PC4 and SFRS1-interacting protein (PSIP1) is a 530-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O75475.
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The mean pLDDT of this model is 62.6 (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 | 28% |
| 70 to 90 | Confident: backbone generally right | 6% |
| 50 to 70 | Low: treat with caution | 18% |
| Below 50 | Very low: often disordered regions | 47% |
What pLDDT means and how to read it
Transcriptional coactivator involved in neuroepithelial stem cell differentiation and neurogenesis. Involved in particular in lens epithelial cell gene regulation and stress responses. May play an important role in lens epithelial to fiber cell terminal differentiation. May play a protective role during stress-induced apoptosis. Isoform 2 is a more general and stronger transcriptional coactivator. Isoform 2 may also act as an adapter to coordinate pre-mRNA splicing. Cellular cofactor for lentiviral integration
Monomer (PubMed:15895093). Interacts with IFRD1/PC4 (PubMed:9822615). Isoform 2 interacts with SFRS1 (PubMed:9885563). Isoform 1 interacts (via IBD domain) with POGZ (via IBM motif) and CDCA7L (via IBM motifs) (PubMed:19244240, PubMed:25082813, PubMed:29997176). Interacts (via IBD domain) with KMT2A (via IBM motifs) with a moderate affinity whereas interacts with the KMT2A-MEN1 complex with a…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6TRJ | X-ray | 1.3 Å | A=345-430 |
| 5N88 | X-ray | 1.7 Å | D=347-425, E=347-424 |
| 2B4J | X-ray | 2.02 Å | C/D=346-442 |
| 5OYM | X-ray | 2.05 Å | A/B/C/D/E/F/G/H=345-431 |
| 4FU6 | X-ray | 2.1 Å | A=1-135 |
| 3HPH | X-ray | 2.64 Å | E/F/G/H=348-435 |
| 8PEO | EM | 2.69 Å | K=1-530 |
| 3U88 | X-ray | 3.0 Å | C/D=347-435 |
| 7OUF | EM | 3.0 Å | C/F=1-325 |
| 8PC5 | EM | 3.04 Å | K=1-530 |
| 8PC6 | EM | 3.04 Å | K/L=1-530 |
| 7OUG | EM | 3.1 Å | C/F=1-325 |
| 3F9K | X-ray | 3.2 Å | C/G/K/O/S/W/a/e/i/m/q/u=347-435 |
| 6S01 | EM | 3.2 Å | K=1-530 |
| 3HPG | X-ray | 3.28 Å | G/H/I/J/K/L=347-435 |
| 8PEP | EM | 3.33 Å | K/L=1-530 |
| 7PEL | EM | 3.34 Å | C/F=1-325 |
| 8CBN | EM | 3.34 Å | K/L=1-530 |
| 7OUH | EM | 3.5 Å | C/F=1-325 |
| 7Z1Z | EM | 3.5 Å | Q/R=347-435 |
Showing 20 of 36 experimental structures (best resolution first).
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