C-Jun-amino-terminal kinase-interacting protein 1 (MAPK8IP1) is a 711-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9UQF2.
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The mean pLDDT of this model is 54.0 (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 | 9% |
| 50 to 70 | Low: treat with caution | 9% |
| Below 50 | Very low: often disordered regions | 64% |
What pLDDT means and how to read it
The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. Required for JNK activation in response to excitotoxic stress. Cytoplasmic MAPK8IP1 causes inhibition of JNK-regulated activity by retaining JNK in the cytoplasm and inhibiting JNK phosphorylation of c-Jun. May also participate in ApoER2-specific reelin signaling. Directly, or indirectly, regulates GLUT2 gene expression and beta-cell function. Appears to have a role in cell signaling in mature and developing nerve terminals. May function as a regulator of vesicle transport, through interactions with…
Forms homo- or heterooligomeric complexes. Binds specific components of the JNK signaling pathway namely, MAPK8/JNK1, MAPK9/JNK2, MAPK10/JNK3, MAP2K7/MKK7, MAP3K11/MLK3 and DLK1. Also binds the proline-rich domain-containing splice variant of apolipoprotein E receptor 2 (ApoER2). Interacts, via the PID domain, with ARHGEF28. Binds the cytoplasmic tails of LRP1 and LRP2 (Megalin). Binds the TPR…
Cytoplasm, Cytoplasm, perinuclear region, Nucleus, Endoplasmic reticulum membrane, Mitochondrion membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7NYO | X-ray | 1.4 Å | AAA/BBB/CCC/DDD=490-549 |
| 7NYK | X-ray | 1.45 Å | AAA/BBB/CCC/DDD=490-549 |
| 7NYN | X-ray | 1.54 Å | AAA/BBB/CCC/DDD/EEE/FFF/GGG/HHH/III/JJJ/KKK/LLL=490-549 |
| 7NYM | X-ray | 1.61 Å | AAA/BBB/CCC/DDD=490-549 |
| 8RPP | X-ray | 1.87 Å | D=490-547 |
| 7NYL | X-ray | 1.95 Å | AAA/BBB=490-549 |
| 7NZB | X-ray | 1.96 Å | AAA/BBB/CCC/DDD/EEE/FFF/GGG/HHH/III/JJJ/KKK/LLL=490-549 |
| 4H39 | X-ray | 1.99 Å | B=158-167 |
| 4HYU | X-ray | 2.15 Å | B=157-167 |
| 3OXI | X-ray | 2.2 Å | J=158-167 |
| 4E73 | X-ray | 2.27 Å | B=157-167 |
| 4IZY | X-ray | 2.3 Å | B=157-167 |
| 4HYS | X-ray | 2.42 Å | B=157-167 |
| 3PTG | X-ray | 2.43 Å | J=157-167 |
| 4G1W | X-ray | 2.45 Å | B=157-167 |
| 3VUM | X-ray | 2.69 Å | F=157-167 |
| 3VUH | X-ray | 2.7 Å | F=157-167 |
| 6FUZ | X-ray | 2.7 Å | A=701-711 |
| 3VUI | X-ray | 2.8 Å | F=157-167 |
| 3VUL | X-ray | 2.81 Å | F=157-167 |
Showing 20 of 27 experimental structures (best resolution first).
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