Mitogen-activated protein kinase 10 (MAPK10) is a 464-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P53779.
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The mean pLDDT of this model is 79.3 (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 | 62% |
| 70 to 90 | Confident: backbone generally right | 12% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 23% |
What pLDDT means and how to read it
Serine/threonine-protein kinase involved in various processes such as neuronal proliferation, differentiation, migration and programmed cell death. Extracellular stimuli such as pro-inflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK10/JNK3. In turn, MAPK10/JNK3 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN and ATF2 and thus regulates AP-1 transcriptional activity. Plays regulatory roles in the signaling pathways during neuronal apoptosis. Phosphorylates…
Interacts with MAPKBP1 (By similarity). Interacts with MAPK8IP1/JIP-1 and MAPK8IP3/JIP-3/JSAP1 (By similarity). Interacts with SPAG9/MAPK8IP4/JIP4 (PubMed:15693750). Interacts with HDAC9 (PubMed:16611996). Interacts with ARRB2; the interaction enhances MAPK10 activation by MAP3K5 (PubMed:18435604). Interacts with SARM1 (By similarity). Interacts with JUND; interaction is inhibited in the…
Cytoplasm, Membrane, Nucleus, Mitochondrion
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3OY1 | X-ray | 1.7 Å | A=40-401 |
| 7ORF | X-ray | 1.7 Å | A=39-402 |
| 7KSI | X-ray | 1.73 Å | A=1-464 |
| 6EMH | X-ray | 1.76 Å | A/B/C/D=39-402 |
| 4WHZ | X-ray | 1.79 Å | A=39-423 |
| 6EQ9 | X-ray | 1.83 Å | A/B=39-402 |
| 7KSK | X-ray | 1.84 Å | A=1-464 |
| 8WGF | X-ray | 1.85 Å | A=39-402 |
| 8BZP | X-ray | 1.86 Å | A/B=39-402 |
| 2B1P | X-ray | 1.9 Å | A=46-400 |
| 4W4W | X-ray | 1.9 Å | A=39-402 |
| 4X21 | X-ray | 1.95 Å | A/B=39-402 |
| 4H39 | X-ray | 1.99 Å | A=45-400 |
| 2ZDT | X-ray | 2.0 Å | A=39-402 |
| 3DA6 | X-ray | 2.0 Å | A=39-402 |
| 4KKH | X-ray | 2.0 Å | A=40-402 |
| 8VNX | X-ray | 2.0 Å | A=1-464 |
| 4W4V | X-ray | 2.01 Å | A=39-402 |
| 4Y46 | X-ray | 2.04 Å | A=39-402 |
| 4Y5H | X-ray | 2.06 Å | A=39-402 |
Showing 20 of 65 experimental structures (best resolution first).
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