Mitogen-activated protein kinase 1 (Mapk1) is a 358-residue protein from Rattus norvegicus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P63086.
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The mean pLDDT of this model is 92.9 (very high 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 | 82% |
| 70 to 90 | Confident: backbone generally right | 13% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 1% |
What pLDDT means and how to read it
Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade also plays a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of…
Binds both upstream activators and downstream substrates in multimolecular complexes. Interacts with ADAM15, ARHGEF2, DAPK1 (via death domain), HSF4, IER3, IPO7, MKNK2, MORG1, NISCH, PEA15, SGK1, and isoform 1 of NEK2 (By similarity). Interacts (via phosphorylated form) with TPR (via C-terminal region and phosphorylated form); the interaction requires dimerization of MAPK1/ERK2 and increases…
Cytoplasm, cytoskeleton, spindle, Nucleus, Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, Cytoplasm, Membrane, caveola, Cell junction, focal adhesion
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4S32 | X-ray | 1.34 Å | A=1-358 |
| 4S31 | X-ray | 1.45 Å | A=1-358 |
| 5HD4 | X-ray | 1.45 Å | A=1-358 |
| 6DCG | X-ray | 1.45 Å | A=1-358 |
| 3QYZ | X-ray | 1.46 Å | A=1-358 |
| 4XP0 | X-ray | 1.46 Å | A=8-358 |
| 4S2Z | X-ray | 1.48 Å | A=1-358 |
| 4S33 | X-ray | 1.48 Å | A=1-358 |
| 6FLE | X-ray | 1.48 Å | A=1-358 |
| 3QYW | X-ray | 1.5 Å | A=1-358 |
| 8QR7 | X-ray | 1.51 Å | A=1-358 |
| 8QRB | X-ray | 1.51 Å | A=1-358 |
| 6FI3 | X-ray | 1.52 Å | A=1-358 |
| 6FRP | X-ray | 1.53 Å | A=1-358 |
| 6FXV | X-ray | 1.53 Å | A=1-358 |
| 8QRA | X-ray | 1.55 Å | A=1-358 |
| 8RM2 | X-ray | 1.55 Å | A=1-358 |
| 8RMB | X-ray | 1.55 Å | A=1-358 |
| 6FR1 | X-ray | 1.56 Å | A=1-358 |
| 6FQ7 | X-ray | 1.6 Å | A=1-358 |
Showing 20 of 78 experimental structures (best resolution first).
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