O15169: Axin-1 (AXIN1)

Axin-1 (AXIN1) is a 862-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O15169.

Gene
AXIN1
Organism
Homo sapiens
Length
862 residues
Mean pLDDT
61.1
Model
AF-O15169-F1 v6
Model created
1 Aug 2025
PDB structures
20

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Model confidence (pLDDT)

The mean pLDDT of this model is 61.1 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate25%
70 to 90Confident: backbone generally right14%
50 to 70Low: treat with caution12%
Below 50Very low: often disordered regions50%

What pLDDT means and how to read it

Function

Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling (PubMed:12192039, PubMed:27098453, PubMed:28829046). Controls dorsoventral patterning via two opposing effects; down-regulates CTNNB1 to inhibit the Wnt signaling pathway and ventralize embryos, but also dorsalizes embryos by activating a Wnt-independent JNK signaling pathway (PubMed:12192039). In Wnt signaling, probably facilitates the phosphorylation of CTNNB1 and APC by GSK3B (PubMed:12192039). Enhances TGF-beta signaling by recruiting the RNF111 E3 ubiquitin ligase and promoting the degradation of inhibitory SMAD7…

Subunit structure

Homodimer (By similarity). Interacts with ZBED3; the interaction is direct, enhanced by protein kinase GSK3B and casein kinase CSNK1E activities and decreases GSK3B-induced beta-catenin serine and threonine phosphorylations (By similarity). Component of the beta-catenin destruction complex, containing at least, CTNNB1, an axin and GSK3B, that regulates CTNNB1 protein levels through…

Subcellular location

Cytoplasm, Nucleus, Membrane, Cell membrane, Late endosome

Disease associations

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
1DK8X-ray1.57 ÅA=74-220
7SXJX-ray1.85 ÅB=384-400
1EMUX-ray1.9 ÅA=80-211
7SXFX-ray1.94 ÅB=385-399
8RU3X-ray2.0 ÅP=468-479
7SXHX-ray2.09 ÅB=385-400
4NM3X-ray2.1 ÅB=383-402
5WZZX-ray2.1 ÅE/F/G/H=375-394
8RU4X-ray2.13 ÅC=469-479
4NM5X-ray2.3 ÅB=383-402
4NM7X-ray2.3 ÅB=383-402
1O9UX-ray2.4 ÅB=383-400
7SXGX-ray2.4 ÅB=385-400
8VMGX-ray2.45 ÅC/D=383-435
4NM0X-ray2.5 ÅB=383-402
4NU1X-ray2.5 ÅB=383-402
7Y1PX-ray2.6 ÅA/B/C/D=74-220
3ZDIX-ray2.64 ÅB=383-400
4B7TX-ray2.77 ÅB=383-400
6JCKX-ray3.09 ÅA=781-862

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