EBF1 (EIN3-BINDING F-BOX PROTEIN 1, At2g25490) is a leucine-rich-repeat F-box protein that serves as the substrate-recognition subunit of an SCF (SKP1-CUL1-F-box) E3 ubiquitin ligase. Through its N-terminal F-box it binds the SKP1-like proteins ASK1/ASK2 and thereby CUL1, and through its LRR domain it binds the EIN3/EIL family transcription factors EIN3 and EIL1, directing their ubiquitination and proteasomal degradation. In the absence of ethylene, SCF(EBF1) and its paralog SCF(EBF2) keep EIN3/EIL1 levels low; ebf1 mutants are ethylene-hypersensitive, ebf1 ebf2 double mutants show a constitutive ethylene response and growth arrest, and EBF1 overexpression confers ethylene insensitivity. Ethylene signalling via EIN2 down-regulates EBF1/EBF2, both by promoting proteasomal turnover of the EBF proteins and by EIN2-directed translational repression of EBF1/EBF2 mRNA through their 3' UTRs, so that EIN3/EIL1 accumulate in the nucleus. EBF1 is the predominant regulator during ethylene-free growth and early responses, whereas EIN3-induced EBF2 acts more in feedback and recovery. EBF1 localizes to the nucleus and cytoplasm.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005515 protein binding | IPI PMID:12169662 The F-box subunit of the SCF E3 complex is encoded by a dive... | MODIFY | Summary: EBF1 interacts with the SCF core subunit ASK11 (PMID:12169662), which is how the F-box protein is assembled into the SCF(EBF1) E3 ligase. Reason: Protein binding is uninformative; binding of the ligase core via the F-box together with substrate recruitment constitutes the adaptor activity of an F-box subunit (membership of the SCF complex is captured by GO:0019005). Proposed replacements: ubiquitin-like ligase-substrate adaptor activity Supporting Evidence: PMID:15090654 two F-box proteins, EBF1 and -2, that work coordinately in SCF complexes to repress ethylene action |
| GO:0005515 protein binding | IPI PMID:12169662 The F-box subunit of the SCF E3 complex is encoded by a dive... | MODIFY | Summary: EBF1 interacts with the SCF core subunit ASK1/SKP1A (PMID:12169662), which is how the F-box protein is assembled into the SCF(EBF1) E3 ligase. Reason: Protein binding is uninformative; binding of the ligase core via the F-box together with substrate recruitment constitutes the adaptor activity of an F-box subunit (membership of the SCF complex is captured by GO:0019005). Proposed replacements: ubiquitin-like ligase-substrate adaptor activity Supporting Evidence: PMID:15090654 two F-box proteins, EBF1 and -2, that work coordinately in SCF complexes to repress ethylene action |
| GO:0005515 protein binding | IPI PMID:12169662 The F-box subunit of the SCF E3 complex is encoded by a dive... | MODIFY | Summary: EBF1 interacts with the SCF core subunit ASK2/SKP1B (PMID:12169662), which is how the F-box protein is assembled into the SCF(EBF1) E3 ligase. Reason: Protein binding is uninformative; binding of the ligase core via the F-box together with substrate recruitment constitutes the adaptor activity of an F-box subunit (membership of the SCF complex is captured by GO:0019005). Proposed replacements: ubiquitin-like ligase-substrate adaptor activity Supporting Evidence: PMID:15090654 two F-box proteins, EBF1 and -2, that work coordinately in SCF complexes to repress ethylene action |
| GO:0005515 protein binding | IPI PMID:14675532 Plant responses to ethylene gas are mediated by SCF(EBF1/EBF... | MODIFY | Summary: EBF1 binds its ubiquitination substrate EIN3 (PMID:14675532); this substrate recognition is the core function of the F-box protein in SCF(EBF1). Reason: Protein binding is uninformative; the substrate-recruiting activity of an F-box subunit is captured by ubiquitin-like ligase-substrate adaptor activity. Proposed replacements: ubiquitin-like ligase-substrate adaptor activity Supporting Evidence: PMID:14675533 we identify two Arabidopsis F box proteins called EBF1 and EBF2 that interact physically with EIN3/EIL transcription factors PMID:14675532 In the absence of ethylene, EIN3 is quickly degraded through a ubiquitin/proteasome pathway mediated by two F box proteins, EBF1 and EBF2. |
