Q01196: Runt-related transcription factor 1 (RUNX1)

Runt-related transcription factor 1 (RUNX1) is a 453-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q01196.

Gene
RUNX1
Organism
Homo sapiens
Length
453 residues
Mean pLDDT
61.0
Model
AF-Q01196-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 61.0 (low 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 accurate26%
70 to 90Confident: backbone generally right8%
50 to 70Low: treat with caution12%
Below 50Very low: often disordered regions55%

What pLDDT means and how to read it

Function

Forms the heterodimeric complex core-binding factor (CBF) with CBFB. RUNX members modulate the transcription of their target genes through recognizing the core consensus binding sequence 5'-TGTGGT-3', or very rarely, 5'-TGCGGT-3', within their regulatory regions via their runt domain, while CBFB is a non-DNA-binding regulatory subunit that allosterically enhances the sequence-specific DNA-binding capacity of RUNX. The heterodimers bind to the core site of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, LCK, IL3 and GM-CSF promoters (Probable). Essential for the development of normal hematopoiesis (PubMed:17431401).…

Subunit structure

Heterodimer with CBFB. RUNX1 binds DNA as a monomer and through the Runt domain. DNA-binding is increased by heterodimerization. Isoform AML-1L can neither bind DNA nor heterodimerize. Interacts with TLE1 and ALYREF/THOC4 (PubMed:9119228, PubMed:9751710). Interacts with ELF1, ELF2 and SPI1 (PubMed:10207087). Interacts via its Runt domain with the ELF4 N-terminal region (PubMed:10207087).…

Subcellular location

Nucleus

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
1LJMX-ray2.5 ÅA/B=51-181
1E50X-ray2.6 ÅA/C/E/G/Q/R=50-183
1H9DX-ray2.6 ÅA/C=50-183
1CMONMRA=52-178
1CO1NMRA=61-175

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