Microtubule-associated protein RP/EB family member 1 (MAPRE1) is a 268-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q15691.
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The mean pLDDT of this model is 80.4 (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 | 56% |
| 70 to 90 | Confident: backbone generally right | 15% |
| 50 to 70 | Low: treat with caution | 13% |
| Below 50 | Very low: often disordered regions | 16% |
What pLDDT means and how to read it
Plus-end tracking protein (+TIP) that binds to the plus-end of microtubules and regulates the dynamics of the microtubule cytoskeleton (PubMed:12388762, PubMed:16109370, PubMed:19632184, PubMed:21646404, PubMed:23001180, PubMed:28726242, PubMed:28814570, PubMed:34608293). Recruits other +TIP proteins to microtubules by binding to a conserved Ser-X-Leu-Pro (SXLP) motif in their polypeptide chains (PubMed:19632184, PubMed:36592928). Promotes cytoplasmic microtubule nucleation and elongation (PubMed:12388762, PubMed:16109370, PubMed:19632184, PubMed:21646404, PubMed:28726242, PubMed:28814570). Involved in mitotic spindle positioning by stabilizing microtubules and promoting dynamic connection…
Homodimer (PubMed:15616574, PubMed:36592928). Heterodimer with MAPRE3 (PubMed:19255245). Interacts with DCTN1, DCTN2, TERF1 and dynein intermediate chain (PubMed:10226031, PubMed:11943150, PubMed:12388762, PubMed:14514668, PubMed:16109370, PubMed:16949363, PubMed:23874158). Interaction with DIAPH1 and DIAPH2 (By similarity). Interacts (via C-terminal residues 206-211) with APC (via C-terminal…
Cytoplasm, cytoskeleton, Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, Golgi apparatus, Cytoplasm, cytoskeleton, spindle, Cytoplasm, cytoskeleton, spindle pole, Cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2QJZ | X-ray | 1.25 Å | A/B=12-133 |
| 2R8U | X-ray | 1.35 Å | A/B=1-268 |
| 1PA7 | X-ray | 1.45 Å | A=1-130 |
| 1WU9 | X-ray | 1.54 Å | A/B=191-268 |
| 5JVM | X-ray | 1.57 Å | A/B=207-257 |
| 1VKA | X-ray | 1.6 Å | A/B=2-140 |
| 5JX1 | X-ray | 1.67 Å | A=210-257 |
| 1TXQ | X-ray | 1.8 Å | B=183-268 |
| 1YIB | X-ray | 1.8 Å | A=185-255 |
| 6YF5 | X-ray | 1.83 Å | A/B/C/D=215-251 |
| 2HKQ | X-ray | 1.86 Å | A=191-268 |
| 2HL5 | X-ray | 1.93 Å | A/B=191-268 |
| 5JVU | X-ray | 1.95 Å | A/B=209-257 |
| 1YIG | X-ray | 2.0 Å | A/B=185-255 |
| 5JV3 | X-ray | 2.01 Å | A/B/C/D=210-257 |
| 2HL3 | X-ray | 2.03 Å | C=263-268 |
| 3MTU | X-ray | 2.1 Å | A/B/C/D=216-257 |
| 5JVP | X-ray | 2.1 Å | A/B/C/D/E/F=211-257 |
| 5JVR | X-ray | 2.1 Å | A/B/C/D/E/F/G/H=207-257 |
| 6PF2 | X-ray | 2.17 Å | A/B=207-257 |
Showing 20 of 32 experimental structures (best resolution first).
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