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 27-MAR-2024, entry version 219. DE RecName: Full=RNA-binding protein FXR1 {ECO:0000305}; DE AltName: Full=FMR1 autosomal homolog 1 {ECO:0000305}; DE AltName: Full=hFXR1p; GN Name=FXR1 {ECO:0000303|PubMed:7781595, ECO:0000312|HGNC:HGNC:4023}; 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 SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=9259278; DOI=10.1093/hmg/6.8.1315; RA Tamanini F., Willemsen R., van Unen L., Bontekoe C., Galjaard H., RA Oostra B.A., Hoogeveen A.T.; RT "Differential expression of FMR1, FXR1 and FXR2 proteins in human brain and RT testis."; RL Hum. Mol. Genet. 6:1315-1322(1997). RN [9] 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 [10] 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 [11] 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 [12] RP FUNCTION. RX PubMed=17382880; DOI=10.1016/j.cell.2007.01.038; RA Vasudevan S., Steitz J.A.; RT "AU-rich-element-mediated upregulation of translation by FXR1 and Argonaute RT 2."; RL Cell 128:1105-1118(2007). RN [13] 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 [14] 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 [15] 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 [16] 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 [17] RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-420, AND MUTAGENESIS RP OF ILE-304; 345-GLY-ASN-346; 348-GLN--ASN-552; 348-GLN--GLU-352 AND RP SER-420. RX PubMed=20417602; DOI=10.1016/j.molcel.2010.04.004; RA Say E., Tay H.G., Zhao Z.S., Baskaran Y., Li R., Lim L., Manser E.; RT "A functional requirement for PAK1 binding to the KH(2) domain of the RT fragile X protein-related FXR1."; RL Mol. Cell 38:236-249(2010). RN [18] 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 [19] 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 [20] 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 [21] 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 [22] 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 [23] 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 [24] 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 [25] 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 [26] RP UBIQUITINATION. RX PubMed=29142209; DOI=10.1038/s41467-017-01199-8; RA Qie S., Majumder M., Mackiewicz K., Howley B.V., Peterson Y.K., Howe P.H., RA Palanisamy V., Diehl J.A.; RT "Fbxo4-mediated degradation of Fxr1 suppresses tumorigenesis in head and RT neck squamous cell carcinoma."; RL Nat. Commun. 8:1534-1534(2017). RN [27] 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 [28] RP FUNCTION, INTERACTION WITH ELAVL1, AND INDUCTION. RX PubMed=30067974; DOI=10.1016/j.celrep.2018.07.002; RA Herman A.B., Vrakas C.N., Ray M., Kelemen S.E., Sweredoski M.J., RA Moradian A., Haines D.S., Autieri M.V.; RT "FXR1 is an IL-19-responsive RNA-binding protein that destabilizes pro- RT inflammatory transcripts in vascular smooth muscle cells."; RL Cell Rep. 24:1176-1189(2018). RN [29] RP INVOLVEMENT IN CMYP9A, INVOLVEMENT IN CMYP9B, 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 [30] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=32706158; DOI=10.15252/embj.2020104467; RA Agote-Aran A., Schmucker S., Jerabkova K., Jmel Boyer I., Berto A., RA Pacini L., Ronchi P., Kleiss C., Guerard L., Schwab Y., Moine H., RA Mandel J.L., Jacquemont S., Bagni C., Sumara I.; RT "Spatial control of nucleoporin condensation by fragile X-related RT proteins."; RL EMBO J. 39:e104467-e104467(2020). RN [31] RP FUNCTION. RX PubMed=34731628; DOI=10.1016/j.celrep.2021.109934; RA