FXR1_HUMAN
ID FXR1_HUMAN Reviewed; 621 AA.
AC P51114; A8K9B8; Q7Z450; Q8N6R8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 3.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=RNA-binding protein FXR1 {ECO:0000305};
DE AltName: Full=FMR1 autosomal homolog 1 {ECO:0000312|HGNC:HGNC:4023};
DE AltName: Full=hFXR1p;
GN Name=FXR1;
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] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION,
RP VARIANT ASN-429, AND TISSUE SPECIFICITY.
RC TISSUE=Cervix carcinoma;
RX PubMed=7781595; DOI=10.1002/j.1460-2075.1995.tb07237.x;
RA Siomi M.C., Siomi H., Sauer W.H., Srinivasan S., Nussbaum R.L.,
RA Dreyfuss G.;
RT "FXR1, an autosomal homolog of the fragile X mental retardation gene.";
RL EMBO J. 14:2401-2408(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Testis;
RA Xu Z.Y., Huang X.Y., Wang H., Xu M., Li J.M., Zhou Z.M., Sha J.H.;
RT "Identification of alternatively spliced genes related to spermatogenesis
RT using cDNA microarrays.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Thymus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cervix;
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 [5]
RP PROTEIN SEQUENCE OF 2-9; 58-70; 246-263 AND 369-376, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Calvo F., Kolch W.;
RL Submitted (MAR-2008) to UniProtKB.
RN [6]
RP INTERACTION WITH FMR1 AND FXR2.
RC TISSUE=Brain;
RX PubMed=7489725; DOI=10.1002/j.1460-2075.1995.tb00220.x;
RA Zhang Y., O'Connor J.P., Siomi M.C., Srinivasan S., Dutra A.,
RA Nussbaum R.L., Dreyfuss G.;
RT "The fragile X mental retardation syndrome protein interacts with novel
RT homologs FXR1 and FXR2.";
RL EMBO J. 14:5358-5366(1995).
RN [7]
RP INTERACTION WITH FMR1.
RX PubMed=8668200; DOI=10.1128/mcb.16.7.3825;
RA Siomi M.C., Zhang Y., Siomi H., Dreyfuss G.;
RT "Specific sequences in the fragile X syndrome protein FMR1 and the FXR
RT proteins mediate their binding to 60S ribosomal subunits and the
RT interactions among them.";
RL Mol. Cell. Biol. 16:3825-3832(1996).
RN [8]
RP INTERACTION WITH FMR1.
RX PubMed=11157796; DOI=10.1093/hmg/10.4.329;
RA Laggerbauer B., Ostareck D., Keidel E.M., Ostareck-Lederer A., Fischer U.;
RT "Evidence that fragile X mental retardation protein is a negative regulator
RT of translation.";
RL Hum. Mol. Genet. 10:329-338(2001).
RN [9]
RP INTERACTION WITH FMR1.
RX PubMed=14532325; DOI=10.1093/hmg/ddg335;
RA Mazroui R., Huot M.E., Tremblay S., Boilard N., Labelle Y., Khandjian E.W.;
RT "Fragile X Mental Retardation protein determinants required for its
RT association with polyribosomal mRNPs.";
RL Hum. Mol. Genet. 12:3087-3096(2003).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP INTERACTION WITH TDRD3.
RX PubMed=18664458; DOI=10.1093/hmg/ddn219;
RA Linder B., Ploettner O., Kroiss M., Hartmann E., Laggerbauer B.,
RA Meister G., Keidel E., Fischer U.;
RT "Tdrd3 is a novel stress granule-associated protein interacting with the
RT Fragile-X syndrome protein FMRP.";
RL Hum. Mol. Genet. 17:3236-3246(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406 AND SER-409, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406; SER-409 AND SER-587,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524 AND SER-528 (ISOFORM 2),
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420 AND SER-423, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
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 [17]
RP INTERACTION WITH HABP4.
