ID RFOX1_HUMAN Reviewed; 397 AA. AC Q9NWB1; Q7Z7I7; Q8TAE3; Q8TAF2; Q8WYB2; Q9NS20; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 2. DT 27-MAR-2024, entry version 189. DE RecName: Full=RNA binding protein fox-1 homolog 1; DE AltName: Full=Ataxin-2-binding protein 1; DE AltName: Full=Fox-1 homolog A; DE AltName: Full=Hexaribonucleotide-binding protein 1; GN Name=RBFOX1; Synonyms=A2BP, A2BP1, FOX1, HRNBP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH ATXN2. RX PubMed=10814712; DOI=10.1093/hmg/9.9.1303; RA Shibata H., Huynh D.P., Pulst S.-M.; RT "A novel protein with RNA-binding motifs interacts with ataxin-2."; RL Hum. Mol. Genet. 9:1303-1313(2000). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 2; 4 AND 5). RA Chen W., Chu Z.-L., Blough R.I., Liu L., Hoppes B., Winkelmann J.C.; RT "Molecular cloning and chromosomal localization of a human brain, heart and RT skeletal muscle specific RNA binding protein gene homologous to fox-1 in RT Caenorhabditis elegans."; RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RA Yu L., Guo J., She X.; RT "An alternative splicing of a novel protein with RNA-binding motifs RT interacts with ataxin-2."; RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP FUNCTION. RX PubMed=16537540; DOI=10.1074/jbc.m511556200; RA Ponthier J.L., Schluepen C., Chen W., Lersch R.A., Gee S.L., Hou V.C., RA Lo A.J., Short S.A., Chasis J.A., Winkelmann J.C., Conboy J.G.; RT "Fox-2 splicing factor binds to a conserved intron motif to promote RT inclusion of protein 4.1R alternative exon 16."; RL J. Biol. Chem. 281:12468-12474(2006). RN [8] RP STRUCTURE BY NMR OF 109-196 IN COMPLEX WITH RNA, AND MUTAGENESIS OF RP HIS-120; PHE-126; PHE-158 AND PHE-160. RX PubMed=16362037; DOI=10.1038/sj.emboj.7600918; RA Auweter S.D., Fasan R., Reymond L., Underwood J.G., Black D.L., Pitsch S., RA Allain F.H.-T.; RT "Molecular basis of RNA recognition by the human alternative splicing RT factor Fox-1."; RL EMBO J. 25:163-173(2006). CC -!- FUNCTION: RNA-binding protein that regulates alternative splicing CC events by binding to 5'-UGCAUGU-3' elements. Regulates alternative CC splicing of tissue-specific exons and of differentially spliced exons CC during erythropoiesis. {ECO:0000269|PubMed:16537540}. CC -!- SUBUNIT: Binds to the C-terminus of ATXN2. CC {ECO:0000269|PubMed:16362037}. CC -!- INTERACTION: CC Q9NWB1; P54259: ATN1; NbExp=2; IntAct=EBI-945906, EBI-945980; CC Q9NWB1; P54253: ATXN1; NbExp=2; IntAct=EBI-945906, EBI-930964; CC Q9NWB1; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-945906, EBI-946029; CC Q9NWB1; Q9Y6R0: NUMBL; NbExp=2; IntAct=EBI-945906, EBI-945925; CC Q9NWB1; Q9HAU0: PLEKHA5; NbExp=2; IntAct=EBI-945906, EBI-945934; CC Q9NWB1; Q92530: PSMF1; NbExp=2; IntAct=EBI-945906, EBI-945916; CC Q9NWB1; Q96PU8: QKI; NbExp=2; IntAct=EBI-945906, EBI-945792; CC Q9NWB1; O43251: RBFOX2; NbExp=2; IntAct=EBI-945906, EBI-746056; CC Q9NWB1; Q93062: RBPMS; NbExp=3; IntAct=EBI-945906, EBI-740322; CC Q9NWB1-5; O95994: AGR2; NbExp=3; IntAct=EBI-12123390, EBI-712648; CC Q9NWB1-5; Q03989: ARID5A; NbExp=3; IntAct=EBI-12123390, EBI-948603; CC Q9NWB1-5; Q86V38: ATN1; NbExp=3; IntAct=EBI-12123390, EBI-11954292; CC Q9NWB1-5; P54253: ATXN1; NbExp=6; IntAct=EBI-12123390, EBI-930964; CC Q9NWB1-5; P0C7T5: ATXN1L; NbExp=3; IntAct=EBI-12123390, EBI-8624731; CC Q9NWB1-5; Q99700-5: ATXN2; NbExp=3; IntAct=EBI-12123390, EBI-25891409; CC Q9NWB1-5; O14503: BHLHE40; NbExp=3; IntAct=EBI-12123390, EBI-711810; CC Q9NWB1-5; P02489: CRYAA; NbExp=3; IntAct=EBI-12123390, EBI-6875961; CC Q9NWB1-5; Q15038: DAZAP2; NbExp=4; IntAct=EBI-12123390, EBI-724310; CC Q9NWB1-5; G5E9A7: DMWD; NbExp=3; IntAct=EBI-12123390, EBI-10976677; CC Q9NWB1-5; Q92567-2: FAM168A; NbExp=4; IntAct=EBI-12123390, EBI-11978259; CC Q9NWB1-5; P22607: FGFR3; NbExp=3; IntAct=EBI-12123390, EBI-348399; CC Q9NWB1-5; A0A024R5S0: hCG_2003792; NbExp=3; IntAct=EBI-12123390, EBI-10188461; CC Q9NWB1-5; Q92876: KLK6; NbExp=3; IntAct=EBI-12123390, EBI-2432309; CC Q9NWB1-5; Q14847-2: LASP1; NbExp=3; IntAct=EBI-12123390, EBI-9088686; CC Q9NWB1-5; P02545: LMNA; NbExp=3; IntAct=EBI-12123390, EBI-351935; CC Q9NWB1-5; Q7Z4N8: P4HA3; NbExp=3; IntAct=EBI-12123390, EBI-10181968; CC Q9NWB1-5; Q7Z3K3: POGZ; NbExp=5; IntAct=EBI-12123390, EBI-1389308; CC Q9NWB1-5; A0AV96: RBM47; NbExp=3; IntAct=EBI-12123390, EBI-2823850; CC Q9NWB1-5; Q93062-3: RBPMS; NbExp=4; IntAct=EBI-12123390, EBI-740343; CC Q9NWB1-5; Q6ZRY4: RBPMS2; NbExp=3; IntAct=EBI-12123390, EBI-11987469; CC Q9NWB1-5; O00241-2: SIRPB1; NbExp=3; IntAct=EBI-12123390, EBI-10179231; CC Q9NWB1-5; Q96LM6: SPMIP9; NbExp=3; IntAct=EBI-12123390, EBI-743976; CC Q9NWB1-5; A0A0S2Z5K8: STRBP; NbExp=3; IntAct=EBI-12123390, EBI-16433759; CC Q9NWB1-5; Q96SI9: STRBP; NbExp=3; IntAct=EBI-12123390, EBI-740355; CC Q9NWB1-5; Q9H0E2: TOLLIP; NbExp=3; IntAct=EBI-12123390, EBI-74615; CC Q9NWB1-5; Q86WV8: TSC1; NbExp=3; IntAct=EBI-12123390, EBI-12806590; CC Q9NWB1-5; O95164: UBL3; NbExp=3; IntAct=EBI-12123390, EBI-12876508; CC Q9NWB1-5; O95231: VENTX; NbExp=3; IntAct=EBI-12123390, EBI-10191303; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=Q9NWB1-1; Sequence=Displayed; CC Name=2; Synonyms=Gamma; CC IsoId=Q9NWB1-2; Sequence=VSP_030874, VSP_030876; CC Name=3; Synonyms=1; CC IsoId=Q9NWB1-3; Sequence=VSP_030875; CC Name=4; Synonyms=Alpha; CC IsoId=Q9NWB1-4; Sequence=VSP_030874, VSP_030876, VSP_030878; CC Name=5; Synonyms=Beta; CC IsoId=Q9NWB1-5; Sequence=VSP_030874, VSP_030876, VSP_030877; CC -!- TISSUE SPECIFICITY: Predominantly expressed in muscle and brain. CC -!- SEQUENCE CAUTION: CC Sequence=AAF78291.