Q13263: Transcription intermediary factor 1-beta (TRIM28)

Transcription intermediary factor 1-beta (TRIM28) is a 835-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13263.

Gene
TRIM28
Organism
Homo sapiens
Length
835 residues
Mean pLDDT
65.1
Model
AF-Q13263-F1 v6
Model created
1 Aug 2025
PDB structures
10

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Model confidence (pLDDT)

The mean pLDDT of this model is 65.1 (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 accurate24%
70 to 90Confident: backbone generally right28%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions39%

What pLDDT means and how to read it

Function

E3 SUMO and ubiquitin ligase that plays a pivotal role in embryonic development, genomic imprinting, and maintenance of genomic stability through repression of repetitive and retroviral elements. Also involved in DNA repair, regulation of innate immunity or cellular energy homeostasis. Acts as a scaffold for assembling transcriptional repression complexes containing methyltransferases, histone deacetylases, and chromatin remodelers. Serves as a nuclear corepressor for KRAB domain-containing zinc finger proteins (KRAB-ZFPs), mediating gene silencing by recruiting CHD3, a subunit of the nucleosome remodeling and deacetylation (NuRD) complex, and SETDB1, which methylates histone H3 at 'Lys-9'…

Subunit structure

Interacts with SETX (PubMed:23149945). Oligomer; the RBCC domain homotrimerizes and interacts with one molecule of KRAB to form the KRAB-KAP1 corepressor complex. Binding to a KRAB domain is an absolute requirement for silencing gene expression. Interacts with CEBPB and NR3C1. Interacts with a number of KRAB-ZFP proteins including ZNF10, ZFP53, ZFP68, ZNF382 and ZNF256. Interacts with NCOR1,…

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
9OSCX-ray1.77 ÅC=483-493
2YVRX-ray1.8 ÅA/B=201-250
9CDWX-ray2.4 ÅE/F=485-490
7Z36X-ray2.8 ÅA/B=56-413
6QAJX-ray2.9 ÅA/B=56-413
6QU1X-ray3.7 ÅA=53-434
6H3AX-ray5.5 ÅA/F=53-434
1FP0NMRA=619-679
2RO1NMRA=624-812
6I9HNMRA=54-145

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