Q96PU4: E3 ubiquitin-protein ligase UHRF2 (UHRF2)

E3 ubiquitin-protein ligase UHRF2 (UHRF2) is a 802-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q96PU4.

Gene
UHRF2
Organism
Homo sapiens
Length
802 residues
Mean pLDDT
79.8
Model
AF-Q96PU4-F1 v6
Model created
1 Aug 2025
PDB structures
9

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Model confidence (pLDDT)

The mean pLDDT of this model is 79.8 (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 accurate52%
70 to 90Confident: backbone generally right25%
50 to 70Low: treat with caution6%
Below 50Very low: often disordered regions17%

What pLDDT means and how to read it

Function

E3 ubiquitin ligase that plays important roles in DNA methylation, histone modifications, cell cycle and DNA repair (PubMed:15178429, PubMed:23404503, PubMed:27743347, PubMed:29506131). Acts as a specific reader for 5-hydroxymethylcytosine (5hmC) and thereby recruits various substrates to these sites to ubiquitinate them (PubMed:24813944, PubMed:27129234). This activity also allows the maintenance of 5mC levels at specific genomic loci and regulates neuron-related gene expression (By similarity). Participates in cell cycle regulation by ubiquitinating cyclins CCND1 and CCNE1 and thereby inducing G1 arrest (PubMed:15178429, PubMed:15361834, PubMed:21952639). Also ubiquitinates PCNP leading…

Subunit structure

Homodimer; disulfide-linked. Binds methylated CpG containing oligonucleotides. Interacts with H3; the interaction has a preference for the 'Lys-9' trimethylated form of H3 (H3K9me3) (By similarity). Interacts with PCNP (PubMed:12176013, PubMed:14741369). Interacts with HDAC1 (PubMed:15361834). Interacts directly with CCNE1; the interaction ubiquitinates CCNE1 and appears independent of CCNE1…

Subcellular location

Nucleus, Chromosome

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4PW7X-ray2.0 ÅA/B/E/F=419-648
1Z6UX-ray2.1 ÅA/B=672-802
4PW5X-ray2.2 ÅA/B/E/F=419-648
5YCOX-ray2.2 ÅE/F=784-800
4TVRX-ray2.29 ÅA=109-395
3OLNX-ray2.3 ÅA/B=419-648
4PW6X-ray3.79 ÅA/B=419-648
1WY8NMRA=1-76
2E6SNMRA=326-395

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