molecular interaction. The inspected evidence does not justify assigning tubulin polymerase activity or converting the BBSome-associated interaction into a new BBS4 catalytic function. |
| GO:0048487 beta-tubulin binding | IDA PMID:17574030 A core complex of BBS proteins cooperates with the GTPase Ra... | KEEP AS NON CORE | Summary: BBS4 has a curated beta-tubulin-binding annotation. Reason: Retain the experimentally curated binding as a contextual molecular interaction. The inspected evidence does not justify assigning tubulin polymerase activity or converting the BBSome-associated interaction into a new BBS4 catalytic function. |
| GO:0051457 maintenance of protein location in nucleus | IGI PMID:15107855 The Bardet-Biedl protein BBS4 targets cargo to the pericentr... | UNDECIDED | Summary: The nuclear protein-retention assertion remains unresolved. Reason: The inspected PMID:15107855 Results concern PCM1 recruitment or retention at the pericentriolar region. GO:0051457 specifically concerns maintaining proteins within the nucleus. The exact curator annotation context, supplementary evidence and any extension have not been reconstructed, so do not confidently remove or replace this experimental IGI assertion. Later nuclear cargo-transport data do not resolve this particular PCM1 claim. |
| GO:0060170 ciliary membrane | IDA PMID:17574030 A core complex of BBS proteins cooperates with the GTPase Ra... | ACCEPT | Summary: BBS4 localizes to the ciliary membrane. Reason: Retain the direct founding-study localization, concordant with the BBSome role in ciliary membrane protein trafficking. Supporting Evidence: PMID:17574030 membrane of the cilium |
| GO:0097730 non-motile cilium | IDA PMID:17574030 A core complex of BBS proteins cooperates with the GTPase Ra... | ACCEPT | Summary: BBS4 localizes to the non-motile cilium. Reason: Retain the direct founding-study localization, concordant with the BBSome role in ciliary membrane protein trafficking. |
| GO:0005813 centrosome | IDA PMID:14520415 Basal body dysfunction is a likely cause of pleiotropic Bard... | ACCEPT | Summary: BBS4 has a curated centrosomal localization. Reason: Retain the target experimental annotation, independently corroborated by the subsequent BBS4 localization study. A BBS8-focused title does not establish that the earlier paper omitted BBS4 assays. |
| GO:0050893 sensory processing | TAS PMID:14520415 Basal body dysfunction is a likely cause of pleiotropic Bard... | UNDECIDED | Summary: The sensory-processing assertion requires its specific supporting context. Reason: GO:0050893 concerns neural interpretation of sensory information, not merely maintenance of a sensory cilium. The available PMID:14520415 abstract does not resolve the exact BBS4 statement behind this TAS annotation. Retain it as undecided rather than declaring it false from a BBS8-focused abstract or treating a peripheral sensory defect as sufficient proof of the narrower process. |
| GO:0007098 centrosome cycle | IMP PMID:15107855 The Bardet-Biedl protein BBS4 targets cargo to the pericentr... | KEEP AS NON CORE | Summary: BBS4 depletion perturbs the centrosome/cell-division cycle. Reason: The primary experiments report replicated centrioles in multinucleated BBS4-depleted cells and altered DNA-content profiles. Retain the curated process as non-core; these observations do not make BBS4 an autonomous centriole-duplication enzyme and do not prove all effects are secondary. |
| GO:0005515 protein binding | IPI PMID:15107855 The Bardet-Biedl protein BBS4 targets cargo to the pericentr... | MODIFY | Summary: BBS4 binds PCM1 in a pericentriolar recruitment/adaptor mechanism. Reason: The original PMID:15107855 itself establishes BBS4 interactions with PCM1 and DCTN1/p150-glued, their dynein-dependent pericentriolar localization and PCM1 dispersal after BBS4 depletion. These interaction, localization and depletion results support a protein- macromolecule adaptor role. Recruitment and retention of PCM1 both remain compatible with the experiments; the study does not directly visualize every cargo-transport step. The separate ACCEPTed IMP annotation from the same paper records perturbation evidence for this same mechanism; the two source assertions are preserved with their distinct evidence codes. Proposed replacements: protein-macromolecule adaptor activity Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17574030 A core complex of BBS proteins cooperates with the GTPase Ra... | KEEP AS NON CORE | Summary: BBS4 is reported to associate with BBS9 (Q3SYG4). Reason: Retain the partner-specific BBSome association. Complex membership does not by itself define a BBS4 heterodimer or an autonomous cargo-recognition activity for this exact pair. |
