Q9P289: Serine/threonine-protein kinase 26 (STK26)

Serine/threonine-protein kinase 26 (STK26) is a 416-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9P289.

Gene
STK26
Organism
Homo sapiens
Length
416 residues
Mean pLDDT
79.6
Model
AF-Q9P289-F1 v6
Model created
1 Aug 2025
PDB structures
9

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Model confidence (pLDDT)

The mean pLDDT of this model is 79.6 (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 accurate51%
70 to 90Confident: backbone generally right25%
50 to 70Low: treat with caution6%
Below 50Very low: often disordered regions18%

What pLDDT means and how to read it

Function

Serine/threonine-protein kinase that acts as a mediator of cell growth (PubMed:11641781, PubMed:17360971). Modulates apoptosis (PubMed:11641781, PubMed:17360971). In association with STK24 negatively regulates Golgi reorientation in polarized cell migration upon RHO activation (PubMed:27807006). Phosphorylates ATG4B at 'Ser-383', thereby increasing autophagic flux (PubMed:29232556). Part of the striatin-interacting phosphatase and kinase (STRIPAK) complexes. STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling. Different types of STRIPAK complexes are…

Subunit structure

Homodimer (PubMed:20730082). Interacts with PDCD10 (PubMed:17360971, PubMed:19370760, PubMed:20332113). Interacts with GOLGA2 (PubMed:15037601, PubMed:20332113). Interacts with CTTNBP2NL (PubMed:18782753). Interacts with RIPOR1 (via C-terminus); this interaction occurs in a PDCD10-dependent and Rho-independent manner (PubMed:27807006). Interacts with PDCD10; this interaction is required for the…

Subcellular location

Cytoplasm, Golgi apparatus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5YF4X-ray1.9 ÅB=320-335
4GEHX-ray1.95 ÅB/D=325-413
7B36X-ray2.11 ÅA/C=1-300
5XY9X-ray2.3 ÅC/D=314-325
3GGFX-ray2.35 ÅA/B=1-300
3W8IX-ray2.4 ÅB=346-416
4FZAX-ray3.15 ÅB=18-297
4FZDX-ray3.25 ÅB=18-297, C=323-327
4FZFX-ray3.64 ÅB=18-297

More AlphaFold highlights

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