Protein scribble homolog (SCRIB) is a 1655-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q14160.
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The mean pLDDT of this model is 62.5 (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 | 31% |
| 70 to 90 | Confident: backbone generally right | 18% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 46% |
What pLDDT means and how to read it
Scaffold protein involved in different aspects of polarized cell differentiation regulating epithelial and neuronal morphogenesis and T-cell polarization (PubMed:15182672, PubMed:16344308, PubMed:16965391, PubMed:18641685, PubMed:18716323, PubMed:19041750, PubMed:27380321). Via its interaction with CRTAM, required for the late phase polarization of a subset of CD4+ T-cells, which in turn regulates TCR-mediated proliferation and IFNG and IL22 production (By similarity). Plays a role in cell directional movement, cell orientation, cell sheet organization and Golgi complex polarization at the cell migration front (By similarity). Promotes epithelial cell layer barrier function via maintaining…
Interacts with UBE3A (PubMed:11027293). Interacts with PAK1 and PAK2 (PubMed:18716323). Interacts (via PDZ domains) with VANGL2 (By similarity). Interacts (via PDZ domains) with LPP and TRIP6; the interaction is direct (PubMed:15649318, PubMed:16137684). Interacts (via PDZ domains) with TJP2 (PubMed:15975580). Interacts (via PDZ domains) with APC; may mediate APC targeting to adherens junctions…
Cell membrane, Cell junction, Cell junction, adherens junction, Cell projection, lamellipodium, Cytoplasm, Postsynapse, Presynapse
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6MYE | X-ray | 1.1 Å | A=725-815 |
| 6EEY | X-ray | 1.15 Å | A=1098-1189 |
| 2W4F | X-ray | 1.3 Å | A=725-815 |
| 6MS1 | X-ray | 1.35 Å | A/B=722-815 |
| 6MYF | X-ray | 1.6 Å | A=725-815 |
| 5VWI | X-ray | 1.75 Å | A/B=1002-1092 |
| 7QRS | X-ray | 1.77 Å | A/B=700-816 |
| 7QS9 | X-ray | 1.8 Å | A/B=700-816 |
| 7QSB | X-ray | 1.84 Å | A/B=1002-1092 |
| 7QS8 | X-ray | 1.85 Å | A/B=1002-1092 |
| 7QRT | X-ray | 1.9 Å | A/B=859-950 |
| 7QTP | X-ray | 1.9 Å | A=700-816 |
| 8CD3 | X-ray | 1.9 Å | B=715-815 |
| 5VWC | X-ray | 1.91 Å | A=725-815 |
| 6XA6 | X-ray | 1.95 Å | A/B=1002-1092 |
| 8B87 | X-ray | 2.0 Å | A/B=700-815 |
| 7QSA | X-ray | 2.02 Å | A/B=1002-1092 |
| 6MTU | X-ray | 2.14 Å | A/B=700-816 |
| 6XA8 | X-ray | 2.2 Å | A/B=700-816 |
| 5VWK | X-ray | 2.35 Å | A/B/C/D=700-816 |
Showing 20 of 36 experimental structures (best resolution first).
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