Q99549: M-phase phosphoprotein 8 (MPHOSPH8)

M-phase phosphoprotein 8 (MPHOSPH8) is a 860-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q99549.

Gene
MPHOSPH8
Organism
Homo sapiens
Length
860 residues
Mean pLDDT
56.4
Model
AF-Q99549-F1 v6
Model created
1 Aug 2025
PDB structures
8

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Model confidence (pLDDT)

The mean pLDDT of this model is 56.4 (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 accurate21%
70 to 90Confident: backbone generally right22%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions53%

What pLDDT means and how to read it

Function

Heterochromatin component that specifically recognizes and binds methylated 'Lys-9' of histone H3 (H3K9me) and promotes recruitment of proteins that mediate epigenetic repression (PubMed:26022416, PubMed:28581500, PubMed:29211708). As part of the HUSH complex, promotes epigenetic repression of mobile genetic elements, such as retroviruses and transposable elements: the HUSH complex mainly represses LINE-1 (L1) retrotransposons that are still capable of transposition (PubMed:29211708). Silencing events often occur within introns of transcriptionally active genes, and lead to the down-regulation of host gene expression (PubMed:29211708). MPHOSPH8 mediates recruitment of the HUSH complex to…

Subunit structure

Homodimer (PubMed:21419134, PubMed:22022377, PubMed:22086334, PubMed:39638237). Interacts (via chromo domain) with histone H3K9me3 (PubMed:20871592). Has the highest affinity for H3K9me3, and lesser affinity for H3K9me2 and H3K9me1 (PubMed:20871592). Component of the HUSH complex; composed of TASOR, PPHLN1 and MPHOSPH8 (PubMed:26022416, PubMed:39013473, PubMed:39489739). Component of the HUSH2…

Subcellular location

Nucleus, Chromosome

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6V2SX-ray1.6 ÅA/B=55-116
9H77X-ray2.01 ÅC/D=53-117
7M5UX-ray2.02 ÅA=55-116
3LWEX-ray2.05 ÅA/B=55-116
3R93X-ray2.06 ÅA/B/C/D=55-116
3SVMX-ray2.31 ÅA=55-116
3QO2X-ray2.49 ÅA/B/C/D=55-116
8QFBX-ray3.04 ÅA/B/C/D/E/F/G/H=546-860

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