Protein c-Fos (FOS) is a 380-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P01100.
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The mean pLDDT of this model is 57.2 (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 | 17% |
| 70 to 90 | Confident: backbone generally right | 5% |
| 50 to 70 | Low: treat with caution | 22% |
| Below 50 | Very low: often disordered regions | 56% |
What pLDDT means and how to read it
Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. In the heterodimer, FOS and JUN/AP-1 basic regions each seems to interact with symmetrical DNA half sites. On TGF-beta activation, forms a multimeric SMAD3/SMAD4/JUN/FOS complex at the AP1/SMAD-binding site to regulate TGF-beta-mediated signaling. Has a critical function in regulating the development of cells destined to form and maintain the skeleton. It is thought to have an important role in signal transduction, cell proliferation and differentiation. In growing cells, activates phospholipid synthesis, possibly by activating CDS1 and PI4K2A. This activity requires…
Heterodimer; with JUN (By similarity). Component of the SMAD3/SMAD4/JUN/FOS complex required for synergistic TGF-beta-mediated transcription at the AP1 promoter site (PubMed:9732876). Interacts with SMAD3; the interaction is weak even on TGF-beta activation (PubMed:9732876). Interacts with MAFB (By similarity). Interacts with TSC22D3 (via N-terminus); this interaction inhibits the binding of…
Nucleus, Endoplasmic reticulum, Cytoplasm, cytosol
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1A02 | X-ray | 2.7 Å | F=138-193 |
| 1FOS | X-ray | 3.05 Å | E/G=139-200 |
| 1S9K | X-ray | 3.1 Å | D=140-192 |
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