Peripheral plasma membrane protein CASK (CASK) is a 926-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O14936.
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The mean pLDDT of this model is 78.9 (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 | 46% |
| 70 to 90 | Confident: backbone generally right | 29% |
| 50 to 70 | Low: treat with caution | 10% |
| Below 50 | Very low: often disordered regions | 15% |
What pLDDT means and how to read it
Multidomain scaffolding Mg(2+)-independent protein kinase that catalyzes the phosphotransfer from ATP to proteins such as NRXN1, and plays a role in synaptic transmembrane protein anchoring and ion channel trafficking (PubMed:18423203). Contributes to neural development and regulation of gene expression via interaction with the transcription factor TBR1. Binds to cell-surface proteins, including amyloid precursor protein, neurexins and syndecans. May mediate a link between the extracellular matrix and the actin cytoskeleton via its interaction with syndecan and with the actin/spectrin-binding protein 4.1. Component of the LIN-10-LIN-2-LIN-7 complex, which associates with the motor protein…
CASK and LIN7 form two mutually exclusive tripartite complexes with APBA1 or CASKIN1 (By similarity). Component of the brain-specific heterotrimeric complex (LIN-10-LIN-2-LIN-7 complex) composed of at least APBA1, CASK, and LIN7, which associates with the motor protein KIF17 to transport vesicles along microtubules (By similarity). Forms a heterotrimeric complex with DLG1 and LIN7B via their L27…
Nucleus, Cytoplasm, Cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1KGD | X-ray | 1.31 Å | A=739-914 |
| 9M6G | X-ray | 1.7 Å | A=1-319 |
| 9KYS | X-ray | 1.76 Å | B/D=287-332 |
| 9M5Y | X-ray | 1.8 Å | A=1-332 |
| 3C0I | X-ray | 1.85 Å | A=1-337 |
| 6NH9 | X-ray | 1.85 Å | A/B/C=487-572 |
| 6NID | X-ray | 1.86 Å | A/B/C=487-572 |
| 1KWA | X-ray | 1.93 Å | A/B=487-572 |
| 7OAJ | X-ray | 1.93 Å | A/B/C/D=1-337 |
| 3MFR | X-ray | 2.0 Å | A=1-337 |
| 3MFS | X-ray | 2.1 Å | A=1-337 |
| 7OAL | X-ray | 2.17 Å | A/B/C/D=1-337 |
| 3C0G | X-ray | 2.19 Å | A/B=1-337 |
| 3MFT | X-ray | 2.2 Å | A=1-337 |
| 3TAC | X-ray | 2.2 Å | A=1-345 |
| 8Y68 | X-ray | 2.2 Å | A/B=1-332 |
| 7OAK | X-ray | 2.23 Å | A/B/C/D=1-337 |
| 3C0H | X-ray | 2.3 Å | A/B=1-337 |
| 3MFU | X-ray | 2.3 Å | A=1-337 |
| 7OAI | X-ray | 2.3 Å | A/B/C/D=1-337 |
Showing 20 of 22 experimental structures (best resolution first).
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