E3 ubiquitin-protein ligase CBL (CBL) is a 906-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P22681.
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The mean pLDDT of this model is 62.8 (low overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.
| pLDDT band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 34% |
| 70 to 90 | Confident: backbone generally right | 13% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 51% |
What pLDDT means and how to read it
E3 ubiquitin-protein ligase that acts as a negative regulator of many signaling pathways by mediating ubiquitination of cell surface receptors (PubMed:10514377, PubMed:11896602, PubMed:14661060, PubMed:14739300, PubMed:15190072, PubMed:17509076, PubMed:18374639, PubMed:19689429, PubMed:21596750, PubMed:28381567, PubMed:40101708). Accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome (PubMed:10514377, PubMed:14661060, PubMed:14739300, PubMed:17094949, PubMed:17509076, PubMed:17974561). Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, CSF1R, EPHA8…
Forms homodimers; IFT20 promotes the formation of stable homodimers (PubMed:29237719). Interacts (phosphorylated at Tyr-731) with PIK3R1. Associates with NCK via its SH3 domain. The phosphorylated C-terminus interacts with CD2AP via its second SH3 domain. Binds to UBE2L3. Interacts with adapters SLA, SLA2 and with the phosphorylated C-terminus of SH2B2. Interacts with EGFR, SYK and ZAP70 via the…
Cytoplasm, Cell membrane, Cell projection, cilium, Golgi apparatus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3BUX | X-ray | 1.35 Å | B/D=23-351 |
| 3BUW | X-ray | 1.45 Å | B/D=23-351 |
| 7SIY | X-ray | 1.48 Å | A=48-351 |
| 5HKY | X-ray | 1.8 Å | A=47-351 |
| 5HKZ | X-ray | 1.8 Å | A=47-351 |
| 5HKX | X-ray | 1.85 Å | A=47-435 |
| 3PLF | X-ray | 1.92 Å | B/D=25-351 |
| 2Y1N | X-ray | 2.0 Å | A/C=47-435 |
| 3BUM | X-ray | 2.0 Å | B=25-351 |
| 3BUN | X-ray | 2.0 Å | B=23-351 |
| 9ERZ | X-ray | 2.02 Å | A/C=47-355 |
| 1YVH | X-ray | 2.05 Å | A=23-351 |
| 2CBL | X-ray | 2.1 Å | A=47-351 |
| 2OO9 | X-ray | 2.1 Å | A/B/C=856-895 |
| 3OB2 | X-ray | 2.1 Å | B=25-351 |
| 1B47 | X-ray | 2.2 Å | A/B/C=47-350 |
| 3OB1 | X-ray | 2.2 Å | B=25-351 |
| 5HL0 | X-ray | 2.2 Å | A=47-351 |
| 4A49 | X-ray | 2.21 Å | A=354-435 |
| 5HKW | X-ray | 2.25 Å | A/B/C=47-351 |
Showing 20 of 33 experimental structures (best resolution first).
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