Q7KZI7: Serine/threonine-protein kinase MARK2 (MARK2)

Serine/threonine-protein kinase MARK2 (MARK2) is a 788-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q7KZI7.

Gene
MARK2
Organism
Homo sapiens
Length
788 residues
Mean pLDDT
67.1
Model
AF-Q7KZI7-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 67.1 (low 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 accurate39%
70 to 90Confident: backbone generally right14%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions45%

What pLDDT means and how to read it

Function

Serine/threonine-protein kinase (PubMed:23666762). Involved in cell polarity and microtubule dynamics regulation. Phosphorylates CRTC2/TORC2, DCX, HDAC7, KIF13B, MAP2, MAP4 and RAB11FIP2. Phosphorylates the microtubule-associated protein MAPT/TAU (PubMed:23666762). Plays a key role in cell polarity by phosphorylating the microtubule-associated proteins MAP2, MAP4 and MAPT/TAU at KXGS motifs, causing detachment from microtubules, and their disassembly. Regulates epithelial cell polarity by phosphorylating RAB11FIP2. Involved in the regulation of neuronal migration through its dual activities in regulating cellular polarity and microtubule dynamics, possibly by phosphorylating and regulating…

Subunit structure

Homodimer. Interacts with PAK5; leading to inhibit the protein kinase activity (By similarity). Interacts with MAPT/TAU (PubMed:23666762). Interacts with MTCL1 isoform 1; the interaction is direct and increases MARK2 microtubule-binding ability (PubMed:23902687). Interacts (when phosphorylated at Thr-596) with YWHAZ (PubMed:15324659). Interacts with YWHAB, YWHAG and YWHAQ (PubMed:16959763)

Subcellular location

Cell membrane, Cytoplasm, Lateral cell membrane, Cytoplasm, cytoskeleton, Cell projection, dendrite

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8TXYX-ray2.1 ÅA/B=47-363
3IECX-ray2.2 ÅA/B/C/D=49-363
5EAKX-ray2.8 ÅA/B=39-364
5KZ7X-ray3.2 ÅA/B=39-364
5KZ8X-ray3.21 ÅA/B=39-364

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