RFOX2_HUMAN
ID RFOX2_HUMAN Reviewed; 390 AA.
AC O43251; A4F5G8; A8K5Z5; B0QYY8; B0QYY9; Q0PRL5; Q0VH35; Q5TF71; Q6IC09;
AC Q8TD00; Q8WYB1; Q96DZ6; Q96NL7; Q9UGW4; Q9UH33;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 11-APR-2003, sequence version 3.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=RNA binding protein fox-1 homolog 2;
DE AltName: Full=Fox-1 homolog B;
DE AltName: Full=Hexaribonucleotide-binding protein 2;
DE AltName: Full=RNA-binding motif protein 9;
DE AltName: Full=RNA-binding protein 9;
DE AltName: Full=Repressor of tamoxifen transcriptional activity;
GN Name=RBFOX2; Synonyms=FOX2, HRNBP2, RBM9, RTA;
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), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11875103; DOI=10.1210/mend.16.3.0787;
RA Norris J.D., Fan D., Sherk A., McDonnell D.P.;
RT "A negative coregulator for the human ER.";
RL Mol. Endocrinol. 16:459-468(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 10).
RA Chen W., Winkelmann J.C.;
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RA Yang G., Huang S.C., Benz E.J. Jr.;
RT "A novel isoform of RNA binding motif protein 9.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9).
RC TISSUE=Placenta;
RX PubMed=12529303; DOI=10.1101/gr.695703;
RA Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S.,
RA Bye J.M., Beare D.M., Dunham I.;
RT "Reevaluating human gene annotation: a second-generation analysis of
RT chromosome 22.";
RL Genome Res. 13:27-36(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 6).
RC TISSUE=Brain;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
RA Zhou G., Nong W., Li H., Ke R., Shen C., Liang M., Tang Z., Huang B.,
RA Lin L., Yang S.;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 10).
RC TISSUE=Adrenal gland, and Uterus;
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 [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-390 (ISOFORM 7).
RA Papin C.;
RT "XRbm9, a new XGld2-interacting protein, enhances translation in Xenopus
RT oocytes.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-67 (ISOFORMS 6 AND 8), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-329, METHYLATION [LARGE SCALE
RP ANALYSIS] AT ARG-249 (ISOFORM 3), METHYLATION [LARGE SCALE ANALYSIS] AT
RP ARG-267 (ISOFORM 5), METHYLATION [LARGE SCALE ANALYSIS] AT ARG-277 (ISOFORM
RP 7), METHYLATION [LARGE SCALE ANALYSIS] AT ARG-268 (ISOFORM 9), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [14]
RP STRUCTURE BY NMR OF 113-202.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RNA binding domain in RNA binding motif protein 9.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: RNA-binding protein that regulates alternative splicing
CC events by binding to 5'-UGCAUGU-3' elements. Prevents binding of U2AF2
CC to the 3'-splice site. Regulates alternative splicing of tissue-
CC specific exons and of differentially spliced exons during
CC erythropoiesis (By similarity). RNA-binding protein that seems to act
CC as a coregulatory factor of ER-alpha. {ECO:0000250,
CC ECO:0000269|PubMed:11875103}.
CC -!- SUBUNIT: Interacts with ER-alpha N-terminal activation domain.
