P05412: Transcription factor Jun (JUN)

Transcription factor Jun (JUN) is a 331-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P05412.

Gene
JUN
Organism
Homo sapiens
Length
331 residues
Mean pLDDT
61.3
Model
AF-P05412-F1 v6
Model created
1 Aug 2025
PDB structures
10

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Model confidence (pLDDT)

The mean pLDDT of this model is 61.3 (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 accurate20%
70 to 90Confident: backbone generally right9%
50 to 70Low: treat with caution33%
Below 50Very low: often disordered regions39%

What pLDDT means and how to read it

Function

Transcription factor that recognizes and binds to the AP-1 consensus motif 5'-TGA[GC]TCA-3' (PubMed:10995748, PubMed:22083952). Heterodimerizes with proteins of the FOS family to form an AP-1 transcription complex, thereby enhancing its DNA binding activity to the AP-1 consensus sequence 5'-TGA[GC]TCA-3' and enhancing its transcriptional activity (By similarity). Together with FOSB, plays a role in activation-induced cell death of T cells by binding to the AP-1 promoter site of FASLG/CD95L, and inducing its transcription in response to activation of the TCR/CD3 signaling pathway (PubMed:12618758). Promotes activity of NR5A1 when phosphorylated by HIPK3 leading to increased steroidogenic…

Subunit structure

Heterodimer with either BATF3 or ATF7 (PubMed:10376527, PubMed:12087103, PubMed:15467742). Heterodimer with FOS (By similarity). Heterodimer with FOSB isoform 1 and 2 (By similarity). Component of an AP-1 transcription factor complex composed of JUN-FOS heterodimers (By similarity). As part of the AP-1 transcription factor complex, forms heterodimers with FOSB, thereby binding to the AP-1…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6Y3VX-ray1.5 ÅP=262-273
5T01X-ray1.89 ÅA/B=254-315
5FV8X-ray1.99 ÅD/E=277-308
1JNMX-ray2.2 ÅA/B=254-315
8SOSX-ray2.33 ÅA/E=276-327
1A02X-ray2.7 ÅJ=253-308
1T2KX-ray3.0 ÅC=254-314
1FOSX-ray3.05 ÅF/H=254-315
1S9KX-ray3.1 ÅE=257-308
1JUNNMRA/B=276-315

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