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF107203; AAF78291.1; ALT_INIT; mRNA. DR EMBL; AF229057; AAL71904.1; -; mRNA. DR EMBL; AF094849; AAL83405.1; -; mRNA. DR EMBL; AF109106; AAL83406.1; -; mRNA. DR EMBL; AF109120; AAL83407.1; -; Genomic_DNA. DR EMBL; AF109107; AAL83407.1; JOINED; Genomic_DNA. DR EMBL; AF109108; AAL83407.1; JOINED; Genomic_DNA. DR EMBL; AF109109; AAL83407.1; JOINED; Genomic_DNA. DR EMBL; AF109110; AAL83407.1; JOINED; Genomic_DNA. DR EMBL; AF109111; AAL83407.1; JOINED; Genomic_DNA. DR EMBL; AF109112; AAL83407.1; JOINED; Genomic_DNA. DR EMBL; AF109113; AAL83407.1; JOINED; Genomic_DNA. DR EMBL; AF109114; AAL83407.1; JOINED; Genomic_DNA. DR EMBL; AF109115; AAL83407.1; JOINED; Genomic_DNA. DR EMBL; AF109116; AAL83407.1; JOINED; Genomic_DNA. DR EMBL; AF109117; AAL83407.1; JOINED; Genomic_DNA. DR EMBL; AF109118; AAL83407.1; JOINED; Genomic_DNA. DR EMBL; AF109119; AAL83407.1; JOINED; Genomic_DNA. DR EMBL; AF109120; AAL83408.1; -; Genomic_DNA. DR EMBL; AF109107; AAL83408.1; JOINED; Genomic_DNA. DR EMBL; AF109108; AAL83408.1; JOINED; Genomic_DNA. DR EMBL; AF109109; AAL83408.1; JOINED; Genomic_DNA. DR EMBL; AF109110; AAL83408.1; JOINED; Genomic_DNA. DR EMBL; AF109111; AAL83408.1; JOINED; Genomic_DNA. DR EMBL; AF109112; AAL83408.1; JOINED; Genomic_DNA. DR EMBL; AF109113; AAL83408.1; JOINED; Genomic_DNA. DR EMBL; AF109114; AAL83408.1; JOINED; Genomic_DNA. DR EMBL; AF109115; AAL83408.1; JOINED; Genomic_DNA. DR EMBL; AF109116; AAL83408.1; JOINED; Genomic_DNA. DR EMBL; AF109117; AAL83408.1; JOINED; Genomic_DNA. DR EMBL; AF109119; AAL83408.1; JOINED; Genomic_DNA. DR EMBL; AF109120; AAL83409.1; -; Genomic_DNA. DR EMBL; AF109107; AAL83409.1; JOINED; Genomic_DNA. DR EMBL; AF109108; AAL83409.1; JOINED; Genomic_DNA. DR EMBL; AF109109; AAL83409.1; JOINED; Genomic_DNA. DR EMBL; AF109110; AAL83409.1; JOINED; Genomic_DNA. DR EMBL; AF109111; AAL83409.1; JOINED; Genomic_DNA. DR EMBL; AF109112; AAL83409.1; JOINED; Genomic_DNA. DR EMBL; AF109113; AAL83409.1; JOINED; Genomic_DNA. DR EMBL; AF109114; AAL83409.1; JOINED; Genomic_DNA. DR EMBL; AF109115; AAL83409.1; JOINED; Genomic_DNA. DR EMBL; AF109116; AAL83409.1; JOINED; Genomic_DNA. DR EMBL; AF109117; AAL83409.1; JOINED; Genomic_DNA. DR EMBL; AF109119; AAL83409.1; JOINED; Genomic_DNA. DR EMBL; AF448859; AAP41925.1; -; mRNA. DR EMBL; AK001027; BAA91472.1; -; mRNA. DR EMBL; AC005774; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC006075; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC006112; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC007012; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC007217; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC007222; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC007223; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC009135; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC022206; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC023829; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC027683; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC079410; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC125796; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC131390; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC113691; AAI13692.1; -; mRNA. DR