Q07955: Serine/arginine-rich splicing factor 1 (SRSF1)

Serine/arginine-rich splicing factor 1 (SRSF1) is a 248-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q07955.

Gene
SRSF1
Organism
Homo sapiens
Length
248 residues
Mean pLDDT
70.8
Model
AF-Q07955-F1 v6
Model created
1 Aug 2025
PDB structures
9

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Model confidence (pLDDT)

The mean pLDDT of this model is 70.8 (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 accurate38%
70 to 90Confident: backbone generally right22%
50 to 70Low: treat with caution6%
Below 50Very low: often disordered regions34%

What pLDDT means and how to read it

Function

Plays a role in preventing exon skipping, ensuring the accuracy of splicing and regulating alternative splicing. Interacts with other spliceosomal components, via the RS domains, to form a bridge between the 5'- and 3'-splice site binding components, U1 snRNP and U2AF. Can stimulate binding of U1 snRNP to a 5'-splice site-containing pre-mRNA. Binds to purine-rich RNA sequences, either the octamer, 5'-RGAAGAAC-3' (r=A or G) or the decamers, AGGACAGAGC/AGGACGAAGC. Binds preferentially to the 5'-CGAGGCG-3' motif in vitro. Three copies of the octamer constitute a powerful splicing enhancer in vitro, the ASF/SF2 splicing enhancer (ASE) which can specifically activate ASE-dependent splicing.…

Subunit structure

Consists of two polypeptides of p32 and p33. Identified in the spliceosome C complex (PubMed:11991638). Component of a ribonucleoprotein complex containing mRNAs and RNA-binding proteins including DDX5, HNRNPH2 and SRSF1 as well as splicing regulator ARVCF (PubMed:24644279). In vitro, self-associates and binds SRSF2, SNRNP70 and U2AF1 but not U2AF2. Binds SREK1/SFRS12. Interacts with SAFB/SAFB1.…

Subcellular location

Chromosome, Cytoplasm, Nucleus speckle

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4C0OX-ray2.56 ÅC/D=106-230
3BEGX-ray2.9 ÅB=105-219
8QO9EM5.29 Åz=1-248
7ABGEM7.8 ÅA6=1-248
1X4ANMRA=1-96
2M7SNMRA=106-195
2M8DNMRB=107-196
2O3DNMRA=107-215
6HPJNMRB=1-97

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