RX PubMed=21771594; DOI=10.1016/j.febslet.2011.07.010;
RA Goncalves K.A., Bressan G.C., Saito A., Morello L.G., Zanchin N.I.,
RA Kobarg J.;
RT "Evidence for the association of the human regulatory protein Ki-1/57 with
RT the translational machinery.";
RL FEBS Lett. 585:2556-2560(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406; SER-409; SER-420;
RP SER-423; SER-485; SER-587 AND THR-611, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401; SER-406; SER-409;
RP SER-420; SER-423; SER-432; SER-587 AND THR-611, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
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 [22]
RP INTERACTION WITH VENEZUELAN EQUINE ENCEPHALITIS VIRUS NON-STRUCTURAL
RP PROTEIN 3 (MICROBIAL INFECTION).
RX PubMed=27509095; DOI=10.1371/journal.ppat.1005810;
RA Kim D.Y., Reynaud J.M., Rasalouskaya A., Akhrymuk I., Mobley J.A.,
RA Frolov I., Frolova E.I.;
RT "New World and Old World Alphaviruses Have Evolved to Exploit Different
RT Components of Stress Granules, FXR and G3BP Proteins, for Assembly of Viral
RT Replication Complexes.";
RL PLoS Pathog. 12:E1005810-E1005810(2016).
RN [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-56, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [24]
RP STRUCTURE BY NMR OF 212-289.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the N-terminal KH domain of human FXR1.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [25]
RP INVOLVEMENT IN MYORIBF, INVOLVEMENT IN MYOPMIL, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=30770808; DOI=10.1038/s41467-019-08548-9;
RA Estan M.C., Fernandez-Nunez E., Zaki M.S., Esteban M.I., Donkervoort S.,
RA Hawkins C., Caparros-Martin J.A., Saade D., Hu Y., Bolduc V., Chao K.R.,
RA Nevado J., Lamuedra A., Largo R., Herrero-Beaumont G., Regadera J.,
RA Hernandez-Chico C., Tizzano E.F., Martinez-Glez V., Carvajal J.J., Zong R.,
RA Nelson D.L., Otaify G.A., Temtamy S., Aglan M., Issa M., Boennemann C.G.,
RA Lapunzina P., Yoon G., Ruiz-Perez V.L.;
RT "Recessive mutations in muscle-specific isoforms of FXR1 cause congenital
RT multi-minicore myopathy.";
RL Nat. Commun. 10:797-797(2019).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-132, AND DOMAINS TUDOR.
RX PubMed=21072162; DOI=10.1371/journal.pone.0013559;
RA Adams-Cioaba M.A., Guo Y., Bian C., Amaya M.F., Lam R., Wasney G.A.,
RA Vedadi M., Xu C., Min J.;
RT "Structural studies of the tandem Tudor domains of fragile X mental
RT retardation related proteins FXR1 and FXR2.";
RL PLoS ONE 5:E13559-E13559(2010).
RN [27]
RP VARIANT [LARGE SCALE ANALYSIS] THR-233.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: RNA-binding protein required for embryonic and postnatal
CC development of muscle tissue (PubMed:30770808). May regulate
CC intracellular transport and local translation of certain mRNAs (By
CC similarity). {ECO:0000250|UniProtKB:Q61584,
CC ECO:0000269|PubMed:30770808}.
CC -!- SUBUNIT: Interacts with FMR1 (PubMed:8668200, PubMed:7489725,
CC PubMed:11157796). Interacts with FRX2 (PubMed:7489725). Interacts with
CC TDRD3 (PubMed:18664458). Interacts with HABP4 (PubMed:21771594).
CC Interacts with CYFIP2 but not with CYFIP1 (By similarity).
CC {ECO:0000250|UniProtKB:Q61584, ECO:0000269|PubMed:11157796,
CC ECO:0000269|PubMed:18664458, ECO:0000269|PubMed:21771594,
CC ECO:0000269|PubMed:7489725, ECO:0000269|PubMed:8668200}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Sindbis virus non-
CC structural protein 3 (via C-terminus); this interaction inhibits the
CC formation of host stress granules on viral mRNAs and the nsp3-FXR1
CC complexes bind viral RNAs and probably orchestrate the assembly of
CC viral replication complexes. {ECO:0000269|PubMed:27509095}.
