TAR DNA-binding protein 43 (TARDBP) is a 414-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13148.
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The mean pLDDT of this model is 65.2 (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 | 1% |
| 70 to 90 | Confident: backbone generally right | 51% |
| 50 to 70 | Low: treat with caution | 10% |
| Below 50 | Very low: often disordered regions | 38% |
What pLDDT means and how to read it
RNA-binding protein that is involved in various steps of RNA biogenesis and processing (PubMed:23519609). Preferentially binds, via its two RNA recognition motifs RRM1 and RRM2, to GU-repeats on RNA molecules predominantly localized within long introns and in the 3'UTR of mRNAs (PubMed:23519609, PubMed:24240615, PubMed:24464995). In turn, regulates the splicing of many non-coding and protein-coding RNAs including proteins involved in neuronal survival, as well as mRNAs that encode proteins relevant for neurodegenerative diseases (PubMed:21358640, PubMed:29438978). Plays a role in maintaining mitochondrial homeostasis by regulating the processing of mitochondrial transcripts…
Homodimer (PubMed:20043239, PubMed:24464995). Homooligomer (via its N-terminal domain) (PubMed:28663553, PubMed:29438978). Interacts with BRDT (By similarity). Binds specifically to pyrimidine-rich motifs of TAR DNA and to single stranded TG repeated sequences. Binds to RNA, specifically to UG repeated sequences with a minimum of six contiguous repeats. Interacts with ATXN2; the interaction is…
Nucleus, Cytoplasm, Cytoplasm, Stress granule, Mitochondrion
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6CF4 | EM | 0.75 Å | A=312-317 |
| 5WHP | X-ray | 1.0 Å | A=312-317 |
| 5WIA | X-ray | 1.0 Å | A=370-375 |
| 5WKB | EM | 1.0 Å | A=312-317 |
| 5WHN | X-ray | 1.1 Å | A=312-317 |
| 5WIQ | X-ray | 1.25 Å | A/B=396-402 |
| 5W50 | X-ray | 1.4 Å | A/B=248-253 |
| 5W52 | EM | 1.4 Å | A=247-257 |
| 6CFH | EM | 1.5 Å | A/B=333-343 |
| 5WKD | X-ray | 1.8 Å | A=300-306 |
| 5MDI | X-ray | 2.1 Å | A/B=2-80 |
| 7N9H | X-ray | 2.2 Å | A=79-102 |
| 8CG3 | EM | 2.39 Å | A/B/C/D/U=1-414 |
| 8CGG | EM | 2.5 Å | A/B/C/D/U=1-414 |
| 6T4B | X-ray | 2.55 Å | A/C/E/G/I=1-80 |
| 7PY2 | EM | 2.6 Å | A/B/C/D=1-414 |
| 4Y0F | X-ray | 2.65 Å | A/B=101-191 |
| 8CGH | EM | 2.68 Å | A/B/C/D/U=1-414 |
| 4IUF | X-ray | 2.75 Å | A=103-179 |
| 9FOR | EM | 2.75 Å | A/C/E/G/o=284-345 |
Showing 20 of 44 experimental structures (best resolution first).
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