Q8NI27: THO complex subunit 2 (THOC2)

THO complex subunit 2 (THOC2) is a 1593-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8NI27.

Gene
THOC2
Organism
Homo sapiens
Length
1593 residues
Mean pLDDT
72.4
Model
AF-Q8NI27-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 72.4 (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 accurate33%
70 to 90Confident: backbone generally right35%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions27%

What pLDDT means and how to read it

Function

Component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA (PubMed:15833825, PubMed:15998806, PubMed:17190602). Required for efficient export of polyadenylated RNA and spliced mRNA (PubMed:23222130). The THOC1-THOC2-THOC3 core complex alone is sufficient to bind export factor NXF1-NXT1 and promote ATPase activity of DDX39B; in the complex THOC2 is the only component that directly interacts with DDX39B (PubMed:33191911). TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the…

Subunit structure

Component of the THO subcomplex, which is composed of THOC1, THOC2, THOC3, THOC5, THOC6 and THOC7 (PubMed:33191911, PubMed:37020021). The THO subcomplex interacts with DDX39B to form the THO-DDX39B complex which multimerizes into a 28-subunit tetrameric assembly (PubMed:33191911, PubMed:37020021). Component of the transcription/export (TREX) complex at least composed of ALYREF/THOC4, DDX39B,…

Subcellular location

Nucleus, Nucleus speckle, Cytoplasm

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7APKEM3.3 ÅB/J/b/j=1-1203
7ZNLEM3.45 ÅB/J/b/j=1-1593
7ZNKEM3.9 ÅB/J/b/j=1-1593
8R7LEM4.12 ÅB=1-1593

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