George J., Li Y., Kadamberi I.P., Parashar D., Tsaih S.W., Gupta P., RA Geethadevi A., Chen C., Ghosh C., Sun Y., Mittal S., Ramchandran R., RA Rui H., Lopez-Berestein G., Rodriguez-Aguayo C., Leone G., Rader J.S., RA Sood A.K., Dey M., Pradeep S., Chaluvally-Raghavan P.; RT "RNA-binding protein FXR1 drives cMYC translation by recruiting eIF4F RT complex to the translation start site."; RL Cell Rep. 37:109934-109934(2021). RN [32] RP FUNCTION, UBIQUITINATION, AND INTERACTION WITH CEP63. RX PubMed=35989368; DOI=10.1038/s41388-022-02439-y; RA Ling H., Cao C.H., Han K., Lv Y.R., Ma X.D., Cao J.H., Chen J.W., Li S., RA Lin J.L., Fang Y.J., Pan Z.Z., Xie D., Wang F.W.; RT "CEP63 upregulates YAP1 to promote colorectal cancer progression through RT stabilizing RNA binding protein FXR1."; RL Oncogene 41:4433-4445(2022). RN [33] RP FUNCTION. RX PubMed=36306353; DOI=10.1126/sciadv.abo1304; RA Datta C., Truesdell S.S., Wu K.Q., Bukhari S.I.A., Ngue H., Buchanan B., RA Le Tonqueze O., Lee S., Kollu S., Granovetter M.A., Boukhali M., RA Kreuzer J., Batool M.S., Balaj L., Haas W., Vasudevan S.; RT "Ribosome changes reprogram translation for chemosurvival in G0 leukemic RT cells."; RL Sci. Adv. 8:eabo1304-eabo1304(2022). RN [34] 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 [35] 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 [36] 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: mRNA-binding protein that acts as a regulator of mRNAs CC translation and/or stability, and which is required for various CC processes, such as neurogenesis, muscle development and spermatogenesis CC (PubMed:17382880, PubMed:20417602, PubMed:30067974, PubMed:34731628, CC PubMed:35989368, PubMed:36306353). Specifically binds to AU-rich CC elements (AREs) in the 3'-UTR of target mRNAs (PubMed:17382880, CC PubMed:34731628). Promotes formation of some phase-separated CC membraneless compartment by undergoing liquid-liquid phase separation CC upon binding to AREs-containing mRNAs, leading to assemble mRNAs into CC cytoplasmic ribonucleoprotein granules that concentrate mRNAs with CC associated regulatory factors (By similarity). Required to activate CC translation of stored mRNAs during late spermatogenesis: acts by CC undergoing liquid-liquid phase separation to assemble target mRNAs into CC cytoplasmic ribonucleoprotein granules that recruit translation CC initiation factor EIF4G3 to activate translation of stored mRNAs in CC late spermatids (By similarity). Promotes translation of MYC CC transcripts by recruiting the eIF4F complex to the translation start CC site (PubMed:34731628). Acts as a negative regulator of inflammation in CC response to IL19 by promoting destabilization of pro-inflammatory CC transcripts (PubMed:30067974). Also acts as an inhibitor of CC inflammation by binding to TNF mRNA, decreasing TNF protein production CC (By similarity). Acts as a negative regulator of AMPA receptor CC GRIA2/GluA2 synthesis during long-lasting synaptic potentiation of CC hippocampal neurons by binding to GRIA2/GluA2 mRNA, thereby inhibiting CC its translation (By similarity). Regulates proliferation of adult CC neural stem cells by binding to CDKN1A mRNA and promoting its CC expression (By similarity). Acts as a regulator of sleep and synaptic CC homeostasis by regulating translation of transcripts in neurons (By CC similarity). Required for embryonic and postnatal development of muscle CC tissue by undergoing liquid-liquid phase separation to assemble target CC mRNAs into cytoplasmic ribonucleoprotein granules (PubMed:30770808). CC Involved in the nuclear pore complex localization to the nuclear CC envelope by preventing cytoplasmic aggregation of nucleoporins: acts by CC preventing ectopic phase separation of nucleoporins in the cytoplasm CC via a microtubule-dependent mechanism (PubMed:32706158). CC {ECO:0000250|UniProtKB:Q61584, ECO:0000269|PubMed:17382880, CC ECO:0000269|PubMed:20417602, ECO:0000269|PubMed:30067974, CC ECO:0000269|PubMed:30770808, ECO:0000269|PubMed:32706158, CC ECO:0000269|PubMed:34731628, ECO:0000269|PubMed:35989368, CC ECO:0000269|PubMed:36306353}. CC -!