Q6Y7W6: GRB10-interacting GYF protein 2 (GIGYF2)

GRB10-interacting GYF protein 2 (GIGYF2) is a 1299-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q6Y7W6.

Gene
GIGYF2
Organism
Homo sapiens
Length
1299 residues
Mean pLDDT
56.4
Model
AF-Q6Y7W6-F1 v6
Model created
1 Aug 2025
PDB structures
3

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Model confidence (pLDDT)

The mean pLDDT of this model is 56.4 (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 accurate5%
70 to 90Confident: backbone generally right30%
50 to 70Low: treat with caution13%
Below 50Very low: often disordered regions52%

What pLDDT means and how to read it

Function

Key component of the 4EHP-GYF2 complex, a multiprotein complex that acts as a repressor of translation initiation (PubMed:22751931, PubMed:31439631, PubMed:35878012). In the 4EHP-GYF2 complex, acts as a factor that bridges EIF4E2 to ZFP36/TTP, linking translation repression with mRNA decay (PubMed:31439631). Also recruits and bridges the association of the 4EHP complex with the decapping effector protein DDX6, which is required for the ZFP36/TTP-mediated down-regulation of AU-rich mRNA (PubMed:31439631). May act cooperatively with GRB10 to regulate tyrosine kinase receptor signaling, including IGF1 and insulin receptors (PubMed:12771153). In association with EIF4E2, assists…

Subunit structure

Component of the 4EHP-GYF2 complex, at least composed of EIF4E2, GIGYF2 and ZNF598 (PubMed:22751931, PubMed:31439631, PubMed:32726578). Interacts (via the 4EHP-binding motif) with EIF4E2; the interaction is direct (PubMed:22751931, PubMed:31439631, PubMed:32726578). Interacts with ZFP36/TTP (via P-P-P-P-G repeats); the interaction is direct (PubMed:31439631). Interacts with GRB10 (By…

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7RUPX-ray1.23 ÅA=529-597
5NVMX-ray2.0 ÅB/D=35-72
5NVLX-ray2.3 ÅB/D=35-105

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