Poly [ADP-ribose] polymerase tankyrase-2 (TNKS2) is a 1166-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9H2K2.
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The mean pLDDT of this model is 83.8 (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 | 63% |
| 70 to 90 | Confident: backbone generally right | 21% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 11% |
What pLDDT means and how to read it
Poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking (PubMed:11739745, PubMed:11802774, PubMed:19759537, PubMed:21478859, PubMed:23622245, PubMed:25043379). Acts as an activator of the Wnt signaling pathway by mediating poly-ADP-ribosylation of AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex: poly-ADP-ribosylated target proteins are recognized by RNF146, which mediates their ubiquitination and subsequent degradation (PubMed:19759537, PubMed:21478859). Also mediates poly-ADP-ribosylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination (PubMed:21478859).…
Oligomerizes and associates with TNKS. Interacts with the cytoplasmic domain of LNPEP/Otase in SLC2A4/GLUT4-vesicles (PubMed:11802774). Binds to the N-terminus of Grb14 and TRF1 with its ankyrin repeat region (PubMed:11802774). Interacts with HIF1AN (PubMed:18936059, PubMed:21251231). Interacts with RNF146; this interaction leads to ubiquitination and proteasomal degradation (PubMed:21799911).…
Cytoplasm, Golgi apparatus membrane, Nucleus, Chromosome, telomere
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5BXO | X-ray | 1.33 Å | A/B=488-649, C/D=5-12 |
| 5BXU | X-ray | 1.35 Å | A=488-649 |
| 5NWG | X-ray | 1.4 Å | A/B=946-1113, H/I=1114-1162 |
| 5NWD | X-ray | 1.45 Å | A/B=946-1113, H/I=1114-1162 |
| 4PNL | X-ray | 1.5 Å | A/B/C/D=959-1164 |
| 5NVE | X-ray | 1.5 Å | A/B=946-1113, H/I=1114-1162 |
| 5NWC | X-ray | 1.5 Å | A/B=946-1113, H/I=1114-1162 |
| 7CE4 | X-ray | 1.5 Å | A=946-1113, B=1114-1162 |
| 5JRT | X-ray | 1.53 Å | A=867-940 |
| 3TWR | X-ray | 1.55 Å | A/B/C/D=488-649 |
| 5C5R | X-ray | 1.55 Å | A/B=946-1113, C/D=1114-1162 |
| 5NVF | X-ray | 1.55 Å | A/B=946-1113, H/I=1114-1162 |
| 4TJU | X-ray | 1.57 Å | A/B/C/D=959-1164 |
| 4BUE | X-ray | 1.6 Å | A/B=946-1162 |
| 4BUU | X-ray | 1.6 Å | A/B=946-1162 |
| 4PNT | X-ray | 1.6 Å | A/B/C/D=959-1164 |
| 4UVZ | X-ray | 1.6 Å | A/C=946-1162 |
| 5NUT | X-ray | 1.6 Å | A/B=952-1162 |
| 5NVC | X-ray | 1.6 Å | A/B=946-1113, C/D=1114-1162 |
| 5NVH | X-ray | 1.6 Å | A/B=946-1113, I/J=1114-1162 |
Showing 20 of 197 experimental structures (best resolution first).
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