CUL1 (cullin-1) is the scaffold subunit of the SCF (SKP1-CUL1-F-box protein) family of cullin-RING E3 ubiquitin ligases, the largest class of E3s in human cells. It is an elongated, rigid protein: an N-terminal stalk of three cullin repeats binds the adaptor SKP1, which carries one of roughly 70 interchangeable F-box substrate receptors (SKP2, beta-TrCP/BTRC/FBXW11, FBXW7, cyclin F, FBXL3, FBXL5, FBXO9, FBXO31 and others), while the C-terminal globular domain binds the RING protein RBX1, which recruits ubiquitin-charged E2 enzymes (CDC34/UBE2R, UBE2D) and the RBR E3 ARIH1. CUL1 has no catalytic activity of its own and forms no ubiquitin thioester; it positions the receptor-bound substrate and the E2 about 100 A apart and contributes to catalysis through this geometry. Its activity is switched on by covalent attachment of NEDD8 to Lys720, which reorients the RBX1 RING and relieves autoinhibition, and it is switched off by COP9 signalosome-mediated deneddylation and by CAND1, which binds unneddylated CUL1, displaces SKP1 and drives exchange of F-box receptors. The neddylated CUL1-RBX1 core is also borrowed by the CUL7-FBXW8 assembly. Through its receptors, CUL1-based SCF ligases build mostly K48-linked chains that send substrates to the proteasome: SCF(SKP2) destroys Thr187-phosphorylated p27/CDKN1B at the G1/S transition, SCF(beta-TrCP) degrades IkappaB-alpha, beta-catenin, EMI1, CDC25A, DEPTOR and MDM2, SCF(FBXW7) degrades cyclin E, MYC and NOTCH, SCF(cyclin F) degrades CP110 and RRM2, SCF(FBXL3) degrades the cryptochromes, and SCF(FBXL5) degrades IRP2. CUL1 therefore acts in both nucleus and cytosol, with receptor-specific pools at centrosomes, membranes and mitochondria, and it underlies cell-cycle progression, signalling homeostasis, circadian timing, iron sensing and protein quality control.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000082 G1/S transition of mitotic cell cycle | IEA GO_REF:0000117 | ACCEPT | Summary: CUL1 scaffolds SCF(SKP2), whose ubiquitination of Thr187-phosphorylated p27/CDKN1B releases CDK2 and commits the cell to S phase; C. elegans cul-1 loss deregulates G1 exit. Reason: Core process: the SCF(SKP2)-p27 switch is the canonical CUL1 output and CUL1 performs the scaffold work of that ligase. The ARBA and TAS/NAS rows agree with the structural and biochemical evidence. Supporting Evidence: file:human/CUL1/CUL1-deep-research-falcon.md SCFβSKP2 targets the cyclin-dependent-kinase inhibitor **p27/CDKN1B** for ubiquitin-dependent turnover, promoting cell-cycle progression. file:human/CUL1/CUL1-uniprot.txt SCF(SKP2) directs ubiquitination of phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. |
| 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: CUL1 scaffolds SCF(SKP2), whose ubiquitination of Thr187-phosphorylated p27/CDKN1B releases CDK2 and commits the cell to S phase; C. elegans cul-1 loss deregulates G1 exit. Reason: Core process: the SCF(SKP2)-p27 switch is the canonical CUL1 output and CUL1 performs the scaffold work of that ligase. The ARBA and TAS/NAS rows agree with the structural and biochemical evidence. Supporting Evidence: PMID:11961546 Cul1 serves as a rigid scaffold that organizes the Skp1-F boxSkp2 and Rbx1 subunits, holding them over 100 A apart file:human/CUL1/CUL1-deep-research-falcon.md SCFβSKP2 targets the cyclin-dependent-kinase inhibitor **p27/CDKN1B** for ubiquitin-dependent turnover, promoting cell-cycle progression. file:human/CUL1/CUL1-uniprot.txt SCF(SKP2) directs ubiquitination of phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. |
| GO:0000082 G1/S transition of mitotic cell cycle | TAS PMID:8681378 cul-1 is required for cell cycle exit in C. elegans and iden... | ACCEPT | Summary: CUL1 scaffolds SCF(SKP2), whose ubiquitination of Thr187-phosphorylated p27/CDKN1B releases CDK2 and commits the cell to S phase; C. elegans cul-1 loss deregulates G1 exit. Reason: Core process: the SCF(SKP2)-p27 switch is the canonical CUL1 output and CUL1 performs the scaffold work of that ligase. The ARBA and TAS/NAS rows agree with the structural and biochemical evidence. Supporting Evidence: PMID:8681378 cul-1 is required for developmentally programmed transitions from the G1 phase of the cell cycle to the GO phase or the apoptotic pathway file:human/CUL1/CUL1-deep-research-falcon.md SCFβSKP2 targets the cyclin-dependent-kinase inhibitor **p27/CDKN1B** for ubiquitin-dependent turnover, promoting cell-cycle progression. file:human/CUL1/CUL1-uniprot.txt SCF(SKP2) directs ubiquitination of phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. |
| GO:0005515 protein binding | IPI PMID:11961546 Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin liga... | MODIFY | Summary: CUL1 interacts with the SCF(SKP2) substrate p27/CDKN1B (CDKN1B); The crystal structure of Cul1-Rbx1-Skp1-Skp2 shows CUL1 as the rigid scaffold holding the substrate-receptor module and the RBX1 catalytic module ~100 A apart. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:11961546 Cul1 serves as a rigid scaffold that organizes the Skp1-F boxSkp2 and Rbx1 subunits, holding them over 100 A apart file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:11961546 Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin liga... | MODIFY | Summary: CUL1 interacts with the RING subunit RBX1, which with CUL1 forms the catalytic core that recruits E2 enzymes (RBX1); The crystal structure of Cul1-Rbx1-Skp1-Skp2 shows CUL1 as the rigid scaffold holding the substrate-receptor module and the RBX1 catalytic module ~100 A apart. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:11961546 Cul1 serves as a rigid scaffold that organizes the Skp1-F boxSkp2 and Rbx1 subunits, holding them over 100 A apart file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:12504025 NEDD8 modification of CUL1 dissociates p120(CAND1), an inhib... | REMOVE | Summary: CUL1 interacts with the exchange factor CAND1, which binds unneddylated CUL1 and blocks SKP1 binding (CAND1). CUL1 is the target of CAND1 inhibition in this study; the interaction describes regulation of CUL1, not a function of CUL1 beyond the scaffold activity already annotated. Reason: CUL1 is the target of CAND1 inhibition in this study; the interaction describes regulation of CUL1, not a function of CUL1 beyond the scaffold activity already annotated. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:12504025 CAND1 dissociated SKP1 from CUL1 and inhibited SCF ligase activity in vitro |
| GO:0005515 protein binding | IPI PMID:12504026 CAND1 binds to unneddylated CUL1 and regulates the formation... | MODIFY | Summary: CUL1 interacts with the RING subunit RBX1, which with CUL1 forms the catalytic core that recruits E2 enzymes (RBX1); This study shows that CUL1 assembles SKP1-SKP2 and RBX1 into an SCF ligase and that CAND1 competes with SKP1 for the CUL1 scaffold. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:12504026 CAND1 prevents the binding of SKP1 and SKP2 to CUL1 while dissociation of CAND1 from CUL1 promotes the reverse reaction file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:12504026 CAND1 binds to unneddylated CUL1 and regulates the formation... | MODIFY | Summary: CUL1 interacts with the adaptor SKP1, which tethers F-box proteins to the CUL1 N-terminal stalk (SKP1); This study shows that CUL1 assembles SKP1-SKP2 and RBX1 into an SCF ligase and that CAND1 competes with SKP1 for the CUL1 scaffold. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:12504026 CAND1 prevents the binding of SKP1 and SKP2 to CUL1 while dissociation of CAND1 from CUL1 promotes the reverse reaction file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:12504026 CAND1 binds to unneddylated CUL1 and regulates the formation... | MODIFY | Summary: CUL1 interacts with the F-box substrate receptor SKP2 (SKP2); This study shows that CUL1 assembles SKP1-SKP2 and RBX1 into an SCF ligase and that CAND1 competes with SKP1 for the CUL1 scaffold. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:12504026 CAND1 prevents the binding of SKP1 and SKP2 to CUL1 while dissociation of CAND1 from CUL1 promotes the reverse reaction file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:12504026 CAND1 binds to unneddylated CUL1 and regulates the formation... | MODIFY | Summary: CUL1 interacts with the exchange factor CAND1, which binds unneddylated CUL1 and blocks SKP1 binding (CAND1); This study shows that CUL1 assembles SKP1-SKP2 and RBX1 into an SCF ligase and that CAND1 competes with SKP1 for the CUL1 scaffold. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:12504026 CAND1 prevents the binding of SKP1 and SKP2 to CUL1 while dissociation of CAND1 from CUL1 promotes the reverse reaction file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:12609982 TIP120A associates with cullins and modulates ubiquitin liga... | MODIFY | Summary: CUL1 interacts with the RING subunit RBX1, which with CUL1 forms the catalytic core that recruits E2 enzymes (RBX1); TIP120A/CAND1 binds the CUL1-RBX1 core and interferes with SKP1/F-box assembly, i.e. the interactions map onto the scaffold function of CUL1. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity 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/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:12609982 TIP120A associates with cullins and modulates ubiquitin liga... | MODIFY | Summary: CUL1 interacts with the adaptor SKP1, which tethers F-box proteins to the CUL1 N-terminal stalk (SKP1); TIP120A/CAND1 binds the CUL1-RBX1 core and interferes with SKP1/F-box assembly, i.e. the interactions map onto the scaffold function of CUL1. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity 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/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:12609982 TIP120A associates with cullins and modulates ubiquitin liga... | MODIFY | Summary: CUL1 interacts with the F-box substrate receptor SKP2 (SKP2); TIP120A/CAND1 binds the CUL1-RBX1 core and interferes with SKP1/F-box assembly, i.e. the interactions map onto the scaffold function of CUL1. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity 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/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:12609982 TIP120A associates with cullins and modulates ubiquitin liga... | MODIFY | Summary: CUL1 interacts with the exchange factor CAND1, which binds unneddylated CUL1 and blocks SKP1 binding (CAND1); TIP120A/CAND1 binds the CUL1-RBX1 core and interferes with SKP1/F-box assembly, i.e. the interactions map onto the scaffold function of CUL1. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity 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/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:12609982 TIP120A associates with cullins and modulates ubiquitin liga... | MODIFY | Summary: CUL1 interacts with the F-box substrate receptor beta-TrCP1/BTRC (BTRC); TIP120A/CAND1 binds the CUL1-RBX1 core and interferes with SKP1/F-box assembly, i.e. the interactions map onto the scaffold function of CUL1. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity 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/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:14685242 The gene product Murr1 restricts HIV-1 replication in restin... | MODIFY | Summary: CUL1 interacts with the adaptor SKP1, which tethers F-box proteins to the CUL1 N-terminal stalk (SKP1); CUL1-SKP1 assembly is the SCF(beta-TrCP) scaffold whose IkappaB-alpha turnover Murr1/COMMD1 restrains. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:14685242 Knockdown of Murr1 increased NF-kappaB activity and decreased IkappaB-alpha concentrations by facilitating phospho-IkappaB-alpha degradation by the proteasome file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:15537541 Structure of the Cand1-Cul1-Roc1 complex reveals regulatory ... | REMOVE | Summary: CUL1 interacts with the exchange factor CAND1, which binds unneddylated CUL1 and blocks SKP1 binding (CAND1). The Cand1-Cul1-Roc1 structure shows CAND1 clamping the CUL1 scaffold; CUL1 is the regulated entity, and no additional CUL1 molecular function is supported. Reason: The Cand1-Cul1-Roc1 structure shows CAND1 clamping the CUL1 scaffold; CUL1 is the regulated entity, and no additional CUL1 molecular function is supported. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:15537541 Cand1, a 120 kDa HEAT repeat protein, forms a tight complex with the Cul1-Roc1 SCF catalytic core, inhibiting the assembly of the multisubunit E3 complex |
| GO:0005515 protein binding | IPI PMID:16051867 Myxoma virus M-T5 protects infected cells from the stress of... | REMOVE | Summary: CUL1 interacts with the myxoma virus ankyrin-repeat host-range protein M-T5 (M-T5). The myxoma virus M-T5 interaction is a viral hijack of the host cullin; it defines no CUL1 molecular function. Reason: The myxoma virus M-T5 interaction is a viral hijack of the host cullin; it defines no CUL1 molecular function. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:16051867 the cell cycle regulatory protein cullin-1 (cul-1) was identified as a cellular binding partner of M-T5 |
| GO:0005515 protein binding | IPI PMID:16278047 Characterization of FBX25, encoding a novel brain-expressed ... | MODIFY | Summary: CUL1 interacts with the F-box protein FBXO4 (FBXO4); FBXO4-type F-box proteins are established as SCF receptors by their binding to SKP1 and CUL1; the informative CUL1 activity is scaffolding. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:16278047 established hFBX25 as an FBP by verifying its interaction with Skp1 and Cul1 file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:16797541 Proteasomal degradation of the multifunctional regulator YB-... | MODIFY | Summary: CUL1 interacts with the SCF(FBXO33) substrate YB-1/YBX1 (YBX1); FBXO33 forms an SCF ligase on the CUL1 scaffold that ubiquitinates YB-1. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:16797541 we identify FBX33 as a component of an SCF E3-ubiquitin ligase that targets the multifunctional regulator Y-box binding protein 1 (YB-1)/dbpB/p50 for polyubiquitination and destruction by the proteasome file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:16797541 Proteasomal degradation of the multifunctional regulator YB-... | MODIFY | Summary: CUL1 interacts with the F-box protein FBXO33 (FBXO33); FBXO33 forms an SCF ligase on the CUL1 scaffold that ubiquitinates YB-1. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:16797541 we identify FBX33 as a component of an SCF E3-ubiquitin ligase that targets the multifunctional regulator Y-box binding protein 1 (YB-1)/dbpB/p50 for polyubiquitination and destruction by the proteasome file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:16861300 Regulation of neddylation and deneddylation of cullin1 in SC... | REMOVE | Summary: CUL1 interacts with the exchange factor CAND1, which binds unneddylated CUL1 and blocks SKP1 binding (CAND1). The CAND1 interaction reflects regulation of CUL1 neddylation by F-box protein and substrate availability; it adds no CUL1 molecular function beyond scaffold activity. Reason: The CAND1 interaction reflects regulation of CUL1 neddylation by F-box protein and substrate availability; it adds no CUL1 molecular function beyond scaffold activity. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:16861300 Neddylation is inhibited by the tight binding of cullins to CAND1 (cullin-associated and neddylation-dissociated 1) protein |
| GO:0005515 protein binding | IPI PMID:16880511 Regulation of p27 degradation and S-phase progression by Ro5... | MODIFY | Summary: CUL1 interacts with the RING protein TRIM21/Ro52, an alternative catalytic-core partner of CUL1 (TRIM21); CUL1 scaffolds an SCF(SKP2)-like p27 ligase whose RING partner is TRIM21/Ro52 instead of RBX1. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:16880511 we identify Skp2 as a component of an Skp1-cullin-F-box complex that is based on a Cul1-Ro52 RING finger B-box coiled-coil motif family protein catalytic core file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:17290223 Impaired DNA damage checkpoint response in MIF-deficient mic... | MODIFY | Summary: CUL1 interacts with the adaptor SKP1, which tethers F-box proteins to the CUL1 N-terminal stalk (SKP1); The CUL1-SKP1/CAND1 interactions studied here are those of the SCF scaffold whose activity MIF/CSN5 modulate. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:17290223 We provide evidence that MIF plays a role in regulating the activity of Cul1-containing SCF ubiquitin ligases file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:17290223 Impaired DNA damage checkpoint response in MIF-deficient mic... | MODIFY | Summary: CUL1 interacts with the exchange factor CAND1, which binds unneddylated CUL1 and blocks SKP1 binding (CAND1); The CUL1-SKP1/CAND1 interactions studied here are those of the SCF scaffold whose activity MIF/CSN5 modulate. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:17290223 We provide evidence that MIF plays a role in regulating the activity of Cul1-containing SCF ubiquitin ligases file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:17318178 CSN controls NF-kappaB by deubiquitinylation of IkappaBalpha... | MODIFY | Summary: CUL1 interacts with the ubiquitin-like protein NEDD8, which is conjugated to CUL1 Lys720 to activate the ligase (NEDD8); CUL1 and beta-TrCP are the scaffold and receptor of the IkappaB-alpha ligase whose stability the CSN controls. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:17318178 Protein expression levels of cullin1 and the CRL substrate adapter beta-TrCP are reduced in nonstimulated cells with a disrupted function of the CSN file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:17318178 CSN controls NF-kappaB by deubiquitinylation of IkappaBalpha... | MODIFY | Summary: CUL1 interacts with the F-box substrate receptor beta-TrCP1/BTRC (BTRC); CUL1 and beta-TrCP are the scaffold and receptor of the IkappaB-alpha ligase whose stability the CSN controls. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:17318178 Protein expression levels of cullin1 and the CRL substrate adapter beta-TrCP are reduced in nonstimulated cells with a disrupted function of the CSN file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:17914462 Commensal bacteria modulate cullin-dependent signaling via g... | REMOVE | Summary: CUL1 interacts with the NEDD8-conjugating enzyme UBE2M/UBC12 (UBE2M). CUL1 is the NEDD8 acceptor whose neddylation is lost when ROS inactivate Ubc12; the row records CUL1 as a substrate, not a function. Reason: CUL1 is the NEDD8 acceptor whose neddylation is lost when ROS inactivate Ubc12; the row records CUL1 as a substrate, not a function. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:17914462 Ubiquitination of these proteins as well as others is catalyzed by the SCF(betaTrCP) ubiquitin ligase, which itself requires regulated modification of the cullin-1 subunit by the ubiquitin-like protein NEDD8 |
| GO:0005515 protein binding | IPI PMID:18203720 Diversity in tissue expression, substrate binding, and SCF c... | MODIFY | Summary: CUL1 interacts with the glycoprotein-binding F-box protein FBXO27 (FBXO27); The FBA-family F-box proteins assemble with SKP1-CUL1 into SCF ligases for glycoproteins. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:18203720 The five proteins comprising this FBA family (FBXO2, FBXO6, FBXO17, FBXO27, and FBXO44) contain a conserved G domain that mediates substrate binding file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:18203720 Diversity in tissue expression, substrate binding, and SCF c... | MODIFY | Summary: CUL1 interacts with the glycoprotein-binding F-box protein FBXO17 (FBXO17); The FBA-family F-box proteins assemble with SKP1-CUL1 into SCF ligases for glycoproteins. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:18203720 The five proteins comprising this FBA family (FBXO2, FBXO6, FBXO17, FBXO27, and FBXO44) contain a conserved G domain that mediates substrate binding file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:18203720 Diversity in tissue expression, substrate binding, and SCF c... | MODIFY | Summary: CUL1 interacts with the F-box protein FBXO44 (FBXO44); The FBA-family F-box proteins assemble with SKP1-CUL1 into SCF ligases for glycoproteins. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:18203720 The five proteins comprising this FBA family (FBXO2, FBXO6, FBXO17, FBXO27, and FBXO44) contain a conserved G domain that mediates substrate binding file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:18239684 Phosphorylation of Skp2 regulated by CDK2 and Cdc14B protect... | MODIFY | Summary: CUL1 interacts with the F-box substrate receptor SKP2 (SKP2); SKP2 is the receptor of the CUL1-scaffolded SCF(SKP2) p27 ligase. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:18239684 The activity of SCF(Skp2) is regulated by the APC(Cdh1), which targets Skp2 for degradation file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:18264111 Identification of conjugation specificity determinants unmas... | REMOVE | Summary: CUL1 interacts with the ubiquitin-like protein NEDD8, which is conjugated to CUL1 Lys720 to activate the ligase (NEDD8). The study concerns Ubc12 specificity for NEDD8; CUL1 is only the NEDD8 acceptor. Reason: The study concerns Ubc12 specificity for NEDD8; CUL1 is only the NEDD8 acceptor. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:18264111 Here we report the basis for UBL selection by UBL conjugating enzyme 12 (Ubc12), which is specific for the neural precursor cell expressed, developmentally down-regulated protein 8 (NEDD8) |