CC -!- INTERACTION:
CC O43251; P54253: ATXN1; NbExp=10; IntAct=EBI-746056, EBI-930964;
CC O43251; Q8N9W6: BOLL; NbExp=4; IntAct=EBI-746056, EBI-998198;
CC O43251; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-746056, EBI-946029;
CC O43251; Q13554: CAMK2B; NbExp=3; IntAct=EBI-746056, EBI-1058722;
CC O43251; O75553: DAB1; NbExp=3; IntAct=EBI-746056, EBI-7875264;
CC O43251; Q15038: DAZAP2; NbExp=4; IntAct=EBI-746056, EBI-724310;
CC O43251; P03372: ESR1; NbExp=4; IntAct=EBI-746056, EBI-78473;
CC O43251; P52597: HNRNPF; NbExp=4; IntAct=EBI-746056, EBI-352986;
CC O43251; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-746056, EBI-716006;
CC O43251; Q8NDC0: MAPK1IP1L; NbExp=3; IntAct=EBI-746056, EBI-741424;
CC O43251; Q96HR8: NAF1; NbExp=3; IntAct=EBI-746056, EBI-2515597;
CC O43251; P25788: PSMA3; NbExp=3; IntAct=EBI-746056, EBI-348380;
CC O43251; Q96PU8: QKI; NbExp=3; IntAct=EBI-746056, EBI-945792;
CC O43251; Q9NWB1: RBFOX1; NbExp=2; IntAct=EBI-746056, EBI-945906;
CC O43251; Q9BQY4: RHOXF2; NbExp=3; IntAct=EBI-746056, EBI-372094;
CC O43251; O76064: RNF8; NbExp=3; IntAct=EBI-746056, EBI-373337;
CC O43251; Q08AM6: VAC14; NbExp=4; IntAct=EBI-746056, EBI-2107455;
CC O43251-3; P42858: HTT; NbExp=3; IntAct=EBI-11531589, EBI-466029;
CC O43251-6; A0A142I5B9; Xeno; NbExp=3; IntAct=EBI-10987522, EBI-20625235;
CC O43251-10; P54253: ATXN1; NbExp=3; IntAct=EBI-11963050, EBI-930964;
CC O43251-10; P0C7T5: ATXN1L; NbExp=3; IntAct=EBI-11963050, EBI-8624731;
CC O43251-10; Q8N9W6-4: BOLL; NbExp=3; IntAct=EBI-11963050, EBI-11983447;
CC O43251-10; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-11963050, EBI-1383687;
CC O43251-10; Q8IWX8: CHERP; NbExp=3; IntAct=EBI-11963050, EBI-2555370;
CC O43251-10; Q15038: DAZAP2; NbExp=4; IntAct=EBI-11963050, EBI-724310;
CC O43251-10; A1KXE4-2: FAM168B; NbExp=3; IntAct=EBI-11963050, EBI-12193763;
CC O43251-10; P52597: HNRNPF; NbExp=3; IntAct=EBI-11963050, EBI-352986;
CC O43251-10; P31943: HNRNPH1; NbExp=3; IntAct=EBI-11963050, EBI-351590;
CC O43251-10; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-11963050, EBI-11962084;
CC O43251-10; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-11963050, EBI-716006;
CC O43251-10; Q8TDS5: OXER1; NbExp=3; IntAct=EBI-11963050, EBI-12813389;
CC O43251-10; Q15365: PCBP1; NbExp=3; IntAct=EBI-11963050, EBI-946095;
CC O43251-10; Q93062-3: RBPMS; NbExp=3; IntAct=EBI-11963050, EBI-740343;
CC O43251-10; Q6ZRY4: RBPMS2; NbExp=5; IntAct=EBI-11963050, EBI-11987469;
CC O43251-10; Q9BQY4: RHOXF2; NbExp=3; IntAct=EBI-11963050, EBI-372094;
CC O43251-10; O76064: RNF8; NbExp=3; IntAct=EBI-11963050, EBI-373337;
CC O43251-10; Q96LM6: TEX37; NbExp=3; IntAct=EBI-11963050, EBI-743976;
CC O43251-10; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-11963050, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=10;
CC Name=1;
CC IsoId=O43251-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43251-2; Sequence=VSP_007180, VSP_030890;
CC Name=3;
CC IsoId=O43251-3; Sequence=VSP_007180, VSP_007181, VSP_007182;
CC Name=4;
CC IsoId=O43251-4; Sequence=VSP_007180, VSP_007183;
CC Name=5;
CC IsoId=O43251-5; Sequence=VSP_007180, VSP_007182;
CC Name=6;
CC IsoId=O43251-6; Sequence=VSP_030889;
CC Name=7;
CC IsoId=O43251-7; Sequence=VSP_007182, VSP_030891;
CC Name=8;
CC IsoId=O43251-8; Sequence=VSP_030889, VSP_030890;
CC Name=9;
CC IsoId=O43251-9; Sequence=VSP_007180, VSP_030890, VSP_007182,
CC VSP_007183;
CC Name=10;
CC IsoId=O43251-10; Sequence=VSP_007180;
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DR EMBL; AY072786; AAL67150.1; -; mRNA.
