FBXO7

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:1903599 positive regulation of autophagy of mitochondrion	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetic assignment of a positive role in mitophagy, consistent with the experimentally demonstrated FBXO7 function downstream of PINK1 in Parkin-mediated mitophagy. Reason: Core biological process; the IBA inference agrees with direct IMP/IDA evidence (PMID:23933751, PMID:26310625) that FBXO7 promotes clearance of depolarized mitochondria. Supporting Evidence: PMID:23933751 Here we show that Fbxo7 participates in mitochondrial maintenance through direct interaction with PINK1 and Parkin and acts in Parkin-mediated mitophagy. file:human/FBXO7/FBXO7-deep-research-falcon.md FBXO7 participates in mitochondrial quality control by interacting with PINK1 and Parkin and facilitating Parkin recruitment to damaged mitochondria in PARK15 biology.
GO:0019901 protein kinase binding	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: Phylogenetic assignment of protein kinase binding, reflecting the documented FBXO7 interactions with the kinases CDK6 and PINK1. Reason: Real and mechanistically meaningful (CDK6 activation of cyclin D complexes; PINK1 in the mitophagy pathway) but a subsidiary binding activity rather than the core adaptor function. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Interacts with CDK6 and promotes its interaction with D-type cyclin.
GO:0005634 nucleus	IEA GO_REF:0000120	KEEP AS NON CORE	Summary: Electronic assignment of nuclear localization; FBXO7 has a documented minor nuclear pool in addition to its predominant cytoplasmic localization. Reason: Nuclear localization is real but minor; the predominant and functionally dominant compartment is the cytoplasm/cytosol. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt A minor proportion is detected in the nucleus (PubMed:16096642).
GO:0005737 cytoplasm	IEA GO_REF:0000044	ACCEPT	Summary: Electronic transfer of cytoplasmic localization from the UniProt subcellular location; the predominant compartment of FBXO7. Reason: Correct predominant localization, supported experimentally (PMID:16096642, PMID:18495667). Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Note=Predominantly cytoplasmic (PubMed:16096642).
GO:0005739 mitochondrion	IEA GO_REF:0000120	ACCEPT	Summary: Electronic assignment of mitochondrial localization, consistent with the experimentally observed relocation of FBXO7 from the cytosol to depolarized mitochondria. Reason: Correct conditional localization; FBXO7 relocates to depolarized mitochondria during mitophagy (PMID:23933751). Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Relocates from the cytosol to depolarized mitochondria (PubMed:23933751).
GO:0005829 cytosol	IEA GO_REF:0000044	ACCEPT	Summary: Electronic transfer of cytosolic localization from the UniProt subcellular location; the predominant compartment of FBXO7. Reason: Correct core localization, supported experimentally (PMID:23933751). Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Cytoplasm, cytosol {ECO:0000269\|PubMed:23933751}.
GO:0019901 protein kinase binding	IEA GO_REF:0000120	KEEP AS NON CORE	Summary: Electronic assignment of protein kinase binding, reflecting documented CDK6 and PINK1 interactions. Reason: Real binding activity (CDK6, PINK1) but subsidiary to the core ligase-substrate adaptor function. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Interacts with CDK6 and promotes its interaction with D-type cyclin.
GO:0005515 protein binding	IPI PMID:16278047 Characterization of FBX25, encoding a novel brain-expressed ...	KEEP AS NON CORE	Summary: Interaction captured during characterization of a related brain-expressed F-box protein (FBX25). Bare protein binding is uninformative. Reason: Records a real interaction but the bare protein binding term is uninformative per curation guidelines. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex
GO:0005515 protein binding	IPI PMID:22632967 Cyclin F-mediated degradation of ribonucleotide reductase M2...	KEEP AS NON CORE	Summary: Interaction captured in a cyclin F (FBXO1)/RRM2 study. Bare protein binding is uninformative. Reason: Records a real interaction but bare protein binding is uninformative. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex
GO:0005515 protein binding	IPI PMID:23933751 The Parkinson's disease-linked proteins Fbxo7 and Parkin int...	KEEP AS NON CORE	Summary: Interaction with PRKN/Parkin (and PINK1) from the mitophagy study; a functionally important interaction, but the bare protein binding term is uninformative. Reason: Records the meaningful FBXO7-PRKN/PINK1 interaction, but bare protein binding is uninformative; the functional relationship is captured by the mitophagy process annotations. Supporting Evidence: PMID:23933751 the Ubl domain of Fbxo7 directly mediates Parkin interaction
GO:0005515 protein binding	IPI PMID:25416956 A proteome-scale map of the human interactome network.	KEEP AS NON CORE	Summary: High-throughput proteome-scale interactome mapping. Bare protein binding is uninformative. Reason: High-throughput interactome; bare protein binding is uninformative and not a core function. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex
GO:0005515 protein binding	IPI PMID:25910212 Widespread macromolecular interaction perturbations in human...	KEEP AS NON CORE	Summary: High-throughput interactome perturbation study. Bare protein binding is uninformative. Reason: High-throughput interactome; bare protein binding is uninformative. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex
GO:0005515 protein binding	IPI PMID:26496610 A human interactome in three quantitative dimensions organiz...	KEEP AS NON CORE	Summary: High-throughput quantitative interactome map. Bare protein binding is uninformative. Reason: High-throughput interactome; bare protein binding is uninformative. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex
GO:0005515 protein binding	IPI PMID:27705803 A High-Density Map for Navigating the Human Polycomb Complex...	KEEP AS NON CORE	Summary: High-throughput Polycomb complexome interaction map. Bare protein binding is uninformative. Reason: High-throughput interactome; bare protein binding is uninformative. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex
GO:0005515 protein binding	IPI PMID:28514442 Architecture of the human interactome defines protein commun...	KEEP AS NON CORE	Summary: High-throughput interactome (protein communities/disease networks). Bare protein binding is uninformative. Reason: High-throughput interactome; bare protein binding is uninformative. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex
GO:0005515 protein binding	IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari...	KEEP AS NON CORE	Summary: High-throughput variant-interactome disruption study. Bare protein binding is uninformative. Reason: High-throughput interactome; bare protein binding is uninformative. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	KEEP AS NON CORE	Summary: High-throughput neurodegenerative-disease interactome map. Bare protein binding is uninformative. Reason: High-throughput interactome; bare protein binding is uninformative. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	KEEP AS NON CORE	Summary: High-throughput dual proteome-scale interactome map. Bare protein binding is uninformative. Reason: High-throughput interactome; bare protein binding is uninformative. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex
GO:0005515 protein binding	IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func...	KEEP AS NON CORE	Summary: High-throughput multimodal cell-map interactome. Bare protein binding is uninformative. Reason: High-throughput interactome; bare protein binding is uninformative. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex
GO:1901526 positive regulation of mitophagy	IEA GO_REF:0000107	ACCEPT	Summary: Ortholog-based electronic assignment of positive regulation of mitophagy, consistent with the experimentally established FBXO7 mitophagy role. Reason: Core biological process; agrees with direct experimental evidence (PMID:23933751, PMID:26310625). Supporting Evidence: PMID:26310625 The WT FBXO7 protein is vital to cell mitophagy and can facilitate mitophagy to protect cells, whereas mutant FBXO7 inhibits mitophagy.
