O00255: Menin (MEN1)

Menin (MEN1) is a 610-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O00255.

Gene
MEN1
Organism
Homo sapiens
Length
610 residues
Mean pLDDT
84.4
Model
AF-O00255-F1 v6
Model created
1 Aug 2025
PDB structures
69

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Model confidence (pLDDT)

The mean pLDDT of this model is 84.4 (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 accurate73%
70 to 90Confident: backbone generally right6%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions20%

What pLDDT means and how to read it

Function

Essential component of a MLL/SET1 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3 (H3K4). Functions as a transcriptional regulator. Binds to the TERT promoter and represses telomerase expression. Plays a role in TGFB1-mediated inhibition of cell-proliferation, possibly regulating SMAD3 transcriptional activity. Represses JUND-mediated transcriptional activation on AP1 sites, as well as that mediated by NFKB subunit RELA. Positively regulates HOXC8 and HOXC6 gene expression. May be involved in normal hematopoiesis through the activation of HOXA9 expression (By similarity). May be involved in DNA repair

Subunit structure

Component of the MLL-HCF complex, at least composed of KMT2A/MLL1, MEN1, ASH2L, RBBP5, DPY30, WDR5, HCFC1 and HCFC2. Component of the menin-associated histone methyltransferase complex, at least composed of KMT2B/MLL4, MEN1, ASH2L, RBBP5, DPY30 and WDR5. Interacts with POLR2B. Interacts with POLR2A phosphorylated at 'Ser-5', but not with the unphosphorylated, nor 'Ser-2' phosphorylated POLR2A…

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
6O5IX-ray1.24 ÅA=1-593
4GQ4X-ray1.27 ÅA=1-593
8VA5X-ray1.3 ÅA=1-593
9C4YX-ray1.31 ÅA=1-593
9C4WX-ray1.4 ÅA=1-593
9C4ZX-ray1.4 ÅA=1-593
4OG4X-ray1.45 ÅA=1-593
4GPQX-ray1.46 ÅA=1-593
9C4TX-ray1.46 ÅA=1-593
9C4VX-ray1.47 ÅA=1-593
4OG6X-ray1.49 ÅA=1-593
5DB0X-ray1.5 ÅA=1-593
6OPJX-ray1.5 ÅA=1-593
9WN9X-ray1.5 ÅA/B=2-583
4OG8X-ray1.53 ÅA=1-593
5DB2X-ray1.54 ÅA=1-593
5DDBX-ray1.54 ÅA=1-593
9C4SX-ray1.54 ÅA=1-593
4GQ6X-ray1.55 ÅA=1-593
4GQ3X-ray1.56 ÅA=1-593

Showing 20 of 69 experimental structures (best resolution first).

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