Q96IZ0: PRKC apoptosis WT1 regulator protein (PAWR)

PRKC apoptosis WT1 regulator protein (PAWR) is a 340-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q96IZ0.

Gene
PAWR
Organism
Homo sapiens
Length
340 residues
Mean pLDDT
63.7
Model
AF-Q96IZ0-F1 v6
Model created
1 Aug 2025
PDB structures
1

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Model confidence (pLDDT)

The mean pLDDT of this model is 63.7 (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 accurate26%
70 to 90Confident: backbone generally right9%
50 to 70Low: treat with caution24%
Below 50Very low: often disordered regions41%

What pLDDT means and how to read it

Function

Pro-apoptotic protein capable of selectively inducing apoptosis in cancer cells, sensitizing the cells to diverse apoptotic stimuli and causing regression of tumors in animal models. Induces apoptosis in certain cancer cells by activation of the Fas prodeath pathway and coparallel inhibition of NF-kappa-B transcriptional activity. Inhibits the transcriptional activation and augments the transcriptional repression mediated by WT1. Down-regulates the anti-apoptotic protein BCL2 via its interaction with WT1. Also seems to be a transcriptional repressor by itself. May be directly involved in regulating the amyloid precursor protein (APP) cleavage activity of BACE1

Subunit structure

Homooligomer. Interacts (via the C-terminal region) with WT1 (PubMed:8943350). Interacts with THAP1 (PubMed:12717420). Interacts with AATF (PubMed:14627703). Interacts with BACE1 (PubMed:15671026). Interacts with SPSB1 (via B30.2/SPRY domain); this interaction is direct and occurs in association with the Elongin BC complex (PubMed:17189197, PubMed:20561531). Interacts with SPSB2 (via B30.2/SPRY…

Subcellular location

Cytoplasm, Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2JK9X-ray1.79 ÅB=67-81

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