GO:0016567 protein ubiquitination	IEA GO_REF:0000041	KEEP AS NON CORE	Summary: UniPathway-derived general protein ubiquitination process, a parent of the specific SCF-dependent catabolic process FBXO7 enables. Reason: Correct but generic; the specific GO:0031146 (SCF-dependent catabolic process) and K48-linked ubiquitination annotations better capture the role. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt PATHWAY: Protein modification; protein ubiquitination.
GO:0005654 nucleoplasm	IDA GO_REF:0000052	KEEP AS NON CORE	Summary: HPA immunofluorescence assignment of nucleoplasm localization, consistent with the documented minor nuclear pool of FBXO7. Reason: Real but minor nuclear localization; the predominant compartment is the cytoplasm/cytosol. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt A minor proportion is detected in the nucleus (PubMed:16096642).
GO:0005829 cytosol	IDA GO_REF:0000052	ACCEPT	Summary: HPA immunofluorescence assignment of cytosolic localization, the predominant FBXO7 compartment. Reason: Correct core localization; supported by direct experimental fractionation (PMID:23933751). Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Cytoplasm, cytosol {ECO:0000269\|PubMed:23933751}.
GO:0005634 nucleus	EXP PMID:16096642 Transforming activity of Fbxo7 is mediated specifically thro...	KEEP AS NON CORE	Summary: Experimental localization showing FBXO7 in the nucleus (minor pool) in addition to predominant cytoplasm. Reason: Real minor nuclear localization documented in this study; predominant compartment is cytoplasmic. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt A minor proportion is detected in the nucleus (PubMed:16096642).
GO:0005737 cytoplasm	EXP PMID:16096642 Transforming activity of Fbxo7 is mediated specifically thro...	ACCEPT	Summary: Experimental localization showing FBXO7 is predominantly cytoplasmic. Core compartment. Reason: Core localization with direct experimental support. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Note=Predominantly cytoplasmic (PubMed:16096642).
GO:0005737 cytoplasm	EXP PMID:18495667 Structure of a conserved dimerization domain within the F-bo...	ACCEPT	Summary: Experimental localization to the cytoplasm consistent with the predominant FBXO7 compartment. Reason: Core localization with direct experimental support. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Cytoplasm {ECO:0000269\|PubMed:16096642, ECO:0000269\|PubMed:18495667}.
GO:0019005 SCF ubiquitin ligase complex	NAS PMID:34445249 The SCF Complex Is Essential to Maintain Genome and Chromoso...	ACCEPT	Summary: Author statement that FBXO7 is an F-box component of an SCF E3 ubiquitin ligase complex. Core complex membership. Reason: Core localization/complex; FBXO7 is the substrate-receptor F-box subunit of SCF(FBXO7) (CUL1, SKP1, RBX1, FBXO7). Supporting Evidence: PMID:34445249 The SKP1, CUL1, F-box protein (SCF) complex encompasses a group of 69 SCF E3 ubiquitin ligase complexes that primarily modify protein substrates with poly-ubiquitin chains to target them for proteasomal degradation.
GO:0031146 SCF-dependent proteasomal ubiquitin-dependent protein catabolic process	NAS PMID:34445249 The SCF Complex Is Essential to Maintain Genome and Chromoso...	ACCEPT	Summary: Author statement linking the SCF complex (including F-box proteins) to SCF-dependent proteasomal degradation. Core biological process. Reason: Core biological process; FBXO7 targets substrates for SCF-dependent proteasomal degradation. Supporting Evidence: PMID:34445249 These SCF complexes are distinguishable by variable F-box proteins, which determine substrate specificity.
GO:0005634 nucleus	IDA PMID:33010352 The E3 ubiquitin ligase SCF(Fbxo7) mediates proteasomal degr...	KEEP AS NON CORE	Summary: Direct evidence that FBXO7 acts in the nucleus, where it colocalizes with and ubiquitinates its substrate UXT-V2. Reason: Documents a functionally relevant nuclear pool (UXT-V2 degradation) but nuclear localization is minor relative to the predominant cytoplasm/cytosol. Supporting Evidence: PMID:33010352 We find that UXT-V2 colocalizes with Fbxo7 in the cell nucleus.
