Q9H3D4: Tumor protein 63 (TP63)

Tumor protein 63 (TP63) is a 680-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9H3D4.

Gene
TP63
Organism
Homo sapiens
Length
680 residues
Mean pLDDT
63.2
Model
AF-Q9H3D4-F1 v6
Model created
1 Aug 2025
PDB structures
26

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Model confidence (pLDDT)

The mean pLDDT of this model is 63.2 (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 accurate35%
70 to 90Confident: backbone generally right14%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions43%

What pLDDT means and how to read it

Function

Acts as a sequence specific DNA binding transcriptional activator or repressor. The isoforms contain a varying set of transactivation and auto-regulating transactivation inhibiting domains thus showing an isoform specific activity. Isoform 2 activates RIPK4 transcription. May be required in conjunction with TP73/p73 for initiation of p53/TP53 dependent apoptosis in response to genotoxic insults and the presence of activated oncogenes. Involved in Notch signaling by probably inducing JAG1 and JAG2. Plays a role in the regulation of epithelial morphogenesis. The ratio of DeltaN-type and TA*-type isoforms may govern the maintenance of epithelial stem cell compartments and regulate the…

Subunit structure

Binds DNA as a homotetramer. Isoform composition of the tetramer may determine transactivation activity. Isoforms Alpha and Gamma interact with HIPK2. Interacts with SSRP1, leading to stimulate coactivator activity. Isoform 1 and isoform 2 interact with WWP1. Interacts with PDS5A. Isoform 5 (via activation domain) interacts with NOC2L

Subcellular location

Nucleus

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2Y9UX-ray1.6 ÅA=545-611
8P9CX-ray1.76 ÅA=397-455
7Z72X-ray1.8 ÅA=545-611
7Z7EX-ray1.8 ÅA=162-363
7Z71X-ray1.85 ÅA/C=162-363
3ZY0X-ray1.9 ÅA/B/C/D=398-427
6RU8X-ray1.92 ÅE/F/G/H=621-632
6RU6X-ray2.05 ÅC=618-630
6RU7X-ray2.08 ÅC/D=618-633
3ZY1X-ray2.15 ÅA=398-441
9N54X-ray2.2 ÅA=372-396
8P9EX-ray2.25 ÅA=397-455
7Z73X-ray2.27 ÅA/B/C/D=397-455
4A9ZX-ray2.29 ÅA/B/C/D=397-455
9GFOX-ray2.4 ÅAAA/BBB/CCC/DDD=373-381
3QYNX-ray2.5 ÅA/B/C/D=166-362
3US0X-ray2.5 ÅA/B/C/D=166-362
8P9DX-ray2.7 ÅA/C=397-455
3US1X-ray2.8 ÅA/D=166-362
3QYMX-ray3.2 ÅA/B/C/D/E/F/G/H=166-362

Showing 20 of 26 experimental structures (best resolution first).

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