Q9UIK4: Death-associated protein kinase 2 (DAPK2)

Death-associated protein kinase 2 (DAPK2) is a 370-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9UIK4.

Gene
DAPK2
Organism
Homo sapiens
Length
370 residues
Mean pLDDT
86.4
Model
AF-Q9UIK4-F1 v6
Model created
1 Aug 2025
PDB structures
11

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Model confidence (pLDDT)

The mean pLDDT of this model is 86.4 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate75%
70 to 90Confident: backbone generally right8%
50 to 70Low: treat with caution6%
Below 50Very low: often disordered regions12%

What pLDDT means and how to read it

Function

Calcium/calmodulin-dependent serine/threonine kinase involved in multiple cellular signaling pathways that trigger cell survival, apoptosis, and autophagy. Regulates both type I apoptotic and type II autophagic cell death signals, depending on the cellular setting. The former is caspase-dependent, while the latter is caspase-independent and is characterized by the accumulation of autophagic vesicles. Acts as a mediator of anoikis and a suppressor of beta-catenin-dependent anchorage-independent growth of malignant epithelial cells. May play a role in granulocytic maturation (PubMed:17347302). Regulates granulocytic motility by controlling cell spreading and polarization (PubMed:24163421)

Subunit structure

Homodimer in its autoinhibited state. Active as monomer (By similarity). Isoform 2 but not isoform 1 can interact with ATF4. Interacts with 14-3-3 proteins YWHAB, YWHAE, YWHAG, YWHAH, YWHAQ, YWHAZ and SFN; the interaction requires DAPK2 phosphorylation at Thr-369 and suppresses DAPK2 kinase activity and DAPK2-induced apoptosis (PubMed:26047703)

Subcellular location

Cytoplasm, Cytoplasmic vesicle, autophagosome lumen

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2A2AX-ray1.47 ÅA/B/C/D=11-330
1ZUZX-ray1.91 ÅB=312-330
1WRZX-ray2.0 ÅB=312-330
7A6YX-ray2.5 ÅJ/K/L/M=364-370
7A6RX-ray2.7 ÅE/F/G/L=364-370
2CKEX-ray2.8 ÅA/B/C/D=11-330
1ZWSX-ray2.9 ÅA/B/C/D/E/F/G/H=11-297
6PAWX-ray2.95 ÅA/B/E/F=12-330
2A27X-ray3.0 ÅA/B/C/D/E/F/G/H=11-330
1WMKX-ray3.6 ÅA/B/C/D/E/F/G/H=11-330
1Z9XX-ray3.93 ÅA/B/C=11-330

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About this viewer

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