Mitogen-activated protein kinase 14 (MAPK14) is a 360-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q16539.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 89.8 (confident 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 | 75% |
| 70 to 90 | Confident: backbone generally right | 17% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 4% |
What pLDDT means and how to read it
Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK14 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as pro-inflammatory cytokines or physical stress leading to direct activation of transcription factors. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. Some of the targets are downstream kinases which are activated through phosphorylation and further phosphorylate additional targets. RPS6KA5/MSK1 and RPS6KA4/MSK2 can directly phosphorylate and…
Component of a signaling complex containing at least AKAP13, PKN1, MAPK14, ZAK and MAP2K3. Within this complex, AKAP13 interacts directly with PKN1, which in turn recruits MAPK14, MAP2K3 and ZAK (PubMed:21224381). Binds to a kinase interaction motif within the protein tyrosine phosphatase, PTPRR (By similarity). This interaction retains MAPK14 in the cytoplasm and prevents nuclear accumulation…
Cytoplasm, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2FST | X-ray | 1.45 Å | X=2-360 |
| 3LFF | X-ray | 1.5 Å | A=2-360 |
| 3OEF | X-ray | 1.6 Å | X=1-360 |
| 3ZS5 | X-ray | 1.6 Å | A=2-360 |
| 4EHV | X-ray | 1.6 Å | A=2-360 |
| 5WJJ | X-ray | 1.6 Å | A=1-360 |
| 6SFI | X-ray | 1.6 Å | A=1-360 |
| 9MHB | X-ray | 1.65 Å | A=2-360 |
| 4GEO | X-ray | 1.66 Å | A=2-360 |
| 6QYX | X-ray | 1.66 Å | A=1-166, A=197-360 |
| 8YD9 | X-ray | 1.66 Å | A=1-360 |
| 2FSL | X-ray | 1.7 Å | X=2-360 |
| 2QD9 | X-ray | 1.7 Å | A=2-360 |
| 3FMK | X-ray | 1.7 Å | A=1-360 |
| 3K3I | X-ray | 1.7 Å | A=5-352 |
| 3ROC | X-ray | 1.7 Å | A=1-360 |
| 5XYY | X-ray | 1.7 Å | A=1-360 |
| 6HWT | X-ray | 1.7 Å | A=2-360 |
| 6HWV | X-ray | 1.7 Å | A=2-360 |
| 6RFO | X-ray | 1.7 Å | A=167-196 |
Showing 20 of 267 experimental structures (best resolution first).
MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.