| GO:0005515 protein binding | IPI PMID:14675532 Plant responses to ethylene gas are mediated by SCF(EBF1/EBF... | MODIFY | Summary: EBF1 binds its ubiquitination substrate EIN3 (PMID:14675532); this substrate recognition is the core function of the F-box protein in SCF(EBF1). Reason: Protein binding is uninformative; the substrate-recruiting activity of an F-box subunit is captured by ubiquitin-like ligase-substrate adaptor activity. Proposed replacements: ubiquitin-like ligase-substrate adaptor activity Supporting Evidence: PMID:14675533 we identify two Arabidopsis F box proteins called EBF1 and EBF2 that interact physically with EIN3/EIL transcription factors PMID:14675532 In the absence of ethylene, EIN3 is quickly degraded through a ubiquitin/proteasome pathway mediated by two F box proteins, EBF1 and EBF2. |
| GO:0005515 protein binding | IPI PMID:14675532 Plant responses to ethylene gas are mediated by SCF(EBF1/EBF... | REMOVE | Summary: The interactor is recorded as P43291 (SRK2A/SnRK2.4), whose UniProt synonyms include 'ASK1'. The Cell 2003 EBF1 papers study EBF1 binding to the SKP1-like ASK1 (SKP1A, Q39255) as part of SCF assembly; the SnRK2 kinase is not discussed in the abstracts, so this row may reflect an identifier mapping between the two 'ASK1' names. Reason: Protein binding is uninformative regardless of partner; removal does not mean an interaction is false. The likely intended SKP1A interaction is covered by the SCF complex and adaptor activity annotations. Interactor identity should be checked by the source curators. Supporting Evidence: PMID:14675533 we identify two Arabidopsis F box proteins called EBF1 and EBF2 that interact physically with EIN3/EIL transcription factors |
| GO:0005515 protein binding | IPI PMID:14675533 EIN3-dependent regulation of plant ethylene hormone signalin... | MODIFY | Summary: EBF1 binds its ubiquitination substrate EIN3 (PMID:14675533); this substrate recognition is the core function of the F-box protein in SCF(EBF1). Reason: Protein binding is uninformative; the substrate-recruiting activity of an F-box subunit is captured by ubiquitin-like ligase-substrate adaptor activity. Proposed replacements: ubiquitin-like ligase-substrate adaptor activity Supporting Evidence: PMID:14675533 we identify two Arabidopsis F box proteins called EBF1 and EBF2 that interact physically with EIN3/EIL transcription factors PMID:14675532 In the absence of ethylene, EIN3 is quickly degraded through a ubiquitin/proteasome pathway mediated by two F box proteins, EBF1 and EBF2. |
| GO:0005515 protein binding | IPI PMID:14675533 EIN3-dependent regulation of plant ethylene hormone signalin... | REMOVE | Summary: The interactor is recorded as P43291 (SRK2A/SnRK2.4), whose UniProt synonyms include 'ASK1'. The Cell 2003 EBF1 papers study EBF1 binding to the SKP1-like ASK1 (SKP1A, Q39255) as part of SCF assembly; the SnRK2 kinase is not discussed in the abstracts, so this row may reflect an identifier mapping between the two 'ASK1' names. Reason: Protein binding is uninformative regardless of partner; removal does not mean an interaction is false. The likely intended SKP1A interaction is covered by the SCF complex and adaptor activity annotations. Interactor identity should be checked by the source curators. Supporting Evidence: PMID:14675533 we identify two Arabidopsis F box proteins called EBF1 and EBF2 that interact physically with EIN3/EIL transcription factors |
| GO:0005515 protein binding | IPI PMID:14675533 EIN3-dependent regulation of plant ethylene hormone signalin... | MODIFY | Summary: EBF1 interacts with the SCF core subunit ASK1/SKP1A (PMID:14675533), which is how the F-box protein is assembled into the SCF(EBF1) E3 ligase. Reason: Protein binding is uninformative; binding of the ligase core via the F-box together with substrate recruitment constitutes the adaptor activity of an F-box subunit (membership of the SCF complex is captured by GO:0019005). Proposed replacements: ubiquitin-like ligase-substrate adaptor activity Supporting Evidence: PMID:15090654 two F-box proteins, EBF1 and -2, that work coordinately in SCF complexes to repress ethylene action |
| GO:0005515 protein binding | IPI PMID:14675533 EIN3-dependent regulation of plant ethylene hormone signalin... | MODIFY | Summary: EBF1 interacts with the SCF core subunit CUL1 (PMID:14675533), which is how the F-box protein is assembled into the SCF(EBF1) E3 ligase. Reason: Protein binding is uninformative; binding of the ligase core via the F-box together with substrate recruitment constitutes the adaptor activity of an F-box subunit (membership of the SCF complex is captured by GO:0019005). Proposed replacements: ubiquitin-like ligase-substrate adaptor activity Supporting Evidence: PMID:15090654 two F-box proteins, EBF1 and -2, that work coordinately in SCF complexes to repress ethylene action |
