Spindlin-1 (SPIN1) is a 262-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9Y657.
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The mean pLDDT of this model is 81.2 (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 | 65% |
| 70 to 90 | Confident: backbone generally right | 9% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 23% |
What pLDDT means and how to read it
Chromatin reader that specifically recognizes and binds histone H3 both trimethylated at 'Lys-4' and 'Lys-9' (H3K4me3K9me3) and is involved in piRNA-mediated retrotransposon silencing during spermatogenesis (PubMed:33574238). Plays a key role in the initiation of the PIWIL4-piRNA pathway, a pathway that directs transposon DNA methylation and silencing in the male embryonic germ cells, by promoting recruitment of DNA methylation machinery to transposons: binds young, but not old, LINE1 transposons, which are specifically marked with H3K4me3K9me3, and promotes the recruitment of PIWIL4 and SPOCD1 to transposons, leading to piRNA-directed DNA methylation (By similarity). Also recognizes and…
Homodimer; may form higher-order oligomers (PubMed:17082182). Interacts with TCF7L2/TCF4; the interaction is direct (PubMed:22258766, PubMed:24589551, PubMed:29061846). Interacts with HABP4 and SERBP1 (By similarity). Interacts with SPINDOC; SPINDOC stabilizes SPIN1 and enhances its association with bivalent H3K4me3K9me3 mark (PubMed:29061846, PubMed:33574238). Interacts with SPOCD1; promoting…
Nucleus, Nucleus, nucleolus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7OCB | X-ray | 1.42 Å | B=49-262 |
| 6I8Y | X-ray | 1.52 Å | A=49-262 |
| 6I8L | X-ray | 1.58 Å | B=49-262 |
| 6QPL | X-ray | 1.6 Å | B=49-262 |
| 7CNA | X-ray | 1.6 Å | A/D=51-262 |
| 4MZG | X-ray | 1.7 Å | B/D=50-262 |
| 6I8B | X-ray | 1.76 Å | B/E=49-262 |
| 8GTX | X-ray | 1.8 Å | A=50-262 |
| 9T2Z | X-ray | 1.87 Å | A=49-262 |
| 4H75 | X-ray | 2.1 Å | A=27-262 |
| 4MZF | X-ray | 2.1 Å | B=50-262 |
| 2NS2 | X-ray | 2.2 Å | A/B=26-262 |
| 4MZH | X-ray | 2.2 Å | A=50-262 |
| 5JSJ | X-ray | 2.35 Å | A/B=50-262 |
| 5JSG | X-ray | 2.5 Å | A/B=50-262 |
| 7E9M | X-ray | 2.5 Å | A/C=1-262 |
| 7EA1 | X-ray | 2.7 Å | A/C=50-262 |
| 7BQZ | X-ray | 3.1 Å | A/C/E/G=45-262 |
| 5Y5W | X-ray | 3.3 Å | A/B/C/D=51-262 |
| 7BU9 | X-ray | 3.5 Å | A/C/E/G=45-262 |
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