| GO:0005515 protein binding | IPI PMID:17574030 A core complex of BBS proteins cooperates with the GTPase Ra... | KEEP AS NON CORE | Summary: BBS4 is reported to associate with BBS1 (Q8NFJ9). Reason: Retain the partner-specific BBSome association. Complex membership does not by itself define a BBS4 heterodimer or an autonomous cargo-recognition activity for this exact pair. |
| GO:0005515 protein binding | IPI PMID:18000879 Novel interaction partners of Bardet-Biedl syndrome proteins... | KEEP AS NON CORE | Summary: BBS4 is reported to associate with EEF1A1 (P68104). Reason: IntAct records EBI-1805886 and EBI-2013866 link BBS4-EEF1A1 to yeast two-hybrid experiments in Tables I and II of PMID:18000879. These curated records support the reported association; the original full article and construct controls were not independently re-read. Retain non-core binding under the explicit project instruction without inferring a BBS4 translation-related activity. |
| GO:0005515 protein binding | IPI PMID:18000879 Novel interaction partners of Bardet-Biedl syndrome proteins... | MODIFY | Summary: BBS4 binds the dynactin subunit DCTN1/p150-glued. Reason: IntAct record EBI-1805881 links the BBS4-DCTN1 pair to the PMID:18000879 Table I yeast two-hybrid experiment. DCTN1 is a dynactin subunit, so dynactin binding refines the identity of the partner. Independent PMID:15107855 corroborates the interaction. The curated source record was checked without newly inspecting the original table or assigning dynein motor activity to BBS4. Proposed replacements: dynactin binding |
| GO:0005515 protein binding | IPI PMID:18000879 Novel interaction partners of Bardet-Biedl syndrome proteins... | KEEP AS NON CORE | Summary: BBS4 has a curated association with PCM1. Reason: IntAct records EBI-1805934 and EBI-2013881 link BBS4-PCM1 to the PMID:18000879 Tables I and II yeast two-hybrid experiments. These curated pair/source/method records were checked; the full paper and construct controls were not independently re-read. Retain this supported interaction as non-core under the explicit project instruction. The complete adaptor mechanism belongs to the separate PMID:15107855 evidence and core function, not to this association assay alone. |
| GO:0005515 protein binding | IPI PMID:18000879 Novel interaction partners of Bardet-Biedl syndrome proteins... | KEEP AS NON CORE | Summary: BBS4 is reported to associate with EPAS1 (Q99814). Reason: IntAct records EBI-1805896 and EBI-1994837 link BBS4-EPAS1 to the PMID:18000879 yeast two-hybrid and co-immunoprecipitation experiments, respectively. The curated pair/source/method linkage was checked; the full article and figure controls were not independently re-read. Retain the supported association as non-core under the explicit project instruction without assigning EPAS1 transcription-factor activity to BBS4. |
| GO:0005515 protein binding | IPI PMID:19081074 A BBSome subunit links ciliogenesis, microtubule stability, ... | KEEP AS NON CORE | Summary: BBS4 has a curated association with PCM1. Reason: Retain this source-specific PCM1 association. The combined PCM1/DCTN1 binding, localization and depletion experiments in PMID:15107855 establish the pericentriolar adaptor mechanism, which is already represented by its own source annotations and the core function. This individual interaction record is not assigned that complete mechanism. The reported association is coherent with the independent PCM1 evidence and is not rejected solely because generic binding is less informative. |
| GO:0005515 protein binding | IPI PMID:19081074 A BBSome subunit links ciliogenesis, microtubule stability, ... | KEEP AS NON CORE | Summary: BBS4 is reported to associate with BBS9 (Q3SYG4). Reason: Retain the partner-specific BBSome association. Complex membership does not by itself define a BBS4 heterodimer or an autonomous cargo-recognition activity for this exact pair. |
| GO:0005515 protein binding | IPI PMID:19081074 A BBSome subunit links ciliogenesis, microtubule stability, ... | KEEP AS NON CORE | Summary: BBS4 is reported to associate with BBS1 (Q8NFJ9). Reason: Retain the partner-specific BBSome association. Complex membership does not by itself define a BBS4 heterodimer or an autonomous cargo-recognition activity for this exact pair. |
| GO:0005515 protein binding | IPI PMID:22500027 Intrinsic protein-protein interaction-mediated and chaperoni... | KEEP AS NON CORE | Summary: BBS4 has a curated association with PCM1. Reason: Retain this source-specific PCM1 association. The combined PCM1/DCTN1 binding, localization and depletion experiments in PMID:15107855 establish the pericentriolar adaptor mechanism, which is already represented by its own source annotations and the core function. This individual interaction record is not assigned that complete mechanism. The reported association is coherent with the independent PCM1 evidence and is not rejected solely because generic binding is less informative. |