CC -!- INTERACTION:
CC P51114; Q6AI12: ANKRD40; NbExp=2; IntAct=EBI-713291, EBI-2838246;
CC P51114; Q96CW1: AP2M1; NbExp=2; IntAct=EBI-713291, EBI-297683;
CC P51114; Q9Y232: CDYL; NbExp=2; IntAct=EBI-713291, EBI-1387386;
CC P51114; Q9P209: CEP72; NbExp=2; IntAct=EBI-713291, EBI-739498;
CC P51114; O00423: EML1; NbExp=2; IntAct=EBI-713291, EBI-751327;
CC P51114; P21333: FLNA; NbExp=2; IntAct=EBI-713291, EBI-350432;
CC P51114; Q06787: FMR1; NbExp=4; IntAct=EBI-713291, EBI-366305;
CC P51114; P51116: FXR2; NbExp=3; IntAct=EBI-713291, EBI-740459;
CC P51114; Q674X7: KAZN; NbExp=2; IntAct=EBI-713291, EBI-949239;
CC P51114; Q8WZ19: KCTD13; NbExp=2; IntAct=EBI-713291, EBI-742916;
CC P51114; Q15233: NONO; NbExp=2; IntAct=EBI-713291, EBI-350527;
CC P51114; Q86UU1: PHLDB1; NbExp=2; IntAct=EBI-713291, EBI-4289858;
CC P51114; Q9UI14: RABAC1; NbExp=2; IntAct=EBI-713291, EBI-712367;
CC P51114; P04637: TP53; NbExp=2; IntAct=EBI-713291, EBI-366083;
CC P51114; P07437: TUBB; NbExp=2; IntAct=EBI-713291, EBI-350864;
CC P51114; PRO_0000449621 [P0DTD1]: rep; Xeno; NbExp=5; IntAct=EBI-713291, EBI-25492388;
CC P51114; PRO_0000449627 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-713291, EBI-25475877;
CC P51114-2; Q9BXS5: AP1M1; NbExp=5; IntAct=EBI-11022345, EBI-541426;
CC P51114-2; P51451: BLK; NbExp=3; IntAct=EBI-11022345, EBI-2105445;
CC P51114-2; Q13895: BYSL; NbExp=3; IntAct=EBI-11022345, EBI-358049;
CC P51114-2; Q9HC52: CBX8; NbExp=3; IntAct=EBI-11022345, EBI-712912;
CC P51114-2; O00311: CDC7; NbExp=3; IntAct=EBI-11022345, EBI-374980;
CC P51114-2; Q07002: CDK18; NbExp=3; IntAct=EBI-11022345, EBI-746238;
CC P51114-2; Q8IVW4: CDKL3; NbExp=3; IntAct=EBI-11022345, EBI-3919850;
CC P51114-2; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-11022345, EBI-5453285;
CC P51114-2; P26196: DDX6; NbExp=3; IntAct=EBI-11022345, EBI-351257;
CC P51114-2; O43143: DHX15; NbExp=3; IntAct=EBI-11022345, EBI-1237044;
CC P51114-2; Q14241: ELOA; NbExp=3; IntAct=EBI-11022345, EBI-742350;
CC P51114-2; P19447: ERCC3; NbExp=3; IntAct=EBI-11022345, EBI-1183307;
CC P51114-2; Q56NI9: ESCO2; NbExp=3; IntAct=EBI-11022345, EBI-3951849;
CC P51114-2; Q3B820: FAM161A; NbExp=3; IntAct=EBI-11022345, EBI-719941;
CC P51114-2; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-11022345, EBI-6658203;
CC P51114-2; Q8IXW7: FMR1; NbExp=3; IntAct=EBI-11022345, EBI-11976595;
CC P51114-2; Q8NHY3: GAS2L2; NbExp=3; IntAct=EBI-11022345, EBI-7960826;
CC P51114-2; Q9HAQ2: KIF9; NbExp=3; IntAct=EBI-11022345, EBI-8472129;
CC P51114-2; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-11022345, EBI-739832;
