Heterogeneous nuclear ribonucleoprotein A1 (HNRNPA1) is a 372-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P09651.
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The mean pLDDT of this model is 67.6 (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 | 41% |
| 70 to 90 | Confident: backbone generally right | 7% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 47% |
What pLDDT means and how to read it
Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and modulation of splice site selection (PubMed:17371836). Plays a role in the splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (PubMed:20010808). Binds to the IRES and thereby inhibits the translation of the apoptosis protease activating factor APAF1 (PubMed:31498791). May bind to specific miRNA hairpins (PubMed:28431233)
Identified in the spliceosome C complex (PubMed:11991638). Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (PubMed:17289661). Interacts with SEPT6 (PubMed:17229681). Interacts with C9orf72 (PubMed:24549040). Interacts with KHDRBS1 (PubMed:17371836). Interacts with UBQLN2 (PubMed:25616961). Interacts with PPIA/CYPA (PubMed:25678563). Interacts (via the…
Nucleus, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5ZGL | X-ray | 0.95 Å | A/B=234-240 |
| 6J60 | EM | 0.96 Å | A=209-217 |
| 1L3K | X-ray | 1.1 Å | A=1-196 |
| 6BXX | X-ray | 1.1 Å | A=243-248 |
| 5ZGD | X-ray | 1.4 Å | A=209-217 |
| 9F4G | X-ray | 1.4 Å | A=2-195 |
| 9F4H | X-ray | 1.4 Å | A=2-195 |
| 9F4J | X-ray | 1.4 Å | A=2-195 |
| 9F4L | X-ray | 1.4 Å | A=2-195 |
| 9F4N | X-ray | 1.4 Å | A=2-195 |
| 9F4O | X-ray | 1.4 Å | A=2-195 |
| 9F4P | X-ray | 1.4 Å | A=2-195 |
| 9F4Q | X-ray | 1.4 Å | A=2-195 |
| 9F4S | X-ray | 1.4 Å | A=2-195 |
| 9F4U | X-ray | 1.4 Å | A=2-195 |
| 9F4V | X-ray | 1.4 Å | A=2-195 |
| 9F4Y | X-ray | 1.4 Å | A=2-195 |
| 9F5F | X-ray | 1.4 Å | A=2-195 |
| 9F4T | X-ray | 1.42 Å | A=2-195 |
| 9F7H | X-ray | 1.43 Å | A=2-195 |
Showing 20 of 73 experimental structures (best resolution first).
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