| GO:0005515 protein binding | IPI PMID:22500027 Intrinsic protein-protein interaction-mediated and chaperoni... | KEEP AS NON CORE | Summary: BBS4 is reported to associate with BBS1 (Q8NFJ9). Reason: Retain the partner-specific BBSome association. Complex membership does not by itself define a BBS4 heterodimer or an autonomous cargo-recognition activity for this exact pair. |
| GO:0005515 protein binding | IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis... | KEEP AS NON CORE | Summary: BBS4 is reported to associate with BBS1 (Q8NFJ9). Reason: Retain the partner-specific BBSome association. Complex membership does not by itself define a BBS4 heterodimer or an autonomous cargo-recognition activity for this exact pair. |
| GO:0005515 protein binding | IPI PMID:29039417 Protein interaction perturbation profiling at amino-acid res... | KEEP AS NON CORE | Summary: BBS4 is reported to associate with BBS9 (Q3SYG4). Reason: Retain the partner-specific BBSome association. Complex membership does not by itself define a BBS4 heterodimer or an autonomous cargo-recognition activity for this exact pair. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: BBS4 is reported to associate with RARA (P10276). Reason: Retain the experimentally curated partner interaction as non-core under the explicit ClinGen project instruction. The inspected evidence does not establish a finer BBS4 molecular function for this pair. The supported association is retained without using generic binding to describe a core mechanism. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: BBS4 is reported to associate with RARG (P13631). Reason: Retain the experimentally curated partner interaction as non-core under the explicit ClinGen project instruction. The inspected evidence does not establish a finer BBS4 molecular function for this pair. The supported association is retained without using generic binding to describe a core mechanism. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: BBS4 is reported to associate with SPIRE1 (Q08AE8). Reason: Retain the experimentally curated partner interaction as non-core under the explicit ClinGen project instruction. The inspected evidence does not establish a finer BBS4 molecular function for this pair. The supported association is retained without using generic binding to describe a core mechanism. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: BBS4 is reported to associate with ZIC1 (Q15915). Reason: Retain the experimentally curated partner interaction as non-core under the explicit ClinGen project instruction. The inspected evidence does not establish a finer BBS4 molecular function for this pair. The supported association is retained without using generic binding to describe a core mechanism. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: BBS4 is reported to associate with C2CD6 (Q53TS8). Reason: Retain the experimentally curated partner interaction as non-core under the explicit ClinGen project instruction. The inspected evidence does not establish a finer BBS4 molecular function for this pair. The supported association is retained without using generic binding to describe a core mechanism. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | KEEP AS NON CORE | Summary: BBS4 is reported to associate with PLP1 isoform 2 (P60201-2). Reason: Retain the experimentally curated partner interaction as non-core under the explicit ClinGen project instruction. The inspected evidence does not establish a finer BBS4 molecular function for this pair. The supported association is retained without using generic binding to describe a core mechanism. |
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Download this section (compressed HTML)Q: What is the relative contribution of dynein-mediated PCM1 recruitment and retention at centriolar satellites to BBS4's adaptor function?
Q: Which ciliary cargoes require BBS4 contacts directly, and which depend on its contribution to the architecture or trafficking of the BBSome?
Q: What experiment and annotation context support the nuclear-retention annotation, and is there direct evidence for BBS4 nuclear residence?
Experiment: Combine acute BBS4 depletion with live PCM1 tracking and separation-of-function mutants affecting PCM1 or DCTN1 interaction to distinguish recruitment from retention, and compare these immediate effects with subsequent cell-division changes.
Experiment: Compare ciliary trafficking of several defined receptor cargoes after BBS4 depletion and rescue, while measuring BBSome assembly and localization, to separate cargo-specific requirements from effects on the complex.
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