CCDS; CCDS10531.1; -. [Q9NWB1-2] DR CCDS; CCDS10532.1; -. [Q9NWB1-5] DR CCDS; CCDS45405.1; -. [Q9NWB1-4] DR CCDS; CCDS55983.1; -. [Q9NWB1-1] DR CCDS; CCDS55984.1; -. [Q9NWB1-3] DR RefSeq; NP_001135805.1; NM_001142333.1. [Q9NWB1-3] DR RefSeq; NP_001135806.1; NM_001142334.1. [Q9NWB1-1] DR RefSeq; NP_061193.2; NM_018723.3. [Q9NWB1-1] DR RefSeq; NP_665898.1; NM_145891.2. [Q9NWB1-2] DR RefSeq; NP_665899.1; NM_145892.2. [Q9NWB1-4] DR RefSeq; NP_665900.1; NM_145893.2. [Q9NWB1-5] DR RefSeq; XP_016878822.1; XM_017023333.1. DR RefSeq; XP_016878827.1; XM_017023338.1. DR PDB; 2ERR; NMR; -; A=109-196. DR PDB; 2N82; NMR; -; B=109-208. DR PDB; 4ZKA; X-ray; 1.80 A; A/B/C/D/E/F=109-208. DR PDB; 7VRL; NMR; -; B=109-208. DR PDBsum; 2ERR; -. DR PDBsum; 2N82; -. DR PDBsum; 4ZKA; -. DR PDBsum; 7VRL; -. DR AlphaFoldDB; Q9NWB1; -. DR BMRB; Q9NWB1; -. DR SMR; Q9NWB1; -. DR BioGRID; 120107; 93. DR IntAct; Q9NWB1; 81. DR MINT; Q9NWB1; -. DR STRING; 9606.ENSP00000391269; -. DR iPTMnet; Q9NWB1; -. DR PhosphoSitePlus; Q9NWB1; -. DR BioMuta; RBFOX1; -. DR DMDM; 166897979; -. DR EPD; Q9NWB1; -. DR jPOST; Q9NWB1; -. DR MassIVE; Q9NWB1; -. DR MaxQB; Q9NWB1; -. DR PaxDb; 9606-ENSP00000309117; -. DR PeptideAtlas; Q9NWB1; -. DR ProteomicsDB; 82917; -. [Q9NWB1-1] DR ProteomicsDB; 82918; -. [Q9NWB1-2] DR ProteomicsDB; 82919; -. [Q9NWB1-3] DR ProteomicsDB; 82920; -. [Q9NWB1-4] DR ProteomicsDB; 82921; -. [Q9NWB1-5] DR Pumba; Q9NWB1; -. DR Antibodypedia; 24505; 427 antibodies from 32 providers. DR DNASU; 54715; -. DR Ensembl; ENST00000311745.9; ENSP00000309117.5; ENSG00000078328.23. [Q9NWB1-2] DR Ensembl; ENST00000355637.9; ENSP00000347855.4; ENSG00000078328.23. [Q9NWB1-5] DR Ensembl; ENST00000436368.6; ENSP00000402745.2; ENSG00000078328.23. [Q9NWB1-4] DR Ensembl; ENST00000547338.5; ENSP00000447717.1; ENSG00000078328.23. [Q9NWB1-1] DR Ensembl; ENST00000550418.6; ENSP00000450031.1; ENSG00000078328.23. [Q9NWB1-1] DR Ensembl; ENST00000553186.5; ENSP00000447753.1; ENSG00000078328.23. [Q9NWB1-3] DR Ensembl; ENST00000675653.1; ENSP00000502718.1; ENSG00000078328.23. [Q9NWB1-1] DR Ensembl; ENST00000675842.1; ENSP00000501599.1; ENSG00000078328.23. [Q9NWB1-1] DR GeneID; 54715; -. DR KEGG; hsa:54715; -. DR MANE-Select; ENST00000550418.6; ENSP00000450031.1; NM_018723.4; NP_061193.2. DR UCSC; uc002cys.2; human. [Q9NWB1-1] DR AGR; HGNC:18222; -. DR CTD; 54715; -. DR DisGeNET; 54715; -. DR GeneCards; RBFOX1; -. DR HGNC; HGNC:18222; RBFOX1. DR HPA; ENSG00000078328; Tissue enhanced (brain, skeletal muscle, tongue). DR MalaCards; RBFOX1; -. DR MIM; 605104; gene. DR neXtProt; NX_Q9NWB1; -. DR