CC P51114-2; P61326: MAGOH; NbExp=3; IntAct=EBI-11022345, EBI-299134;
CC P51114-2; Q96A72: MAGOHB; NbExp=3; IntAct=EBI-11022345, EBI-746778;
CC P51114-2; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-11022345, EBI-348259;
CC P51114-2; P55081: MFAP1; NbExp=3; IntAct=EBI-11022345, EBI-1048159;
CC P51114-2; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-11022345, EBI-14086479;
CC P51114-2; Q9BU76: MMTAG2; NbExp=5; IntAct=EBI-11022345, EBI-742459;
CC P51114-2; Q8NEY8-5: PPHLN1; NbExp=3; IntAct=EBI-11022345, EBI-22734102;
CC P51114-2; Q96QH2: PRAM1; NbExp=3; IntAct=EBI-11022345, EBI-2860740;
CC P51114-2; Q99633: PRPF18; NbExp=3; IntAct=EBI-11022345, EBI-2798416;
CC P51114-2; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-11022345, EBI-1567797;
CC P51114-2; P78362: SRPK2; NbExp=3; IntAct=EBI-11022345, EBI-593303;
CC P51114-2; O75716: STK16; NbExp=3; IntAct=EBI-11022345, EBI-749295;
CC P51114-2; Q9UMX1: SUFU; NbExp=3; IntAct=EBI-11022345, EBI-740595;
CC P51114-2; Q5T7P8-2: SYT6; NbExp=3; IntAct=EBI-11022345, EBI-10246152;
CC P51114-2; Q9NU19: TBC1D22B; NbExp=3; IntAct=EBI-11022345, EBI-8787464;
CC P51114-2; Q15560: TCEA2; NbExp=3; IntAct=EBI-11022345, EBI-710310;
CC P51114-2; Q7Z4N2-7: TRPM1; NbExp=3; IntAct=EBI-11022345, EBI-12371223;
CC P51114-2; Q14157: UBAP2L; NbExp=3; IntAct=EBI-11022345, EBI-347762;
CC P51114-2; P07947: YES1; NbExp=3; IntAct=EBI-11022345, EBI-515331;
CC P51114-2; Q96NC0: ZMAT2; NbExp=3; IntAct=EBI-11022345, EBI-2682299;
CC P51114-2; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-11022345, EBI-740727;
CC P51114-2; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-11022345, EBI-11962468;
CC P51114-2; Q9NQZ8: ZNF71; NbExp=3; IntAct=EBI-11022345, EBI-7138235;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:30770808,
CC ECO:0000269|PubMed:7781595}. Note=Adjacent to Z-lines in muscles.
CC {ECO:0000250|UniProtKB:Q61584}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Alternative splicing appears to be tissue-specific.;
CC Name=1; Synonyms=Long;
CC IsoId=P51114-1; Sequence=Displayed;
CC Name=2; Synonyms=b, Short;
CC IsoId=P51114-2; Sequence=VSP_019710, VSP_019711;
CC Name=3;
CC IsoId=P51114-3; Sequence=VSP_019709;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined including heart,
CC brain, kidney and testis. {ECO:0000269|PubMed:7781595}.
CC -!- DOMAIN: The tandem Agenet-like domains preferentially recognize
CC trimethylated histone peptides. {ECO:0000269|PubMed:21072162}.
CC -!- PTM: Arg-445 is dimethylated, probably to asymmetric dimethylarginine.