| GO:0005515 protein binding | IPI PMID:14675533 EIN3-dependent regulation of plant ethylene hormone signalin... | MODIFY | Summary: EBF1 interacts with the SCF core subunit ASK2/SKP1B (PMID:14675533), which is how the F-box protein is assembled into the SCF(EBF1) E3 ligase. Reason: Protein binding is uninformative; binding of the ligase core via the F-box together with substrate recruitment constitutes the adaptor activity of an F-box subunit (membership of the SCF complex is captured by GO:0019005). Proposed replacements: ubiquitin-like ligase-substrate adaptor activity Supporting Evidence: PMID:15090654 two F-box proteins, EBF1 and -2, that work coordinately in SCF complexes to repress ethylene action |
| GO:0005515 protein binding | IPI PMID:14749489 Expression and interaction analysis of Arabidopsis Skp1-rela... | MODIFY | Summary: EBF1 interacts with the SCF core subunit ASK11 (PMID:14749489), which is how the F-box protein is assembled into the SCF(EBF1) E3 ligase. Reason: Protein binding is uninformative; binding of the ligase core via the F-box together with substrate recruitment constitutes the adaptor activity of an F-box subunit (membership of the SCF complex is captured by GO:0019005). Proposed replacements: ubiquitin-like ligase-substrate adaptor activity Supporting Evidence: PMID:15090654 two F-box proteins, EBF1 and -2, that work coordinately in SCF complexes to repress ethylene action |
| GO:0005515 protein binding | IPI PMID:14749489 Expression and interaction analysis of Arabidopsis Skp1-rela... | MODIFY | Summary: EBF1 interacts with the SCF core subunit ASK1/SKP1A (PMID:14749489), which is how the F-box protein is assembled into the SCF(EBF1) E3 ligase. Reason: Protein binding is uninformative; binding of the ligase core via the F-box together with substrate recruitment constitutes the adaptor activity of an F-box subunit (membership of the SCF complex is captured by GO:0019005). Proposed replacements: ubiquitin-like ligase-substrate adaptor activity Supporting Evidence: PMID:15090654 two F-box proteins, EBF1 and -2, that work coordinately in SCF complexes to repress ethylene action |
| GO:0005515 protein binding | IPI PMID:14749489 Expression and interaction analysis of Arabidopsis Skp1-rela... | MODIFY | Summary: EBF1 interacts with the SCF core subunit ASK2/SKP1B (PMID:14749489), which is how the F-box protein is assembled into the SCF(EBF1) E3 ligase. Reason: Protein binding is uninformative; binding of the ligase core via the F-box together with substrate recruitment constitutes the adaptor activity of an F-box subunit (membership of the SCF complex is captured by GO:0019005). Proposed replacements: ubiquitin-like ligase-substrate adaptor activity Supporting Evidence: PMID:15090654 two F-box proteins, EBF1 and -2, that work coordinately in SCF complexes to repress ethylene action |
| GO:0005515 protein binding | IPI PMID:21737749 Derepression of ethylene-stabilized transcription factors (E... | MODIFY | Summary: EBF1 binds its ubiquitination substrate EIN3 (PMID:21737749); this substrate recognition is the core function of the F-box protein in SCF(EBF1). Reason: Protein binding is uninformative; the substrate-recruiting activity of an F-box subunit is captured by ubiquitin-like ligase-substrate adaptor activity. Proposed replacements: ubiquitin-like ligase-substrate adaptor activity Supporting Evidence: PMID:14675533 we identify two Arabidopsis F box proteins called EBF1 and EBF2 that interact physically with EIN3/EIL transcription factors |
| GO:0005515 protein binding | IPI PMID:21798944 Evidence for network evolution in an Arabidopsis interactome... | MODIFY | Summary: EBF1 interacts with the SCF core subunit ASK1/SKP1A (PMID:21798944), which is how the F-box protein is assembled into the SCF(EBF1) E3 ligase. Reason: Protein binding is uninformative; binding of the ligase core via the F-box together with substrate recruitment constitutes the adaptor activity of an F-box subunit (membership of the SCF complex is captured by GO:0019005). Proposed replacements: ubiquitin-like ligase-substrate adaptor activity Supporting Evidence: PMID:15090654 two F-box proteins, EBF1 and -2, that work coordinately in SCF complexes to repress ethylene action |
