RFOX1_HUMAN
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 03-AUG-2022, entry version 180.
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; A0A0S2Z5K8: STRBP; NbExp=3; IntAct=EBI-12123390, EBI-16433759;
CC Q9NWB1-5; Q96SI9: STRBP; NbExp=3; IntAct=EBI-12123390, EBI-740355;
CC Q9NWB1-5; Q96LM6: TEX37; NbExp=3; IntAct=EBI-12123390, EBI-743976;
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};
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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. [Q9NWB1-1]
DR RefSeq; XP_016878827.1; XM_017023338.1. [Q9NWB1-3]
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 PDBsum; 2ERR; -.
DR PDBsum; 2N82; -.
DR PDBsum; 4ZKA; -.
DR AlphaFoldDB; Q9NWB1; -.
DR BMRB; Q9NWB1; -.
DR SMR; Q9NWB1; -.
DR BioGRID; 120107; 88.
DR IntAct; Q9NWB1; 79.
DR STRING; 9606.ENSP00000309117; -.
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; Q9NWB1; -.
DR PeptideAtlas; Q9NWB1; -.
DR PRIDE; 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 Antibodypedia; 24505; 389 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 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; DXNAFAP; -.
DR OrthoDB; 871288at2759; -.
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; 9 hits in 1067 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 170 other tissues.
DR ExpressionAtlas; Q9NWB1; baseline and differential.
DR Genevisible; Q9NWB1; HS.
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:0008022; F:protein C-terminus binding; IPI:UniProtKB.
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; RNA-bd_Fox-1.
DR InterPro; IPR000504; RRM_dom.
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; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
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