CC -!- DISEASE: Myopathy, congenital, with respiratory insufficiency and bone
CC fractures (MYORIBF) [MIM:618822]: An autosomal recessive muscular
CC disorder characterized by severe hypotonia apparent at birth, poor
CC feeding, ulnar deviation of the hands, laterally deviated feet,
CC fractures of the long bones, respiratory insufficiency due to muscle
CC weakness, and death in infancy. {ECO:0000269|PubMed:30770808}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Myopathy, congenital proximal, with minicore lesions (MYOPMIL)
CC [MIM:618823]: An autosomal recessive, slowly progressive muscular
CC disorder characterized by primarily proximal muscle weakness, neonatal
CC hypotonia leading to delayed motor development, mildly delayed walking
CC in childhood, and difficulty running or climbing. Cardiac function is
CC unaffected, but most patients have obstructive sleep apnea. Muscle
CC biopsy shows type 1 fiber predominance with disorganized Z-lines and
CC minicores that disrupt the myofibrillar striation pattern.
CC {ECO:0000269|PubMed:30770808}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the FMR1 family. {ECO:0000305}.
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DR EMBL; U25165; AAC50155.1; -; mRNA.
DR EMBL; AY341428; AAQ20045.1; -; mRNA.
DR EMBL; AK292633; BAF85322.1; -; mRNA.
DR EMBL; BC028983; AAH28983.1; -; mRNA.
DR CCDS; CCDS3238.1; -. [P51114-1]
DR CCDS; CCDS33894.1; -. [P51114-3]
DR CCDS; CCDS46965.1; -. [P51114-2]
DR PIR; S55330; S55330.
DR RefSeq; NP_001013456.1; NM_001013438.2. [P51114-2]
DR RefSeq; NP_001013457.1; NM_001013439.2. [P51114-3]
DR RefSeq; NP_005078.2; NM_005087.3. [P51114-1]
DR PDB; 2CPQ; NMR; -; A=212-289.
DR PDB; 3KUF; X-ray; 2.70 A; A=2-132.
DR PDB; 3O8V; X-ray; 2.50 A; A=2-132.
DR PDBsum; 2CPQ; -.
DR PDBsum; 3KUF; -.
DR PDBsum; 3O8V; -.
DR AlphaFoldDB; P51114; -.
DR SMR; P51114; -.
DR BioGRID; 113760; 500.
DR CORUM; P51114; -.
DR DIP; DIP-40789N; -.
DR IntAct; P51114; 335.
DR MINT; P51114; -.
DR STRING; 9606.ENSP00000350170; -.
DR BindingDB; P51114; -.
DR ChEMBL; CHEMBL3879858; -.
DR GlyGen; P51114; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P51114; -.
DR MetOSite; P51114; -.
DR PhosphoSitePlus; P51114; -.
DR SwissPalm; P51114; -.
DR BioMuta; FXR1; -.
DR DMDM; 189047132; -.
DR EPD; P51114; -.
DR jPOST; P51114; -.
DR MassIVE; P51114; -.
DR MaxQB; P51114; -.
DR PaxDb; P51114; -.
DR PeptideAtlas; P51114; -.
DR PRIDE; P51114; -.
DR ProteomicsDB; 56278; -. [P51114-1]
DR ProteomicsDB; 56279; -. [P51114-2]
DR ProteomicsDB; 56280; -. [P51114-3]
DR Antibodypedia; 18845; 353 antibodies from 39 providers.
DR DNASU; 8087; -.
DR Ensembl; ENST00000305586.11; ENSP00000307633.7; ENSG00000114416.18. [P51114-3]
DR Ensembl; ENST00000357559.9; ENSP00000350170.3; ENSG00000114416.18. [P51114-1]
DR Ensembl; ENST00000445140.6; ENSP00000388828.2; ENSG00000114416.18. [P51114-2]
DR GeneID; 8087; -.
DR KEGG; hsa:8087; -.
DR MANE-Select; ENST00000357559.9; ENSP00000350170.3; NM_005087.4; NP_005078.2.
DR UCSC; uc003fkp.4; human. [P51114-1]
DR CTD; 8087; -.
