Q13043: Serine/threonine-protein kinase 4 (STK4)

Serine/threonine-protein kinase 4 (STK4) is a 487-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13043.

Gene
STK4
Organism
Homo sapiens
Length
487 residues
Mean pLDDT
75.9
Model
AF-Q13043-F1 v6
Model created
1 Aug 2025
PDB structures
16

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Model confidence (pLDDT)

The mean pLDDT of this model is 75.9 (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 accurate49%
70 to 90Confident: backbone generally right19%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions24%

What pLDDT means and how to read it

Function

Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its…

Subunit structure

Homodimer; mediated via the coiled-coil region. Interacts with NORE1, which inhibits autoactivation. Interacts with and stabilizes SAV1. Interacts with RASSF1. Interacts with FOXO3. Interacts with RASSF2 (via SARAH domain). Interacts with AR, PKB/AKT1, TNNI3 and SIRT1. Interacts with DLG5 (via PDZ domain 3). Interacts with MARK3 in the presence of DLG5 (PubMed:28087714). Interacts with SCRIB in…

Subcellular location

Cytoplasm, Nucleus

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8PAVX-ray1.9 ÅA/B=1-311
4NR2X-ray2.0 ÅA/B/C/D/E/F/G/H=432-480
8A5JX-ray2.12 ÅA/B=28-309
8PAWX-ray2.14 ÅA/B=1-311
3COMX-ray2.2 ÅA/B=2-311
4OH8X-ray2.28 ÅA=432-480
5TWGX-ray2.3 ÅE=343-356
9VX3X-ray2.39 ÅA/D=431-480, B/E=398-480
5TWHX-ray2.5 ÅE=358-374
7CEAX-ray2.55 ÅA=431-480, B=414-480
6YATX-ray2.58 ÅA/B=1-311
9IICX-ray2.78 ÅA/B=11-311
7CEBX-ray2.89 ÅC=431-480, D=412-480
8JG5EM3.04 ÅC/E=431-480, D/F=340-480
7CECEM3.9 ÅF/H=431-480, G=412-480, I=414-480
2JO8NMRA/B=432-480

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