| GO:0005515 protein binding | IPI PMID:18274552 Ribosomal proteins are targets for the NEDD8 pathway. | REMOVE | Summary: CUL1 interacts with the ubiquitin-like protein NEDD8, which is conjugated to CUL1 Lys720 to activate the ligase (NEDD8). The study identifies ribosomal proteins as NEDD8 targets; the CUL1-NEDD8 interaction is incidental (CUL1 as neddylation substrate). Reason: The study identifies ribosomal proteins as NEDD8 targets; the CUL1-NEDD8 interaction is incidental (CUL1 as neddylation substrate). Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:18274552 we identified a subset of ribosomal proteins as novel targets for the NEDD8 pathway |
| GO:0005515 protein binding | IPI PMID:18354482 Control of chromosome stability by the beta-TrCP-REST-Mad2 a... | MODIFY | Summary: CUL1 interacts with the F-box substrate receptor beta-TrCP2/FBXW11 (FBXW11); beta-TrCP1/2 are receptors of the CUL1-scaffolded SCF(beta-TrCP) ligase that degrades REST. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:18354482 REST is degraded by means of the ubiquitin ligase SCF(beta-TrCP) during the G2 phase of the cell cycle file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:18354482 Control of chromosome stability by the beta-TrCP-REST-Mad2 a... | MODIFY | Summary: CUL1 interacts with the F-box substrate receptor beta-TrCP1/BTRC (BTRC); beta-TrCP1/2 are receptors of the CUL1-scaffolded SCF(beta-TrCP) ligase that degrades REST. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:18354482 REST is degraded by means of the ubiquitin ligase SCF(beta-TrCP) during the G2 phase of the cell cycle file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:18644861 Regulation of Chk2 ubiquitination and signaling through auto... | MODIFY | Summary: CUL1 interacts with the checkpoint kinase CHK2, a substrate of a CUL1-containing ligase (CHEK2); CHK2 is ubiquitinated by a CUL1-containing E3, i.e. by an SCF in which CUL1 supplies the scaffold. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:18644861 Serine 379 (S379) was identified as a novel IR-inducible autophosphorylation site required for ubiquitination of Chk2 by a Cullin 1-containing E3 ligase complex file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:18667692 Poxvirus ankyrin repeat proteins are a unique class of F-box... | MODIFY | Summary: CUL1 interacts with the Orf virus ankyrin-repeat protein ORF008, which carries a poxviral F-box-like motif (ORF008); Poxviral ANK proteins carry functional F-boxes and engage the SKP1-CUL1 scaffold like cellular F-box proteins. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:18667692 all five ANK proteins of a representative poxvirus, Orf virus, interact in vivo with core components of the SCF1 ubiquitin ligase complex file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:18723677 Autoinhibitory regulation of SCF-mediated ubiquitination by ... | MODIFY | Summary: CUL1 interacts with the ubiquitin-like protein NEDD8, which is conjugated to CUL1 Lys720 to activate the ligase (NEDD8); The CUL1 extreme C-terminal domain autoinhibits the scaffold; NEDD8 conjugation relieves it and activates SCF(beta-TrCP2). Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:18723677 deletion of ECTD, or missense mutations designed to disrupt the predicted ECTD x ROC1 interaction, markedly increased the ability of SCF(betaTrCP2) to promote IkappaB alpha polyubiquitination file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:18775313 UBXD7 binds multiple ubiquitin ligases and implicates p97 in... | REMOVE | Summary: CUL1 interacts with the p97/VCP cofactor UBXN7/UBXD7, which binds neddylated cullins (UBXN7). UBXD7 links p97 to cullin ligases; the interaction describes a downstream handler of neddylated CRLs, not a CUL1 activity. Reason: UBXD7 links p97 to cullin ligases; the interaction describes a downstream handler of neddylated CRLs, not a CUL1 activity. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:18775313 The UBX proteins that bind ubiquitin conjugates also interact with dozens of E3 ubiquitin ligases |
| GO:0005515 protein binding | IPI PMID:18805092 Structural insights into NEDD8 activation of cullin-RING lig... | MODIFY | Summary: CUL1 interacts with the SCF(SKP2) substrate p27/CDKN1B (CDKN1B); NEDD8 conjugation reorients the CUL1 WHB domain and RBX1 RING, the structural basis of the activated scaffold. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:18805092 In NEDD8ylated CRL structures, the cullin WHB and Rbx1 RING subdomains are dramatically reoriented, eliminating a CAND1-binding site and imparting multiple potential catalytic geometries to an associated E2 file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:18805092 Structural insights into NEDD8 activation of cullin-RING lig... | MODIFY | Summary: CUL1 interacts with the NEDD8-conjugating enzyme UBE2M/UBC12 (UBE2M); NEDD8 conjugation reorients the CUL1 WHB domain and RBX1 RING, the structural basis of the activated scaffold. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:18805092 In NEDD8ylated CRL structures, the cullin WHB and Rbx1 RING subdomains are dramatically reoriented, eliminating a CAND1-binding site and imparting multiple potential catalytic geometries to an associated E2 file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:18805092 Structural insights into NEDD8 activation of cullin-RING lig... | MODIFY | Summary: CUL1 interacts with the RING subunit RBX1, which with CUL1 forms the catalytic core that recruits E2 enzymes (RBX1); NEDD8 conjugation reorients the CUL1 WHB domain and RBX1 RING, the structural basis of the activated scaffold. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:18805092 In NEDD8ylated CRL structures, the cullin WHB and Rbx1 RING subdomains are dramatically reoriented, eliminating a CAND1-binding site and imparting multiple potential catalytic geometries to an associated E2 file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:18805092 Structural insights into NEDD8 activation of cullin-RING lig... | MODIFY | Summary: CUL1 interacts with the ubiquitin-like protein NEDD8, which is conjugated to CUL1 Lys720 to activate the ligase (NEDD8); NEDD8 conjugation reorients the CUL1 WHB domain and RBX1 RING, the structural basis of the activated scaffold. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:18805092 In NEDD8ylated CRL structures, the cullin WHB and Rbx1 RING subdomains are dramatically reoriented, eliminating a CAND1-binding site and imparting multiple potential catalytic geometries to an associated E2 file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:18818696 Structural and functional coupling of Hsp90- and Sgt1-centre... | MODIFY | Summary: CUL1 interacts with the adaptor SKP1, which tethers F-box proteins to the CUL1 N-terminal stalk (SKP1); SKP1 binding to CUL1 defines the substrate-specific arm of SCF that Sgt1/HSP90 engage. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:18818696 Sgt1 bridges the Hsp90 molecular chaperone system to the substrate-specific arm of SCF ubiquitin ligase complexes file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:18826954 SCCRO (DCUN1D1) is an essential component of the E3 complex ... | REMOVE | Summary: CUL1 interacts with the NEDD8 co-E3 DCUN1D1/DCNL1 (DCUN1D1). SCCRO/DCUN1D1 is a NEDD8 co-E3 acting on CUL1; CUL1 is the substrate of this interaction. Reason: SCCRO/DCUN1D1 is a NEDD8 co-E3 acting on CUL1; CUL1 is the substrate of this interaction. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:18826954 SCCRO (also known as DCUN1D1) binds to the components of the neddylation pathway (Cullin-ROC1, Ubc12, and CAND1) and augments but is not required for cullin neddylation |
| GO:0005515 protein binding | IPI PMID:18929646 Multiple isoforms of beta-TrCP display differential activiti... | MODIFY | Summary: CUL1 interacts with the adaptor SKP1, which tethers F-box proteins to the CUL1 N-terminal stalk (SKP1); beta-TrCP isoform binding to SKP1 determines recruitment into the CUL1-scaffolded SCF. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:18929646 beta-TrCP1 isoforms containing exon III, which are the most highly expressed isoforms in most tissues, do not interact with Skp1 file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:19615732 Defining the human deubiquitinating enzyme interaction lands... | REMOVE | Summary: CUL1 interacts with the F-box substrate receptor beta-TrCP2/FBXW11 (FBXW11). High-throughput DUB interactome (CompPASS); bare binding from a screen is uninformative for CUL1 function. Reason: High-throughput DUB interactome (CompPASS); bare binding from a screen is uninformative for CUL1 function. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:19615732 We identified 774 candidate interacting proteins associated with 75 Dubs |
| GO:0005515 protein binding | IPI PMID:19615732 Defining the human deubiquitinating enzyme interaction lands... | REMOVE | Summary: CUL1 interacts with the F-box substrate receptor beta-TrCP1/BTRC (BTRC). High-throughput DUB interactome (CompPASS); bare binding from a screen is uninformative for CUL1 function. Reason: High-throughput DUB interactome (CompPASS); bare binding from a screen is uninformative for CUL1 function. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:19615732 We identified 774 candidate interacting proteins associated with 75 Dubs |
| GO:0005515 protein binding | IPI PMID:19713960 Regulation of nucleolar signalling to p53 through NEDDylatio... | REMOVE | Summary: CUL1 interacts with the ubiquitin-like protein NEDD8, which is conjugated to CUL1 Lys720 to activate the ligase (NEDD8). The paper concerns NEDD8 modification of ribosomal protein L11; CUL1 is not the subject. Reason: The paper concerns NEDD8 modification of ribosomal protein L11; CUL1 is not the subject. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:19713960 NEDD8 acts as a crucial, new regulator of nucleolar signalling to p53 |
| GO:0005515 protein binding | IPI PMID:19945379 Rapid E2-E3 assembly and disassembly enable processive ubiqu... | MODIFY | Summary: CUL1 interacts with the E2 ubiquitin-conjugating enzyme CDC34/UBE2R1 (CDC34); CDC34 binds the CUL1 basic canyon with nanomolar affinity but rapid kinetics, enabling processive chain synthesis by SCF. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. For CDC34 the interaction is E2 recruitment through the CUL1 basic canyon, so GO:0031624 is proposed as well. Proposed replacements: ubiquitin conjugating enzyme binding ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:19945379 rapid association driven by electrostatic interactions between the acidic tail of Cdc34 and a basic 'canyon' in the Cul1 subunit of SCF file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:19945379 Rapid E2-E3 assembly and disassembly enable processive ubiqu... | MODIFY | Summary: CUL1 interacts with the adaptor SKP1, which tethers F-box proteins to the CUL1 N-terminal stalk (SKP1); CDC34 binds the CUL1 basic canyon with nanomolar affinity but rapid kinetics, enabling processive chain synthesis by SCF. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:19945379 rapid association driven by electrostatic interactions between the acidic tail of Cdc34 and a basic 'canyon' in the Cul1 subunit of SCF file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:19945379 Rapid E2-E3 assembly and disassembly enable processive ubiqu... | MODIFY | Summary: CUL1 interacts with the F-box substrate receptor beta-TrCP1/BTRC (BTRC); CDC34 binds the CUL1 basic canyon with nanomolar affinity but rapid kinetics, enabling processive chain synthesis by SCF. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:19945379 rapid association driven by electrostatic interactions between the acidic tail of Cdc34 and a basic 'canyon' in the Cul1 subunit of SCF file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:20399188 Structural insights into the COP9 signalosome and its common... | MODIFY | Summary: CUL1 interacts with the RING subunit RBX1, which with CUL1 forms the catalytic core that recruits E2 enzymes (RBX1); CUL1-RBX1 is the deneddylation substrate/scaffold used to demonstrate functional assembly of recombinant CSN. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:20399188 we report recombinant insect cell expression and two-step purification of human CSN and demonstrate its functional assembly file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:20596027 SCF(Cyclin F) controls centrosome homeostasis and mitotic fi... | MODIFY | Summary: CUL1 interacts with the F-box protein cyclin F (CCNF); Cyclin F assembles with SKP1-CUL1-RBX1 into SCF(cyclin F), which ubiquitinates CP110. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:20596027 we identified CP110, a protein that is essential for centrosome duplication, as an interactor and substrate of Cyclin F file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:20708156 Phosphorylation by casein kinase I promotes the turnover of ... | MODIFY | Summary: CUL1 interacts with the SCF(beta-TrCP) substrate MDM2 (MDM2); MDM2 is recruited to the CUL1-scaffolded SCF(beta-TrCP) for ubiquitination after CKI phosphorylation. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:20708156 phosphorylation of Mdm2 by casein kinase I (CKI) at multiple sites triggers its interaction with, and subsequent ubiquitination and destruction, by SCF(beta-TRCP) file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:21102408 CSN complex controls the stability of selected synaptic prot... | REMOVE | Summary: CUL1 interacts with the ubiquitin-like protein NEDD8, which is conjugated to CUL1 Lys720 to activate the ligase (NEDD8). The CSN/torsinA study reports NEDD8 pathway effects on synaptic proteins; the CUL1-NEDD8 row carries no CUL1 function. Reason: The CSN/torsinA study reports NEDD8 pathway effects on synaptic proteins; the CUL1-NEDD8 row carries no CUL1 function. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:21102408 the stability of stonin 2 is regulated by neddylation, another CSN-associated activity |
| GO:0005515 protein binding | IPI PMID:21119685 Notch-induced Asb2 expression promotes protein ubiquitinatio... | MODIFY | Summary: CUL1 interacts with the SOCS-box protein ASB2, which bridges CUL5 and SCF(SKP2) modules (ASB2); ASB2 bridges non-canonical dimeric ligases that include the SKP1-CUL1 scaffold via SKP2. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:21119685 Asb2 bridges the formation of non-canonical cullin-based complexes through interaction with not only ElonginB/C and Cullin (Cul) 5, but also the F-box-containing protein, Skp2, which is known to associate with Skp1 and Cul1 file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:21145461 Dynamics of cullin-RING ubiquitin ligase network revealed by... | REMOVE | Summary: CUL1 interacts with the chaperone HSP90AB1 (HSP90AB1). Quantitative proteomics of CRL network stoichiometry; the many interactions are informative about assembly states but each bare binding row adds no molecular function. Reason: Quantitative proteomics of CRL network stoichiometry; the many interactions are informative about assembly states but each bare binding row adds no molecular function. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:21145461 independent of cullin neddylation, a large fraction of cullins are assembled with adaptor modules, whereas only a small fraction are associated with CAND1 |
| GO:0005515 protein binding | IPI PMID:21145461 Dynamics of cullin-RING ubiquitin ligase network revealed by... | REMOVE | Summary: CUL1 interacts with the adaptor SKP1, which tethers F-box proteins to the CUL1 N-terminal stalk (SKP1). Quantitative proteomics of CRL network stoichiometry; the many interactions are informative about assembly states but each bare binding row adds no molecular function. Reason: Quantitative proteomics of CRL network stoichiometry; the many interactions are informative about assembly states but each bare binding row adds no molecular function. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:21145461 independent of cullin neddylation, a large fraction of cullins are assembled with adaptor modules, whereas only a small fraction are associated with CAND1 |
| GO:0005515 protein binding | IPI PMID:21145461 Dynamics of cullin-RING ubiquitin ligase network revealed by... | REMOVE | Summary: CUL1 interacts with the SCF(FBXO33) substrate YB-1/YBX1 (YBX1). Quantitative proteomics of CRL network stoichiometry; the many interactions are informative about assembly states but each bare binding row adds no molecular function. Reason: Quantitative proteomics of CRL network stoichiometry; the many interactions are informative about assembly states but each bare binding row adds no molecular function. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:21145461 independent of cullin neddylation, a large fraction of cullins are assembled with adaptor modules, whereas only a small fraction are associated with CAND1 |
| GO:0005515 protein binding | IPI PMID:21145461 Dynamics of cullin-RING ubiquitin ligase network revealed by... | REMOVE | Summary: CUL1 interacts with the F-box substrate receptor SKP2 (SKP2). Quantitative proteomics of CRL network stoichiometry; the many interactions are informative about assembly states but each bare binding row adds no molecular function. Reason: Quantitative proteomics of CRL network stoichiometry; the many interactions are informative about assembly states but each bare binding row adds no molecular function. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:21145461 independent of cullin neddylation, a large fraction of cullins are assembled with adaptor modules, whereas only a small fraction are associated with CAND1 |
| GO:0005515 protein binding | IPI PMID:21145461 Dynamics of cullin-RING ubiquitin ligase network revealed by... | REMOVE | Summary: CUL1 interacts with the ubiquitin-like protein NEDD8, which is conjugated to CUL1 Lys720 to activate the ligase (NEDD8). Quantitative proteomics of CRL network stoichiometry; the many interactions are informative about assembly states but each bare binding row adds no molecular function. Reason: Quantitative proteomics of CRL network stoichiometry; the many interactions are informative about assembly states but each bare binding row adds no molecular function. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:21145461 independent of cullin neddylation, a large fraction of cullins are assembled with adaptor modules, whereas only a small fraction are associated with CAND1 |
| GO:0005515 protein binding | IPI PMID:21145461 Dynamics of cullin-RING ubiquitin ligase network revealed by... | REMOVE | Summary: CUL1 interacts with the F-box protein FBXO33 (FBXO33). Quantitative proteomics of CRL network stoichiometry; the many interactions are informative about assembly states but each bare binding row adds no molecular function. Reason: Quantitative proteomics of CRL network stoichiometry; the many interactions are informative about assembly states but each bare binding row adds no molecular function. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:21145461 independent of cullin neddylation, a large fraction of cullins are assembled with adaptor modules, whereas only a small fraction are associated with CAND1 |
| GO:0005515 protein binding | IPI PMID:21145461 Dynamics of cullin-RING ubiquitin ligase network revealed by... | REMOVE | Summary: CUL1 interacts with the exchange factor CAND1, which binds unneddylated CUL1 and blocks SKP1 binding (CAND1). Quantitative proteomics of CRL network stoichiometry; the many interactions are informative about assembly states but each bare binding row adds no molecular function. Reason: Quantitative proteomics of CRL network stoichiometry; the many interactions are informative about assembly states but each bare binding row adds no molecular function. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:21145461 independent of cullin neddylation, a large fraction of cullins are assembled with adaptor modules, whereas only a small fraction are associated with CAND1 |
