TGF-beta-activated kinase 1 and MAP3K7-binding protein 1 (TAB1) is a 504-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q15750.
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The mean pLDDT of this model is 78.1 (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 | 60% |
| 70 to 90 | Confident: backbone generally right | 13% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 24% |
What pLDDT means and how to read it
Key adapter protein that plays an essential role in JNK and NF-kappa-B activation and proinflammatory cytokines production in response to stimulation with TLRs and cytokines (PubMed:22307082, PubMed:24403530). Mechanistically, associates with the catalytic domain of MAP3K7/TAK1 to trigger MAP3K7/TAK1 autophosphorylation leading to its full activation (PubMed:10838074, PubMed:25260751, PubMed:37832545). Similarly, associates with MAPK14 and triggers its autophosphorylation and subsequent activation (PubMed:11847341, PubMed:29229647). In turn, MAPK14 phosphorylates TAB1 and inhibits MAP3K7/TAK1 activation in a feedback control mechanism (PubMed:14592977). Also plays a role in recruiting…
Interacts with XIAP and BIRC7 (PubMed:11865055, PubMed:17560374). Interacts with TRAF6 and MAP3K7; during IL-1 signaling (PubMed:10094049, PubMed:10838074, PubMed:11323434, PubMed:8638164). Identified in the TRIKA2 complex composed of MAP3K7, TAB1 and TAB2 (PubMed:11460167). Interacts with TRAF6 and MAPK14; these interactions allow MAPK14 autophosphorylation (PubMed:11847341). Interacts with…
Cytoplasm, cytosol, Endoplasmic reticulum membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7NTH | X-ray | 1.97 Å | A=468-504 |
| 7NTI | X-ray | 1.98 Å | A=468-504 |
| 5JGA | X-ray | 2.0 Å | A=468-504 |
| 5V5N | X-ray | 2.01 Å | A=468-497 |
| 8GW3 | X-ray | 2.05 Å | A/B/C/D=468-504 |
| 5DIY | X-ray | 2.06 Å | P/Q=392-398 |
| 5E7R | X-ray | 2.11 Å | A=468-504 |
| 4GS6 | X-ray | 2.2 Å | A=468-504 |
| 2J4O | X-ray | 2.25 Å | A=1-401 |
| 2POM | X-ray | 2.27 Å | A=1-370 |
| 5J7S | X-ray | 2.37 Å | A=468-504 |
| 5JH6 | X-ray | 2.37 Å | A=468-504 |
| 5JK3 | X-ray | 2.37 Å | A=468-504 |
| 4O91 | X-ray | 2.39 Å | A=468-504 |
| 5J8I | X-ray | 2.4 Å | A=468-504 |
| 9FPD | X-ray | 2.4 Å | A=468-504 |
| 2YIY | X-ray | 2.49 Å | A=468-497 |
| 5O90 | X-ray | 2.49 Å | B=386-414 |
| 4L52 | X-ray | 2.54 Å | A=468-496 |
| 2YDS | X-ray | 2.55 Å | T=392-398 |
Showing 20 of 35 experimental structures (best resolution first).
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