OpenTargets; ENSG00000078328; -. DR VEuPathDB; HostDB:ENSG00000078328; -. DR eggNOG; KOG0125; Eukaryota. DR GeneTree; ENSGT00940000160685; -. DR InParanoid; Q9NWB1; -. DR OMA; MNCLSSQ; -. DR OrthoDB; 5406502at2759; -. DR PhylomeDB; Q9NWB1; -. DR TreeFam; TF315942; -. DR PathwayCommons; Q9NWB1; -. DR Reactome; R-HSA-9022707; MECP2 regulates transcription factors. DR SignaLink; Q9NWB1; -. DR SIGNOR; Q9NWB1; -. DR BioGRID-ORCS; 54715; 11 hits in 1146 CRISPR screens. DR ChiTaRS; RBFOX1; human. DR EvolutionaryTrace; Q9NWB1; -. DR GeneWiki; RBFOX1; -. DR GenomeRNAi; 54715; -. DR Pharos; Q9NWB1; Tbio. DR PRO; PR:Q9NWB1; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q9NWB1; Protein. DR Bgee; ENSG00000078328; Expressed in middle temporal gyrus and 172 other cell types or tissues. DR ExpressionAtlas; Q9NWB1; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:FlyBase. DR GO; GO:0097165; C:nuclear stress granule; IDA:FlyBase. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB. DR GO; GO:0003730; F:mRNA 3'-UTR binding; IEA:Ensembl. DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; NAS:UniProtKB. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. DR GO; GO:0007399; P:nervous system development; IBA:GO_Central. DR GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl. DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IBA:GO_Central. DR GO; GO:2001014; P:regulation of skeletal muscle cell differentiation; IEA:Ensembl. DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. DR GO; GO:0050658; P:RNA transport; NAS:UniProtKB. DR CDD; cd12407; RRM_FOX1_like; 1. DR Gene3D; 3.30.70.330; -; 1. DR InterPro; IPR025670; Fox-1_C_dom. DR InterPro; IPR034237; FOX1_RRM. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR017325; RBFOX1-3. DR InterPro; IPR047131; RBFOX1-like. DR InterPro; IPR000504; RRM_dom. DR PANTHER; PTHR15597; ATAXIN 2-BINDING PROTEIN 1-RELATED; 1. DR PANTHER; PTHR15597:SF26; RNA BINDING PROTEIN FOX-1 HOMOLOG 1; 1. DR Pfam; PF12414; Fox-1_C; 1. DR Pfam; PF00076; RRM_1; 1. DR PIRSF; PIRSF037932; Ataxin_2_bd_A2BP; 1. DR SMART; SM00360; RRM; 1. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1. DR PROSITE; PS50102; RRM; 1. DR Genevisible; Q9NWB1; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Methylation; KW mRNA processing; mRNA splicing; Nucleus; Reference proteome; RNA-binding. FT CHAIN 1..397 FT /note="RNA binding protein fox-1 homolog 1" FT /id="PRO_0000081480" FT DOMAIN 117..193 FT /note="RRM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT REGION 1..121 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 55..119 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 118 FT /note="Interaction with RNA" FT SITE 126 FT /note="Interaction with RNA" FT SITE 127 FT /note="Interaction with RNA" FT SITE 151 FT /note="Interaction with RNA" FT SITE 156 FT /note="Interaction with