Q9UPP1: Histone lysine demethylase PHF8 (PHF8)

Histone lysine demethylase PHF8 (PHF8) is a 1060-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9UPP1.

Gene
PHF8
Organism
Homo sapiens
Length
1060 residues
Mean pLDDT
62.4
Model
AF-Q9UPP1-F1 v6
Model created
1 Aug 2025
PDB structures
6

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Model confidence (pLDDT)

The mean pLDDT of this model is 62.4 (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 accurate34%
70 to 90Confident: backbone generally right9%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions53%

What pLDDT means and how to read it

Function

Histone lysine demethylase with selectivity for mono- and dimethylated residues. It plays an essential role in cell cycle progression and rDNA transcription (PubMed:19843542, PubMed:20531378, PubMed:20548336, PubMed:20622854). Demethylates mono- and dimethylated histone H3 'Lys-9' residue (H3K9Me1 and H3K9Me2) and monomethylated histone H4 'Lys-20' residue (H4K20Me1). Acts as a transcription activator as H3K9Me1, H3K9Me2, H3K27Me2 and H4K20Me1 are epigenetic repressive marks (PubMed:20101266, PubMed:20208542, PubMed:20346720, PubMed:20622853, PubMed:20622854). Displays a very low intrinsic activity toward dimethylated H3 'Lys-27' (H3K27Me2) (PubMed:20346720). May also have weak activity…

Subunit structure

Interacts with POLR1B, UBTF, SETD1A, HCFC1, E2F1 and ZNF711. Interacts with ZNF263; recruited to the SIX3 promoter along with other proteins involved in chromatin modification and transcriptional corepression where it contributes to transcriptional repression (PubMed:32051553)

Subcellular location

Nucleus, Nucleus, nucleolus

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7CMZX-ray1.7 ÅB=842-863
3K3OX-ray2.1 ÅA=122-483
2WWUX-ray2.15 ÅA=115-483
3KV4X-ray2.19 ÅA=37-483
3K3NX-ray2.4 ÅA=122-483
4DO0X-ray2.55 ÅA=115-483

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