- SUBUNIT: Interacts with FMR1 (PubMed:11157796, PubMed:7489725, CC PubMed:8668200). 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). Interacts CC with EIF4G3; promoting translation of target mRNAs (By similarity). CC Interacts with ELAVL1 (PubMed:30067974). Interacts with CEP63; CC inhibiting 'Lys-63'-linked ubiquitination (PubMed:35989368). CC {ECO:0000250|UniProtKB:Q61584, ECO:0000269|PubMed:11157796, CC ECO:0000269|PubMed:18664458, ECO:0000269|PubMed:21771594, CC ECO:0000269|PubMed:30067974, ECO:0000269|PubMed:35989368, 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=6; 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, Cytoplasmic ribonucleoprotein granule CC {ECO:0000269|PubMed:32706158}. Cytoplasm, Stress granule CC {ECO:0000269|PubMed:20417602}. Cytoplasm {ECO:0000269|PubMed:30770808, CC ECO:0000269|PubMed:7781595, ECO:0000269|PubMed:9259278}. Cell CC projection, dendrite {ECO:0000250|UniProtKB:Q61584}. Cell projection, CC dendritic spine {ECO:0000250|UniProtKB:Q61584}. Cell projection, axon CC {ECO:0000250|UniProtKB:Q61584}. Nucleus envelope CC {ECO:0000269|PubMed:32706158}. Postsynapse CC {ECO:0000250|UniProtKB:Q61584}. Note=Specifically localizes to CC cytoplasmic ribonucleoprotein membraneless compartments (By CC similarity). Localizes to stress granules following phosphorylation at CC Ser-420 by PAK1 (PubMed:20417602). Adjacent to Z-lines in muscles (By CC similarity). {ECO:0000250|UniProtKB:Q61584, CC ECO:0000269|PubMed:20417602}. 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 (PubMed:7781595, PubMed:9259278). In brain, CC present at high level in neurons and especially in the Purkinje cells CC at the interface between the granular layer and the molecular layer (at CC protein level) (PubMed:9259278). {ECO:0000269|PubMed:7781595, CC ECO:0000269|PubMed:9259278}. CC -!- INDUCTION: By Interleukin-19 (IL19). {ECO:0000269|PubMed:30067974}. CC -!- DOMAIN: The tandem Agenet-like domains preferentially recognize CC trimethylated histone peptides. {ECO:0000269|PubMed:21072162}. CC -!- DOMAIN: Disordered region at the C-terminus undergoes liquid-liquid CC phase separation (LLPS) for the formation of a membraneless compartment CC that stores mRNAs. {ECO:0000250|UniProtKB:Q61584}. CC -!- PTM: Phosphorylation at Ser-420 by PAK1 promotes its relocalization to CC stress granules and activity (PubMed:20417602). Phosphorylated by CC MAPK1/ERK2, promoting subsequent phosphorylation by GSK3B (By CC similarity). Phosphorylated by GSK3B, promoting ubiquitination and CC degradation by the proteasome (By similarity). CC {ECO:0000250|UniProtKB:Q61584, ECO:0000269|PubMed:20417602}. CC -!- PTM: Ubiquitinated by the SCF(FBXO4) complex, leading to its CC degradation by the proteasome: ubiquitination by the SCF(FBXO4) complex CC takes place following phosphorylation by GSK3B (PubMed:29142209). CC Ubiquitinated and degraded in a GSK3B-dependent manner in during both CC scaling and sleep deprivation (By similarity). Ubiquitinated via 'Lys- CC 63'-linked ubiquitin, leading to its degradation: interaction with CC CEP63 inhibits 'Lys-63'-linked ubiquitination (PubMed:35989368). CC {ECO:0000250|UniProtKB:Q61584, ECO:0000269|PubMed:29142209, CC ECO:0000269|PubMed:35989368}. CC -!