RBX1 (ROC1, RNF75) is a 108-residue RING-H2 protein that forms the catalytic subunit of most human cullin-RING ubiquitin ligases (CRLs). Its N-terminal strand pairs with the C-terminal domain of a cullin through an intermolecular beta-sheet, while its cross-braced RING domain, which coordinates two structural zinc ions (a third is seen in SCF structures), binds a modifier-charged E2 enzyme and holds it in the closed, transfer-competent conformation. RBX1 forms no thioester of its own: ubiquitin passes directly from the E2 (CDC34/UBE2R, UBE2D) to a lysine on a substrate that a variable receptor module has recruited at the far end of the cullin, roughly 100 A away. The same RING also acts in the NEDD8 pathway, where RBX1 binds UBE2M/UBC12~NEDD8 - assisted by DCN-type co-E3s (DCUN1D1-5) - and rotates to neddylate the conserved cullin lysine, the modification that activates the ligase and blocks CAND1 binding; the paralogue RBX2/RNF7 performs the equivalent reaction with UBE2F for CUL5. RBX1 is therefore shared by CRL1/SCF (with SKP1 and about 70 F-box proteins), CRL2 (elongin BC with VHL-box receptors), CRL3 (BTB proteins such as KEAP1, SPOP, KLHL and KCTD family members), CRL4A/B (DDB1 with DCAFs) and the CUL7-FBXW8 and hexameric CUL9 assemblies, and substrate choice resides in these receptors rather than in RBX1 itself. Its outputs are correspondingly broad: mainly K48-linked chains that commit substrates to the proteasome (p27/CDKN1B via SCF(SKP2) at the G1/S transition, IkappaB-alpha, beta-catenin and DEPTOR via SCF(beta-TrCP), c-Myc and NOTCH via SCF(FBXW7), CDT1 and p21 via CRL4(CDT2), NRF2 via CUL3-KEAP1, HIF-alpha via CRL2(VHL), RNA polymerase II subunits via CRL3(ARMC5) and CRL4(CSA)), but also monoubiquitination (SEC31, PCNA) and K63- or K27-linked signals. RBX1 acts in both nucleus and cytosol, with its effective location set by the assembled ligase, and it is essential: mouse Rbx1 disruption causes p27 accumulation, hypoproliferation and early embryonic lethality that deleting p27 only partly delays.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000082 G1/S transition of mitotic cell cycle | NAS PMID:11961546 Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin liga... | ACCEPT | Summary: Through SCF(SKP2), which degrades Thr187-phosphorylated p27/CDKN1B, and through CRL1/CRL4 turnover of CDT1, p21 and E2F1, RBX1 is required for the G1/S transition; mouse Rbx1 disruption accumulates p27 and causes early embryonic lethality with hypoproliferation. Reason: Core process: RBX1 performs the ubiquitin-transfer step of the p27 degradation switch, and the genetic evidence shows the requirement is not redundant with RBX2. Supporting Evidence: PMID:11961546 Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0000109 nucleotide-excision repair complex | IPI PMID:22118460 The molecular basis of CRL4DDB2/CSA ubiquitin ligase archite... | MODIFY | Summary: IPI row from the CRL4(DDB2)/CRL4(CSA) architecture study; the RBX1-containing entity characterised there is the DDB1-DDB2-CUL4A/B-RBX1 ubiquitin ligase, which acts in nucleotide-excision repair. Reason: The complex RBX1 belongs to is the Cul4A-RING ligase (GO:0031464, annotated from the same paper), not the NER incision machinery that 'nucleotide-excision repair complex' denotes; CRL4(DDB2) delivers ubiquitin to chromatin at the lesion and is regulated by the CSN, but it is not a subcomplex of the repair machinery itself. Proposed replacements: Cul4A-RING E3 ubiquitin ligase complex Supporting Evidence: PMID:22118460 The DDB1-CUL4-RBX1 (CRL4) ubiquitin ligase family regulates a diverse set of cellular pathways through dedicated substrate receptors (DCAFs). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0000122 negative regulation of transcription by RNA polymerase II | NAS PMID:28591624 Crystal Structure of the Cul2-Rbx1-EloBC-VHL Ubiquitin Ligas... | MARK AS OVER ANNOTATED | Summary: Author statement from the CRL2(VHL) crystal-structure paper. Reason: Over-annotation: the paper establishes complex architecture, not a role for RBX1 in repressing Pol II transcription. The CRL2 complex membership from the same reference is the supportable claim. Supporting Evidence: PMID:28591624 Crystal Structure of the Cul2-Rbx1-EloBC-VHL Ubiquitin Ligase Complex. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0000165 MAPK cascade | TAS Reactome:R-HSA-5673001 | MARK AS OVER ANNOTATED | Summary: Reactome places RBX1-containing ligases in the RAF/MAP kinase cascade pathway. Reason: Over-annotation: RBX1 does not transduce the cascade; it ubiquitinates substrates whose turnover impinges on it. The direct events are already annotated as ubiquitination and CRL-dependent proteolysis. Supporting Evidence: Reactome:R-HSA-5673001 The RAS-RAF-MEK-ERK pathway regulates processes such as proliferation, differentiation, survival, senescence and cell motility in response to growth factors, hormones and cytokines, among others. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0000209 protein polyubiquitination | IDA PMID:14528312 Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubi... | ACCEPT | Summary: BTB-CUL3-ROC1 ligases assembled in vitro build polyubiquitin chains on receptor-bound substrates such as MEI-1/katanin. Reason: Core process: polyubiquitination is the characteristic output of RBX1-containing CRLs, and RBX1 performs the transfer step. Supporting Evidence: PMID:14528312 Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin ligases. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0004842 ubiquitin-protein transferase activity | IDA PMID:15983046 Ubiquitination of Keap1, a BTB-Kelch substrate adaptor prote... | ACCEPT | Summary: RBX1 supplies the RING activity that transfers ubiquitin from a charged E2 onto CRL-recruited substrates; the annotation is the parent of the more precise ubiquitin protein ligase activity (GO:0061630) also annotated here. Reason: Correct, if one step broader than GO:0061630: RBX1 does not form a ubiquitin thioester itself but activates the E2~ubiquitin conjugate for direct transfer, which is what ubiquitin-protein transferase activity denotes. The contributes_to qualifier on the IDA rows is appropriate for a subunit that is catalytic only within an assembled cullin-RING complex. Supporting Evidence: PMID:15983046 Keap1 is a BTB-Kelch protein that functions as a substrate adaptor protein for a Cul3-dependent E3 ubiquitin ligase complex. file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0004842 ubiquitin-protein transferase activity | IDA PMID:20389280 The Cullin 3 substrate adaptor KLHL20 mediates DAPK ubiquiti... | ACCEPT | Summary: RBX1 supplies the RING activity that transfers ubiquitin from a charged E2 onto CRL-recruited substrates; the annotation is the parent of the more precise ubiquitin protein ligase activity (GO:0061630) also annotated here. Reason: Correct, if one step broader than GO:0061630: RBX1 does not form a ubiquitin thioester itself but activates the E2~ubiquitin conjugate for direct transfer, which is what ubiquitin-protein transferase activity denotes. The contributes_to qualifier on the IDA rows is appropriate for a subunit that is catalytic only within an assembled cullin-RING complex. Supporting Evidence: PMID:20389280 The KLHL20-Cul3-ROC1 E3 ligase complex promotes DAPK polyubiquitination, thereby inducing the proteasomal degradation of DAPK. file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0004842 ubiquitin-protein transferase activity | IEA GO_REF:0000117 | ACCEPT | Summary: RBX1 supplies the RING activity that transfers ubiquitin from a charged E2 onto CRL-recruited substrates; the annotation is the parent of the more precise ubiquitin protein ligase activity (GO:0061630) also annotated here. Reason: Correct, if one step broader than GO:0061630: RBX1 does not form a ubiquitin thioester itself but activates the E2~ubiquitin conjugate for direct transfer, which is what ubiquitin-protein transferase activity denotes. The contributes_to qualifier on the IDA rows is appropriate for a subunit that is catalytic only within an assembled cullin-RING complex. Supporting Evidence: file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0004842 ubiquitin-protein transferase activity | TAS Reactome:R-HSA-69598 | ACCEPT | Summary: RBX1 supplies the RING activity that transfers ubiquitin from a charged E2 onto CRL-recruited substrates; the annotation is the parent of the more precise ubiquitin protein ligase activity (GO:0061630) also annotated here. Reason: Correct, if one step broader than GO:0061630: RBX1 does not form a ubiquitin thioester itself but activates the E2~ubiquitin conjugate for direct transfer, which is what ubiquitin-protein transferase activity denotes. The contributes_to qualifier on the IDA rows is appropriate for a subunit that is catalytic only within an assembled cullin-RING complex. Supporting Evidence: Reactome:R-HSA-69598 <p>Exposure of various human cell lines to ultraviolet (UV) light leads to rapid appearance of polyubiquitinated CDC25A (PolyUb-CDC25A) (Mailand et al. 2000). file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:11961546 Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin liga... | MODIFY | Summary: IPI row recording the interaction of RBX1 with CUL1. Reason: RBX1's binding to cullin C-terminal domains is exactly what cullin family protein binding (GO:0097602) denotes, and that term is already supported by IDA and by PAINT inference; the generic protein-binding row should be replaced by it rather than removed, because the specific function is established. Proposed replacements: cullin family protein binding Supporting Evidence: PMID:11961546 Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:12504026 CAND1 binds to unneddylated CUL1 and regulates the formation... | MODIFY | Summary: IPI row recording the interaction of RBX1 with CUL1. Reason: RBX1's binding to cullin C-terminal domains is exactly what cullin family protein binding (GO:0097602) denotes, and that term is already supported by IDA and by PAINT inference; the generic protein-binding row should be replaced by it rather than removed, because the specific function is established. Proposed replacements: cullin family protein binding Supporting Evidence: PMID:12504026 We found the majority of CUL1 is in a complex with CAND1 and ROC1 independent of SKP1 and F box protein SKP2. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:12609982 TIP120A associates with cullins and modulates ubiquitin liga... | MODIFY | Summary: IPI row recording the interaction of RBX1 with CUL1. Reason: RBX1's binding to cullin C-terminal domains is exactly what cullin family protein binding (GO:0097602) denotes, and that term is already supported by IDA and by PAINT inference; the generic protein-binding row should be replaced by it rather than removed, because the specific function is established. Proposed replacements: cullin family protein binding Supporting Evidence: PMID:12609982 TIP120A formed a complex with CUL1 and Rbx1, but interfered with the binding of Skp1 and F-box proteins to CUL1. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:12609982 TIP120A associates with cullins and modulates ubiquitin liga... | MODIFY | Summary: IPI row recording the interaction of RBX1 with CUL4B. Reason: RBX1's binding to cullin C-terminal domains is exactly what cullin family protein binding (GO:0097602) denotes, and that term is already supported by IDA and by PAINT inference; the generic protein-binding row should be replaced by it rather than removed, because the specific function is established. Proposed replacements: cullin family protein binding Supporting Evidence: PMID:12609982 TIP120A formed a complex with CUL1 and Rbx1, but interfered with the binding of Skp1 and F-box proteins to CUL1. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:15601820 VHL-box and SOCS-box domains determine binding specificity f... | MODIFY | Summary: IPI row recording the interaction of RBX1 with CUL2. Reason: RBX1's binding to cullin C-terminal domains is exactly what cullin family protein binding (GO:0097602) denotes, and that term is already supported by IDA and by PAINT inference; the generic protein-binding row should be replaced by it rather than removed, because the specific function is established. Proposed replacements: cullin family protein binding Supporting Evidence: PMID:15601820 VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:17183367 COMMD1 promotes the ubiquitination of NF-kappaB subunits thr... | MODIFY | Summary: IPI row recording the interaction of RBX1 with CUL2. Reason: RBX1's binding to cullin C-terminal domains is exactly what cullin family protein binding (GO:0097602) denotes, and that term is already supported by IDA and by PAINT inference; the generic protein-binding row should be replaced by it rather than removed, because the specific function is established. Proposed replacements: cullin family protein binding Supporting Evidence: PMID:17183367 COMMD1 promotes the ubiquitination of NF-kappaB subunits through a cullin-containing ubiquitin ligase. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:17543862 A Cul3-based E3 ligase removes Aurora B from mitotic chromos... | MODIFY | Summary: IPI row recording the interaction of RBX1 with CUL3. Reason: RBX1's binding to cullin C-terminal domains is exactly what cullin family protein binding (GO:0097602) denotes, and that term is already supported by IDA and by PAINT inference; the generic protein-binding row should be replaced by it rather than removed, because the specific function is established. Proposed replacements: cullin family protein binding Supporting Evidence: PMID:17543862 Moreover, Aurora B is ubiquitylated in a Cul3-dependent manner in vivo, and by reconstituted Cul3/KLHL9/KLHL13 ligase in vitro. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:18239684 Phosphorylation of Skp2 regulated by CDK2 and Cdc14B protect... | REMOVE | Summary: IPI row pairing RBX1 with SKP2 in a study of how CDK2/Cdc14B phosphorylation protects SKP2 from APC(Cdh1). Reason: SKP2 joins the SCF through SKP1 and the CUL1 N-terminus, not through RBX1, and this paper characterises SKP2 stability rather than an RBX1 activity. The supportable statements (SCF complex membership, SCF-dependent proteolysis) are annotated from other references. Per repository policy for bare GO:0005515 rows, this records that the generic term is uninformative, not that the reported interaction is false. Supporting Evidence: PMID:18239684 The activity of SCF(Skp2) is regulated by the APC(Cdh1), which targets Skp2 for degradation. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0005515 protein binding | IPI PMID:18805092 Structural insights into NEDD8 activation of cullin-RING lig... | MODIFY | Summary: IPI row recording the interaction of RBX1 with CUL1. Reason: RBX1's binding to cullin C-terminal domains is exactly what cullin family protein binding (GO:0097602) denotes, and that term is already supported by IDA and by PAINT inference; the generic protein-binding row should be replaced by it rather than removed, because the specific function is established. Proposed replacements: cullin family protein binding Supporting Evidence: PMID:18805092 Second, in a model of Rbx1 bound to a ubiquitin E2, a predicted ~60Γ
gap between an E2βs Cys and the substrate binding site raises the question of how ubiquitin is transferred to targets. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:18805092 Structural insights into NEDD8 activation of cullin-RING lig... | MODIFY | Summary: IPI row recording the interaction of RBX1 with CUL5. Reason: RBX1's binding to cullin C-terminal domains is exactly what cullin family protein binding (GO:0097602) denotes, and that term is already supported by IDA and by PAINT inference; the generic protein-binding row should be replaced by it rather than removed, because the specific function is established. Proposed replacements: cullin family protein binding Supporting Evidence: PMID:18805092 Second, in a model of Rbx1 bound to a ubiquitin E2, a predicted ~60Γ
gap between an E2βs Cys and the substrate binding site raises the question of how ubiquitin is transferred to targets. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:18826954 SCCRO (DCUN1D1) is an essential component of the E3 complex ... | MODIFY | Summary: RBX1 binds the DCN-type (DCUN1D/SCCRO) neddylation co-E3 proteins (DCUN1D1), which deliver UBE2M~NEDD8 to the cullin-RBX1 module. Reason: These interactions define a bipartite NEDD8 E3 in which the DCNL protein positions UBE2M~NEDD8 and RBX1 provides the RING that catalyses transfer to the cullin; NEDD8 ligase activity (GO:0061663) is the informative function behind the interaction, whereas bare protein binding is not. Proposed replacements: NEDD8 ligase activity Supporting Evidence: PMID:18826954 In contrast to findings in cellular systems where no binding is seen, we show that SCCRO and CAND1 can bind to the neddylated Cul1-ROC1 complex in assays using purified recombinant proteins. file:human/RBX1/RBX1-uniprot.txt Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 also works with UBE2M~NEDD8 to neddylate cullins and activate CRLs. |
| GO:0005515 protein binding | IPI PMID:19250909 E2-RING expansion of the NEDD8 cascade confers specificity t... | MODIFY | Summary: IPI row recording the interaction of RBX1 with the NEDD8-conjugating E2 UBE2M/UBC12. Reason: The informative function is engagement of the charged E2: RBX1 binds UBE2M~NEDD8 and rotates its RING to position the E2 next to the cullin acceptor lysine. Ubiquitin conjugating enzyme binding (GO:0031624) captures this; the catalytic consequence is annotated as NEDD8 transferase/ligase activity. Proposed replacements: ubiquitin conjugating enzyme binding Supporting Evidence: PMID:19250909 The largest ubiquitin E3 subclass consists of cullin-RING ligases (CRLs), which contain one each of several cullins (CUL1, -2, -3, -4, or -5) and RING proteins (RBX1 or -2). file:human/RBX1/RBX1-uniprot.txt Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 also works with UBE2M~NEDD8 to neddylate cullins and activate CRLs. |
| GO:0005515 protein binding | IPI PMID:19327355 Requirement for microtubule integrity in the SOCS1-mediated ... | MODIFY | Summary: IPI row recording the interaction of RBX1 with CUL2. Reason: RBX1's binding to cullin C-terminal domains is exactly what cullin family protein binding (GO:0097602) denotes, and that term is already supported by IDA and by PAINT inference; the generic protein-binding row should be replaced by it rather than removed, because the specific function is established. Proposed replacements: cullin family protein binding Supporting Evidence: PMID:19327355 SOCS1 facilitates Gag ubiquitination and the co-expression of a dominant-negative ubiquitin significantly inhibits the association of Gag with microtubules. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:19549727 Analysis of the human E2 ubiquitin conjugating enzyme protei... | REMOVE | Summary: Generic protein-binding row recording RBX1 with UBE2M, from a systematic yeast two-hybrid map of E2/E3-RING pairs. Reason: The source is a systematic, proteome-scale interaction screen and 'protein binding' conveys no functional information about RBX1. Its informative binding activities - cullin family protein binding (GO:0097602) and engagement of ubiquitin-charged E2s - are annotated from focused studies. Per repository policy for bare GO:0005515 rows, this records that the generic term is uninformative, not that the reported interaction is false. Supporting Evidence: PMID:19549727 Analysis of the human E2 ubiquitin conjugating enzyme protein interaction network. file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:20399188 Structural insights into the COP9 signalosome and its common... | MODIFY | Summary: IPI row recording the interaction of RBX1 with CUL1. Reason: RBX1's binding to cullin C-terminal domains is exactly what cullin family protein binding (GO:0097602) denotes, and that term is already supported by IDA and by PAINT inference; the generic protein-binding row should be replaced by it rather than removed, because the specific function is established. Proposed replacements: cullin family protein binding Supporting Evidence: PMID:20399188 Structural insights into the COP9 signalosome and its common architecture with the 26S proteasome lid and eIF3. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:21765416 A RING E3-substrate complex poised for ubiquitin-like protei... | MODIFY | Summary: IPI row recording the interaction of RBX1 with the NEDD8-conjugating E2 UBE2M/UBC12. Reason: The informative function is engagement of the charged E2: RBX1 binds UBE2M~NEDD8 and rotates its RING to position the E2 next to the cullin acceptor lysine. Ubiquitin conjugating enzyme binding (GO:0031624) captures this; the catalytic consequence is annotated as NEDD8 transferase/ligase activity. Proposed replacements: ubiquitin conjugating enzyme binding Supporting Evidence: PMID:21765416 The NEDD8-modified CUL1 assembles with SKP1βF-box proteinβsubstrate, RBX1 binds a ubiquitin-charged E2 such as UBCH5 or CDC34, and ubiquitin is ligated to a substrate15,16. file:human/RBX1/RBX1-uniprot.txt Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 also works with UBE2M~NEDD8 to neddylate cullins and activate CRLs. |
| GO:0005515 protein binding | IPI PMID:21765416 A RING E3-substrate complex poised for ubiquitin-like protei... | MODIFY | Summary: IPI row recording the interaction of RBX1 with CUL1. Reason: RBX1's binding to cullin C-terminal domains is exactly what cullin family protein binding (GO:0097602) denotes, and that term is already supported by IDA and by PAINT inference; the generic protein-binding row should be replaced by it rather than removed, because the specific function is established. Proposed replacements: cullin family protein binding Supporting Evidence: PMID:21765416 The NEDD8-modified CUL1 assembles with SKP1βF-box proteinβsubstrate, RBX1 binds a ubiquitin-charged E2 such as UBCH5 or CDC34, and ubiquitin is ligated to a substrate15,16. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:22660580 F-box protein FBXL19-mediated ubiquitination and degradation... | MODIFY | Summary: IPI row recording the interaction of RBX1 with CUL1. Reason: RBX1's binding to cullin C-terminal domains is exactly what cullin family protein binding (GO:0097602) denotes, and that term is already supported by IDA and by PAINT inference; the generic protein-binding row should be replaced by it rather than removed, because the specific function is established. Proposed replacements: cullin family protein binding Supporting Evidence: PMID:22660580 Three enzyme complexes (E1, E2 and E3) are involved in linking ubiquitin chains onto target proteins25. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:23238014 CRL4B catalyzes H2AK119 monoubiquitination and coordinates w... | MODIFY | Summary: IPI row recording the interaction of RBX1 with CUL4B. Reason: RBX1's binding to cullin C-terminal domains is exactly what cullin family protein binding (GO:0097602) denotes, and that term is already supported by IDA and by PAINT inference; the generic protein-binding row should be replaced by it rather than removed, because the specific function is established. Proposed replacements: cullin family protein binding Supporting Evidence: PMID:23238014 CRL4B catalyzes H2AK119 monoubiquitination and coordinates with PRC2 to promote tumorigenesis. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:23274085 Sestrins activate Nrf2 by promoting p62-dependent autophagic... | REMOVE | Summary: IPI row recording RBX1 (Rbx1) among the proteins that sestrin-1/2 associate with, alongside KEAP1 and p62. Reason: The mechanism established here is p62-dependent autophagic degradation of KEAP1, with the sestrins as the adaptors; the RBX1 contact is incidental and 'protein binding' states nothing about RBX1 function. Per repository policy for bare GO:0005515 rows, this records that the generic term is uninformative, not that the reported interaction is false. Supporting Evidence: PMID:23274085 We now show that Sesn1 and Sesn2 interact with the Nrf2 suppressor Keap1, the autophagy substrate p62, and the ubiquitin ligase Rbx1 and that the antioxidant function of Sesns is mediated through activation of Nrf2 in a manner reliant on p62-dependent autophagic degradation of Keap1. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 supplies catalytic E2 recruitment but ordinarily does **not** select protein substrates by itself. |
| GO:0005515 protein binding | IPI PMID:23401859 DCNL1 functions as a substrate sensor and activator of culli... | MODIFY | Summary: Co-purification of RBX1 with the CRL2/ECV components VHL, CUL2: DCNL1 senses substrate engagement by VHL and triggers CUL2 neddylation. Reason: The interaction recorded is membership of the elongin BC-CUL2-VHL (ECV/CRL2) ligase, which is informative, whereas 'protein binding' is not; HIF1A/EPAS1 appear as the substrates recruited by VHL, not as RBX1-binding partners. Proposed replacements: Cul2-RING ubiquitin ligase complex Supporting Evidence: PMID:23401859 Substrate engagement by F-box proteins promotes NEDD8 modification of cullins, which is necessary for the activation of cullin-RING E3 ubiquitin ligases (CRLs). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0005515 protein binding | IPI PMID:23401859 DCNL1 functions as a substrate sensor and activator of culli... | MODIFY | Summary: Co-purification of RBX1 with the CRL2/ECV components VHL, CUL2, ELOB, HIF1A: DCNL1 senses substrate engagement by VHL and triggers CUL2 neddylation. Reason: The interaction recorded is membership of the elongin BC-CUL2-VHL (ECV/CRL2) ligase, which is informative, whereas 'protein binding' is not; HIF1A/EPAS1 appear as the substrates recruited by VHL, not as RBX1-binding partners. Proposed replacements: Cul2-RING ubiquitin ligase complex Supporting Evidence: PMID:23401859 Substrate engagement by F-box proteins promotes NEDD8 modification of cullins, which is necessary for the activation of cullin-RING E3 ubiquitin ligases (CRLs). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0005515 protein binding | IPI PMID:23401859 DCNL1 functions as a substrate sensor and activator of culli... | MODIFY | Summary: Co-purification of RBX1 with the CRL2/ECV components VHL, CUL2, HIF1A: DCNL1 senses substrate engagement by VHL and triggers CUL2 neddylation. Reason: The interaction recorded is membership of the elongin BC-CUL2-VHL (ECV/CRL2) ligase, which is informative, whereas 'protein binding' is not; HIF1A/EPAS1 appear as the substrates recruited by VHL, not as RBX1-binding partners. Proposed replacements: Cul2-RING ubiquitin ligase complex Supporting Evidence: PMID:23401859 Substrate engagement by F-box proteins promotes NEDD8 modification of cullins, which is necessary for the activation of cullin-RING E3 ubiquitin ligases (CRLs). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0005515 protein binding | IPI PMID:23401859 DCNL1 functions as a substrate sensor and activator of culli... | MODIFY | Summary: Co-purification of RBX1 with the CRL2/ECV components VHL, CUL2, EPAS1: DCNL1 senses substrate engagement by VHL and triggers CUL2 neddylation. Reason: The interaction recorded is membership of the elongin BC-CUL2-VHL (ECV/CRL2) ligase, which is informative, whereas 'protein binding' is not; HIF1A/EPAS1 appear as the substrates recruited by VHL, not as RBX1-binding partners. Proposed replacements: Cul2-RING ubiquitin ligase complex Supporting Evidence: PMID:23401859 Substrate engagement by F-box proteins promotes NEDD8 modification of cullins, which is necessary for the activation of cullin-RING E3 ubiquitin ligases (CRLs). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0005515 protein binding | IPI PMID:23401859 DCNL1 functions as a substrate sensor and activator of culli... | MODIFY | Summary: IPI row recording the interaction of RBX1 with CUL2. Reason: RBX1's binding to cullin C-terminal domains is exactly what cullin family protein binding (GO:0097602) denotes, and that term is already supported by IDA and by PAINT inference; the generic protein-binding row should be replaced by it rather than removed, because the specific function is established. Proposed replacements: cullin family protein binding Supporting Evidence: PMID:23401859 Substrate engagement by F-box proteins promotes NEDD8 modification of cullins, which is necessary for the activation of cullin-RING E3 ubiquitin ligases (CRLs). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:24192928 Oncogenic function of SCCRO5/DCUN1D5 requires its Neddylatio... | MODIFY | Summary: RBX1 binds the DCN-type (DCUN1D/SCCRO) neddylation co-E3 proteins (DCUN1D1), which deliver UBE2M~NEDD8 to the cullin-RBX1 module. Reason: These interactions define a bipartite NEDD8 E3 in which the DCNL protein positions UBE2M~NEDD8 and RBX1 provides the RING that catalyses transfer to the cullin; NEDD8 ligase activity (GO:0061663) is the informative function behind the interaction, whereas bare protein binding is not. Proposed replacements: NEDD8 ligase activity Supporting Evidence: PMID:24192928 Our previous work showed that SCCRO promotes nuclear translocation of Cullin-ROC1, which is required for neddylation in vivo. file:human/RBX1/RBX1-uniprot.txt Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 also works with UBE2M~NEDD8 to neddylate cullins and activate CRLs. |
| GO:0005515 protein binding | IPI PMID:24192928 Oncogenic function of SCCRO5/DCUN1D5 requires its Neddylatio... | MODIFY | Summary: RBX1 binds the DCN-type (DCUN1D/SCCRO) neddylation co-E3 proteins (DCUN1D5), which deliver UBE2M~NEDD8 to the cullin-RBX1 module. Reason: These interactions define a bipartite NEDD8 E3 in which the DCNL protein positions UBE2M~NEDD8 and RBX1 provides the RING that catalyses transfer to the cullin; NEDD8 ligase activity (GO:0061663) is the informative function behind the interaction, whereas bare protein binding is not. Proposed replacements: NEDD8 ligase activity Supporting Evidence: PMID:24192928 Our previous work showed that SCCRO promotes nuclear translocation of Cullin-ROC1, which is required for neddylation in vivo. file:human/RBX1/RBX1-uniprot.txt Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 also works with UBE2M~NEDD8 to neddylate cullins and activate CRLs. |
| GO:0005515 protein binding | IPI PMID:24793696 CUL9 mediates the functions of the 3M complex and ubiquityla... | MODIFY | Summary: IPI row recording the interaction of RBX1 with CUL9. Reason: RBX1's binding to cullin C-terminal domains is exactly what cullin family protein binding (GO:0097602) denotes, and that term is already supported by IDA and by PAINT inference; the generic protein-binding row should be replaced by it rather than removed, because the specific function is established. Proposed replacements: cullin family protein binding Supporting Evidence: PMID:24793696 Together, these results indicate that ROC1 mediates CUL7-CUL9 heterodimerization. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:24949976 Structure of a RING E3 trapped in action reveals ligation me... | MODIFY | Summary: IPI row recording the interaction of RBX1 with CUL1. Reason: RBX1's binding to cullin C-terminal domains is exactly what cullin family protein binding (GO:0097602) denotes, and that term is already supported by IDA and by PAINT inference; the generic protein-binding row should be replaced by it rather than removed, because the specific function is established. Proposed replacements: cullin family protein binding Supporting Evidence: PMID:24949976 Nonetheless, RING E3 mechanisms matching a specific UBL and acceptor lysine remain elusive, including for RBX1, which mediates NEDD8 ligation to cullins and >10% of all ubiquitination. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:25619834 KLHL39 suppresses colon cancer metastasis by blocking KLHL20... | MODIFY | Summary: IPI row recording the interaction of RBX1 with CUL3. Reason: RBX1's binding to cullin C-terminal domains is exactly what cullin family protein binding (GO:0097602) denotes, and that term is already supported by IDA and by PAINT inference; the generic protein-binding row should be replaced by it rather than removed, because the specific function is established. Proposed replacements: cullin family protein binding Supporting Evidence: PMID:25619834 Instead, KLHL39 blocks KLHL20-mediated ubiquitination of PML and DAPK by disrupting the binding of these substrates to KLHL20 as well as the binding of KLHL20 to Cul3. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:25684205 CUL3-KBTBD6/KBTBD7 ubiquitin ligase cooperates with GABARAP ... | MODIFY | Summary: RBX1 co-purifies with the BTB adaptors KBTBD6 in the CUL3-KBTBD6/KBTBD7 ligase that degrades TIAM1. Reason: The evidence supports membership of a Cul3-RING ligase complex (GO:0031463, also annotated from this paper), which is informative; bare protein binding is not, and the BTB proteins bind CUL3 rather than RBX1. Proposed replacements: Cul3-RING ubiquitin ligase complex Supporting Evidence: PMID:25684205 CUL3-KBTBD6/KBTBD7 ubiquitin ligase cooperates with GABARAP proteins to spatially restrict TIAM1-RAC1 signaling. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0005515 protein binding | IPI PMID:25684205 CUL3-KBTBD6/KBTBD7 ubiquitin ligase cooperates with GABARAP ... | MODIFY | Summary: RBX1 co-purifies with the BTB adaptors KBTBD7 in the CUL3-KBTBD6/KBTBD7 ligase that degrades TIAM1. Reason: The evidence supports membership of a Cul3-RING ligase complex (GO:0031463, also annotated from this paper), which is informative; bare protein binding is not, and the BTB proteins bind CUL3 rather than RBX1. Proposed replacements: Cul3-RING ubiquitin ligase complex Supporting Evidence: PMID:25684205 CUL3-KBTBD6/KBTBD7 ubiquitin ligase cooperates with GABARAP proteins to spatially restrict TIAM1-RAC1 signaling. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | REMOVE | Summary: Generic protein-binding row recording RBX1 with CUL4B, from a quantitative proteome-wide interactome survey. Reason: The source is a systematic, proteome-scale interaction screen and 'protein binding' conveys no functional information about RBX1. Its informative binding activities - cullin family protein binding (GO:0097602) and engagement of ubiquitin-charged E2s - are annotated from focused studies. Per repository policy for bare GO:0005515 rows, this records that the generic term is uninformative, not that the reported interaction is false. Supporting Evidence: PMID:26496610 A human interactome in three quantitative dimensions organized by stoichiometries and abundances. file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:26906416 Characterization of the mammalian family of DCN-type NEDD8 E... | MODIFY | Summary: RBX1 binds the DCN-type (DCUN1D/SCCRO) neddylation co-E3 proteins (DCUN1D2), which deliver UBE2M~NEDD8 to the cullin-RBX1 module. Reason: These interactions define a bipartite NEDD8 E3 in which the DCNL protein positions UBE2M~NEDD8 and RBX1 provides the RING that catalyses transfer to the cullin; NEDD8 ligase activity (GO:0061663) is the informative function behind the interaction, whereas bare protein binding is not. Proposed replacements: NEDD8 ligase activity Supporting Evidence: PMID:26906416 Cullin-RING ligases (CRL) are ubiquitin E3 enzymes that bind substrates through variable substrate receptor proteins and are activated by attachment of the ubiquitin-like protein NEDD8 to the cullin subunit. file:human/RBX1/RBX1-uniprot.txt Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 also works with UBE2M~NEDD8 to neddylate cullins and activate CRLs. |