| GO:0005515 protein binding | IPI PMID:21145461 Dynamics of cullin-RING ubiquitin ligase network revealed by... | REMOVE | Summary: CUL1 interacts with the F-box protein FBXO22 (FBXO22). Quantitative proteomics of CRL network stoichiometry; the many interactions are informative about assembly states but each bare binding row adds no molecular function. Reason: Quantitative proteomics of CRL network stoichiometry; the many interactions are informative about assembly states but each bare binding row adds no molecular function. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:21145461 independent of cullin neddylation, a large fraction of cullins are assembled with adaptor modules, whereas only a small fraction are associated with CAND1 |
| GO:0005515 protein binding | IPI PMID:21145461 Dynamics of cullin-RING ubiquitin ligase network revealed by... | REMOVE | Summary: CUL1 interacts with the F-box substrate receptor FBXW7 (FBXW7). Quantitative proteomics of CRL network stoichiometry; the many interactions are informative about assembly states but each bare binding row adds no molecular function. Reason: Quantitative proteomics of CRL network stoichiometry; the many interactions are informative about assembly states but each bare binding row adds no molecular function. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:21145461 independent of cullin neddylation, a large fraction of cullins are assembled with adaptor modules, whereas only a small fraction are associated with CAND1 |
| GO:0005515 protein binding | IPI PMID:21145461 Dynamics of cullin-RING ubiquitin ligase network revealed by... | REMOVE | Summary: CUL1 interacts with the glycoprotein-binding F-box protein FBXO17 (FBXO17). Quantitative proteomics of CRL network stoichiometry; the many interactions are informative about assembly states but each bare binding row adds no molecular function. Reason: Quantitative proteomics of CRL network stoichiometry; the many interactions are informative about assembly states but each bare binding row adds no molecular function. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:21145461 independent of cullin neddylation, a large fraction of cullins are assembled with adaptor modules, whereas only a small fraction are associated with CAND1 |
| GO:0005515 protein binding | IPI PMID:21145461 Dynamics of cullin-RING ubiquitin ligase network revealed by... | REMOVE | Summary: CUL1 interacts with the F-box protein FBXO3 (FBXO3). Quantitative proteomics of CRL network stoichiometry; the many interactions are informative about assembly states but each bare binding row adds no molecular function. Reason: Quantitative proteomics of CRL network stoichiometry; the many interactions are informative about assembly states but each bare binding row adds no molecular function. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:21145461 independent of cullin neddylation, a large fraction of cullins are assembled with adaptor modules, whereas only a small fraction are associated with CAND1 |
| GO:0005515 protein binding | IPI PMID:21145461 Dynamics of cullin-RING ubiquitin ligase network revealed by... | REMOVE | Summary: CUL1 interacts with the F-box substrate receptor beta-TrCP2/FBXW11 (FBXW11). Quantitative proteomics of CRL network stoichiometry; the many interactions are informative about assembly states but each bare binding row adds no molecular function. Reason: Quantitative proteomics of CRL network stoichiometry; the many interactions are informative about assembly states but each bare binding row adds no molecular function. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:21145461 independent of cullin neddylation, a large fraction of cullins are assembled with adaptor modules, whereas only a small fraction are associated with CAND1 |
| GO:0005515 protein binding | IPI PMID:21145461 Dynamics of cullin-RING ubiquitin ligase network revealed by... | REMOVE | Summary: CUL1 interacts with the F-box protein FBXW2 (FBXW2). Quantitative proteomics of CRL network stoichiometry; the many interactions are informative about assembly states but each bare binding row adds no molecular function. Reason: Quantitative proteomics of CRL network stoichiometry; the many interactions are informative about assembly states but each bare binding row adds no molecular function. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:21145461 independent of cullin neddylation, a large fraction of cullins are assembled with adaptor modules, whereas only a small fraction are associated with CAND1 |
| GO:0005515 protein binding | IPI PMID:21145461 Dynamics of cullin-RING ubiquitin ligase network revealed by... | REMOVE | Summary: CUL1 interacts with the F-box substrate receptor beta-TrCP1/BTRC (BTRC). Quantitative proteomics of CRL network stoichiometry; the many interactions are informative about assembly states but each bare binding row adds no molecular function. Reason: Quantitative proteomics of CRL network stoichiometry; the many interactions are informative about assembly states but each bare binding row adds no molecular function. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:21145461 independent of cullin neddylation, a large fraction of cullins are assembled with adaptor modules, whereas only a small fraction are associated with CAND1 |
| GO:0005515 protein binding | IPI PMID:21145461 Dynamics of cullin-RING ubiquitin ligase network revealed by... | REMOVE | Summary: CUL1 interacts with the RBR E3 ligase ARIH1/HHARI, which is activated by neddylated CUL1-RBX1 (ARIH1). Quantitative proteomics of CRL network stoichiometry; the many interactions are informative about assembly states but each bare binding row adds no molecular function. Reason: Quantitative proteomics of CRL network stoichiometry; the many interactions are informative about assembly states but each bare binding row adds no molecular function. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:21145461 independent of cullin neddylation, a large fraction of cullins are assembled with adaptor modules, whereas only a small fraction are associated with CAND1 |
| GO:0005515 protein binding | IPI PMID:21765416 A RING E3-substrate complex poised for ubiquitin-like protei... | REMOVE | Summary: CUL1 interacts with yeast Ubc12, the NEDD8-conjugating enzyme (Ubc12). Structural study of how RBX1 positions UBC12 to neddylate CUL1; CUL1 is the neddylation substrate here. Reason: Structural study of how RBX1 positions UBC12 to neddylate CUL1; CUL1 is the neddylation substrate here. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:21765416 we address how the RING E3 RBX1 positions NEDD8's E2 (UBC12) and substrate (CUL1) |
| GO:0005515 protein binding | IPI PMID:21765416 A RING E3-substrate complex poised for ubiquitin-like protei... | REMOVE | Summary: CUL1 interacts with the RING subunit RBX1, which with CUL1 forms the catalytic core that recruits E2 enzymes (RBX1). Structural study of how RBX1 positions UBC12 to neddylate CUL1; CUL1 is the neddylation substrate here. Reason: Structural study of how RBX1 positions UBC12 to neddylate CUL1; CUL1 is the neddylation substrate here. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:21765416 we address how the RING E3 RBX1 positions NEDD8's E2 (UBC12) and substrate (CUL1) |
| GO:0005515 protein binding | IPI PMID:21765416 A RING E3-substrate complex poised for ubiquitin-like protei... | REMOVE | Summary: CUL1 interacts with the ubiquitin-like protein NEDD8, which is conjugated to CUL1 Lys720 to activate the ligase (NEDD8). Structural study of how RBX1 positions UBC12 to neddylate CUL1; CUL1 is the neddylation substrate here. Reason: Structural study of how RBX1 positions UBC12 to neddylate CUL1; CUL1 is the neddylation substrate here. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:21765416 we address how the RING E3 RBX1 positions NEDD8's E2 (UBC12) and substrate (CUL1) |
| GO:0005515 protein binding | IPI PMID:21778237 COMMD1 (copper metabolism MURR1 domain-containing protein 1)... | REMOVE | Summary: CUL1 interacts with COMMD1, which displaces CAND1 from cullins (COMMD1). COMMD1 displaces CAND1 from cullins; this regulates CUL1 and defines no CUL1 activity. Reason: COMMD1 displaces CAND1 from cullins; this regulates CUL1 and defines no CUL1 activity. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:21778237 COMMD1 can actively displace CAND1 from CRLs |
| GO:0005515 protein binding | IPI PMID:21778237 COMMD1 (copper metabolism MURR1 domain-containing protein 1)... | REMOVE | Summary: CUL1 interacts with COMMD8, a COMMD-family CAND1 antagonist (COMMD8). COMMD1 displaces CAND1 from cullins; this regulates CUL1 and defines no CUL1 activity. Reason: COMMD1 displaces CAND1 from cullins; this regulates CUL1 and defines no CUL1 activity. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:21778237 COMMD1 can actively displace CAND1 from CRLs |
| GO:0005515 protein binding | IPI PMID:21778237 COMMD1 (copper metabolism MURR1 domain-containing protein 1)... | REMOVE | Summary: CUL1 interacts with COMMD9, a COMMD-family CAND1 antagonist (COMMD9). COMMD1 displaces CAND1 from cullins; this regulates CUL1 and defines no CUL1 activity. Reason: COMMD1 displaces CAND1 from cullins; this regulates CUL1 and defines no CUL1 activity. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:21778237 COMMD1 can actively displace CAND1 from CRLs |
| GO:0005515 protein binding | IPI PMID:22466964 NEDD8 links cullin-RING ubiquitin ligase function to the p97... | REMOVE | Summary: CUL1 interacts with the p97/VCP cofactor UBXN7/UBXD7, which binds neddylated cullins (UBXN7). UBXD7 binds neddylated cullins via its UIM; CUL1 is the recognized entity, not the actor. Reason: UBXD7 binds neddylated cullins via its UIM; CUL1 is the recognized entity, not the actor. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:22466964 UBXD7 and its yeast ortholog, Ubx5, associate only with the active, NEDD8- or Rub1-modified form of cullins |
| GO:0005515 protein binding | IPI PMID:22479149 Mediator acts upstream of the transcriptional activator Gal4... | REMOVE | Summary: CUL1 interacts with the Mediator subunit MED6 (MED6). The cached abstract concerns yeast Mediator and Gal4/Gal80 turnover; the human MED6-CUL1 interaction cannot be tied to a CUL1 function from the available text. Reason: The cached abstract concerns yeast Mediator and Gal4/Gal80 turnover; the human MED6-CUL1 interaction cannot be tied to a CUL1 function from the available text. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:22479149 the protein degradation of the inhibitor Gal80, and not of the activator Gal4, is required for galactose induction of the GAL genes |
| GO:0005515 protein binding | IPI PMID:22632967 Cyclin F-mediated degradation of ribonucleotide reductase M2... | MODIFY | Summary: CUL1 interacts with the F-box protein cyclin F (CCNF); Cyclin F is the receptor of CUL1-scaffolded SCF(cyclin F), which degrades RRM2 in G2. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:22632967 during G2, following CDK-mediated phosphorylation of Thr33, RRM2 is degraded via SCF(cyclin F) to maintain balanced dNTP pools and genome stability file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:22660580 F-box protein FBXL19-mediated ubiquitination and degradation... | MODIFY | Summary: CUL1 interacts with the RING subunit RBX1, which with CUL1 forms the catalytic core that recruits E2 enzymes (RBX1); FBXL19 assembles with SKP1-CUL1-RBX1 into the SCF that ubiquitinates ST2L. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:22660580 FBXL19, an 'orphan' member of the Skp1-Cullin-F-box family of E3 ubiquitin ligases, selectively bound to ST2L to mediate its polyubiquitination and elimination in the proteasome file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:22660580 F-box protein FBXL19-mediated ubiquitination and degradation... | MODIFY | Summary: CUL1 interacts with the adaptor SKP1, which tethers F-box proteins to the CUL1 N-terminal stalk (SKP1); FBXL19 assembles with SKP1-CUL1-RBX1 into the SCF that ubiquitinates ST2L. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:22660580 FBXL19, an 'orphan' member of the Skp1-Cullin-F-box family of E3 ubiquitin ligases, selectively bound to ST2L to mediate its polyubiquitination and elimination in the proteasome file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:22939624 Quantitative analysis of HSP90-client interactions reveals p... | REMOVE | Summary: CUL1 interacts with the chaperone HSP90AB1 (HSP90AB1). Systematic HSP90 client survey; a bare HSP90AB1 interaction is uninformative. Reason: Systematic HSP90 client survey; a bare HSP90AB1 interaction is uninformative. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:22939624 We systematically and quantitatively surveyed most human kinases, transcription factors, and E3 ligases for interaction with HSP90 and its cochaperone CDC37 |
| GO:0005515 protein binding | IPI PMID:23108047 FBXW7-mediated degradation of CCDC6 is impaired by ATM durin... | MODIFY | Summary: CUL1 interacts with the F-box substrate receptor FBXW7 (FBXW7); The F-box proteins bound here (FBXW7, FBXO6, FBXO4, FBXW2) are receptors on the CUL1 scaffold; SCF(FBXW7) degrades CCDC6. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:23108047 FBXW7 interacts with and targets CCDC6 for ubiquitin-mediated proteasomal degradation file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:23108047 FBXW7-mediated degradation of CCDC6 is impaired by ATM durin... | MODIFY | Summary: CUL1 interacts with the glycoprotein-binding F-box protein FBXO6 (FBXO6); The F-box proteins bound here (FBXW7, FBXO6, FBXO4, FBXW2) are receptors on the CUL1 scaffold; SCF(FBXW7) degrades CCDC6. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:23108047 FBXW7 interacts with and targets CCDC6 for ubiquitin-mediated proteasomal degradation file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:23108047 FBXW7-mediated degradation of CCDC6 is impaired by ATM durin... | MODIFY | Summary: CUL1 interacts with the F-box protein FBXO4 (FBXO4); The F-box proteins bound here (FBXW7, FBXO6, FBXO4, FBXW2) are receptors on the CUL1 scaffold; SCF(FBXW7) degrades CCDC6. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:23108047 FBXW7 interacts with and targets CCDC6 for ubiquitin-mediated proteasomal degradation file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:23108047 FBXW7-mediated degradation of CCDC6 is impaired by ATM durin... | MODIFY | Summary: CUL1 interacts with the F-box protein FBXW2 (FBXW2); The F-box proteins bound here (FBXW7, FBXO6, FBXO4, FBXW2) are receptors on the CUL1 scaffold; SCF(FBXW7) degrades CCDC6. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:23108047 FBXW7 interacts with and targets CCDC6 for ubiquitin-mediated proteasomal degradation file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:23452855 Competing E3 ubiquitin ligases govern circadian periodicity ... | MODIFY | Summary: CUL1 interacts with mouse Fbxl21, the cytoplasmic CRY-directed F-box protein (Fbxl21); FBXL21 forms an SCF complex on the CUL1 scaffold that degrades cytoplasmic CRY. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:23452855 FBXL21 forms an SCF E3 ligase complex that slowly degrades CRY in the cytoplasm but antagonizes the stronger E3 ligase activity of FBXL3 in the nucleus file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:23452855 Competing E3 ubiquitin ligases govern circadian periodicity ... | MODIFY | Summary: CUL1 interacts with mouse Fbxl3, the nuclear CRY-directed F-box protein (Fbxl3); FBXL21 forms an SCF complex on the CUL1 scaffold that degrades cytoplasmic CRY. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:23452855 FBXL21 forms an SCF E3 ligase complex that slowly degrades CRY in the cytoplasm but antagonizes the stronger E3 ligase activity of FBXL3 in the nucleus file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:23452856 FBXL21 regulates oscillation of the circadian clock through ... | MODIFY | Summary: CUL1 interacts with mouse Fbxl21, the cytoplasmic CRY-directed F-box protein (Fbxl21); FBXL21 and FBXL3 assemble SCF ligases on CUL1 with opposing effects on CRY stability. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:23452856 FBXL21 also ubiquitinates CRYs but counteracts FBXL3 file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:23452856 FBXL21 regulates oscillation of the circadian clock through ... | MODIFY | Summary: CUL1 interacts with mouse Fbxl3, the nuclear CRY-directed F-box protein (Fbxl3); FBXL21 and FBXL3 assemble SCF ligases on CUL1 with opposing effects on CRY stability. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:23452856 FBXL21 also ubiquitinates CRYs but counteracts FBXL3 file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:23563313 CCDC22 deficiency in humans blunts activation of proinflamma... | REMOVE | Summary: CUL1 interacts with CCDC22, a COMMD-complex partner (CCDC22). CCDC22 acts with COMMD proteins on CRL regulation; no CUL1 molecular function is defined. Reason: CCDC22 acts with COMMD proteins on CRL regulation; no CUL1 molecular function is defined. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:23563313 patient-derived cells demonstrated impaired NF-ΞΊB activation due to decreased IΞΊB ubiquitination and degradation |
| GO:0005515 protein binding | IPI PMID:23776465 Myeloma overexpressed 2 (Myeov2) regulates L11 subnuclear lo... | REMOVE | Summary: CUL1 interacts with COP9 signalosome subunit 9 (isoform 2) (COPS9). COPS9/Myeov2 study of L11 neddylation; the CUL1 interaction is incidental. Reason: COPS9/Myeov2 study of L11 neddylation; the CUL1 interaction is incidental. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:23776465 Although Myeov2 interacted with a Nedd8 deconjugation enzyme COP9 signalosome |
| GO:0005515 protein binding | IPI PMID:24076655 TRIAD1 and HHARI bind to and are activated by distinct neddy... | MODIFY | Summary: CUL1 interacts with the RBR E3 ligase ARIH1/HHARI, which is activated by neddylated CUL1-RBX1 (ARIH1); neddylated CRL binding stimulates the RBR ligase activity of ARIH1/HHARI. Reason: ARIH1 is a bona fide E3 ligase and its binding to neddylated CUL1-RBX1 is functionally consequential (tandem SCF/ARIH1 ubiquitination), so GO:0031625 ubiquitin protein ligase binding is the informative replacement. Proposed replacements: ubiquitin protein ligase binding Supporting Evidence: PMID:24076655 binding of the cognate neddylated CRL to TRIAD1 or HHARI greatly stimulates RBR ligase activity in vitro file:human/CUL1/CUL1-uniprot.txt SCF complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins |
| GO:0005515 protein binding | IPI PMID:24192928 Oncogenic function of SCCRO5/DCUN1D5 requires its Neddylatio... | REMOVE | Summary: CUL1 interacts with the NEDD8 co-E3 DCUN1D1/DCNL1 (DCUN1D1). DCUN1D1/DCUN1D5 are NEDD8 co-E3s acting on CUL1; CUL1 is their substrate. Reason: DCUN1D1/DCUN1D5 are NEDD8 co-E3s acting on CUL1; CUL1 is their substrate. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:24192928 SCCRO5 promoted cullin neddylation while maintaining conserved reaction processivity paradigms |
| GO:0005515 protein binding | IPI PMID:24192928 Oncogenic function of SCCRO5/DCUN1D5 requires its Neddylatio... | REMOVE | Summary: CUL1 interacts with the NEDD8 co-E3 DCUN1D5/DCNL5 (DCUN1D5). DCUN1D1/DCUN1D5 are NEDD8 co-E3s acting on CUL1; CUL1 is their substrate. Reason: DCUN1D1/DCUN1D5 are NEDD8 co-E3s acting on CUL1; CUL1 is their substrate. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:24192928 SCCRO5 promoted cullin neddylation while maintaining conserved reaction processivity paradigms |
| GO:0005515 protein binding | IPI PMID:24794231 Phosphorylation of cyclin Y by CDK14 induces its ubiquitinat... | MODIFY | Summary: CUL1 interacts with cyclin Y, an SCF substrate after CDK14 phosphorylation (CCNY); Cyclin Y is stabilized when Cul1 is inactivated, identifying SCF as its ligase after CDK14 phosphorylation. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:24794231 Inactivation of either CDK14 or Cul1 results in accumulation of CCNY file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:24949976 Structure of a RING E3 trapped in action reveals ligation me... | REMOVE | Summary: CUL1 interacts with the NEDD8-conjugating enzyme UBE2M/UBC12 (UBE2M). Structure of RBX1-UBC12~NEDD8-CUL1-DCN1 neddylation intermediate; CUL1 is the acceptor target in this reaction. Reason: Structure of RBX1-UBC12~NEDD8-CUL1-DCN1 neddylation intermediate; CUL1 is the acceptor target in this reaction. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:24949976 which reveals the mechanism of NEDD8 ligation and how a particular UBL and acceptor lysine are matched by a multifunctional RING E3 |
| GO:0005515 protein binding | IPI PMID:24949976 Structure of a RING E3 trapped in action reveals ligation me... | REMOVE | Summary: CUL1 interacts with the RING subunit RBX1, which with CUL1 forms the catalytic core that recruits E2 enzymes (RBX1). Structure of RBX1-UBC12~NEDD8-CUL1-DCN1 neddylation intermediate; CUL1 is the acceptor target in this reaction. Reason: Structure of RBX1-UBC12~NEDD8-CUL1-DCN1 neddylation intermediate; CUL1 is the acceptor target in this reaction. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:24949976 which reveals the mechanism of NEDD8 ligation and how a particular UBL and acceptor lysine are matched by a multifunctional RING E3 |