- DISEASE: Congenital myopathy 9A (CMYP9A) [MIM:618822]: An autosomal CC recessive muscular disorder characterized by severe hypotonia apparent CC at birth, poor feeding, ulnar deviation of the hands, laterally CC deviated feet, fractures of the long bones, respiratory insufficiency CC due to muscle weakness, and death in infancy. CC {ECO:0000269|PubMed:30770808}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Congenital myopathy 9B, proximal, with minicore lesions CC (CMYP9B) [MIM:618823]: An autosomal recessive, slowly progressive CC muscular disorder characterized by primarily proximal muscle weakness, CC neonatal hypotonia leading to delayed motor development, mildly delayed CC walking in childhood, and difficulty running or climbing. Cardiac CC function is unaffected, but most patients have obstructive sleep apnea. CC Muscle biopsy shows type 1 fiber predominance with disorganized Z-lines CC and 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}. 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; 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; 556. DR CORUM; P51114; -. DR DIP; DIP-40789N; -. DR IntAct; P51114; 349. DR MINT; P51114; -. DR STRING; 9606.ENSP00000350170; -. DR BindingDB; P51114; -. DR ChEMBL; CHEMBL3879858; -. DR GlyCosmos; P51114; 1 site, 1 glycan. 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; 9606-ENSP00000350170; -. DR PeptideAtlas; P51114; -. DR ProteomicsDB; 56278; -. [P51114-1] DR ProteomicsDB; 56279; -. [P51114-2] DR ProteomicsDB; 56280; -. [P51114-3] DR Pumba; P51114; -. DR Antibodypedia; 18845; 387 antibodies from 39 providers. DR DNASU; 8087; -. DR Ensembl; ENST00000305586.11; ENSP00000307633.7; ENSG00000114416.19. [P51114-3] DR Ensembl; ENST00000357559.9; ENSP00000350170.3; ENSG00000114416.19. [P51114-1] DR Ensembl; ENST00000445140.6; ENSP00000388828.2; ENSG00000114416.19. [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 AGR; HGNC:4023; -. 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; WPARITK; -. DR OrthoDB; 2995592at2759; -. DR PhylomeDB; P51114; -. DR TreeFam; TF105427; -. DR PathwayCommons; P51114; -. DR Reactome; R-HSA-6802952; Signaling by BRAF and RAF1 fusions. DR SignaLink; P51114; -. DR SIGNOR; P51114; -. DR BioGRID-ORCS; 8087; 21 hits in 1165 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 207 other cell types or tissues. DR ExpressionAtlas; P51114; baseline and differential. DR GO; GO:0030424; C:axon; IBA:GO_Central. DR GO; GO:0043034; C:costamere; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:UniProtKB. DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. 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:0043232; C:intracellular non-membrane-bounded organelle; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central. DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB. 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:0005840; C:ribosome; IEA:Ensembl. DR GO; GO:0140693; F:molecular condensate scaffold activity; ISS:UniProtKB. DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:UniProtKB. DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProt. DR GO; GO:1905538; F:polysome binding; IEA:Ensembl. 