P62258: 14-3-3 protein epsilon (YWHAE)

14-3-3 protein epsilon (YWHAE) is a 255-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P62258.

Gene
YWHAE
Organism
Homo sapiens
Length
255 residues
Mean pLDDT
92.9
Model
AF-P62258-F1 v6
Model created
1 Aug 2025
PDB structures
11

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Model confidence (pLDDT)

The mean pLDDT of this model is 92.9 (very high 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 accurate85%
70 to 90Confident: backbone generally right9%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions4%

What pLDDT means and how to read it

Function

Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways (PubMed:21189250). Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif (PubMed:35343654). Binding generally results in the modulation of the activity of the binding partner (By similarity). Positively regulates phosphorylated protein HSF1 nuclear export to the cytoplasm (PubMed:12917326). Plays a positive role in the antiviral signaling pathway upstream of TBK1 via interaction with RIGI (PubMed:37555661). Mechanistically, directs RIGI redistribution from the cytosol to mitochondrial associated membranes where it mediates…

Subunit structure

Homodimer (PubMed:17085597). Heterodimerizes with YWHAZ (PubMed:16376338). Interacts with PKA-phosphorylated AANAT (PubMed:11427721). Interacts with ABL1 (phosphorylated form); the interaction retains it in the cytoplasm (PubMed:15696159). Interacts with ARHGEF28 (By similarity). Interacts with BEX3 (By similarity). Weakly interacts with CDKN1B (PubMed:12042314). Interacts with the 'Thr-369'…

Subcellular location

Nucleus, Cytoplasm, Melanosome

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2BR9X-ray1.75 ÅA=1-233
3UALX-ray1.8 ÅA=1-232
7V9BX-ray1.85 ÅA=1-232
3UBWX-ray1.9 ÅA=1-234
6EIHX-ray2.7 ÅA=3-232
8DGPX-ray2.7 ÅA/B/C/D=1-255
8DP5EM3.1 ÅD=1-255
7C8EX-ray3.16 ÅA/B=1-232
8DGNX-ray3.16 ÅA=1-255
8DGMX-ray3.2 ÅA=1-255
8Q1SX-ray3.23 ÅA/B=1-255

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