Splicing factor U2AF 65 kDa subunit (U2AF2) is a 475-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P26368.
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The mean pLDDT of this model is 73.2 (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 | 31% |
| 70 to 90 | Confident: backbone generally right | 33% |
| 50 to 70 | Low: treat with caution | 11% |
| Below 50 | Very low: often disordered regions | 25% |
What pLDDT means and how to read it
Plays a role in pre-mRNA splicing and 3'-end processing (PubMed:17024186). By recruiting PRPF19 and the PRP19C/Prp19 complex/NTC/Nineteen complex to the RNA polymerase II C-terminal domain (CTD), and thereby pre-mRNA, may couple transcription to splicing (PubMed:21536736). Induces cardiac troponin-T (TNNT2) pre-mRNA exon inclusion in muscle. Regulates the TNNT2 exon 5 inclusion through competition with MBNL1. Binds preferentially to a single-stranded structure within the polypyrimidine tract of TNNT2 intron 4 during spliceosome assembly. Required for the export of mRNA out of the nucleus, even if the mRNA is encoded by an intron-less gene. Represses the splicing of MAPT/Tau exon 10.…
Interacts with U2AF1L4 (By similarity). Heterodimer with U2AF1 (PubMed:11551507). Binds unphosphorylated SF1 (PubMed:10449420, PubMed:12718882). Interacts with SCAF11 and SNW1 (PubMed:21460037, PubMed:9447963). Interacts with ZRSR2/U2AF1-RS2. Interacts with RBM17 (PubMed:17589525). Interacts with PRPF19; the interaction is direct. Interacts with POLR2A (via the C-terminal domain); recruits…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5W0G | X-ray | 1.07 Å | A=148-229 |
| 5W0H | X-ray | 1.11 Å | A=258-336 |
| 6XLV | X-ray | 1.4 Å | A=141-341 |
| 9C7A | X-ray | 1.4 Å | A=141-341 |
| 9C7B | X-ray | 1.4 Å | A=141-341 |
| 2HZC | X-ray | 1.47 Å | A=148-229 |
| 7S3A | X-ray | 1.48 Å | A=141-341 |
| 5EV3 | X-ray | 1.5 Å | A=141-341 |
| 6XLW | X-ray | 1.5 Å | A=141-341 |
| 7S3C | X-ray | 1.51 Å | A=141-341 |
| 5EV4 | X-ray | 1.57 Å | A=141-341 |
| 6XLX | X-ray | 1.7 Å | A=141-341 |
| 7SN6 | X-ray | 1.8 Å | A/B=375-475 |
| 5EV2 | X-ray | 1.86 Å | A=141-341 |
| 7S3B | X-ray | 1.89 Å | A=141-341 |
| 3VAJ | X-ray | 1.9 Å | A/B=148-336 |
| 4TU8 | X-ray | 1.92 Å | A/B=148-336 |
| 4TU9 | X-ray | 1.99 Å | A/B=148-336 |
| 5EV1 | X-ray | 2.04 Å | A=141-341 |
| 4TU7 | X-ray | 2.09 Å | A/B=148-336 |
Showing 20 of 40 experimental structures (best resolution first).
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