DR EMBL; AF229058; AAL71905.1; -; mRNA.
DR EMBL; AY960684; AAX84843.1; -; mRNA.
DR EMBL; AL009266; CAA15842.1; -; mRNA.
DR EMBL; CR456559; CAG30445.1; -; mRNA.
DR EMBL; AK055213; BAB70875.1; -; mRNA.
DR EMBL; AK291460; BAF84149.1; -; mRNA.
DR EMBL; DQ778625; ABG77459.1; -; mRNA.
DR EMBL; AL049748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL079295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013115; AAH13115.1; -; mRNA.
DR EMBL; BC025281; AAH25281.1; -; mRNA.
DR EMBL; AM419009; CAL91352.1; -; mRNA.
DR CCDS; CCDS13921.1; -. [O43251-9]
DR CCDS; CCDS43013.1; -. [O43251-8]
DR CCDS; CCDS46699.1; -. [O43251-4]
DR CCDS; CCDS46700.1; -. [O43251-10]
DR CCDS; CCDS46701.1; -. [O43251-5]
DR RefSeq; NP_001026865.1; NM_001031695.2. [O43251-10]
DR RefSeq; NP_001076045.1; NM_001082576.1. [O43251-5]
DR RefSeq; NP_001076046.1; NM_001082577.1. [O43251-4]
DR RefSeq; NP_001076047.1; NM_001082578.1. [O43251-8]
DR RefSeq; NP_055124.1; NM_014309.2. [O43251-9]
DR RefSeq; XP_005261494.1; XM_005261437.1.
DR PDB; 2CQ3; NMR; -; A=113-202.
DR PDBsum; 2CQ3; -.
DR AlphaFoldDB; O43251; -.
DR SMR; O43251; -.
DR BioGRID; 117087; 279.
DR IntAct; O43251; 126.
DR MINT; O43251; -.
DR STRING; 9606.ENSP00000413035; -.
DR iPTMnet; O43251; -.
DR PhosphoSitePlus; O43251; -.
DR BioMuta; RBFOX2; -.
DR EPD; O43251; -.
DR jPOST; O43251; -.
DR MassIVE; O43251; -.
DR MaxQB; O43251; -.
DR PaxDb; O43251; -.
DR PeptideAtlas; O43251; -.
DR PRIDE; O43251; -.
DR ProteomicsDB; 48827; -. [O43251-1]
DR ProteomicsDB; 48828; -. [O43251-10]
DR ProteomicsDB; 48829; -. [O43251-2]
DR ProteomicsDB; 48830; -. [O43251-3]
DR ProteomicsDB; 48831; -. [O43251-4]
DR ProteomicsDB; 48832; -. [O43251-5]
DR ProteomicsDB; 48833; -. [O43251-6]
DR ProteomicsDB; 48834; -. [O43251-7]
DR ProteomicsDB; 48835; -. [O43251-8]
DR ProteomicsDB; 48836; -. [O43251-9]
DR Antibodypedia; 331; 259 antibodies from 27 providers.
DR DNASU; 23543; -.