| GO:0005515 protein binding | IPI PMID:24949976 Structure of a RING E3 trapped in action reveals ligation me... | REMOVE | Summary: CUL1 interacts with the ubiquitin-like protein NEDD8, which is conjugated to CUL1 Lys720 to activate the ligase (NEDD8). Structure of RBX1-UBC12~NEDD8-CUL1-DCN1 neddylation intermediate; CUL1 is the acceptor target in this reaction. Reason: Structure of RBX1-UBC12~NEDD8-CUL1-DCN1 neddylation intermediate; CUL1 is the acceptor target in this reaction. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:24949976 which reveals the mechanism of NEDD8 ligation and how a particular UBL and acceptor lysine are matched by a multifunctional RING E3 |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | REMOVE | Summary: CUL1 interacts with the F-box substrate receptor beta-TrCP2/FBXW11 (FBXW11). Proximity-ligation screen of 1204 endogenous PPIs; bare binding from a screen is uninformative. Reason: Proximity-ligation screen of 1204 endogenous PPIs; bare binding from a screen is uninformative. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:25241761 an in situ proximity ligation assay, to investigate 1204 endogenous PPIs in HeLa cells, and 557 PPIs of them tested positive |
| GO:0005515 protein binding | IPI PMID:25435324 Structural mechanism of nuclear transport mediated by import... | REMOVE | Summary: CUL1 interacts with the exchange factor CAND1, which binds unneddylated CUL1 and blocks SKP1 binding (CAND1). Study of HEAT-repeat proteins (including CAND1) passing through the nuclear pore; no CUL1 function is defined. Reason: Study of HEAT-repeat proteins (including CAND1) passing through the nuclear pore; no CUL1 function is defined. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:25435324 not only karyopherin Ξ² family proteins but also other proteins with HEAT repeats could pass through the NPC by themselves |
| GO:0005515 protein binding | IPI PMID:25557911 Cyclin F suppresses B-Myb activity to promote cell cycle che... | MODIFY | Summary: CUL1 interacts with the F-box protein cyclin F (CCNF); Cyclin F is the receptor of CUL1-scaffolded SCF(cyclin F) that controls the G2 checkpoint. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:25557911 the F-box protein cyclin F plays an important role in checkpoint control following ionizing radiation file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:25609649 Proteomic analyses reveal distinct chromatin-associated and ... | REMOVE | Summary: CUL1 interacts with the F-box substrate receptor beta-TrCP2/FBXW11 (FBXW11). TAP-MS survey of transcription factor complexes; screen-derived bare binding is uninformative. Reason: TAP-MS survey of transcription factor complexes; screen-derived bare binding is uninformative. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:25609649 we performed proteomics analyses of soluble and chromatin-associated complexes of 56 TFs |
| GO:0005515 protein binding | IPI PMID:26906416 Characterization of the mammalian family of DCN-type NEDD8 E... | REMOVE | Summary: CUL1 interacts with the NEDD8 co-E3 DCUN1D2/DCNL2 (DCUN1D2). DCNL proteins are NEDD8 co-E3s that form reserve complexes with CAND1-cullins; CUL1 is the neddylation substrate. Reason: DCNL proteins are NEDD8 co-E3s that form reserve complexes with CAND1-cullins; CUL1 is the neddylation substrate. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:26906416 DCNLs form stable stoichiometric complexes with CAND1 and cullins that can only be neddylated in the presence of a substrate adaptor |
| GO:0005515 protein binding | IPI PMID:26906416 Characterization of the mammalian family of DCN-type NEDD8 E... | REMOVE | Summary: CUL1 interacts with the NEDD8 co-E3 DCUN1D3/DCNL3 (DCUN1D3). DCNL proteins are NEDD8 co-E3s that form reserve complexes with CAND1-cullins; CUL1 is the neddylation substrate. Reason: DCNL proteins are NEDD8 co-E3s that form reserve complexes with CAND1-cullins; CUL1 is the neddylation substrate. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:26906416 DCNLs form stable stoichiometric complexes with CAND1 and cullins that can only be neddylated in the presence of a substrate adaptor |
| GO:0005515 protein binding | IPI PMID:26906416 Characterization of the mammalian family of DCN-type NEDD8 E... | REMOVE | Summary: CUL1 interacts with the NEDD8 co-E3 DCUN1D4/DCNL4 (DCUN1D4). DCNL proteins are NEDD8 co-E3s that form reserve complexes with CAND1-cullins; CUL1 is the neddylation substrate. Reason: DCNL proteins are NEDD8 co-E3s that form reserve complexes with CAND1-cullins; CUL1 is the neddylation substrate. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:26906416 DCNLs form stable stoichiometric complexes with CAND1 and cullins that can only be neddylated in the presence of a substrate adaptor |
| GO:0005515 protein binding | IPI PMID:26906416 Characterization of the mammalian family of DCN-type NEDD8 E... | REMOVE | Summary: CUL1 interacts with the NEDD8 co-E3 DCUN1D1/DCNL1 (DCUN1D1). DCNL proteins are NEDD8 co-E3s that form reserve complexes with CAND1-cullins; CUL1 is the neddylation substrate. Reason: DCNL proteins are NEDD8 co-E3s that form reserve complexes with CAND1-cullins; CUL1 is the neddylation substrate. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:26906416 DCNLs form stable stoichiometric complexes with CAND1 and cullins that can only be neddylated in the presence of a substrate adaptor |
| GO:0005515 protein binding | IPI PMID:26906416 Characterization of the mammalian family of DCN-type NEDD8 E... | REMOVE | Summary: CUL1 interacts with the NEDD8 co-E3 DCUN1D5/DCNL5 (DCUN1D5). DCNL proteins are NEDD8 co-E3s that form reserve complexes with CAND1-cullins; CUL1 is the neddylation substrate. Reason: DCNL proteins are NEDD8 co-E3s that form reserve complexes with CAND1-cullins; CUL1 is the neddylation substrate. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:26906416 DCNLs form stable stoichiometric complexes with CAND1 and cullins that can only be neddylated in the presence of a substrate adaptor |
| GO:0005515 protein binding | IPI PMID:27542266 DCUN1D3 activates SCFSKP2 ubiquitin E3 ligase activity and c... | MODIFY | Summary: CUL1 interacts with the F-box substrate receptor SKP2; the NEDD8 co-E3 DCUN1D3/DCNL3 (SKP2, DCUN1D3); DCUN1D3-driven CUL1 neddylation is required to form the active SCF(SKP2) that degrades p27. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:27542266 the silence of DCUN1D3 can inhibit the formation of SCFSKP2 complex by reducing Cullin-1 neddylation file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:27705803 A High-Density Map for Navigating the Human Polycomb Complex... | REMOVE | Summary: CUL1 interacts with the adaptor SKP1, which tethers F-box proteins to the CUL1 N-terminal stalk (SKP1). Polycomb complexome AP-MS map; screen-derived bare binding is uninformative. Reason: Polycomb complexome AP-MS map; screen-derived bare binding is uninformative. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:27705803 we systematically mapped the human PcG complexome using a robust affinity purification mass spectrometry approach |
| GO:0005515 protein binding | IPI PMID:28007894 The pseudophosphatase STYX targets the F-box of FBXW7 and in... | MODIFY | Summary: CUL1 interacts with the adaptor SKP1, which tethers F-box proteins to the CUL1 N-terminal stalk; the F-box substrate receptor FBXW7 (isoform 1) (SKP1, FBXW7); STYX blocks recruitment of FBXW7 into the SCF, i.e. its binding to the SKP1-CUL1 scaffold. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:28007894 STYX binds to the F-box domain of FBXW7 and disables its recruitment into the SCF complex file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: CUL1 interacts with the F-box substrate receptor SKP2 (SKP2). BioPlex 2.0 interactome; screen-derived bare binding is uninformative. Reason: BioPlex 2.0 interactome; screen-derived bare binding is uninformative. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:28514442 Here we present BioPlex 2.0 (Biophysical Interactions of ORFeome-derived complexes) |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: CUL1 interacts with the F-box substrate receptor FBXW7 (FBXW7). BioPlex 2.0 interactome; screen-derived bare binding is uninformative. Reason: BioPlex 2.0 interactome; screen-derived bare binding is uninformative. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:28514442 Here we present BioPlex 2.0 (Biophysical Interactions of ORFeome-derived complexes) |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: CUL1 interacts with the glycoprotein-binding F-box protein FBXO17 (FBXO17). BioPlex 2.0 interactome; screen-derived bare binding is uninformative. Reason: BioPlex 2.0 interactome; screen-derived bare binding is uninformative. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:28514442 Here we present BioPlex 2.0 (Biophysical Interactions of ORFeome-derived complexes) |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: CUL1 interacts with the glycoprotein-binding F-box protein FBXO6 (FBXO6). BioPlex 2.0 interactome; screen-derived bare binding is uninformative. Reason: BioPlex 2.0 interactome; screen-derived bare binding is uninformative. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:28514442 Here we present BioPlex 2.0 (Biophysical Interactions of ORFeome-derived complexes) |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: CUL1 interacts with the F-box protein FBXO4 (FBXO4). BioPlex 2.0 interactome; screen-derived bare binding is uninformative. Reason: BioPlex 2.0 interactome; screen-derived bare binding is uninformative. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:28514442 Here we present BioPlex 2.0 (Biophysical Interactions of ORFeome-derived complexes) |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: CUL1 interacts with the RBR E3 ligase ARIH1/HHARI, which is activated by neddylated CUL1-RBX1 (ARIH1). BioPlex 2.0 interactome; screen-derived bare binding is uninformative. Reason: BioPlex 2.0 interactome; screen-derived bare binding is uninformative. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:28514442 Here we present BioPlex 2.0 (Biophysical Interactions of ORFeome-derived complexes) |
| GO:0005515 protein binding | IPI PMID:29149593 NOTCH2 Hajdu-Cheney Mutations Escape SCF(FBW7)-Dependent Pro... | MODIFY | Summary: CUL1 interacts with the RING subunit RBX1, which with CUL1 forms the catalytic core that recruits E2 enzymes; the adaptor SKP1, which tethers F-box proteins to the CUL1 N-terminal stalk; the SCF(FBXW7) substrate NOTCH2; the F-box substrate receptor FBXW7 (RBX1, SKP1, NOTCH2, FBXW7); NOTCH2 is degraded by SCF(FBW7) built on the SKP1-CUL1-RBX1 scaffold; Hajdu-Cheney truncations escape it. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:29149593 sustained osteoclast activity is largely due to accumulation of NOTCH2 carrying a truncated C terminus that escapes FBW7-mediated ubiquitination and degradation file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:30833792 A protein-interaction network of interferon-stimulated genes... | REMOVE | Summary: CUL1 interacts with the glycoprotein-binding F-box protein FBXO6 (FBXO6). ISG interactome survey; screen-derived bare binding is uninformative. Reason: ISG interactome survey; screen-derived bare binding is uninformative. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:30833792 We identified interactions between 104 ISGs and 1,401 cellular binding partners |
| GO:0005515 protein binding | IPI PMID:32726803 Papain-like protease regulates SARS-CoV-2 viral spread and i... | REMOVE | Summary: CUL1 interacts with the RING subunit RBX1, which with CUL1 forms the catalytic core that recruits E2 enzymes (RBX1). SARS-CoV-2 PLpro deconjugation study in which neddylated CUL1-RBX1 serves as a substrate reagent; no CUL1 function is defined. Reason: SARS-CoV-2 PLpro deconjugation study in which neddylated CUL1-RBX1 serves as a substrate reagent; no CUL1 function is defined. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:32726803 SCoV2-PLpro and SCoV-PLpro share 83% sequence identity but exhibit different host substrate preferences |
| GO:0005515 protein binding | IPI PMID:32726803 Papain-like protease regulates SARS-CoV-2 viral spread and i... | REMOVE | Summary: CUL1 interacts with the ubiquitin-like protein NEDD8, which is conjugated to CUL1 Lys720 to activate the ligase (NEDD8). SARS-CoV-2 PLpro deconjugation study in which neddylated CUL1-RBX1 serves as a substrate reagent; no CUL1 function is defined. Reason: SARS-CoV-2 PLpro deconjugation study in which neddylated CUL1-RBX1 serves as a substrate reagent; no CUL1 function is defined. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:32726803 SCoV2-PLpro and SCoV-PLpro share 83% sequence identity but exhibit different host substrate preferences |
| GO:0005515 protein binding | IPI PMID:33692209 KDM2B Overexpression Facilitates Lytic De Novo KSHV Infectio... | MODIFY | Summary: CUL1 interacts with the RING subunit RBX1, which with CUL1 forms the catalytic core that recruits E2 enzymes (RBX1); KDM2B binds the SCF complex through its F-box, using the CUL1 scaffold to stabilize c-Jun. Reason: The informative molecular function behind this interaction is CUL1 acting as the ubiquitin ligase complex scaffold (GO:0160072) that joins the SKP1/F-box receptor module to the RBX1 catalytic module; bare protein binding does not capture it. Proposed replacements: ubiquitin ligase complex scaffold activity Supporting Evidence: PMID:33692209 This effect is dependent upon the binding of KDM2B to the SKP1-CUL1-F-box (SCF) E3 ubiquitin ligase complex via its F-box domain file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: CUL1 interacts with the RING subunit RBX1, which with CUL1 forms the catalytic core that recruits E2 enzymes (RBX1). BioPlex 3.0/HCT116 interactome; screen-derived bare binding is uninformative. Reason: BioPlex 3.0/HCT116 interactome; screen-derived bare binding is uninformative. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:33961781 The first, BioPlex 3.0, results from affinity purification of 10,128 human proteins |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: CUL1 interacts with the adaptor SKP1, which tethers F-box proteins to the CUL1 N-terminal stalk (SKP1). BioPlex 3.0/HCT116 interactome; screen-derived bare binding is uninformative. Reason: BioPlex 3.0/HCT116 interactome; screen-derived bare binding is uninformative. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:33961781 The first, BioPlex 3.0, results from affinity purification of 10,128 human proteins |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: CUL1 interacts with the F-box substrate receptor FBXW7 (FBXW7). BioPlex 3.0/HCT116 interactome; screen-derived bare binding is uninformative. Reason: BioPlex 3.0/HCT116 interactome; screen-derived bare binding is uninformative. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:33961781 The first, BioPlex 3.0, results from affinity purification of 10,128 human proteins |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: CUL1 interacts with the glycoprotein-binding F-box protein FBXO17 (FBXO17). BioPlex 3.0/HCT116 interactome; screen-derived bare binding is uninformative. Reason: BioPlex 3.0/HCT116 interactome; screen-derived bare binding is uninformative. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:33961781 The first, BioPlex 3.0, results from affinity purification of 10,128 human proteins |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: CUL1 interacts with the glycoprotein-binding F-box protein FBXO6 (FBXO6). BioPlex 3.0/HCT116 interactome; screen-derived bare binding is uninformative. Reason: BioPlex 3.0/HCT116 interactome; screen-derived bare binding is uninformative. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:33961781 The first, BioPlex 3.0, results from affinity purification of 10,128 human proteins |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: CUL1 interacts with the F-box protein FBXO3 (FBXO3). BioPlex 3.0/HCT116 interactome; screen-derived bare binding is uninformative. Reason: BioPlex 3.0/HCT116 interactome; screen-derived bare binding is uninformative. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:33961781 The first, BioPlex 3.0, results from affinity purification of 10,128 human proteins |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: CUL1 interacts with the F-box protein FBXO4 (FBXO4). BioPlex 3.0/HCT116 interactome; screen-derived bare binding is uninformative. Reason: BioPlex 3.0/HCT116 interactome; screen-derived bare binding is uninformative. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:33961781 The first, BioPlex 3.0, results from affinity purification of 10,128 human proteins |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: CUL1 interacts with the F-box substrate receptor beta-TrCP1/BTRC (BTRC). BioPlex 3.0/HCT116 interactome; screen-derived bare binding is uninformative. Reason: BioPlex 3.0/HCT116 interactome; screen-derived bare binding is uninformative. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:33961781 The first, BioPlex 3.0, results from affinity purification of 10,128 human proteins |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: CUL1 interacts with the RBR E3 ligase ARIH1/HHARI, which is activated by neddylated CUL1-RBX1 (ARIH1). BioPlex 3.0/HCT116 interactome; screen-derived bare binding is uninformative. Reason: BioPlex 3.0/HCT116 interactome; screen-derived bare binding is uninformative. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:33961781 The first, BioPlex 3.0, results from affinity purification of 10,128 human proteins |
| GO:0005515 protein binding | IPI PMID:34591642 A protein network map of head and neck cancer reveals PIK3CA... | REMOVE | Summary: CUL1 interacts with the F-box substrate receptor FBXW7 (FBXW7). Head-and-neck cancer PPI network; screen-derived bare binding is uninformative. Reason: Head-and-neck cancer PPI network; screen-derived bare binding is uninformative. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:34591642 This network uncovers 771 interactions from cancer and noncancerous cell states |
| GO:0005515 protein binding | IPI PMID:35156780 CFTR interactome mapping using the mammalian membrane two-hy... | REMOVE | Summary: CUL1 interacts with the chloride channel CFTR (CFTR). CFTR MaMTH-HTS interactome; screen-derived bare binding is uninformative. Reason: CFTR MaMTH-HTS interactome; screen-derived bare binding is uninformative. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:35156780 Here, we report the application of a high-throughput screening variant of the Mammalian Membrane Two-Hybrid (MaMTH-HTS) |
| GO:0005515 protein binding | IPI PMID:36012204 Differential CFTR-Interactome Proximity Labeling Procedures ... | REMOVE | Summary: CUL1 interacts with the chloride channel CFTR (CFTR). CFTR proximity-labeling interactome; screen-derived bare binding is uninformative. Reason: CFTR proximity-labeling interactome; screen-derived bare binding is uninformative. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:36012204 we evaluated TurboID- and APEX2-based proximity labeling of WT CFTR and compared the obtained data to those reported in databases |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: CUL1 interacts with the adaptor SKP1, which tethers F-box proteins to the CUL1 N-terminal stalk (SKP1). Multimodal U2OS cell map; screen-derived bare binding is uninformative. Reason: Multimodal U2OS cell map; screen-derived bare binding is uninformative. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:40205054 we construct a global map of human subcellular architecture through joint measurement of biophysical interactions and immunofluorescence images for over 5,100 proteins |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: CUL1 interacts with the F-box substrate receptor FBXW7 (FBXW7). Multimodal U2OS cell map; screen-derived bare binding is uninformative. Reason: Multimodal U2OS cell map; screen-derived bare binding is uninformative. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:40205054 we construct a global map of human subcellular architecture through joint measurement of biophysical interactions and immunofluorescence images for over 5,100 proteins |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: CUL1 interacts with the glycoprotein-binding F-box protein FBXO17 (FBXO17). Multimodal U2OS cell map; screen-derived bare binding is uninformative. Reason: Multimodal U2OS cell map; screen-derived bare binding is uninformative. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:40205054 we construct a global map of human subcellular architecture through joint measurement of biophysical interactions and immunofluorescence images for over 5,100 proteins |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: CUL1 interacts with the glycoprotein-binding F-box protein FBXO6 (FBXO6). Multimodal U2OS cell map; screen-derived bare binding is uninformative. Reason: Multimodal U2OS cell map; screen-derived bare binding is uninformative. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:40205054 we construct a global map of human subcellular architecture through joint measurement of biophysical interactions and immunofluorescence images for over 5,100 proteins |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: CUL1 interacts with the F-box protein FBXO3 (FBXO3). Multimodal U2OS cell map; screen-derived bare binding is uninformative. Reason: Multimodal U2OS cell map; screen-derived bare binding is uninformative. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:40205054 we construct a global map of human subcellular architecture through joint measurement of biophysical interactions and immunofluorescence images for over 5,100 proteins |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: CUL1 interacts with the F-box substrate receptor beta-TrCP2/FBXW11 (FBXW11). Multimodal U2OS cell map; screen-derived bare binding is uninformative. Reason: Multimodal U2OS cell map; screen-derived bare binding is uninformative. Per repository policy for bare GO:0005515 rows, removal records that the generic term is uninformative, not that the interaction is false. Supporting Evidence: PMID:40205054 we construct a global map of human subcellular architecture through joint measurement of biophysical interactions and immunofluorescence images for over 5,100 proteins |