RNA" FT SITE 160 FT /note="Interaction with RNA" FT SITE 184 FT /note="Interaction with RNA" FT SITE 194 FT /note="Interaction with RNA" FT MOD_RES 317 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0000250|UniProtKB:Q9JJ43" FT MOD_RES 388 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q9JJ43" FT VAR_SEQ 1..9 FT /note="MNCEREQLR -> MLASQGVLLHPYGVPMIVPAAPYLPGLIQ (in FT isoform 2, isoform 4 and isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2" FT /id="VSP_030874" FT VAR_SEQ 226..253 FT /note="GTVLLCQANQEGSSMYSAPSSLVYTSAM -> V (in isoform 3)" FT /evidence="ECO:0000303|PubMed:10814712, FT ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3" FT /id="VSP_030875" FT VAR_SEQ 302..310 FT /note="DGFYGADIY -> EPVYGNKLLQ (in isoform 2, isoform 4 and FT isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2" FT /id="VSP_030876" FT VAR_SEQ 332..397 FT /note="SYGRVYAADPYHHALAPAPTYGVGAMNAFAPLTDAKTRSHADDVGLVLSSLQ FT ASIYRGGYNRFAPY -> RNQFVFVAADEISCNTSAVTDEFMLPTPTTTHLLQPPPTAL FT VP (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2" FT /id="VSP_030877" FT VAR_SEQ 358..383 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_030878" FT MUTAGEN 120 FT /note="H->A: Reduces RNA-binding affinity 160-fold." FT /evidence="ECO:0000269|PubMed:16362037" FT MUTAGEN 126 FT /note="F->A,I,R: Reduces RNA-binding affinity 1500-fold." FT /evidence="ECO:0000269|PubMed:16362037" FT MUTAGEN 126 FT /note="F->H,W: Reduces RNA-binding affinity 15-fold." FT /evidence="ECO:0000269|PubMed:16362037" FT MUTAGEN 126 FT /note="F->Y: No effect on RNA-binding." FT /evidence="ECO:0000269|PubMed:16362037" FT MUTAGEN 158 FT /note="F->A: Reduces RNA-binding affinity 700-fold." FT /evidence="ECO:0000269|PubMed:16362037" FT MUTAGEN 160 FT /note="F->A: Reduces RNA-binding affinity 30'000-fold." FT /evidence="ECO:0000269|PubMed:16362037" FT CONFLICT 92 FT /note="T -> A (in Ref. 4; BAA91472)" FT /evidence="ECO:0000305" FT TURN 110..112 FT /evidence="ECO:0007829|PDB:2N82" FT STRAND 117..123 FT /evidence="ECO:0007829|PDB:4ZKA" FT HELIX 130..138 FT /evidence="ECO:0007829|PDB:4ZKA" FT STRAND 143..151 FT /evidence="ECO:0007829|PDB:4ZKA" FT STRAND 154..165 FT /evidence="ECO:0007829|PDB:4ZKA" FT HELIX 166..176 FT /evidence="ECO:0007829|PDB:4ZKA" FT STRAND 187..190 FT /evidence="ECO:0007829|PDB:4ZKA" FT HELIX 204..206 FT /evidence="ECO:0007829|PDB:2N82" SQ SEQUENCE 397 AA; 42784 MW; EA96AA7B6E144D80 CRC64; MNCEREQLRG NQEAAAAPDT MAQPYASAQF APPQNGIPAE YTAPHPHPAP EYTGQTTVPE HTLNLYPPAQ THSEQSPADT SAQTVSGTAT QTDDAAPTDG QPQTQPSENT ENKSQPKRLH VSNIPFRFRD PDLRQMFGQF GKILDVEIIF NERGSKGFGF VTFENSADAD RAREKLHGTV VEGRKIEVNN ATARVMTNKK TVNPYTNGWK LNPVVGAVYS PEFYAGTVLL CQANQEGSSM YSAPSSLVYT SAMPGFPYPA ATAAAAYRGA HLRGRGRTVY NTFRAAAPPP PIPAYGGVVY QDGFYGADIY GGYAAYRYAQ PTPATAAAYS DSYGRVYAAD PYHHALAPAP TYGVGAMNAF APLTDAKTRS HADDVGLVLS SLQASIYRGG YNRFAPY //