DR DisGeNET; 8087; -.
DR GeneCards; FXR1; -.
DR HGNC; HGNC:4023; FXR1.
DR HPA; ENSG00000114416; Group enriched (skeletal muscle, tongue).
DR MalaCards; FXR1; -.
DR MIM; 600819; gene.
DR MIM; 618822; phenotype.
DR MIM; 618823; phenotype.
DR neXtProt; NX_P51114; -.
DR OpenTargets; ENSG00000114416; -.
DR PharmGKB; PA28439; -.
DR VEuPathDB; HostDB:ENSG00000114416; -.
DR eggNOG; ENOG502QPKJ; Eukaryota.
DR GeneTree; ENSGT00950000183189; -.
DR HOGENOM; CLU_020699_3_0_1; -.
DR InParanoid; P51114; -.
DR OMA; DQQQRGY; -.
DR PhylomeDB; P51114; -.
DR TreeFam; TF105427; -.
DR PathwayCommons; P51114; -.
DR Reactome; R-HSA-6802952; Signaling by BRAF and RAF1 fusions.
DR SignaLink; P51114; -.
DR BioGRID-ORCS; 8087; 20 hits in 1085 CRISPR screens.
DR ChiTaRS; FXR1; human.
DR EvolutionaryTrace; P51114; -.
DR GeneWiki; FXR1; -.
DR GenomeRNAi; 8087; -.
DR Pharos; P51114; Tbio.
DR PRO; PR:P51114; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P51114; protein.
DR Bgee; ENSG00000114416; Expressed in sperm and 205 other tissues.
DR ExpressionAtlas; P51114; baseline and differential.
DR Genevisible; P51114; HS.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0043034; C:costamere; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IMP:UniProtKB.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:1902737; C:dendritic filopodium; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0044326; C:dendritic spine neck; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0030426; C:growth cone; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; TAS:ProtInc.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005844; C:polysome; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IBA:GO_Central.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0033592; F:RNA strand annealing activity; IDA:UniProtKB.
DR GO; GO:0045182; F:translation regulator activity; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007517; P:muscle organ development; IMP:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central.
DR GO; GO:2000637; P:positive regulation of miRNA-mediated gene silencing; IDA:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR GO; GO:2001022; P:positive regulation of response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0045727; P:positive regulation of translation; IBA:GO_Central.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0051489; P:regulation of filopodium assembly; IBA:GO_Central.
DR GO; GO:0043488; P:regulation of mRNA stability; IBA:GO_Central.
DR GO; GO:0060538; P:skeletal muscle organ development; IMP:UniProtKB.
DR Gene3D; 3.30.1370.10; -; 2.
DR InterPro; IPR008395; Agenet-like_dom.
DR InterPro; IPR040148; FMR1.
DR InterPro; IPR040472; FMRP_KH0.
DR InterPro; IPR022034; FXMRP1_C_core.
DR InterPro; IPR032172; FXR_C1.
DR InterPro; IPR032177; FXR_C3.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR041560; Tudor_FRX1.
DR PANTHER; PTHR10603; PTHR10603; 2.
DR Pfam; PF05641; Agenet; 1.
DR Pfam; PF12235; FXMRP1_C_core; 2.
DR Pfam; PF16096; FXR_C1; 1.
DR Pfam; PF16097; FXR_C3; 1.
DR Pfam; PF00013; KH_1; 1.
DR Pfam; PF17904; KH_9; 1.
DR Pfam; PF18336; Tudor_FRX1; 1.
DR SMART; SM00322; KH; 2.
DR SUPFAM; SSF54791; SSF54791; 2.
DR PROSITE; PS51641; AGENET_LIKE; 2.
