Q8TD19: Serine/threonine-protein kinase Nek9 (NEK9)

Serine/threonine-protein kinase Nek9 (NEK9) is a 979-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8TD19.

Gene
NEK9
Organism
Homo sapiens
Length
979 residues
Mean pLDDT
73.9
Model
AF-Q8TD19-F1 v6
Model created
1 Aug 2025
PDB structures
2

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Model confidence (pLDDT)

The mean pLDDT of this model is 73.9 (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 accurate44%
70 to 90Confident: backbone generally right24%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions25%

What pLDDT means and how to read it

Function

Pleiotropic regulator of mitotic progression, participating in the control of spindle dynamics and chromosome separation (PubMed:12101123, PubMed:12840024, PubMed:14660563, PubMed:19941817). Phosphorylates different histones, myelin basic protein, beta-casein, and BICD2 (PubMed:11864968). Phosphorylates histone H3 on serine and threonine residues and beta-casein on serine residues (PubMed:11864968). Important for G1/S transition and S phase progression (PubMed:12840024, PubMed:14660563, PubMed:19941817). Phosphorylates NEK6 and NEK7 and stimulates their activity by releasing the autoinhibitory functions of Tyr-108 and Tyr-97 respectively (PubMed:12840024, PubMed:14660563, PubMed:19941817,…

Subunit structure

Homodimer; homodimerization is required to activate NEK7 (PubMed:23482567, PubMed:26522158). Binds to Ran GTPase (PubMed:12101123). Has a greater affinity for Ran-GDP over Ran-GTP (PubMed:12101123). Interacts with SSRP1 and SUPT16H, the 2 subunits of the FACT complex (PubMed:14660563). Interacts with DYNLL1; phosphorylation at Ser-944 strongly reduces DYNLL1 binding (PubMed:23482567)

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
3ZKEX-ray2.2 ÅB/D/F/H/J/L=940-950
3ZKFX-ray2.6 ÅB/D/F/H/J/L=940-950

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