pre-mRNA splicing regulator USH1G (USH1G) is a 461-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q495M9.
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The mean pLDDT of this model is 68.3 (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 | 34% |
| 70 to 90 | Confident: backbone generally right | 18% |
| 50 to 70 | Low: treat with caution | 10% |
| Below 50 | Very low: often disordered regions | 38% |
What pLDDT means and how to read it
Plays a role in pre-mRNA splicing by regulating the release and transfer of U4/U6.U5 tri-small nuclear ribonucleoprotein (tri-snRNP) complexes from their assembly site in Cajal bodies to nuclear speckles, thereby contributing to the assembly of the pre-catalytic spliceosome on target pre-mRNAs (PubMed:34023904). May also participate in recycling of snRNPs back to Cajal bodies during splicing (PubMed:34023904). Plays a role in regulating MAGI2-mediated endocytosis (PubMed:24608321). Anchoring/scaffolding protein that is a part of the functional network formed by USH1C, USH1G, CDH23 and MYO7A that mediates mechanotransduction in cochlear hair cells. Required for normal development and…
Part of a complex composed of USH1C, USH1G and MYO7A (PubMed:21311020, PubMed:21709241). Interacts with USH1C (via the first PDZ domain) (PubMed:12588794, PubMed:20142502). Interacts with PDZD7 (PubMed:19028668). Interacts with CDH23 and PCDH15; these interactions may recruit USH1G to the plasma membrane (By similarity). Interacts with intraflagellar transport proteins IFT20, IFT52 and IFT57…
Cytoplasm, cytosol, Cytoplasm, cytoskeleton, Cell membrane, Cell projection, cilium, Nucleus speckle, Nucleus, Cajal body, Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, Photoreceptor inner segment
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3K1R | X-ray | 2.3 Å | B=388-461 |
| 3PVL | X-ray | 2.8 Å | B=295-390 |
| 2L7T | NMR | A=370-380 |
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