| GO:0005515 protein binding | IPI PMID:26906416 Characterization of the mammalian family of DCN-type NEDD8 E... | MODIFY | Summary: RBX1 binds the DCN-type (DCUN1D/SCCRO) neddylation co-E3 proteins (DCUN1D3), which deliver UBE2M~NEDD8 to the cullin-RBX1 module. Reason: These interactions define a bipartite NEDD8 E3 in which the DCNL protein positions UBE2M~NEDD8 and RBX1 provides the RING that catalyses transfer to the cullin; NEDD8 ligase activity (GO:0061663) is the informative function behind the interaction, whereas bare protein binding is not. Proposed replacements: NEDD8 ligase activity Supporting Evidence: PMID:26906416 Cullin-RING ligases (CRL) are ubiquitin E3 enzymes that bind substrates through variable substrate receptor proteins and are activated by attachment of the ubiquitin-like protein NEDD8 to the cullin subunit. file:human/RBX1/RBX1-uniprot.txt Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 also works with UBE2M~NEDD8 to neddylate cullins and activate CRLs. |
| GO:0005515 protein binding | IPI PMID:26906416 Characterization of the mammalian family of DCN-type NEDD8 E... | MODIFY | Summary: RBX1 binds the DCN-type (DCUN1D/SCCRO) neddylation co-E3 proteins (DCUN1D4), which deliver UBE2M~NEDD8 to the cullin-RBX1 module. Reason: These interactions define a bipartite NEDD8 E3 in which the DCNL protein positions UBE2M~NEDD8 and RBX1 provides the RING that catalyses transfer to the cullin; NEDD8 ligase activity (GO:0061663) is the informative function behind the interaction, whereas bare protein binding is not. Proposed replacements: NEDD8 ligase activity Supporting Evidence: PMID:26906416 Cullin-RING ligases (CRL) are ubiquitin E3 enzymes that bind substrates through variable substrate receptor proteins and are activated by attachment of the ubiquitin-like protein NEDD8 to the cullin subunit. file:human/RBX1/RBX1-uniprot.txt Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 also works with UBE2M~NEDD8 to neddylate cullins and activate CRLs. |
| GO:0005515 protein binding | IPI PMID:26906416 Characterization of the mammalian family of DCN-type NEDD8 E... | MODIFY | Summary: RBX1 binds the DCN-type (DCUN1D/SCCRO) neddylation co-E3 proteins (DCUN1D1), which deliver UBE2M~NEDD8 to the cullin-RBX1 module. Reason: These interactions define a bipartite NEDD8 E3 in which the DCNL protein positions UBE2M~NEDD8 and RBX1 provides the RING that catalyses transfer to the cullin; NEDD8 ligase activity (GO:0061663) is the informative function behind the interaction, whereas bare protein binding is not. Proposed replacements: NEDD8 ligase activity Supporting Evidence: PMID:26906416 Cullin-RING ligases (CRL) are ubiquitin E3 enzymes that bind substrates through variable substrate receptor proteins and are activated by attachment of the ubiquitin-like protein NEDD8 to the cullin subunit. file:human/RBX1/RBX1-uniprot.txt Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 also works with UBE2M~NEDD8 to neddylate cullins and activate CRLs. |
| GO:0005515 protein binding | IPI PMID:26906416 Characterization of the mammalian family of DCN-type NEDD8 E... | MODIFY | Summary: RBX1 binds the DCN-type (DCUN1D/SCCRO) neddylation co-E3 proteins (DCUN1D5), which deliver UBE2M~NEDD8 to the cullin-RBX1 module. Reason: These interactions define a bipartite NEDD8 E3 in which the DCNL protein positions UBE2M~NEDD8 and RBX1 provides the RING that catalyses transfer to the cullin; NEDD8 ligase activity (GO:0061663) is the informative function behind the interaction, whereas bare protein binding is not. Proposed replacements: NEDD8 ligase activity Supporting Evidence: PMID:26906416 Cullin-RING ligases (CRL) are ubiquitin E3 enzymes that bind substrates through variable substrate receptor proteins and are activated by attachment of the ubiquitin-like protein NEDD8 to the cullin subunit. file:human/RBX1/RBX1-uniprot.txt Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 also works with UBE2M~NEDD8 to neddylate cullins and activate CRLs. |
| GO:0005515 protein binding | IPI PMID:29149593 NOTCH2 Hajdu-Cheney Mutations Escape SCF(FBW7)-Dependent Pro... | MODIFY | Summary: RBX1 was found with SKP1, CUL1 and FBXW7 in the SCF(FBW7) complex that degrades NOTCH2; Hajdu-Cheney mutations let NOTCH2 escape it. Reason: The informative statement is that RBX1 is part of the SCF(FBW7) ligase (GO:0019005); NOTCH2 is the substrate, recruited by FBXW7 rather than by RBX1. Proposed replacements: SCF ubiquitin ligase complex Supporting Evidence: PMID:29149593 Furthermore, Skp1 and Rbx1, additional components of the SCF complex, also interacted with NOTCH2 in cells (Figures S1D and S1E). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0005515 protein binding | IPI PMID:29294217 RBX1-mediated ubiquitination of SESN2 promotes cell death up... | MODIFY | Summary: RBX1 was identified as an interacting partner and E3 ligase for sestrin-2, mediating its K48-linked ubiquitination after prolonged mitochondrial damage. Reason: The paper supports an informative molecular function rather than bare binding: RBX1 acts as the ubiquitin ligase for SESN2, so ubiquitin protein ligase activity (GO:0061630) is the term the evidence justifies. As always for RBX1 the substrate is presented by a cullin receptor module, so the specificity should not be read as intrinsic to RBX1. Proposed replacements: ubiquitin protein ligase activity Supporting Evidence: PMID:29294217 RBX1-mediated ubiquitination of SESN2 promotes cell death upon prolonged mitochondrial damage in SH-SY5Y neuroblastoma cells. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md RBX1 supplies catalytic E2 recruitment but ordinarily does **not** select protein substrates by itself. |
| GO:0005515 protein binding | IPI PMID:30945288 Inflammation-dependent overexpression of c-Myc enhances CRL4... | MODIFY | Summary: IPI row recording the interaction of RBX1 with CUL4B. Reason: RBX1's binding to cullin C-terminal domains is exactly what cullin family protein binding (GO:0097602) denotes, and that term is already supported by IDA and by PAINT inference; the generic protein-binding row should be replaced by it rather than removed, because the specific function is established. Proposed replacements: cullin family protein binding Supporting Evidence: PMID:30945288 Inflammation-dependent overexpression of c-Myc enhances CRL4(DCAF4) E3 ligase activity and promotes ubiquitination of ST7 in colitis-associated cancer. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein-binding row recording RBX1 with KRTAP12-2, from the HuRI binary interactome map. Reason: The source is a systematic, proteome-scale interaction screen and 'protein binding' conveys no functional information about RBX1. Its informative binding activities - cullin family protein binding (GO:0097602) and engagement of ubiquitin-charged E2s - are annotated from focused studies. Per repository policy for bare GO:0005515 rows, this records that the generic term is uninformative, not that the reported interaction is false. Supporting Evidence: PMID:32296183 A reference map of the human binary protein interactome. file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein-binding row recording RBX1 with UBE2M, from the HuRI binary interactome map. Reason: The source is a systematic, proteome-scale interaction screen and 'protein binding' conveys no functional information about RBX1. Its informative binding activities - cullin family protein binding (GO:0097602) and engagement of ubiquitin-charged E2s - are annotated from focused studies. Per repository policy for bare GO:0005515 rows, this records that the generic term is uninformative, not that the reported interaction is false. Supporting Evidence: PMID:32296183 A reference map of the human binary protein interactome. file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein-binding row recording RBX1 with CUL2, from the HuRI binary interactome map. Reason: The source is a systematic, proteome-scale interaction screen and 'protein binding' conveys no functional information about RBX1. Its informative binding activities - cullin family protein binding (GO:0097602) and engagement of ubiquitin-charged E2s - are annotated from focused studies. Per repository policy for bare GO:0005515 rows, this records that the generic term is uninformative, not that the reported interaction is false. Supporting Evidence: PMID:32296183 A reference map of the human binary protein interactome. file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein-binding row recording RBX1 with GLMN, from the HuRI binary interactome map. Reason: The source is a systematic, proteome-scale interaction screen and 'protein binding' conveys no functional information about RBX1. Its informative binding activities - cullin family protein binding (GO:0097602) and engagement of ubiquitin-charged E2s - are annotated from focused studies. Per repository policy for bare GO:0005515 rows, this records that the generic term is uninformative, not that the reported interaction is false. Supporting Evidence: PMID:32296183 A reference map of the human binary protein interactome. file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein-binding row recording RBX1 with PBX4, from the HuRI binary interactome map. Reason: The source is a systematic, proteome-scale interaction screen and 'protein binding' conveys no functional information about RBX1. Its informative binding activities - cullin family protein binding (GO:0097602) and engagement of ubiquitin-charged E2s - are annotated from focused studies. Per repository policy for bare GO:0005515 rows, this records that the generic term is uninformative, not that the reported interaction is false. Supporting Evidence: PMID:32296183 A reference map of the human binary protein interactome. file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:32726803 Papain-like protease regulates SARS-CoV-2 viral spread and i... | MODIFY | Summary: IPI row recording the interaction of RBX1 with CUL1. Reason: RBX1's binding to cullin C-terminal domains is exactly what cullin family protein binding (GO:0097602) denotes, and that term is already supported by IDA and by PAINT inference; the generic protein-binding row should be replaced by it rather than removed, because the specific function is established. Proposed replacements: cullin family protein binding Supporting Evidence: PMID:32726803 CUL1βRBX1, SKP1βΞ²-TRCP2, UBE2M, UBE2D3, NEDD8, UB, APPBP1βUBA3 and UBA1 were purified as previously described47. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:33692209 KDM2B Overexpression Facilitates Lytic De Novo KSHV Infectio... | MODIFY | Summary: IPI row recording the interaction of RBX1 with CUL1. Reason: RBX1's binding to cullin C-terminal domains is exactly what cullin family protein binding (GO:0097602) denotes, and that term is already supported by IDA and by PAINT inference; the generic protein-binding row should be replaced by it rather than removed, because the specific function is established. Proposed replacements: cullin family protein binding Supporting Evidence: PMID:33692209 CUL1 acts as the scaffold protein in the SCF complex recruiting ROC1, which is the E3 ubiquitin ligase component of SCF ( 22 ). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein-binding row recording RBX1 with SKP2, from the BioPlex proteome-scale affinity-purification network. Reason: The source is a systematic, proteome-scale interaction screen and 'protein binding' conveys no functional information about RBX1. Its informative binding activities - cullin family protein binding (GO:0097602) and engagement of ubiquitin-charged E2s - are annotated from focused studies. Per repository policy for bare GO:0005515 rows, this records that the generic term is uninformative, not that the reported interaction is false. Supporting Evidence: PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein-binding row recording RBX1 with CUL1, from the BioPlex proteome-scale affinity-purification network. Reason: The source is a systematic, proteome-scale interaction screen and 'protein binding' conveys no functional information about RBX1. Its informative binding activities - cullin family protein binding (GO:0097602) and engagement of ubiquitin-charged E2s - are annotated from focused studies. Per repository policy for bare GO:0005515 rows, this records that the generic term is uninformative, not that the reported interaction is false. Supporting Evidence: PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein-binding row recording RBX1 with CUL2, from the BioPlex proteome-scale affinity-purification network. Reason: The source is a systematic, proteome-scale interaction screen and 'protein binding' conveys no functional information about RBX1. Its informative binding activities - cullin family protein binding (GO:0097602) and engagement of ubiquitin-charged E2s - are annotated from focused studies. Per repository policy for bare GO:0005515 rows, this records that the generic term is uninformative, not that the reported interaction is false. Supporting Evidence: PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein-binding row recording RBX1 with CUL4B, from the BioPlex proteome-scale affinity-purification network. Reason: The source is a systematic, proteome-scale interaction screen and 'protein binding' conveys no functional information about RBX1. Its informative binding activities - cullin family protein binding (GO:0097602) and engagement of ubiquitin-charged E2s - are annotated from focused studies. Per repository policy for bare GO:0005515 rows, this records that the generic term is uninformative, not that the reported interaction is false. Supporting Evidence: PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein-binding row recording RBX1 with GLMN, from the BioPlex proteome-scale affinity-purification network. Reason: The source is a systematic, proteome-scale interaction screen and 'protein binding' conveys no functional information about RBX1. Its informative binding activities - cullin family protein binding (GO:0097602) and engagement of ubiquitin-charged E2s - are annotated from focused studies. Per repository policy for bare GO:0005515 rows, this records that the generic term is uninformative, not that the reported interaction is false. Supporting Evidence: PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:34591642 A protein network map of head and neck cancer reveals PIK3CA... | REMOVE | Summary: Generic protein-binding row recording RBX1 with CUL3, from a head-and-neck-cancer protein network map. Reason: The source is a systematic, proteome-scale interaction screen and 'protein binding' conveys no functional information about RBX1. Its informative binding activities - cullin family protein binding (GO:0097602) and engagement of ubiquitin-charged E2s - are annotated from focused studies. Per repository policy for bare GO:0005515 rows, this records that the generic term is uninformative, not that the reported interaction is false. Supporting Evidence: PMID:34591642 A protein network map of head and neck cancer reveals PIK3CA mutant drug sensitivity. file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005515 protein binding | IPI PMID:37788672 Cryo-EM structure of the KLHL22 E3 ligase bound to an oligom... | MODIFY | Summary: IPI row recording the interaction of RBX1 with CUL3. Reason: RBX1's binding to cullin C-terminal domains is exactly what cullin family protein binding (GO:0097602) denotes, and that term is already supported by IDA and by PAINT inference; the generic protein-binding row should be replaced by it rather than removed, because the specific function is established. Proposed replacements: cullin family protein binding Supporting Evidence: PMID:37788672 CULLIN3KLHL22-RBX1 ligase mediated the polyubiquitination of GDH1 in vitro. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0005634 nucleus | IBA GO_REF:0000033 | ACCEPT | Summary: RBX1 is present in the nucleus, where CRL1/CRL2/CRL3/CRL4 ligases act on nuclear substrates (p27, cyclin E, CDT1, NRF2, RNA Pol II subunits); ROC1 binding also promotes nuclear accumulation of CUL1. Reason: Well-supported nuclear pool: direct immunofluorescence/fractionation, curator inference from nuclear CRL substrates, the UniProt subcellular location, and a PAINT inference placed at the RING-box family node whose descendants (yeast Hrt1/Apc11, fly and mouse Rbx1, human RBX1) all act on nuclear substrates. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000129805 Β· PANTHER:PTN000129805 SUPPORTS TRANSFER RING-box family node spanning RBX1, RBX2/RNF7 and APC11; the descendant experimental evidence includes human RBX1 itself, mouse Rbx1, fly Roc1a/Roc1b and yeast Hrt1/Rbx1 and Apc11, so the function is inherited rather than lineage-specific. Supporting Evidence: file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005634 nucleus | IC PMID:11027288 The CUL1 C-terminal sequence and ROC1 are required for effic... | ACCEPT | Summary: RBX1 is present in the nucleus, where CRL1/CRL2/CRL3/CRL4 ligases act on nuclear substrates (p27, cyclin E, CDT1, NRF2, RNA Pol II subunits); ROC1 binding also promotes nuclear accumulation of CUL1. Reason: Well-supported nuclear pool: direct immunofluorescence/fractionation, curator inference from nuclear CRL substrates, the UniProt subcellular location, and a PAINT inference placed at the RING-box family node whose descendants (yeast Hrt1/Apc11, fly and mouse Rbx1, human RBX1) all act on nuclear substrates. Supporting Evidence: PMID:11027288 The CUL1 C-terminal sequence and ROC1 are required for efficient nuclear accumulation, NEDD8 modification, and ubiquitin ligase activity of CUL1. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005634 nucleus | IC PMID:20870715 HIV-1 Vpr loads uracil DNA glycosylase-2 onto DCAF1, a subst... | ACCEPT | Summary: RBX1 is present in the nucleus, where CRL1/CRL2/CRL3/CRL4 ligases act on nuclear substrates (p27, cyclin E, CDT1, NRF2, RNA Pol II subunits); ROC1 binding also promotes nuclear accumulation of CUL1. Reason: Well-supported nuclear pool: direct immunofluorescence/fractionation, curator inference from nuclear CRL substrates, the UniProt subcellular location, and a PAINT inference placed at the RING-box family node whose descendants (yeast Hrt1/Apc11, fly and mouse Rbx1, human RBX1) all act on nuclear substrates. Supporting Evidence: PMID:20870715 To date, three of the four HIV-1 accessory proteins, including Vpr, have been found to interact with cullin-RING finger E3 ubiquitin ligases (CRLs). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005634 nucleus | IC PMID:27626656 Hepatitis B Virus X Protein Promotes Degradation of SMC5/6 t... | ACCEPT | Summary: RBX1 is present in the nucleus, where CRL1/CRL2/CRL3/CRL4 ligases act on nuclear substrates (p27, cyclin E, CDT1, NRF2, RNA Pol II subunits); ROC1 binding also promotes nuclear accumulation of CUL1. Reason: Well-supported nuclear pool: direct immunofluorescence/fractionation, curator inference from nuclear CRL substrates, the UniProt subcellular location, and a PAINT inference placed at the RING-box family node whose descendants (yeast Hrt1/Apc11, fly and mouse Rbx1, human RBX1) all act on nuclear substrates. Supporting Evidence: PMID:27626656 These findings suggest that HBx may assemble an HBx-DDB1-CUL4-ROC1 E3 ligase complex (referred to as CRL4HBx hereafter) to target host proteins that antagonize HBV replication for ubiquitylation and degradation. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005634 nucleus | IDA PMID:11027288 The CUL1 C-terminal sequence and ROC1 are required for effic... | ACCEPT | Summary: RBX1 is present in the nucleus, where CRL1/CRL2/CRL3/CRL4 ligases act on nuclear substrates (p27, cyclin E, CDT1, NRF2, RNA Pol II subunits); ROC1 binding also promotes nuclear accumulation of CUL1. Reason: Well-supported nuclear pool: direct immunofluorescence/fractionation, curator inference from nuclear CRL substrates, the UniProt subcellular location, and a PAINT inference placed at the RING-box family node whose descendants (yeast Hrt1/Apc11, fly and mouse Rbx1, human RBX1) all act on nuclear substrates. Supporting Evidence: PMID:11027288 The CUL1 C-terminal sequence and ROC1 are required for efficient nuclear accumulation, NEDD8 modification, and ubiquitin ligase activity of CUL1. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005634 nucleus | IEA GO_REF:0000044 | ACCEPT | Summary: RBX1 is present in the nucleus, where CRL1/CRL2/CRL3/CRL4 ligases act on nuclear substrates (p27, cyclin E, CDT1, NRF2, RNA Pol II subunits); ROC1 binding also promotes nuclear accumulation of CUL1. Reason: Well-supported nuclear pool: direct immunofluorescence/fractionation, curator inference from nuclear CRL substrates, the UniProt subcellular location, and a PAINT inference placed at the RING-box family node whose descendants (yeast Hrt1/Apc11, fly and mouse Rbx1, human RBX1) all act on nuclear substrates. Supporting Evidence: file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005634 nucleus | NAS PMID:22118460 The molecular basis of CRL4DDB2/CSA ubiquitin ligase archite... | ACCEPT | Summary: RBX1 is present in the nucleus, where CRL1/CRL2/CRL3/CRL4 ligases act on nuclear substrates (p27, cyclin E, CDT1, NRF2, RNA Pol II subunits); ROC1 binding also promotes nuclear accumulation of CUL1. Reason: Well-supported nuclear pool: direct immunofluorescence/fractionation, curator inference from nuclear CRL substrates, the UniProt subcellular location, and a PAINT inference placed at the RING-box family node whose descendants (yeast Hrt1/Apc11, fly and mouse Rbx1, human RBX1) all act on nuclear substrates. Supporting Evidence: PMID:22118460 The DDB1-CUL4-RBX1 (CRL4) ubiquitin ligase family regulates a diverse set of cellular pathways through dedicated substrate receptors (DCAFs). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | IDA GO_REF:0000052 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-1234169 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-1234169 The VHL component of the VHL:ElonginB:ElonginC:CUL2:RBX1 binds HIF-alpha that have hydroxylated proline residues (Cockman et al. 2000, Ohh et al. 2000, Tanimoto et al. 2000, Jaakkola et al. 2001, Ivan et al. 2001, Yu et al. 2001, Bonicalzi et al. 2001). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-1234172 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-1234172 VHL is an E3 ubiquitin ligase that conjugates ubiquitin to hydroxylated HIF-alpha (Iwai et al. 1999, Kamura et al. 2000, Ohh et al. 2000, Groulx and Lee 2002, Maynard et al. 2003). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-1234175 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-1234175 When hypoxic cells return to normoxia, HIF-alpha is ubiquitinated in the nucleus and exported to the cytosol (Groulx and Lee 2002). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-2220967 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-2220967 As binding of WD40 repeats of FBXW7 requires conserved phosphodegron in the PEST domain of NICD1, especially phosphorylation of threonine residue T2511 and serine residue S2513, FBXW7 cannot bind NICD1 PEST domain mutants which lack the conserved phosphodegron due to truncation of the PEST domain, file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-2220978 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-2220978 FBXW7 (FBW7) mutations are found in ~20% of T-cell acute lymphoblastic leukemia samples. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5635854 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-5635854 SPOP:CUL3:RBX1-mediated ubiquitination of the transcriptionally active GLI proteins attenuates Hh-dependent signaling by promoting their degradation by the proteasome (Zhang et al, 2009; Chen et al, 2009; Humke et al, 2010; Tukachinsky et al, 2010; Wen et al, 2010). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5635855 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-5635855 Full-length GLI proteins are labile transcription factors that are rapidly degraded after ubiquitination by the SPOP:CUL3:RBX1 E3 ligase (Ohlmeyer et al, 1998; Humke et al, 2010; Tukachinsky et al, 2010; Chen et al, 2009; Zhang et al, 2009; Wen et al, 2010). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5635856 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-5635856 The transcriptional activity of full-length activated Ci/GLI proteins is restricted by their rapid ubiquitin-mediated degradation after initiation of Hh signaling (Ohlmeyer et al, 1998; Humke et al, 2010; Tukachinsky et al, 2010; Wen et al, 2010). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5652005 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-5652005 The complex of RAD18, an E3 ubiquitin ligase, and UBE2B (RAD6), an E2 ubiquitin-conjugating enzyme, binds the replication complex consisting of PCNA, DNA polymerase complex delta (POLD) or DNA polymerase complex epsilon (POLE), RPA and RFC on damaged dsDNA. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5652009 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-5652009 The complex of RAD18, an E3 ubiquitin ligase, and UBE2B (RAD6), an E2 ubiquitin conjugating enzyme, monoubiquitinates PCNA associated with damaged DNA on lysine residue K164, using the ubiquitin residue K63 to create the covalent bond (Hoege et al. 2002). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5689317 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-5689317 Once an open bubble structure is generated in damaged dsDNA through a DNA helicase activity of the TFIIH complex, the RPA heterotrimer composed of RPA1, RPA2 and RPA3, coats the undamaged single strand DNA (ssDNA) (de Laat et al. 1998), thereby protecting it from incision and enabling the correct file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5689861 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-5689861 XPA binds the DNA damage site through interaction with the TFIIH complex subunit GTF2H5 (TTDA) (Ziani et al. 2014), and also interacts with the DDB2 subunit of the UV-DDB complex (Wakasugi et al. 2001, Wakasugi et al. 2009, Takedachi et al. 2010). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5690213 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-5690213 The DNA repair synthesis complex, consisting of PCNA, RFC, RPA and polymerase delta (POLD) or epsilon (POLE) complexes, or DNA translesion synthesis polymerase kappa (POLK) (Ogi et al. 2010), is formed at the nucleotide excision repair (NER) site following the incision of the damaged DNA strand 5' file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5690988 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-5690988 In global genome nucleotide excision repair (GG-NER), as well as transcription-coupled nucleotide excision repair (TC-NER), the cleavage of the damaged DNA strand 3' to the site of damage is carried out by a DNA endonuclease XPG (ERCC5). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5690990 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-5690990 In global genome nucleotide excision repair (GG-NER), just like in transcription-coupled nucleotide excision repair (TC-NER), the cleavage of the damaged strand of DNA 5' to the site of damage occurs at the junction of single-stranded DNA and double-stranded DNA that is formed when the DNA duplex file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5690991 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-5690991 ERCC1:ERCC4 (ERCC1:XPF) DNA endonuclease complex binds 5' to the DNA damage at global genome nucleotide excision repair (GG-NER) sites to form the incision complex. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5690996 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-5690996 Two DNA helicases XPB (ERCC3) and XPD (ERCC2), which are part of the TFIIH complex, unwind the distorted DNA duplex around the lesion to form an open bubble structure that exposes the damaged site. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5691000 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-5691000 Transcription factor II H (TFIIH) complex is recruited to DNA damage sites after the damage is recognized by the XPC:RAD23:CETN2 complex and the UV-DDB complex (DDB1:DDB2) (Volker et al. 2001, Araujo and Wood 1999).<p>TFIIH consists of ten subunits organized into a ring-like structure (Schultz et file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5691006 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-5691006 XPC, in complex with RAD23B or RAD23A and CETN2, employs a two-stage process to recognize a distorted DNA helix. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5696655 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-5696655 PARP1 and/or PARP2 homo- or heterodimers recruited to global genomic nucleotide excision repair (GG-NER) site poly(ADP)ribosylate (PARylate) DDB2 and also progressively autoPARylate. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5696664 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-5696664 PARP1 (or PARP2) is recruited to global genomic nucleotide excision repair (GG-NER) site through interaction with DDB2 and, probably, distorted single strand DNA (Pines et al. 2012, Robu et al. 2013). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5696670 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-5696670 A chromatin remodeling enzyme CHD1L (ALC1) is recruited to DNA damage sites through interaction with PARylated PARP1 (or possibly PARP2) (Ahel et al. 2009) or PARylated DDB2 (Pines et al. 2012). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6781833 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-6781833 Cockayne syndrome protein A (ERCC8, also known as CSA) is recruited to a stalled RNA polymerase II complex (RNA Pol II) at a site of DNA damage in an ERCC6 (CSB) dependent manner (Kamiuchi et al. 2002; van der Weegen et al. 2020). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6781867 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-6781867 The ubiquitin ligase complex ERCC8:DDB1:CUL4:RBX1 may ubiquitinate ERCC6 (CSB) (Groisman et al. 2006) at the later steps of TC-NER and may also be required in the ubiquitination of the RNA Pol II subunit POLR2A in response to damage (Bregman et al. 1996, Lee et al. 2002). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782004 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-6782004 In addition to ERCC6 (CSB) and the ERCC8 (CSA) ubiquitin ligase complex, several other proteins and protein complexes are loaded onto stalled RNA polymerase II (RNA Pol II) at DNA damage sites to form a pre-incision complex that operates in the transcription-coupled nucleotide excision repair file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782069 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-6782069 UVSSA stabilizes ERCC6 (CSB) during transcription-coupled nucleotide excision repair (TC-NER) by targeting ubiquitin protease USP7 to ubiquitinated ERCC6, thus preventing proteasome-mediated degradation of ERCC6. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782131 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-6782131 The DNA helicase XPD (ERCC2), which is part of the TFIIH complex, unwinds the distorted DNA duplex around the lesion to form an open bubble structure that exposes the damaged site. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782138 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-6782138 It has been suggested that, similar to the UvrD helicase involved in TC-NER in E.coli, the DNA helicase activity of TFIIH complex may facilitate damage-stalled RNA polymerase II (RNA Pol II) backtracking (Epshtein et al. 2014). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782141 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-6782141 ERCC1:ERCC4 (ERCC1:XPF) DNA endonuclease complex binds to the pre-incision complex at the transcription-coupled nucleotide excision repair (TC-NER) site to form the incision complex. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782204 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-6782204 In transcription-coupled nucleotide excision repair (TC-NER), just like in global genome nucleotide excision repair (GG-NER), the cleavage of the damaged strand of DNA 5' to the site of damage occurs at the junction of single-stranded DNA and double-stranded DNA that is formed when the DNA duplex file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782208 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-6782208 In transcription-coupled nucleotide excision repair (TC-NER), as well as in global genome nucleotide excision repair (GG-NER), the DNA synthesis complex (NER post-incision complex) consisting of PCNA, RPA, RFC and polymerase delta (POLD) or epsilon (POLE) complexes performs DNA repair synthesis file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782211 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-6782211 The DNA repair synthesis complex, consisting of PCNA, RFC, RPA and polymerase delta (POLD) or epsilon (POLE) complexes, or polymerase kappa (POLK), is formed at the transcription coupled nucleotide excision repair (TC-NER) site, as well as the global genome nucleotide excision repair (GG-NER) site, file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782224 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-6782224 In transcription-coupled nucleotide excision repair (TC-NER), as well as in global genome nucleotide excision repair (GG-NER), the cleavage of the damaged DNA strand 3' to the site of damage is carried out by a DNA endonuclease XPG (ERCC5). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782227 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-6782227 The nucleotide excision repair (NER) is completed when the newly synthesized fragment is ligated to the incised DNA strand, thus sealing the single stranded nick (SSB). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782234 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-6782234 After DNA repair synthesis is completed at transcription-coupled nucleotide excision repair (TC-NER) sites, transcription resumes. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6782943 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-6782943 The role of UV-DDB-mediated ubiquitination in global genome nucleotide excision repair (GG-NER) has not been fully elucidated.<p>In the absence of DNA damage, the ubiquitin ligase activity of UV-DDB complex is inhibited by association with the COP9 signalosome (CSN complex), which dissociates from file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6790454 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-6790454 XPC undergoes SUMOylation following UV irradiation on several consensus SUMOylation sites (van Cuijk et al. 2015). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6790487 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-6790487 SUMOylated XPC is recognized by the SUMO-targeted ubiquitin ligase RNF111 (Arcadia) that, together with the E2 ubiquitin conjugating complex of UBE2N (UBC13) and UBE2V2 (MMS2), generates K63-linked polyubiquitin chains on XPC (Poulsen et al. 2013) to efficiently release XPC from UV lesions (van file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-68946 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-68946 ORC1 is ubiquitinated by the SKP2-containing ubiquitin ligase complex and targeted for proteasome-mediated degradation, which may play an important role in the maintenace of ploidy. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-69598 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-69598 <p>Exposure of various human cell lines to ultraviolet (UV) light leads to rapid appearance of polyubiquitinated CDC25A (PolyUb-CDC25A) (Mailand et al. 2000). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8939688 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-8939688 The E3 ubiquitin ligase complex SCF binds RUNX2 through direct interaction between SKP2 subunit of the SCF complex and RUNX2 (Thacker et al. 2016). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8939706 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-8939706 The SCF(SKP2) E3 ubiquitin ligase complex polyubiquitinates RUNX2 on unknown lysine residues, targeting it for proteasome-mediated degradation. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8952638 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-8952638 UBE2M transfers NEDD8 to lysine 705 of CUL4A and lysine 859 of CUL4B (Hori et al, 1999; Duda et al, 2008). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8952639 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-8952639 UBE2M is the E2 for CRL complexes containing cullin 1, 2, 3 and 4 (Huang et al, 2009; Monda et al, 2013). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8955245 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-8955245 CRL complexes consist of a cullin protein (CUL1, 2, 3, 4A, 4B, 5, 7 and 9 in humans) and a RING box protein (RBX1 or 2) in addition to one or more substrate binding proteins that confer substrate specificity to the complex (reviewed in Petroski and Deshaies, 2005; Lipkowitz and Weismann, 2011). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8955285 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-8955285 COMMD1 is a member of a family of 10 copper metabolism MURR1 domain-containing proteins that have pleiotropic roles in copper metabolism, NF kappa beta-mediated transcription, the hypoxic response and electrolyte transport (Burstein et al, 2005; reviewed in Maine and Burstein, 2007). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8956045 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-8956045 The COP9 signalosome (also known as CSN) is a highly conserved multi-subunit enzymatic complex that plays a role as the sole CRL ubiquitin ligase deneddylase. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9684118 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-9684118 The DNA helicase XPB (ERCC3), which is part of the TFIIH complex, unwinds the distorted DNA duplex around the lesion to form an open bubble structure that exposes the damaged site. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9708517 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-9708517 The leucine-rich repeat family of F-box proteins (FBXLs) function as adapter for the SKP1-CUL1-F-box protein (SCF) E3 ubiquitin ligase. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9708525 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-9708525 The leucine-rich repeat family of F-box proteins (FBXLs) function as adapter for the SKP1-CUL1-F-box protein (SCF) E3 ubiquitin ligase. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9725023 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-9725023 ZC3HC1, also known as NIPA (nuclear interacting partner of anaplastic lymphoma kinase), was identified as a protein partner of NPM-ALK fusion in two hybrid and co-imuunoprecipitation studies (Ouyang et al, 2003). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9725030 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-9725030 NPM-ALK-mediated activation of the MAP kinase signaling pathway leads to phosphorylation and activation of MAPK1 (ERK2) (Illert et al, 2012). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9762091 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-9762091 GSK3-dependent phosphorylation of NFE2L2 promotes its subsequent ubiquitination by a BTRC:CUL1 E3 ligase complex (Salazar et al, 2006; Rada et al, 2011; Rada et al, 2012; Rojo et al, 2012; reviewed in Baird and Yamamoto, 2020; Yamamoto et al, 2018). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9762093 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-9762093 In response to GSK3B-dependent phosphorylation at, minimally, serine residues 344 and 347, the CUL1:BTRC complex binds to NFE2L2 through the Neh6 domain (Salazar et al, 2006; Rada et al, 2011; Rada et al, 2012; Rojo et al, 2012; reviewed in Baird and Yamamoto, 2020; Yamamoto et al, 2018). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9762096 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-HSA-9762096 After BTRC:CUL1-mediated ubiquitination, NFE2L2 is degraded by the proteasome (Rada et al, 2011; Rada et al, 2012; reviewed in Baird and Yamamoto, 2020; Yamamoto et al, 2018). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-NUL-2064853 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-NUL-2064853 The E3 ubiquitin ligase FBXW7, a homologue of C. elegans sel-10, binds to Notch1 intracellular domain NICD1. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-NUL-2064883 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-NUL-2064883 A recombinant mouse NICD1 was shown to be ubiquitinated upon binding to recombinant human FBXW7 (Oberg et al. 2001), which is followed by NICD1 degradation (Fyer et al. 2004). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005654 nucleoplasm | TAS Reactome:R-NUL-9604628 | ACCEPT | Summary: Nucleoplasmic localisation of RBX1-containing ligases, as assigned to the individual Reactome reactions in which the RBX1-cullin catalytic module ubiquitinates nuclear substrates, and as seen by immunofluorescence. Reason: Consistent with the nuclear CRL substrates (HIF-alpha, GLI2/3, beta-catenin, PCNA, RNA Pol II, NER factors) and with the UniProt nuclear localisation; these are pathway compartment assignments rather than RBX1-specific imaging, but they are not in conflict with the direct evidence. Supporting Evidence: Reactome:R-NUL-9604628 The human E3 ubiquitin ligase FBXW7, a component of the SCF ubiquitin ligase complex, binds to and ubiquitinates phosphorylated mouse NICD4 (Notch4 intracellular domain fragment), targeting it for proteasome-mediated degradation (Wu et al. 2001). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005737 cytoplasm | IC PMID:27708159 Insulin resistance and diabetes caused by genetic or diet-in... | ACCEPT | Summary: RBX1 also functions in the cytoplasm, where CRLs degrade signalling proteins (IkappaB-alpha, DEPTOR, IRS1, p85alpha, RhoA/RhoB) and where cullin neddylation is initiated. Reason: Direct evidence plus the UniProt cytoplasmic location; a cytoplasmic pool is expected for a subunit shared by ligases with cytoplasmic receptors. Supporting Evidence: PMID:27708159 Kbtbd2 encodes a BTB-Kelch family substrate recognition subunit of the Cullin-3-based E3 ubiquitin ligase. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005737 cytoplasm | IC PMID:36394357 XAF1 prevents hyperproduction of type I interferon upon vira... | ACCEPT | Summary: RBX1 also functions in the cytoplasm, where CRLs degrade signalling proteins (IkappaB-alpha, DEPTOR, IRS1, p85alpha, RhoA/RhoB) and where cullin neddylation is initiated. Reason: Direct evidence plus the UniProt cytoplasmic location; a cytoplasmic pool is expected for a subunit shared by ligases with cytoplasmic receptors. Supporting Evidence: PMID:36394357 Mechanistically, we find that the XAF1-XIAP axis controls the activity of KLHL22, an adaptor of the BTB-CUL3-RBX1 E3 ligase complex through a ubiquitin-dependent pathway. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005737 cytoplasm | IDA PMID:27708159 Insulin resistance and diabetes caused by genetic or diet-in... | ACCEPT | Summary: RBX1 also functions in the cytoplasm, where CRLs degrade signalling proteins (IkappaB-alpha, DEPTOR, IRS1, p85alpha, RhoA/RhoB) and where cullin neddylation is initiated. Reason: Direct evidence plus the UniProt cytoplasmic location; a cytoplasmic pool is expected for a subunit shared by ligases with cytoplasmic receptors. Supporting Evidence: PMID:27708159 Kbtbd2 encodes a BTB-Kelch family substrate recognition subunit of the Cullin-3-based E3 ubiquitin ligase. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005737 cytoplasm | IDA PMID:34065512 CRL4-DCAF12 Ubiquitin Ligase Controls MOV10 RNA Helicase dur... | ACCEPT | Summary: RBX1 also functions in the cytoplasm, where CRLs degrade signalling proteins (IkappaB-alpha, DEPTOR, IRS1, p85alpha, RhoA/RhoB) and where cullin neddylation is initiated. Reason: Direct evidence plus the UniProt cytoplasmic location; a cytoplasmic pool is expected for a subunit shared by ligases with cytoplasmic receptors. Supporting Evidence: PMID:34065512 CRL4-DCAF12 Ubiquitin Ligase Controls MOV10 RNA Helicase during Spermatogenesis and T Cell Activation. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: RBX1 also functions in the cytoplasm, where CRLs degrade signalling proteins (IkappaB-alpha, DEPTOR, IRS1, p85alpha, RhoA/RhoB) and where cullin neddylation is initiated. Reason: Direct evidence plus the UniProt cytoplasmic location; a cytoplasmic pool is expected for a subunit shared by ligases with cytoplasmic receptors. Supporting Evidence: file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005794 Golgi apparatus | IDA PMID:34065512 CRL4-DCAF12 Ubiquitin Ligase Controls MOV10 RNA Helicase dur... | KEEP AS NON CORE | Summary: Golgi-apparatus signal for RBX1 reported alongside the CRL4-DCAF12 study of MOV10 turnover. Reason: Retained but non-core: no Golgi-specific function of RBX1 is established, and a shared CRL subunit is expected to appear wherever a receptor concentrates it. The observation is kept as a context-specific localisation rather than a site of the core ligase activity. Supporting Evidence: PMID:34065512 CRL4-DCAF12 Ubiquitin Ligase Controls MOV10 RNA Helicase during Spermatogenesis and T Cell Activation. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005813 centrosome | NAS PMID:20596027 SCF(Cyclin F) controls centrosome homeostasis and mitotic fi... | KEEP AS NON CORE | Summary: Author statement placing the SCF(cyclin F) ligase, which contains RBX1, on centrioles in G2 where it degrades CP110. Reason: Genuine but receptor-specific: cyclin F, not RBX1, targets the complex to centrosomes. Kept as a non-core localisation of the shared catalytic module. Supporting Evidence: PMID:20596027 SCF(Cyclin F) controls centrosome homeostasis and mitotic fidelity through CP110 degradation. file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0005829 cytosol | IEA GO_REF:0000107 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | ISS GO_REF:0000024 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1170539 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-1170539 PRLR is regulated by ubiquitination of the activated receptor, leading to lysosomal degradation (Djiane et al. 1981, 1982, Lu et al. 2002). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1234159 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-1234159 Destruction of ubiquitinated HIF-alpha can occur in both the cytosol and nucleus (Berra et al. 2001). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1234163 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-1234163 VHL is an E3 ubiquitin ligase that conjugates ubiquitin to hydroxylated HIF-alpha (Iwai et al. 1999, Kamura et al. 2000, Ohh et al. 2000, Groulx and Lee 2002, Maynard et al. 2003). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1234173 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-1234173 Proline hydroxylases PHD2 (EGLN1) and PHD3 (EGLN3) located in the cytosol (Metzen et al. 2003) hydroxylate HIF3A at proline-492 (Hirsila et al. 2003, Maynard et al. 2003). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1234175 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-1234175 When hypoxic cells return to normoxia, HIF-alpha is ubiquitinated in the nucleus and exported to the cytosol (Groulx and Lee 2002). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1234177 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-1234177 Proline hydroxylases PHD2 (EGLN1) and PHD3 (EGLN3) located in the cytosol (Metzen et al. 2003) hydroxylate HIF1A at proline-402 and proline-564 (Bruick and McKnight 2001, Jaakkola et al. 2001, Ivan et al. 2001, Ivan et al. 2002, Berra et al. 2003, Hirsila et al. 2003, Appelhoff et al. 2004, file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1234183 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-1234183 VHL within the VHL:ElonginB:ElonginC:CUL2:RBX1 Complex binds HIF-alpha subunits that have hydroxylated proline residues (Cockman et al. 2000, Ohh et al. 2000, Tanimoto et al. 2000, Jaakkola et al. 2001, Ivan et al. 2001, Yu et al. 2001). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1370500 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-1370500 Phosphorylation of PRLR on Ser-349 by an unidentified kinase enables recruitment of the SCF beta-TrCP ubiquitin ligase complex, which catalyzes ubiquitination of the receptor (Li et al. 2004). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1504190 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-1504190 CUL3:KLHL12:RBX1 polyubiquitinates Dishevelled, targeting it for degradation by the proteasome (Angers et al, 2006). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1504193 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-1504193 Ubiquitinated Dishevelled is degraded by the proteasome. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1504213 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-1504213 In response to WNT signaling, DVL is recruited to the CUL3:KLHL12:RBX1 ubiquitin ligase complex and is subsequently polyubiquitinated and degraded. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-180540 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-180540 APOBEC3G is multi-ubiquitinated by the Vif-Cul5-SCF complex. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-180555 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-180555 The interaction between Vif and the E3 ubiquitin ligase complex (Cullin5, Elongin B and Elongin C, and Rbx1) takes place through direct binding of the SOCS box motif in the viral protein Vif to the host protein Elongin C. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-180603 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-180603 Following multi-ubiquitination by the Vif-Cul5-SCF complex, APOBEC3G is degraded by the 26S proteasome. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-209063 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-209063 SCF (Beta-TrCP) ubiquitinates phosphorylated I kappa B alpha. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-209125 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-209125 Human beta-TrCP forms part of the SCF E3 ubiquitin ligase complex which binds to phosphorylated residues Ser32 and Ser 36 at the IKK target motif in IKBA complex with P65:P50 heterodimer. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2130279 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-2130279 B-TrCP associates with phosphorylated beta-catenin through the B-TrCP WD40 repeat region. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2130282 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-2130282 Ubiquitinated beta-catenin is degraded by the proteasome. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2130286 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-2130286 Beta-catenin is ubiquitinated by the SCF-B-TrCP1 complex. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5610742 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-5610742 GLI1 protein is degraded by the proteasome in the absence of Hh signal. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5610746 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-5610746 Hyperphosphorylated GLI3 binds directly with beta-TrCP though at least three independent domains and is polyubiquitinated at lysines 773, 778, 784 and 800 (Tempe et al, 2006). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5658424 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-5658424 NF1 levels are controlled by proteasomal degradation in response to stimulation by some growth factors (Cichowski et al, 2003). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8853496 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-8853496 FBXL7, a component of the SCF E3 ubiquitin ligase complex, associates with aurora kinase A (AURKA) during mitosis (Coon et al. 2012). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8854041 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-8854041 The SCF-FBXL7 E3 ubiquitin ligase complex, composed of SKP1, CUL1, RBX1 and FBXL7, ubiquitinates aurora kinase A (AURKA), targeting it for degradation (Coon et al. 2012). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8854044 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-8854044 Upon ubiquitination by the SCF-FBXL7 E3 ubiquitin ligase complex, aurora kinase A (AURKA) is degraded by the proteasome (Coon et al. 2012). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8854051 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-8854051 FBXL18, a substrate recognition subunit of the SCF E3 ubiquitin ligase complex can bind to the FQ motif of FBXL7. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8854052 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-8854052 FBXL7 associates with SKP1, CUL1 and RBX1 to form the SCF E3 ubiquitin ligase complex (Coon et al. 2011). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8932327 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-8932327 Under the basal resting conditions, cytosolic Nuclear factor erythroid 2-related NFE2L2 (NRF2) is maintained at low basal levels by constitutive proteasomal degradation. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8952618 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-8952618 UBE2M transfers NEDD8 to lysine 720 of CUL1 in the CRL E3 ubiquitin ligase complex (Hori et al, 1999; Duda et al, 2008). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8952620 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-8952620 UBE2M is the E2 for CRL complexes containing cullin 1, 2, 3 and 4 (Huang et al, 2009; Monda et al, 2013). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8952625 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-8952625 UBE2M is the E2 ubiquitin ligase for CRL complexes containing cullin 1, 2, 3 and 4 (Huang et al, 2009; Monda et al, 2013). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8952626 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-8952626 UBE2M transfers NEDD8 to lysine 689 of CUL2 in the E3 ligase complex (Hori et al, 1999; Duda et al, 2008). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8952630 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-8952630 UBE2M is the E2 for CRL complexes containing cullin 1, 2, 3 and 4 (Huang et al, 2009; Monda et al, 2013). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8952631 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-8952631 UBE2M transfers NEDD8 to lysine 712 of CUL3 in the E3 ligase complex (Hori et al, 1999; Duda et al, 2008). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8955241 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-8955241 CRL complexes consist of a cullin protein (CUL1, 2, 3, 4A, 4B, 5, 7 and 9 in humans) and a RING box protein (RBX1 or 2) in addition to one or more substrate binding proteins that confer substrate specificity to the complex (reviewed in Petroski and Deshaies, 2005; Lipkowitz and Weismann, 2011). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8955289 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-8955289 COMMD1 is a member of a family of 10 copper metabolism MURR1 domain-containing proteins that have pleiotropic roles in copper metabolism, NF kappa beta-mediated transcription, the hypoxic response and electrolyte transport (Burstein et al, 2005; reviewed in Maine and Burstein, 2007). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8956025 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-8956025 UBE2M transfers NEDD8 to lysine 1881 of CUL9 (Skaar et al, 2007; Li et al, 2014). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8956026 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-8956026 One defined target of CUL9 ubiquitin ligase is BIRC5 (also known as Survivin), which has roles in cellular proliferation, inhibition of apoptosis and maintenance of genome stability (Zhao et al, 2000; Watanabe, 2010). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8956031 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-8956031 CUL9 (also known as PARC for p53-associated PARkin-like cytoplasmic protein) is an atypical cullin that has been shown to form a ubiquitin ligase complex with RBX1, although other components of the putative CRL9 complex have not yet been identified (Skaar et al, 2007; Li et al, 2014). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8956040 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-8956040 The COP9 signalosome (also known as CSN) is a highly conserved multi-subunit enzymatic complex that plays a role as the sole CRL ubiquitin ligase deneddylase. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8956050 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-8956050 CUL7, CCDC8 and OBSL1 are part of a 3M complex that has roles in maintenace of genome stability and microtubule dynamics (Li et al, 2014; Yan et al, 2014). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8956099 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-8956099 The best characterized CRL2 substrate binding F-box protein is the von Hippel- Lindau (VHL) tumor suppressor, which targets the alpha subunit of hypoxia inducible factor (HIFalpha) for ubiquitination and degradation through VCP/p97 and the 26 S proteasome (Sufan and Ohh, 2006; Heir et al, 2013; file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8956103 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-8956103 The best characterized CRL2 substrate binding F-box protein is the von Hippel- Lindau (VHL) tumor suppressor, which targets the alpha subunit of hypoxia inducible factor (HIFalpha) for ubiquitination and degradation through VCP/p97 and the 26 S proteasome (Sufan and Ohh, 2006; Heir et al, 2013; file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8956106 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-8956106 VHL is the substrate binding protein of a CUL2-based E3 ubiquitin ligase complex that conjugates ubiquitin to hydroxylated HIF-alpha (Iwai et al. 1999, Kamura et al. 2000, Ohh et al. 2000, Groulx and Lee 2002, Maynard et al. 2003). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8956200 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-8956200 DCUN1D3 binds to CRL1 ligase complexes to antagonize their neddylation and activation. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9712274 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-9712274 KEAP1:CUL3:RBX1-mediated degradation of NFE2L2 is relieved in the presence of oxidative or electrophilic stress, allowing NFE2L2 to translocate to the nucleus to support expression of target genes. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9755303 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-9755303 Destruction of ubiquitinated HIF-alpha can occur in both the cytosol and nucleus (Berra et al. 2001). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9755505 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-9755505 The KEAP1:CUL3:RBX1 E3-ubiquitin ligase complex is a negative regulator of Nuclear factor erythroid 2-related (NFE2L2). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9755507 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-9755507 VCP (also known as p97) is a hexameric ATPase with known roles in extracting ubiquinated substrates from multimeric E3 ligase complexes to promote their degradation by the 26S proteasome (Richly et al, 2005; Meyer et al, 2000; Rape et al, 2001; Tao et al, 2017; reviewed in van den Boom and Meyer, file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9758090 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-9758090 The complex of VCP/p97 with cofactors UFD1, NPLOC4 and UBXN7 extract ubiquitinated NFE2L2 from the KEAP1-CUL3 ubiquitin ligase complex prior to its 26S proteasome-mediated degradation (Tao et al, 2017; Di Gregorio et al, 2021; reviewed in van den Boom and Meyer, 2020). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9759169 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-9759169 SQSTM1 binds to the KEAP1 subunit of the CRL3 ubiquitin ligase complex through the KEAP1 interacting region (KIR) located at residues 339-358 (Jain et al, 2010). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9759172 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-9759172 SQSTM1 is an adaptor protein that mediates aggregation of target proteins for selective autophagy (reviewed in Lamark et al, 2017). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9766645 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-9766645 KEAP1 is ubiquitinated by the CUL3:RBX1 complex in an SQSTM1-dependent manner (Zhang et al, 2005). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9766656 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-9766656 KEAP1 is a substrate for SQSTM1-mediated autophagy (Zhang et al, 2005; Jain et al, 2010; Fan et al, 2010; Taguchi et al, 2012). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9766677 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-9766677 SQSTM1 targets ubiquitinated cargo such as KEAP1 for degradation through the selective autophagy pathway. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9766687 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-9766687 SESN1 and SESN2 are proteins with roles in oxidative stress response. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-983140 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-983140 Interaction of E3 with both substrate and E2-Ub, brings them into proximity so that ubiquitin is transferred from E2 to the substrate. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-983147 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-983147 K48 polyubiquitinated substrate dissociates from E3 to become a substrate for a multicatalytic complex called the 26S proteasome. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-983156 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-983156 Monoubiquitinated substrate acquires additional ubiquitin modifications in the form of multiple single attachments or a ubiquitin chain. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-983157 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-983157 Ubiquitin E3 ligases confer specificity to ubiquitination by recognizing target substrates and mediating transfer of ubiquitin from an E2 ubiquitin-conjugating enzyme to substrate (Raymond et al. 2009). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9833107 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-9833107 hRSV nonstructural protein 1C (NS1) binds to the elongin C (ELOC) and cullin-5 (CUL5) components of the Cul5-SCF complex to direct the ubiquitination and proteasome-dependent degradation of STAT2 (Elliott et al, 2007). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9833155 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-9833155 Human signal transducer and activator of transcription 2 (STAT2) is subject to ubiquitination by, among other E3 ubiquitin ligases, a complex consisting of human respiratory syncytial virus (hRSV) protein NS1 with elongin C (ELOC) and cullin-5 (CUL5). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9929350 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-9929350 Ξ²-TrCP-SCF complex catalyses PD-L1(CD274) polyubiquitination in the presence of GSK3Ξ². file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9929352 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-9929352 PD-L1 (CD274) is targeted for 26S proteasomal degradation through phosphorylation by GSK3B and the subsequent ubiquitination by the beta-TrCP-SCF E3 ubiquitin ligase complex (Li et al., 2016). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9929353 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-9929353 COP9 signalosome 5 (CSN5) poses deubiquitination activity and is known to regulate the SCF (Skp1- cullinF-box)-containing complexes. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9929357 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-9929357 Ξ²-TrCP (BTRC) is the substrate recognizing subunit of the E3 ubiquitin ligase complex SCF (Skip-Cullin-F-box). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9929484 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-9929484 The SPOP:CUL3:RBX1 E3 ubiquitin ligase complex regulates the ubiquitination and degradation of PD-L1(CD274) protein. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9929486 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-9929486 PD-L1 (CD274) polyubiquitinated by the SPOP:CUL3:RBX1 E3 ubiquitin ligase complex gets degraded by the 26S proteasome complex (Zhang et al., 2018, Dong et al, 2022). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9929490 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-9929490 SPOP:CUL3:RBX1 E3-ubiquitin ligase complex polyubiquitinates PD-L1 and induces its proteasomal degradation (Zhang et al., 2018, Dong et al., 2022). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9954721 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-9954721 The CRL-KLHDC10 E3 ubiquitin ligase complex (NEDD8-K699-CUL2:ELOB:ELOC:RBX1:KLHDC10) polymerizes ubiquitin monomers with K48 linkages onto exposed lysine residues of an alanine-tailed nascent peptide that has been extracted from a 60S ribosomal subunit (Thrun et al. 2021). file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9954723 | ACCEPT | Summary: Cytosolic pool of the RBX1-cullin catalytic module, as assigned to Reactome reactions such as cytosolic VHL-EloBC-CUL2-RBX1 ubiquitination of hydroxyprolyl-HIF-alpha and SCF(beta-TrCP)-mediated degradation events. Reason: Cytosol is a legitimate site of RBX1 activity and is consistent with the UniProt cytoplasmic annotation and with ortholog-based transfer from mouse Rbx1. Supporting Evidence: Reactome:R-HSA-9954723 The CRL2-KLHDC10 ubiquitin E3 ligase complex (NEDD8-K699-CUL2:ELOB:ELOC:RBX1:KLHDC10) binds C-terminal alanine residues that have been polymerized ("CAT-tailed") by NEMF onto a nascent peptide from a 60S ribosomal subunit that has been dissociated from a stalled 80S ribosome (Thrun et al. 2021, file:human/RBX1/RBX1-deep-research-falcon.md RBX1 is reported in both the **nucleus and cytoplasm**, consistent with degradation of substrates in both compartments. |
| GO:0006283 transcription-coupled nucleotide-excision repair | IDA PMID:34526721 Structural basis of human transcription-DNA repair coupling. | KEEP AS NON CORE | Summary: In the CSA/ERCC8-CUL4-DDB1-RBX1 complex, RBX1 ubiquitinates RPB1/POLR2A at Lys1268 at DNA damage-stalled Pol II, a checkpoint step of transcription-coupled repair. Reason: A real, structurally defined contribution, but specific to the ERCC8 receptor; kept as non-core for a RING shared by all CRLs. Supporting Evidence: PMID:34526721 RBX1 and the E2 enzymeβdonor ubiquitin complex were modelled as described in the Methods. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0006289 nucleotide-excision repair | NAS PMID:22118460 The molecular basis of CRL4DDB2/CSA ubiquitin ligase archite... | KEEP AS NON CORE | Summary: Author statement from the CRL4(DDB2) architecture study: the DDB2-CUL4-RBX1 ligase creates a ubiquitination zone around UV lesions and is required for nucleotide-excision repair. Reason: Receptor-specific (DDB2) role of the shared catalytic subunit; retained as non-core, with the precise molecular event (ubiquitination at the lesion) annotated separately. Supporting Evidence: PMID:22118460 The DDB1-CUL4-RBX1 (CRL4) ubiquitin ligase family regulates a diverse set of cellular pathways through dedicated substrate receptors (DCAFs). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0006355 regulation of DNA-templated transcription | NAS PMID:36372232 Identification of an E3 ligase that targets the catalytic su... | MARK AS OVER ANNOTATED | Summary: SCF(FBXL14) containing RBX1 degrades the Pol I catalytic subunit RPA194 under transcription stress. Reason: Over-annotation for the shared RING: the direct process is ubiquitination leading to proteasomal degradation of a polymerase subunit; 'regulation of DNA-templated transcription' is a distal consequence. Supporting Evidence: PMID:36372232 RBX1 is a RING protein that recruits a ubiquitin-charged E2 to the E3 ligase. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0006511 ubiquitin-dependent protein catabolic process | IBA GO_REF:0000033 | ACCEPT | Summary: Ubiquitin-dependent protein catabolism is the general destination of RBX1-catalysed ubiquitination, via K48 chains read by the proteasome. Reason: Core process. The IBA at the RING-box family node is consistent with the experimental rows and with the conserved role of yeast Hrt1/Roc1 in Sic1 and Cln2 turnover. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000129805 Β· PANTHER:PTN000129805 SUPPORTS TRANSFER RING-box family node spanning RBX1, RBX2/RNF7 and APC11; the descendant experimental evidence includes human RBX1 itself, mouse Rbx1, fly Roc1a/Roc1b and yeast Hrt1/Rbx1 and Apc11, so the function is inherited rather than lineage-specific. Supporting Evidence: file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0006511 ubiquitin-dependent protein catabolic process | IDA PMID:17636018 ASB4 is a hydroxylation substrate of FIH and promotes vascul... | ACCEPT | Summary: Ubiquitin-dependent protein catabolism is the general destination of RBX1-catalysed ubiquitination, via K48 chains read by the proteasome. Reason: Core process. The IBA at the RING-box family node is consistent with the experimental rows and with the conserved role of yeast Hrt1/Roc1 in Sic1 and Cln2 turnover. Supporting Evidence: PMID:17636018 Like other SOCS box-containing proteins, ASB4 is the substrate recognition molecule of an elongin B/elongin C/cullin/Roc ubiquitin ligase complex that mediates the ubiquitination and degradation of substrate protein(s). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0006511 ubiquitin-dependent protein catabolic process | IDA PMID:18498745 The CUL7 E3 ubiquitin ligase targets insulin receptor substr... | ACCEPT | Summary: Ubiquitin-dependent protein catabolism is the general destination of RBX1-catalysed ubiquitination, via K48 chains read by the proteasome. Reason: Core process. The IBA at the RING-box family node is consistent with the experimental rows and with the conserved role of yeast Hrt1/Roc1 in Sic1 and Cln2 turnover. Supporting Evidence: PMID:18498745 Recent genetic studies have documented a pivotal growth-regulatory role played by the Cullin 7 (CUL7) E3 ubiquitin ligase complex containing the Fbw8-substrate-targeting subunit, Skp1, and the ROC1 RING finger protein. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0006513 protein monoubiquitination | IDA PMID:22358839 Ubiquitin-dependent regulation of COPII coat size and functi... | ACCEPT | Summary: RBX1-containing CRLs also perform monoubiquitination, e.g. CUL3-KLHL12-RBX1 monoubiquitinates the COPII subunit SEC31 and CRL4(CDT2) monoubiquitinates PCNA. Reason: Core process with a non-degradative output; the same RING chemistry produces mono- or polyubiquitin depending on the E2 and the assembly. Supporting Evidence: PMID:22358839 For in vitro ubiquitination reactions, Cul3/Rbx1 purified from Sf9 cells was conjugated to NEDD8 using recombinant APPBP1-UBA3, Ubc12, and NEDD8. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0006513 protein monoubiquitination | IEA GO_REF:0000117 | ACCEPT | Summary: RBX1-containing CRLs also perform monoubiquitination, e.g. CUL3-KLHL12-RBX1 monoubiquitinates the COPII subunit SEC31 and CRL4(CDT2) monoubiquitinates PCNA. Reason: Core process with a non-degradative output; the same RING chemistry produces mono- or polyubiquitin depending on the E2 and the assembly. Supporting Evidence: file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0006879 intracellular iron ion homeostasis | NAS PMID:19762597 An E3 ligase possessing an iron-responsive hemerythrin domai... | KEEP AS NON CORE | Summary: SCF(FBXL5) containing RBX1 degrades IRP2 when iron and oxygen are plentiful; FBXL5's hemerythrin domain is the sensor. Reason: Genuine but FBXL5-specific output; kept as non-core. Supporting Evidence: PMID:19762597 Degradation of FBXL5 would then preclude the assembly of the SCF complex allowing IRP2 to accumulate and bind IREs. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0006974 DNA damage response | EXP PMID:22118460 The molecular basis of CRL4DDB2/CSA ubiquitin ligase archite... | KEEP AS NON CORE | Summary: CRL4(DDB2), CRL4(CSA) and SCF(FBXO31)/SCF(FBXO46) ligases containing RBX1 act in the DNA-damage response, degrading MDM2 and FBXO31 and ubiquitinating chromatin and stalled Pol II. Reason: Genuine participation through several damage-specific receptors, but 'DNA damage response' is a receptor- and context-defined output of the shared RING rather than its core function. Supporting Evidence: PMID:22118460 The DDB1-CUL4-RBX1 (CRL4) ubiquitin ligase family regulates a diverse set of cellular pathways through dedicated substrate receptors (DCAFs). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0006974 DNA damage response | IDA PMID:26124108 F-box protein FBXO31 directs degradation of MDM2 to facilita... | KEEP AS NON CORE | Summary: CRL4(DDB2), CRL4(CSA) and SCF(FBXO31)/SCF(FBXO46) ligases containing RBX1 act in the DNA-damage response, degrading MDM2 and FBXO31 and ubiquitinating chromatin and stalled Pol II. Reason: Genuine participation through several damage-specific receptors, but 'DNA damage response' is a receptor- and context-defined output of the shared RING rather than its core function. Supporting Evidence: PMID:26124108 Following DNA damage, MDM2 is degraded rapidly, resulting in increased p53 stability. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0006974 DNA damage response | IDA PMID:30171069 The SCF(FBXO46) ubiquitin ligase complex mediates degradatio... | KEEP AS NON CORE | Summary: CRL4(DDB2), CRL4(CSA) and SCF(FBXO31)/SCF(FBXO46) ligases containing RBX1 act in the DNA-damage response, degrading MDM2 and FBXO31 and ubiquitinating chromatin and stalled Pol II. Reason: Genuine participation through several damage-specific receptors, but 'DNA damage response' is a receptor- and context-defined output of the shared RING rather than its core function. Supporting Evidence: PMID:30171069 The SCF(FBXO46) ubiquitin ligase complex mediates degradation of the tumor suppressor FBXO31 and thereby prevents premature cellular senescence. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0006974 DNA damage response | ISS GO_REF:0000114 | KEEP AS NON CORE | Summary: CRL4(DDB2), CRL4(CSA) and SCF(FBXO31)/SCF(FBXO46) ligases containing RBX1 act in the DNA-damage response, degrading MDM2 and FBXO31 and ubiquitinating chromatin and stalled Pol II. Reason: Genuine participation through several damage-specific receptors, but 'DNA damage response' is a receptor- and context-defined output of the shared RING rather than its core function. Supporting Evidence: file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0007283 spermatogenesis | IDA PMID:34065512 CRL4-DCAF12 Ubiquitin Ligase Controls MOV10 RNA Helicase dur... | KEEP AS NON CORE | Summary: CRL4-DCAF12 containing RBX1 degrades the RNA helicase MOV10 during spermatogenesis, and Dcaf17-null mice are infertile. Reason: Receptor-specific developmental output; kept as non-core. Supporting Evidence: PMID:34065512 CRL4-DCAF12 Ubiquitin Ligase Controls MOV10 RNA Helicase during Spermatogenesis and T Cell Activation. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0007283 spermatogenesis | NAS PMID:29907856 Deletion of DDB1- and CUL4- associated factor-17 (Dcaf17) ge... | KEEP AS NON CORE | Summary: CRL4-DCAF12 containing RBX1 degrades the RNA helicase MOV10 during spermatogenesis, and Dcaf17-null mice are infertile. Reason: Receptor-specific developmental output; kept as non-core. Supporting Evidence: PMID:29907856 CUL4 proteins interact with the E2 enzyme via the RING finger protein Hrt1/ROC1/Rbx1 at their C terminus. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0007346 regulation of mitotic cell cycle | NAS PMID:36395886 The SCF-FBXW7 E3 ubiquitin ligase triggers degradation of hi... | MARK AS OVER ANNOTATED | Summary: NAS row from the SCF(FBXW7)-WDR5 study of mitotic slippage. Reason: Over-annotation at the pathway level: RBX1's contribution is the ubiquitin transfer in SCF(FBXW7); the cell-cycle terms it does support (G1/S transition, SCF-dependent proteolysis) are annotated directly. Supporting Evidence: PMID:36395886 SKP1-CUL1-F-Box-FBXW7 mediates ubiquitination of WDR5 and targets it for proteasomal degradation. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0008270 zinc ion binding | IEA GO_REF:0000002 | ACCEPT | Summary: The RING-H2 domain of RBX1 coordinates two zinc ions in a cross-brace arrangement, plus a third zinc ion seen in SCF structures. Reason: Structural zinc binding is intrinsic to the RING-H2 fold and required for ligase activity; the InterPro-derived IEA is correct. Supporting Evidence: file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity |
| GO:0008283 cell population proliferation | NAS PMID:30945288 Inflammation-dependent overexpression of c-Myc enhances CRL4... | MARK AS OVER ANNOTATED | Summary: NAS row from a CRL4(DCAF4) study in colitis-associated cancer. Reason: Over-annotation: proliferation phenotypes follow from the loss of many CRL substrates at once and do not describe a process RBX1 performs. Supporting Evidence: PMID:30945288 Inflammation-dependent overexpression of c-Myc enhances CRL4(DCAF4) E3 ligase activity and promotes ubiquitination of ST7 in colitis-associated cancer. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0010506 regulation of autophagy | NAS PMID:31267705 Regulation of MAGE-A3/6 by the CRL4-DCAF12 ubiquitin ligase ... | KEEP AS NON CORE | Summary: CRL4-DCAF12 degrades MAGE-A3/6, which is required for starvation-induced autophagy; CRL inactivation also stabilises DEPTOR. Reason: Receptor- and context-specific; kept as non-core. Supporting Evidence: PMID:31267705 Regulation of MAGE-A3/6 by the CRL4-DCAF12 ubiquitin ligase and nutrient availability. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0010564 regulation of cell cycle process | NAS PMID:31424118 E2F1 proteolysis via SCF-cyclin F underlies synthetic lethal... | MARK AS OVER ANNOTATED | Summary: NAS rows from reviews and studies of SCF-dependent cell-cycle proteolysis (cyclin F-E2F1, SCF genome stability, ubiquitination in metastasis). Reason: Over-annotation: 'regulation of cell cycle process' adds nothing beyond the SCF-dependent catabolic and G1/S annotations, and the cited sources are review-level statements about SCF ligases generally. Supporting Evidence: PMID:31424118 Cyclin F, through the Fβbox domain, forms a functional Skp1βCul1βFβBox (SCF) complex acting as an E3 ubiquitin ligase. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0010564 regulation of cell cycle process | NAS PMID:34445249 The SCF Complex Is Essential to Maintain Genome and Chromoso... | MARK AS OVER ANNOTATED | Summary: NAS rows from reviews and studies of SCF-dependent cell-cycle proteolysis (cyclin F-E2F1, SCF genome stability, ubiquitination in metastasis). Reason: Over-annotation: 'regulation of cell cycle process' adds nothing beyond the SCF-dependent catabolic and G1/S annotations, and the cited sources are review-level statements about SCF ligases generally. 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. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0010564 regulation of cell cycle process | NAS PMID:35414786 The role of ubiquitination and deubiquitination in tumor inv... | MARK AS OVER ANNOTATED | Summary: NAS rows from reviews and studies of SCF-dependent cell-cycle proteolysis (cyclin F-E2F1, SCF genome stability, ubiquitination in metastasis). Reason: Over-annotation: 'regulation of cell cycle process' adds nothing beyond the SCF-dependent catabolic and G1/S annotations, and the cited sources are review-level statements about SCF ligases generally. Supporting Evidence: PMID:35414786 Ubiquitination is catalyzed by a three-enzyme cascade composed of the E1 Ub-activating enzyme, the E2 Ub-conjugating enzyme, and the E3 Ub ligase. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0010824 regulation of centrosome duplication | NAS PMID:29348145 FBXL13 directs the proteolysis of CEP192 to regulate centros... | KEEP AS NON CORE | Summary: SCF(FBXL13) containing RBX1 degrades CEP192, and SCF(cyclin F) degrades CP110, restraining centrosome duplication. Reason: Receptor-specific output; kept as non-core. Supporting Evidence: PMID:29348145 Here, we report that FBXL13, a binding determinant of SCF (SKP1-CUL1-F-box)-family E3 ubiquitin ligases, is enriched at centrosomes and interacts with the centrosomal proteins Centrin-2, Centrin-3, CEP152 and CEP192. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0014033 neural crest cell differentiation | NAS PMID:30190310 Dimerization quality control ensures neuronal development an... | KEEP AS NON CORE | Summary: SCF(FBXL17) containing RBX1 clears aberrant BTB dimers (dimerisation quality control), which is required for neural-crest and neuronal development; CUL3(KBTBD8) likewise drives neural-crest specification. Reason: Developmental output of specific receptors; non-core for the shared RING. Supporting Evidence: PMID:30190310 We conclude that metazoan organisms actively monitor BTB dimerization, and we predict that distinct E3 ligases similarly control complex formation by other recurrent domains. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0016485 protein processing | TAS PMID:16705181 Multisite protein kinase A and glycogen synthase kinase 3bet... | MARK AS OVER ANNOTATED | Summary: TAS row from the Gli3 study: SCF(beta-TrCP)-mediated ubiquitination is required for proteolytic processing of Gli3 into its repressor form. Reason: Over-annotation: RBX1 performs the ubiquitination, while the limited proteolysis that generates the Gli3 repressor is carried out by the proteasome. Protein ubiquitination and CRL-dependent catabolism already capture RBX1's role. Supporting Evidence: PMID:16705181 Multisite protein kinase A and glycogen synthase kinase 3beta phosphorylation leads to Gli3 ubiquitination by SCFbetaTrCP. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0016567 protein ubiquitination | IBA GO_REF:0000033 | ACCEPT | Summary: Protein ubiquitination is the process RBX1 executes: as the RING subunit it delivers ubiquitin from a charged E2 to substrates recruited by any cullin-RING receptor. Reason: Core process, supported by IDA in multiple reconstituted CRLs, by the PAINT inference at the RING-box node, and by the UniProt pathway assignment (protein modification; protein ubiquitination). Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000129805 Β· PANTHER:PTN000129805 SUPPORTS TRANSFER RING-box family node spanning RBX1, RBX2/RNF7 and APC11; the descendant experimental evidence includes human RBX1 itself, mouse Rbx1, fly Roc1a/Roc1b and yeast Hrt1/Rbx1 and Apc11, so the function is inherited rather than lineage-specific. Supporting Evidence: file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0016567 protein ubiquitination | IDA PMID:15103331 Phosphorylation-dependent degradation of c-Myc is mediated b... | ACCEPT | Summary: Protein ubiquitination is the process RBX1 executes: as the RING subunit it delivers ubiquitin from a charged E2 to substrates recruited by any cullin-RING receptor. Reason: Core process, supported by IDA in multiple reconstituted CRLs, by the PAINT inference at the RING-box node, and by the UniProt pathway assignment (protein modification; protein ubiquitination). Supporting Evidence: PMID:15103331 The SCF complex consists of four components: the invariable subunits Skp1, Cul1 (also known as Cdc53) and Rbx1 (Roc1, Hrt1) and a variable F-box protein that serves as a receptor for target proteins and thereby determines target specificity ( Elledge and Harper, 1998 ; file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0016567 protein ubiquitination | IDA PMID:17543862 A Cul3-based E3 ligase removes Aurora B from mitotic chromos... | ACCEPT | Summary: Protein ubiquitination is the process RBX1 executes: as the RING subunit it delivers ubiquitin from a charged E2 to substrates recruited by any cullin-RING receptor. Reason: Core process, supported by IDA in multiple reconstituted CRLs, by the PAINT inference at the RING-box node, and by the UniProt pathway assignment (protein modification; protein ubiquitination). Supporting Evidence: PMID:17543862 Moreover, Aurora B is ubiquitylated in a Cul3-dependent manner in vivo, and by reconstituted Cul3/KLHL9/KLHL13 ligase in vitro. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0016567 protein ubiquitination | IDA PMID:20389280 The Cullin 3 substrate adaptor KLHL20 mediates DAPK ubiquiti... | ACCEPT | Summary: Protein ubiquitination is the process RBX1 executes: as the RING subunit it delivers ubiquitin from a charged E2 to substrates recruited by any cullin-RING receptor. Reason: Core process, supported by IDA in multiple reconstituted CRLs, by the PAINT inference at the RING-box node, and by the UniProt pathway assignment (protein modification; protein ubiquitination). Supporting Evidence: PMID:20389280 The KLHL20-Cul3-ROC1 E3 ligase complex promotes DAPK polyubiquitination, thereby inducing the proteasomal degradation of DAPK. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0016567 protein ubiquitination | IDA PMID:34526721 Structural basis of human transcription-DNA repair coupling. | ACCEPT | Summary: Protein ubiquitination is the process RBX1 executes: as the RING subunit it delivers ubiquitin from a charged E2 to substrates recruited by any cullin-RING receptor. Reason: Core process, supported by IDA in multiple reconstituted CRLs, by the PAINT inference at the RING-box node, and by the UniProt pathway assignment (protein modification; protein ubiquitination). Supporting Evidence: PMID:34526721 RBX1 and the E2 enzymeβdonor ubiquitin complex were modelled as described in the Methods. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0016567 protein ubiquitination | IEA GO_REF:0000120 | ACCEPT | Summary: Protein ubiquitination is the process RBX1 executes: as the RING subunit it delivers ubiquitin from a charged E2 to substrates recruited by any cullin-RING receptor. Reason: Core process, supported by IDA in multiple reconstituted CRLs, by the PAINT inference at the RING-box node, and by the UniProt pathway assignment (protein modification; protein ubiquitination). Supporting Evidence: file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0016567 protein ubiquitination | IPI PMID:14739464 Human De-etiolated-1 regulates c-Jun by assembling a CUL4A u... | ACCEPT | Summary: Protein ubiquitination is the process RBX1 executes: as the RING subunit it delivers ubiquitin from a charged E2 to substrates recruited by any cullin-RING receptor. Reason: Core process, supported by IDA in multiple reconstituted CRLs, by the PAINT inference at the RING-box node, and by the UniProt pathway assignment (protein modification; protein ubiquitination). Supporting Evidence: PMID:14739464 Human De-etiolated-1 regulates c-Jun by assembling a CUL4A ubiquitin ligase. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0019005 SCF ubiquitin ligase complex | IDA PMID:11956208 The novel human DNA helicase hFBH1 is an F-box protein. | ACCEPT | Summary: RBX1 is an invariant subunit of SCF (SKP1-CUL1-F-box-RBX1) ligases; with CUL1 it forms the catalytic core that all ~70 F-box receptors plug into. Reason: Core complex membership, established structurally (the CUL1-RBX1-SKP1-SKP2 crystal structure) and in every SCF reconstitution cited here. Supporting Evidence: PMID:11956208 The hFBH1 enzyme interacted with human SKP1 and formed an SCF (SKP1/Cullin/F-box) complex together with human Cullin and ROC1. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0019005 SCF ubiquitin ligase complex | IDA PMID:15103331 Phosphorylation-dependent degradation of c-Myc is mediated b... | ACCEPT | Summary: RBX1 is an invariant subunit of SCF (SKP1-CUL1-F-box-RBX1) ligases; with CUL1 it forms the catalytic core that all ~70 F-box receptors plug into. Reason: Core complex membership, established structurally (the CUL1-RBX1-SKP1-SKP2 crystal structure) and in every SCF reconstitution cited here. Supporting Evidence: PMID:15103331 The SCF complex consists of four components: the invariable subunits Skp1, Cul1 (also known as Cdc53) and Rbx1 (Roc1, Hrt1) and a variable F-box protein that serves as a receptor for target proteins and thereby determines target specificity ( Elledge and Harper, 1998 ; file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0019005 SCF ubiquitin ligase complex | IDA PMID:16705181 Multisite protein kinase A and glycogen synthase kinase 3bet... | ACCEPT | Summary: RBX1 is an invariant subunit of SCF (SKP1-CUL1-F-box-RBX1) ligases; with CUL1 it forms the catalytic core that all ~70 F-box receptors plug into. Reason: Core complex membership, established structurally (the CUL1-RBX1-SKP1-SKP2 crystal structure) and in every SCF reconstitution cited here. Supporting Evidence: PMID:16705181 Multisite protein kinase A and glycogen synthase kinase 3beta phosphorylation leads to Gli3 ubiquitination by SCFbetaTrCP. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0019005 SCF ubiquitin ligase complex | IDA PMID:21572392 SCFFBXLΒΉβ΅ regulates BMP signalling by directing the degradat... | ACCEPT | Summary: RBX1 is an invariant subunit of SCF (SKP1-CUL1-F-box-RBX1) ligases; with CUL1 it forms the catalytic core that all ~70 F-box receptors plug into. Reason: Core complex membership, established structurally (the CUL1-RBX1-SKP1-SKP2 crystal structure) and in every SCF reconstitution cited here. Supporting Evidence: PMID:21572392 Here, we report that F-box and LRR domain-containing protein 15 (FBXL15), an F-box protein of the FBXL family, forms an Skp1-Cullin1-F-box protein-Roc1 (SCF) FBXL15 ubiquitin ligase complex and targets Smurf1 for ubiquitination and proteasomal degradation. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0019005 SCF ubiquitin ligase complex | IDA PMID:23263282 SCFFbxo9 and CK2 direct the cellular response to growth fact... | ACCEPT | Summary: RBX1 is an invariant subunit of SCF (SKP1-CUL1-F-box-RBX1) ligases; with CUL1 it forms the catalytic core that all ~70 F-box receptors plug into. Reason: Core complex membership, established structurally (the CUL1-RBX1-SKP1-SKP2 crystal structure) and in every SCF reconstitution cited here. Supporting Evidence: PMID:23263282 SCFFbxo9 and CK2 direct the cellular response to growth factor withdrawal via Tel2/Tti1 degradation and promote survival in multiple myeloma. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0019005 SCF ubiquitin ligase complex | IDA PMID:25585578 FBH1 influences DNA replication fork stability and homologou... | ACCEPT | Summary: RBX1 is an invariant subunit of SCF (SKP1-CUL1-F-box-RBX1) ligases; with CUL1 it forms the catalytic core that all ~70 F-box receptors plug into. Reason: Core complex membership, established structurally (the CUL1-RBX1-SKP1-SKP2 crystal structure) and in every SCF reconstitution cited here. Supporting Evidence: PMID:25585578 Here we report that the central player in HR, RAD51, is ubiquitylated by the SCF(FBH1) complex. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0019005 SCF ubiquitin ligase complex | IEA GO_REF:0000120 | ACCEPT | Summary: RBX1 is an invariant subunit of SCF (SKP1-CUL1-F-box-RBX1) ligases; with CUL1 it forms the catalytic core that all ~70 F-box receptors plug into. Reason: Core complex membership, established structurally (the CUL1-RBX1-SKP1-SKP2 crystal structure) and in every SCF reconstitution cited here. Supporting Evidence: file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0019005 SCF ubiquitin ligase complex | IPI PMID:11961546 Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin liga... | ACCEPT | Summary: RBX1 is an invariant subunit of SCF (SKP1-CUL1-F-box-RBX1) ligases; with CUL1 it forms the catalytic core that all ~70 F-box receptors plug into. Reason: Core complex membership, established structurally (the CUL1-RBX1-SKP1-SKP2 crystal structure) and in every SCF reconstitution cited here. Supporting Evidence: PMID:11961546 Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0019005 SCF ubiquitin ligase complex | IPI PMID:17098746 FBXO11 promotes the Neddylation of p53 and inhibits its tran... | ACCEPT | Summary: RBX1 is an invariant subunit of SCF (SKP1-CUL1-F-box-RBX1) ligases; with CUL1 it forms the catalytic core that all ~70 F-box receptors plug into. Reason: Core complex membership, established structurally (the CUL1-RBX1-SKP1-SKP2 crystal structure) and in every SCF reconstitution cited here. Supporting Evidence: PMID:17098746 It is unclear how the modular SCF complex, which comprises three constant subunits, Skp1, Cullin1, Roc1, and a variable substrate-binding F-box protein could distinguish between Nedd8 and ubiquitin conjugation. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0019005 SCF ubiquitin ligase complex | IPI PMID:19762597 An E3 ligase possessing an iron-responsive hemerythrin domai... | ACCEPT | Summary: RBX1 is an invariant subunit of SCF (SKP1-CUL1-F-box-RBX1) ligases; with CUL1 it forms the catalytic core that all ~70 F-box receptors plug into. Reason: Core complex membership, established structurally (the CUL1-RBX1-SKP1-SKP2 crystal structure) and in every SCF reconstitution cited here. Supporting Evidence: PMID:19762597 Degradation of FBXL5 would then preclude the assembly of the SCF complex allowing IRP2 to accumulate and bind IREs. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0019005 SCF ubiquitin ligase complex | IPI PMID:21572392 SCFFBXLΒΉβ΅ regulates BMP signalling by directing the degradat... | ACCEPT | Summary: RBX1 is an invariant subunit of SCF (SKP1-CUL1-F-box-RBX1) ligases; with CUL1 it forms the catalytic core that all ~70 F-box receptors plug into. Reason: Core complex membership, established structurally (the CUL1-RBX1-SKP1-SKP2 crystal structure) and in every SCF reconstitution cited here. Supporting Evidence: PMID:21572392 Here, we report that F-box and LRR domain-containing protein 15 (FBXL15), an F-box protein of the FBXL family, forms an Skp1-Cullin1-F-box protein-Roc1 (SCF) FBXL15 ubiquitin ligase complex and targets Smurf1 for ubiquitination and proteasomal degradation. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0019005 SCF ubiquitin ligase complex | IPI PMID:33692209 KDM2B Overexpression Facilitates Lytic De Novo KSHV Infectio... | ACCEPT | Summary: RBX1 is an invariant subunit of SCF (SKP1-CUL1-F-box-RBX1) ligases; with CUL1 it forms the catalytic core that all ~70 F-box receptors plug into. Reason: Core complex membership, established structurally (the CUL1-RBX1-SKP1-SKP2 crystal structure) and in every SCF reconstitution cited here. Supporting Evidence: PMID:33692209 CUL1 acts as the scaffold protein in the SCF complex recruiting ROC1, which is the E3 ubiquitin ligase component of SCF ( 22 ). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0019005 SCF ubiquitin ligase complex | ISS GO_REF:0000024 | ACCEPT | Summary: RBX1 is an invariant subunit of SCF (SKP1-CUL1-F-box-RBX1) ligases; with CUL1 it forms the catalytic core that all ~70 F-box receptors plug into. Reason: Core complex membership, established structurally (the CUL1-RBX1-SKP1-SKP2 crystal structure) and in every SCF reconstitution cited here. Supporting Evidence: file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0019005 SCF ubiquitin ligase complex | NAS PMID:15520277 Systematic analysis and nomenclature of mammalian F-box prot... | ACCEPT | Summary: RBX1 is an invariant subunit of SCF (SKP1-CUL1-F-box-RBX1) ligases; with CUL1 it forms the catalytic core that all ~70 F-box receptors plug into. Reason: Core complex membership, established structurally (the CUL1-RBX1-SKP1-SKP2 crystal structure) and in every SCF reconstitution cited here. Supporting Evidence: PMID:15520277 CUL1 interacts with RBX1 through its C terminus and with SKP1 through its N terminus. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0019005 SCF ubiquitin ligase complex | NAS PMID:20498703 Lamin A rod domain mutants target heterochromatin protein 1a... | ACCEPT | Summary: RBX1 is an invariant subunit of SCF (SKP1-CUL1-F-box-RBX1) ligases; with CUL1 it forms the catalytic core that all ~70 F-box receptors plug into. Reason: Core complex membership, established structurally (the CUL1-RBX1-SKP1-SKP2 crystal structure) and in every SCF reconstitution cited here. Supporting Evidence: PMID:20498703 On the other hand, moderate induction of the HECW2 ligase and RNF123 RING finger protein was observed with G232E and R386K-expressing cells respectively (but not both). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0019005 SCF ubiquitin ligase complex | NAS PMID:20596027 SCF(Cyclin F) controls centrosome homeostasis and mitotic fi... | ACCEPT | Summary: RBX1 is an invariant subunit of SCF (SKP1-CUL1-F-box-RBX1) ligases; with CUL1 it forms the catalytic core that all ~70 F-box receptors plug into. Reason: Core complex membership, established structurally (the CUL1-RBX1-SKP1-SKP2 crystal structure) and in every SCF reconstitution cited here. Supporting Evidence: PMID:20596027 SCF(Cyclin F) controls centrosome homeostasis and mitotic fidelity through CP110 degradation. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0019005 SCF ubiquitin ligase complex | NAS PMID:26171402 The Human IL-22 Receptor Is Regulated through the Action of ... | ACCEPT | Summary: RBX1 is an invariant subunit of SCF (SKP1-CUL1-F-box-RBX1) ligases; with CUL1 it forms the catalytic core that all ~70 F-box receptors plug into. Reason: Core complex membership, established structurally (the CUL1-RBX1-SKP1-SKP2 crystal structure) and in every SCF reconstitution cited here. Supporting Evidence: PMID:26171402 Skp-1, Rbx1, and Cul-1 were from Abnova (Taipei, Taiwan), and TnT Coupled Reticulocyte was from Promega (Madison, WI). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0019005 SCF ubiquitin ligase complex | NAS PMID:34445249 The SCF Complex Is Essential to Maintain Genome and Chromoso... | ACCEPT | Summary: RBX1 is an invariant subunit of SCF (SKP1-CUL1-F-box-RBX1) ligases; with CUL1 it forms the catalytic core that all ~70 F-box receptors plug into. Reason: Core complex membership, established structurally (the CUL1-RBX1-SKP1-SKP2 crystal structure) and in every SCF reconstitution cited here. 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. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0019005 SCF ubiquitin ligase complex | NAS PMID:35982156 Structure of CRL7(FBXW8) reveals coupling with CUL1-RBX1/ROC... | ACCEPT | Summary: RBX1 is an invariant subunit of SCF (SKP1-CUL1-F-box-RBX1) ligases; with CUL1 it forms the catalytic core that all ~70 F-box receptors plug into. Reason: Core complex membership, established structurally (the CUL1-RBX1-SKP1-SKP2 crystal structure) and in every SCF reconstitution cited here. Supporting Evidence: PMID:35982156 Several observations are consistent with CUL7 recruiting TP53 for neddylated CUL1βRBX1-mediated ubiquitination. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0019788 NEDD8 transferase activity | TAS Reactome:R-HSA-8952618 | ACCEPT | Summary: RBX1 is the RING E3 of the cullin neddylation reaction, binding UBE2M~NEDD8 and transferring NEDD8 to the conserved lysine of CUL1-CUL4. Reason: Core function, supported by structure (the trapped RBX1-UBC12~NEDD8-CUL1-DCN1 intermediate) and by UniProt's EC 2.3.2.32 assignment; RBX2/RNF7-UBE2F provides the parallel activity for CUL5. Supporting Evidence: Reactome:R-HSA-8952618 UBE2M transfers NEDD8 to lysine 720 of CUL1 in the CRL E3 ubiquitin ligase complex (Hori et al, 1999; Duda et al, 2008). file:human/RBX1/RBX1-uniprot.txt Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 also works with UBE2M~NEDD8 to neddylate cullins and activate CRLs. |
| GO:0019788 NEDD8 transferase activity | TAS Reactome:R-HSA-8952626 | ACCEPT | Summary: RBX1 is the RING E3 of the cullin neddylation reaction, binding UBE2M~NEDD8 and transferring NEDD8 to the conserved lysine of CUL1-CUL4. Reason: Core function, supported by structure (the trapped RBX1-UBC12~NEDD8-CUL1-DCN1 intermediate) and by UniProt's EC 2.3.2.32 assignment; RBX2/RNF7-UBE2F provides the parallel activity for CUL5. Supporting Evidence: Reactome:R-HSA-8952626 UBE2M transfers NEDD8 to lysine 689 of CUL2 in the E3 ligase complex (Hori et al, 1999; Duda et al, 2008). file:human/RBX1/RBX1-uniprot.txt Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 also works with UBE2M~NEDD8 to neddylate cullins and activate CRLs. |
| GO:0019788 NEDD8 transferase activity | TAS Reactome:R-HSA-8952631 | ACCEPT | Summary: RBX1 is the RING E3 of the cullin neddylation reaction, binding UBE2M~NEDD8 and transferring NEDD8 to the conserved lysine of CUL1-CUL4. Reason: Core function, supported by structure (the trapped RBX1-UBC12~NEDD8-CUL1-DCN1 intermediate) and by UniProt's EC 2.3.2.32 assignment; RBX2/RNF7-UBE2F provides the parallel activity for CUL5. Supporting Evidence: Reactome:R-HSA-8952631 UBE2M transfers NEDD8 to lysine 712 of CUL3 in the E3 ligase complex (Hori et al, 1999; Duda et al, 2008). file:human/RBX1/RBX1-uniprot.txt Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 also works with UBE2M~NEDD8 to neddylate cullins and activate CRLs. |
| GO:0019788 NEDD8 transferase activity | TAS Reactome:R-HSA-8952638 | ACCEPT | Summary: RBX1 is the RING E3 of the cullin neddylation reaction, binding UBE2M~NEDD8 and transferring NEDD8 to the conserved lysine of CUL1-CUL4. Reason: Core function, supported by structure (the trapped RBX1-UBC12~NEDD8-CUL1-DCN1 intermediate) and by UniProt's EC 2.3.2.32 assignment; RBX2/RNF7-UBE2F provides the parallel activity for CUL5. Supporting Evidence: Reactome:R-HSA-8952638 UBE2M transfers NEDD8 to lysine 705 of CUL4A and lysine 859 of CUL4B (Hori et al, 1999; Duda et al, 2008). file:human/RBX1/RBX1-uniprot.txt Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 also works with UBE2M~NEDD8 to neddylate cullins and activate CRLs. |
| GO:0030174 regulation of DNA-templated DNA replication initiation | NAS PMID:16861906 L2DTL/CDT2 interacts with the CUL4/DDB1 complex and PCNA and... | KEEP AS NON CORE | Summary: CRL4(CDT2) and SCF(SKP2) ligases containing RBX1 destroy CDT1 in S phase and after DNA damage, restraining re-licensing of replication origins. Reason: Real but receptor-defined; RBX1's direct role is the ubiquitination. Kept as non-core. Supporting Evidence: PMID:16861906 Our studies suggest that L2DTL and PCNA interact with CUL4/DDB1 complexes and are involved in CDT1 degradation after DNA damage. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0030510 regulation of BMP signaling pathway | NAS PMID:21572392 SCFFBXLΒΉβ΅ regulates BMP signalling by directing the degradat... | KEEP AS NON CORE | Summary: SCF(FBXL15) containing RBX1 degrades the HECT ligase SMURF1, positively regulating BMP signalling. Reason: Receptor-specific pathway output; non-core. Supporting Evidence: PMID:21572392 Here, we report that F-box and LRR domain-containing protein 15 (FBXL15), an F-box protein of the FBXL family, forms an Skp1-Cullin1-F-box protein-Roc1 (SCF) FBXL15 ubiquitin ligase complex and targets Smurf1 for ubiquitination and proteasomal degradation. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0031146 SCF-dependent proteasomal ubiquitin-dependent protein catabolic process | IDA PMID:10230407 ROC1, a homolog of APC11, represents a family of cullin part... | ACCEPT | Summary: SCF-dependent proteasomal degradation: RBX1 provides the ligase activity for SCF(SKP2) (p27/CDKN1B), SCF(beta-TrCP) (IkappaB-alpha, beta-catenin, DEPTOR), SCF(FBXW7) (c-Myc, NOTCH), SCF(cyclin F), SCF(FBXL3/FBXL5) and many other F-box receptors. Reason: Core process for the shared catalytic module: the F-box protein selects the substrate, but RBX1 performs the ubiquitin transfer that commits it to the proteasome. Supporting Evidence: PMID:10230407 ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0031146 SCF-dependent proteasomal ubiquitin-dependent protein catabolic process | IDA PMID:15103331 Phosphorylation-dependent degradation of c-Myc is mediated b... | ACCEPT | Summary: SCF-dependent proteasomal degradation: RBX1 provides the ligase activity for SCF(SKP2) (p27/CDKN1B), SCF(beta-TrCP) (IkappaB-alpha, beta-catenin, DEPTOR), SCF(FBXW7) (c-Myc, NOTCH), SCF(cyclin F), SCF(FBXL3/FBXL5) and many other F-box receptors. Reason: Core process for the shared catalytic module: the F-box protein selects the substrate, but RBX1 performs the ubiquitin transfer that commits it to the proteasome. Supporting Evidence: PMID:15103331 The SCF complex consists of four components: the invariable subunits Skp1, Cul1 (also known as Cdc53) and Rbx1 (Roc1, Hrt1) and a variable F-box protein that serves as a receptor for target proteins and thereby determines target specificity ( Elledge and Harper, 1998 ; file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0031146 SCF-dependent proteasomal ubiquitin-dependent protein catabolic process | IDA PMID:19762597 An E3 ligase possessing an iron-responsive hemerythrin domai... | ACCEPT | Summary: SCF-dependent proteasomal degradation: RBX1 provides the ligase activity for SCF(SKP2) (p27/CDKN1B), SCF(beta-TrCP) (IkappaB-alpha, beta-catenin, DEPTOR), SCF(FBXW7) (c-Myc, NOTCH), SCF(cyclin F), SCF(FBXL3/FBXL5) and many other F-box receptors. Reason: Core process for the shared catalytic module: the F-box protein selects the substrate, but RBX1 performs the ubiquitin transfer that commits it to the proteasome. Supporting Evidence: PMID:19762597 Degradation of FBXL5 would then preclude the assembly of the SCF complex allowing IRP2 to accumulate and bind IREs. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0031146 SCF-dependent proteasomal ubiquitin-dependent protein catabolic process | IDA PMID:22017875 mTOR drives its own activation via SCF(Ξ²TrCP)-dependent degr... | ACCEPT | Summary: SCF-dependent proteasomal degradation: RBX1 provides the ligase activity for SCF(SKP2) (p27/CDKN1B), SCF(beta-TrCP) (IkappaB-alpha, beta-catenin, DEPTOR), SCF(FBXW7) (c-Myc, NOTCH), SCF(cyclin F), SCF(FBXL3/FBXL5) and many other F-box receptors. Reason: Core process for the shared catalytic module: the F-box protein selects the substrate, but RBX1 performs the ubiquitin transfer that commits it to the proteasome. Supporting Evidence: PMID:22017875 To purify SCFΞ²-TRCP complex, 293T cells were transfected with vectors encoding GST-Ξ²-TRCP1, Myc-Cul-1, Myc-Skp1, and HA-Rbx1. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0031146 SCF-dependent proteasomal ubiquitin-dependent protein catabolic process | IDA PMID:22017876 DEPTOR, an mTOR inhibitor, is a physiological substrate of S... | ACCEPT | Summary: SCF-dependent proteasomal degradation: RBX1 provides the ligase activity for SCF(SKP2) (p27/CDKN1B), SCF(beta-TrCP) (IkappaB-alpha, beta-catenin, DEPTOR), SCF(FBXW7) (c-Myc, NOTCH), SCF(cyclin F), SCF(FBXL3/FBXL5) and many other F-box receptors. Reason: Core process for the shared catalytic module: the F-box protein selects the substrate, but RBX1 performs the ubiquitin transfer that commits it to the proteasome. Supporting Evidence: PMID:22017876 Here we report that DEPTOR is a physiological substrate of SCF(Ξ²TrCP) E3 ligase for targeted degradation. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0031146 SCF-dependent proteasomal ubiquitin-dependent protein catabolic process | IDA PMID:24936062 F-box only protein 31 (FBXO31) negatively regulates p38 mito... | ACCEPT | Summary: SCF-dependent proteasomal degradation: RBX1 provides the ligase activity for SCF(SKP2) (p27/CDKN1B), SCF(beta-TrCP) (IkappaB-alpha, beta-catenin, DEPTOR), SCF(FBXW7) (c-Myc, NOTCH), SCF(cyclin F), SCF(FBXL3/FBXL5) and many other F-box receptors. Reason: Core process for the shared catalytic module: the F-box protein selects the substrate, but RBX1 performs the ubiquitin transfer that commits it to the proteasome. Supporting Evidence: PMID:24936062 Here we report that the accumulation of F-box only protein 31 (FBXO31), a component of Skp1 Β· Cul1 Β· F-box protein E3 ligase, negatively regulated p38 activation in cancer cells upon genotoxic stresses. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0031146 SCF-dependent proteasomal ubiquitin-dependent protein catabolic process | IDA PMID:26124108 F-box protein FBXO31 directs degradation of MDM2 to facilita... | ACCEPT | Summary: SCF-dependent proteasomal degradation: RBX1 provides the ligase activity for SCF(SKP2) (p27/CDKN1B), SCF(beta-TrCP) (IkappaB-alpha, beta-catenin, DEPTOR), SCF(FBXW7) (c-Myc, NOTCH), SCF(cyclin F), SCF(FBXL3/FBXL5) and many other F-box receptors. Reason: Core process for the shared catalytic module: the F-box protein selects the substrate, but RBX1 performs the ubiquitin transfer that commits it to the proteasome. Supporting Evidence: PMID:26124108 Following DNA damage, MDM2 is degraded rapidly, resulting in increased p53 stability. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0031146 SCF-dependent proteasomal ubiquitin-dependent protein catabolic process | IDA PMID:30171069 The SCF(FBXO46) ubiquitin ligase complex mediates degradatio... | ACCEPT | Summary: SCF-dependent proteasomal degradation: RBX1 provides the ligase activity for SCF(SKP2) (p27/CDKN1B), SCF(beta-TrCP) (IkappaB-alpha, beta-catenin, DEPTOR), SCF(FBXW7) (c-Myc, NOTCH), SCF(cyclin F), SCF(FBXL3/FBXL5) and many other F-box receptors. Reason: Core process for the shared catalytic module: the F-box protein selects the substrate, but RBX1 performs the ubiquitin transfer that commits it to the proteasome. Supporting Evidence: PMID:30171069 The SCF(FBXO46) ubiquitin ligase complex mediates degradation of the tumor suppressor FBXO31 and thereby prevents premature cellular senescence. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0031146 SCF-dependent proteasomal ubiquitin-dependent protein catabolic process | IDA PMID:36608670 A central role for regulated protein stability in the contro... | ACCEPT | Summary: SCF-dependent proteasomal degradation: RBX1 provides the ligase activity for SCF(SKP2) (p27/CDKN1B), SCF(beta-TrCP) (IkappaB-alpha, beta-catenin, DEPTOR), SCF(FBXW7) (c-Myc, NOTCH), SCF(cyclin F), SCF(FBXL3/FBXL5) and many other F-box receptors. Reason: Core process for the shared catalytic module: the F-box protein selects the substrate, but RBX1 performs the ubiquitin transfer that commits it to the proteasome. Supporting Evidence: PMID:36608670 The pulse reaction was quenched for 5 minutes on ice with 50 mM EDTA, and *ubiquitin was chased from UBE2D2 to SCF substrates. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0031146 SCF-dependent proteasomal ubiquitin-dependent protein catabolic process | IEA GO_REF:0000120 | ACCEPT | Summary: SCF-dependent proteasomal degradation: RBX1 provides the ligase activity for SCF(SKP2) (p27/CDKN1B), SCF(beta-TrCP) (IkappaB-alpha, beta-catenin, DEPTOR), SCF(FBXW7) (c-Myc, NOTCH), SCF(cyclin F), SCF(FBXL3/FBXL5) and many other F-box receptors. Reason: Core process for the shared catalytic module: the F-box protein selects the substrate, but RBX1 performs the ubiquitin transfer that commits it to the proteasome. Supporting Evidence: file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0031146 SCF-dependent proteasomal ubiquitin-dependent protein catabolic process | ISS GO_REF:0000024 | ACCEPT | Summary: SCF-dependent proteasomal degradation: RBX1 provides the ligase activity for SCF(SKP2) (p27/CDKN1B), SCF(beta-TrCP) (IkappaB-alpha, beta-catenin, DEPTOR), SCF(FBXW7) (c-Myc, NOTCH), SCF(cyclin F), SCF(FBXL3/FBXL5) and many other F-box receptors. Reason: Core process for the shared catalytic module: the F-box protein selects the substrate, but RBX1 performs the ubiquitin transfer that commits it to the proteasome. Supporting Evidence: file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0031146 SCF-dependent proteasomal ubiquitin-dependent protein catabolic process | NAS PMID:11961546 Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin liga... | ACCEPT | Summary: SCF-dependent proteasomal degradation: RBX1 provides the ligase activity for SCF(SKP2) (p27/CDKN1B), SCF(beta-TrCP) (IkappaB-alpha, beta-catenin, DEPTOR), SCF(FBXW7) (c-Myc, NOTCH), SCF(cyclin F), SCF(FBXL3/FBXL5) and many other F-box receptors. Reason: Core process for the shared catalytic module: the F-box protein selects the substrate, but RBX1 performs the ubiquitin transfer that commits it to the proteasome. Supporting Evidence: PMID:11961546 Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0031146 SCF-dependent proteasomal ubiquitin-dependent protein catabolic process | NAS PMID:15520277 Systematic analysis and nomenclature of mammalian F-box prot... | ACCEPT | Summary: SCF-dependent proteasomal degradation: RBX1 provides the ligase activity for SCF(SKP2) (p27/CDKN1B), SCF(beta-TrCP) (IkappaB-alpha, beta-catenin, DEPTOR), SCF(FBXW7) (c-Myc, NOTCH), SCF(cyclin F), SCF(FBXL3/FBXL5) and many other F-box receptors. Reason: Core process for the shared catalytic module: the F-box protein selects the substrate, but RBX1 performs the ubiquitin transfer that commits it to the proteasome. Supporting Evidence: PMID:15520277 CUL1 interacts with RBX1 through its C terminus and with SKP1 through its N terminus. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0031146 SCF-dependent proteasomal ubiquitin-dependent protein catabolic process | NAS PMID:20498703 Lamin A rod domain mutants target heterochromatin protein 1a... | ACCEPT | Summary: SCF-dependent proteasomal degradation: RBX1 provides the ligase activity for SCF(SKP2) (p27/CDKN1B), SCF(beta-TrCP) (IkappaB-alpha, beta-catenin, DEPTOR), SCF(FBXW7) (c-Myc, NOTCH), SCF(cyclin F), SCF(FBXL3/FBXL5) and many other F-box receptors. Reason: Core process for the shared catalytic module: the F-box protein selects the substrate, but RBX1 performs the ubiquitin transfer that commits it to the proteasome. Supporting Evidence: PMID:20498703 On the other hand, moderate induction of the HECW2 ligase and RNF123 RING finger protein was observed with G232E and R386K-expressing cells respectively (but not both). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0031146 SCF-dependent proteasomal ubiquitin-dependent protein catabolic process | NAS PMID:20596027 SCF(Cyclin F) controls centrosome homeostasis and mitotic fi... | ACCEPT | Summary: SCF-dependent proteasomal degradation: RBX1 provides the ligase activity for SCF(SKP2) (p27/CDKN1B), SCF(beta-TrCP) (IkappaB-alpha, beta-catenin, DEPTOR), SCF(FBXW7) (c-Myc, NOTCH), SCF(cyclin F), SCF(FBXL3/FBXL5) and many other F-box receptors. Reason: Core process for the shared catalytic module: the F-box protein selects the substrate, but RBX1 performs the ubiquitin transfer that commits it to the proteasome. Supporting Evidence: PMID:20596027 SCF(Cyclin F) controls centrosome homeostasis and mitotic fidelity through CP110 degradation. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0031146 SCF-dependent proteasomal ubiquitin-dependent protein catabolic process | NAS PMID:21572392 SCFFBXLΒΉβ΅ regulates BMP signalling by directing the degradat... | ACCEPT | Summary: SCF-dependent proteasomal degradation: RBX1 provides the ligase activity for SCF(SKP2) (p27/CDKN1B), SCF(beta-TrCP) (IkappaB-alpha, beta-catenin, DEPTOR), SCF(FBXW7) (c-Myc, NOTCH), SCF(cyclin F), SCF(FBXL3/FBXL5) and many other F-box receptors. Reason: Core process for the shared catalytic module: the F-box protein selects the substrate, but RBX1 performs the ubiquitin transfer that commits it to the proteasome. Supporting Evidence: PMID:21572392 Here, we report that F-box and LRR domain-containing protein 15 (FBXL15), an F-box protein of the FBXL family, forms an Skp1-Cullin1-F-box protein-Roc1 (SCF) FBXL15 ubiquitin ligase complex and targets Smurf1 for ubiquitination and proteasomal degradation. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0031146 SCF-dependent proteasomal ubiquitin-dependent protein catabolic process | NAS PMID:26171402 The Human IL-22 Receptor Is Regulated through the Action of ... | ACCEPT | Summary: SCF-dependent proteasomal degradation: RBX1 provides the ligase activity for SCF(SKP2) (p27/CDKN1B), SCF(beta-TrCP) (IkappaB-alpha, beta-catenin, DEPTOR), SCF(FBXW7) (c-Myc, NOTCH), SCF(cyclin F), SCF(FBXL3/FBXL5) and many other F-box receptors. Reason: Core process for the shared catalytic module: the F-box protein selects the substrate, but RBX1 performs the ubiquitin transfer that commits it to the proteasome. Supporting Evidence: PMID:26171402 Skp-1, Rbx1, and Cul-1 were from Abnova (Taipei, Taiwan), and TnT Coupled Reticulocyte was from Promega (Madison, WI). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0031146 SCF-dependent proteasomal ubiquitin-dependent protein catabolic process | NAS PMID:33234069 The FBXL family of F-box proteins: variations on a theme. | ACCEPT | Summary: SCF-dependent proteasomal degradation: RBX1 provides the ligase activity for SCF(SKP2) (p27/CDKN1B), SCF(beta-TrCP) (IkappaB-alpha, beta-catenin, DEPTOR), SCF(FBXW7) (c-Myc, NOTCH), SCF(cyclin F), SCF(FBXL3/FBXL5) and many other F-box receptors. Reason: Core process for the shared catalytic module: the F-box protein selects the substrate, but RBX1 performs the ubiquitin transfer that commits it to the proteasome. Supporting Evidence: PMID:33234069 Rbx1 engages an E2 enzyme conjugated to activated ubiquitin, thus enabling the direct transfer of ubiquitin to the substrate (figure 1). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| 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: SCF-dependent proteasomal degradation: RBX1 provides the ligase activity for SCF(SKP2) (p27/CDKN1B), SCF(beta-TrCP) (IkappaB-alpha, beta-catenin, DEPTOR), SCF(FBXW7) (c-Myc, NOTCH), SCF(cyclin F), SCF(FBXL3/FBXL5) and many other F-box receptors. Reason: Core process for the shared catalytic module: the F-box protein selects the substrate, but RBX1 performs the ubiquitin transfer that commits it to the proteasome. 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. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0031146 SCF-dependent proteasomal ubiquitin-dependent protein catabolic process | NAS PMID:35982156 Structure of CRL7(FBXW8) reveals coupling with CUL1-RBX1/ROC... | ACCEPT | Summary: SCF-dependent proteasomal degradation: RBX1 provides the ligase activity for SCF(SKP2) (p27/CDKN1B), SCF(beta-TrCP) (IkappaB-alpha, beta-catenin, DEPTOR), SCF(FBXW7) (c-Myc, NOTCH), SCF(cyclin F), SCF(FBXL3/FBXL5) and many other F-box receptors. Reason: Core process for the shared catalytic module: the F-box protein selects the substrate, but RBX1 performs the ubiquitin transfer that commits it to the proteasome. Supporting Evidence: PMID:35982156 Several observations are consistent with CUL7 recruiting TP53 for neddylated CUL1βRBX1-mediated ubiquitination. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0031297 replication fork processing | NAS PMID:30018425 The replication initiation determinant protein (RepID) modul... | KEEP AS NON CORE | Summary: CRL4(DCAF14) and CRL4(RepID/PHIP) ligases containing RBX1 act at stalled replication forks to protect nascent DNA. Reason: Receptor-specific genome-maintenance output; non-core. Supporting Evidence: PMID:30018425 In the absence of RepID, cells rely on the alternative ubiquitin ligase, SKP2-containing SCF, to progress through the cell cycle. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0031297 replication fork processing | NAS PMID:33503431 DCAF14 promotes stalled fork stability to maintain genome in... | KEEP AS NON CORE | Summary: CRL4(DCAF14) and CRL4(RepID/PHIP) ligases containing RBX1 act at stalled replication forks to protect nascent DNA. Reason: Receptor-specific genome-maintenance output; non-core. Supporting Evidence: PMID:33503431 CRL4s utilize DDB1- and CUL4-associated factors (DCAFs) as substrate receptors to recruit substrates for ubiquitination. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0031461 cullin-RING ubiquitin ligase complex | IBA GO_REF:0000033 | ACCEPT | Summary: RBX1 is the RING subunit of cullin-RING ubiquitin ligase complexes generally - the parent statement covering its membership in CRL1 through CRL4, CRL5, CRL7 and CRL9. Reason: Core complex membership; the PAINT inference at the RING-box family node and the direct evidence (including Glomulin binding to the RBX1 RING within CRLs) agree. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000129805 Β· PANTHER:PTN000129805 SUPPORTS TRANSFER RING-box family node spanning RBX1, RBX2/RNF7 and APC11; the descendant experimental evidence includes human RBX1 itself, mouse Rbx1, fly Roc1a/Roc1b and yeast Hrt1/Rbx1 and Apc11, so the function is inherited rather than lineage-specific. Supporting Evidence: file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0031461 cullin-RING ubiquitin ligase complex | IDA PMID:22405651 The glomuvenous malformation protein Glomulin binds Rbx1 and... | ACCEPT | Summary: RBX1 is the RING subunit of cullin-RING ubiquitin ligase complexes generally - the parent statement covering its membership in CRL1 through CRL4, CRL5, CRL7 and CRL9. Reason: Core complex membership; the PAINT inference at the RING-box family node and the direct evidence (including Glomulin binding to the RBX1 RING within CRLs) agree. Supporting Evidence: PMID:22405651 The glomuvenous malformation protein Glomulin binds Rbx1 and regulates cullin RING ligase-mediated turnover of Fbw7. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0031462 Cul2-RING ubiquitin ligase complex | IDA PMID:17636018 ASB4 is a hydroxylation substrate of FIH and promotes vascul... | ACCEPT | Summary: RBX1 is the RING subunit of CRL2 complexes (CUL2-ELOB/ELOC plus a VHL-box receptor such as VHL, LRR1, FEM1A/B/C, PRAME, APPBP2 or KLHDC3). Reason: Core complex membership: VHL-box receptors select CUL2-RBX1 while SOCS-box receptors select CUL5-RBX2, and the CRL2(VHL) and CRL2(APPBP2) structures contain RBX1 directly. Supporting Evidence: PMID:17636018 Like other SOCS box-containing proteins, ASB4 is the substrate recognition molecule of an elongin B/elongin C/cullin/Roc ubiquitin ligase complex that mediates the ubiquitination and degradation of substrate protein(s). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031462 Cul2-RING ubiquitin ligase complex | IDA PMID:35978186 Post-translational control of beige fat biogenesis by PRDM16... | ACCEPT | Summary: RBX1 is the RING subunit of CRL2 complexes (CUL2-ELOB/ELOC plus a VHL-box receptor such as VHL, LRR1, FEM1A/B/C, PRAME, APPBP2 or KLHDC3). Reason: Core complex membership: VHL-box receptors select CUL2-RBX1 while SOCS-box receptors select CUL5-RBX2, and the CRL2(VHL) and CRL2(APPBP2) structures contain RBX1 directly. Supporting Evidence: PMID:35978186 The CUL2βAPPBP2 E3 ligase complex catalyses polyubiquitination of PRDM16. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031462 Cul2-RING ubiquitin ligase complex | IDA PMID:37844242 Molecular basis for C-degron recognition by CRL2(APPBP2) ubi... | ACCEPT | Summary: RBX1 is the RING subunit of CRL2 complexes (CUL2-ELOB/ELOC plus a VHL-box receptor such as VHL, LRR1, FEM1A/B/C, PRAME, APPBP2 or KLHDC3). Reason: Core complex membership: VHL-box receptors select CUL2-RBX1 while SOCS-box receptors select CUL5-RBX2, and the CRL2(VHL) and CRL2(APPBP2) structures contain RBX1 directly. Supporting Evidence: PMID:37844242 Cryo-EM samples were generated by mixing two complexes, APPBP2-EB-EC-Peptide and NEDD8-CUL2ΞΒ·RBX1, in a 1:1 ratio. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031462 Cul2-RING ubiquitin ligase complex | IPI PMID:15601820 VHL-box and SOCS-box domains determine binding specificity f... | ACCEPT | Summary: RBX1 is the RING subunit of CRL2 complexes (CUL2-ELOB/ELOC plus a VHL-box receptor such as VHL, LRR1, FEM1A/B/C, PRAME, APPBP2 or KLHDC3). Reason: Core complex membership: VHL-box receptors select CUL2-RBX1 while SOCS-box receptors select CUL5-RBX2, and the CRL2(VHL) and CRL2(APPBP2) structures contain RBX1 directly. Supporting Evidence: PMID:15601820 VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031462 Cul2-RING ubiquitin ligase complex | IPI PMID:21822215 The tumour antigen PRAME is a subunit of a Cul2 ubiquitin li... | ACCEPT | Summary: RBX1 is the RING subunit of CRL2 complexes (CUL2-ELOB/ELOC plus a VHL-box receptor such as VHL, LRR1, FEM1A/B/C, PRAME, APPBP2 or KLHDC3). Reason: Core complex membership: VHL-box receptors select CUL2-RBX1 while SOCS-box receptors select CUL5-RBX2, and the CRL2(VHL) and CRL2(APPBP2) structures contain RBX1 directly. Supporting Evidence: PMID:21822215 The tumour antigen PRAME is a subunit of a Cul2 ubiquitin ligase and associates with active NFY promoters. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031462 Cul2-RING ubiquitin ligase complex | IPI PMID:28591624 Crystal Structure of the Cul2-Rbx1-EloBC-VHL Ubiquitin Ligas... | ACCEPT | Summary: RBX1 is the RING subunit of CRL2 complexes (CUL2-ELOB/ELOC plus a VHL-box receptor such as VHL, LRR1, FEM1A/B/C, PRAME, APPBP2 or KLHDC3). Reason: Core complex membership: VHL-box receptors select CUL2-RBX1 while SOCS-box receptors select CUL5-RBX2, and the CRL2(VHL) and CRL2(APPBP2) structures contain RBX1 directly. Supporting Evidence: PMID:28591624 Crystal Structure of the Cul2-Rbx1-EloBC-VHL Ubiquitin Ligase Complex. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031462 Cul2-RING ubiquitin ligase complex | NAS PMID:22649776 The Role of Elongin BC-Containing Ubiquitin Ligases. | ACCEPT | Summary: RBX1 is the RING subunit of CRL2 complexes (CUL2-ELOB/ELOC plus a VHL-box receptor such as VHL, LRR1, FEM1A/B/C, PRAME, APPBP2 or KLHDC3). Reason: Core complex membership: VHL-box receptors select CUL2-RBX1 while SOCS-box receptors select CUL5-RBX2, and the CRL2(VHL) and CRL2(APPBP2) structures contain RBX1 directly. Supporting Evidence: PMID:22649776 The S phase kinase-associated protein 1 (Skp1)βCullin 1 (Cul1)βF box protein (SCF) family is a member of the RING finger-containing ubiquitin ligase family (Lipkowitz and Weissman, 2011). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031462 Cul2-RING ubiquitin ligase complex | NAS PMID:29779948 The Eukaryotic Proteome Is Shaped by E3Β Ubiquitin Ligases Ta... | ACCEPT | Summary: RBX1 is the RING subunit of CRL2 complexes (CUL2-ELOB/ELOC plus a VHL-box receptor such as VHL, LRR1, FEM1A/B/C, PRAME, APPBP2 or KLHDC3). Reason: Core complex membership: VHL-box receptors select CUL2-RBX1 while SOCS-box receptors select CUL5-RBX2, and the CRL2(VHL) and CRL2(APPBP2) structures contain RBX1 directly. Supporting Evidence: PMID:29779948 We characterize eight Cullin-RING E3 ubiquitin ligase (CRL) complex adaptors that regulate C-terminal degrons, including six CRL2 and two CRL4 complexes, and computationally implicate multiple non-CRLs in end recognition. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031462 Cul2-RING ubiquitin ligase complex | NAS PMID:33398168 Molecular basis for arginine C-terminal degron recognition b... | ACCEPT | Summary: RBX1 is the RING subunit of CRL2 complexes (CUL2-ELOB/ELOC plus a VHL-box receptor such as VHL, LRR1, FEM1A/B/C, PRAME, APPBP2 or KLHDC3). Reason: Core complex membership: VHL-box receptors select CUL2-RBX1 while SOCS-box receptors select CUL5-RBX2, and the CRL2(VHL) and CRL2(APPBP2) structures contain RBX1 directly. Supporting Evidence: PMID:33398168 Recently, a few classes of C-terminal degrons (C-degrons) that are recognized by dedicated cullin-RING ligases (CRLs) have been identified. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031462 Cul2-RING ubiquitin ligase complex | NAS PMID:34743205 CRL2-KLHDC3 E3 ubiquitin ligase complex suppresses ferroptos... | ACCEPT | Summary: RBX1 is the RING subunit of CRL2 complexes (CUL2-ELOB/ELOC plus a VHL-box receptor such as VHL, LRR1, FEM1A/B/C, PRAME, APPBP2 or KLHDC3). Reason: Core complex membership: VHL-box receptors select CUL2-RBX1 while SOCS-box receptors select CUL5-RBX2, and the CRL2(VHL) and CRL2(APPBP2) structures contain RBX1 directly. Supporting Evidence: PMID:34743205 CRL2-KLHDC3 E3 ubiquitin ligase complex suppresses ferroptosis through promoting p14(ARF) degradation. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031463 Cul3-RING ubiquitin ligase complex | IDA PMID:14528312 Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubi... | ACCEPT | Summary: RBX1 is the RING subunit of BTB-CUL3-RBX1 (BCR/CRL3) ligases formed with BTB-domain receptors such as KEAP1, SPOP, KLHL9/13, KLHL20, KLHL22, KCTD10, KBTBD6/7 and ARMC5. Reason: Core complex membership, reconstituted repeatedly in vitro (Cul3-RBX1 with KEAP1, KLHL12, KLHL20, KLHL22, KBTBD13) and resolved in CRL3 cryo-EM structures. Supporting Evidence: PMID:14528312 Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin ligases. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031463 Cul3-RING ubiquitin ligase complex | IDA PMID:15983046 Ubiquitination of Keap1, a BTB-Kelch substrate adaptor prote... | ACCEPT | Summary: RBX1 is the RING subunit of BTB-CUL3-RBX1 (BCR/CRL3) ligases formed with BTB-domain receptors such as KEAP1, SPOP, KLHL9/13, KLHL20, KLHL22, KCTD10, KBTBD6/7 and ARMC5. Reason: Core complex membership, reconstituted repeatedly in vitro (Cul3-RBX1 with KEAP1, KLHL12, KLHL20, KLHL22, KBTBD13) and resolved in CRL3 cryo-EM structures. Supporting Evidence: PMID:15983046 Keap1 is a BTB-Kelch protein that functions as a substrate adaptor protein for a Cul3-dependent E3 ubiquitin ligase complex. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031463 Cul3-RING ubiquitin ligase complex | IDA PMID:17543862 A Cul3-based E3 ligase removes Aurora B from mitotic chromos... | ACCEPT | Summary: RBX1 is the RING subunit of BTB-CUL3-RBX1 (BCR/CRL3) ligases formed with BTB-domain receptors such as KEAP1, SPOP, KLHL9/13, KLHL20, KLHL22, KCTD10, KBTBD6/7 and ARMC5. Reason: Core complex membership, reconstituted repeatedly in vitro (Cul3-RBX1 with KEAP1, KLHL12, KLHL20, KLHL22, KBTBD13) and resolved in CRL3 cryo-EM structures. Supporting Evidence: PMID:17543862 Moreover, Aurora B is ubiquitylated in a Cul3-dependent manner in vivo, and by reconstituted Cul3/KLHL9/KLHL13 ligase in vitro. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031463 Cul3-RING ubiquitin ligase complex | IDA PMID:19782033 Cullin mediates degradation of RhoA through evolutionarily c... | ACCEPT | Summary: RBX1 is the RING subunit of BTB-CUL3-RBX1 (BCR/CRL3) ligases formed with BTB-domain receptors such as KEAP1, SPOP, KLHL9/13, KLHL20, KLHL22, KCTD10, KBTBD6/7 and ARMC5. Reason: Core complex membership, reconstituted repeatedly in vitro (Cul3-RBX1 with KEAP1, KLHL12, KLHL20, KLHL22, KBTBD13) and resolved in CRL3 cryo-EM structures. Supporting Evidence: PMID:19782033 BACURDs form ubiquitin ligase complexes, which selectively ubiquitinate RhoA, with Cul3. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031463 Cul3-RING ubiquitin ligase complex | IDA PMID:20389280 The Cullin 3 substrate adaptor KLHL20 mediates DAPK ubiquiti... | ACCEPT | Summary: RBX1 is the RING subunit of BTB-CUL3-RBX1 (BCR/CRL3) ligases formed with BTB-domain receptors such as KEAP1, SPOP, KLHL9/13, KLHL20, KLHL22, KCTD10, KBTBD6/7 and ARMC5. Reason: Core complex membership, reconstituted repeatedly in vitro (Cul3-RBX1 with KEAP1, KLHL12, KLHL20, KLHL22, KBTBD13) and resolved in CRL3 cryo-EM structures. Supporting Evidence: PMID:20389280 The KLHL20-Cul3-ROC1 E3 ligase complex promotes DAPK polyubiquitination, thereby inducing the proteasomal degradation of DAPK. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031463 Cul3-RING ubiquitin ligase complex | IDA PMID:22358839 Ubiquitin-dependent regulation of COPII coat size and functi... | ACCEPT | Summary: RBX1 is the RING subunit of BTB-CUL3-RBX1 (BCR/CRL3) ligases formed with BTB-domain receptors such as KEAP1, SPOP, KLHL9/13, KLHL20, KLHL22, KCTD10, KBTBD6/7 and ARMC5. Reason: Core complex membership, reconstituted repeatedly in vitro (Cul3-RBX1 with KEAP1, KLHL12, KLHL20, KLHL22, KBTBD13) and resolved in CRL3 cryo-EM structures. Supporting Evidence: PMID:22358839 For in vitro ubiquitination reactions, Cul3/Rbx1 purified from Sf9 cells was conjugated to NEDD8 using recombinant APPBP1-UBA3, Ubc12, and NEDD8. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031463 Cul3-RING ubiquitin ligase complex | IDA PMID:35687106 ARMC5 is part of an RPB1-specific ubiquitin ligase implicate... | ACCEPT | Summary: RBX1 is the RING subunit of BTB-CUL3-RBX1 (BCR/CRL3) ligases formed with BTB-domain receptors such as KEAP1, SPOP, KLHL9/13, KLHL20, KLHL22, KCTD10, KBTBD6/7 and ARMC5. Reason: Core complex membership, reconstituted repeatedly in vitro (Cul3-RBX1 with KEAP1, KLHL12, KLHL20, KLHL22, KBTBD13) and resolved in CRL3 cryo-EM structures. Supporting Evidence: PMID:35687106 ARMC5-CUL3-RBX1 as an RPB1-specific E3 based on in vivo and in vitro ubiquitination. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031463 Cul3-RING ubiquitin ligase complex | IDA PMID:38225631 ARMC5 controls the degradation of most Pol II subunits, and ... | ACCEPT | Summary: RBX1 is the RING subunit of BTB-CUL3-RBX1 (BCR/CRL3) ligases formed with BTB-domain receptors such as KEAP1, SPOP, KLHL9/13, KLHL20, KLHL22, KCTD10, KBTBD6/7 and ARMC5. Reason: Core complex membership, reconstituted repeatedly in vitro (Cul3-RBX1 with KEAP1, KLHL12, KLHL20, KLHL22, KBTBD13) and resolved in CRL3 cryo-EM structures. Supporting Evidence: PMID:38225631 ARMC5-CUL3-RBX1 was a novel dominant E3 controlling the degradation of all 12 Pol II subunits under physiological conditions. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031463 Cul3-RING ubiquitin ligase complex | IDA PMID:39504960 Redundant pathways for removal of defective RNA polymerase I... | ACCEPT | Summary: RBX1 is the RING subunit of BTB-CUL3-RBX1 (BCR/CRL3) ligases formed with BTB-domain receptors such as KEAP1, SPOP, KLHL9/13, KLHL20, KLHL22, KCTD10, KBTBD6/7 and ARMC5. Reason: Core complex membership, reconstituted repeatedly in vitro (Cul3-RBX1 with KEAP1, KLHL12, KLHL20, KLHL22, KBTBD13) and resolved in CRL3 cryo-EM structures. Supporting Evidence: PMID:39504960 Tellingly, CUL3 E3 ligase relies on BTB domain-containing proteins as adaptors to recognize substrates for ubiquitylation75, suggesting that ARMC5 might connect CUL3 to RNAPII. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031463 Cul3-RING ubiquitin ligase complex | IDA PMID:39667934 CRL3(ARMC5) ubiquitin ligase and Integrator phosphatase form... | ACCEPT | Summary: RBX1 is the RING subunit of BTB-CUL3-RBX1 (BCR/CRL3) ligases formed with BTB-domain receptors such as KEAP1, SPOP, KLHL9/13, KLHL20, KLHL22, KCTD10, KBTBD6/7 and ARMC5. Reason: Core complex membership, reconstituted repeatedly in vitro (Cul3-RBX1 with KEAP1, KLHL12, KLHL20, KLHL22, KBTBD13) and resolved in CRL3 cryo-EM structures. Supporting Evidence: PMID:39667934 CRL3(ARMC5) ubiquitin ligase and Integrator phosphatase form parallel mechanisms to control early stages of RNA Pol II transcription. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031463 Cul3-RING ubiquitin ligase complex | IPI PMID:15601839 BTB protein Keap1 targets antioxidant transcription factor N... | ACCEPT | Summary: RBX1 is the RING subunit of BTB-CUL3-RBX1 (BCR/CRL3) ligases formed with BTB-domain receptors such as KEAP1, SPOP, KLHL9/13, KLHL20, KLHL22, KCTD10, KBTBD6/7 and ARMC5. Reason: Core complex membership, reconstituted repeatedly in vitro (Cul3-RBX1 with KEAP1, KLHL12, KLHL20, KLHL22, KBTBD13) and resolved in CRL3 cryo-EM structures. Supporting Evidence: PMID:15601839 BTB protein Keap1 targets antioxidant transcription factor Nrf2 for ubiquitination by the Cullin 3-Roc1 ligase. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031463 Cul3-RING ubiquitin ligase complex | IPI PMID:22542517 KBTBD13 interacts with Cullin 3 to form a functional ubiquit... | ACCEPT | Summary: RBX1 is the RING subunit of BTB-CUL3-RBX1 (BCR/CRL3) ligases formed with BTB-domain receptors such as KEAP1, SPOP, KLHL9/13, KLHL20, KLHL22, KCTD10, KBTBD6/7 and ARMC5. Reason: Core complex membership, reconstituted repeatedly in vitro (Cul3-RBX1 with KEAP1, KLHL12, KLHL20, KLHL22, KBTBD13) and resolved in CRL3 cryo-EM structures. Supporting Evidence: PMID:22542517 Taken together, our data demonstrate that KBTBD13βCul3βRbx1 is a muscle specific ubiquitin ligase. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031463 Cul3-RING ubiquitin ligase complex | IPI PMID:25684205 CUL3-KBTBD6/KBTBD7 ubiquitin ligase cooperates with GABARAP ... | ACCEPT | Summary: RBX1 is the RING subunit of BTB-CUL3-RBX1 (BCR/CRL3) ligases formed with BTB-domain receptors such as KEAP1, SPOP, KLHL9/13, KLHL20, KLHL22, KCTD10, KBTBD6/7 and ARMC5. Reason: Core complex membership, reconstituted repeatedly in vitro (Cul3-RBX1 with KEAP1, KLHL12, KLHL20, KLHL22, KBTBD13) and resolved in CRL3 cryo-EM structures. Supporting Evidence: PMID:25684205 CUL3-KBTBD6/KBTBD7 ubiquitin ligase cooperates with GABARAP proteins to spatially restrict TIAM1-RAC1 signaling. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031463 Cul3-RING ubiquitin ligase complex | IPI PMID:26399832 Cell-fate determination by ubiquitin-dependent regulation of... | ACCEPT | Summary: RBX1 is the RING subunit of BTB-CUL3-RBX1 (BCR/CRL3) ligases formed with BTB-domain receptors such as KEAP1, SPOP, KLHL9/13, KLHL20, KLHL22, KCTD10, KBTBD6/7 and ARMC5. Reason: Core complex membership, reconstituted repeatedly in vitro (Cul3-RBX1 with KEAP1, KLHL12, KLHL20, KLHL22, KBTBD13) and resolved in CRL3 cryo-EM structures. Supporting Evidence: PMID:26399832 CUL3(KBTBD8) monoubiquitylates NOLC1 and its paralogue TCOF1, the mutation of which underlies the neurocristopathy Treacher Collins syndrome. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031463 Cul3-RING ubiquitin ligase complex | IPI PMID:37788672 Cryo-EM structure of the KLHL22 E3 ligase bound to an oligom... | ACCEPT | Summary: RBX1 is the RING subunit of BTB-CUL3-RBX1 (BCR/CRL3) ligases formed with BTB-domain receptors such as KEAP1, SPOP, KLHL9/13, KLHL20, KLHL22, KCTD10, KBTBD6/7 and ARMC5. Reason: Core complex membership, reconstituted repeatedly in vitro (Cul3-RBX1 with KEAP1, KLHL12, KLHL20, KLHL22, KBTBD13) and resolved in CRL3 cryo-EM structures. Supporting Evidence: PMID:37788672 CULLIN3KLHL22-RBX1 ligase mediated the polyubiquitination of GDH1 in vitro. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031463 Cul3-RING ubiquitin ligase complex | IPI PMID:38332366 Dynamic molecular architecture and substrate recruitment of ... | ACCEPT | Summary: RBX1 is the RING subunit of BTB-CUL3-RBX1 (BCR/CRL3) ligases formed with BTB-domain receptors such as KEAP1, SPOP, KLHL9/13, KLHL20, KLHL22, KCTD10, KBTBD6/7 and ARMC5. Reason: Core complex membership, reconstituted repeatedly in vitro (Cul3-RBX1 with KEAP1, KLHL12, KLHL20, KLHL22, KBTBD13) and resolved in CRL3 cryo-EM structures. Supporting Evidence: PMID:38332366 KBTBD2 assembles with Cullin3 (Cul3) and Rbx1 into the Cullin3-RING E3 ubiquitin ligase (CRL3KBTBD2). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031463 Cul3-RING ubiquitin ligase complex | NAS PMID:22632832 Adaptor protein self-assembly drives the control of a cullin... | ACCEPT | Summary: RBX1 is the RING subunit of BTB-CUL3-RBX1 (BCR/CRL3) ligases formed with BTB-domain receptors such as KEAP1, SPOP, KLHL9/13, KLHL20, KLHL22, KCTD10, KBTBD6/7 and ARMC5. Reason: Core complex membership, reconstituted repeatedly in vitro (Cul3-RBX1 with KEAP1, KLHL12, KLHL20, KLHL22, KBTBD13) and resolved in CRL3 cryo-EM structures. Supporting Evidence: PMID:22632832 Adaptor protein self-assembly drives the control of a cullin-RING ubiquitin ligase. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031463 Cul3-RING ubiquitin ligase complex | NAS PMID:29249570 Cullin 3-Based Ubiquitin Ligases as Master Regulators of Mam... | ACCEPT | Summary: RBX1 is the RING subunit of BTB-CUL3-RBX1 (BCR/CRL3) ligases formed with BTB-domain receptors such as KEAP1, SPOP, KLHL9/13, KLHL20, KLHL22, KCTD10, KBTBD6/7 and ARMC5. Reason: Core complex membership, reconstituted repeatedly in vitro (Cul3-RBX1 with KEAP1, KLHL12, KLHL20, KLHL22, KBTBD13) and resolved in CRL3 cryo-EM structures. Supporting Evidence: PMID:29249570 Cullin 3-Based Ubiquitin Ligases as Master Regulators of Mammalian Cell Differentiation. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031463 Cul3-RING ubiquitin ligase complex | NAS PMID:31898230 CRL3s: The BTB-CUL3-RING E3 Ubiquitin Ligases. | ACCEPT | Summary: RBX1 is the RING subunit of BTB-CUL3-RBX1 (BCR/CRL3) ligases formed with BTB-domain receptors such as KEAP1, SPOP, KLHL9/13, KLHL20, KLHL22, KCTD10, KBTBD6/7 and ARMC5. Reason: Core complex membership, reconstituted repeatedly in vitro (Cul3-RBX1 with KEAP1, KLHL12, KLHL20, KLHL22, KBTBD13) and resolved in CRL3 cryo-EM structures. Supporting Evidence: PMID:31898230 In most of Cullin-RING ubiquitin ligase (CRL) complexes, separate linker and adaptor proteins build the substrate recognition module. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031463 Cul3-RING ubiquitin ligase complex | NAS PMID:37628845 The Role of PIK3R1 in Metabolic Function and Insulin Sensiti... | ACCEPT | Summary: RBX1 is the RING subunit of BTB-CUL3-RBX1 (BCR/CRL3) ligases formed with BTB-domain receptors such as KEAP1, SPOP, KLHL9/13, KLHL20, KLHL22, KCTD10, KBTBD6/7 and ARMC5. Reason: Core complex membership, reconstituted repeatedly in vitro (Cul3-RBX1 with KEAP1, KLHL12, KLHL20, KLHL22, KBTBD13) and resolved in CRL3 cryo-EM structures. Supporting Evidence: PMID:37628845 KBTBD2 interacts with CUL3 and the iSH2 domain of p85Ξ± and leads to the degradation of p85Ξ± [69]. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | EXP PMID:22118460 The molecular basis of CRL4DDB2/CSA ubiquitin ligase archite... | ACCEPT | Summary: RBX1 is the RING subunit of CUL4A-DDB1-DCAF ligases, including the DDB2 and CSA (ERCC8) complexes, DET1-COP1, CRL4(CDT2), CRL4(CRBN) and CRL4(DCAF15). Reason: Core complex membership; CUL4A-DDB1-RBX1 is the catalytic core in every CRL4 reconstitution and structure cited here. Supporting Evidence: PMID:22118460 The DDB1-CUL4-RBX1 (CRL4) ubiquitin ligase family regulates a diverse set of cellular pathways through dedicated substrate receptors (DCAFs). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | IDA PMID:12732143 The ubiquitin ligase activity in the DDB2 and CSA complexes ... | ACCEPT | Summary: RBX1 is the RING subunit of CUL4A-DDB1-DCAF ligases, including the DDB2 and CSA (ERCC8) complexes, DET1-COP1, CRL4(CDT2), CRL4(CRBN) and CRL4(DCAF15). Reason: Core complex membership; CUL4A-DDB1-RBX1 is the catalytic core in every CRL4 reconstitution and structure cited here. Supporting Evidence: PMID:12732143 Both complexes contain cullin 4A and Roc1 and display ubiquitin ligase activity. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | IDA PMID:14739464 Human De-etiolated-1 regulates c-Jun by assembling a CUL4A u... | ACCEPT | Summary: RBX1 is the RING subunit of CUL4A-DDB1-DCAF ligases, including the DDB2 and CSA (ERCC8) complexes, DET1-COP1, CRL4(CDT2), CRL4(CRBN) and CRL4(DCAF15). Reason: Core complex membership; CUL4A-DDB1-RBX1 is the catalytic core in every CRL4 reconstitution and structure cited here. Supporting Evidence: PMID:14739464 Human De-etiolated-1 regulates c-Jun by assembling a CUL4A ubiquitin ligase. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | IDA PMID:17085480 DTL/CDT2 is essential for both CDT1 regulation and the early... | ACCEPT | Summary: RBX1 is the RING subunit of CUL4A-DDB1-DCAF ligases, including the DDB2 and CSA (ERCC8) complexes, DET1-COP1, CRL4(CDT2), CRL4(CRBN) and CRL4(DCAF15). Reason: Core complex membership; CUL4A-DDB1-RBX1 is the catalytic core in every CRL4 reconstitution and structure cited here. Supporting Evidence: PMID:17085480 We show that DTL associates with the CUL4-DDB1 E3 ubiquitin ligase and is required for CDT1 down-regulation in unperturbed cells and following DNA damage. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | IDA PMID:18794347 PCNA-dependent regulation of p21 ubiquitylation and degradat... | ACCEPT | Summary: RBX1 is the RING subunit of CUL4A-DDB1-DCAF ligases, including the DDB2 and CSA (ERCC8) complexes, DET1-COP1, CRL4(CDT2), CRL4(CRBN) and CRL4(DCAF15). Reason: Core complex membership; CUL4A-DDB1-RBX1 is the catalytic core in every CRL4 reconstitution and structure cited here. Supporting Evidence: PMID:18794347 Cdt2 functions as the substrate recruiting factor for p21 to the rest of the CRL4 ubiquitin ligase complex. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | IDA PMID:20129063 CRL4(Cdt2) E3 ubiquitin ligase monoubiquitinates PCNA to pro... | ACCEPT | Summary: RBX1 is the RING subunit of CUL4A-DDB1-DCAF ligases, including the DDB2 and CSA (ERCC8) complexes, DET1-COP1, CRL4(CDT2), CRL4(CRBN) and CRL4(DCAF15). Reason: Core complex membership; CUL4A-DDB1-RBX1 is the catalytic core in every CRL4 reconstitution and structure cited here. Supporting Evidence: PMID:20129063 CRL4Cdt2 consists of Cul4A or Cul4B, DDB1 (damage-specific DNA binding protein 1), the RING-finger protein ROC1 and the DCAF (DDB1 and Cul4-associated factor) and substrate recognition factor/WD40 protein Cdt2. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | IDA PMID:20223979 Identification of a primary target of thalidomide teratogeni... | ACCEPT | Summary: RBX1 is the RING subunit of CUL4A-DDB1-DCAF ligases, including the DDB2 and CSA (ERCC8) complexes, DET1-COP1, CRL4(CDT2), CRL4(CRBN) and CRL4(DCAF15). Reason: Core complex membership; CUL4A-DDB1-RBX1 is the catalytic core in every CRL4 reconstitution and structure cited here. Supporting Evidence: PMID:20223979 CRBN forms an E3 ubiquitin ligase complex with damaged DNA binding protein 1 (DDB1) and Cul4A that is important for limb outgrowth and expression of the fibroblast growth factor Fgf8 in zebrafish and chicks. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | IDA PMID:27113764 The antiobesity factor WDTC1 suppresses adipogenesis via the... | ACCEPT | Summary: RBX1 is the RING subunit of CUL4A-DDB1-DCAF ligases, including the DDB2 and CSA (ERCC8) complexes, DET1-COP1, CRL4(CDT2), CRL4(CRBN) and CRL4(DCAF15). Reason: Core complex membership; CUL4A-DDB1-RBX1 is the catalytic core in every CRL4 reconstitution and structure cited here. Supporting Evidence: PMID:27113764 Here, we demonstrate that WDTC1 is a component of a DDB1-CUL4-ROC1 (CRL4) E3 ligase. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | IEA GO_REF:0000117 | ACCEPT | Summary: RBX1 is the RING subunit of CUL4A-DDB1-DCAF ligases, including the DDB2 and CSA (ERCC8) complexes, DET1-COP1, CRL4(CDT2), CRL4(CRBN) and CRL4(DCAF15). Reason: Core complex membership; CUL4A-DDB1-RBX1 is the catalytic core in every CRL4 reconstitution and structure cited here. Supporting Evidence: file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | IPI PMID:22118460 The molecular basis of CRL4DDB2/CSA ubiquitin ligase archite... | ACCEPT | Summary: RBX1 is the RING subunit of CUL4A-DDB1-DCAF ligases, including the DDB2 and CSA (ERCC8) complexes, DET1-COP1, CRL4(CDT2), CRL4(CRBN) and CRL4(DCAF15). Reason: Core complex membership; CUL4A-DDB1-RBX1 is the catalytic core in every CRL4 reconstitution and structure cited here. Supporting Evidence: PMID:22118460 The DDB1-CUL4-RBX1 (CRL4) ubiquitin ligase family regulates a diverse set of cellular pathways through dedicated substrate receptors (DCAFs). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | IPI PMID:31693891 Aryl Sulfonamides Degrade RBM39 and RBM23 by Recruitment to ... | ACCEPT | Summary: RBX1 is the RING subunit of CUL4A-DDB1-DCAF ligases, including the DDB2 and CSA (ERCC8) complexes, DET1-COP1, CRL4(CDT2), CRL4(CRBN) and CRL4(DCAF15). Reason: Core complex membership; CUL4A-DDB1-RBX1 is the catalytic core in every CRL4 reconstitution and structure cited here. Supporting Evidence: PMID:31693891 Ubiquitination AssaysRecombinant human Cul4a-Rbx1(Ξ1β14), DCAF15-DDB1-DDA1, and RBM39 (full-length) were combined with E1 enzyme (UBA1, Boston Biochem), E2 enzyme (UbcH5a and UbcH5b, Boston Biochem), and ubiquitin (Boston Biochem). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | IPI PMID:34595758 The CRL4(DCAF1) cullin-RING ubiquitin ligase is activated fo... | ACCEPT | Summary: RBX1 is the RING subunit of CUL4A-DDB1-DCAF ligases, including the DDB2 and CSA (ERCC8) complexes, DET1-COP1, CRL4(CDT2), CRL4(CRBN) and CRL4(DCAF15). Reason: Core complex membership; CUL4A-DDB1-RBX1 is the catalytic core in every CRL4 reconstitution and structure cited here. Supporting Evidence: PMID:34595758 This architecture renders the RING domain of RBX1 inaccessible for the E2 ubiquitinβconjugating enzyme. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | NAS PMID:16861906 L2DTL/CDT2 interacts with the CUL4/DDB1 complex and PCNA and... | ACCEPT | Summary: RBX1 is the RING subunit of CUL4A-DDB1-DCAF ligases, including the DDB2 and CSA (ERCC8) complexes, DET1-COP1, CRL4(CDT2), CRL4(CRBN) and CRL4(DCAF15). Reason: Core complex membership; CUL4A-DDB1-RBX1 is the catalytic core in every CRL4 reconstitution and structure cited here. Supporting Evidence: PMID:16861906 Our studies suggest that L2DTL and PCNA interact with CUL4/DDB1 complexes and are involved in CDT1 degradation after DNA damage. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | NAS PMID:16949367 A family of diverse Cul4-Ddb1-interacting proteins includes ... | ACCEPT | Summary: RBX1 is the RING subunit of CUL4A-DDB1-DCAF ligases, including the DDB2 and CSA (ERCC8) complexes, DET1-COP1, CRL4(CDT2), CRL4(CRBN) and CRL4(DCAF15). Reason: Core complex membership; CUL4A-DDB1-RBX1 is the catalytic core in every CRL4 reconstitution and structure cited here. Supporting Evidence: PMID:16949367 Cul4 E3 ubiquitin ligases contain the cullin 4 scaffold and the triple beta propeller Ddb1 adaptor protein, but few substrate receptors have been identified. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | NAS PMID:25108355 Structure of the human Cereblon-DDB1-lenalidomide complex re... | ACCEPT | Summary: RBX1 is the RING subunit of CUL4A-DDB1-DCAF ligases, including the DDB2 and CSA (ERCC8) complexes, DET1-COP1, CRL4(CDT2), CRL4(CRBN) and CRL4(DCAF15). Reason: Core complex membership; CUL4A-DDB1-RBX1 is the catalytic core in every CRL4 reconstitution and structure cited here. Supporting Evidence: PMID:25108355 The Cul4-Rbx1-DDB1-Cereblon E3 ubiquitin ligase complex is the target of thalidomide, lenalidomide and pomalidomide, therapeutically important drugs for multiple myeloma and other B-cell malignancies. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | NAS PMID:25499913 AMBRA1 interplay with cullin E3 ubiquitin ligases regulates ... | ACCEPT | Summary: RBX1 is the RING subunit of CUL4A-DDB1-DCAF ligases, including the DDB2 and CSA (ERCC8) complexes, DET1-COP1, CRL4(CDT2), CRL4(CRBN) and CRL4(DCAF15). Reason: Core complex membership; CUL4A-DDB1-RBX1 is the catalytic core in every CRL4 reconstitution and structure cited here. Supporting Evidence: PMID:25499913 AMBRA1 interplay with cullin E3 ubiquitin ligases regulates autophagy dynamics. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | NAS PMID:28212551 NRIP/DCAF6 stabilizes the androgen receptor protein by displ... | ACCEPT | Summary: RBX1 is the RING subunit of CUL4A-DDB1-DCAF ligases, including the DDB2 and CSA (ERCC8) complexes, DET1-COP1, CRL4(CDT2), CRL4(CRBN) and CRL4(DCAF15). Reason: Core complex membership; CUL4A-DDB1-RBX1 is the catalytic core in every CRL4 reconstitution and structure cited here. Supporting Evidence: PMID:28212551 More importantly, our previous in vitro study indicated that DDB2 enhances the ubiquitination and proteasomal degradation of the AR, mediated by the DDB2-DDB1-Cul4 complex [23]. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | NAS PMID:29691401 Methylated DNMT1 and E2F1 are targeted for proteolysis by L3... | ACCEPT | Summary: RBX1 is the RING subunit of CUL4A-DDB1-DCAF ligases, including the DDB2 and CSA (ERCC8) complexes, DET1-COP1, CRL4(CDT2), CRL4(CRBN) and CRL4(DCAF15). Reason: Core complex membership; CUL4A-DDB1-RBX1 is the catalytic core in every CRL4 reconstitution and structure cited here. Supporting Evidence: PMID:29691401 The cullin-RING ubiquitin ligases (CRLs) comprise the largest families of ubiquitin E3 ligases23. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031464 Cul4A-RING E3 ubiquitin ligase complex | NAS PMID:30945288 Inflammation-dependent overexpression of c-Myc enhances CRL4... | ACCEPT | Summary: RBX1 is the RING subunit of CUL4A-DDB1-DCAF ligases, including the DDB2 and CSA (ERCC8) complexes, DET1-COP1, CRL4(CDT2), CRL4(CRBN) and CRL4(DCAF15). Reason: Core complex membership; CUL4A-DDB1-RBX1 is the catalytic core in every CRL4 reconstitution and structure cited here. Supporting Evidence: PMID:30945288 Inflammation-dependent overexpression of c-Myc enhances CRL4(DCAF4) E3 ligase activity and promotes ubiquitination of ST7 in colitis-associated cancer. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | IDA PMID:18794347 PCNA-dependent regulation of p21 ubiquitylation and degradat... | ACCEPT | Summary: RBX1 is equally the RING subunit of the CUL4B-DDB1-DCAF ligases, which act largely on chromatin. Reason: Core complex membership; CUL4A and CUL4B share DDB1, RBX1 and the DCAF receptor repertoire. Supporting Evidence: PMID:18794347 Cdt2 functions as the substrate recruiting factor for p21 to the rest of the CRL4 ubiquitin ligase complex. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | IPI PMID:27113764 The antiobesity factor WDTC1 suppresses adipogenesis via the... | ACCEPT | Summary: RBX1 is equally the RING subunit of the CUL4B-DDB1-DCAF ligases, which act largely on chromatin. Reason: Core complex membership; CUL4A and CUL4B share DDB1, RBX1 and the DCAF receptor repertoire. Supporting Evidence: PMID:27113764 Here, we demonstrate that WDTC1 is a component of a DDB1-CUL4-ROC1 (CRL4) E3 ligase. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | NAS PMID:16861906 L2DTL/CDT2 interacts with the CUL4/DDB1 complex and PCNA and... | ACCEPT | Summary: RBX1 is equally the RING subunit of the CUL4B-DDB1-DCAF ligases, which act largely on chromatin. Reason: Core complex membership; CUL4A and CUL4B share DDB1, RBX1 and the DCAF receptor repertoire. Supporting Evidence: PMID:16861906 Our studies suggest that L2DTL and PCNA interact with CUL4/DDB1 complexes and are involved in CDT1 degradation after DNA damage. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | NAS PMID:16949367 A family of diverse Cul4-Ddb1-interacting proteins includes ... | ACCEPT | Summary: RBX1 is equally the RING subunit of the CUL4B-DDB1-DCAF ligases, which act largely on chromatin. Reason: Core complex membership; CUL4A and CUL4B share DDB1, RBX1 and the DCAF receptor repertoire. Supporting Evidence: PMID:16949367 Cul4 E3 ubiquitin ligases contain the cullin 4 scaffold and the triple beta propeller Ddb1 adaptor protein, but few substrate receptors have been identified. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | NAS PMID:22118460 The molecular basis of CRL4DDB2/CSA ubiquitin ligase archite... | ACCEPT | Summary: RBX1 is equally the RING subunit of the CUL4B-DDB1-DCAF ligases, which act largely on chromatin. Reason: Core complex membership; CUL4A and CUL4B share DDB1, RBX1 and the DCAF receptor repertoire. Supporting Evidence: PMID:22118460 The DDB1-CUL4-RBX1 (CRL4) ubiquitin ligase family regulates a diverse set of cellular pathways through dedicated substrate receptors (DCAFs). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | NAS PMID:25108355 Structure of the human Cereblon-DDB1-lenalidomide complex re... | ACCEPT | Summary: RBX1 is equally the RING subunit of the CUL4B-DDB1-DCAF ligases, which act largely on chromatin. Reason: Core complex membership; CUL4A and CUL4B share DDB1, RBX1 and the DCAF receptor repertoire. Supporting Evidence: PMID:25108355 The Cul4-Rbx1-DDB1-Cereblon E3 ubiquitin ligase complex is the target of thalidomide, lenalidomide and pomalidomide, therapeutically important drugs for multiple myeloma and other B-cell malignancies. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | NAS PMID:25499913 AMBRA1 interplay with cullin E3 ubiquitin ligases regulates ... | ACCEPT | Summary: RBX1 is equally the RING subunit of the CUL4B-DDB1-DCAF ligases, which act largely on chromatin. Reason: Core complex membership; CUL4A and CUL4B share DDB1, RBX1 and the DCAF receptor repertoire. Supporting Evidence: PMID:25499913 AMBRA1 interplay with cullin E3 ubiquitin ligases regulates autophagy dynamics. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | NAS PMID:29691401 Methylated DNMT1 and E2F1 are targeted for proteolysis by L3... | ACCEPT | Summary: RBX1 is equally the RING subunit of the CUL4B-DDB1-DCAF ligases, which act largely on chromatin. Reason: Core complex membership; CUL4A and CUL4B share DDB1, RBX1 and the DCAF receptor repertoire. Supporting Evidence: PMID:29691401 The cullin-RING ubiquitin ligases (CRLs) comprise the largest families of ubiquitin E3 ligases23. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | NAS PMID:30945288 Inflammation-dependent overexpression of c-Myc enhances CRL4... | ACCEPT | Summary: RBX1 is equally the RING subunit of the CUL4B-DDB1-DCAF ligases, which act largely on chromatin. Reason: Core complex membership; CUL4A and CUL4B share DDB1, RBX1 and the DCAF receptor repertoire. Supporting Evidence: PMID:30945288 Inflammation-dependent overexpression of c-Myc enhances CRL4(DCAF4) E3 ligase activity and promotes ubiquitination of ST7 in colitis-associated cancer. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | NAS PMID:31452512 Systematic identification of cancer cell vulnerabilities to ... | ACCEPT | Summary: RBX1 is equally the RING subunit of the CUL4B-DDB1-DCAF ligases, which act largely on chromatin. Reason: Core complex membership; CUL4A and CUL4B share DDB1, RBX1 and the DCAF receptor repertoire. Supporting Evidence: PMID:31452512 CRL4 complexes enable cells to mark proteins for proteosomal degradation, helping regulate intracellular protein homeostasis. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | NAS PMID:33898171 OTUD1 Activates Caspase-Independent and Caspase-Dependent Ap... | ACCEPT | Summary: RBX1 is equally the RING subunit of the CUL4B-DDB1-DCAF ligases, which act largely on chromatin. Reason: Core complex membership; CUL4A and CUL4B share DDB1, RBX1 and the DCAF receptor repertoire. Supporting Evidence: PMID:33898171 The ubiquitination reaction is carried out by a threeβstep enzymatic catalysis process involving ubiquitinβactivating enzymes (E1), ubiquitinβconjugating enzymes (E2) and ubiquitin ligases (E3). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031465 Cul4B-RING E3 ubiquitin ligase complex | NAS PMID:34595758 The CRL4(DCAF1) cullin-RING ubiquitin ligase is activated fo... | ACCEPT | Summary: RBX1 is equally the RING subunit of the CUL4B-DDB1-DCAF ligases, which act largely on chromatin. Reason: Core complex membership; CUL4A and CUL4B share DDB1, RBX1 and the DCAF receptor repertoire. Supporting Evidence: PMID:34595758 This architecture renders the RING domain of RBX1 inaccessible for the E2 ubiquitinβconjugating enzyme. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031466 Cul5-RING ubiquitin ligase complex | IDA PMID:17636018 ASB4 is a hydroxylation substrate of FIH and promotes vascul... | KEEP AS NON CORE | Summary: IDA row placing RBX1 in a CUL5-based elongin BC ligase (the ASB4 ECS complex); UniProt likewise records a CRL5 containing CUL5, ELOB, ELOC, ELOA and RBX1. Reason: Kept but non-core: CUL5 preferentially pairs with the paralogue RBX2/RNF7 (SOCS-box receptors select CUL5-RBX2), so RBX1-CUL5 assemblies are the exception rather than the shared rule. The evidence is experimental and is not contradicted, so it is retained rather than removed. Supporting Evidence: PMID:17636018 Like other SOCS box-containing proteins, ASB4 is the substrate recognition molecule of an elongin B/elongin C/cullin/Roc ubiquitin ligase complex that mediates the ubiquitination and degradation of substrate protein(s). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0031467 Cul7-RING ubiquitin ligase complex | IDA PMID:18498745 The CUL7 E3 ubiquitin ligase targets insulin receptor substr... | ACCEPT | Summary: RBX1 is a core subunit of the CUL7-SKP1-FBXW8 ligase, which targets IRS1 for degradation. Reason: Correct complex membership. Note that in CRL7(FBXW8) the RBX1 RING is held in a non-productive orientation, so ubiquitination is carried out by a neddylated CUL1-RBX1 module recruited through SKP1-FBXW8 - RBX1 is present in both halves of that arrangement. Supporting Evidence: PMID:18498745 Recent genetic studies have documented a pivotal growth-regulatory role played by the Cullin 7 (CUL7) E3 ubiquitin ligase complex containing the Fbw8-substrate-targeting subunit, Skp1, and the ROC1 RING finger protein. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0031625 ubiquitin protein ligase binding | IDA PMID:17636018 ASB4 is a hydroxylation substrate of FIH and promotes vascul... | MODIFY | Summary: IDA rows recording RBX1 engagement with components of the cullin-RING assemblies it works in (the elongin BC-cullin-ROC module and CUL3-KLHL22). Reason: The partners here are cullin scaffolds and BTB adaptors rather than ubiquitin ligases in their own right, so cullin family protein binding (GO:0097602) states the same interaction more accurately. RBX1 does engage a genuine partner ligase - the RBR E3 ARIH1 on neddylated CRLs - but that is not what these rows record. Proposed replacements: cullin family protein binding Supporting Evidence: PMID:17636018 Like other SOCS box-containing proteins, ASB4 is the substrate recognition molecule of an elongin B/elongin C/cullin/Roc ubiquitin ligase complex that mediates the ubiquitination and degradation of substrate protein(s). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0031625 ubiquitin protein ligase binding | IDA PMID:29769719 KLHL22 activates amino-acid-dependent mTORC1 signalling to p... | MODIFY | Summary: IDA rows recording RBX1 engagement with components of the cullin-RING assemblies it works in (the elongin BC-cullin-ROC module and CUL3-KLHL22). Reason: The partners here are cullin scaffolds and BTB adaptors rather than ubiquitin ligases in their own right, so cullin family protein binding (GO:0097602) states the same interaction more accurately. RBX1 does engage a genuine partner ligase - the RBR E3 ARIH1 on neddylated CRLs - but that is not what these rows record. Proposed replacements: cullin family protein binding Supporting Evidence: PMID:29769719 Here we find that in response to amino acids, the CUL3-KLHL22 E3 ubiquitin ligase promotes K48-linked polyubiquitination and degradation of DEPDC5, an essential subunit of GATOR1. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0032006 regulation of TOR signaling | NAS PMID:23263282 SCFFbxo9 and CK2 direct the cellular response to growth fact... | KEEP AS NON CORE | Summary: SCF(FBXO9) containing RBX1 degrades TEL2/TTI1 within mTORC1 after growth-factor withdrawal. Reason: Receptor-specific regulation of TOR signalling; kept as non-core. Supporting Evidence: PMID:23263282 SCFFbxo9 and CK2 direct the cellular response to growth factor withdrawal via Tel2/Tti1 degradation and promote survival in multiple myeloma. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0032436 positive regulation of proteasomal ubiquitin-dependent protein catabolic process | IPI PMID:14739464 Human De-etiolated-1 regulates c-Jun by assembling a CUL4A u... | MODIFY | Summary: IPI row from the CUL4A-DDB1-DET1-COP1-ROC1 study, where the assembled ligase ubiquitinates c-Jun and promotes its proteasomal destruction. Reason: As for the other positive-regulation-of-catabolism rows, RBX1 executes rather than regulates the degradative step; GO:0043161 is the accurate term. Proposed replacements: proteasome-mediated ubiquitin-dependent protein catabolic process Supporting Evidence: PMID:14739464 Human De-etiolated-1 regulates c-Jun by assembling a CUL4A ubiquitin ligase. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0032480 negative regulation of type I interferon production | IDA PMID:36394357 XAF1 prevents hyperproduction of type I interferon upon vira... | KEEP AS NON CORE | Summary: The BTB-CUL3-RBX1 ligase with the KLHL22 adaptor, controlled by the XAF1-XIAP axis, limits IRF7 accumulation and thereby type I interferon production. Reason: Genuine receptor-specific output; non-core for a RING shared by all CRL3 ligases. Supporting Evidence: PMID:36394357 Mechanistically, we find that the XAF1-XIAP axis controls the activity of KLHL22, an adaptor of the BTB-CUL3-RBX1 E3 ligase complex through a ubiquitin-dependent pathway. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0032814 regulation of natural killer cell activation | NAS PMID:31452512 Systematic identification of cancer cell vulnerabilities to ... | KEEP AS NON CORE | Summary: Loss of the CRL4 substrate receptor DCAF15 sensitises leukaemia cells to natural killer cells. Reason: Receptor-specific immunomodulatory output; kept as non-core for RBX1. Supporting Evidence: PMID:31452512 CRL4 complexes enable cells to mark proteins for proteosomal degradation, helping regulate intracellular protein homeostasis. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0034450 ubiquitin-ubiquitin ligase activity | IDA PMID:10230407 ROC1, a homolog of APC11, represents a family of cullin part... | ACCEPT | Summary: ROC1 immunocomplexes catalyse isopeptide ligation into polyubiquitin chains in an E1- and E2-dependent manner, i.e. RBX1-containing CRLs elongate chains on already-conjugated ubiquitin. Reason: Chain elongation by the RBX1 RING is genuine and distinguishable from chain initiation (which for many CRL substrates is primed by ARIH1); the term is narrow but accurate for this activity. Supporting Evidence: PMID:10230407 ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity. file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity |
| GO:0034599 cellular response to oxidative stress | IDA PMID:15601839 BTB protein Keap1 targets antioxidant transcription factor N... | KEEP AS NON CORE | Summary: Under basal conditions the KEAP1-CUL3-RBX1 ligase ubiquitinates NRF2, keeping the antioxidant response low; oxidative or electrophilic stress modifies KEAP1 and relieves this. Reason: Genuine involvement, but the redox sensor is KEAP1 and the pathway is one of many CRL3 outputs; kept as non-core for the shared RING. Supporting Evidence: PMID:15601839 BTB protein Keap1 targets antioxidant transcription factor Nrf2 for ubiquitination by the Cullin 3-Roc1 ligase. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0034599 cellular response to oxidative stress | IDA PMID:39880951 C-terminal amides mark proteins for degradation via SCF-FBXO... | KEEP AS NON CORE | Summary: Under basal conditions the KEAP1-CUL3-RBX1 ligase ubiquitinates NRF2, keeping the antioxidant response low; oxidative or electrophilic stress modifies KEAP1 and relieves this. Reason: Genuine involvement, but the redox sensor is KEAP1 and the pathway is one of many CRL3 outputs; kept as non-core for the shared RING. Supporting Evidence: PMID:39880951 FBXO31 is a substrate receptor for the SKP1-CUL1-F-box protein (SCF) ubiquitin ligase SCF-FBXO31, which ubiquitylates CTAPs for subsequent proteasomal degradation. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0034644 cellular response to UV | EXP PMID:22118460 The molecular basis of CRL4DDB2/CSA ubiquitin ligase archite... | KEEP AS NON CORE | Summary: The CRL4(DDB2) ligase containing RBX1 is activated on UV-damaged DNA when the COP9 signalosome is displaced, and UV-induced histone H3/H4 ubiquitination has been attributed to it. Reason: Real but DDB2-dependent; kept as a non-core, context-specific process for the shared RING. Supporting Evidence: PMID:22118460 The DDB1-CUL4-RBX1 (CRL4) ubiquitin ligase family regulates a diverse set of cellular pathways through dedicated substrate receptors (DCAFs). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0034644 cellular response to UV | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: The CRL4(DDB2) ligase containing RBX1 is activated on UV-damaged DNA when the COP9 signalosome is displaced, and UV-induced histone H3/H4 ubiquitination has been attributed to it. Reason: Real but DDB2-dependent; kept as a non-core, context-specific process for the shared RING. Supporting Evidence: file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0034644 cellular response to UV | ISS GO_REF:0000114 | KEEP AS NON CORE | Summary: The CRL4(DDB2) ligase containing RBX1 is activated on UV-damaged DNA when the COP9 signalosome is displaced, and UV-induced histone H3/H4 ubiquitination has been attributed to it. Reason: Real but DDB2-dependent; kept as a non-core, context-specific process for the shared RING. Supporting Evidence: file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0040029 epigenetic regulation of gene expression | NAS PMID:30111536 DCAF13 promotes pluripotency by negatively regulating SUV39H... | MARK AS OVER ANNOTATED | Summary: NAS rows citing CRL4 ligases that act on chromatin regulators (DNMT1, DNMT3A, SUV39H1, PHGDH). Reason: Over-annotation for RBX1: degrading a chromatin modifier is ubiquitination with an epigenetic consequence, not participation in epigenetic regulation by the ligase subunit itself. Supporting Evidence: PMID:30111536 Mechanistically, CRL4-DCAF13 targets SUV39H1 for polyubiquitination and proteasomal degradation and therefore facilitates H3K9me3 removal and zygotic gene expression. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0040029 epigenetic regulation of gene expression | NAS PMID:34429321 Systematic Profiling of DNMT3A Variants Reveals Protein Inst... | MARK AS OVER ANNOTATED | Summary: NAS rows citing CRL4 ligases that act on chromatin regulators (DNMT1, DNMT3A, SUV39H1, PHGDH). Reason: Over-annotation for RBX1: degrading a chromatin modifier is ubiquitination with an epigenetic consequence, not participation in epigenetic regulation by the ligase subunit itself. Supporting Evidence: PMID:34429321 Systematic Profiling of DNMT3A Variants Reveals Protein Instability Mediated by the DCAF8 E3 Ubiquitin Ligase Adaptor. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0040029 epigenetic regulation of gene expression | NAS PMID:34720086 Cul4A-DDB1-mediated monoubiquitination of phosphoglycerate d... | MARK AS OVER ANNOTATED | Summary: NAS rows citing CRL4 ligases that act on chromatin regulators (DNMT1, DNMT3A, SUV39H1, PHGDH). Reason: Over-annotation for RBX1: degrading a chromatin modifier is ubiquitination with an epigenetic consequence, not participation in epigenetic regulation by the ligase subunit itself. Supporting Evidence: PMID:34720086 Cul4A-DDB1-mediated monoubiquitination of phosphoglycerate dehydrogenase promotes colorectal cancer metastasis via increased S-adenosylmethionine. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0042110 T cell activation | IDA PMID:34065512 CRL4-DCAF12 Ubiquitin Ligase Controls MOV10 RNA Helicase dur... | KEEP AS NON CORE | Summary: The same CRL4-DCAF12 ligase controls MOV10 during T-cell activation, and Dcaf12 loss alters CD4+ and NKT populations. Reason: Context-specific immunological output of one DCAF; non-core. Supporting Evidence: PMID:34065512 CRL4-DCAF12 Ubiquitin Ligase Controls MOV10 RNA Helicase during Spermatogenesis and T Cell Activation. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0042127 regulation of cell population proliferation | NAS PMID:33869224 Hippo-Independent Regulation of Yki/Yap/Taz: A Non-canonical... | MARK AS OVER ANNOTATED | Summary: NAS row from a review of Hippo-independent YAP/TAZ regulation. Reason: Over-annotation of a downstream phenotype; the supportable claims are ubiquitination and proteasomal degradation of the relevant substrates. Supporting Evidence: PMID:33869224 Zhao et al., 2010), which is a substrate recognition subunit of a family of modular E3 ubiquitin ligases containing SKP1-Cul1-F-box protein (SCF) complexes (Jiang and Struhl, 1998; file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0042752 regulation of circadian rhythm | NAS PMID:17463251 SCFFbxl3 controls the oscillation of the circadian clock by ... | KEEP AS NON CORE | Summary: SCF(FBXL3) and SCF(FBXL21) ligases containing RBX1 degrade the cryptochromes CRY1/CRY2, setting circadian period. Reason: A well-established F-box-specific output; non-core for the shared catalytic subunit. Supporting Evidence: PMID:17463251 We found that both Cry1 and Cry2 proteins are ubiquitinated and degraded via the SCF(Fbxl3) ubiquitin ligase complex. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0042752 regulation of circadian rhythm | NAS PMID:23452855 Competing E3 ubiquitin ligases govern circadian periodicity ... | KEEP AS NON CORE | Summary: SCF(FBXL3) and SCF(FBXL21) ligases containing RBX1 degrade the cryptochromes CRY1/CRY2, setting circadian period. Reason: A well-established F-box-specific output; non-core for the shared catalytic subunit. Supporting Evidence: PMID:23452855 In Vitro Ubiquitination AssaysCRY1 containing SCF complex were purified from Sf9 cells (Invitrogen) using M2 FLAG agarose. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0042770 signal transduction in response to DNA damage | IDA PMID:24936062 F-box only protein 31 (FBXO31) negatively regulates p38 mito... | KEEP AS NON CORE | Summary: SCF(FBXO31) containing RBX1 mediates K48-linked ubiquitination and degradation of MKK6 after genotoxic stress, damping p38 signalling. Reason: The molecular event RBX1 performs is the ubiquitination; participation in damage signalling is a downstream, receptor-specific consequence. Kept as non-core. Supporting Evidence: PMID:24936062 Here we report that the accumulation of F-box only protein 31 (FBXO31), a component of Skp1 Β· Cul1 Β· F-box protein E3 ligase, negatively regulated p38 activation in cancer cells upon genotoxic stresses. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0042981 regulation of apoptotic process | NAS PMID:25654763 F-box protein Fbxl18 mediates polyubiquitylation and proteas... | MARK AS OVER ANNOTATED | Summary: NAS rows from studies of SCF(FBXL18)/FBXL7 and OTUD1-CRL4(DCAF10)-MCL1 in apoptosis. Reason: Over-annotation: degradation of pro- and anti-apoptotic substrates by different receptors cannot be summed into a role for RBX1 in regulating apoptosis. Supporting Evidence: PMID:25654763 Neddylation-deficient Cul1-Rbx1 largely decreased the polyubiquitylation of Fbxl7, in support that Fbxl7 polyubiquitylation is dependent on a fully functional SCFFbxl18 complex. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0042981 regulation of apoptotic process | NAS PMID:33898171 OTUD1 Activates Caspase-Independent and Caspase-Dependent Ap... | MARK AS OVER ANNOTATED | Summary: NAS rows from studies of SCF(FBXL18)/FBXL7 and OTUD1-CRL4(DCAF10)-MCL1 in apoptosis. Reason: Over-annotation: degradation of pro- and anti-apoptotic substrates by different receptors cannot be summed into a role for RBX1 in regulating apoptosis. Supporting Evidence: PMID:33898171 The ubiquitination reaction is carried out by a threeβstep enzymatic catalysis process involving ubiquitinβactivating enzymes (E1), ubiquitinβconjugating enzymes (E2) and ubiquitin ligases (E3). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0043123 positive regulation of canonical NF-kappaB signal transduction | IDA PMID:10644755 Homodimer of two F-box proteins betaTrCP1 or betaTrCP2 binds... | KEEP AS NON CORE | Summary: SCF(beta-TrCP) ligases containing RBX1 ubiquitinate phosphorylated IkappaB-alpha, releasing NF-kappaB; ROC1 immunocomplexes ubiquitinate phospho-IkappaB-alpha in vitro. Reason: A classic, well-supported SCF output, but positive regulation of NF-kappaB signalling is a pathway-level consequence of one receptor; kept as non-core. Supporting Evidence: PMID:10644755 These results indicate that not only betaTrCP1 but also betaTrCP2 participates in the ubiquitination-dependent destruction of IkappaBalpha by forming SCF(betaTrCP1-betaTrCP1) and SCF(betaTrCP2-betaTrCP2) ubiquitin-ligase complexes. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0043124 negative regulation of canonical NF-kappaB signal transduction | IDA PMID:33010352 The E3 ubiquitin ligase SCF(Fbxo7) mediates proteasomal degr... | KEEP AS NON CORE | Summary: SCF(FBXO7) containing RBX1 degrades UXT isoform 2, dampening NF-kappaB signalling. Reason: Opposite-sign output of a different F-box receptor, which is exactly why such pathway terms are non-core for the shared RING; the annotation itself is defensible. Supporting Evidence: PMID:33010352 Fbxo7 is an F-box protein that interacts with SKP1, Cullin1 and RBX1 proteins to form an SCF(Fbxo7) E3 ubiquitin ligase complex. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IC PMID:36646384 E3 ligase adaptor FBXO7 contributes to ubiquitination and pr... | ACCEPT | Summary: Proteasome-mediated ubiquitin-dependent catabolism of CRL substrates across all cullin families (NRF2, RhoA/RhoB, WNK4, DAPK, TIAM1, p14ARF, RNA Pol II subunits, DEPTOR and others). Reason: Core process; RBX1 catalyses the K48-linked ubiquitination that targets these substrates for degradation. Supporting Evidence: PMID:36646384 For example, the SCFβFBXO7 interaction mediates the ubiquitination and degradation of PINK1 (21). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IDA PMID:10230407 ROC1, a homolog of APC11, represents a family of cullin part... | ACCEPT | Summary: Proteasome-mediated ubiquitin-dependent catabolism of CRL substrates across all cullin families (NRF2, RhoA/RhoB, WNK4, DAPK, TIAM1, p14ARF, RNA Pol II subunits, DEPTOR and others). Reason: Core process; RBX1 catalyses the K48-linked ubiquitination that targets these substrates for degradation. Supporting Evidence: PMID:10230407 ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IDA PMID:15601839 BTB protein Keap1 targets antioxidant transcription factor N... | ACCEPT | Summary: Proteasome-mediated ubiquitin-dependent catabolism of CRL substrates across all cullin families (NRF2, RhoA/RhoB, WNK4, DAPK, TIAM1, p14ARF, RNA Pol II subunits, DEPTOR and others). Reason: Core process; RBX1 catalyses the K48-linked ubiquitination that targets these substrates for degradation. Supporting Evidence: PMID:15601839 BTB protein Keap1 targets antioxidant transcription factor Nrf2 for ubiquitination by the Cullin 3-Roc1 ligase. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IDA PMID:19782033 Cullin mediates degradation of RhoA through evolutionarily c... | ACCEPT | Summary: Proteasome-mediated ubiquitin-dependent catabolism of CRL substrates across all cullin families (NRF2, RhoA/RhoB, WNK4, DAPK, TIAM1, p14ARF, RNA Pol II subunits, DEPTOR and others). Reason: Core process; RBX1 catalyses the K48-linked ubiquitination that targets these substrates for degradation. Supporting Evidence: PMID:19782033 BACURDs form ubiquitin ligase complexes, which selectively ubiquitinate RhoA, with Cul3. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IDA PMID:20389280 The Cullin 3 substrate adaptor KLHL20 mediates DAPK ubiquiti... | ACCEPT | Summary: Proteasome-mediated ubiquitin-dependent catabolism of CRL substrates across all cullin families (NRF2, RhoA/RhoB, WNK4, DAPK, TIAM1, p14ARF, RNA Pol II subunits, DEPTOR and others). Reason: Core process; RBX1 catalyses the K48-linked ubiquitination that targets these substrates for degradation. Supporting Evidence: PMID:20389280 The KLHL20-Cul3-ROC1 E3 ligase complex promotes DAPK polyubiquitination, thereby inducing the proteasomal degradation of DAPK. