Q96J02: E3 ubiquitin-protein ligase Itchy homolog (ITCH)

E3 ubiquitin-protein ligase Itchy homolog (ITCH) is a 903-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q96J02.

Gene
ITCH
Organism
Homo sapiens
Length
903 residues
Mean pLDDT
74.7
Model
AF-Q96J02-F1 v6
Model created
1 Aug 2025
PDB structures
12

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Model confidence (pLDDT)

The mean pLDDT of this model is 74.7 (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 accurate36%
70 to 90Confident: backbone generally right35%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions23%

What pLDDT means and how to read it

Function

Acts as an Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (PubMed:11046148, PubMed:14602072, PubMed:15051726, PubMed:16387660, PubMed:17028573, PubMed:18718448, PubMed:18718449, PubMed:19116316, PubMed:19592251, PubMed:19881509, PubMed:20068034, PubMed:20392206, PubMed:20491914, PubMed:23146885, PubMed:24790097, PubMed:25631046). Catalyzes 'Lys-29'-, 'Lys-48'- and 'Lys-63'-linked ubiquitin conjugation (PubMed:17028573, PubMed:18718448, PubMed:19131965, PubMed:19881509). Involved in the control of inflammatory signaling pathways…

Subunit structure

Monomer. Part of a ternary complex composed of SMAD3, ITCH/AIP4 and NEDD9/HEF1; within the complex NEDD9/HEF1 interacts (via N-terminus) with ITCH/AIP4 (via WW domains); the complex mediates ubiquitination and proteasomal degradation of NEDD9/HEF1 (PubMed:15051726). Interacts (via WW domains) with OCNL (By similarity). Interacts (via WW domains) with NOTCH1 (By similarity). Interacts (via WW…

Subcellular location

Cell membrane, Cytoplasm, Nucleus, Early endosome membrane, Endosome membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5CQ2X-ray1.4 ÅA=433-521
5DZDX-ray1.57 ÅA/B=475-514
5DWSX-ray1.65 ÅA/C/E/G=436-474
5SXPX-ray1.65 ÅF/G=249-269
2NQ3X-ray1.8 ÅA=1-155
2P4RX-ray2.0 ÅT=246-270
4ROFX-ray2.03 ÅA/B=436-474
3TUGX-ray2.27 ÅA=524-903
5C7MX-ray3.03 ÅA=524-899
2DMVNMRA=328-357
2KYKNMRA=359-392
2YSFNMRA=480-512

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