Q96QT6: PHD finger protein 12 (PHF12)

PHD finger protein 12 (PHF12) is a 1004-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q96QT6.

Gene
PHF12
Organism
Homo sapiens
Length
1004 residues
Mean pLDDT
55.2
Model
AF-Q96QT6-F1 v6
Model created
1 Aug 2025
PDB structures
6

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Model confidence (pLDDT)

The mean pLDDT of this model is 55.2 (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 accurate6%
70 to 90Confident: backbone generally right26%
50 to 70Low: treat with caution17%
Below 50Very low: often disordered regions52%

What pLDDT means and how to read it

Function

Transcriptional repressor acting as key scaffolding subunit of SIN3 complexes which contributes to complex assembly by contacting each core subunit domain, stabilizes the complex and constitutes the substrate receptor by recruiting the H3 histone tail (PubMed:37137925). SIN3 complexes are composed of a SIN3 scaffold subunit, one catalytic core (HDAC1 or HDAC2) and 2 chromatin targeting modules (PubMed:11390640, PubMed:37137925). SIN3B complex represses transcription and counteracts the histone acetyltransferase activity of EP300 through the recognition H3K27ac marks by PHF12 and the activity of the histone deacetylase HDAC2 (PubMed:37137925). SIN3B complex is recruited downstream of the…

Subunit structure

Component of SIN3 complexes (PubMed:11390640, PubMed:37137925). Interacts with SIN3A in a complex composed of HDAC1, SAP30 and SIN3A (PubMed:11390640). Component of the SIN3B complex, which includes SIN3B, HDAC2 or HDAC1, PHF12 and MORF4L1; interacts directly with all subunits (PubMed:21041482, PubMed:37137925). Interacts with TLE5 (PubMed:11390640)

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8BPBEM2.8 ÅC=1-364
8BPCEM2.8 ÅC=1-364
8C60EM3.4 ÅC=1-1004
8BPAEM3.7 ÅC=1-1004
2L9SNMRA=200-241
2LKMNMRA=200-241

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