Q13077: TNF receptor-associated factor 1 (TRAF1)

TNF receptor-associated factor 1 (TRAF1) is a 416-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13077.

Gene
TRAF1
Organism
Homo sapiens
Length
416 residues
Mean pLDDT
79.3
Model
AF-Q13077-F1 v6
Model created
1 Aug 2025
PDB structures
3

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Model confidence (pLDDT)

The mean pLDDT of this model is 79.3 (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 accurate55%
70 to 90Confident: backbone generally right14%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions21%

What pLDDT means and how to read it

Function

Adapter molecule that is involved in multiple signaling pathways including the NF-kappa-B and MAPK pathways and thus influences inflammatory and apoptotic responses. Plays a critical role in regulating T-cell activation both through restricting the costimulation-independent activation of NIK in activated T-cells and by promoting the TNFRSF9-induced classical NF-kappa-B pathway (By similarity). Forms a heterotrimer with TRAF2 as part of an E3 ubiquitin-protein ligase complex that mediates ubiquitination of target proteins such as MAP3K14 and gasdermin D/GSDMD (PubMed:40097387). This complex also recruits the antiapoptotic E3 ligases BIRC2 and BIRC3 to TNFRSF1B/TNFR2 (PubMed:19287455). Acts…

Subunit structure

Homotrimer (PubMed:15383523, PubMed:20385093, PubMed:27151821). Heterotrimer with TRAF2 (PubMed:19287455, PubMed:20385093, PubMed:8069916). Interacts with TNFRSF1A/TNFR1, TNFRSF1B/TNFR2, TNFRSF4, TNFRSF5/CD40, TNFRSF8/CD30, TNFRSF9/CD137, TNFRSF11A/RANK, TNFRSF13C, TNFRSF18/AITR, TNFRSF17/BCMA, TNFRSF19/TROY, TNFRSF19L/RELT, XEDAR, EDAR, TANK/ITRAF, TRAIP and RIPK2 (PubMed:10037686,…

Subcellular location

Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3M0DX-ray2.8 ÅC=181-244
5E1TX-ray2.8 ÅA/B/C=220-416
5H10X-ray3.21 ÅA/B/C=220-416

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