GO:0031146 SCF-dependent proteasomal ubiquitin-dependent protein catabolic process	IDA PMID:33010352 The E3 ubiquitin ligase SCF(Fbxo7) mediates proteasomal degr...	ACCEPT	Summary: Direct evidence that SCF(FBXO7) mediates SCF-dependent proteasomal degradation of UXT-V2. Core biological process. Reason: Core biological process with direct experimental support; SCF(FBXO7) polyubiquitinates UXT-V2 for proteasomal degradation. Supporting Evidence: PMID:33010352 Together, our study reveals that SCF(Fbxo7) mediates the proteasomal degradation of UXT-V2 causing the inhibition of the NF-κB signaling pathway.
GO:0043124 negative regulation of canonical NF-kappaB signal transduction	IDA PMID:33010352 The E3 ubiquitin ligase SCF(Fbxo7) mediates proteasomal degr...	ACCEPT	Summary: Direct evidence that SCF(FBXO7)-mediated degradation of UXT-V2 inhibits NF-kappa-B signaling. Well-supported biological process. Reason: Directly demonstrated; FBXO7 negatively regulates NF-kappa-B signaling via UXT-V2 (and TRAF2/cIAP1) ubiquitination. Supporting Evidence: PMID:33010352 Together, our study reveals that SCF(Fbxo7) mediates the proteasomal degradation of UXT-V2 causing the inhibition of the NF-κB signaling pathway.
GO:0070936 protein K48-linked ubiquitination	IDA PMID:33010352 The E3 ubiquitin ligase SCF(Fbxo7) mediates proteasomal degr...	ACCEPT	Summary: Direct evidence that SCF(FBXO7) builds K48 (and K63) polyubiquitin chains on UXT-V2. Reason: Directly demonstrated K48-linked ubiquitination of a substrate, the canonical degradative topology used by SCF(FBXO7). Supporting Evidence: PMID:33010352 This substrate is polyubiquitinated by SCF(Fbxo7) with K48 and K63 ubiquitin chain linkages in vitro and in vivo.
GO:1901526 positive regulation of mitophagy	IDA PMID:26310625 F-box protein 7 mutations promote protein aggregation in mit...	ACCEPT	Summary: Direct evidence that WT FBXO7 facilitates mitophagy whereas PD-linked mutants inhibit it. Core biological process. Reason: Core biological process with direct experimental support. Supporting Evidence: PMID:26310625 The WT FBXO7 protein is vital to cell mitophagy and can facilitate mitophagy to protect cells, whereas mutant FBXO7 inhibits mitophagy.
GO:1903377 negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway	IMP PMID:25029497 FBXO7 Y52C polymorphism as a potential protective factor in ...	KEEP AS NON CORE	Summary: Mutant-phenotype evidence linking an FBXO7 variant (Y52C) to altered TRAF2 turnover and neuronal outgrowth in a PD-protective context. Reason: A context-specific neuronal stress/apoptosis-modulating role inferred from variant phenotypes, not the core SCF adaptor function. Supporting Evidence: PMID:25029497 After induced differentiation, SH-SY5Y cells expressing Cys52 FBXO7 displayed increased neuronal outgrowth.
GO:1903377 negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway	IDA PMID:26310625 F-box protein 7 mutations promote protein aggregation in mit...	KEEP AS NON CORE	Summary: Evidence that FBXO7 acts as a stress-response protein with cytoprotective (and, when mutant/aggregated, neurotoxic) effects under oxidative stress. Reason: A context-specific neuronal stress-response role; mechanistically downstream of the core mitophagy/proteostasis functions rather than a distinct core process. Supporting Evidence: PMID:26310625 Here we demonstrated that wild-type (WT) FBXO7 is a stress response protein and it can play both cytoprotective and neurotoxic roles.
GO:0005634 nucleus	IDA PMID:36646384 E3 ligase adaptor FBXO7 contributes to ubiquitination and pr...	KEEP AS NON CORE	Summary: Direct evidence that FBXO7 colocalizes with its substrate SIRT7 mainly in the nucleus, where it acts to degrade SIRT7. Reason: Documents a functionally relevant nuclear pool (SIRT7 degradation) but nuclear localization is minor relative to the predominant cytoplasm/cytosol. Supporting Evidence: PMID:36646384 immunohistochemical analysis of SH-SY5Y cells revealed that endogenous FBXO7 and SIRT7 colocalized mainly in the nucleus
GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process	IDA PMID:36646384 E3 ligase adaptor FBXO7 contributes to ubiquitination and pr...	ACCEPT	Summary: Direct evidence that FBXO7 drives SCF-dependent proteasomal degradation of SIRT7. Core biological process. Reason: Core biological process; FBXO7 promotes proteasomal degradation of SIRT7 (the more specific GO:0031146 SCF-dependent process is also annotated). Supporting Evidence: PMID:36646384 we identified FBXO7 as a novel E3 ligase for SIRT7 that negatively regulates intracellular SIRT7 levels through SCF-dependent Lys-48-linked polyubiquitination and proteasomal degradation
GO:0070936 protein K48-linked ubiquitination	IDA PMID:36646384 E3 ligase adaptor FBXO7 contributes to ubiquitination and pr...	ACCEPT	Summary: Direct evidence that FBXO7 promotes K48-linked polyubiquitination of SIRT7. Reason: Directly demonstrated K48-linked ubiquitination of a substrate (SIRT7), the canonical degradative topology of SCF(FBXO7). Supporting Evidence: PMID:36646384 These results demonstrated that FBXO7 directly mediates the polyubiquitination of SIRT7 by targeting K48-linked polyubiquitin chains.