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IDA PMID:23453970 Impaired KLHL3-mediated ubiquitination of WNK4 causes human ... | ACCEPT | Summary: Proteasome-mediated ubiquitin-dependent catabolism of CRL substrates across all cullin families (NRF2, RhoA/RhoB, WNK4, DAPK, TIAM1, p14ARF, RNA Pol II subunits, DEPTOR and others). Reason: Core process; RBX1 catalyses the K48-linked ubiquitination that targets these substrates for degradation. Supporting Evidence: PMID:23453970 Impaired KLHL3-mediated ubiquitination of WNK4 causes human hypertension. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IDA PMID:29249570 Cullin 3-Based Ubiquitin Ligases as Master Regulators of Mam... | ACCEPT | Summary: Proteasome-mediated ubiquitin-dependent catabolism of CRL substrates across all cullin families (NRF2, RhoA/RhoB, WNK4, DAPK, TIAM1, p14ARF, RNA Pol II subunits, DEPTOR and others). Reason: Core process; RBX1 catalyses the K48-linked ubiquitination that targets these substrates for degradation. Supporting Evidence: PMID:29249570 Cullin 3-Based Ubiquitin Ligases as Master Regulators of Mammalian Cell Differentiation. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IDA PMID:29681526 A Designed Peptide Targets Two Types of Modifications of p53... | ACCEPT | Summary: Proteasome-mediated ubiquitin-dependent catabolism of CRL substrates across all cullin families (NRF2, RhoA/RhoB, WNK4, DAPK, TIAM1, p14ARF, RNA Pol II subunits, DEPTOR and others). Reason: Core process; RBX1 catalyses the K48-linked ubiquitination that targets these substrates for degradation. Supporting Evidence: PMID:29681526 We found that Morn3, a cancer-testis antigen, recruits different PTM enzymes, such as sirtuin deacetylase and ubiquitin ligase, to confer composite modifications on p53. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IDA PMID:29769719 KLHL22 activates amino-acid-dependent mTORC1 signalling to p... | ACCEPT | Summary: Proteasome-mediated ubiquitin-dependent catabolism of CRL substrates across all cullin families (NRF2, RhoA/RhoB, WNK4, DAPK, TIAM1, p14ARF, RNA Pol II subunits, DEPTOR and others). Reason: Core process; RBX1 catalyses the K48-linked ubiquitination that targets these substrates for degradation. Supporting Evidence: PMID:29769719 Here we find that in response to amino acids, the CUL3-KLHL22 E3 ubiquitin ligase promotes K48-linked polyubiquitination and degradation of DEPDC5, an essential subunit of GATOR1. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IDA PMID:29779948 The Eukaryotic Proteome Is Shaped by E3Β Ubiquitin Ligases Ta... | ACCEPT | Summary: Proteasome-mediated ubiquitin-dependent catabolism of CRL substrates across all cullin families (NRF2, RhoA/RhoB, WNK4, DAPK, TIAM1, p14ARF, RNA Pol II subunits, DEPTOR and others). Reason: Core process; RBX1 catalyses the K48-linked ubiquitination that targets these substrates for degradation. Supporting Evidence: PMID:29779948 We characterize eight Cullin-RING E3 ubiquitin ligase (CRL) complex adaptors that regulate C-terminal degrons, including six CRL2 and two CRL4 complexes, and computationally implicate multiple non-CRLs in end recognition. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IDA PMID:34480022 Endotoxin stabilizes protein arginine methyltransferase 4 (P... | ACCEPT | Summary: Proteasome-mediated ubiquitin-dependent catabolism of CRL substrates across all cullin families (NRF2, RhoA/RhoB, WNK4, DAPK, TIAM1, p14ARF, RNA Pol II subunits, DEPTOR and others). Reason: Core process; RBX1 catalyses the K48-linked ubiquitination that targets these substrates for degradation. Supporting Evidence: PMID:34480022 Among E3 ubiquitin ligases, a family of SCF (Skp1-Cullin1-Fbox) E3 proteins have been linked to bacterial infection, antiviral immunity, and host defense [29β36]. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IDA PMID:35687106 ARMC5 is part of an RPB1-specific ubiquitin ligase implicate... | ACCEPT | Summary: Proteasome-mediated ubiquitin-dependent catabolism of CRL substrates across all cullin families (NRF2, RhoA/RhoB, WNK4, DAPK, TIAM1, p14ARF, RNA Pol II subunits, DEPTOR and others). Reason: Core process; RBX1 catalyses the K48-linked ubiquitination that targets these substrates for degradation. Supporting Evidence: PMID:35687106 ARMC5-CUL3-RBX1 as an RPB1-specific E3 based on in vivo and in vitro ubiquitination. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IDA PMID:37788672 Cryo-EM structure of the KLHL22 E3 ligase bound to an oligom... | ACCEPT | Summary: Proteasome-mediated ubiquitin-dependent catabolism of CRL substrates across all cullin families (NRF2, RhoA/RhoB, WNK4, DAPK, TIAM1, p14ARF, RNA Pol II subunits, DEPTOR and others). Reason: Core process; RBX1 catalyses the K48-linked ubiquitination that targets these substrates for degradation. Supporting Evidence: PMID:37788672 CULLIN3KLHL22-RBX1 ligase mediated the polyubiquitination of GDH1 in vitro. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IDA PMID:38225631 ARMC5 controls the degradation of most Pol II subunits, and ... | ACCEPT | Summary: Proteasome-mediated ubiquitin-dependent catabolism of CRL substrates across all cullin families (NRF2, RhoA/RhoB, WNK4, DAPK, TIAM1, p14ARF, RNA Pol II subunits, DEPTOR and others). Reason: Core process; RBX1 catalyses the K48-linked ubiquitination that targets these substrates for degradation. Supporting Evidence: PMID:38225631 ARMC5-CUL3-RBX1 was a novel dominant E3 controlling the degradation of all 12 Pol II subunits under physiological conditions. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IDA PMID:39504960 Redundant pathways for removal of defective RNA polymerase I... | ACCEPT | Summary: Proteasome-mediated ubiquitin-dependent catabolism of CRL substrates across all cullin families (NRF2, RhoA/RhoB, WNK4, DAPK, TIAM1, p14ARF, RNA Pol II subunits, DEPTOR and others). Reason: Core process; RBX1 catalyses the K48-linked ubiquitination that targets these substrates for degradation. Supporting Evidence: PMID:39504960 Tellingly, CUL3 E3 ligase relies on BTB domain-containing proteins as adaptors to recognize substrates for ubiquitylation75, suggesting that ARMC5 might connect CUL3 to RNAPII. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IDA PMID:39667934 CRL3(ARMC5) ubiquitin ligase and Integrator phosphatase form... | ACCEPT | Summary: Proteasome-mediated ubiquitin-dependent catabolism of CRL substrates across all cullin families (NRF2, RhoA/RhoB, WNK4, DAPK, TIAM1, p14ARF, RNA Pol II subunits, DEPTOR and others). Reason: Core process; RBX1 catalyses the K48-linked ubiquitination that targets these substrates for degradation. Supporting Evidence: PMID:39667934 CRL3(ARMC5) ubiquitin ligase and Integrator phosphatase form parallel mechanisms to control early stages of RNA Pol II transcription. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IDA PMID:39880951 C-terminal amides mark proteins for degradation via SCF-FBXO... | ACCEPT | Summary: Proteasome-mediated ubiquitin-dependent catabolism of CRL substrates across all cullin families (NRF2, RhoA/RhoB, WNK4, DAPK, TIAM1, p14ARF, RNA Pol II subunits, DEPTOR and others). Reason: Core process; RBX1 catalyses the K48-linked ubiquitination that targets these substrates for degradation. Supporting Evidence: PMID:39880951 FBXO31 is a substrate receptor for the SKP1-CUL1-F-box protein (SCF) ubiquitin ligase SCF-FBXO31, which ubiquitylates CTAPs for subsequent proteasomal degradation. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | ISS GO_REF:0000024 | ACCEPT | Summary: Proteasome-mediated ubiquitin-dependent catabolism of CRL substrates across all cullin families (NRF2, RhoA/RhoB, WNK4, DAPK, TIAM1, p14ARF, RNA Pol II subunits, DEPTOR and others). Reason: Core process; RBX1 catalyses the K48-linked ubiquitination that targets these substrates for degradation. Supporting Evidence: file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | NAS PMID:22542517 KBTBD13 interacts with Cullin 3 to form a functional ubiquit... | ACCEPT | Summary: Proteasome-mediated ubiquitin-dependent catabolism of CRL substrates across all cullin families (NRF2, RhoA/RhoB, WNK4, DAPK, TIAM1, p14ARF, RNA Pol II subunits, DEPTOR and others). Reason: Core process; RBX1 catalyses the K48-linked ubiquitination that targets these substrates for degradation. Supporting Evidence: PMID:22542517 Taken together, our data demonstrate that KBTBD13βCul3βRbx1 is a muscle specific ubiquitin ligase. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | NAS PMID:22632832 Adaptor protein self-assembly drives the control of a cullin... | ACCEPT | Summary: Proteasome-mediated ubiquitin-dependent catabolism of CRL substrates across all cullin families (NRF2, RhoA/RhoB, WNK4, DAPK, TIAM1, p14ARF, RNA Pol II subunits, DEPTOR and others). Reason: Core process; RBX1 catalyses the K48-linked ubiquitination that targets these substrates for degradation. Supporting Evidence: PMID:22632832 Adaptor protein self-assembly drives the control of a cullin-RING ubiquitin ligase. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | NAS PMID:25684205 CUL3-KBTBD6/KBTBD7 ubiquitin ligase cooperates with GABARAP ... | ACCEPT | Summary: Proteasome-mediated ubiquitin-dependent catabolism of CRL substrates across all cullin families (NRF2, RhoA/RhoB, WNK4, DAPK, TIAM1, p14ARF, RNA Pol II subunits, DEPTOR and others). Reason: Core process; RBX1 catalyses the K48-linked ubiquitination that targets these substrates for degradation. Supporting Evidence: PMID:25684205 CUL3-KBTBD6/KBTBD7 ubiquitin ligase cooperates with GABARAP proteins to spatially restrict TIAM1-RAC1 signaling. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | NAS PMID:26399832 Cell-fate determination by ubiquitin-dependent regulation of... | ACCEPT | Summary: Proteasome-mediated ubiquitin-dependent catabolism of CRL substrates across all cullin families (NRF2, RhoA/RhoB, WNK4, DAPK, TIAM1, p14ARF, RNA Pol II subunits, DEPTOR and others). Reason: Core process; RBX1 catalyses the K48-linked ubiquitination that targets these substrates for degradation. Supporting Evidence: PMID:26399832 CUL3(KBTBD8) monoubiquitylates NOLC1 and its paralogue TCOF1, the mutation of which underlies the neurocristopathy Treacher Collins syndrome. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | NAS PMID:29249570 Cullin 3-Based Ubiquitin Ligases as Master Regulators of Mam... | ACCEPT | Summary: Proteasome-mediated ubiquitin-dependent catabolism of CRL substrates across all cullin families (NRF2, RhoA/RhoB, WNK4, DAPK, TIAM1, p14ARF, RNA Pol II subunits, DEPTOR and others). Reason: Core process; RBX1 catalyses the K48-linked ubiquitination that targets these substrates for degradation. Supporting Evidence: PMID:29249570 Cullin 3-Based Ubiquitin Ligases as Master Regulators of Mammalian Cell Differentiation. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | NAS PMID:31273098 A glycine-specific N-degron pathway mediates the quality con... | ACCEPT | Summary: Proteasome-mediated ubiquitin-dependent catabolism of CRL substrates across all cullin families (NRF2, RhoA/RhoB, WNK4, DAPK, TIAM1, p14ARF, RNA Pol II subunits, DEPTOR and others). Reason: Core process; RBX1 catalyses the K48-linked ubiquitination that targets these substrates for degradation. Supporting Evidence: PMID:31273098 In addition to uncovering extended specificities of UBR E3 ligases, we characterized two related Cullin-RING E3 ligase complexes, Cul2ZYG11B and Cul2ZER1, that act redundantly to target N-terminal glycine. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | NAS PMID:31898230 CRL3s: The BTB-CUL3-RING E3 Ubiquitin Ligases. | ACCEPT | Summary: Proteasome-mediated ubiquitin-dependent catabolism of CRL substrates across all cullin families (NRF2, RhoA/RhoB, WNK4, DAPK, TIAM1, p14ARF, RNA Pol II subunits, DEPTOR and others). Reason: Core process; RBX1 catalyses the K48-linked ubiquitination that targets these substrates for degradation. Supporting Evidence: PMID:31898230 In most of Cullin-RING ubiquitin ligase (CRL) complexes, separate linker and adaptor proteins build the substrate recognition module. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | NAS PMID:37628845 The Role of PIK3R1 in Metabolic Function and Insulin Sensiti... | ACCEPT | Summary: Proteasome-mediated ubiquitin-dependent catabolism of CRL substrates across all cullin families (NRF2, RhoA/RhoB, WNK4, DAPK, TIAM1, p14ARF, RNA Pol II subunits, DEPTOR and others). Reason: Core process; RBX1 catalyses the K48-linked ubiquitination that targets these substrates for degradation. Supporting Evidence: PMID:37628845 KBTBD2 interacts with CUL3 and the iSH2 domain of p85Ξ± and leads to the degradation of p85Ξ± [69]. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0043687 post-translational protein modification | TAS Reactome:R-HSA-597592 | MARK AS OVER ANNOTATED | Summary: Reactome's top-level 'post-translational protein modification' assignment for RBX1. Reason: Correct but uninformatively broad; protein ubiquitination (GO:0016567) and protein neddylation (GO:0045116) are the modifications RBX1 actually catalyses. Supporting Evidence: Reactome:R-HSA-597592 After translation, many newly formed proteins undergo further covalent modifications that alter their functional properties. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0044314 protein K27-linked ubiquitination | IDA PMID:40307251 F-box protein FBXO32 ubiquitinates and stabilizes D-type cyc... | ACCEPT | Summary: K27-linked ubiquitination by an SCF(FBXO32) ligase, in which the modification stabilises rather than destroys D-type cyclins. Reason: Accepted as another linkage type produced by the shared RING; RBX1 performs the transfer, while the unusual (stabilising) outcome is a property of the receptor and substrate. Supporting Evidence: PMID:40307251 F-box protein FBXO32 ubiquitinates and stabilizes D-type cyclins to drive cancer progression. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0045116 protein neddylation | IDA PMID:19250909 E2-RING expansion of the NEDD8 cascade confers specificity t... | ACCEPT | Summary: Protein neddylation: RBX1 with UBE2M transfers NEDD8 onto the conserved lysine of CUL1-CUL4, the modification that activates their ligases. Reason: Core process, distinct from the ubiquitination role and supported by the RBX1-UBC12~NEDD8-CUL1-DCN1 structure and the UniProt neddylation pathway assignment. Supporting Evidence: PMID:19250909 The largest ubiquitin E3 subclass consists of cullin-RING ligases (CRLs), which contain one each of several cullins (CUL1, -2, -3, -4, or -5) and RING proteins (RBX1 or -2). file:human/RBX1/RBX1-uniprot.txt Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 also works with UBE2M~NEDD8 to neddylate cullins and activate CRLs. |
| GO:0045116 protein neddylation | IEA GO_REF:0000041 | ACCEPT | Summary: Protein neddylation: RBX1 with UBE2M transfers NEDD8 onto the conserved lysine of CUL1-CUL4, the modification that activates their ligases. Reason: Core process, distinct from the ubiquitination role and supported by the RBX1-UBC12~NEDD8-CUL1-DCN1 structure and the UniProt neddylation pathway assignment. Supporting Evidence: file:human/RBX1/RBX1-uniprot.txt Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 also works with UBE2M~NEDD8 to neddylate cullins and activate CRLs. |
| GO:0045724 positive regulation of cilium assembly | IDA PMID:29358211 The Cullin-3-Rbx1-KCTD10 complex controls endothelial barrie... | KEEP AS NON CORE | Summary: Author-supported role of CUL3-RBX1 ligases in ciliogenesis, alongside the KCTD10-dependent control of RhoB. Reason: Kept as a non-core, receptor-specific output; RBX1's molecular contribution is the ubiquitin transfer. Supporting Evidence: PMID:29358211 The Cullin-3-Rbx1-KCTD10 complex controls endothelial barrier function via K63 ubiquitination of RhoB. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0045732 positive regulation of protein catabolic process | IDA PMID:11027288 The CUL1 C-terminal sequence and ROC1 are required for effic... | MODIFY | Summary: IDA rows in which an RBX1-containing ligase (CUL1-ROC1 toward IkappaB-alpha, SCF(SKP2)/CRL4(CDT2) toward CDT1, CRL4(HBx) toward SMC5/6) promotes degradation of a substrate. Reason: RBX1 does not regulate catabolism from outside; it catalyses the ubiquitination that commits the substrate to the proteasome. Proteasome-mediated ubiquitin-dependent protein catabolic process (GO:0043161) states the participation directly, and is already annotated from other references. Proposed replacements: proteasome-mediated ubiquitin-dependent protein catabolic process Supporting Evidence: PMID:11027288 The CUL1 C-terminal sequence and ROC1 are required for efficient nuclear accumulation, NEDD8 modification, and ubiquitin ligase activity of CUL1. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0045732 positive regulation of protein catabolic process | IDA PMID:16482215 Two E3 ubiquitin ligases, SCF-Skp2 and DDB1-Cul4, target hum... | MODIFY | Summary: IDA rows in which an RBX1-containing ligase (CUL1-ROC1 toward IkappaB-alpha, SCF(SKP2)/CRL4(CDT2) toward CDT1, CRL4(HBx) toward SMC5/6) promotes degradation of a substrate. Reason: RBX1 does not regulate catabolism from outside; it catalyses the ubiquitination that commits the substrate to the proteasome. Proteasome-mediated ubiquitin-dependent protein catabolic process (GO:0043161) states the participation directly, and is already annotated from other references. Proposed replacements: proteasome-mediated ubiquitin-dependent protein catabolic process Supporting Evidence: PMID:16482215 This suggests that SCF-Skp2 is a major degradation pathway in this cell line. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0045732 positive regulation of protein catabolic process | IDA PMID:27626656 Hepatitis B Virus X Protein Promotes Degradation of SMC5/6 t... | MODIFY | Summary: IDA rows in which an RBX1-containing ligase (CUL1-ROC1 toward IkappaB-alpha, SCF(SKP2)/CRL4(CDT2) toward CDT1, CRL4(HBx) toward SMC5/6) promotes degradation of a substrate. Reason: RBX1 does not regulate catabolism from outside; it catalyses the ubiquitination that commits the substrate to the proteasome. Proteasome-mediated ubiquitin-dependent protein catabolic process (GO:0043161) states the participation directly, and is already annotated from other references. Proposed replacements: proteasome-mediated ubiquitin-dependent protein catabolic process Supporting Evidence: PMID:27626656 These findings suggest that HBx may assemble an HBx-DDB1-CUL4-ROC1 E3 ligase complex (referred to as CRL4HBx hereafter) to target host proteins that antagonize HBV replication for ubiquitylation and degradation. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0045879 negative regulation of smoothened signaling pathway | TAS PMID:16705181 Multisite protein kinase A and glycogen synthase kinase 3bet... | KEEP AS NON CORE | Summary: SCF(beta-TrCP) containing RBX1 ubiquitinates phosphorylated GLI3 (and GLI1/GLI2 via CUL3-SPOP), promoting the processing/degradation that represses Hedgehog signalling. Reason: Real pathway output through beta-TrCP and SPOP; kept as non-core. Supporting Evidence: PMID:16705181 Multisite protein kinase A and glycogen synthase kinase 3beta phosphorylation leads to Gli3 ubiquitination by SCFbetaTrCP. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0045995 regulation of embryonic development | NAS PMID:30111536 DCAF13 promotes pluripotency by negatively regulating SUV39H... | KEEP AS NON CORE | Summary: CRL4-DCAF13 containing RBX1 degrades SUV39H1 during early embryonic development. Reason: Receptor-specific developmental role; kept as non-core. Supporting Evidence: PMID:30111536 Mechanistically, CRL4-DCAF13 targets SUV39H1 for polyubiquitination and proteasomal degradation and therefore facilitates H3K9me3 removal and zygotic gene expression. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0046627 negative regulation of insulin receptor signaling pathway | IDA PMID:18498745 The CUL7 E3 ubiquitin ligase targets insulin receptor substr... | KEEP AS NON CORE | Summary: The CUL7-SKP1-FBXW8-RBX1 ligase degrades IRS1, attenuating insulin/IGF1 signalling. Reason: Genuine but receptor-specific (FBXW8); kept as non-core. Supporting Evidence: PMID:18498745 Recent genetic studies have documented a pivotal growth-regulatory role played by the Cullin 7 (CUL7) E3 ubiquitin ligase complex containing the Fbw8-substrate-targeting subunit, Skp1, and the ROC1 RING finger protein. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0050727 regulation of inflammatory response | NAS PMID:23542741 A combinatorial F box protein directed pathway controls TRAF... | KEEP AS NON CORE | Summary: SCF(FBXO3) containing RBX1 destabilises FBXL2 and thereby raises TRAF levels and cytokine output. Reason: Receptor-specific inflammatory output; non-core. Supporting Evidence: PMID:23542741 The SCF apparatus contains Rbx1 and Cullin1, which form a scaffold to link the E2 conjugating enzyme (Ubc) with a substrate specificity module 14β16. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0050727 regulation of inflammatory response | NAS PMID:35127719 Diverse Roles of F-BoxProtein3 in Regulation of Various Cell... | KEEP AS NON CORE | Summary: SCF(FBXO3) containing RBX1 destabilises FBXL2 and thereby raises TRAF levels and cytokine output. Reason: Receptor-specific inflammatory output; non-core. Supporting Evidence: PMID:35127719 The ubiquitin protein ligase complex Skp1-Cullin1-F-Box (SCF) is composed of four subunits: F-box protein, SKP1, CULLIN1, and RBX1 (Skaar et al., 2014). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0051298 centrosome duplication | NAS PMID:34388369 Structure of the human signal peptidase complex reveals the ... | MODIFY | Summary: NAS row for centrosome duplication; the cited reference is the cryo-EM structure of the human signal peptidase complex, which does not concern RBX1. Reason: The identifier does not support the claim, and even on the real evidence (SCF(cyclin F) degrading CP110, SCF(FBXL13) degrading CEP192) RBX1 restrains rather than executes centrosome duplication. Regulation of centrosome duplication (GO:0010824), already annotated, is the defensible term. Proposed replacements: regulation of centrosome duplication Supporting Evidence: PMID:34388369 Structure of the human signal peptidase complex reveals the determinants for signal peptide cleavage. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0051726 regulation of cell cycle | NAS PMID:33234069 The FBXL family of F-box proteins: variations on a theme. | MARK AS OVER ANNOTATED | Summary: NAS row from a review of the FBXL family. Reason: Over-annotation: too broad for the shared catalytic subunit, and redundant with the SCF-dependent proteolysis and G1/S annotations. Supporting Evidence: PMID:33234069 Rbx1 engages an E2 enzyme conjugated to activated ubiquitin, thus enabling the direct transfer of ubiquitin to the substrate (figure 1). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0060090 molecular adaptor activity | EXP PMID:11961546 Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin liga... | MODIFY | Summary: From the SCF(SKP2) crystal structure: CUL1 holds the SKP1-F-box receptor module and RBX1 more than 100 A apart, with RBX1 forming the two-subunit catalytic core that recruits the ubiquitin-conjugating enzyme. Reason: 'Molecular adaptor activity' understates and mistypes RBX1's role: the scaffolding is done by CUL1 (GO:0160072), while RBX1 recruits and activates the E2. Ubiquitin conjugating enzyme binding captures what the structure shows; the catalytic consequence is already annotated as GO:0061630. Proposed replacements: ubiquitin conjugating enzyme binding Supporting Evidence: PMID:11961546 Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex. file:human/RBX1/RBX1-uniprot.txt Recruits the E2 ubiquitin-conjugating enzyme CDC34 to the complex and brings it into close proximity to the substrate. file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0060173 limb development | NAS PMID:10471509 A novel member of the F-box/WD40 gene family, encoding dacty... | MARK AS OVER ANNOTATED | Summary: NAS row citing the positional cloning of mouse dactylaplasia (Dac/Fbxw4), an F-box/WD40 gene required for maintenance of the apical ectodermal ridge. Reason: Over-annotation: the reference concerns a mouse F-box protein, not RBX1, and limb development is far downstream of the shared RING's activity. Supporting Evidence: PMID:10471509 We report here the positional cloning of Dac and show that it belongs to the F-box/WD40 gene family, which encodes adapters that target specific proteins for destruction by presenting them to the ubiquitination machinery. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0060271 cilium assembly | NAS PMID:34368969 SCF(Fbxw5) targets kinesin-13 proteins to facilitate cilioge... | KEEP AS NON CORE | Summary: SCF(FBXW5) containing RBX1 degrades kinesin-13 proteins (MCAK, KIF2A/B) in G2, permitting ciliogenesis in the following G1/G0. Reason: Genuine but FBXW5-specific; non-core for the shared RING. Supporting Evidence: PMID:34368969 SCFFbxw5 complexes for all ubiquitylation experiments were prepared by mixing equimolar amounts of Fbxw5/Skp1 and Cul1ΛNedd8/Rbx1 subβcomplexes. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0060964 regulation of miRNA-mediated gene silencing | NAS PMID:34065512 CRL4-DCAF12 Ubiquitin Ligase Controls MOV10 RNA Helicase dur... | KEEP AS NON CORE | Summary: CRL4-DCAF12-mediated turnover of MOV10, a RISC-associated helicase, links RBX1-dependent proteolysis to miRNA-mediated silencing. Reason: Indirect, receptor-specific effect; kept as non-core. Supporting Evidence: PMID:34065512 CRL4-DCAF12 Ubiquitin Ligase Controls MOV10 RNA Helicase during Spermatogenesis and T Cell Activation. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0061629 RNA polymerase II-specific DNA-binding transcription factor binding | IPI PMID:14739464 Human De-etiolated-1 regulates c-Jun by assembling a CUL4A u... | REMOVE | Summary: IPI row pairing RBX1 with c-Jun (JUN) in the study that defined the CUL4A-DDB1-DET1-COP1-ROC1 ligase for c-Jun. Reason: c-Jun is the substrate of this ligase, and it is recruited by COP1/DET1, not by RBX1; RBX1 contributes the catalytic RING. Annotating RBX1 with transcription factor binding attributes the receptor's specificity to the shared catalytic subunit. The informative statements from this paper (protein ubiquitination, CRL4A complex membership) are annotated separately. Supporting Evidence: PMID:14739464 Human De-etiolated-1 regulates c-Jun by assembling a CUL4A ubiquitin ligase. file:human/RBX1/RBX1-uniprot.txt The functional specificity of the E3 ubiquitin-protein ligase complexes depends on the variable substrate recognition components. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 supplies catalytic E2 recruitment but ordinarily does **not** select protein substrates by itself. |
| GO:0061630 ubiquitin protein ligase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000129805 Β· PANTHER:PTN000129805 SUPPORTS TRANSFER RING-box family node spanning RBX1, RBX2/RNF7 and APC11; the descendant experimental evidence includes human RBX1 itself, mouse Rbx1, fly Roc1a/Roc1b and yeast Hrt1/Rbx1 and Apc11, so the function is inherited rather than lineage-specific. Supporting Evidence: file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | IC PMID:24936062 F-box only protein 31 (FBXO31) negatively regulates p38 mito... | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: PMID:24936062 Here we report that the accumulation of F-box only protein 31 (FBXO31), a component of Skp1 Β· Cul1 Β· F-box protein E3 ligase, negatively regulated p38 activation in cancer cells upon genotoxic stresses. file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | IC PMID:26124108 F-box protein FBXO31 directs degradation of MDM2 to facilita... | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: PMID:26124108 Following DNA damage, MDM2 is degraded rapidly, resulting in increased p53 stability. file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | IC PMID:30171069 The SCF(FBXO46) ubiquitin ligase complex mediates degradatio... | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: PMID:30171069 The SCF(FBXO46) ubiquitin ligase complex mediates degradation of the tumor suppressor FBXO31 and thereby prevents premature cellular senescence. file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | IDA PMID:10230407 ROC1, a homolog of APC11, represents a family of cullin part... | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: PMID:10230407 ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity. file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | IDA PMID:11027288 The CUL1 C-terminal sequence and ROC1 are required for effic... | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: PMID:11027288 The CUL1 C-terminal sequence and ROC1 are required for efficient nuclear accumulation, NEDD8 modification, and ubiquitin ligase activity of CUL1. file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | IDA PMID:15601839 BTB protein Keap1 targets antioxidant transcription factor N... | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: PMID:15601839 BTB protein Keap1 targets antioxidant transcription factor Nrf2 for ubiquitination by the Cullin 3-Roc1 ligase. file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | IDA PMID:16482215 Two E3 ubiquitin ligases, SCF-Skp2 and DDB1-Cul4, target hum... | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: PMID:16482215 This suggests that SCF-Skp2 is a major degradation pathway in this cell line. file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | IDA PMID:17636018 ASB4 is a hydroxylation substrate of FIH and promotes vascul... | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: PMID:17636018 Like other SOCS box-containing proteins, ASB4 is the substrate recognition molecule of an elongin B/elongin C/cullin/Roc ubiquitin ligase complex that mediates the ubiquitination and degradation of substrate protein(s). file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | IDA PMID:18498745 The CUL7 E3 ubiquitin ligase targets insulin receptor substr... | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: PMID:18498745 Recent genetic studies have documented a pivotal growth-regulatory role played by the Cullin 7 (CUL7) E3 ubiquitin ligase complex containing the Fbw8-substrate-targeting subunit, Skp1, and the ROC1 RING finger protein. file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | IDA PMID:19782033 Cullin mediates degradation of RhoA through evolutionarily c... | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: PMID:19782033 BACURDs form ubiquitin ligase complexes, which selectively ubiquitinate RhoA, with Cul3. file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | IDA PMID:20870715 HIV-1 Vpr loads uracil DNA glycosylase-2 onto DCAF1, a subst... | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: PMID:20870715 To date, three of the four HIV-1 accessory proteins, including Vpr, have been found to interact with cullin-RING finger E3 ubiquitin ligases (CRLs). file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | IDA PMID:22017875 mTOR drives its own activation via SCF(Ξ²TrCP)-dependent degr... | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: PMID:22017875 To purify SCFΞ²-TRCP complex, 293T cells were transfected with vectors encoding GST-Ξ²-TRCP1, Myc-Cul-1, Myc-Skp1, and HA-Rbx1. file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | IDA PMID:22017876 DEPTOR, an mTOR inhibitor, is a physiological substrate of S... | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: PMID:22017876 Here we report that DEPTOR is a physiological substrate of SCF(Ξ²TrCP) E3 ligase for targeted degradation. file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | IDA PMID:22405651 The glomuvenous malformation protein Glomulin binds Rbx1 and... | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: PMID:22405651 The glomuvenous malformation protein Glomulin binds Rbx1 and regulates cullin RING ligase-mediated turnover of Fbw7. file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | IDA PMID:23453970 Impaired KLHL3-mediated ubiquitination of WNK4 causes human ... | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: PMID:23453970 Impaired KLHL3-mediated ubiquitination of WNK4 causes human hypertension. file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | IDA PMID:27626656 Hepatitis B Virus X Protein Promotes Degradation of SMC5/6 t... | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: PMID:27626656 These findings suggest that HBx may assemble an HBx-DDB1-CUL4-ROC1 E3 ligase complex (referred to as CRL4HBx hereafter) to target host proteins that antagonize HBV replication for ubiquitylation and degradation. file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | IDA PMID:29779948 The Eukaryotic Proteome Is Shaped by E3Β Ubiquitin Ligases Ta... | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: PMID:29779948 We characterize eight Cullin-RING E3 ubiquitin ligase (CRL) complex adaptors that regulate C-terminal degrons, including six CRL2 and two CRL4 complexes, and computationally implicate multiple non-CRLs in end recognition. file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | IDA PMID:34526721 Structural basis of human transcription-DNA repair coupling. | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: PMID:34526721 RBX1 and the E2 enzymeβdonor ubiquitin complex were modelled as described in the Methods. file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | IDA PMID:35687106 ARMC5 is part of an RPB1-specific ubiquitin ligase implicate... | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: PMID:35687106 ARMC5-CUL3-RBX1 as an RPB1-specific E3 based on in vivo and in vitro ubiquitination. file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | IDA PMID:36608670 A central role for regulated protein stability in the contro... | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: PMID:36608670 The pulse reaction was quenched for 5 minutes on ice with 50 mM EDTA, and *ubiquitin was chased from UBE2D2 to SCF substrates. file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | IDA PMID:37844242 Molecular basis for C-degron recognition by CRL2(APPBP2) ubi... | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: PMID:37844242 Cryo-EM samples were generated by mixing two complexes, APPBP2-EB-EC-Peptide and NEDD8-CUL2ΞΒ·RBX1, in a 1:1 ratio. file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | IDA PMID:38225631 ARMC5 controls the degradation of most Pol II subunits, and ... | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: PMID:38225631 ARMC5-CUL3-RBX1 was a novel dominant E3 controlling the degradation of all 12 Pol II subunits under physiological conditions. file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | IDA PMID:39504960 Redundant pathways for removal of defective RNA polymerase I... | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: PMID:39504960 Tellingly, CUL3 E3 ligase relies on BTB domain-containing proteins as adaptors to recognize substrates for ubiquitylation75, suggesting that ARMC5 might connect CUL3 to RNAPII. file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | IDA PMID:39667934 CRL3(ARMC5) ubiquitin ligase and Integrator phosphatase form... | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: PMID:39667934 CRL3(ARMC5) ubiquitin ligase and Integrator phosphatase form parallel mechanisms to control early stages of RNA Pol II transcription. file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | IDA PMID:39880951 C-terminal amides mark proteins for degradation via SCF-FBXO... | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: PMID:39880951 FBXO31 is a substrate receptor for the SKP1-CUL1-F-box protein (SCF) ubiquitin ligase SCF-FBXO31, which ubiquitylates CTAPs for subsequent proteasomal degradation. file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | IEA GO_REF:0000003 | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | ISS GO_REF:0000024 | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | TAS Reactome:R-HSA-1504190 | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: Reactome:R-HSA-1504190 CUL3:KLHL12:RBX1 polyubiquitinates Dishevelled, targeting it for degradation by the proteasome (Angers et al, 2006). file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | TAS Reactome:R-HSA-5635856 | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: Reactome:R-HSA-5635856 The transcriptional activity of full-length activated Ci/GLI proteins is restricted by their rapid ubiquitin-mediated degradation after initiation of Hh signaling (Ohlmeyer et al, 1998; Humke et al, 2010; Tukachinsky et al, 2010; Wen et al, 2010). file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | TAS Reactome:R-HSA-5658424 | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: Reactome:R-HSA-5658424 NF1 levels are controlled by proteasomal degradation in response to stimulation by some growth factors (Cichowski et al, 2003). file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | TAS Reactome:R-HSA-9755505 | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: Reactome:R-HSA-9755505 The KEAP1:CUL3:RBX1 E3-ubiquitin ligase complex is a negative regulator of Nuclear factor erythroid 2-related (NFE2L2). file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | TAS Reactome:R-HSA-9759172 | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: Reactome:R-HSA-9759172 SQSTM1 is an adaptor protein that mediates aggregation of target proteins for selective autophagy (reviewed in Lamark et al, 2017). file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | TAS Reactome:R-HSA-9762091 | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: Reactome:R-HSA-9762091 GSK3-dependent phosphorylation of NFE2L2 promotes its subsequent ubiquitination by a BTRC:CUL1 E3 ligase complex (Salazar et al, 2006; Rada et al, 2011; Rada et al, 2012; Rojo et al, 2012; reviewed in Baird and Yamamoto, 2020; Yamamoto et al, 2018). file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061630 ubiquitin protein ligase activity | TAS Reactome:R-HSA-9766645 | ACCEPT | Summary: Core molecular function: RBX1 is the RING E3 of cullin-RING ligases, binding ubiquitin-charged E2s (CDC34/UBE2R, UBE2D) and positioning them for transfer onto substrates recruited by the cullin's receptor module. Reason: This is the central, repeatedly reconstituted activity of RBX1: RING mutations abolish ligase activity of ROC1 immunocomplexes without disturbing complex assembly, and every CRL reconstitution cited here depends on RBX1 for ubiquitin transfer. Supporting Evidence: Reactome:R-HSA-9766645 KEAP1 is ubiquitinated by the CUL3:RBX1 complex in an SQSTM1-dependent manner (Zhang et al, 2005). file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0061663 NEDD8 ligase activity | IDA PMID:19250909 E2-RING expansion of the NEDD8 cascade confers specificity t... | ACCEPT | Summary: NEDD8 ligase activity of the RBX1-UBE2M pair that activates cullin-RING ligases by neddylating the cullin C-terminal domain. Reason: Core function; the EC 2.3.2.32 mapping and the IDA from the UBE2M/UBE2F specificity study agree, and cullin neddylation is what couples RBX1's two catalytic roles (it neddylates the cullin that in turn reorients its own RING for ubiquitin transfer). Supporting Evidence: PMID:19250909 The largest ubiquitin E3 subclass consists of cullin-RING ligases (CRLs), which contain one each of several cullins (CUL1, -2, -3, -4, or -5) and RING proteins (RBX1 or -2). file:human/RBX1/RBX1-uniprot.txt Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 also works with UBE2M~NEDD8 to neddylate cullins and activate CRLs. |
