Q06330: Recombining binding protein suppressor of hairless (RBPJ)

Recombining binding protein suppressor of hairless (RBPJ) is a 500-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q06330.

Gene
RBPJ
Organism
Homo sapiens
Length
500 residues
Mean pLDDT
85.0
Model
AF-Q06330-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 85.0 (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 accurate71%
70 to 90Confident: backbone generally right10%
50 to 70Low: treat with caution6%
Below 50Very low: often disordered regions13%

What pLDDT means and how to read it

Function

Transcriptional regulator that plays a central role in Notch signaling, a signaling pathway involved in cell-cell communication that regulates a broad spectrum of cell-fate determinations (PubMed:41086914, PubMed:36129980). Acts as a transcriptional repressor when it is not associated with Notch proteins. When associated with some NICD product of Notch proteins (Notch intracellular domain), it acts as a transcriptional activator that activates transcription of Notch target genes. Probably represses or activates transcription via the recruitment of chromatin remodeling complexes containing histone deacetylase or histone acetylase proteins, respectively. Specifically binds to the…

Subunit structure

Interacts with activated NOTCH1, NOTCH2 or NOTCH3. Interacts with MINT/SHARP. This interaction may mediate the recruitment of large corepressor complexes containing proteins such as HDAC1, HDAC2, NCOR2, SAP30, FHL1/KYOT2 and CIRSR. Interacts with EP300, MAML1 and PTF1A. Interacts with RITA1/C12orf52, leading to nuclear export, prevent the interaction between RBPJ and NICD product and subsequent…

Subcellular location

Nucleus, Cytoplasm

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2F8XX-ray3.25 ÅC=23-449
3NBNX-ray3.45 ÅA/D=23-448
6PY8X-ray3.75 ÅC/E=23-466
3V79X-ray3.85 ÅC=23-449

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