GO:1990756 ubiquitin-like ligase-substrate adaptor activity	IDA PMID:36646384 E3 ligase adaptor FBXO7 contributes to ubiquitination and pr...	ACCEPT	Summary: Direct evidence that FBXO7 acts as an SCF substrate-recognition adaptor recruiting SIRT7 for ubiquitination. Core molecular function. Reason: Core molecular function; FBXO7 is the substrate-recognition adaptor of SCF(FBXO7), bridging substrates to the catalytic cullin-RING core. Supporting Evidence: PMID:36646384 FBXO7 is an adaptor protein in the SKP1-Cullin-1-F-box (SCF) E3 ligase complex that facilitates the ubiquitination of substrates.
GO:0019005 SCF ubiquitin ligase complex	IDA PMID:15145941 Fbx7 functions in the SCF complex regulating Cdk1-cyclin B-p...	ACCEPT	Summary: Direct evidence that FBXO7 functions within an SCF(FBXO7) complex (with SKP1 and CUL1) to ubiquitinate HURP/DLGAP5. Core complex membership. Reason: Core localization/complex; FBXO7 is a functional F-box subunit of an SCF ubiquitin-ligase complex. Supporting Evidence: PMID:15145941 In the SCF(Fbx7) complex, Fbx7 recruits HURP through its C-terminal proline-rich region in a Cdk1-cyclin B-phosphorylation dependent manner.
GO:1990756 ubiquitin-like ligase-substrate adaptor activity	IDA PMID:15145941 Fbx7 functions in the SCF complex regulating Cdk1-cyclin B-p...	ACCEPT	Summary: Direct evidence that FBXO7 functions as a substrate-recruiting adaptor of the SCF complex, binding HURP via its proline-rich region. Core molecular function. Reason: Core molecular function; FBXO7 is a functional SCF adaptor with the proline-rich region serving as the substrate-binding module. Supporting Evidence: PMID:15145941 Thus, Fbx7 is a functional adaptor of the SCF complex with a proline-rich region as the substrate-binding module.
GO:0005515 protein binding	IPI PMID:21378169 A Competitive binding mechanism between Skp1 and exportin 1 ...	KEEP AS NON CORE	Summary: Interaction captured in a study of SKP1/CRM1 competition controlling F-box protein localization. Bare protein binding is uninformative. Reason: Records a real interaction relevant to FBXO7 nuclear/cytoplasmic shuttling (SKP1, CRM1) but bare protein binding is uninformative. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complex SCF(FBXO7) formed of CUL1, SKP1, RBX1 and FBXO7.
GO:0005739 mitochondrion	IDA PMID:26310625 F-box protein 7 mutations promote protein aggregation in mit...	ACCEPT	Summary: Direct evidence that FBXO7 concentrates into mitochondria upon stress, forming aggregates. Conditional/stress-induced localization. Reason: Correct conditional localization; FBXO7 relocates to mitochondria under stress/depolarization, consistent with its mitophagy role. Supporting Evidence: PMID:26310625 Upon stress, the endogenous WT FBXO7 gets up-regulated, concentrates into mitochondria and forms FBXO7 aggregates in mitochondria.
GO:0005515 protein binding	IPI PMID:25029497 FBXO7 Y52C polymorphism as a potential protective factor in ...	KEEP AS NON CORE	Summary: Interaction with TRAF2 captured in the FBXO7 Y52C polymorphism study. Bare protein binding is uninformative. Reason: Records the functionally meaningful FBXO7-TRAF2 interaction but bare protein binding is uninformative; the substrate relationship is captured by the ubiquitination/NF-kappa-B annotations. Supporting Evidence: PMID:25029497 Moreover, Cys52 FBXO7 showed stronger interaction with TRAF2 and promoted TRAF2 ubiquitination
GO:0005634 nucleus	IDA PMID:16510124 The F-box protein Fbxo7 interacts with human inhibitor of ap...	KEEP AS NON CORE	Summary: Direct evidence of FBXO7 nuclear localization (colocalized with cIAP1/BIRC2 in cytoplasm and nucleus). Minor nuclear pool. Reason: Real but minor nuclear localization; predominant compartment is cytoplasm/cytosol. Supporting Evidence: PMID:16510124 When co-expressed in cells, cIAP1 and Fbxo7 co-localized remarkably both in the cytoplasm and nucleus
GO:0005634 nucleus	IDA PMID:25029497 FBXO7 Y52C polymorphism as a potential protective factor in ...	KEEP AS NON CORE	Summary: Direct evidence of FBXO7 nuclear localization, consistent with the documented minor nuclear pool. Reason: Real but minor nuclear localization; predominant compartment is cytoplasm/cytosol. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt A minor proportion is detected in the nucleus (PubMed:16096642).
GO:0005737 cytoplasm	IDA PMID:16510124 The F-box protein Fbxo7 interacts with human inhibitor of ap...	ACCEPT	Summary: Direct evidence of FBXO7 cytoplasmic localization (colocalized with cIAP1/BIRC2). Core compartment. Reason: Core localization with direct experimental support. Supporting Evidence: PMID:16510124 When co-expressed in cells, cIAP1 and Fbxo7 co-localized remarkably both in the cytoplasm and nucleus
GO:0005737 cytoplasm	IDA PMID:25029497 FBXO7 Y52C polymorphism as a potential protective factor in ...	ACCEPT	Summary: Direct evidence of FBXO7 cytoplasmic localization. Core compartment. Reason: Core localization with direct experimental support. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Note=Predominantly cytoplasmic (PubMed:16096642).
GO:0006511 ubiquitin-dependent protein catabolic process	IDA PMID:25029497 FBXO7 Y52C polymorphism as a potential protective factor in ...	KEEP AS NON CORE	Summary: Direct evidence that FBXO7 promotes ubiquitination and turnover of TRAF2. A parent of the more specific SCF-dependent catabolic process. Reason: Correct but generic relative to the specific GO:0031146 (SCF-dependent proteasomal catabolic process); here the substrate is TRAF2. Supporting Evidence: PMID:25029497 In cells expressing Cys52 FBXO7, the level of TNF receptor-associated factor 2 (TRAF2) was significantly reduced.
