Transportin-1 (TNPO1) is a 898-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q92973.
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The mean pLDDT of this model is 92.4 (very high 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 | 84% |
| 70 to 90 | Confident: backbone generally right | 12% |
| 50 to 70 | Low: treat with caution | 1% |
| Below 50 | Very low: often disordered regions | 3% |
What pLDDT means and how to read it
Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates (PubMed:24753571). May mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of…
Identified in a complex that contains TNPO1, RAN and RANBP1 (PubMed:9428644). Binds HNRPA1, HNRPA2, HNRNPDL, RPS7, RPL5 and RAN. Interacts with H2A, H2B, H3 and H4 histones (By similarity). Interacts with isoform 1 and isoform 5 of ADAR/ADAR1 (via DRBM 3 domain) (PubMed:19124606, PubMed:24753571). Interacts with SNAI1 (via zinc fingers); the interaction mediates SNAI1 nuclear import…
Cytoplasm, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4FDD | X-ray | 2.3 Å | A=9-331, A=375-898 |
| 2Z5K | X-ray | 2.6 Å | A=9-898 |
| 4OO6 | X-ray | 2.7 Å | A=375-898, A=9-331 |
| 7CYL | X-ray | 2.7 Å | A=9-344, A=376-898 |
| 5YVI | X-ray | 2.9 Å | A=9-344, A=376-898 |
| 1QBK | X-ray | 3.0 Å | B=9-898 |
| 2QMR | X-ray | 3.0 Å | A/B/C/D=9-898 |
| 2Z5M | X-ray | 3.0 Å | A=9-898 |
| 4FQ3 | X-ray | 3.0 Å | A=9-898 |
| 5TQC | X-ray | 3.0 Å | A=9-343, A=375-898 |
| 2H4M | X-ray | 3.05 Å | A/B=376-898, A/B=9-343 |
| 4JLQ | X-ray | 3.05 Å | A=9-898 |
| 5J3V | X-ray | 3.05 Å | A/B=9-331, A/B=375-898 |
| 2OT8 | X-ray | 3.1 Å | A/B=9-331, A/B=375-898 |
| 5YVH | X-ray | 3.15 Å | A=9-344, A=376-898 |
| 8SGH | EM | 3.17 Å | A=8-898 |
| 2Z5N | X-ray | 3.2 Å | A=9-898 |
| 2Z5O | X-ray | 3.2 Å | A=9-898 |
| 2Z5J | X-ray | 3.4 Å | A=9-898 |
| 7VPW | X-ray | 3.76 Å | A=8-344, A=376-898 |
Showing 20 of 21 experimental structures (best resolution first).
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