Q9QZS2: E3 ubiquitin-protein ligase RNF4 (Rnf4)

E3 ubiquitin-protein ligase RNF4 (Rnf4) is a 194-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9QZS2.

Gene
Rnf4
Organism
Mus musculus
Length
194 residues
Mean pLDDT
71.9
Model
AF-Q9QZS2-F1 v6
Model created
1 Aug 2025
PDB structures
1

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Model confidence (pLDDT)

The mean pLDDT of this model is 71.9 (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 accurate30%
70 to 90Confident: backbone generally right13%
50 to 70Low: treat with caution50%
Below 50Very low: often disordered regions7%

What pLDDT means and how to read it

Function

E3 ubiquitin-protein ligase which binds polysumoylated chains covalently attached to proteins and mediates 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination of those substrates and their subsequent targeting to the proteasome for degradation (PubMed:20681948). Regulates the degradation of several proteins including PML and the transcriptional activator PEA3 (By similarity). Involved in chromosome alignment and spindle assembly, it regulates the kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI to proteasomal degradation (By similarity). Regulates the cellular responses to hypoxia and heat shock through degradation of respectively EPAS1 and PARP1…

Subunit structure

Homodimer (via RING-type zinc finger domain) (PubMed:20681948). Interacts with GSC2 (PubMed:10822263). Interacts with AR/the androgen receptor and TBP (By similarity). Interacts with TCF20 (PubMed:10849425). Interacts with PATZ1 (By similarity). Interacts with TRPS1; negatively regulates TRPS1 transcriptional repressor activity (PubMed:12885770). Interacts with PML (isoform PML-1, isoform PML-2,…

Subcellular location

Cytoplasm, Nucleus, Nucleus, PML body

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2MP2NMRC=45-69

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