P35226: Polycomb complex protein BMI-1 (BMI1)

Polycomb complex protein BMI-1 (BMI1) is a 326-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P35226.

Gene
BMI1
Organism
Homo sapiens
Length
326 residues
Mean pLDDT
76.8
Model
AF-P35226-F1 v6
Model created
1 Aug 2025
PDB structures
13

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Model confidence (pLDDT)

The mean pLDDT of this model is 76.8 (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 right10%
50 to 70Low: treat with caution13%
Below 50Very low: often disordered regions25%

What pLDDT means and how to read it

Function

Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility (PubMed:15386022, PubMed:16359901, PubMed:16714294, PubMed:21772249, PubMed:25355358, PubMed:26151332, PubMed:27827373). The complex composed of RNF2, UB2D3 and BMI1 binds nucleosomes, and has activity only with nucleosomal histone H2A (PubMed:21772249, PubMed:25355358). In the PRC1-like complex,…

Subunit structure

Component of a PRC1-like complex (PubMed:12167701, PubMed:15386022, PubMed:19636380, PubMed:21282530, PubMed:21772249, PubMed:25355358, PubMed:26151332). Identified in a PRC1-like HPRC-H complex with CBX2, CBX4, CBX8, PHC1, PHC2, PHC3 RING1 and RNF2 (PubMed:12167701). Interacts with RNF2/RING2 (PubMed:16714294, PubMed:21772249, PubMed:25355358). Interacts with RING1 (By similarity). Part of a…

Subcellular location

Nucleus, Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6WI7X-ray1.7 ÅA=1-104
2H0DX-ray2.5 ÅA=5-101
5FR6X-ray2.51 ÅA=121-235
3RPGX-ray2.65 ÅB=1-109
9DBYEM2.8 ÅK=1-326
8PP7EM2.91 ÅK/M=1-326
9DGGEM2.98 ÅK=1-326
8GRMEM3.05 ÅM=2-102
6WI8X-ray3.09 ÅA/B=1-104
9DDEEM3.2 ÅK=1-326
4R8PX-ray3.28 ÅK/M=2-109
2NA1NMRA=121-235
7ND1NMRH=4-104

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