GO:0010975 regulation of neuron projection development	IMP PMID:25029497 FBXO7 Y52C polymorphism as a potential protective factor in ...	KEEP AS NON CORE	Summary: Mutant-phenotype evidence that an FBXO7 variant alters neuronal outgrowth in differentiated SH-SY5Y cells. Reason: A context-specific neuronal phenotype linked to an FBXO7 variant, not the core SCF adaptor function. Supporting Evidence: PMID:25029497 After induced differentiation, SH-SY5Y cells expressing Cys52 FBXO7 displayed increased neuronal outgrowth.
GO:0016567 protein ubiquitination	IDA PMID:16510124 The F-box protein Fbxo7 interacts with human inhibitor of ap...	KEEP AS NON CORE	Summary: Direct evidence that FBXO7 overexpression promotes ubiquitination of cIAP1/BIRC2. Generic parent process. Reason: Correct but generic; the specific SCF-dependent catabolic process (GO:0031146) better captures the role. The cIAP1/BIRC2 substrate relationship is meaningful. Supporting Evidence: PMID:16510124 Furthermore, we showed that overexpression of Fbxo7 promotes the ubiquitination of cIAP1.
GO:0019901 protein kinase binding	IPI PMID:18495667 Structure of a conserved dimerization domain within the F-bo...	KEEP AS NON CORE	Summary: Interaction with the kinase CDK6 (and PSMF1) documented in the FP-domain structural study. Reason: Real CDK6 binding (FBXO7 activates cyclin D-CDK6) but subsidiary to the core adaptor function. Supporting Evidence: PMID:18495667 SCF(Fbxo7) is known to catalyze the ubiquitination of hepatoma-up-regulated protein (HURP) and the inhibitor of apoptosis (IAP) protein but also functions as an activator of cyclin D-Cdk6 complexes.
GO:0031625 ubiquitin protein ligase binding	IPI PMID:16510124 The F-box protein Fbxo7 interacts with human inhibitor of ap...	KEEP AS NON CORE	Summary: Interaction with the ubiquitin ligase cIAP1/BIRC2 (itself a RING E3) documented as an FBXO7 substrate interaction. Reason: Records a real interaction with a ubiquitin ligase substrate (BIRC2) but is subsidiary to the core adaptor function. Supporting Evidence: PMID:16510124 we performed a yeast two-hybrid screen and identified an F-box protein Fbxo7 as a cIAP1 interacting protein.
GO:0043130 ubiquitin binding	IDA PMID:25029497 FBXO7 Y52C polymorphism as a potential protective factor in ...	KEEP AS NON CORE	Summary: Assignment of ubiquitin binding to FBXO7. A plausible but ancillary activity relative to the core substrate-adaptor function. Reason: If accurate, ubiquitin binding is a subsidiary molecular feature; the core function is the ligase-substrate adaptor activity. Not central to the documented FBXO7 roles. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt The ubiquitin-like region mediates interaction with PRKN.
GO:0046982 protein heterodimerization activity	IPI PMID:18495667 Structure of a conserved dimerization domain within the F-bo...	KEEP AS NON CORE	Summary: Direct evidence that FBXO7 heterodimerizes with PSMF1/PI31 via the shared FP domain (and homodimerizes). Reason: Real FP-domain-mediated dimerization with PSMF1/PI31 (relevant to proteasome regulation) but a structural/binding property rather than the core adaptor function. Supporting Evidence: PMID:18495667 We identify PI31 as an Fbxo7.Skp1 binding partner and show that this interaction requires an N-terminal domain present in both proteins that we term the FP (Fbxo7/PI31) domain.
GO:0005634 nucleus	IDA PMID:21347293 Loss of nuclear activity of the FBXO7 protein in patients wi...	KEEP AS NON CORE	Summary: Direct evidence that wild-type FBXO7 isoform 1 displays mostly diffuse nuclear localization, with loss of nuclear localization in PARK15 mutants. Reason: This study emphasizes a nuclear pool, but UniProt and other studies establish that FBXO7 is predominantly cytoplasmic; nuclear localization is treated as non-core. Supporting Evidence: PMID:21347293 the endogenous or over-expressed, wild type FBXO7 isoform 1 displays mostly a diffuse nuclear localization
GO:0005737 cytoplasm	IDA PMID:21347293 Loss of nuclear activity of the FBXO7 protein in patients wi...	ACCEPT	Summary: Direct evidence of FBXO7 cytoplasmic localization, including mutant-induced cytoplasmic mislocalization. Core compartment. Reason: Core localization with direct experimental support; PARK15 N-terminal mutations shift FBXO7 to the cytoplasm. Supporting Evidence: PMID:21347293 N-terminal modification by PARK15-linked missense mutation, or N-terminus tag leads to cytoplasmic mislocalization
GO:0005634 nucleus	IDA PMID:23656991 FBXO7 immunoreactivity in α-synuclein-containing inclusions ...	KEEP AS NON CORE	Summary: Immunohistochemical detection of FBXO7 in human brain neurons; widespread expression. Reported nuclear/cytoplasmic neuronal staining. Reason: Brain immunoreactivity localization; nuclear pool is minor relative to predominant cytoplasm. Supporting Evidence: PMID:23656991 We detected widespread brain FBXO7 immunoreactivity, with the highest levels in neurons of the cerebral cortex, putamen, and cerebellum.
GO:0005737 cytoplasm	IDA PMID:23656991 FBXO7 immunoreactivity in α-synuclein-containing inclusions ...	ACCEPT	Summary: Immunohistochemical detection of FBXO7 in the cytoplasm of human brain neurons. Consistent with predominant cytoplasmic localization. Reason: Consistent with the core cytoplasmic localization of FBXO7 in neurons. Supporting Evidence: PMID:23656991 We detected widespread brain FBXO7 immunoreactivity, with the highest levels in neurons of the cerebral cortex, putamen, and cerebellum.