| GO:0005515 protein binding | IPI PMID:21798944 Evidence for network evolution in an Arabidopsis interactome... | MODIFY | Summary: EBF1 interacts with the SCF core subunit ASK2/SKP1B (PMID:21798944), which is how the F-box protein is assembled into the SCF(EBF1) E3 ligase. Reason: Protein binding is uninformative; binding of the ligase core via the F-box together with substrate recruitment constitutes the adaptor activity of an F-box subunit (membership of the SCF complex is captured by GO:0019005). Proposed replacements: ubiquitin-like ligase-substrate adaptor activity Supporting Evidence: PMID:15090654 two F-box proteins, EBF1 and -2, that work coordinately in SCF complexes to repress ethylene action |
| GO:0005515 protein binding | IPI PMID:23166809 A comprehensive analysis of interaction and localization of ... | MODIFY | Summary: EBF1 interacts with the SCF core subunit ASK4 (PMID:23166809), which is how the F-box protein is assembled into the SCF(EBF1) E3 ligase. Reason: Protein binding is uninformative; binding of the ligase core via the F-box together with substrate recruitment constitutes the adaptor activity of an F-box subunit (membership of the SCF complex is captured by GO:0019005). Proposed replacements: ubiquitin-like ligase-substrate adaptor activity Supporting Evidence: PMID:15090654 two F-box proteins, EBF1 and -2, that work coordinately in SCF complexes to repress ethylene action |
| GO:0005515 protein binding | IPI PMID:23166809 A comprehensive analysis of interaction and localization of ... | MODIFY | Summary: EBF1 interacts with the SCF core subunit ASK1/SKP1A (PMID:23166809), which is how the F-box protein is assembled into the SCF(EBF1) E3 ligase. Reason: Protein binding is uninformative; binding of the ligase core via the F-box together with substrate recruitment constitutes the adaptor activity of an F-box subunit (membership of the SCF complex is captured by GO:0019005). Proposed replacements: ubiquitin-like ligase-substrate adaptor activity Supporting Evidence: PMID:15090654 two F-box proteins, EBF1 and -2, that work coordinately in SCF complexes to repress ethylene action |
| GO:0005515 protein binding | IPI PMID:23166809 A comprehensive analysis of interaction and localization of ... | MODIFY | Summary: EBF1 interacts with the SCF core subunit ASK2/SKP1B (PMID:23166809), which is how the F-box protein is assembled into the SCF(EBF1) E3 ligase. Reason: Protein binding is uninformative; binding of the ligase core via the F-box together with substrate recruitment constitutes the adaptor activity of an F-box subunit (membership of the SCF complex is captured by GO:0019005). Proposed replacements: ubiquitin-like ligase-substrate adaptor activity Supporting Evidence: PMID:15090654 two F-box proteins, EBF1 and -2, that work coordinately in SCF complexes to repress ethylene action |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: Binary interaction (UniProtKB:A0A1I9LTW1) detected in the large-scale phytohormone protein-interaction (Y2H) network. The physiological relevance for EBF1 function is unknown, and protein binding conveys no functional information. Reason: Uninformative protein binding from a high-throughput screen with no demonstrated functional consequence; removal does not mean the interaction is false. |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: Binary interaction (UniProtKB:A8MRK9) detected in the large-scale phytohormone protein-interaction (Y2H) network. The physiological relevance for EBF1 function is unknown, and protein binding conveys no functional information. Reason: Uninformative protein binding from a high-throughput screen with no demonstrated functional consequence; removal does not mean the interaction is false. |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: Binary interaction (UniProtKB:O22768) detected in the large-scale phytohormone protein-interaction (Y2H) network. The physiological relevance for EBF1 function is unknown, and protein binding conveys no functional information. Reason: Uninformative protein binding from a high-throughput screen with no demonstrated functional consequence; removal does not mean the interaction is false. |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: Binary interaction (UniProtKB:O23160) detected in the large-scale phytohormone protein-interaction (Y2H) network. The physiological relevance for EBF1 function is unknown, and protein binding conveys no functional information. Reason: Uninformative protein binding from a high-throughput screen with no demonstrated functional consequence; removal does not mean the interaction is false. |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: Binary interaction (UniProtKB:P46639) detected in the large-scale phytohormone protein-interaction (Y2H) network. The physiological relevance for EBF1 function is unknown, and protein binding conveys no functional information. Reason: Uninformative protein binding from a high-throughput screen with no demonstrated functional consequence; removal does not mean the interaction is false. |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | MODIFY | Summary: EBF1 interacts with the SCF core subunit ASK1/SKP1A (PMID:32612234), which is how the F-box protein is assembled into the SCF(EBF1) E3 ligase. Reason: Protein binding is uninformative; binding of the ligase core via the F-box together with substrate recruitment constitutes the adaptor activity of an F-box subunit (membership of the SCF complex is captured by GO:0019005). Proposed replacements: ubiquitin-like ligase-substrate adaptor activity Supporting Evidence: PMID:15090654 two F-box proteins, EBF1 and -2, that work coordinately in SCF complexes to repress ethylene action |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: Binary interaction (UniProtKB:Q5CCK4) detected in the large-scale phytohormone protein-interaction (Y2H) network. The physiological relevance for EBF1 function is unknown, and protein binding conveys no functional information. Reason: Uninformative protein binding from a high-throughput screen with no demonstrated functional consequence; removal does not mean the interaction is false. |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: Binary interaction (UniProtKB:Q84MB2) detected in the large-scale phytohormone protein-interaction (Y2H) network. The physiological relevance for EBF1 function is unknown, and protein binding conveys no functional information. Reason: Uninformative protein binding from a high-throughput screen with no demonstrated functional consequence; removal does not mean the interaction is false. |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: Binary interaction (UniProtKB:Q8RXD6) detected in the large-scale phytohormone protein-interaction (Y2H) network. The physiological relevance for EBF1 function is unknown, and protein binding conveys no functional information. Reason: Uninformative protein binding from a high-throughput screen with no demonstrated functional consequence; removal does not mean the interaction is false. |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | MODIFY | Summary: EBF1 interacts with the SCF core subunit CUL1 (PMID:32612234), which is how the F-box protein is assembled into the SCF(EBF1) E3 ligase. Reason: Protein binding is uninformative; binding of the ligase core via the F-box together with substrate recruitment constitutes the adaptor activity of an F-box subunit (membership of the SCF complex is captured by GO:0019005). Proposed replacements: ubiquitin-like ligase-substrate adaptor activity Supporting Evidence: PMID:15090654 two F-box proteins, EBF1 and -2, that work coordinately in SCF complexes to repress ethylene action |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: Binary interaction (UniProtKB:Q9CAN4) detected in the large-scale phytohormone protein-interaction (Y2H) network. The physiological relevance for EBF1 function is unknown, and protein binding conveys no functional information. Reason: Uninformative protein binding from a high-throughput screen with no demonstrated functional consequence; removal does not mean the interaction is false. |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: Binary interaction (UniProtKB:Q9FUA4) detected in the large-scale phytohormone protein-interaction (Y2H) network. The physiological relevance for EBF1 function is unknown, and protein binding conveys no functional information. Reason: Uninformative protein binding from a high-throughput screen with no demonstrated functional consequence; removal does not mean the interaction is false. |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: Binary interaction (UniProtKB:Q9LQF0) detected in the large-scale phytohormone protein-interaction (Y2H) network. The physiological relevance for EBF1 function is unknown, and protein binding conveys no functional information. Reason: Uninformative protein binding from a high-throughput screen with no demonstrated functional consequence; removal does not mean the interaction is false. |
