Q13164: Mitogen-activated protein kinase 7 (MAPK7)

Mitogen-activated protein kinase 7 (MAPK7) is a 816-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13164.

Gene
MAPK7
Organism
Homo sapiens
Length
816 residues
Mean pLDDT
65.1
Model
AF-Q13164-F1 v6
Model created
1 Aug 2025
PDB structures
14

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Model confidence (pLDDT)

The mean pLDDT of this model is 65.1 (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 accurate33%
70 to 90Confident: backbone generally right12%
50 to 70Low: treat with caution12%
Below 50Very low: often disordered regions43%

What pLDDT means and how to read it

Function

Plays a role in various cellular processes such as proliferation, differentiation and cell survival. The upstream activator of MAPK7 is the MAPK kinase MAP2K5. Upon activation, it translocates to the nucleus and phosphorylates various downstream targets including MEF2C. EGF activates MAPK7 through a Ras-independent and MAP2K5-dependent pathway. As part of the MAPK/ERK signaling pathway, acts as a negative regulator of apoptosis in cardiomyocytes via interaction with STUB1/CHIP and promotion of STUB1-mediated ubiquitination and degradation of ICER-type isoforms of CREM (By similarity). May have a role in muscle cell differentiation. May be important for endothelial function and maintenance…

Subunit structure

Interacts with MAP2K5. Forms oligomers (By similarity). Interacts with MEF2A, MEF2C and MEF2D; the interaction phosphorylates the MEF2s and enhances transcriptional activity of MEF2A, MEF2C but not MEF2D (By similarity). Interacts with SGK1. Preferentially interacts with PML isoform PML-4 but shows interaction also with its other isoforms: isoform PML-1, isoform PML-2, isoform PML-3 and isoform…

Subcellular location

Cytoplasm, Nucleus, Nucleus, PML body

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5BYZX-ray1.65 ÅA=48-395
4ZSGX-ray1.79 ÅA=47-393
2Q8YX-ray2.0 ÅB=215-223
4ZSLX-ray2.25 ÅA=53-393
6HKNX-ray2.33 ÅA=54-393
9LTAX-ray2.33 ÅA/B=48-393
5O7IX-ray2.38 ÅA=46-402
6HKMX-ray2.47 ÅA=49-395
4ZSJX-ray2.48 ÅA=50-393
7PUSX-ray2.59 ÅAAA=46-402
4IC7X-ray2.6 ÅA/D=1-431
5BYYX-ray2.79 ÅA=49-394
4B99X-ray2.8 ÅA=1-397
4IC8X-ray2.8 ÅA/B=1-431

More AlphaFold highlights

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