RBFOX1

RNA binding protein, fox-1 homolog (C. elegans) 1
PDB rendering based on 2cq3.
Available structures PDB 2cq3, 2err
Identifiers
Symbols	RBFOX1; A2BP1; FOX-1; FOX1; HRNBP1
External IDs	OMIM: 605104 MGI: 1926224 HomoloGene: 69339 GeneCards: RBFOX1 Gene
Gene Ontology Molecular function • nucleotide binding • RNA binding • protein binding • protein C-terminus binding Cellular component • nucleus • cytoplasm • trans-Golgi network Biological process • mRNA processing • RNA splicing • RNA transport Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	54715	268859
Ensembl	ENSG00000078328	ENSMUSG00000008658
UniProt	Q9NWB1	Q3UYA8
RefSeq (mRNA)	NM_001142333.1	NM_021477
RefSeq (protein)	NP_001135805.1	NP_067452
Location (UCSC)	Chr 16: 6.37 – 7.76 Mb	Chr 16: 6.81 – 7.41 Mb
PubMed search	[1]	[2]

Fox-1 homolog A also known as ataxin 2-binding protein 1 (A2BP1) or hexaribonucleotide-binding protein 1 (HRNBP1) or RNA binding protein, fox-1 homolog (RBFOX1), is a protein that in humans is encoded by the RBFOX1 gene.

Function

Ataxin 2-binding protein 1 has an RNP motif that is highly conserved among RNA-binding proteins. This protein binds to the C-terminus of ataxin-2, and may contribute to the restricted pathology of spinocerebellar ataxia type 2 (SCA2). Ataxin-2 is the gene product of the SCA2 gene which causes familial neurodegenerative diseases. Ataxin 2-binding protein 1 and ataxin-2 are both localized in the trans-Golgi network. Four alternatively spliced transcript variants have been found for this gene. Additional transcript variants have been found but their full length nature has not been determined.

Further reading

• Shibata H, Huynh DP, Pulst SM (2000). "A novel protein with RNA-binding motifs interacts with ataxin-2.". Hum. Mol. Genet. 9 (9): 1303–13. doi:10.1093/hmg/9.9.1303. PMID 10814712. 
• Kiehl TR, Shibata H, Vo T, et al. (2002). "Identification and expression of a mouse ortholog of A2BP1.". Mamm. Genome 12 (8): 595–601. doi:10.1007/s00335-001-2056-4. PMID 11471052. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
• Underwood JG, Boutz PL, Dougherty JD, et al. (2005). "Homologues of the Caenorhabditis elegans Fox-1 protein are neuronal splicing regulators in mammals.". Mol. Cell. Biol. 25 (22): 10005–16. doi:10.1128/MCB.25.22.10005-10016.2005. PMC 1280273. PMID 16260614. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1280273. 
• Auweter SD, Fasan R, Reymond L, et al. (2006). "Molecular basis of RNA recognition by the human alternative splicing factor Fox-1.". EMBO J. 25 (1): 163–73. doi:10.1038/sj.emboj.7600918. PMC 1356361. PMID 16362037. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1356361. 
• Ponthier JL, Schluepen C, Chen W, et al. (2006). "Fox-2 splicing factor binds to a conserved intron motif to promote inclusion of protein 4.1R alternative exon 16.". J. Biol. Chem. 281 (18): 12468–74. doi:10.1074/jbc.M511556200. PMID 16537540. 
• Lim J, Hao T, Shaw C, et al. (2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration.". Cell 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569. 
• Zhou HL, Baraniak AP, Lou H (2007). "Role for Fox-1/Fox-2 in mediating the neuronal pathway of calcitonin/calcitonin gene-related peptide alternative RNA processing.". Mol. Cell. Biol. 27 (3): 830–41. doi:10.1128/MCB.01015-06. PMC 1800674. PMID 17101796. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1800674.