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"FOX-2" redirects here. For other uses, see Fox 2.
RNA binding protein, fox-1 homolog (C. elegans) 2
Protein RBM9 PDB 2cq3.png
PDB rendering based on 2cq3.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols RBFOX2 ; FOX2; Fox-2; HNRBP2; HRNBP2; RBM9; RTA; dJ106I20.3; fxh
External IDs OMIM612149 MGI1933973 HomoloGene49375 GeneCards: RBFOX2 Gene
RNA expression pattern
PBB GE RBM9 212104 s at tn.png
PBB GE RBM9 213901 x at tn.png
More reference expression data
Species Human Mouse
Entrez 23543 93686
Ensembl ENSG00000100320 ENSMUSG00000033565
UniProt O43251 Q8BP71
RefSeq (mRNA) NM_001031695 NM_001110827
RefSeq (protein) NP_001026865 NP_001104297
Location (UCSC) Chr 22:
36.13 – 36.42 Mb
Chr 15:
77.08 – 77.31 Mb
PubMed search [1] [2]

RNA binding motif protein 9, also known as RBM9 or FOX-2, is a protein which in humans is encoded by the RBM9 gene.[1]


RBM9 is one of several human genes similar to the C. elegans gene Fox-1. This gene encodes an RNA binding protein that is thought to be a key regulator of alternative exon splicing in the nervous system and other cell types. The protein binds to a conserved UGCAUG element found downstream of many alternatively spliced exons and promotes inclusion of the alternative exon in mature transcripts. The protein also interacts with the estrogen receptor 1 transcription factor and regulates estrogen receptor 1 transcriptional activity. Multiple transcript variants encoding different isoforms have been found for this gene.[1]

RBM9, as determined by CLIP-seq, binds near alternatively spliced exons and regulates the inclusion or exclusion of exons during alternative splicing by binding in introns either downstream (inclusion) or upstream (exon skipping) of exons. Its presence is important for stem cell survival and knockdowns of RBM9 activate markers for apoptosis.[2]


  1. ^ a b "Entrez Gene: RBM9 RNA binding motif protein 9". 
  2. ^ Yeo GW, Coufal NG, Liang TY, Peng GE, Fu XD, Gage FH (February 2009). "An RNA code for the FOX2 splicing regulator revealed by mapping RNA-protein interactions in stem cells". Nature Structural & Molecular Biology 16 (2): 130–137. doi:10.1038/nsmb.1545. PMC 2735254. PMID 19136955. 

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