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; IDA: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:0021542; P:dentate gyrus development; ISS:UniProtKB. DR GO; GO:0061157; P:mRNA destabilization; IDA:UniProtKB. DR GO; GO:0007517; P:muscle organ development; IMP:UniProtKB. DR GO; GO:0050728; P:negative regulation of inflammatory response; IDA:UniProtKB. DR GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; ISS:UniProtKB. DR GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central. DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISS:UniProtKB. DR GO; GO:0140694; P:non-membrane-bounded organelle assembly; ISS:UniProtKB. DR GO; GO:0051292; P:nuclear pore complex assembly; IDA:UniProtKB. DR GO; GO:0051664; P:nuclear pore localization; IDA:UniProtKB. 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:0045727; P:positive regulation of translation; IDA:UniProtKB. DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IBA:GO_Central. DR GO; GO:0045187; P:regulation of circadian sleep/wake cycle, sleep; ISS:UniProtKB. 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:0050767; P:regulation of neurogenesis; ISS:UniProtKB. DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; ISS:UniProtKB. DR GO; GO:0060538; P:skeletal muscle organ development; IMP:UniProtKB. DR GO; GO:0007286; P:spermatid development; ISS:UniProtKB. DR CDD; cd22504; KH_I_FXR1_rpt1; 1. DR CDD; cd22507; KH_I_FXR1_rpt2; 1. DR CDD; cd22510; KH_I_FXR1_rpt3; 1. DR CDD; cd20472; Tudor_Agenet_FXR1_rpt1; 1. DR CDD; cd20475; Tudor_Agenet_FXR1_rpt2; 1. DR Gene3D; 2.30.30.140; -; 2. DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 2. DR InterPro; IPR008395; Agenet-like_dom. DR InterPro; IPR040148; FMR1. DR InterPro; IPR022034; FMR1-like_C_core. DR InterPro; IPR040472; FMRP_KH0. DR InterPro; IPR032172; FXR1_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; IPR047494; KH_I_FXR1_rpt1. DR InterPro; IPR047495; KH_I_FXR1_rpt2. DR InterPro; IPR047496; KH_I_FXR1_rpt3. DR InterPro; IPR047425; Tudor_Agenet_FXR1_rpt1. DR InterPro; IPR047427; Tudor_Agenet_FXR1_rpt2. DR InterPro; IPR041560; Tudor_FRM1. DR PANTHER; PTHR10603; FRAGILE X MENTAL RETARDATION SYNDROME-RELATED PROTEIN; 1. DR PANTHER; PTHR10603:SF6; FRAGILE X MENTAL RETARDATION SYNDROME-RELATED PROTEIN 1; 1. 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; 2. DR Pfam; PF17904; KH_9; 1. DR Pfam; PF18336; Tudor_FRX1; 1. DR SMART; SM00322; KH; 2. DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 2. DR PROSITE; PS51641; AGENET_LIKE; 2. DR PROSITE; PS50084; KH_TYPE_1; 2. DR Genevisible; P51114; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cell projection; KW Cytoplasm; Developmental protein; Differentiation; KW Direct protein sequencing; Isopeptide bond; Methylation; Myogenesis; KW Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding; KW Spermatogenesis; Synapse; 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; by PAK1" FT /evidence="ECO:0000269|PubMed:20417602, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT 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 MUTAGEN 304 FT /note="I->N: Abolished binding to PAK1." FT /evidence="ECO:0000269|PubMed:20417602" FT MUTAGEN 345..346 FT /note="GN->DA: Does not affect binding to PAK1." FT /evidence="ECO:0000269|PubMed:20417602" FT MUTAGEN 348..352 FT /note="QVLLE->KVLLA: Abolished binding to PAK1." FT /evidence="ECO:0000269|PubMed:20417602" FT MUTAGEN 352..353 FT /note="EY->AA: Reduced binding to PAK1." FT /evidence="ECO:0000269|PubMed:20417602" FT MUTAGEN 420 FT /note="S->A: Abolished phosphorylation by PAK1, leading to FT impaired activity." FT /evidence="ECO:0000269|PubMed:20417602" FT MUTAGEN 420 FT /note="S->D: Mimics phosphorylation state; leading to FT increased activity." FT /evidence="ECO:0000269|PubMed:20417602" 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 //