Q63ZY3: KN motif and ankyrin repeat domain-containing protein 2 (KANK2)

KN motif and ankyrin repeat domain-containing protein 2 (KANK2) is a 851-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q63ZY3.

Gene
KANK2
Organism
Homo sapiens
Length
851 residues
Mean pLDDT
60.1
Model
AF-Q63ZY3-F1 v6
Model created
1 Aug 2025
PDB structures
3

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Model confidence (pLDDT)

The mean pLDDT of this model is 60.1 (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 accurate27%
70 to 90Confident: backbone generally right15%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions53%

What pLDDT means and how to read it

Function

Involved in transcription regulation by sequestering in the cytoplasm nuclear receptor coactivators such as NCOA1, NCOA2 and NCOA3 (PubMed:17476305). Involved in regulation of caspase-independent apoptosis by sequestering the proapoptotic factor AIFM1 in mitochondria (PubMed:22371500). Pro-apoptotic stimuli can induce its proteasomal degradation allowing the translocation of AIFM1 to the nucleus to induce apoptosis (PubMed:22371500). Involved in the negative control of vitamin D receptor signaling pathway (PubMed:24671081). Involved in actin stress fibers formation through its interaction with ARHGDIA and the regulation of the Rho signaling pathway (PubMed:17996375, PubMed:25961457). May…

Subunit structure

Interacts (non-phosphorylated form) with NCOA1; NCOA2 AND NCOA3 (PubMed:17476305). Interacts with AIFM1 (PubMed:22371500). Interacts with ARHGDIA; the interaction is direct and may regulate the interaction of ARHGDIA with RHOA, RAC1 and CDC42 (PubMed:25961457). Interacts (via ANK repeats 1-5) with KIF21A (via residues 1146-1167) (PubMed:29183992)

Subcellular location

Cytoplasm, Mitochondrion

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6TMDX-ray1.5 ÅA=583-832
4HBDX-ray1.72 ÅA=578-832
5YBVX-ray2.12 ÅA/B=578-832

More AlphaFold highlights

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