GO:0019005 SCF ubiquitin ligase complex	TAS PMID:16510124 The F-box protein Fbxo7 interacts with human inhibitor of ap...	ACCEPT	Summary: Author statement that F-box proteins such as FBXO7 are specificity-determining subunits of SCF ubiquitin ligases. Core complex membership. Reason: Core localization/complex; FBXO7 is the F-box substrate-receptor subunit of an SCF E3 ligase. Supporting Evidence: PMID:16510124 Since F-box proteins are specificity determining subunits of SCF ubiquitin protein ligases, our results suggest that Fbxo7 can mediate the ubiquitination of cIAP1 by SCF ubiquitin protein ligase
GO:0097409 glial cytoplasmic inclusion	IDA PMID:23656991 FBXO7 immunoreactivity in α-synuclein-containing inclusions ...	KEEP AS NON CORE	Summary: Direct immunoreactivity for FBXO7 within alpha-synuclein-positive glial cytoplasmic inclusions in multiple system atrophy. A disease-pathology localization. Reason: Real IDA immunoreactivity in pathological inclusions, but this is a disease-associated localization, not a core physiological compartment. Supporting Evidence: PMID:23656991 FBXO7 immunoreactivity was detected in large proportions of α-synuclein-positive inclusions (Lewy bodies, Lewy neurites, glial cytoplasmic inclusions)
GO:0097414 classical Lewy body	IDA PMID:23656991 FBXO7 immunoreactivity in α-synuclein-containing inclusions ...	KEEP AS NON CORE	Summary: Direct immunoreactivity for FBXO7 within alpha-synuclein-positive Lewy bodies in Parkinson disease. A disease-pathology localization. Reason: Real IDA immunoreactivity in pathological inclusions, but a disease-associated localization, not a core physiological compartment. Supporting Evidence: PMID:23656991 FBXO7 immunoreactivity was detected in large proportions of α-synuclein-positive inclusions (Lewy bodies, Lewy neurites, glial cytoplasmic inclusions)
GO:0097462 Lewy neurite	IDA PMID:23656991 FBXO7 immunoreactivity in α-synuclein-containing inclusions ...	KEEP AS NON CORE	Summary: Direct immunoreactivity for FBXO7 within alpha-synuclein-positive Lewy neurites. A disease-pathology localization. Reason: Real IDA immunoreactivity in pathological inclusions, but a disease-associated localization, not a core physiological compartment. Supporting Evidence: PMID:23656991 FBXO7 immunoreactivity was detected in large proportions of α-synuclein-positive inclusions (Lewy bodies, Lewy neurites, glial cytoplasmic inclusions)
GO:1990037 Lewy body core	IDA PMID:23656991 FBXO7 immunoreactivity in α-synuclein-containing inclusions ...	KEEP AS NON CORE	Summary: Direct immunoreactivity for FBXO7 colocalizing with alpha-synuclein in Lewy body structures. A disease-pathology localization. Reason: Real IDA immunoreactivity in pathological inclusions, but a disease-associated localization, not a core physiological compartment. Supporting Evidence: PMID:23656991 where it colocalized with α-synuclein in PD and MSA cases
GO:1990038 Lewy body corona	IDA PMID:23656991 FBXO7 immunoreactivity in α-synuclein-containing inclusions ...	KEEP AS NON CORE	Summary: Direct immunoreactivity for FBXO7 colocalizing with alpha-synuclein in Lewy body structures. A disease-pathology localization. Reason: Real IDA immunoreactivity in pathological inclusions, but a disease-associated localization, not a core physiological compartment. Supporting Evidence: PMID:23656991 where it colocalized with α-synuclein in PD and MSA cases
GO:0005634 nucleus	IDA PMID:21378169 A Competitive binding mechanism between Skp1 and exportin 1 ...	KEEP AS NON CORE	Summary: Direct evidence relating to FBXO7 nuclear/cytoplasmic distribution governed by SKP1/CRM1 competition. Reason: Real but minor nuclear localization governed by SKP1/CRM1 shuttling; predominant compartment is cytoplasm. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt A minor proportion is detected in the nucleus (PubMed:16096642).
GO:0005737 cytoplasm	IDA PMID:21378169 A Competitive binding mechanism between Skp1 and exportin 1 ...	ACCEPT	Summary: Direct evidence of FBXO7 cytoplasmic localization controlled by SKP1/CRM1 competition. Core compartment. Reason: Core localization with direct experimental support. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Note=Predominantly cytoplasmic (PubMed:16096642).
GO:0040012 regulation of locomotion	IDA PMID:26310625 F-box protein 7 mutations promote protein aggregation in mit...	KEEP AS NON CORE	Summary: Organismal locomotor phenotype associated with FBXO7 (Drosophila dopamine-neuron degeneration and PD-related models), reflecting its mitophagy/neuroprotection role. Reason: An organismal/neurodegeneration phenotype downstream of the core mitophagy function rather than a distinct cell-autonomous core process. Supporting Evidence: PMID:26310625 The overexpression of WT FBXO7 could lead to FBXO7 protein aggregation and dopamine neuron degeneration in transgenic Drosophila heads.
GO:0005829 cytosol	TAS Reactome:R-HSA-8952618	ACCEPT	Summary: Reactome neddylation/CRL-machinery pathway annotation placing FBXO7 in the cytosol. The cytosol is the predominant FBXO7 compartment. Reason: Correct core localization; cytosol is the predominant compartment for the SCF(FBXO7) complex. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Cytoplasm, cytosol {ECO:0000269\|PubMed:23933751}.