DR Ensembl; ENST00000262829.11; ENSP00000262829.7; ENSG00000100320.23. [O43251-3]
DR Ensembl; ENST00000405409.6; ENSP00000384944.2; ENSG00000100320.23. [O43251-9]
DR Ensembl; ENST00000414461.6; ENSP00000407855.2; ENSG00000100320.23. [O43251-4]
DR Ensembl; ENST00000416721.6; ENSP00000405651.2; ENSG00000100320.23. [O43251-5]
DR Ensembl; ENST00000438146.7; ENSP00000413035.2; ENSG00000100320.23. [O43251-8]
DR Ensembl; ENST00000449924.6; ENSP00000391670.2; ENSG00000100320.23. [O43251-10]
DR Ensembl; ENST00000618140.3; ENSP00000482053.2; ENSG00000277564.4. [O43251-9]
DR Ensembl; ENST00000619768.4; ENSP00000479761.1; ENSG00000277564.4. [O43251-10]
DR Ensembl; ENST00000626107.2; ENSP00000485984.1; ENSG00000277564.4. [O43251-4]
DR Ensembl; ENST00000627946.2; ENSP00000487477.1; ENSG00000277564.4. [O43251-5]
DR Ensembl; ENST00000631365.2; ENSP00000485711.1; ENSG00000277564.4. [O43251-3]
DR GeneID; 23543; -.
DR KEGG; hsa:23543; -.
DR UCSC; uc003aoh.5; human. [O43251-1]
DR CTD; 23543; -.
DR DisGeNET; 23543; -.
DR GeneCards; RBFOX2; -.
DR HGNC; HGNC:9906; RBFOX2.
DR HPA; ENSG00000100320; Low tissue specificity.
DR MIM; 612149; gene.
DR neXtProt; NX_O43251; -.
DR OpenTargets; ENSG00000100320; -.
DR PharmGKB; PA34272; -.
DR VEuPathDB; HostDB:ENSG00000100320; -.
DR eggNOG; KOG0125; Eukaryota.
DR GeneTree; ENSGT00940000157534; -.
DR InParanoid; O43251; -.
DR OMA; TYIPLIX; -.
DR OrthoDB; 871288at2759; -.
DR PhylomeDB; O43251; -.
DR TreeFam; TF315942; -.
DR PathwayCommons; O43251; -.
DR Reactome; R-HSA-6803529; FGFR2 alternative splicing.
DR SignaLink; O43251; -.
DR SIGNOR; O43251; -.
DR BioGRID-ORCS; 23543; 30 hits in 1085 CRISPR screens.
DR ChiTaRS; RBFOX2; human.
DR EvolutionaryTrace; O43251; -.
DR GeneWiki; RBM9; -.
DR GenomeRNAi; 23543; -.
DR Pharos; O43251; Tbio.
DR PRO; PR:O43251; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; O43251; protein.
DR Bgee; ENSG00000100320; Expressed in cortical plate and 103 other tissues.
DR ExpressionAtlas; O43251; baseline and differential.
DR Genevisible; O43251; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:BHF-UCL.
DR GO; GO:0042127; P:regulation of cell population proliferation; TAS:UniProtKB.
