Q8VDF2: E3 ubiquitin-protein ligase UHRF1 (Uhrf1)

E3 ubiquitin-protein ligase UHRF1 (Uhrf1) is a 782-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8VDF2.

Gene
Uhrf1
Organism
Mus musculus
Length
782 residues
Mean pLDDT
80.1
Model
AF-Q8VDF2-F1 v6
Model created
1 Aug 2025
PDB structures
17

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Model confidence (pLDDT)

The mean pLDDT of this model is 80.1 (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 accurate48%
70 to 90Confident: backbone generally right30%
50 to 70Low: treat with caution11%
Below 50Very low: often disordered regions12%

What pLDDT means and how to read it

Function

E3 ubiquitin-protein ligase that acts as a key epigenetic regulator by bridging DNA methylation and chromatin modification (PubMed:12058012, PubMed:12084726, PubMed:14993289, PubMed:17673620, PubMed:26065575, PubMed:30392929). Plays a key role in DNA methylation inheritance by promoting recruitment of DNMT1 to hemimethylated DNA and ensure faithful propagation of the DNA methylation patterns through DNA replication (PubMed:17673620, PubMed:21268065, PubMed:26065575). Acts both as a histone reader and writer: specifically recognizes and binds (1) hemimethylated DNA at replication forks and (2) histone H3 trimethylated at 'Lys-9' and unmethylated at 'Arg-2' (H3K9me3 and H3R2me0,…

Subunit structure

Interacts with DNMT1; the interaction is direct (PubMed:17994007, PubMed:21268065). Interacts with DNMT3A and DNMT3B (PubMed:19798101). Interacts with HDAC1, but not with HDAC2 (PubMed:15361834). Interacts with BLTP3A. Interacts with EHMT2 (PubMed:19056828). Interacts with PRAMEL7 (PubMed:28604677). Interacts with ZNF263; recruited to the SIX3 promoter along with other proteins involved in…

Subcellular location

Nucleus, Chromosome

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3FDEX-ray1.41 ÅA/B=419-628
2ZKDX-ray1.6 ÅA/B=404-613
2ZKGX-ray1.77 ÅA/B/C/D=404-613
2ZO1X-ray1.96 ÅB=419-628
3F8JX-ray1.99 ÅB=417-628
2ZO0X-ray2.19 ÅB=419-628
3F8IX-ray2.29 ÅA/B=418-628
2ZKFX-ray2.55 ÅA=404-613
2ZKEX-ray2.6 ÅA=404-613
6M2VX-ray3.0 ÅA/B=417-628
2ZO2X-ray3.09 ÅB=419-628
9XRLEM3.74 ÅAL/AR/x=1-782
9SFPEM4.2 Åd=1-782
9W2MEM4.2 ÅP/Q/p/q=1-782
6VEENMRA=122-305
6VFONMRA=303-380
7XGANMRA=304-372

More AlphaFold highlights

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