DR PROSITE; PS50084; KH_TYPE_1; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Developmental protein; Differentiation; Direct protein sequencing;
KW Isopeptide bond; Methylation; Myogenesis; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:22814378"
FT CHAIN 2..621
FT /note="RNA-binding protein FXR1"
FT /id="PRO_0000050106"
FT DOMAIN 4..50
FT /note="Agenet-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00973"
FT DOMAIN 63..115
FT /note="Agenet-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00973"
FT DOMAIN 222..251
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 285..314
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 381..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..457
FT /note="RNA-binding RGG-box"
FT REGION 545..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:22814378"
FT MOD_RES 68
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q61584"
FT MOD_RES 401
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5XI81"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 447
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 447
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 453
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 453
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 455
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 455
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 483
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q61584"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51116"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 611
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 56
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..85
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_019709"
FT VAR_SEQ 535..539
FT /note="VTVAD -> GKRCD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:7781595"
FT /id="VSP_019710"
FT VAR_SEQ 540..621
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:7781595"
FT /id="VSP_019711"
FT VARIANT 233
FT /note="A -> T (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036050"
FT VARIANT 429
FT /note="D -> N (in dbSNP:rs1051080)"
FT /evidence="ECO:0000269|PubMed:7781595"
FT /id="VAR_016077"
FT VARIANT 614
FT /note="A -> V (in dbSNP:rs11499)"
FT /id="VAR_014890"
FT CONFLICT 3..4
FT /note="EL -> DV (in Ref. 1; AAC50155)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="S -> P (in Ref. 3; BAF85322)"
FT /evidence="ECO:0000305"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:3O8V"
FT STRAND 15..23
FT /evidence="ECO:0007829|PDB:3O8V"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:3O8V"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:3O8V"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:3O8V"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:3O8V"
FT STRAND 78..88
FT /evidence="ECO:0007829|PDB:3O8V"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:3O8V"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:3O8V"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:3O8V"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:3O8V"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:2CPQ"
FT STRAND 218..224
FT /evidence="ECO:0007829|PDB:2CPQ"
FT HELIX 227..234
FT /evidence="ECO:0007829|PDB:2CPQ"
FT HELIX 239..245
FT /evidence="ECO:0007829|PDB:2CPQ"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:2CPQ"
FT TURN 257..260
FT /evidence="ECO:0007829|PDB:2CPQ"
FT STRAND 261..268
FT /evidence="ECO:0007829|PDB:2CPQ"
FT HELIX 269..279
FT /evidence="ECO:0007829|PDB:2CPQ"
FT MOD_RES P51114-2:524
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES P51114-2:528
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
SQ SEQUENCE 621 AA; 69721 MW; 0474A9B593C7C228 CRC64;
MAELTVEVRG SNGAFYKGFI KDVHEDSLTV VFENNWQPER QVPFNEVRLP PPPDIKKEIS
EGDEVEVYSR ANDQEPCGWW LAKVRMMKGE FYVIEYAACD ATYNEIVTFE RLRPVNQNKT
VKKNTFFKCT VDVPEDLREA CANENAHKDF KKAVGACRIF YHPETTQLMI LSASEATVKR
VNILSDMHLR SIRTKLMLMS RNEEATKHLE CTKQLAAAFH EEFVVREDLM GLAIGTHGSN
IQQARKVPGV TAIELDEDTG TFRIYGESAD AVKKARGFLE FVEDFIQVPR NLVGKVIGKN
GKVIQEIVDK SGVVRVRIEG DNENKLPRED GMVPFVFVGT KESIGNVQVL LEYHIAYLKE
VEQLRMERLQ IDEQLRQIGS RSYSGRGRGR RGPNYTSGYG TNSELSNPSE TESERKDELS
DWSLAGEDDR DSRHQRDSRR RPGGRGRSVS GGRGRGGPRG GKSSISSVLK DPDSNPYSLL
DNTESDQTAD TDASESHHST NRRRRSRRRR TDEDAVLMDG MTESDTASVN ENGLVTVADY
ISRAESQSRQ RNLPRETLAK NKKEMAKDVI EEHGPSEKAI NGPTSASGDD ISKLQRTPGE
EKINTLKEEN TQEAAVLNGV S