DR GO; GO:0016070; P:RNA metabolic process; TAS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
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; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT CHAIN 1..390
FT /note="RNA binding protein fox-1 homolog 2"
FT /id="PRO_0000081766"
FT DOMAIN 121..197
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..49
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 122
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 130
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 131
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 155
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 160
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 164
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 188
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 198
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT MOD_RES 281
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8BP71"
FT MOD_RES 297
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8BP71"
FT MOD_RES 329
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 381
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BP71"
FT MOD_RES 381
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BP71"
FT MOD_RES 386
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BP71"
FT MOD_RES 386
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BP71"
FT VAR_SEQ 1..18
FT /note="MQNEPLTPGYHGFPARDS -> MEKKKMVT (in isoform 2,
FT isoform 3, isoform 4, isoform 5, isoform 9 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:12529303,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15461802,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2,
FT ECO:0000303|Ref.3"
FT /id="VSP_007180"
FT VAR_SEQ 1
FT /note="M -> MAEGAQPHQPPQLGPGAAARGMKRESELELPVPGAGGDGADPGLSKR
FT PRTEEAAADGGGGM (in isoform 6 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.7"
FT /id="VSP_030889"
FT VAR_SEQ 94
FT /note="T -> TQ (in isoform 2, isoform 8 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:12529303,
FT ECO:0000303|PubMed:14702039, ECO:0000303|Ref.7"
FT /id="VSP_030890"
FT VAR_SEQ 143..160
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007181"
FT VAR_SEQ 261..265
FT /note="SLPLV -> I (in isoform 3, isoform 5, isoform 7 and
FT isoform 9)"
FT /evidence="ECO:0000303|PubMed:12529303,
FT ECO:0000303|PubMed:15461802, ECO:0000303|PubMed:15489334,
FT ECO:0000303|Ref.10"
FT /id="VSP_007182"
FT VAR_SEQ 311..390
FT /note="VYQDGFYGADLYGGYAAYRYAQPATATAATAAAAAAAAYSDGYGRVYTADPY
FT HALAPAASYGVGAVASLYRGGYSRFAPY -> DMQPTDMHSLLLQPQPPLLQPLQPLTV
FT TVMAGCTQPTPTMPLPLPLAMELALWRVYTEVATADLPPTEVT (in isoform 4
FT and isoform 9)"
FT /evidence="ECO:0000303|PubMed:12529303, ECO:0000303|Ref.3"
FT /id="VSP_007183"
FT VAR_SEQ 323..390
FT /note="GGYAAYRYAQPATATAATAAAAAAAAYSDGYGRVYTADPYHALAPAASYGVG
FT AVASLYRGGYSRFAPY -> IESANCFRSNRVDMQPTDMHSLLLQPQPPLLQPLQPLTV
FT TVMAGCTQPTPTMPLPLPLAMELALWRVYTEVATADLPPTEVT (in isoform 7)"
FT /evidence="ECO:0000303|Ref.10"
FT /id="VSP_030891"
FT CONFLICT 116
FT /note="S -> G (in Ref. 6; AAX84843)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="S -> F (in Ref. 4; BAB70875)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="A -> V (in Ref. 9; AAH13115)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="S -> G (in Ref. 4; BAB70875)"
FT /evidence="ECO:0000305"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:2CQ3"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:2CQ3"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:2CQ3"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:2CQ3"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:2CQ3"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:2CQ3"
FT HELIX 170..180
FT /evidence="ECO:0007829|PDB:2CQ3"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:2CQ3"
FT MOD_RES O43251-3:249
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES O43251-5:267
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES O43251-6:67
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CONFLICT O43251-6:8
FT /note="H -> Q (in Ref. 4; BAB70875)"
FT /evidence="ECO:0000305"
FT MOD_RES O43251-7:277
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES O43251-8:67
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES O43251-9:268
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
SQ SEQUENCE 390 AA; 41374 MW; 40D6C8C40764B317 CRC64;
MQNEPLTPGY HGFPARDSQG NQEPTTTPDA MVQPFTTIPF PPPPQNGIPT EYGVPHTQDY
AGQTGEHNLT LYGSTQAHGE QSSNSPSTQN GSLTTEGGAQ TDGQQSQTQS SENSESKSTP
KRLHVSNIPF RFRDPDLRQM FGQFGKILDV EIIFNERGSK GFGFVTFENS ADADRAREKL
HGTVVEGRKI EVNNATARVM TNKKMVTPYA NGWKLSPVVG AVYGPELYAA SSFQADVSLG
NDAAVPLSGR GGINTYIPLI SLPLVPGFPY PTAATTAAAF RGAHLRGRGR TVYGAVRAVP
PTAIPAYPGV VYQDGFYGAD LYGGYAAYRY AQPATATAAT AAAAAAAAYS DGYGRVYTAD
PYHALAPAAS YGVGAVASLY RGGYSRFAPY