| GO:0061663 NEDD8 ligase activity | IEA GO_REF:0000003 | ACCEPT | Summary: NEDD8 ligase activity of the RBX1-UBE2M pair that activates cullin-RING ligases by neddylating the cullin C-terminal domain. Reason: Core function; the EC 2.3.2.32 mapping and the IDA from the UBE2M/UBE2F specificity study agree, and cullin neddylation is what couples RBX1's two catalytic roles (it neddylates the cullin that in turn reorients its own RING for ubiquitin transfer). Supporting Evidence: file:human/RBX1/RBX1-uniprot.txt Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M. file:human/RBX1/RBX1-deep-research-falcon.md RBX1 also works with UBE2M~NEDD8 to neddylate cullins and activate CRLs. |
| GO:0062197 cellular response to chemical stress | TAS Reactome:R-HSA-9711123 | KEEP AS NON CORE | Summary: Reactome assigns RBX1-containing CRL3(KEAP1) activity to the cellular response to chemical stress (the NRF2 pathway). Reason: Defensible as pathway context; non-core for the shared RING, whose direct role is NRF2 ubiquitination. Supporting Evidence: Reactome:R-HSA-9711123 Cells are equipped with versatile physiological stress responses to prevent hazardous consequences resulting from exposure to chemical insults of endogenous and exogenous origin. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0070534 protein K63-linked ubiquitination | IDA PMID:29358211 The Cullin-3-Rbx1-KCTD10 complex controls endothelial barrie... | ACCEPT | Summary: The CUL3-RBX1-KCTD10 ligase attaches K63-linked chains to RhoB, targeting it to lysosomes rather than the proteasome. Reason: Core chemistry in a non-degradative mode; the linkage type is set by the E2 and assembly geometry, not by a different RBX1 activity. Supporting Evidence: PMID:29358211 The Cullin-3-Rbx1-KCTD10 complex controls endothelial barrier function via K63 ubiquitination of RhoB. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0070936 protein K48-linked ubiquitination | IC PMID:36646384 E3 ligase adaptor FBXO7 contributes to ubiquitination and pr... | ACCEPT | Summary: K48-linked polyubiquitination by RBX1-containing CRLs - shown for c-Myc (SCF(FBXW7)), TIAM1 (CRL3(KBTBD6/7)), p85alpha (CRL3(KBTBD2)) and NRF2 (CUL3-KEAP1-RBX1, where arsenite binding to the RBX1 RING blocks it). Reason: Core process and the predominant chain type built by CRLs; the arsenite study is direct evidence that the RBX1 RING is the catalytic element for this linkage. Supporting Evidence: PMID:36646384 For example, the SCFβFBXO7 interaction mediates the ubiquitination and degradation of PINK1 (21). file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity |
| GO:0070936 protein K48-linked ubiquitination | IDA PMID:15103331 Phosphorylation-dependent degradation of c-Myc is mediated b... | ACCEPT | Summary: K48-linked polyubiquitination by RBX1-containing CRLs - shown for c-Myc (SCF(FBXW7)), TIAM1 (CRL3(KBTBD6/7)), p85alpha (CRL3(KBTBD2)) and NRF2 (CUL3-KEAP1-RBX1, where arsenite binding to the RBX1 RING blocks it). Reason: Core process and the predominant chain type built by CRLs; the arsenite study is direct evidence that the RBX1 RING is the catalytic element for this linkage. Supporting Evidence: PMID:15103331 The SCF complex consists of four components: the invariable subunits Skp1, Cul1 (also known as Cdc53) and Rbx1 (Roc1, Hrt1) and a variable F-box protein that serves as a receptor for target proteins and thereby determines target specificity ( Elledge and Harper, 1998 ; file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity |
| GO:0070936 protein K48-linked ubiquitination | IDA PMID:25684205 CUL3-KBTBD6/KBTBD7 ubiquitin ligase cooperates with GABARAP ... | ACCEPT | Summary: K48-linked polyubiquitination by RBX1-containing CRLs - shown for c-Myc (SCF(FBXW7)), TIAM1 (CRL3(KBTBD6/7)), p85alpha (CRL3(KBTBD2)) and NRF2 (CUL3-KEAP1-RBX1, where arsenite binding to the RBX1 RING blocks it). Reason: Core process and the predominant chain type built by CRLs; the arsenite study is direct evidence that the RBX1 RING is the catalytic element for this linkage. Supporting Evidence: PMID:25684205 CUL3-KBTBD6/KBTBD7 ubiquitin ligase cooperates with GABARAP proteins to spatially restrict TIAM1-RAC1 signaling. file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity |
| GO:0070936 protein K48-linked ubiquitination | IDA PMID:27708159 Insulin resistance and diabetes caused by genetic or diet-in... | ACCEPT | Summary: K48-linked polyubiquitination by RBX1-containing CRLs - shown for c-Myc (SCF(FBXW7)), TIAM1 (CRL3(KBTBD6/7)), p85alpha (CRL3(KBTBD2)) and NRF2 (CUL3-KEAP1-RBX1, where arsenite binding to the RBX1 RING blocks it). Reason: Core process and the predominant chain type built by CRLs; the arsenite study is direct evidence that the RBX1 RING is the catalytic element for this linkage. Supporting Evidence: PMID:27708159 Kbtbd2 encodes a BTB-Kelch family substrate recognition subunit of the Cullin-3-based E3 ubiquitin ligase. file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity |
| GO:0070936 protein K48-linked ubiquitination | IDA PMID:29658272 Arsenite Targets the RING Finger Domain of Rbx1 E3 Ubiquitin... | ACCEPT | Summary: K48-linked polyubiquitination by RBX1-containing CRLs - shown for c-Myc (SCF(FBXW7)), TIAM1 (CRL3(KBTBD6/7)), p85alpha (CRL3(KBTBD2)) and NRF2 (CUL3-KEAP1-RBX1, where arsenite binding to the RBX1 RING blocks it). Reason: Core process and the predominant chain type built by CRLs; the arsenite study is direct evidence that the RBX1 RING is the catalytic element for this linkage. Supporting Evidence: PMID:29658272 It is well established that Nrf2 is ubiquitinated by the Keap1βCul3βRbx1 E3 ligase complex.36 When endogenous Rbx1 was depleted using siRNA, the ubiquitination level of Nrf2 was dramatically decreased (Figure 5c, lanes 1β2). file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity |
| GO:0070936 protein K48-linked ubiquitination | IEA GO_REF:0000117 | ACCEPT | Summary: K48-linked polyubiquitination by RBX1-containing CRLs - shown for c-Myc (SCF(FBXW7)), TIAM1 (CRL3(KBTBD6/7)), p85alpha (CRL3(KBTBD2)) and NRF2 (CUL3-KEAP1-RBX1, where arsenite binding to the RBX1 RING blocks it). Reason: Core process and the predominant chain type built by CRLs; the arsenite study is direct evidence that the RBX1 RING is the catalytic element for this linkage. Supporting Evidence: file:human/RBX1/RBX1-uniprot.txt The RING-type zinc finger domain is essential for ubiquitin ligase activity |
| GO:0071230 cellular response to amino acid stimulus | IDA PMID:29769719 KLHL22 activates amino-acid-dependent mTORC1 signalling to p... | KEEP AS NON CORE | Summary: The same CUL3-KLHL22-RBX1 event is triggered by amino-acid stimulation. Reason: Context-specific stimulus response mediated by a single receptor; non-core. Supporting Evidence: PMID:29769719 Here we find that in response to amino acids, the CUL3-KLHL22 E3 ubiquitin ligase promotes K48-linked polyubiquitination and degradation of DEPDC5, an essential subunit of GATOR1. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0080008 Cul4-RING E3 ubiquitin ligase complex | IDA PMID:32355176 The cooperative action of CSB, CSA, and UVSSA target TFIIH t... | ACCEPT | Summary: RBX1 is the RING subunit of CUL4-RING ligases at the family level (the parent of the CUL4A- and CUL4B-specific terms). Reason: Core complex membership, directly observed in the CSA/ERCC8 and CRL4 structures. Supporting Evidence: PMID:32355176 Immunoprecipitation of RNAPIIo revealed a UV-specific association with the CSB and CSA proteins, as well as with CUL4, DDB1 and RBX1, which are subunits of a DDB1-CUL4 (CRL4) E3 ubiquitin ligase complex that associates with CSA24,27. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0080008 Cul4-RING E3 ubiquitin ligase complex | IDA PMID:34526721 Structural basis of human transcription-DNA repair coupling. | ACCEPT | Summary: RBX1 is the RING subunit of CUL4-RING ligases at the family level (the parent of the CUL4A- and CUL4B-specific terms). Reason: Core complex membership, directly observed in the CSA/ERCC8 and CRL4 structures. Supporting Evidence: PMID:34526721 RBX1 and the E2 enzymeβdonor ubiquitin complex were modelled as described in the Methods. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0080135 regulation of cellular response to stress | NAS PMID:31586112 TFEB activates Nrf2 by repressing its E3 ubiquitin ligase DC... | MARK AS OVER ANNOTATED | Summary: NAS row from a TFEB/DCAF11-NRF2 study. Reason: Over-annotation: too broad and indirect for the shared RING; the supportable claim is CRL4(DCAF11)-dependent ubiquitination of NRF2. Supporting Evidence: PMID:31586112 DCAF11 and DDB1-Cul4/Roc1 bind to the DIDLID sequence of the Neh2 domain of Nrf2 to mediate its degradation19. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0090090 negative regulation of canonical Wnt signaling pathway | TAS Reactome:R-HSA-4641258 | KEEP AS NON CORE | Summary: CUL3-KLHL12-RBX1 ubiquitinates DVL, and SCF(beta-TrCP) degrades phospho-beta-catenin, both negative inputs to canonical Wnt signalling. Reason: Pathway-level consequence of two receptor-specific ligases; kept as non-core. Supporting Evidence: Reactome:R-HSA-4641258 DVL protein levels are regulated by both proteasomal and lysosomal degradation (reviewed in Gao and Chen, 2010). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0090734 site of DNA damage | IDA PMID:34526721 Structural basis of human transcription-DNA repair coupling. | ACCEPT | Summary: The CRL4(CSA) ligase containing RBX1 is recruited to DNA damage-stalled RNA polymerase II, where it ubiquitinates RPB1/POLR2A at Lys1268. Reason: A defined site of RBX1 catalysis established by cryo-EM of the transcription-coupled repair complex; the RBX1 RING and its E2 are part of the modelled assembly. Supporting Evidence: PMID:34526721 RBX1 and the E2 enzymeβdonor ubiquitin complex were modelled as described in the Methods. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins |
| GO:0097602 cullin family protein binding | IBA GO_REF:0000033 | ACCEPT | Summary: RBX1 binds the C-terminal domain of all cullins through an intermolecular beta-sheet; ROC1/ROC2 interact with cullins generally, whereas the paralogue APC11 is restricted to the cullin-like APC2. Reason: Core molecular function and the basis of RBX1's promiscuity across CRL families; supported by IDA, by the SCF and CRL2/CRL3/CRL4 structures, and by the PAINT inference at the RING-box family node. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000129805 Β· PANTHER:PTN000129805 SUPPORTS TRANSFER RING-box family node spanning RBX1, RBX2/RNF7 and APC11; the descendant experimental evidence includes human RBX1 itself, mouse Rbx1, fly Roc1a/Roc1b and yeast Hrt1/Rbx1 and Apc11, so the function is inherited rather than lineage-specific. Supporting Evidence: file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0097602 cullin family protein binding | IDA PMID:10230407 ROC1, a homolog of APC11, represents a family of cullin part... | ACCEPT | Summary: RBX1 binds the C-terminal domain of all cullins through an intermolecular beta-sheet; ROC1/ROC2 interact with cullins generally, whereas the paralogue APC11 is restricted to the cullin-like APC2. Reason: Core molecular function and the basis of RBX1's promiscuity across CRL families; supported by IDA, by the SCF and CRL2/CRL3/CRL4 structures, and by the PAINT inference at the RING-box family node. Supporting Evidence: PMID:10230407 ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0097602 cullin family protein binding | IPI PMID:14528312 Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubi... | ACCEPT | Summary: RBX1 binds the C-terminal domain of all cullins through an intermolecular beta-sheet; ROC1/ROC2 interact with cullins generally, whereas the paralogue APC11 is restricted to the cullin-like APC2. Reason: Core molecular function and the basis of RBX1's promiscuity across CRL families; supported by IDA, by the SCF and CRL2/CRL3/CRL4 structures, and by the PAINT inference at the RING-box family node. Supporting Evidence: PMID:14528312 Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin ligases. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Its N-terminal region binds the C terminus of a cullin scaffold, whereas its RING domain recruits a modifier-loaded E2 enzyme. |
| GO:0140627 ubiquitin-dependent protein catabolic process via the C-end degron rule pathway | IDA PMID:34065512 CRL4-DCAF12 Ubiquitin Ligase Controls MOV10 RNA Helicase dur... | ACCEPT | Summary: C-end degron (C-degron) pathways: CRL2 receptors (FEM1A/B/C, KLHDC2/3, APPBP2) and CRL4(DCAF12) recognise C-terminal degrons, and RBX1 provides the ligase activity of these complexes. Reason: Core process for the shared RING within a well-defined branch of CRL-dependent proteolysis; the CRL2(APPBP2) cryo-EM structures include NEDD8-CUL2-RBX1. Supporting Evidence: PMID:34065512 CRL4-DCAF12 Ubiquitin Ligase Controls MOV10 RNA Helicase during Spermatogenesis and T Cell Activation. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0140627 ubiquitin-dependent protein catabolic process via the C-end degron rule pathway | IDA PMID:37844242 Molecular basis for C-degron recognition by CRL2(APPBP2) ubi... | ACCEPT | Summary: C-end degron (C-degron) pathways: CRL2 receptors (FEM1A/B/C, KLHDC2/3, APPBP2) and CRL4(DCAF12) recognise C-terminal degrons, and RBX1 provides the ligase activity of these complexes. Reason: Core process for the shared RING within a well-defined branch of CRL-dependent proteolysis; the CRL2(APPBP2) cryo-EM structures include NEDD8-CUL2-RBX1. Supporting Evidence: PMID:37844242 Cryo-EM samples were generated by mixing two complexes, APPBP2-EB-EC-Peptide and NEDD8-CUL2ΞΒ·RBX1, in a 1:1 ratio. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0140627 ubiquitin-dependent protein catabolic process via the C-end degron rule pathway | NAS PMID:15601820 VHL-box and SOCS-box domains determine binding specificity f... | ACCEPT | Summary: C-end degron (C-degron) pathways: CRL2 receptors (FEM1A/B/C, KLHDC2/3, APPBP2) and CRL4(DCAF12) recognise C-terminal degrons, and RBX1 provides the ligase activity of these complexes. Reason: Core process for the shared RING within a well-defined branch of CRL-dependent proteolysis; the CRL2(APPBP2) cryo-EM structures include NEDD8-CUL2-RBX1. Supporting Evidence: PMID:15601820 VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0140627 ubiquitin-dependent protein catabolic process via the C-end degron rule pathway | NAS PMID:21822215 The tumour antigen PRAME is a subunit of a Cul2 ubiquitin li... | ACCEPT | Summary: C-end degron (C-degron) pathways: CRL2 receptors (FEM1A/B/C, KLHDC2/3, APPBP2) and CRL4(DCAF12) recognise C-terminal degrons, and RBX1 provides the ligase activity of these complexes. Reason: Core process for the shared RING within a well-defined branch of CRL-dependent proteolysis; the CRL2(APPBP2) cryo-EM structures include NEDD8-CUL2-RBX1. Supporting Evidence: PMID:21822215 The tumour antigen PRAME is a subunit of a Cul2 ubiquitin ligase and associates with active NFY promoters. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0140627 ubiquitin-dependent protein catabolic process via the C-end degron rule pathway | NAS PMID:22649776 The Role of Elongin BC-Containing Ubiquitin Ligases. | ACCEPT | Summary: C-end degron (C-degron) pathways: CRL2 receptors (FEM1A/B/C, KLHDC2/3, APPBP2) and CRL4(DCAF12) recognise C-terminal degrons, and RBX1 provides the ligase activity of these complexes. Reason: Core process for the shared RING within a well-defined branch of CRL-dependent proteolysis; the CRL2(APPBP2) cryo-EM structures include NEDD8-CUL2-RBX1. Supporting Evidence: PMID:22649776 The S phase kinase-associated protein 1 (Skp1)βCullin 1 (Cul1)βF box protein (SCF) family is a member of the RING finger-containing ubiquitin ligase family (Lipkowitz and Weissman, 2011). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0140627 ubiquitin-dependent protein catabolic process via the C-end degron rule pathway | NAS PMID:29779948 The Eukaryotic Proteome Is Shaped by E3Β Ubiquitin Ligases Ta... | ACCEPT | Summary: C-end degron (C-degron) pathways: CRL2 receptors (FEM1A/B/C, KLHDC2/3, APPBP2) and CRL4(DCAF12) recognise C-terminal degrons, and RBX1 provides the ligase activity of these complexes. Reason: Core process for the shared RING within a well-defined branch of CRL-dependent proteolysis; the CRL2(APPBP2) cryo-EM structures include NEDD8-CUL2-RBX1. Supporting Evidence: PMID:29779948 We characterize eight Cullin-RING E3 ubiquitin ligase (CRL) complex adaptors that regulate C-terminal degrons, including six CRL2 and two CRL4 complexes, and computationally implicate multiple non-CRLs in end recognition. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0140627 ubiquitin-dependent protein catabolic process via the C-end degron rule pathway | NAS PMID:33398168 Molecular basis for arginine C-terminal degron recognition b... | ACCEPT | Summary: C-end degron (C-degron) pathways: CRL2 receptors (FEM1A/B/C, KLHDC2/3, APPBP2) and CRL4(DCAF12) recognise C-terminal degrons, and RBX1 provides the ligase activity of these complexes. Reason: Core process for the shared RING within a well-defined branch of CRL-dependent proteolysis; the CRL2(APPBP2) cryo-EM structures include NEDD8-CUL2-RBX1. Supporting Evidence: PMID:33398168 Recently, a few classes of C-terminal degrons (C-degrons) that are recognized by dedicated cullin-RING ligases (CRLs) have been identified. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0140627 ubiquitin-dependent protein catabolic process via the C-end degron rule pathway | NAS PMID:34743205 CRL2-KLHDC3 E3 ubiquitin ligase complex suppresses ferroptos... | ACCEPT | Summary: C-end degron (C-degron) pathways: CRL2 receptors (FEM1A/B/C, KLHDC2/3, APPBP2) and CRL4(DCAF12) recognise C-terminal degrons, and RBX1 provides the ligase activity of these complexes. Reason: Core process for the shared RING within a well-defined branch of CRL-dependent proteolysis; the CRL2(APPBP2) cryo-EM structures include NEDD8-CUL2-RBX1. Supporting Evidence: PMID:34743205 CRL2-KLHDC3 E3 ubiquitin ligase complex suppresses ferroptosis through promoting p14(ARF) degradation. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0160240 RNA polymerase II transcription initiation surveillance | IDA PMID:39504960 Redundant pathways for removal of defective RNA polymerase I... | KEEP AS NON CORE | Summary: CRL3(ARMC5) containing RBX1 ubiquitinates Ser5-phosphorylated RPB1, removing excessive or defective RNA polymerase II at the promoter-proximal checkpoint. Reason: A precise, well-supported process in which RBX1 performs the ubiquitination, but it is specific to the ARMC5 receptor; kept as non-core for the shared RING. Supporting Evidence: PMID:39504960 Tellingly, CUL3 E3 ligase relies on BTB domain-containing proteins as adaptors to recognize substrates for ubiquitylation75, suggesting that ARMC5 might connect CUL3 to RNAPII. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0160240 RNA polymerase II transcription initiation surveillance | IDA PMID:39667934 CRL3(ARMC5) ubiquitin ligase and Integrator phosphatase form... | KEEP AS NON CORE | Summary: CRL3(ARMC5) containing RBX1 ubiquitinates Ser5-phosphorylated RPB1, removing excessive or defective RNA polymerase II at the promoter-proximal checkpoint. Reason: A precise, well-supported process in which RBX1 performs the ubiquitination, but it is specific to the ARMC5 receptor; kept as non-core for the shared RING. Supporting Evidence: PMID:39667934 CRL3(ARMC5) ubiquitin ligase and Integrator phosphatase form parallel mechanisms to control early stages of RNA Pol II transcription. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:0160276 negative regulation of beige fat cell differentiation | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Ortholog-based transfer from mouse Rbx1: the CRL2(APPBP2) ligase polyubiquitinates PRDM16, restraining beige-fat biogenesis. Reason: The mouse evidence is sound and RBX1 is 100% identical between human and mouse, so the transfer is safe; the process is nonetheless a receptor-specific metabolic output and non-core. Supporting Evidence: file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:1900076 regulation of cellular response to insulin stimulus | IC PMID:27708159 Insulin resistance and diabetes caused by genetic or diet-in... | KEEP AS NON CORE | Summary: Curator inference from CRL3(KBTBD2), which degrades the PI3K regulatory subunit p85alpha; its loss causes insulin resistance in mice. Reason: Defensible receptor-specific output; non-core for the shared catalytic subunit. Supporting Evidence: PMID:27708159 Kbtbd2 encodes a BTB-Kelch family substrate recognition subunit of the Cullin-3-based E3 ubiquitin ligase. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:1901524 regulation of mitophagy | NAS PMID:36135912 Mitochondrial Fission and Fusion: Molecular Mechanisms, Biol... | MARK AS OVER ANNOTATED | Summary: NAS row citing a review of mitochondrial fission and fusion, in which FBXL4-containing CRL1 is mentioned. Reason: Over-annotation: the cited review does not assay RBX1, and mitophagy regulation by one F-box receptor does not generalise to the shared catalytic subunit. Supporting Evidence: PMID:36135912 Post-translational phosphorylation, SUMOylation, and ubiquitination regulate DNM1L on the mitochondria [29]. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:1901525 negative regulation of mitophagy | IC PMID:17636018 ASB4 is a hydroxylation substrate of FIH and promotes vascul... | KEEP AS NON CORE | Summary: Curator inference that elongin BC-cullin-ROC ligases containing RBX1 limit mitophagy. Reason: Inference-level and receptor-specific; kept as non-core. Supporting Evidence: PMID:17636018 Like other SOCS box-containing proteins, ASB4 is the substrate recognition molecule of an elongin B/elongin C/cullin/Roc ubiquitin ligase complex that mediates the ubiquitination and degradation of substrate protein(s). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:1901987 regulation of cell cycle phase transition | NAS PMID:16861906 L2DTL/CDT2 interacts with the CUL4/DDB1 complex and PCNA and... | MARK AS OVER ANNOTATED | Summary: NAS rows from CRL4(CDT2) and AMBRA1 studies, where CRL-dependent turnover of licensing and autophagy factors affects phase transitions. Reason: Over-annotation for RBX1: the direct process is CRL-dependent ubiquitination; the phase-transition effect is downstream and receptor-specific. Supporting Evidence: PMID:16861906 Our studies suggest that L2DTL and PCNA interact with CUL4/DDB1 complexes and are involved in CDT1 degradation after DNA damage. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:1901987 regulation of cell cycle phase transition | NAS PMID:25499913 AMBRA1 interplay with cullin E3 ubiquitin ligases regulates ... | MARK AS OVER ANNOTATED | Summary: NAS rows from CRL4(CDT2) and AMBRA1 studies, where CRL-dependent turnover of licensing and autophagy factors affects phase transitions. Reason: Over-annotation for RBX1: the direct process is CRL-dependent ubiquitination; the phase-transition effect is downstream and receptor-specific. Supporting Evidence: PMID:25499913 AMBRA1 interplay with cullin E3 ubiquitin ligases regulates autophagy dynamics. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:1902412 regulation of mitotic cytokinesis | NAS PMID:34758320 Phosphorylation at Ser68 facilitates DCAF11-mediated ubiquit... | KEEP AS NON CORE | Summary: CRL4(DCAF11) containing RBX1 degrades Ser68-phosphorylated CENP-A during the cell cycle. Reason: Receptor-specific; kept as non-core. Supporting Evidence: PMID:34758320 Furthermore, we find that DCAF11 (DDB1 and CUL4 associated factor 11/WDR23) is the E3 ligase that specifically mediates the observed polyubiquitination. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:1902499 positive regulation of protein autoubiquitination | IMP PMID:14528312 Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubi... | ACCEPT | Summary: RBX1 stimulates autoubiquitination of the E2 CDC34 with which it works, an activity traced to the RING domain. Reason: A direct consequence of RBX1 activating the E2~ubiquitin conjugate; UniProt records the same property. Supporting Evidence: PMID:14528312 Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin ligases. file:human/RBX1/RBX1-uniprot.txt Probably also stimulates CDC34 autoubiquitination. |
| GO:1902883 negative regulation of response to oxidative stress | IDA PMID:11027288 The CUL1 C-terminal sequence and ROC1 are required for effic... | KEEP AS NON CORE | Summary: By supporting KEAP1-CUL3-RBX1-dependent degradation of NRF2, RBX1 restrains the antioxidant response, and disabling the CUL1/ROC1 module diminishes CRL ligase activity toward such substrates. Reason: Defensible as a downstream consequence of CRL3(KEAP1) activity; kept as non-core because the sign of the effect is set by the receptor and substrate, not by RBX1. Supporting Evidence: PMID:11027288 The CUL1 C-terminal sequence and ROC1 are required for efficient nuclear accumulation, NEDD8 modification, and ubiquitin ligase activity of CUL1. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:1904178 negative regulation of adipose tissue development | NAS PMID:27113764 The antiobesity factor WDTC1 suppresses adipogenesis via the... | KEEP AS NON CORE | Summary: The CRL4(WDTC1) ligase containing RBX1 suppresses adipogenesis, in part through H2AK119 monoubiquitination. Reason: Receptor-specific metabolic output; non-core. Supporting Evidence: PMID:27113764 Here, we demonstrate that WDTC1 is a component of a DDB1-CUL4-ROC1 (CRL4) E3 ligase. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:1904263 positive regulation of TORC1 signaling | IDA PMID:29769719 KLHL22 activates amino-acid-dependent mTORC1 signalling to p... | KEEP AS NON CORE | Summary: CUL3-KLHL22-RBX1 ubiquitinates DEPDC5 in response to amino acids, relieving GATOR1 inhibition and activating mTORC1. Reason: Genuine, mechanistically defined contribution through one BTB receptor; kept as non-core. Supporting Evidence: PMID:29769719 Here we find that in response to amino acids, the CUL3-KLHL22 E3 ubiquitin ligase promotes K48-linked polyubiquitination and degradation of DEPDC5, an essential subunit of GATOR1. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:1904415 regulation of xenophagy | NAS PMID:34515398 FBXO2/SCF ubiquitin ligase complex directs xenophagy through... | KEEP AS NON CORE | Summary: SCF(FBXO2) containing RBX1 ubiquitinates group A Streptococcus surface glycans to direct xenophagy; SKP1, CUL1 and ROC1 are all required. Reason: Genuine but receptor-specific defence output; non-core. Supporting Evidence: PMID:34515398 Furthermore, SCF components such as SKP1, CUL1, and ROC1 are required for ubiquitin-mediated xenophagy against GAS. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:1990116 ribosome-associated ubiquitin-dependent protein catabolic process | NAS PMID:33909987 Convergence of mammalian RQC and C-end rule proteolytic path... | KEEP AS NON CORE | Summary: RBX1-containing CRL2 ligases (ZYG11B/ZER1-type C-degron receptors) participate in degradation of alanine-tailed ribosome-associated quality-control substrates. Reason: Receptor-specific branch of CRL-dependent proteolysis; kept as non-core. Supporting Evidence: PMID:33909987 Incompletely synthesized nascent chains obstructing large ribosomal subunits are targeted for degradation by ribosome-associated quality control (RQC). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:2000001 regulation of DNA damage checkpoint | NAS PMID:33784509 FBX4 mediates rapid cyclin D1 proteolysis upon DNA damage in... | KEEP AS NON CORE | Summary: SCF ligases containing RBX1 (via FBX4/FBXO31) degrade cyclin D1 after DNA damage, contributing to checkpoint responses. Reason: Receptor-specific and downstream; kept as non-core. Supporting Evidence: PMID:33784509 Much focus has been placed on identifying the E3 ligases responsible for mediating cyclin D1 degradation. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:2000036 regulation of stem cell population maintenance | NAS PMID:29691401 Methylated DNMT1 and E2F1 are targeted for proteolysis by L3... | KEEP AS NON CORE | Summary: CRL4(DCAF5) ligases containing RBX1 degrade methylated SOX2 and DNMT1, influencing stem-cell maintenance. Reason: Receptor-specific output; kept as non-core. Supporting Evidence: PMID:29691401 The cullin-RING ubiquitin ligases (CRLs) comprise the largest families of ubiquitin E3 ligases23. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:2000036 regulation of stem cell population maintenance | NAS PMID:30442713 Proteolysis of methylated SOX2 protein is regulated by L3MBT... | KEEP AS NON CORE | Summary: CRL4(DCAF5) ligases containing RBX1 degrade methylated SOX2 and DNMT1, influencing stem-cell maintenance. Reason: Receptor-specific output; kept as non-core. Supporting Evidence: PMID:30442713 Proteolysis of methylated SOX2 protein is regulated by L3MBTL3 and CRL4(DCAF5) ubiquitin ligase. file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
| GO:2000104 negative regulation of DNA-templated DNA replication | NAS PMID:22649776 The Role of Elongin BC-Containing Ubiquitin Ligases. | KEEP AS NON CORE | Summary: Elongin BC-containing CRL2 ligases with RBX1 act on replication-licensing and other substrates, limiting re-replication. Reason: Author-statement-level and receptor-specific; kept as non-core. Supporting Evidence: PMID:22649776 The S phase kinase-associated protein 1 (Skp1)βCullin 1 (Cul1)βF box protein (SCF) family is a member of the RING finger-containing ubiquitin ligase family (Lipkowitz and Weissman, 2011). file:human/RBX1/RBX1-uniprot.txt E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins file:human/RBX1/RBX1-deep-research-falcon.md Specificity is chiefly imposed by modular receptors |
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Download this section (compressed HTML)Q: Should the ~55 GO:0005515 rows recording RBX1 with individual cullins, substrate receptors and CRL substrates be re-curated as cullin family protein binding (GO:0097602) plus complex membership, or captured in GO-CAM as has_input relations on the receptor and RBX1 activity nodes, rather than as bare protein binding on the shared catalytic subunit?
Q: Which receptor-specific pathway outputs (circadian rhythm, iron homeostasis, TORC1, BMP, xenophagy, ciliogenesis, spermatogenesis, beige-fat differentiation) should be annotated to RBX1 at all, given that RBX1 is shared by every CRL and that the same subunit supports opposite-sign outputs through different receptors?
Q: How should the division of labour between RBX1 and ARIH1 be annotated? Neddylated CUL1-RBX1 activates ARIH1, which primes many CRL substrates with the first ubiquitin while the RBX1-E2 pair elongates the chain - a distinction that current terms (GO:0061630 versus GO:0034450) only partly express.
Experiment: Reconstitute neddylated CUL1-RBX1 and CUL3-RBX1 ligases carrying RING linchpin and E2-interface mutations, and compare priming versus elongation kinetics on SCF(beta-TrCP), SCF(FBXW7) and CUL3(KEAP1) substrates with and without ARIH1, reading out chain length by ubiquitin-remnant mass spectrometry.
Hypothesis: The RBX1 RING is required for chain elongation but dispensable for ARIH1-mediated priming of a defined subset of CRL substrates.
Type: structure-guided mutational reconstitution with ubiquitination kinetics
Experiment: Rescue RBX1-depleted human cells with alleles selectively impaired in UBE2M binding versus in ubiquitin-charged E2 binding, then measure cullin neddylation state, accumulation of canonical substrates (p27, CDT1, NRF2, DEPTOR) and proliferation/senescence, comparing each to NEDD8-E1 inhibition.
Hypothesis: RBX1's neddylation and ubiquitination activities can be separated in cells, so that loss of cullin neddylation accounts for only part of the RBX1-null phenotype.
Type: separation-of-function rescue in cells
Experiment: Quantify RBX1 and RBX2 occupancy on CUL5 complexes across cell types and receptor classes (SOCS-box versus elongin A) by targeted proteomics of endogenous CUL5 pulldowns in RBX2-null and RBX1-degron cells.
Hypothesis: RBX1 associates with CUL5 only in defined contexts, whereas RBX2/RNF7 is the default CUL5 partner.
Type: quantitative interaction proteomics with genetic controls
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