| GO:0005634 nucleus | IDA PMID:14675533 EIN3-dependent regulation of plant ethylene hormone signalin... | ACCEPT | Summary: Nuclear localization of EBF1 reported by Potuschak et al. Reason: Consistent with EBF1 targeting the nuclear transcription factors EIN3/EIL1. Supporting Evidence: PMID:14675533 we identify two Arabidopsis F box proteins called EBF1 and EBF2 that interact physically with EIN3/EIL transcription factors |
| GO:0005634 nucleus | IDA PMID:23166809 A comprehensive analysis of interaction and localization of ... | ACCEPT | Summary: GFP-EBF1 (At2g25490) localized to both nucleus and cytoplasm in a large-scale F-box localization study. Reason: Direct localization evidence; nucleus is where EIN3/EIL1 are targeted. Supporting Evidence: PMID:23166809 Six (At1g21760, At1g47730, At2g25490, At4g05460, At4g27050 and At5g21040) localized in both the nucleus and the cytoplasm |
| GO:0005634 nucleus | IEA GO_REF:0000120 | ACCEPT | Summary: Automated nuclear localization consistent with experimental data. Reason: EBF1 acts on nuclear EIN3/EIL1. |
| GO:0005634 nucleus | TAS PMID:14675533 EIN3-dependent regulation of plant ethylene hormone signalin... | ACCEPT | Summary: Nuclear localization of EBF1 reported by Potuschak et al. Reason: Consistent with EBF1 targeting the nuclear transcription factors EIN3/EIL1. Supporting Evidence: PMID:14675533 we identify two Arabidopsis F box proteins called EBF1 and EBF2 that interact physically with EIN3/EIL transcription factors |
| GO:0005737 cytoplasm | IDA PMID:23166809 A comprehensive analysis of interaction and localization of ... | ACCEPT | Summary: GFP-EBF1 is detected in the cytoplasm as well as the nucleus. Reason: Direct localization evidence; EBF1 mRNA translational control by EIN2 also occurs in the cytoplasm. Supporting Evidence: PMID:23166809 Six (At1g21760, At1g47730, At2g25490, At4g05460, At4g27050 and At5g21040) localized in both the nucleus and the cytoplasm |
| GO:0005737 cytoplasm | ISM GO_REF:0000122 | ACCEPT | Summary: AtSubP prediction of cytoplasmic localization; consistent with GFP localization data. Reason: Consistent with IDA. |
| GO:0006511 ubiquitin-dependent protein catabolic process | IEA GO_REF:0000117 | ACCEPT | Summary: EBF1 directs ubiquitin-dependent proteasomal degradation of EIN3/EIL1. Correct but less specific than the SCF-dependent term. Reason: Correct process for an SCF F-box subunit. Supporting Evidence: PMID:14675532 In the absence of ethylene, EIN3 is quickly degraded through a ubiquitin/proteasome pathway mediated by two F box proteins, EBF1 and EBF2. |
| GO:0006511 ubiquitin-dependent protein catabolic process | TAS PMID:11019805 Protein degradation in signaling. | ACCEPT | Summary: General review on F-box proteins/protein degradation in plant signalling (PMID:11019805), predating EBF1 characterization. The process is correct for EBF1 based on later primary data. Reason: Correct process; supported by primary studies (PMID:14675532, PMID:15090654). Supporting Evidence: PMID:14675532 In the absence of ethylene, EIN3 is quickly degraded through a ubiquitin/proteasome pathway mediated by two F box proteins, EBF1 and EBF2. |
| GO:0006511 ubiquitin-dependent protein catabolic process | TAS PMID:11077244 F-box proteins in Arabidopsis. | ACCEPT | Summary: General review on F-box proteins/protein degradation in plant signalling (PMID:11077244), predating EBF1 characterization. The process is correct for EBF1 based on later primary data. Reason: Correct process; supported by primary studies (PMID:14675532, PMID:15090654). Supporting Evidence: PMID:14675532 In the absence of ethylene, EIN3 is quickly degraded through a ubiquitin/proteasome pathway mediated by two F box proteins, EBF1 and EBF2. |
| GO:0006511 ubiquitin-dependent protein catabolic process | TAS PMID:14675532 Plant responses to ethylene gas are mediated by SCF(EBF1/EBF... | ACCEPT | Summary: Guo and Ecker showed that EIN3 degradation via the ubiquitin/proteasome pathway depends on EBF1/EBF2. Reason: Core process, directly supported. Supporting Evidence: PMID:14675532 In the absence of ethylene, EIN3 is quickly degraded through a ubiquitin/proteasome pathway mediated by two F box proteins, EBF1 and EBF2. |
| GO:0009723 response to ethylene | IEA GO_REF:0000117 | ACCEPT | Summary: ARBA prediction; EBF1 acts in the ethylene response. Reason: Consistent with genetic data. |
