Microtubule-associated protein tau (MAPT) is a 758-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P10636.
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The mean pLDDT of this model is 49.2 (very 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 | 0% |
| 70 to 90 | Confident: backbone generally right | 8% |
| 50 to 70 | Low: treat with caution | 27% |
| Below 50 | Very low: often disordered regions | 66% |
What pLDDT means and how to read it
Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity (PubMed:21985311). The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both (PubMed:21985311, PubMed:32961270). Axonal polarity is predetermined by TAU/MAPT localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization
Interacts with MARK1, MARK2, MARK3 and MARK4 (PubMed:23666762). Interacts with PSMC2 through SQSTM1 (By similarity). Interacts with SQSTM1 when polyubiquitinated (PubMed:15953362). Interacts with FKBP4 (By similarity). Binds to CSNK1D (PubMed:14761950). Interacts with SGK1 (PubMed:16982696). Interacts with EPM2A; the interaction dephosphorylates MAPT at Ser-396 (PubMed:19542233). Interacts with…
Cytoplasm, cytosol, Cell membrane, Cytoplasm, cytoskeleton, Cell projection, axon, Cell projection, dendrite, Secreted
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6ODG | X-ray | 1.0 Å | A/B=622-627 |
| 8KDX | X-ray | 1.01 Å | B=524-538 |
| 5K7N | EM | 1.1 Å | Z=623-628 |
| 9GG8 | X-ray | 1.1 Å | P=527-539 |
| 9GG7 | X-ray | 1.24 Å | C/P=635-648 |
| 5V5C | EM | 1.25 Å | A=592-597 |
| 6FAU | X-ray | 1.25 Å | B=528-533, D=529-533 |
| 8GCK | X-ray | 1.37 Å | C/E=733-738 |
| 4Y5I | X-ray | 1.4 Å | F/G=528-534 |
| 6FAV | X-ray | 1.4 Å | B=528-533, D=529-533 |
| 6FAW | X-ray | 1.4 Å | B=528-533, D=529-533 |
| 9GHK | X-ray | 1.42 Å | Q=528-537 |
| 6FBW | X-ray | 1.45 Å | B/D=528-533 |
| 9FVG | X-ray | 1.45 Å | P=527-539 |
| 9FVH | X-ray | 1.45 Å | P=527-539 |
| 5E2W | X-ray | 1.5 Å | P=511-528 |
| 5V5B | EM | 1.5 Å | A=591-600 |
| 6FBY | X-ray | 1.5 Å | B=528-533, D=529-533 |
| 9FVN | X-ray | 1.5 Å | P=527-539 |
| 2ON9 | X-ray | 1.51 Å | A/B=623-628 |
Showing 20 of 288 experimental structures (best resolution first).
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