| GO:0005634 nucleus | IBA GO_REF:0000033 | ACCEPT | Summary: CUL1-based SCF ligases act on nuclear substrates (p27, cyclin E, MYC, E2F1, CRY, REST, HURP), so a nuclear pool is core. Reason: PAINT-inferred and curator-inferred nuclear localization is consistent with the nuclear SCF substrates and with GO-CAM models placing CUL1 scaffold activity in the nucleus. Supporting Evidence: file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005634 nucleus | IC PMID:15145941 Fbx7 functions in the SCF complex regulating Cdk1-cyclin B-p... | ACCEPT | Summary: CUL1-based SCF ligases act on nuclear substrates (p27, cyclin E, MYC, E2F1, CRY, REST, HURP), so a nuclear pool is core. Reason: PAINT-inferred and curator-inferred nuclear localization is consistent with the nuclear SCF substrates and with GO-CAM models placing CUL1 scaffold activity in the nucleus. Supporting Evidence: PMID:15145941 In the SCF(Fbx7) complex, Fbx7 recruits HURP through its C-terminal proline-rich region in a Cdk1-cyclin B-phosphorylation dependent manner file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-1363328 | ACCEPT | Summary: Nucleoplasmic SCF in the Reactome reaction "Phosphorylated p130 (RBL2) binds SCF(Skp2):Cks1 complex". Reason: Core localisation: the Reactome reaction places the CUL1-containing SCF in the nucleoplasm, where the CDK-inhibitor, replication-factor, transcription-factor and NICD degradations occur. Supporting Evidence: Reactome:R-HSA-1363328 Phosphorylated p130 (RBL2) binds SCF (Skp2) ubiquitin ligase in complex with Cks1. Phosphorylation of p130 (RBL2) serine residue S672 by CDK4/6 is critical for this interaction. file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-1363331 | ACCEPT | Summary: Nucleoplasmic SCF in the Reactome reaction "Ubiquitination of p130 (RBL2) by SCF (Skp2)". Reason: Core localisation: the Reactome reaction places the CUL1-containing SCF in the nucleoplasm, where the CDK-inhibitor, replication-factor, transcription-factor and NICD degradations occur. Supporting Evidence: Reactome:R-HSA-1363331 As quiescent G0 cells reenter the cell cycle, p130 (RBL2) is phosphorylated by CDK4/6. This phosphorylated p130 (RBL2) binds ubiquitin ligase SCF (Skp2) in complex with Cks1, and is subsequently ubiquitinated and degrade file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-187545 | ACCEPT | Summary: Nucleoplasmic SCF in the Reactome reaction "Association of Cks1 with SCF(Skp2) complex". Reason: Core localisation: the Reactome reaction places the CUL1-containing SCF in the nucleoplasm, where the CDK-inhibitor, replication-factor, transcription-factor and NICD degradations occur. Supporting Evidence: Reactome:R-HSA-187545 The accessory protein, Cks1 promotes efficient interaction between phosphorylated p27 and the SCF (Skp2) complex (Ganoth et al., 2001; Spruck et al., 2001). Cks1 binds to Skp2 in the leucine-rich repeat (LRR) domain and file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-187552 | ACCEPT | Summary: Nucleoplasmic SCF in the Reactome reaction "Binding of phospho-p27/p21:Cdk2:Cyclin E/A to the SCF(Skp2):Cks1 complex". Reason: Core localisation: the Reactome reaction places the CUL1-containing SCF in the nucleoplasm, where the CDK-inhibitor, replication-factor, transcription-factor and NICD degradations occur. Supporting Evidence: Reactome:R-HSA-187552 The association of Cks1 with both Skp2 and phosphorylated p27 promotes a tight interaction between p27 and the SCF complex (Hao et al., 2005). file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-187574 | ACCEPT | Summary: Nucleoplasmic SCF in the Reactome reaction "Degradation of ubiquitinated p27/p21 by the 26S proteasome". Reason: Core localisation: the Reactome reaction places the CUL1-containing SCF in the nucleoplasm, where the CDK-inhibitor, replication-factor, transcription-factor and NICD degradations occur. Supporting Evidence: Reactome:R-HSA-187574 Following ubiquitination by the SCF(Skp2):Cks1 complex, phospho-p27/p21 is degraded by the 26S proteasome. file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-187575 | ACCEPT | Summary: Nucleoplasmic SCF in the Reactome reaction "Ubiquitination of phospho-p27/p21". Reason: Core localisation: the Reactome reaction places the CUL1-containing SCF in the nucleoplasm, where the CDK-inhibitor, replication-factor, transcription-factor and NICD degradations occur. Supporting Evidence: Reactome:R-HSA-187575 Once in tight contact with the SCF (Skp2):Cks1 complex, phosphorylated p27/p21 is ubiquitinated. file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-2220967 | ACCEPT | Summary: Nucleoplasmic SCF in the Reactome reaction "p-NICD1 PEST domain mutants do not bind FBXW7". Reason: Core localisation: the Reactome reaction places the CUL1-containing SCF in the nucleoplasm, where the CDK-inhibitor, replication-factor, transcription-factor and NICD degradations occur. 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 mutant file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-2220978 | ACCEPT | Summary: Nucleoplasmic SCF in the Reactome reaction "FBXW7 WD mutants do not bind NICD1". Reason: Core localisation: the Reactome reaction places the CUL1-containing SCF in the nucleoplasm, where the CDK-inhibitor, replication-factor, transcription-factor and NICD degradations occur. Supporting Evidence: Reactome:R-HSA-2220978 FBXW7 (FBW7) mutations are found in ~20% of T-cell acute lymphoblastic leukemia samples. Although a homozygous FBXW7 deletion has been reported, mutations found in FBXW7 are predominantly dominant negative missense mutat file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-68946 | ACCEPT | Summary: Nucleoplasmic SCF in the Reactome reaction "Phosphorylated Orc1 is ubiquitinated while still associated with chromatin". Reason: Core localisation: the Reactome reaction places the CUL1-containing SCF in the nucleoplasm, where the CDK-inhibitor, replication-factor, transcription-factor and NICD degradations occur. 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. While the ORC1 region phosphorylated b file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-69598 | ACCEPT | Summary: Nucleoplasmic SCF in the Reactome reaction "Ubiquitination of phosphorylated CDC25A". Reason: Core localisation: the Reactome reaction places the CUL1-containing SCF in the nucleoplasm, where the CDK-inhibitor, replication-factor, transcription-factor and NICD degradations occur. 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). Instability of CDC25A during interphase and upon exposure to file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8939688 | ACCEPT | Summary: Nucleoplasmic SCF in the Reactome reaction "SCF(SKP2) complex binds RUNX2". Reason: Core localisation: the Reactome reaction places the CUL1-containing SCF in the nucleoplasm, where the CDK-inhibitor, replication-factor, transcription-factor and NICD degradations occur. 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). This process is inhibited by glucose uptake in osteoblasts (Wei et al. 2 file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8939706 | ACCEPT | Summary: Nucleoplasmic SCF in the Reactome reaction "SCF(SKP2) polyubiquitinates RUNX2". Reason: Core localisation: the Reactome reaction places the CUL1-containing SCF in the nucleoplasm, where the CDK-inhibitor, replication-factor, transcription-factor and NICD degradations occur. 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. SKP2-triggered RUNX2 degradation negatively regulates osteogenesis by inhibi file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9708517 | ACCEPT | Summary: Nucleoplasmic SCF in the Reactome reaction "FBXL17 ubiquitinates BACH1 (in BACH1:FBXL17:SCF (SKP2))". Reason: Core localisation: the Reactome reaction places the CUL1-containing SCF in the nucleoplasm, where the CDK-inhibitor, replication-factor, transcription-factor and NICD degradations occur. 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. FBXL17 is a regulator of the nuclear factor erythroid 2-related factor 2 (NFE2L2) ox file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9708525 | ACCEPT | Summary: Nucleoplasmic SCF in the Reactome reaction "BACH1:FBXL17 binds SCF(SKP2) complex". Reason: Core localisation: the Reactome reaction places the CUL1-containing SCF in the nucleoplasm, where the CDK-inhibitor, replication-factor, transcription-factor and NICD degradations occur. 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. FBXL17 is a regulator of the nuclear factor erythroid 2-related factor 2 (NFE2L2) ox file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9725023 | ACCEPT | Summary: Nucleoplasmic SCF in the Reactome reaction "NPM1-ALK fusion dimer binds SKP1:CUL1:RBX1:ZC3HC1". Reason: Core localisation: the Reactome reaction places the CUL1-containing SCF in the nucleoplasm, where the CDK-inhibitor, replication-factor, transcription-factor and NICD degradations occur. 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). ZC3HC1 file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9725030 | ACCEPT | Summary: Nucleoplasmic SCF in the Reactome reaction "MAPK1 phsophorylates ZC3HCF1 in a NPM-ALK-dependent manner". Reason: Core localisation: the Reactome reaction places the CUL1-containing SCF in the nucleoplasm, where the CDK-inhibitor, replication-factor, transcription-factor and NICD degradations occur. 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). Nuclear MAPK1 phosphorylates ZC3HC1 at a number of serine residues, with resid file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9762091 | ACCEPT | Summary: Nucleoplasmic SCF in the Reactome reaction "NFE2L2 is ubiquitinated by BTRC:SKP1:CUL1:RBX1". Reason: Core localisation: the Reactome reaction places the CUL1-containing SCF in the nucleoplasm, where the CDK-inhibitor, replication-factor, transcription-factor and NICD degradations occur. 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, file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9762093 | ACCEPT | Summary: Nucleoplasmic SCF in the Reactome reaction "BTRC binds p-S344, 347 NFE2L2". Reason: Core localisation: the Reactome reaction places the CUL1-containing SCF in the nucleoplasm, where the CDK-inhibitor, replication-factor, transcription-factor and NICD degradations occur. 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 a file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9762096 | ACCEPT | Summary: Nucleoplasmic SCF in the Reactome reaction "Ub,pS335,S338,T NFE2L2 is degraded". Reason: Core localisation: the Reactome reaction places the CUL1-containing SCF in the nucleoplasm, where the CDK-inhibitor, replication-factor, transcription-factor and NICD degradations occur. 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/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005654 nucleoplasm | TAS Reactome:R-NUL-2064853 | ACCEPT | Summary: Nucleoplasmic SCF in the Reactome reaction "FBXW7 binds phosphorylated NICD1". Reason: Core localisation: the Reactome reaction places the CUL1-containing SCF in the nucleoplasm, where the CDK-inhibitor, replication-factor, transcription-factor and NICD degradations occur. Supporting Evidence: Reactome:R-NUL-2064853 The E3 ubiquitin ligase FBXW7, a homologue of C. elegans sel-10, binds to Notch1 intracellular domain NICD1. This interaction was demonstrated by co-immunoprecipitation of the human recombinant FBXW7 and mouse recombinan file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005654 nucleoplasm | TAS Reactome:R-NUL-2064883 | ACCEPT | Summary: Nucleoplasmic SCF in the Reactome reaction "FBXW7 mediates ubiquitination of phosphorylated NICD1". Reason: Core localisation: the Reactome reaction places the CUL1-containing SCF in the nucleoplasm, where the CDK-inhibitor, replication-factor, transcription-factor and NICD degradations occur. 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). Ubiquitination and degradation of NICD1 by F file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005654 nucleoplasm | TAS Reactome:R-NUL-9604628 | ACCEPT | Summary: Nucleoplasmic SCF in the Reactome reaction "FBXW7 promotes ubiquitination of mouse p-NICD4". Reason: Core localisation: the Reactome reaction places the CUL1-containing SCF in the nucleoplasm, where the CDK-inhibitor, replication-factor, transcription-factor and NICD degradations occur. 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 deg file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005737 cytoplasm | IC PMID:11961546 Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin liga... | ACCEPT | Summary: Cytoplasmic CUL1 scaffolds SCF(beta-TrCP) and other cytoplasmic ligases (IkappaB-alpha, beta-catenin, DEPTOR, cytoplasmic CRY). Reason: Curator inference from the SCF structure paper; cytoplasmic SCF activity is well documented and is a core site of action. Supporting Evidence: PMID:11961546 Cul1 serves as a rigid scaffold that organizes the Skp1-F boxSkp2 and Rbx1 subunits, holding them over 100 A apart file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | IEA GO_REF:0000117 | ACCEPT | Summary: Cytosolic localisation of CUL1 (ARBA rule), consistent with the many cytosolic SCF reactions. Reason: Agrees with Reactome and literature: a large fraction of CUL1 is cytosolic, where SCF(beta-TrCP) and the CAND1/NEDD8 cycle operate. Supporting Evidence: file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1168642 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "SCF with beta-TrCP1 or beta-TrCP2 binds NF-kappaB:phospho-IkB". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. Supporting Evidence: Reactome:R-HSA-1168642 SKP:Cul:F-box (SCF) complexes containing F-box factors Beta-TrCP1 (BTRCP, E3RSIkappaB) or beta-TrCP2 (BTRCP2, FBXW11, HOS) bind IkappaB (Yaron et al. 1998, Fuchs et al. 1999, Suzuki et al. 1999, Tan et al. 1999, Winston file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1168643 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "SCF-beta-TrCP ubiquitinylates IkB". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. Supporting Evidence: Reactome:R-HSA-1168643 SKP:Cul:F-box (SCF) complexes containing F-box factors Beta-TrCP1 (BTRCP, E3RSIkappaB) or beta-TrCP2 (BTRCP2, FBXW11, HOS) catalyze the polyubiquitination of IkappaB (Yaron et al. 1998, Fuchs et al. 1999, Suzuki et al. 1 file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1170539 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "Prolactin receptor is internalized". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. 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). Recruitment of the SCFbeta-TrCP ubiquitin ligase complex enables receptor ubiqui file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1370500 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "PRLR binds SCF beta-TrCP complex". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. 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). This downregulation mechani file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-174159 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "Ubiquitination of Emi1 by SCF-beta-TrCP". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. Supporting Evidence: Reactome:R-HSA-174159 Following its association with SCF-ΓTrCP, phospho-Emi1 is poly-ubiquitinated. file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-174203 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "SCF-mediated degradation of Emi1". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. Supporting Evidence: Reactome:R-HSA-174203 Multiubiquitinated Emi1 is degraded by the 26S proteasome. file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-174209 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "Phosphorylated Emi1 binds the beta-TrCP in the SCF complex". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. Supporting Evidence: Reactome:R-HSA-174209 Cdk mediated phosphorylation of Emi1 is believed to promotes its phospho- Ser145-Ser149 dependent association with beta-TrCP. file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-209063 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "Beta-TrCP ubiquitinates NFKB p50:p65:phospho IKBA complex". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. Supporting Evidence: Reactome:R-HSA-209063 SCF (Beta-TrCP) ubiquitinates phosphorylated I kappa B alpha. file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-209125 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "'SCF Beta-TrCP complex binds to NFKB p50:p65: phospho IKBA complex'". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. 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/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2130279 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "Association of beta-catenin with the RBX1:SCF(beta-TrCP1) ubiquitin". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. Supporting Evidence: Reactome:R-HSA-2130279 B-TrCP associates with phosphorylated beta-catenin through the B-TrCP WD40 repeat region. Currently, it is unclear whether the ubiquitin ligase binds beta-catenin after it leaves the complex. It is equally possible that file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2130282 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "Degradation of ubiquitinated beta catenin by the proteasome". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. Supporting Evidence: Reactome:R-HSA-2130282 Ubiquitinated beta-catenin is degraded by the proteasome. file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2130286 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "Multi-ubiquitination of phospho-beta-catenin by RBX1:SCF(beta-TrCP1)". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. Supporting Evidence: Reactome:R-HSA-2130286 Beta-catenin is ubiquitinated by the SCF-B-TrCP1 complex. file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-3000335 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "SCF-beta-TrCp1/2 ubiquitinates phosphorylated BORA". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. Supporting Evidence: Reactome:R-HSA-3000335 SCF-beta-TrCP ubiquitin ligases promote ubiquitination and degradation of BORA phosphorylated by PLK1, and this is required for timely mitotic progression (Seki et al. 2008). file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-3000339 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "Phosphorylated BORA binds SCF-beta-TrCp1/2". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. Supporting Evidence: Reactome:R-HSA-3000339 The substrate recognition subunits beta-TrCP (BTRC) and beta-TrCP2 (FBXW11) of SCF-beta-TrPC1 and SCF-beta-TrPC2 ubiquitin ligases, respectively, bind the phosphorylated DSGYNT motif of BORA (Seki et al. 2008). file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5607723 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "SCF-beta-TRCP binds p-7S-p100 in active NIK:p-S176,180-IKKA dimer:p-7S-p100:RELB". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. Supporting Evidence: Reactome:R-HSA-5607723 Phosphorylated C-terminal serines 866, 870 and 872 in NFKB2 creates binding site for beta-TRCP (beta-transducin repeat-containing protein), the receptor subunit of a SCF-type of E3 ubiquitin ligase, SCF beta-TRCP (Liang file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5607725 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "SCF-beta-TRCP ubiquitinates p-7S-p100:RELB in active NIK:p-176,S180-IKKA". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. Supporting Evidence: Reactome:R-HSA-5607725 Ubiquitination of p100 is very specific. Lysine residue K855 has been identified as the anchoring site for ubiquitin and required for signaling mediated processing of p100 to p52. In the presence of SCF-beta-TRCP E3 liga file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5607728 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "beta-TRCP ubiquitinates IkB-alpha in p-S32,33-IkB-alpha:NF-kB complex". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. Supporting Evidence: Reactome:R-HSA-5607728 Two major signaling steps are required for the removal of IkappaB (IkB) alpha an inhibitor of NF-kB: activation of the IkB kinase (IKK) and degradation of the phosphorylated IkB alpha. IKK activation and IkB degradation file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5610742 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "SCF(beta-TrCP) ubiquitinates p-GLI1". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. Supporting Evidence: Reactome:R-HSA-5610742 GLI1 protein is degraded by the proteasome in the absence of Hh signal. GLI1 levels are stabilized by treatment of cells with the proteasome inhibitor MG312, and GLI1 and beta-TrCP1 co-precipitate when expressed in NIH 3 file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5610746 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "SCF(beta-TrCP) ubiquitinates p-GLI3". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. 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). After ubiquitination, GLI3 is processed to t file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5684248 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "SCF betaTrCP1,2 binds p-NFkB p105:TPL2:ABIN2". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. Supporting Evidence: Reactome:R-HSA-5684248 IKK-mediated NFkB p105 phosphorylation generates a binding site for betaTrCP, the receptor subunit of the SCF-type beta-TrCP ubiquitin E3 ligase complex. file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5684250 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "'SCF betaTrCP ubiquitinates NFKB p105 within p-S927, S932-NFkB p105:TPL2:ABIN2 '". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. Supporting Evidence: Reactome:R-HSA-5684250 Beta-TrCP ubiquitinates p105 at several lysine residues within the C-terminal region 660-968. The level of ubiquitination is variable; in this reaction p105 is represented with 3 ubiquitinated lysine residues. Removal of file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5691108 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "SKP1:FBXL5:CUL1:NEDD8 ubiquitinylates IREB2". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. Supporting Evidence: Reactome:R-HSA-5691108 Cellular iron homeostasis is maintained by the coordinate posttranscriptional regulation of iron metabolism genes. The E3 ubiquitin ligase complex containing the F-box/LRR-repeat protein 5 (FBXL5) protein (SKP1:FBXL5:CUL file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5691131 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "CANDI binds CUL1". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. Supporting Evidence: Reactome:R-HSA-5691131 Cullin-associated NEDD8-dissociated protein 1 (CANDI, TIP120) is a key assembly factor of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes, acting as a F-box protein exchange factor. CANDI binds cullin-1 (CUL1 file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5691167 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "CUL1, SKP1, FBXL5 bind". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. Supporting Evidence: Reactome:R-HSA-5691167 Cellular iron homeostasis is maintained by the coordinate posttranscriptional regulation of iron metabolism genes. The E3 ubiquitin ligase complex comprising the F-box/LRR-repeat protein 5 (FBXL5) protein, S-phase kinase file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5691176 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "NEDD8 binds CUL1 (in SKP1:CUL1:FXBL5)". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. Supporting Evidence: Reactome:R-HSA-5691176 Cellular iron homeostasis is maintained by the coordinate posttranscriptional regulation of iron metabolism genes. The E3 ubiquitin ligase complex comprising the F-box/LRR-repeat protein 5 (FBXL5) protein, S-phase kinase file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8853496 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "SCF:FBXL7 binds AURKA". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. 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/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8854041 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "SCF-FBXL7 ubiquitinates AURKA". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. 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/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8854044 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "Proteasome degrades AURKA ubiquitinated by SCF-FBXL7". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. 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/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8854051 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "SCF-FBXL18 ubiquitinates FBXL7". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. 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. The E3 ubiquitin ligase complex SCF-FBXL18 (SKP1:CUL1:RBX1:FBXL18) polyubiquitinates FBXL7 on lysine resid file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8854052 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "Formation of the SCF-FBXL7 complex". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. 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/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8952618 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "AcM-UBE2M transfers NEDD8 to CRL1 E3 ubiquitin ligase complex". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. 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). Neddylation increases the ubiquitination activity of the E3 complex towards its targets, and preven file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8952620 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "NEDD8:AcM-UBE2M binds CRL1 E3 ubiquitin ligase complex". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. 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). Interaction between UBE2M and the CUL1 E3 complex is facilitated by a DCUN1D (also known as DCNL) scaffold protein file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8955241 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "CAND1 binds cytosolic CRL E3 ubiquitin ligases". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. 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 compl file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8955289 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "COMMDs displace CAND1 from cytosolic CRL E3 ubiquitin ligase complexes". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. 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 transpo file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8956040 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "COP9 signalosome deneddylates cytosolic CRL E3 ubiquitin ligase complexes". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. 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. Deneddylation decreases ubiquitin ligase activity of CRL comp file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8956200 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "MyrG-DCUN1D3 binds CRL1 E3 ubiquitin ligase complex". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. Supporting Evidence: Reactome:R-HSA-8956200 DCUN1D3 binds to CRL1 ligase complexes to antagonize their neddylation and activation. DCUN1D3 is unique among the DCUN1D family members in that is N-terminally myristolyated, resulting in plasma membrane localization. B file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-983140 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "Transfer of Ub from E2 to substrate and release of E2". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. 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. In most cases the transfer of ubiquitin is direct from E2 to substrate, but in a smal file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-983147 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "Release of E3 from polyubiquitinated substrate". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. 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/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-983156 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "Polyubiquitination of substrate". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. Supporting Evidence: Reactome:R-HSA-983156 Monoubiquitinated substrate acquires additional ubiquitin modifications in the form of multiple single attachments or a ubiquitin chain. Polyubiquitin chains added through K48 residue of ubiquitin typically targets the s file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-983157 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "Interaction of E3 with substrate and E2-Ub complex". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. 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). E3 ligases includ file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9929350 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "Ubiquitination of CD274 by BTRC-SCF E3-ligase complex". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. Supporting Evidence: Reactome:R-HSA-9929350 Ξ²-TrCP-SCF complex catalyses PD-L1(CD274) polyubiquitination in the presence of GSK3Ξ². Deletion of the destruction box domain or mutation of the GSK3B phosphorylation motif abrogates GSK3Ξ²-mediated PD-L1 ubiquitination a file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9929352 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "Ubiquitinated CD274 is degraded by the 26S proteasome". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. 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/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9929353 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "Deubiquitination of CD274". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. 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. In the study by Lim et al., 2016, CSN5 induced by TNF-alpha signalling was shown to aug file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9929357 | ACCEPT | Summary: Cytosolic CUL1/SCF in the Reactome reaction "p-S184,T180-CD274 binds to BTRC-SCF E3 ubiquitin ligase complex". Reason: Core localisation: SCF(beta-TrCP)-mediated IkappaB, beta-catenin, EMI1 and BORA turnover and the CAND1/NEDD8/CSN regulatory cycle are cytosolic. 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). PD-L1 (CD274) contains a Ξ²-TrCP destruction box domain next to GSK3Ξ² phosphorylation sites that facilitates b file:human/CUL1/CUL1-deep-research-falcon.md SCF-mediated cell-cycle regulation occurs in cytoplasmic and nuclear contexts, whereas a receptor can recruit a distinct CUL1 pool to an organelle. |
| GO:0005886 plasma membrane | IDA PMID:19617556 The human Dcn1-like protein DCNL3 promotes Cul3 neddylation ... | KEEP AS NON CORE | Summary: A membrane-recruited cullin pool: myristoylated DCNL3 accumulates at the plasma membrane and recruits cullins for neddylation there. Reason: Experimental (IDA) annotation from a full-text paper whose cached abstract foregrounds CUL3; the curator read the full text and the DCNL3-CUL1 interaction is documented (PMID:19617556, PMID:26906416). A minor membrane pool is not the core site of SCF action, so it is kept as non-core rather than removed. Supporting Evidence: PMID:19617556 Membrane-bound DCNL3 is able to recruit Cul3 to membranes and is functionally important for Cul3 neddylation in vivo PMID:26906416 DCNLs form stable stoichiometric complexes with CAND1 and cullins that can only be neddylated in the presence of a substrate adaptor |
| 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) ubiquitinates the Pol I catalytic subunit RPA194 under transcription stress. Reason: The direct process is SCF-dependent proteasomal degradation of a polymerase subunit; "regulation of DNA-templated transcription" is a distal consequence and too broad for the shared scaffold (NAS). Supporting Evidence: PMID:36372232 We establish Skp-Cullin-F-box protein complex F-box protein FBXL14 as an E3 ligase for RPA194 file:human/CUL1/CUL1-deep-research-falcon.md Substrate specificity belongs primarily to the associated F-box receptor. |
| GO:0006511 ubiquitin-dependent protein catabolic process | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro cullin-domain mapping to ubiquitin-dependent protein catabolism. Reason: Correct but general; the more specific SCF-dependent term (GO:0031146) is also annotated. Acceptable as an IEA parent. Supporting Evidence: file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| 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) degrades IRP2 in an iron/oxygen-dependent manner; CUL1 scaffolds the ligase. Reason: Genuine but F-box-specific output (FBXL5 senses iron via its hemerythrin domain); non-core for the shared cullin scaffold. Supporting Evidence: PMID:19762597 an E3 ubiquitin ligase complex containing the FBXL5 protein targets IRP2 for proteasomal degradation |
| GO:0007346 regulation of mitotic cell cycle | NAS PMID:36395886 The SCF-FBXW7 E3 ubiquitin ligase triggers degradation of hi... | KEEP AS NON CORE | Summary: SCF(FBXW7) degrades WDR5 to control mitotic cell fate during prolonged mitotic arrest. Reason: F-box-specific (FBXW7) regulatory output; CUL1 supplies the scaffold. Non-core. Supporting Evidence: PMID:36395886 SKP1-CUL1-F-Box-FBXW7 mediates ubiquitination of WDR5 and targets it for proteasomal degradation |
| GO:0010564 regulation of cell cycle process | NAS PMID:31424118 E2F1 proteolysis via SCF-cyclin F underlies synthetic lethal... | KEEP AS NON CORE | Summary: SCF(cyclin F) degrades E2F1 in G2/M to prevent replication stress. Reason: Cyclin F-specific output of the CUL1 scaffold; non-core. Supporting Evidence: PMID:31424118 SCF-cyclin F controls E2F1 ubiquitylation and degradation during the G2/M phase of the cell cycle |
| GO:0010564 regulation of cell cycle process | NAS PMID:34445249 The SCF Complex Is Essential to Maintain Genome and Chromoso... | KEEP AS NON CORE | Summary: Review: SCF complexes (69 in human) time the degradation of primary cell-cycle regulators. Reason: Review-level (NAS) statement that is correct at the family level; the general regulation term is non-core relative to G1/S transition. Supporting Evidence: PMID:34445249 The SKP1, CUL1, F-box protein (SCF) complex encompasses a group of 69 SCF E3 ubiquitin ligase complexes that primarily modify protein substrates with poly-ubiquitin chains to target them for proteasomal degradation |
| GO:0010564 regulation of cell cycle process | NAS PMID:35414786 The role of ubiquitination and deubiquitination in tumor inv... | KEEP AS NON CORE | Summary: General review of ubiquitination in tumour invasion cited for cell-cycle regulation. Reason: Weak (NAS from a broad review), but the term is not wrong for CUL1; kept as non-core, consistent with the other rows for this term. Supporting Evidence: PMID:35414786 E3 ubiquitin ligases and deubiquitinases have the most prominent roles in modulating tumor metastasis |
| 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) degrades CEP192 at centrosomes to limit microtubule nucleation. Reason: F-box-specific (FBXL13; also FBXW5-SAS-6 and cyclin F-CP110) regulatory output; non-core for the scaffold. Supporting Evidence: PMID:29348145 FBXL13, a binding determinant of SCF (SKP1-CUL1-F-box)-family E3 ubiquitin ligases, is enriched at centrosomes PMID:21725316 We identify the centriolar protein HsSAS-6 (refs 4,5) as a critical substrate of the SCF-FBXW5 complex |
| GO:0014033 neural crest cell differentiation | NAS PMID:30190310 Dimerization quality control ensures neuronal development an... | MARK AS OVER ANNOTATED | Summary: SCF(FBXL17) dimerization quality control is required for neural crest and neuronal differentiation. Reason: A developmental phenotype of one F-box receptor pathway, several steps removed from the CUL1 scaffold activity; over-annotation for CUL1 (NAS). Supporting Evidence: PMID:30190310 SCFFBXL17 is required for the differentiation, function, and survival of neural crest and neuronal cells |
| GO:0016567 protein ubiquitination | IBA GO_REF:0000033 | ACCEPT | Summary: CUL1 is the scaffold of SCF ubiquitin ligases; the complex ubiquitinates F-box-bound substrates. Reason: Core process. PAINT, direct assays (SCF(Fbw7)-c-Myc) and the UniPathway mapping agree. Supporting Evidence: file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0016567 protein ubiquitination | IDA PMID:15103331 Phosphorylation-dependent degradation of c-Myc is mediated b... | ACCEPT | Summary: CUL1 is the scaffold of SCF ubiquitin ligases; the complex ubiquitinates F-box-bound substrates. Reason: Core process. PAINT, direct assays (SCF(Fbw7)-c-Myc) and the UniPathway mapping agree. Supporting Evidence: PMID:15103331 the F-box protein Fbw7 interacts with and thereby destabilizes c-Myc in a manner dependent on phosphorylation of MB1 file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0016567 protein ubiquitination | IEA GO_REF:0000041 | ACCEPT | Summary: CUL1 is the scaffold of SCF ubiquitin ligases; the complex ubiquitinates F-box-bound substrates. Reason: Core process. PAINT, direct assays (SCF(Fbw7)-c-Myc) and the UniPathway mapping agree. Supporting Evidence: file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0019005 SCF ubiquitin ligase complex | IBA GO_REF:0000033 | ACCEPT | Summary: CUL1 is the defining cullin subunit of the SCF (SKP1-CUL1-F-box-RBX1) complex. Reason: Core complex membership, supported structurally (PMID:11961546) and by every reconstituted SCF cited here. Supporting Evidence: file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0019005 SCF ubiquitin ligase complex | IDA PMID:11956208 The novel human DNA helicase hFBH1 is an F-box protein. | ACCEPT | Summary: CUL1 is the defining cullin subunit of the SCF (SKP1-CUL1-F-box-RBX1) complex. Reason: Core complex membership, supported structurally (PMID:11961546) and by every reconstituted SCF 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/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0019005 SCF ubiquitin ligase complex | IDA PMID:15103331 Phosphorylation-dependent degradation of c-Myc is mediated b... | ACCEPT | Summary: CUL1 is the defining cullin subunit of the SCF (SKP1-CUL1-F-box-RBX1) complex. Reason: Core complex membership, supported structurally (PMID:11961546) and by every reconstituted SCF cited here. Supporting Evidence: PMID:15103331 the F-box protein Fbw7 interacts with and thereby destabilizes c-Myc in a manner dependent on phosphorylation of MB1 file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0019005 SCF ubiquitin ligase complex | IDA PMID:15145941 Fbx7 functions in the SCF complex regulating Cdk1-cyclin B-p... | ACCEPT | Summary: CUL1 is the defining cullin subunit of the SCF (SKP1-CUL1-F-box-RBX1) complex. Reason: Core complex membership, supported structurally (PMID:11961546) and by every reconstituted SCF cited here. Supporting Evidence: PMID:15145941 In the SCF(Fbx7) complex, Fbx7 recruits HURP through its C-terminal proline-rich region in a Cdk1-cyclin B-phosphorylation dependent manner file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0019005 SCF ubiquitin ligase complex | IDA PMID:16880511 Regulation of p27 degradation and S-phase progression by Ro5... | ACCEPT | Summary: CUL1 is the defining cullin subunit of the SCF (SKP1-CUL1-F-box-RBX1) complex. Reason: Core complex membership, supported structurally (PMID:11961546) and by every reconstituted SCF cited here. Supporting Evidence: PMID:16880511 we identify Skp2 as a component of an Skp1-cullin-F-box complex that is based on a Cul1-Ro52 RING finger B-box coiled-coil motif family protein catalytic core file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0019005 SCF ubiquitin ligase complex | IDA PMID:20596027 SCF(Cyclin F) controls centrosome homeostasis and mitotic fi... | ACCEPT | Summary: CUL1 is the defining cullin subunit of the SCF (SKP1-CUL1-F-box-RBX1) complex. Reason: Core complex membership, supported structurally (PMID:11961546) and by every reconstituted SCF cited here. Supporting Evidence: PMID:20596027 we identified CP110, a protein that is essential for centrosome duplication, as