Q9UHX1: Poly(U)-binding-splicing factor PUF60 (PUF60)

Poly(U)-binding-splicing factor PUF60 (PUF60) is a 559-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9UHX1.

Gene
PUF60
Organism
Homo sapiens
Length
559 residues
Mean pLDDT
67.9
Model
AF-Q9UHX1-F1 v6
Model created
1 Aug 2025
PDB structures
16

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Model confidence (pLDDT)

The mean pLDDT of this model is 67.9 (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 accurate23%
70 to 90Confident: backbone generally right34%
50 to 70Low: treat with caution9%
Below 50Very low: often disordered regions34%

What pLDDT means and how to read it

Function

DNA- and RNA-binding protein, involved in several nuclear processes such as pre-mRNA splicing, apoptosis and transcription regulation. In association with FUBP1 regulates MYC transcription at the P2 promoter through the core-TFIIH basal transcription factor. Acts as a transcriptional repressor through the core-TFIIH basal transcription factor. Represses FUBP1-induced transcriptional activation but not basal transcription. Decreases ERCC3 helicase activity. Does not repress TFIIH-mediated transcription in xeroderma pigmentosum complementation group B (XPB) cells. Is also involved in pre-mRNA splicing. Promotes splicing of an intron with weak 3'-splice site and pyrimidine tract in a…

Subunit structure

Homodimer (PubMed:10606266). Associates with the spliceosome (PubMed:17579712). Found in a complex with RO60 and Y5 RNA (PubMed:10668799). Found in a complex with FUBP1 and far upstream element (FUSE) DNA segment (PubMed:10882074). Interacts directly with ERCC3 (PubMed:11239393). Interacts with CDK7 and GTF2H1 (PubMed:10882074). Interacts with SRSF11/P54 (PubMed:10606266). Does not interact with…

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
3UE2X-ray1.23 ÅA=443-559
3US5X-ray1.38 ÅA=443-559
7Z3XX-ray1.65 ÅA/B=114-308
5KW6X-ray1.91 ÅA/B=118-316
6SLOX-ray1.94 ÅA/B/C/D=460-559
5KVYX-ray1.95 ÅA/B=118-316
6LURX-ray2.0 ÅA/B/C/D/E/F/G/H=460-559
7Q8AX-ray2.05 ÅA/B=114-310
2QFJX-ray2.1 ÅA/B=118-316
5KW1X-ray2.1 ÅA/B=118-316
3DXBX-ray2.2 ÅA/B/C/D/E/F/G/H=460-559
3UWTX-ray2.5 ÅA=118-316
5KWQX-ray2.8 ÅA/B=118-316
2DNYNMRA=454-559
2KXFNMRA=119-314
2KXHNMRA=119-314

More AlphaFold highlights

About this viewer

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