P26368: Splicing factor U2AF 65 kDa subunit (U2AF2)

Splicing factor U2AF 65 kDa subunit (U2AF2) is a 475-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P26368.

Gene
U2AF2
Organism
Homo sapiens
Length
475 residues
Mean pLDDT
73.2
Model
AF-P26368-F1 v6
Model created
1 Aug 2025
PDB structures
40

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Model confidence (pLDDT)

The mean pLDDT of this model is 73.2 (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 accurate31%
70 to 90Confident: backbone generally right33%
50 to 70Low: treat with caution11%
Below 50Very low: often disordered regions25%

What pLDDT means and how to read it

Function

Plays a role in pre-mRNA splicing and 3'-end processing (PubMed:17024186). By recruiting PRPF19 and the PRP19C/Prp19 complex/NTC/Nineteen complex to the RNA polymerase II C-terminal domain (CTD), and thereby pre-mRNA, may couple transcription to splicing (PubMed:21536736). Induces cardiac troponin-T (TNNT2) pre-mRNA exon inclusion in muscle. Regulates the TNNT2 exon 5 inclusion through competition with MBNL1. Binds preferentially to a single-stranded structure within the polypyrimidine tract of TNNT2 intron 4 during spliceosome assembly. Required for the export of mRNA out of the nucleus, even if the mRNA is encoded by an intron-less gene. Represses the splicing of MAPT/Tau exon 10.…

Subunit structure

Interacts with U2AF1L4 (By similarity). Heterodimer with U2AF1 (PubMed:11551507). Binds unphosphorylated SF1 (PubMed:10449420, PubMed:12718882). Interacts with SCAF11 and SNW1 (PubMed:21460037, PubMed:9447963). Interacts with ZRSR2/U2AF1-RS2. Interacts with RBM17 (PubMed:17589525). Interacts with PRPF19; the interaction is direct. Interacts with POLR2A (via the C-terminal domain); recruits…

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
5W0GX-ray1.07 ÅA=148-229
5W0HX-ray1.11 ÅA=258-336
6XLVX-ray1.4 ÅA=141-341
9C7AX-ray1.4 ÅA=141-341
9C7BX-ray1.4 ÅA=141-341
2HZCX-ray1.47 ÅA=148-229
7S3AX-ray1.48 ÅA=141-341
5EV3X-ray1.5 ÅA=141-341
6XLWX-ray1.5 ÅA=141-341
7S3CX-ray1.51 ÅA=141-341
5EV4X-ray1.57 ÅA=141-341
6XLXX-ray1.7 ÅA=141-341
7SN6X-ray1.8 ÅA/B=375-475
5EV2X-ray1.86 ÅA=141-341
7S3BX-ray1.89 ÅA=141-341
3VAJX-ray1.9 ÅA/B=148-336
4TU8X-ray1.92 ÅA/B=148-336
4TU9X-ray1.99 ÅA/B=148-336
5EV1X-ray2.04 ÅA=141-341
4TU7X-ray2.09 ÅA/B=148-336

Showing 20 of 40 experimental structures (best resolution first).

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