| GO:0009723 response to ethylene | IMP PMID:14675532 Plant responses to ethylene gas are mediated by SCF(EBF1/EBF... | ACCEPT | Summary: ebf1 mutants are hypersensitive to ethylene and EBF1 overexpression confers insensitivity. Reason: Direct genetic evidence that EBF1 controls the ethylene response. Supporting Evidence: PMID:14675532 Plants containing mutations in either gene show enhanced ethylene response by stabilizing EIN3 |
| GO:0010105 negative regulation of ethylene-activated signaling pathway | IEA GO_REF:0000117 | ACCEPT | Summary: SCF(EBF1) negatively regulates ethylene signalling by degrading EIN3/EIL1; ebf1 ebf2 mutants show constitutive ethylene responses. Reason: Core biological role. Supporting Evidence: PMID:14675533 plants carrying the ebf1 and ebf2 mutations display a constitutive ethylene response and accumulate the EIN3 protein in the absence of the hormone PMID:17307926 the SCF EBF1 and SCF EBF2 E3 complexes work in concert to fine-tune the abundance of EIN3/EIL1 in response to ambient hormone levels |
| GO:0010105 negative regulation of ethylene-activated signaling pathway | TAS PMID:14675533 EIN3-dependent regulation of plant ethylene hormone signalin... | ACCEPT | Summary: SCF(EBF1) negatively regulates ethylene signalling by degrading EIN3/EIL1; ebf1 ebf2 mutants show constitutive ethylene responses. Reason: Core biological role. Supporting Evidence: PMID:14675533 plants carrying the ebf1 and ebf2 mutations display a constitutive ethylene response and accumulate the EIN3 protein in the absence of the hormone PMID:17307926 the SCF EBF1 and SCF EBF2 E3 complexes work in concert to fine-tune the abundance of EIN3/EIL1 in response to ambient hormone levels |
| GO:0016567 protein ubiquitination | IEA GO_REF:0000041 | ACCEPT | Summary: UniPathway mapping to protein ubiquitination. SCF(EBF1) ubiquitinates EIN3; the more informative process is SCF-dependent proteasomal protein catabolism. Reason: Correct for an SCF substrate adaptor subunit. Supporting Evidence: PMID:15090654 two F-box proteins, EBF1 and -2, that work coordinately in SCF complexes to repress ethylene action |
| GO:0019005 SCF ubiquitin ligase complex | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT inference that LRR F-box proteins of this clade are SCF complex subunits; EBF1 binds ASK1/ASK2 and CUL1 and works in SCF complexes. Reason: Supported by EBF1-specific interaction and genetic data. Supporting Evidence: PMID:15090654 two F-box proteins, EBF1 and -2, that work coordinately in SCF complexes to repress ethylene action |
| GO:0031146 SCF-dependent proteasomal ubiquitin-dependent protein catabolic process | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT inference; SCF(EBF1) directs proteasomal degradation of EIN3/EIL1. Reason: Correct, specific process for EBF1. Supporting Evidence: PMID:14675532 In the absence of ethylene, EIN3 is quickly degraded through a ubiquitin/proteasome pathway mediated by two F box proteins, EBF1 and EBF2. PMID:17307926 the SCF EBF1 and SCF EBF2 E3 complexes work in concert to fine-tune the abundance of EIN3/EIL1 in response to ambient hormone levels |
| GO:1990756 ubiquitin-like ligase-substrate adaptor activity | IDA PMID:15090654 Arabidopsis EIN3-binding F-box 1 and 2 form ubiquitin-protei... | NEW | Summary: Proposed informative MF summarizing the many protein-binding rows: EBF1 bridges SCF core subunits (ASK1/2, CUL1) and the substrates EIN3/EIL1. Reason: Standard MF for a substrate-recruiting F-box subunit; supported by direct interaction and degradation data. Supporting Evidence: PMID:15090654 EBF1 and -2 interact directly with ethylene insensitive 3 (EIN3) PMID:15090654 two F-box proteins, EBF1 and -2, that work coordinately in SCF complexes to repress ethylene action |
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Download this section (compressed HTML)Q: What residues or degrons in EIN3/EIL1 does the EBF1 LRR domain recognize, and is recognition regulated by phosphorylation or other modifications?
Q: What E3 or other mechanism drives the ethylene-induced proteasomal turnover of EBF1 itself?
Experiment: Map the EBF1-EIN3 interface by structural analysis (cryo-EM or crystallography of the EBF1 LRR with EIN3 degron peptides) and test interface mutants for EIN3 stabilization in planta.
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