Q91YE7: RNA-binding protein 5 (Rbm5)

RNA-binding protein 5 (Rbm5) is a 815-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q91YE7.

Gene
Rbm5
Organism
Mus musculus
Length
815 residues
Mean pLDDT
63.3
Model
AF-Q91YE7-F1 v6
Model created
1 Aug 2025
PDB structures
2

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Model confidence (pLDDT)

The mean pLDDT of this model is 63.3 (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 accurate7%
70 to 90Confident: backbone generally right42%
50 to 70Low: treat with caution12%
Below 50Very low: often disordered regions39%

What pLDDT means and how to read it

Function

Component of the spliceosome A complex. Binds to ssRNA containing the consensus sequence 5'-AGGUAA-3' (By similarity). Regulates alternative splicing of a number of mRNAs. May modulate splice site pairing after recruitment of the U1 and U2 snRNPs to the 5' and 3' splice sites of the intron. May both positively and negatively regulate apoptosis by regulating the alternative splicing of several genes involved in this process, including FAS and CASP2/caspase-2. In the case of FAS, promotes production of a soluble form of FAS that inhibits apoptosis. In the case of CASP2/caspase-2, promotes production of a catalytically active form of CASP2/Caspase-2 that induces apoptosis (By similarity)

Subunit structure

Component of the spliceosome A complex (also known as the prespliceosome). Appears to dissociate from the spliceosome upon formation of the spliceosome B complex (also known as the precatalytic spliceosome), in which the heterotrimeric U4/U6.U5 snRNPs are bound. Interacts with U2AF2; this interaction is direct. Also interacts with ACIN1, PRPF8, SFRS3, SNRPB, SNRPN, SNRNP70 and SNRNP200; these…

Subcellular location

Nucleus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2CLVX-ray1.9 ÅC/M=484-491
2OL3X-ray2.9 ÅP=484-491

More AlphaFold highlights

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