GO:0005829 cytosol	TAS Reactome:R-HSA-8952620	ACCEPT	Summary: Reactome CRL-machinery pathway annotation placing FBXO7 in the cytosol. Reason: Correct core localization; cytosol is the predominant compartment. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Cytoplasm, cytosol {ECO:0000269\|PubMed:23933751}.
GO:0005829 cytosol	TAS Reactome:R-HSA-8955241	ACCEPT	Summary: Reactome CRL-machinery pathway annotation (CAND1 binding) placing FBXO7 in the cytosol. Reason: Correct core localization; cytosol is the predominant compartment. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Cytoplasm, cytosol {ECO:0000269\|PubMed:23933751}.
GO:0005829 cytosol	TAS Reactome:R-HSA-8955289	ACCEPT	Summary: Reactome CRL-machinery pathway annotation (COMMD/CAND1) placing FBXO7 in the cytosol. Reason: Correct core localization; cytosol is the predominant compartment. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Cytoplasm, cytosol {ECO:0000269\|PubMed:23933751}.
GO:0005829 cytosol	TAS Reactome:R-HSA-8956040	ACCEPT	Summary: Reactome CRL-machinery pathway annotation (COP9 signalosome deneddylation) placing FBXO7 in the cytosol. Reason: Correct core localization; cytosol is the predominant compartment. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Cytoplasm, cytosol {ECO:0000269\|PubMed:23933751}.
GO:0005829 cytosol	TAS Reactome:R-HSA-8956200	ACCEPT	Summary: Reactome CRL-machinery pathway annotation (DCUN1D3) placing FBXO7 in the cytosol. Reason: Correct core localization; cytosol is the predominant compartment. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Cytoplasm, cytosol {ECO:0000269\|PubMed:23933751}.
GO:0005829 cytosol	TAS Reactome:R-HSA-983140	ACCEPT	Summary: Reactome ubiquitination-pathway annotation (Ub transfer from E2 to substrate) placing FBXO7 in the cytosol. Reason: Correct core localization; cytosol is the predominant compartment. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Cytoplasm, cytosol {ECO:0000269\|PubMed:23933751}.
GO:0005829 cytosol	TAS Reactome:R-HSA-983147	ACCEPT	Summary: Reactome ubiquitination-pathway annotation (release of E3 from polyubiquitinated substrate) placing FBXO7 in the cytosol. Reason: Correct core localization; cytosol is the predominant compartment. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Cytoplasm, cytosol {ECO:0000269\|PubMed:23933751}.
GO:0005829 cytosol	TAS Reactome:R-HSA-983156	ACCEPT	Summary: Reactome ubiquitination-pathway annotation (polyubiquitination of substrate) placing FBXO7 in the cytosol. Reason: Correct core localization; cytosol is the predominant compartment. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Cytoplasm, cytosol {ECO:0000269\|PubMed:23933751}.
GO:0005829 cytosol	TAS Reactome:R-HSA-983157	ACCEPT	Summary: Reactome ubiquitination-pathway annotation (interaction of E3 with substrate and E2-Ub complex) placing FBXO7 in the cytosol. Reason: Correct core localization; cytosol is the predominant compartment. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Cytoplasm, cytosol {ECO:0000269\|PubMed:23933751}.
GO:0005634 nucleus	IDA PMID:18495667 Structure of a conserved dimerization domain within the F-bo...	KEEP AS NON CORE	Summary: Direct evidence of FBXO7 nuclear localization documented in the FP-domain study. Minor nuclear pool. Reason: Real but minor nuclear localization; predominant compartment is cytoplasm/cytosol. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Nucleus {ECO:0000269\|PubMed:16096642, ECO:0000269\|PubMed:18495667, ECO:0000269\|PubMed:33010352}.
GO:0005829 cytosol	IDA PMID:18495667 Structure of a conserved dimerization domain within the F-bo...	ACCEPT	Summary: Direct evidence of FBXO7 cytosolic localization. Core compartment. Reason: Core localization with direct experimental support. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Cytoplasm {ECO:0000269\|PubMed:16096642, ECO:0000269\|PubMed:18495667}.
GO:0000151 ubiquitin ligase complex	IDA PMID:23933751 The Parkinson's disease-linked proteins Fbxo7 and Parkin int...	KEEP AS NON CORE	Summary: Direct evidence that FBXO7 is part of a ubiquitin ligase complex (the SCF(FBXO7) complex). Generic parent of the specific SCF complex term. Reason: Correct but generic; the more specific GO:0019005 (SCF ubiquitin ligase complex) better captures FBXO7's complex membership. Supporting Evidence: PMID:23933751 F-box domain-containing proteins target substrates to SCF-type (Skp1-Cul1-F-box) E3-ubiquitin ligase complexes
GO:0000422 autophagy of mitochondrion	IMP PMID:23933751 The Parkinson's disease-linked proteins Fbxo7 and Parkin int...	ACCEPT	Summary: Mutant-phenotype evidence that reducing FBXO7 impairs CCCP-induced mitophagy and that FBXO7 acts in Parkin-mediated mitophagy. Core biological process. Reason: Core biological process with direct experimental (IMP) support; FBXO7 knockdown reduces mitophagy and FBXO7 rescues parkin mutant phenotypes. Supporting Evidence: PMID:23933751 Cells with reduced Fbxo7 expression showed deficiencies in translocation of Parkin to mitochondria, ubiquitination of mitofusin 1 and mitophagy.
