Q14258: E3 ubiquitin/ISG15 ligase TRIM25 (TRIM25)

E3 ubiquitin/ISG15 ligase TRIM25 (TRIM25) is a 630-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q14258.

Gene
TRIM25
Organism
Homo sapiens
Length
630 residues
Mean pLDDT
84.1
Model
AF-Q14258-F1 v6
Model created
1 Aug 2025
PDB structures
10

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Model confidence (pLDDT)

The mean pLDDT of this model is 84.1 (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 accurate67%
70 to 90Confident: backbone generally right16%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions15%

What pLDDT means and how to read it

Function

Functions as a ubiquitin E3 ligase and as an ISG15 E3 ligase (PubMed:16352599). Involved in innate immune defense against viruses by mediating ubiquitination of RIGI and IFIH1 (PubMed:17392790, PubMed:29357390, PubMed:30193849, PubMed:31710640, PubMed:33849980, PubMed:36045682, PubMed:40719442). Mediates 'Lys-63'-linked polyubiquitination of the RIGI N-terminal CARD-like region and may play a role in signal transduction that leads to the production of interferons in response to viral infection (PubMed:17392790, PubMed:23950712). Mediates 'Lys-63'-linked polyubiquitination of IFIH1 (PubMed:30193849). Promotes ISGylation of 14-3-3 sigma (SFN), an adapter protein implicated in the regulation…

Subunit structure

Forms homodimers (PubMed:27154206, PubMed:27425606, PubMed:29357390, PubMed:31710640). Interacts (via SPRY domain) with RIGI (via CARD domain). Interacts with ZFHX3. Interacts with NLRP12; this interaction reduces the E3 ubiquitin ligase TRIM25-mediated 'Lys-63'-linked RIGI activation. Interacts with the KHDC3L/FILIA-OOEP/FLOPED scaffold complex and BLM at DNA replication forks (By similarity).…

Subcellular location

Cytoplasm, Cytoplasm, Stress granule, Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9I0TX-ray1.8 ÅA=435-630
6FLMX-ray2.01 ÅA/B/C=435-630
5FERX-ray2.34 ÅA/D=1-82
5EYAX-ray2.4 ÅF/G=1-83
4LTBX-ray2.59 ÅA/B=189-379
9IUNX-ray2.7 ÅA/B/C/D/E/F/G/H/I/J/K/L=433-630
4CFGX-ray2.8 ÅA/B=1-630
5NT1X-ray2.82 ÅA/E/I=190-379
6FLNX-ray3.6 ÅA/B/E=189-630
5NT2X-ray4.26 ÅA/I/N/V=190-379

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