Q15717: ELAV-like protein 1 (ELAVL1)

ELAV-like protein 1 (ELAVL1) is a 326-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q15717.

Gene
ELAVL1
Organism
Homo sapiens
Length
326 residues
Mean pLDDT
79.8
Model
AF-Q15717-F1 v6
Model created
1 Aug 2025
PDB structures
11

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Model confidence (pLDDT)

The mean pLDDT of this model is 79.8 (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 accurate57%
70 to 90Confident: backbone generally right19%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions21%

What pLDDT means and how to read it

Function

RNA-binding protein that binds to the 3'-UTR region of mRNAs and increases their stability (PubMed:14517288, PubMed:18285462, PubMed:31358969). Involved in embryonic stem cell (ESC) differentiation: preferentially binds mRNAs that are not methylated by N6-methyladenosine (m6A), stabilizing them, promoting ESC differentiation (By similarity). Has also been shown to be capable of binding to m6A-containing mRNAs and contributes to MYC stability by binding to m6A-containing MYC mRNAs (PubMed:32245947). Binds to poly-U elements and AU-rich elements (AREs) in the 3'-UTR of target mRNAs (PubMed:14731398, PubMed:17632515, PubMed:18285462, PubMed:23519412, PubMed:8626503). Binds avidly to the…

Subunit structure

Monomer and homodimer (in vitro) (PubMed:17632515, PubMed:20219472). Interacts with ANP32A (PubMed:11729309). Interacts with ZNF385A; the interaction is indirect and mRNA-dependent and may regulate p53/TP53 expression (By similarity). Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1…

Subcellular location

Cytoplasm, Nucleus, Cytoplasm, Stress granule, Cytoplasm, P-body

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6GD3X-ray1.35 ÅA/B/C=243-326
4FXVX-ray1.9 ÅA/B/C/D=20-99
6GC5X-ray1.9 ÅA/B/C/D=241-326
6GD2X-ray1.9 ÅA/B/C=243-326
3HI9X-ray2.0 ÅA/B/C/D=18-99
4ED5X-ray2.0 ÅA/B=18-186
6G2KX-ray2.01 ÅA/B/C=243-326
6GD1X-ray2.01 ÅA/B=243-326
4EGLX-ray2.9 ÅA=18-186
9W2FEM3.4 ÅC=15-99
5SZWNMRA=1-99

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