Q9BRV8: Suppressor of IKBKE 1 (SIKE1)

Suppressor of IKBKE 1 (SIKE1) is a 207-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9BRV8.

Gene
SIKE1
Organism
Homo sapiens
Length
207 residues
Mean pLDDT
85.4
Model
AF-Q9BRV8-F1 v6
Model created
1 Aug 2025
PDB structures
3

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Model confidence (pLDDT)

The mean pLDDT of this model is 85.4 (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 accurate61%
70 to 90Confident: backbone generally right18%
50 to 70Low: treat with caution15%
Below 50Very low: often disordered regions5%

What pLDDT means and how to read it

Function

Physiological suppressor of IKK-epsilon and TBK1 that plays an inhibitory role in virus- and TLR3-triggered IRF3. Inhibits TLR3-mediated activation of interferon-stimulated response elements (ISRE) and the IFN-beta promoter. May act by disrupting the interactions of IKBKE or TBK1 with TICAM1/TRIF, IRF3 and RIGI. Does not inhibit NF-kappa-B activation pathways (PubMed:16281057). Associates with the striatin-interacting phosphatase and kinase (STRIPAK) core complex, forming the extended (SIKE1:SLMAP)STRIPAK complex (PubMed:30622739). The (SIKE1:SLMAP)STRIPAK complex dephosphorylates STK3 leading to the inhibition of Hippo signaling and the control of cell growth (PubMed:30622739)

Subunit structure

Interacts with IKBKE and TBK1 via its coiled coil region. Interaction with TBK1 is disrupted upon viral infection or TLR3 stimulation (PubMed:16281057). Interacts with CDC42BPB (PubMed:25743393). Interacts with SIKE1 which mediates association with the STRIPAK core complex composed of PP2A catalytic and scaffolding subunits, the striatins (PP2A regulatory subunits), the striatin-associated…

Subcellular location

Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6AKKX-ray1.5 ÅA/B=72-121
6AKLX-ray1.75 ÅA/B=72-121
6AKMX-ray2.3 ÅA=5-65

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