Q9H0M0: NEDD4-like E3 ubiquitin-protein ligase WWP1 (WWP1)

NEDD4-like E3 ubiquitin-protein ligase WWP1 (WWP1) is a 922-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9H0M0.

Gene
WWP1
Organism
Homo sapiens
Length
922 residues
Mean pLDDT
75.4
Model
AF-Q9H0M0-F1 v6
Model created
1 Aug 2025
PDB structures
8

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Model confidence (pLDDT)

The mean pLDDT of this model is 75.4 (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 accurate40%
70 to 90Confident: backbone generally right31%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions24%

What pLDDT means and how to read it

Function

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. Ubiquitinates ERBB4 isoforms JM-A CYT-1 and JM-B CYT-1, KLF2, KLF5 and TP63 and promotes their proteasomal degradation. Ubiquitinates RNF11 without targeting it for degradation. Ubiquitinates and promotes degradation of TGFBR1; the ubiquitination is enhanced by SMAD7. Ubiquitinates SMAD6 and SMAD7. Ubiquitinates and promotes degradation of SMAD2 in response to TGF-beta signaling, which requires interaction with TGIF. Activates the Hippo signaling pathway in response to cell contact inhibition and recruitment…

Subunit structure

Interacts with the Crumbs complex components PALS1 and PATJ; interaction with the Crumbs complex is enhanced by WWP1's interaction with AMOTL2 and facilitates WWP1 localization to the plasma membrane (PubMed:34404733). Interaction with the Crumbs complex promotes WWP1 monoubiquitination of AMOTL2, which activates the Hippo signaling pathway (PubMed:34404733). Binds KLF2 and HIVEP3 (By…

Subcellular location

Cytoplasm, Cell membrane, Nucleus, Cell junction

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5HPSX-ray2.05 ÅA=537-917
1ND7X-ray2.1 ÅA=546-917
6J1XX-ray2.3 ÅB=379-922
8EI4X-ray2.43 ÅA=546-917
6J1YX-ray2.55 ÅA/B=410-922
5HPTX-ray2.84 ÅA/D/G=537-917
9EQKX-ray3.0 ÅA/B=379-922
2OP7NMRA=494-532

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