O95155: Ubiquitin conjugation factor E4 B (UBE4B)

Ubiquitin conjugation factor E4 B (UBE4B) is a 1302-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O95155.

Gene
UBE4B
Organism
Homo sapiens
Length
1302 residues
Mean pLDDT
75.0
Model
AF-O95155-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 75.0 (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 accurate51%
70 to 90Confident: backbone generally right22%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions25%

What pLDDT means and how to read it

Function

Acts as an E3 ubiquitin ligase and E4 ubiquitin chain elongation enzyme specifically involved in polyubiquitin chain assembly (PubMed:21317885). Plays an essential role in cardiac development and in the protection of neurons from degeneration evoked by ER stress (By similarity). Is recruited to early endosomes via interaction with the ESCRT-0 component HGS, where it ubiquitinates membrane protein cargo such as EGFR and APP to promote their sorting into multivesicular bodies and subsequent lysosomal degradation (PubMed:24344129, PubMed:32841720). Promotes MDM2-mediated polyubiquitination and subsequent degradation of the tumor suppressor TP53 (PubMed:21317885). May regulate myosin assembly…

Subunit structure

Interacts with VCP/p97. Interacts with STUB1/CHIP and UNC45B. Interacts with HGS; this interaction recruits UBE4B to endosomal membranes in response to EGFR activation (PubMed:24344129). Interacts with MDM2 (PubMed:21317885). Interacts with ubiquitin-conjugating enzyme E2s UBCH5C AND UBC4 (PubMed:20696396)

Subcellular location

Early endosome, Cytoplasm, Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5O75X-ray1.48 ÅA=1226-1302
3L1XX-ray2.6 ÅA=1208-1302
3L1ZX-ray3.17 ÅB=1208-1302
2KRENMRA=1208-1302

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