an interactor and substrate of Cyclin F file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0019005 SCF ubiquitin ligase complex | IDA PMID:21572392 SCFFBXLΒΉβ΅ regulates BMP signalling by directing the degradat... | ACCEPT | Summary: CUL1 is the defining cullin subunit of the SCF (SKP1-CUL1-F-box-RBX1) complex. Reason: Core complex membership, supported structurally (PMID:11961546) and by every reconstituted SCF cited here. Supporting Evidence: PMID:21572392 FBXL15, through its leucine-rich repeat domain, specifically recognizes the large subdomain within the N-lobe of the Smurf1 HECT domain and promotes the ubiquitination of Smurf1 on K355 and K357 file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0019005 SCF ubiquitin ligase complex | IDA PMID:21725316 The SCF-FBXW5 E3-ubiquitin ligase is regulated by PLK4 and t... | ACCEPT | Summary: CUL1 is the defining cullin subunit of the SCF (SKP1-CUL1-F-box-RBX1) complex. Reason: Core complex membership, supported structurally (PMID:11961546) and by every reconstituted SCF cited here. Supporting Evidence: PMID:21725316 We identify the centriolar protein HsSAS-6 (refs 4,5) as a critical substrate of the SCF-FBXW5 complex file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0019005 SCF ubiquitin ligase complex | IDA PMID:23263282 SCFFbxo9 and CK2 direct the cellular response to growth fact... | ACCEPT | Summary: CUL1 is the defining cullin subunit of the SCF (SKP1-CUL1-F-box-RBX1) complex. Reason: Core complex membership, supported structurally (PMID:11961546) and by every reconstituted SCF cited here. Supporting Evidence: PMID:23263282 Tel2 and Tti1 are targeted for degradation within mTORC1 by the SCFFbxo9 ubiquitin ligase to adjust mTOR signalling to growth factor availability file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0019005 SCF ubiquitin ligase complex | IDA PMID:25585578 FBH1 influences DNA replication fork stability and homologou... | ACCEPT | Summary: CUL1 is the defining cullin subunit of the SCF (SKP1-CUL1-F-box-RBX1) complex. Reason: Core complex membership, supported structurally (PMID:11961546) and by every reconstituted SCF cited here. Supporting Evidence: PMID:25585578 the central player in HR, RAD51, is ubiquitylated by the SCF(FBH1) complex file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0019005 SCF ubiquitin ligase complex | IDA PMID:28007894 The pseudophosphatase STYX targets the F-box of FBXW7 and in... | ACCEPT | Summary: CUL1 is the defining cullin subunit of the SCF (SKP1-CUL1-F-box-RBX1) complex. Reason: Core complex membership, supported structurally (PMID:11961546) and by every reconstituted SCF cited here. Supporting Evidence: PMID:28007894 STYX binds to the F-box domain of FBXW7 and disables its recruitment into the SCF complex file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0019005 SCF ubiquitin ligase complex | IDA PMID:31413110 The tumor suppressor FBXO31 preserves genomic integrity by r... | ACCEPT | Summary: CUL1 is the defining cullin subunit of the SCF (SKP1-CUL1-F-box-RBX1) complex. Reason: Core complex membership, supported structurally (PMID:11961546) and by every reconstituted SCF cited here. Supporting Evidence: PMID:31413110 FBXO31 is essential for maintaining optimum expression of the cell-cycle protein cyclin A for efficient cell-cycle progression file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0019005 SCF ubiquitin ligase complex | IEA GO_REF:0000120 | ACCEPT | Summary: CUL1 is the defining cullin subunit of the SCF (SKP1-CUL1-F-box-RBX1) complex. Reason: Core complex membership, supported structurally (PMID:11961546) and by every reconstituted SCF cited here. Supporting Evidence: file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0019005 SCF ubiquitin ligase complex | IPI PMID:11961546 Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin liga... | ACCEPT | Summary: CUL1 is the defining cullin subunit of the SCF (SKP1-CUL1-F-box-RBX1) complex. Reason: Core complex membership, supported structurally (PMID:11961546) and by every reconstituted SCF cited here. Supporting Evidence: PMID:11961546 Cul1 serves as a rigid scaffold that organizes the Skp1-F boxSkp2 and Rbx1 subunits, holding them over 100 A apart file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0019005 SCF ubiquitin ligase complex | IPI PMID:17098746 FBXO11 promotes the Neddylation of p53 and inhibits its tran... | ACCEPT | Summary: CUL1 is the defining cullin subunit of the SCF (SKP1-CUL1-F-box-RBX1) complex. Reason: Core complex membership, supported structurally (PMID:11961546) and by every reconstituted SCF cited here. Supporting Evidence: PMID:17098746 FBXO11, a member of the F-box protein family and a component of the Skp1.Cullin1.F-box (SCF) complex file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0019005 SCF ubiquitin ligase complex | IPI PMID:19762597 An E3 ligase possessing an iron-responsive hemerythrin domai... | ACCEPT | Summary: CUL1 is the defining cullin subunit of the SCF (SKP1-CUL1-F-box-RBX1) complex. Reason: Core complex membership, supported structurally (PMID:11961546) and by every reconstituted SCF cited here. Supporting Evidence: PMID:19762597 an E3 ubiquitin ligase complex containing the FBXL5 protein targets IRP2 for proteasomal degradation file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0019005 SCF ubiquitin ligase complex | IPI PMID:21572392 SCFFBXLΒΉβ΅ regulates BMP signalling by directing the degradat... | ACCEPT | Summary: CUL1 is the defining cullin subunit of the SCF (SKP1-CUL1-F-box-RBX1) complex. Reason: Core complex membership, supported structurally (PMID:11961546) and by every reconstituted SCF cited here. Supporting Evidence: PMID:21572392 FBXL15, through its leucine-rich repeat domain, specifically recognizes the large subdomain within the N-lobe of the Smurf1 HECT domain and promotes the ubiquitination of Smurf1 on K355 and K357 file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0019005 SCF ubiquitin ligase complex | IPI PMID:33692209 KDM2B Overexpression Facilitates Lytic De Novo KSHV Infectio... | ACCEPT | Summary: CUL1 is the defining cullin subunit of the SCF (SKP1-CUL1-F-box-RBX1) complex. Reason: Core complex membership, supported structurally (PMID:11961546) and by every reconstituted SCF cited here. Supporting Evidence: PMID:33692209 This effect is dependent upon the binding of KDM2B to the SKP1-CUL1-F-box (SCF) E3 ubiquitin ligase complex via its F-box domain file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0019005 SCF ubiquitin ligase complex | ISS GO_REF:0000024 | ACCEPT | Summary: CUL1 is the defining cullin subunit of the SCF (SKP1-CUL1-F-box-RBX1) complex. Reason: Core complex membership, supported structurally (PMID:11961546) and by every reconstituted SCF cited here. Supporting Evidence: file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0019005 SCF ubiquitin ligase complex | NAS PMID:15520277 Systematic analysis and nomenclature of mammalian F-box prot... | ACCEPT | Summary: CUL1 is the defining cullin subunit of the SCF (SKP1-CUL1-F-box-RBX1) complex. Reason: Core complex membership, supported structurally (PMID:11961546) and by every reconstituted SCF cited here. Supporting Evidence: PMID:15520277 The CUL1/RBX1 complex functions as a scaffold to assemble the E2 ubiquitin conjugating enzyme with the substrate specificity mod file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0019005 SCF ubiquitin ligase complex | NAS PMID:20498703 Lamin A rod domain mutants target heterochromatin protein 1a... | ACCEPT | Summary: CUL1 is the defining cullin subunit of the SCF (SKP1-CUL1-F-box-RBX1) complex. Reason: Core complex membership, supported structurally (PMID:11961546) and by every reconstituted SCF cited here. Supporting Evidence: PMID:20498703 other members of these complexes such as the cullins, CAND1, RBX1 and SKP1 were also analyzed, but transcript levels of these genes were not significantly affected file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0019005 SCF ubiquitin ligase complex | NAS PMID:20596027 SCF(Cyclin F) controls centrosome homeostasis and mitotic fi... | ACCEPT | Summary: CUL1 is the defining cullin subunit of the SCF (SKP1-CUL1-F-box-RBX1) complex. Reason: Core complex membership, supported structurally (PMID:11961546) and by every reconstituted SCF cited here. Supporting Evidence: PMID:20596027 we identified CP110, a protein that is essential for centrosome duplication, as an interactor and substrate of Cyclin F file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0019005 SCF ubiquitin ligase complex | NAS PMID:26171402 The Human IL-22 Receptor Is Regulated through the Action of ... | ACCEPT | Summary: CUL1 is the defining cullin subunit of the SCF (SKP1-CUL1-F-box-RBX1) complex. Reason: Core complex membership, supported structurally (PMID:11961546) and by every reconstituted SCF cited here. Supporting Evidence: PMID:26171402 in human cells IL-22R is destabilized by FBXW12 file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0019005 SCF ubiquitin ligase complex | NAS PMID:34445249 The SCF Complex Is Essential to Maintain Genome and Chromoso... | ACCEPT | Summary: CUL1 is the defining cullin subunit of the SCF (SKP1-CUL1-F-box-RBX1) complex. Reason: Core complex membership, supported structurally (PMID:11961546) and by every reconstituted SCF 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/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| GO:0019005 SCF ubiquitin ligase complex | NAS PMID:35982156 Structure of CRL7(FBXW8) reveals coupling with CUL1-RBX1/ROC... | ACCEPT | Summary: CUL1 is the defining cullin subunit of the SCF (SKP1-CUL1-F-box-RBX1) complex. Reason: Core complex membership, supported structurally (PMID:11961546) and by every reconstituted SCF cited here. Supporting Evidence: PMID:35982156 our data indicate that CRL7 serves as a substrate receptor linked via SKP1-FBXW8 to a neddylated CUL1-RBX1 catalytic module mediating ubiquitination file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. |
| 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) degrades the HECT ligase Smurf1, thereby positively regulating BMP signalling. Reason: FBXL15-specific pathway output; non-core for the scaffold. Supporting Evidence: PMID:21572392 FBXL15, through its leucine-rich repeat domain, specifically recognizes the large subdomain within the N-lobe of the Smurf1 HECT domain and promotes the ubiquitination of Smurf1 on K355 and K357 |
| GO:0031146 SCF-dependent proteasomal ubiquitin-dependent protein catabolic process | IBA GO_REF:0000033 | ACCEPT | Summary: SCF ligases built on CUL1 target substrates (DEPTOR, IRP2, TFE3/MITF, c-Myc, p27) for proteasomal degradation. Reason: Core process: this is the defining output of the CUL1-scaffolded SCF complex, with direct evidence from multiple receptors. Supporting Evidence: file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| 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 ligases built on CUL1 target substrates (DEPTOR, IRP2, TFE3/MITF, c-Myc, p27) for proteasomal degradation. Reason: Core process: this is the defining output of the CUL1-scaffolded SCF complex, with direct evidence from multiple receptors. Supporting Evidence: PMID:15103331 the F-box protein Fbw7 interacts with and thereby destabilizes c-Myc in a manner dependent on phosphorylation of MB1 file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| 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 ligases built on CUL1 target substrates (DEPTOR, IRP2, TFE3/MITF, c-Myc, p27) for proteasomal degradation. Reason: Core process: this is the defining output of the CUL1-scaffolded SCF complex, with direct evidence from multiple receptors. Supporting Evidence: PMID:19762597 an E3 ubiquitin ligase complex containing the FBXL5 protein targets IRP2 for proteasomal degradation file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| 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 ligases built on CUL1 target substrates (DEPTOR, IRP2, TFE3/MITF, c-Myc, p27) for proteasomal degradation. Reason: Core process: this is the defining output of the CUL1-scaffolded SCF complex, with direct evidence from multiple receptors. Supporting Evidence: PMID:22017875 Here we describe an mTOR-dependent phosphorylation-driven pathway for DEPTOR destruction via SCF(Ξ²TrCP) file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| 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 ligases built on CUL1 target substrates (DEPTOR, IRP2, TFE3/MITF, c-Myc, p27) for proteasomal degradation. Reason: Core process: this is the defining output of the CUL1-scaffolded SCF complex, with direct evidence from multiple receptors. Supporting Evidence: PMID:22017876 DEPTOR is a physiological substrate of SCF(Ξ²TrCP) E3 ligase for targeted degradation file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| 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 ligases built on CUL1 target substrates (DEPTOR, IRP2, TFE3/MITF, c-Myc, p27) for proteasomal degradation. Reason: Core process: this is the defining output of the CUL1-scaffolded SCF complex, with direct evidence from multiple receptors. Supporting Evidence: PMID:36608670 leading to ubiquitination by CUL1Ξ²-TrCP and degradation file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| GO:0031146 SCF-dependent proteasomal ubiquitin-dependent protein catabolic process | IEA GO_REF:0000120 | ACCEPT | Summary: SCF ligases built on CUL1 target substrates (DEPTOR, IRP2, TFE3/MITF, c-Myc, p27) for proteasomal degradation. Reason: Core process: this is the defining output of the CUL1-scaffolded SCF complex, with direct evidence from multiple receptors. Supporting Evidence: file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| GO:0031146 SCF-dependent proteasomal ubiquitin-dependent protein catabolic process | ISS GO_REF:0000024 | ACCEPT | Summary: SCF ligases built on CUL1 target substrates (DEPTOR, IRP2, TFE3/MITF, c-Myc, p27) for proteasomal degradation. Reason: Core process: this is the defining output of the CUL1-scaffolded SCF complex, with direct evidence from multiple receptors. Supporting Evidence: file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| 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 ligases built on CUL1 target substrates (DEPTOR, IRP2, TFE3/MITF, c-Myc, p27) for proteasomal degradation. Reason: Core process: this is the defining output of the CUL1-scaffolded SCF complex, with direct evidence from multiple receptors. Supporting Evidence: PMID:11961546 Cul1 serves as a rigid scaffold that organizes the Skp1-F boxSkp2 and Rbx1 subunits, holding them over 100 A apart file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| 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 ligases built on CUL1 target substrates (DEPTOR, IRP2, TFE3/MITF, c-Myc, p27) for proteasomal degradation. Reason: Core process: this is the defining output of the CUL1-scaffolded SCF complex, with direct evidence from multiple receptors. Supporting Evidence: PMID:15520277 The CUL1/RBX1 complex functions as a scaffold to assemble the E2 ubiquitin conjugating enzyme with the substrate specificity mod file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| 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 ligases built on CUL1 target substrates (DEPTOR, IRP2, TFE3/MITF, c-Myc, p27) for proteasomal degradation. Reason: Core process: this is the defining output of the CUL1-scaffolded SCF complex, with direct evidence from multiple receptors. Supporting Evidence: PMID:20498703 other members of these complexes such as the cullins, CAND1, RBX1 and SKP1 were also analyzed, but transcript levels of these genes were not significantly affected file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| 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 ligases built on CUL1 target substrates (DEPTOR, IRP2, TFE3/MITF, c-Myc, p27) for proteasomal degradation. Reason: Core process: this is the defining output of the CUL1-scaffolded SCF complex, with direct evidence from multiple receptors. Supporting Evidence: PMID:20596027 we identified CP110, a protein that is essential for centrosome duplication, as an interactor and substrate of Cyclin F file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| GO:0031146 SCF-dependent proteasomal ubiquitin-dependent protein catabolic process | NAS PMID:21572392 SCFFBXLΒΉβ΅ regulates BMP signalling by directing the degradat... | ACCEPT | Summary: SCF ligases built on CUL1 target substrates (DEPTOR, IRP2, TFE3/MITF, c-Myc, p27) for proteasomal degradation. Reason: Core process: this is the defining output of the CUL1-scaffolded SCF complex, with direct evidence from multiple receptors. Supporting Evidence: PMID:21572392 FBXL15, through its leucine-rich repeat domain, specifically recognizes the large subdomain within the N-lobe of the Smurf1 HECT domain and promotes the ubiquitination of Smurf1 on K355 and K357 file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| 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 ligases built on CUL1 target substrates (DEPTOR, IRP2, TFE3/MITF, c-Myc, p27) for proteasomal degradation. Reason: Core process: this is the defining output of the CUL1-scaffolded SCF complex, with direct evidence from multiple receptors. Supporting Evidence: PMID:26171402 in human cells IL-22R is destabilized by FBXW12 file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| 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 ligases built on CUL1 target substrates (DEPTOR, IRP2, TFE3/MITF, c-Myc, p27) for proteasomal degradation. Reason: Core process: this is the defining output of the CUL1-scaffolded SCF complex, with direct evidence from multiple receptors. Supporting Evidence: PMID:33234069 F-box proteins (FBPs) are substrate-recruiting subunits of Skp1-cullin1-FBP (SCF)-type E3 ubiquitin ligases that determine which proteins are ubiquitinated file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| 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 ligases built on CUL1 target substrates (DEPTOR, IRP2, TFE3/MITF, c-Myc, p27) for proteasomal degradation. Reason: Core process: this is the defining output of the CUL1-scaffolded SCF complex, with direct evidence from multiple receptors. 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/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| 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 ligases built on CUL1 target substrates (DEPTOR, IRP2, TFE3/MITF, c-Myc, p27) for proteasomal degradation. Reason: Core process: this is the defining output of the CUL1-scaffolded SCF complex, with direct evidence from multiple receptors. Supporting Evidence: PMID:35982156 our data indicate that CRL7 serves as a substrate receptor linked via SKP1-FBXW8 to a neddylated CUL1-RBX1 catalytic module mediating ubiquitination file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| GO:0031461 cullin-RING ubiquitin ligase complex | IDA PMID:22405651 The glomuvenous malformation protein Glomulin binds Rbx1 and... | ACCEPT | Summary: CUL1-RBX1 is the catalytic core of a cullin-RING ligase (CRL1); Glomulin binds the RBX1 RING in this core. Reason: Correct parent of SCF complex; the CUL1-RBX1 core also serves the CUL7-FBXW8 assembly (PMID:35982156). Supporting Evidence: PMID:22405651 binds directly to the RING domain of Rbx1 and inhibits its E3 ubiquitin ligase activity file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| GO:0031461 cullin-RING ubiquitin ligase complex | IEA GO_REF:0000002 | ACCEPT | Summary: CUL1-RBX1 is the catalytic core of a cullin-RING ligase (CRL1); Glomulin binds the RBX1 RING in this core. Reason: Correct parent of SCF complex; the CUL1-RBX1 core also serves the CUL7-FBXW8 assembly (PMID:35982156). Supporting Evidence: file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| GO:0031625 ubiquitin protein ligase binding | IBA GO_REF:0000033 | ACCEPT | Summary: CUL1 binds the RING E3 RBX1 through an intermolecular beta-sheet and, when neddylated, the RBR E3 ARIH1. Reason: True and inherited across cullins (PAINT); binding to the RING ligase RBX1 is intrinsic to the scaffold role and neddylated CUL1-RBX1 additionally activates ARIH1 (PMID:24076655). Supporting Evidence: file:human/CUL1/CUL1-uniprot.txt SCF complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins |
| GO:0031625 ubiquitin protein ligase binding | IDA PMID:11961546 Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin liga... | ACCEPT | Summary: CUL1 binds the RING E3 RBX1 through an intermolecular beta-sheet and, when neddylated, the RBR E3 ARIH1. Reason: True and inherited across cullins (PAINT); binding to the RING ligase RBX1 is intrinsic to the scaffold role and neddylated CUL1-RBX1 additionally activates ARIH1 (PMID:24076655). Supporting Evidence: PMID:11961546 Cul1 serves as a rigid scaffold that organizes the Skp1-F boxSkp2 and Rbx1 subunits, holding them over 100 A apart file:human/CUL1/CUL1-uniprot.txt SCF complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins |
| GO:0031625 ubiquitin protein ligase binding | IEA GO_REF:0000002 | ACCEPT | Summary: CUL1 binds the RING E3 RBX1 through an intermolecular beta-sheet and, when neddylated, the RBR E3 ARIH1. Reason: True and inherited across cullins (PAINT); binding to the RING ligase RBX1 is intrinsic to the scaffold role and neddylated CUL1-RBX1 additionally activates ARIH1 (PMID:24076655). Supporting Evidence: file:human/CUL1/CUL1-uniprot.txt SCF complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins |
| 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) degrades TEL2/TTI1 within mTORC1 after growth-factor withdrawal; SCF(beta-TrCP) degrades DEPTOR. Reason: Receptor-specific (FBXO9, beta-TrCP) regulatory outputs of the scaffold; non-core. Supporting Evidence: PMID:23263282 Tel2 and Tti1 are targeted for degradation within mTORC1 by the SCFFbxo9 ubiquitin ligase to adjust mTOR signalling to growth factor availability PMID:22017875 Here we describe an mTOR-dependent phosphorylation-driven pathway for DEPTOR destruction via SCF(Ξ²TrCP) |
| 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: SCF(FBXO31) reads C-terminal amides on chemically damaged proteins and degrades them. Reason: Direct (IDA) evidence for an SCF(FBXO31) role; the oxidative-stress response is an FBXO31-specific output of the scaffold, so non-core. Supporting Evidence: PMID:39880951 A CRISPR screen identified FBXO31 as a reader of C-terminal amides file:human/CUL1/CUL1-uniprot.txt The SCF(FBXO31) protein ligase complex specifically mediates the ubiquitination of proteins amidated at their C-terminus in response to oxidative stress |
| 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) ubiquitinate CRY1/2, setting circadian period. Reason: FBXL3/FBXL21-specific output of the scaffold; non-core. Supporting Evidence: PMID:17463251 both Cry1 and Cry2 proteins are ubiquitinated and degraded via the SCF(Fbxl3) ubiquitin ligase complex |
| 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) ubiquitinate CRY1/2, setting circadian period. Reason: FBXL3/FBXL21-specific output of the scaffold; non-core. Supporting Evidence: PMID:23452855 FBXL21 forms an SCF E3 ligase complex that slowly degrades CRY in the cytoplasm but antagonizes the stronger E3 ligase activity of FBXL3 in the nucleus |
| GO:0042981 regulation of apoptotic process | NAS PMID:25654763 F-box protein Fbxl18 mediates polyubiquitylation and proteas... | MARK AS OVER ANNOTATED | Summary: SCF(FBXL18) degrades the pro-apoptotic F-box protein FBXL7. Reason: The regulatory effect on apoptosis is two steps removed (FBXL18 degrades FBXL7, whose overexpression is pro-apoptotic); too indirect and broad for CUL1 (NAS). Supporting Evidence: PMID:25654763 an orphan F-box protein, Fbxl18, targets Fbxl7 for its polyubiquitylation and proteasomal degradation |
| 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) ubiquitinates phospho-IkappaB-alpha, releasing NF-kappaB. Reason: Direct evidence that the CUL1-containing SCF(beta-TrCP) performs the IkappaB-alpha ubiquitination that activates NF-kappaB; a receptor-specific pathway output, so non-core. Supporting Evidence: PMID:10644755 deletion mutants of betaTrCP1 and betaTrCP2 lacking the F-box domain suppressed ubiquitination and destruction of pIkappaBalpha as well as transcriptional activation of NF-kappaB |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IDA PMID:10644755 Homodimer of two F-box proteins betaTrCP1 or betaTrCP2 binds... | ACCEPT | Summary: CUL1-scaffolded SCF ligases (beta-TrCP, FBXO7, FBXO9, FBXO31) direct substrates to the proteasome. Reason: Core process; direct evidence for multiple receptors. Redundant with, but not wrong relative to, GO:0031146. Supporting Evidence: PMID:10644755 deletion mutants of betaTrCP1 and betaTrCP2 lacking the F-box domain suppressed ubiquitination and destruction of pIkappaBalpha as well as transcriptional activation of NF-kappaB file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IDA PMID:15145941 Fbx7 functions in the SCF complex regulating Cdk1-cyclin B-p... | ACCEPT | Summary: CUL1-scaffolded SCF ligases (beta-TrCP, FBXO7, FBXO9, FBXO31) direct substrates to the proteasome. Reason: Core process; direct evidence for multiple receptors. Redundant with, but not wrong relative to, GO:0031146. Supporting Evidence: PMID:15145941 In the SCF(Fbx7) complex, Fbx7 recruits HURP through its C-terminal proline-rich region in a Cdk1-cyclin B-phosphorylation dependent manner file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IDA PMID:34480022 Endotoxin stabilizes protein arginine methyltransferase 4 (P... | ACCEPT | Summary: CUL1-scaffolded SCF ligases (beta-TrCP, FBXO7, FBXO9, FBXO31) direct substrates to the proteasome. Reason: Core process; direct evidence for multiple receptors. Redundant with, but not wrong relative to, GO:0031146. Supporting Evidence: PMID:34480022 PRMT4 is normally targeted for its degradation by an E3 ubiquitin ligase, SCFFBXO9, that interacts with PRMT4 via a phosphodegron to ubiquitinate the chromatin modulator at K228 file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IDA PMID:39880951 C-terminal amides mark proteins for degradation via SCF-FBXO... | ACCEPT | Summary: CUL1-scaffolded SCF ligases (beta-TrCP, FBXO7, FBXO9, FBXO31) direct substrates to the proteasome. Reason: Core process; direct evidence for multiple receptors. Redundant with, but not wrong relative to, GO:0031146. Supporting Evidence: PMID:39880951 A CRISPR screen identified FBXO31 as a reader of C-terminal amides file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| 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) degrades FBXL2, stabilizing TRAF proteins and driving cytokine secretion. Reason: FBXO3-specific output (NAS); non-core. Supporting Evidence: PMID:23542741 a ubiquitin E3 ligase component, Fbxo3, potently stimulates cytokine secretion from human inflammatory cells by destabilizing a sentinel TRAF inhibitor, Fbxl2 |
| 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) degrades FBXL2, stabilizing TRAF proteins and driving cytokine secretion. Reason: FBXO3-specific output (NAS); non-core. Supporting Evidence: PMID:35127719 we focus on the role of FBXO3 in inflammatory disorders and human malignancies |
| GO:0051298 centrosome duplication | NAS PMID:34388369 Structure of the human signal peptidase complex reveals the ... | MODIFY | Summary: SCF(FBXW5) degrades SAS-6 and SCF(cyclin F) degrades CP110 to restrain centrosome duplication; the cited reference, however, is the signal peptidase complex structure. Reason: PMID:34388369 describes the ER signal peptidase complex and does not concern CUL1 (wrong identifier). The real evidence (PMID:21725316, PMID:20596027) shows SCF ligases degrading duplication factors, i.e. regulation of centrosome duplication (GO:0010824, already annotated) rather than execution of duplication. Proposed replacements: regulation of centrosome duplication Supporting Evidence: PMID:21725316 We identify the centriolar protein HsSAS-6 (refs 4,5) as a critical substrate of the SCF-FBXW5 complex PMID:20596027 we identified CP110, a protein that is essential for centrosome duplication, as an interactor and substrate of Cyclin F |
| GO:0051726 regulation of cell cycle | NAS PMID:33234069 The FBXL family of F-box proteins: variations on a theme. | KEEP AS NON CORE | Summary: Review of FBXL-family SCF ligases and their cell-cycle substrates. Reason: Correct but general (NAS from a review); the specific core process is G1/S transition. Supporting Evidence: PMID:33234069 F-box proteins (FBPs) are substrate-recruiting subunits of Skp1-cullin1-FBP (SCF)-type E3 ubiquitin ligases that determine which proteins are ubiquitinated |
| GO:0060173 limb development | NAS PMID:10471509 A novel member of the F-box/WD40 gene family, encoding dacty... | MARK AS OVER ANNOTATED | Summary: The mouse dactylaplasia locus encodes the F-box/WD40 protein dactylin (Fbxw4). Reason: A mouse limb phenotype of an F-box gene with no CUL1 data; limb development is a developmental phenotype far downstream of the scaffold (NAS). Supporting Evidence: PMID:10471509 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 |
| GO:0060271 cilium assembly | NAS PMID:34368969 SCF(Fbxw5) targets kinesin-13 proteins to facilitate cilioge... | MODIFY | Summary: SCF(Fbxw5) degrades the kinesin-13 MCAK in G2, permitting ciliogenesis in the next G1/G0. Reason: The ligase does not build the cilium; it removes a depolymerase whose excess blocks ciliogenesis. A regulation term fits the evidence better. Proposed replacements: regulation of cilium assembly Supporting Evidence: PMID:34368969 MCAK and its closely related orthologs Kif2a and Kif2b become efficiently polyubiquitylated by neddylated SCFFbxw5 and Cdc34 |
| GO:0070936 protein K48-linked ubiquitination | IDA PMID:15145941 Fbx7 functions in the SCF complex regulating Cdk1-cyclin B-p... | ACCEPT | Summary: SCF complexes on CUL1 build K48-linked chains for proteasomal targeting (HURP, TEL2/TTI1). Reason: Core chain type of SCF-mediated degradative ubiquitination. Supporting Evidence: PMID:15145941 In the SCF(Fbx7) complex, Fbx7 recruits HURP through its C-terminal proline-rich region in a Cdk1-cyclin B-phosphorylation dependent manner file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| GO:0070936 protein K48-linked ubiquitination | IDA PMID:23263282 SCFFbxo9 and CK2 direct the cellular response to growth fact... | ACCEPT | Summary: SCF complexes on CUL1 build K48-linked chains for proteasomal targeting (HURP, TEL2/TTI1). Reason: Core chain type of SCF-mediated degradative ubiquitination. Supporting Evidence: PMID:23263282 Tel2 and Tti1 are targeted for degradation within mTORC1 by the SCFFbxo9 ubiquitin ligase to adjust mTOR signalling to growth factor availability file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| GO:0070936 protein K48-linked ubiquitination | IEA GO_REF:0000117 | ACCEPT | Summary: SCF complexes on CUL1 build K48-linked chains for proteasomal targeting (HURP, TEL2/TTI1). Reason: Core chain type of SCF-mediated degradative ubiquitination. Supporting Evidence: file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| GO:0097193 intrinsic apoptotic signaling pathway | IEA GO_REF:0000117 | MARK AS OVER ANNOTATED | Summary: C. elegans cul-1 mutants show hyperplasia and fail programmed G1-to-G0/apoptotic transitions. Reason: The worm phenotype (and the ARBA rule derived from it) reflects failed cell-cycle exit, not participation of CUL1 in the intrinsic apoptotic signaling cascade; over-annotation. Supporting Evidence: file:human/CUL1/CUL1-deep-research-falcon.md Substrate specificity belongs primarily to the associated F-box receptor. |
| GO:0097193 intrinsic apoptotic signaling pathway | TAS PMID:8681378 cul-1 is required for cell cycle exit in C. elegans and iden... | MARK AS OVER ANNOTATED | Summary: C. elegans cul-1 mutants show hyperplasia and fail programmed G1-to-G0/apoptotic transitions. Reason: The worm phenotype (and the ARBA rule derived from it) reflects failed cell-cycle exit, not participation of CUL1 in the intrinsic apoptotic signaling cascade; over-annotation. Supporting Evidence: PMID:8681378 cul-1 is required for developmentally programmed transitions from the G1 phase of the cell cycle to the GO phase or the apoptotic pathway file:human/CUL1/CUL1-deep-research-falcon.md Substrate specificity belongs primarily to the associated F-box receptor. |
| GO:0160072 ubiquitin ligase complex scaffold activity | IBA GO_REF:0000033 | ACCEPT | Summary: CUL1 is the rigid scaffold that joins the SKP1/F-box substrate receptor to the RBX1 RING/E2 module in SCF ligases. Reason: Core molecular function, inherited across the cullin family (PAINT) and shown directly by structure and reconstitution. Supporting Evidence: file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| GO:0160072 ubiquitin ligase complex scaffold activity | IDA PMID:10644755 Homodimer of two F-box proteins betaTrCP1 or betaTrCP2 binds... | ACCEPT | Summary: CUL1 is the rigid scaffold that joins the SKP1/F-box substrate receptor to the RBX1 RING/E2 module in SCF ligases. Reason: Core molecular function, inherited across the cullin family (PAINT) and shown directly by structure and reconstitution. Supporting Evidence: PMID:10644755 deletion mutants of betaTrCP1 and betaTrCP2 lacking the F-box domain suppressed ubiquitination and destruction of pIkappaBalpha as well as transcriptional activation of NF-kappaB file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| GO:0160072 ubiquitin ligase complex scaffold activity | IDA PMID:15145941 Fbx7 functions in the SCF complex regulating Cdk1-cyclin B-p... | ACCEPT | Summary: CUL1 is the rigid scaffold that joins the SKP1/F-box substrate receptor to the RBX1 RING/E2 module in SCF ligases. Reason: Core molecular function, inherited across the cullin family (PAINT) and shown directly by structure and reconstitution. Supporting Evidence: PMID:15145941 In the SCF(Fbx7) complex, Fbx7 recruits HURP through its C-terminal proline-rich region in a Cdk1-cyclin B-phosphorylation dependent manner file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| GO:0160072 ubiquitin ligase complex scaffold activity | IDA PMID:22017875 mTOR drives its own activation via SCF(Ξ²TrCP)-dependent degr... | ACCEPT | Summary: CUL1 is the rigid scaffold that joins the SKP1/F-box substrate receptor to the RBX1 RING/E2 module in SCF ligases. Reason: Core molecular function, inherited across the cullin family (PAINT) and shown directly by structure and reconstitution. Supporting Evidence: PMID:22017875 Here we describe an mTOR-dependent phosphorylation-driven pathway for DEPTOR destruction via SCF(Ξ²TrCP) file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| GO:0160072 ubiquitin ligase complex scaffold activity | IDA PMID:22017876 DEPTOR, an mTOR inhibitor, is a physiological substrate of S... | ACCEPT | Summary: CUL1 is the rigid scaffold that joins the SKP1/F-box substrate receptor to the RBX1 RING/E2 module in SCF ligases. Reason: Core molecular function, inherited across the cullin family (PAINT) and shown directly by structure and reconstitution. Supporting Evidence: PMID:22017876 DEPTOR is a physiological substrate of SCF(Ξ²TrCP) E3 ligase for targeted degradation file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| GO:0160072 ubiquitin ligase complex scaffold activity | IDA PMID:23263282 SCFFbxo9 and CK2 direct the cellular response to growth fact... | ACCEPT | Summary: CUL1 is the rigid scaffold that joins the SKP1/F-box substrate receptor to the RBX1 RING/E2 module in SCF ligases. Reason: Core molecular function, inherited across the cullin family (PAINT) and shown directly by structure and reconstitution. Supporting Evidence: PMID:23263282 Tel2 and Tti1 are targeted for degradation within mTORC1 by the SCFFbxo9 ubiquitin ligase to adjust mTOR signalling to growth factor availability file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| GO:0160072 ubiquitin ligase complex scaffold activity | IDA PMID:36608670 A central role for regulated protein stability in the contro... | ACCEPT | Summary: CUL1 is the rigid scaffold that joins the SKP1/F-box substrate receptor to the RBX1 RING/E2 module in SCF ligases. Reason: Core molecular function, inherited across the cullin family (PAINT) and shown directly by structure and reconstitution. Supporting Evidence: PMID:36608670 leading to ubiquitination by CUL1Ξ²-TrCP and degradation file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| GO:0160072 ubiquitin ligase complex scaffold activity | IDA PMID:39880951 C-terminal amides mark proteins for degradation via SCF-FBXO... | ACCEPT | Summary: CUL1 is the rigid scaffold that joins the SKP1/F-box substrate receptor to the RBX1 RING/E2 module in SCF ligases. Reason: Core molecular function, inherited across the cullin family (PAINT) and shown directly by structure and reconstitution. Supporting Evidence: PMID:39880951 A CRISPR screen identified FBXO31 as a reader of C-terminal amides file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| GO:0160072 ubiquitin ligase complex scaffold activity | IEA GO_REF:0000117 | ACCEPT | Summary: CUL1 is the rigid scaffold that joins the SKP1/F-box substrate receptor to the RBX1 RING/E2 module in SCF ligases. Reason: Core molecular function, inherited across the cullin family (PAINT) and shown directly by structure and reconstitution. Supporting Evidence: file:human/CUL1/CUL1-uniprot.txt In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. file:human/CUL1/CUL1-deep-research-falcon.md CUL1 is a regulated molecular scaffold and catalytic organizer for SCF/CRL1 E3 ubiquitin ligases, bringing F-box-bound substrates near RBX1-associated ubiquitin-transfer machinery to control proteolysis and other ubiquitin signals. |
| GO:1901524 regulation of mitophagy | NAS PMID:36135912 Mitochondrial Fission and Fusion: Molecular Mechanisms, Biol... | KEEP AS NON CORE | Summary: SCF(FBXL4) at the outer mitochondrial membrane degrades the mitophagy receptors NIX and BNIP3. Reason: The cited review only lists FBXL4; the primary evidence (Nguyen-Dien 2023, summarised in the deep research) supports an FBXL4-specific output. Non-core. Supporting Evidence: PMID:36135912 mitochondrial disorders caused by defects in fission and fusion are summarized, including disorders related to MFN2, MSTO1, OPA1, YME1L1, FBXL4, DNM1L, and MFF genes file:human/CUL1/CUL1-deep-research-falcon.md Under unstressed conditions, the complex constitutively ubiquitylates and destabilizes these mitophagy receptors, thereby restraining basal mitophagy. |
| GO:1904415 regulation of xenophagy | NAS PMID:34515398 FBXO2/SCF ubiquitin ligase complex directs xenophagy through... | KEEP AS NON CORE | Summary: SCF(FBXO2) recognises GlcNAc on group A Streptococcus and ubiquitinates it for xenophagy; SKP1, CUL1 and ROC1 are required. Reason: FBXO2-specific output with direct evidence for CUL1 requirement; non-core. Supporting Evidence: PMID:34515398 SCF components such as SKP1, CUL1, and ROC1 are required for ubiquitin-mediated xenophagy against GAS |
| GO:1990452 Parkin-FBXW7-Cul1 ubiquitin ligase complex | IPI PMID:12628165 Parkin is a component of an SCF-like ubiquitin ligase comple... | KEEP AS NON CORE | Summary: Parkin was reported to function in an SCF-like complex with hSel-10/FBXW7 and Cullin-1 targeting cyclin E in neurons. Reason: Single-study (abstract-only) complex; consistent in principle with neddylated CUL1 activating RBR ligases, but not independently reproduced. Kept as non-core; flagged for expert review. Supporting Evidence: PMID:12628165 parkin functions in a multiprotein ubiquitin ligase complex that includes the F-box/WD repeat protein hSel-10 and Cullin-1 PMID:24076655 binding of the cognate neddylated CRL to TRIAD1 or HHARI greatly stimulates RBR ligase activity in vitro |
| 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(FBX4) mediates rapid cyclin D1 proteolysis after DNA damage. Reason: FBXO4-specific output (NAS); non-core. Supporting Evidence: PMID:33784509 rapid reduction of cyclin D1 upon DNA damage was attributed to proteasomal degradation |
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Download this section (compressed HTML)Q: Should the ~140 GO:0005515 rows recording CUL1 with individual F-box proteins and SCF substrates be re-curated in GO-CAM as has_input/has_output relations on the receptor and RBX1 activities, rather than as bare protein-binding annotations on the shared scaffold?
Q: Is GO:1990452 Parkin-FBXW7-Cul1 ubiquitin ligase complex still supported by evidence beyond the single 2003 report, given that neddylated CUL1-RBX1 activates RBR ligases such as ARIH1 rather than parkin in later reconstitutions?
Q: Which of the receptor-specific pathway outputs (circadian rhythm, iron homeostasis, TOR, BMP, mitophagy, xenophagy, centrosome duplication) should be annotated to CUL1 at all, versus only to the F-box receptor, when the scaffold is shared by all ~70 SCF ligases?
Experiment: Rescue CUL1-depleted human cells with canyon charge-reversal mutants and measure chain length and degradation kinetics of SKP2, beta-TrCP and FBXW7 substrates by ubiquitin-remnant proteomics and cycloheximide chase.
Hypothesis: The CUL1 basic canyon that binds the CDC34 acidic tail is required for processive K48 chain synthesis by all SCF ligases regardless of receptor.
Type: structure-guided mutational rescue with ubiquitination kinetics
Experiment: Compare substrate ubiquitination and turnover in ARIH1-null cells reconstituted with a CRL-binding-deficient ARIH1 allele against CUL1 K720R cells, using SCF(beta-TrCP) and SCF(FBXW7) substrates as readouts.
Hypothesis: Neddylated CUL1-RBX1 activation of ARIH1 is required in vivo for priming of a defined subset of SCF substrates.
Type: genetic separation of tandem E3 activity
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