P21580: Tumor necrosis factor alpha-induced protein 3 (TNFAIP3)

Tumor necrosis factor alpha-induced protein 3 (TNFAIP3) is a 790-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P21580.

Gene
TNFAIP3
Organism
Homo sapiens
Length
790 residues
Mean pLDDT
73.8
Model
AF-P21580-F1 v6
Model created
1 Aug 2025
PDB structures
17

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Model confidence (pLDDT)

The mean pLDDT of this model is 73.8 (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 accurate35%
70 to 90Confident: backbone generally right30%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions24%

What pLDDT means and how to read it

Function

Ubiquitin-editing enzyme that contains both ubiquitin ligase and deubiquitinase activities. Involved in immune and inflammatory responses signaled by cytokines, such as TNF and IL-1 beta, or pathogens via Toll-like receptors (TLRs) through terminating NF-kappa-B activity. Essential component of a ubiquitin-editing protein complex, comprising also RNF11, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. In cooperation with TAX1BP1 promotes disassembly of E2-E3 ubiquitin protein ligase complexes in IL-1R and TNFR-1 pathways; affected are at least E3 ligases TRAF6, TRAF2 and BIRC2, and E2 ubiquitin-conjugating enzymes UBE2N and UBE2D3. In cooperation with…

Subunit structure

Homodimer. Interacts with TNIP1, TAX1BP1 and TRAF2. Interacts with RNF11, ITCH and TAX1BP1 only after TNF stimulation; these interaction are transient and they are lost after 1 hour of stimulation with TNF (By similarity). Interacts with YWHAZ and YWHAH. Interacts with IKBKG; the interaction is induced by TNF stimulation and by polyubiquitin. Interacts with RIPK1. Interacts with UBE2N; the…

Subcellular location

Cytoplasm, Nucleus, Lysosome

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3VUXX-ray1.7 ÅE/F/G=757-790
3ZJEX-ray1.84 ÅA/B=1-366
3ZJDX-ray1.87 ÅA/B=1-366
3ZJGX-ray1.92 ÅA/B=1-366
3VUWX-ray1.95 ÅE/F/G=757-789
3VUYX-ray1.98 ÅD/E/F=757-790
3ZJFX-ray2.2 ÅA/B=1-366
3DKBX-ray2.5 ÅA/B/C/D/E/F=1-370
3OJ3X-ray2.5 ÅI/J/K/L/M/N/O/P=592-635
5V3PX-ray2.5 ÅA/B/C/D/E/F=1-366
5LRXX-ray2.85 ÅA/C/E/F=1-366
5V3BX-ray3.0 ÅA/B/C/D/E/F=1-366
2VFJX-ray3.2 ÅA/B/C/D=1-366
3OJ4X-ray3.4 ÅC/F=592-635
2EQENMRA=597-631
2EQFNMRA=758-790
2EQGNMRA=381-416

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