GO:0005739 mitochondrion	IDA PMID:23933751 The Parkinson's disease-linked proteins Fbxo7 and Parkin int...	ACCEPT	Summary: Direct evidence that FBXO7 relocates from the cytosol to depolarized mitochondria following CCCP treatment. Conditional localization. Reason: Correct conditional/stress-induced localization central to the mitophagy function. Supporting Evidence: PMID:23933751 endogenous Fbxo7 levels were found to decrease steadily in the cytosolic fraction and increase concurrently in the mitochondrial fractions
GO:0005829 cytosol	IDA PMID:23933751 The Parkinson's disease-linked proteins Fbxo7 and Parkin int...	ACCEPT	Summary: Direct evidence that FBXO7 is predominantly cytosolic (before relocating to depolarized mitochondria). Core compartment. Reason: Core localization with direct experimental support (cell fractionation). Supporting Evidence: PMID:23933751 although both proteins localise predominantly to the cytosol
GO:0016567 protein ubiquitination	IMP PMID:23933751 The Parkinson's disease-linked proteins Fbxo7 and Parkin int...	KEEP AS NON CORE	Summary: Mutant-phenotype evidence that FBXO7 is required for CCCP-induced mitofusin 1 ubiquitination (via promoting Parkin recruitment). Generic parent process. Reason: Correct but generic; FBXO7 facilitates substrate (Mfn1) ubiquitination chiefly by promoting Parkin recruitment. The specific mitophagy annotations better capture the role. Supporting Evidence: PMID:23933751 Cells with reduced Fbxo7 expression showed deficiencies in translocation of Parkin to mitochondria, ubiquitination of mitofusin 1 and mitophagy.
GO:0070585 protein localization to mitochondrion	IMP PMID:23933751 The Parkinson's disease-linked proteins Fbxo7 and Parkin int...	ACCEPT	Summary: Mutant-phenotype evidence that FBXO7 is required for Parkin translocation to depolarized mitochondria. Well-supported process. Reason: Directly demonstrated; FBXO7 facilitates Parkin recruitment to mitochondria, a key step in mitophagy. Supporting Evidence: PMID:23933751 Overall, these data indicate that Fbxo7 facilitates Parkin translocation to the mitochondria in response to depolarisation.
GO:0032991 protein-containing complex	IDA GO_REF:0000054	KEEP AS NON CORE	Summary: LIFEdb fusion-protein localization assignment of generic protein-containing complex membership. Reason: Correct but generic; the specific SCF ubiquitin ligase complex (GO:0019005) is far more informative. Supporting Evidence: file:human/FBXO7/FBXO7-uniprot.txt Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complex SCF(FBXO7) formed of CUL1, SKP1, RBX1 and FBXO7.
GO:0031647 regulation of protein stability	IDA PMID:15145941 Fbx7 functions in the SCF complex regulating Cdk1-cyclin B-p...	KEEP AS NON CORE	Summary: Direct evidence that FBXO7 controls the stability/abundance of its substrate HURP via ubiquitination. Reason: Correct but generic; FBXO7 regulates substrate stability through the more specific SCF-dependent catabolic process (GO:0031146). Supporting Evidence: PMID:15145941 Depletion of Fbx7 by small interfering RNA leads to depression of HURP ubiquitination and accumulation of HURP abundance.
GO:0005515 protein binding	IPI PMID:15145941 Fbx7 functions in the SCF complex regulating Cdk1-cyclin B-p...	KEEP AS NON CORE	Summary: Interaction with the substrate DLGAP5/HURP (and CUL1/SKP1) from the HURP proteolysis study. Bare protein binding is uninformative. Reason: Records the meaningful FBXO7-HURP/DLGAP5 substrate interaction, but bare protein binding is uninformative; captured by the SCF/adaptor annotations. Supporting Evidence: PMID:15145941 In the SCF(Fbx7) complex, Fbx7 recruits HURP through its C-terminal proline-rich region in a Cdk1-cyclin B-phosphorylation dependent manner.
GO:0000151 ubiquitin ligase complex	TAS PMID:10531035 Identification of a family of human F-box proteins.	KEEP AS NON CORE	Summary: Author statement that F-box proteins are subunits of SCF ubiquitin protein ligases. Generic parent of the SCF complex term. Reason: Correct but generic; the more specific GO:0019005 (SCF ubiquitin ligase complex) better captures FBXO7's membership. Supporting Evidence: PMID:10531035 In fact, F-box proteins are one of the four subunits of ubiquitin protein ligases called SCFs.
GO:0004842 ubiquitin-protein transferase activity	TAS PMID:10531035 Identification of a family of human F-box proteins.	MODIFY	Summary: Family-level author statement assigning ubiquitin-protein transferase activity to F-box-containing SCF ligases. FBXO7 is the substrate-recognition adaptor, not the catalytic transferase (the catalytic RING is RBX1). Reason: FBXO7 itself is not the ubiquitin transferase; it is the substrate-recognition adaptor of the SCF complex. The catalytic transfer is performed by the E2 recruited by the RBX1 RING. The informative molecular function is the ligase-substrate adaptor activity. Proposed replacements: ubiquitin-like ligase-substrate adaptor activity Supporting Evidence: PMID:36646384 FBXO7 is an adaptor protein in the SKP1-Cullin-1-F-box (SCF) E3 ligase complex that facilitates the ubiquitination of substrates.
GO:0006511 ubiquitin-dependent protein catabolic process	TAS PMID:10531035 Identification of a family of human F-box proteins.	KEEP AS NON CORE	Summary: Family-level author statement that F-box/SCF proteins drive controlled degradation of cellular regulatory proteins. Generic parent of the specific SCF-dependent process. Reason: Correct but generic; the specific GO:0031146 (SCF-dependent proteasomal catabolic process) better captures FBXO7's role. Supporting Evidence: PMID:10531035 Some F-box proteins have been shown to be critical for the controlled degradation of cellular regulatory proteins

Gene Description

Existing Annotations Review

Core Functions

Negative regulator of canonical NF-kappa-B signaling, achieved by SCF(FBXO7)-mediated K48/K63 polyubiquitination and proteasomal degradation of the NF-kappa-B cofactor UXT isoform 2 (and ubiquitination of TRAF2 and cIAP1/BIRC2).

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