ID FXR2_HUMAN Reviewed; 673 AA. AC P51116; B2R9M2; D3DTQ1; Q86V09; Q8WUM2; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 2. DT 27-MAR-2024, entry version 204. DE RecName: Full=RNA-binding protein FXR2 {ECO:0000305}; DE Short=FXR2P {ECO:0000250|UniProtKB:Q9WVR4}; DE AltName: Full=FMR1 autosomal homolog 2 {ECO:0000305}; GN Name=FXR2 {ECO:0000303|PubMed:7489725, ECO:0000312|HGNC:HGNC:4024}; GN Synonyms=FMR1L2; 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], AND INTERACTION WITH FMR1 AND FXR1. 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; 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 GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-252. RC TISSUE=Lymph, PNS, and Skin; 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 [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27. RX PubMed=9437788; DOI=10.1016/s0039-128x(97)00087-1; RA Joseph D.R.; RT "The rat androgen-binding protein (ABP/SHBG) gene contains triplet repeats RT similar to unstable triplets: evidence that the ABP/SHBG and the fragile X- RT related 2 genes overlap."; RL Steroids 63:2-4(1998). 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=15144186; DOI=10.1021/ac035352d; RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., RA Peters E.C.; RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from RT human T cells using immobilized metal affinity chromatography and tandem RT mass spectrometry."; RL Anal. Chem. 76:2763-2772(2004). 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 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-598, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-411; SER-533; SER-566; RP THR-598; SER-601 AND SER-603, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [16] 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-598; SER-601 AND SER-603, AND RP 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-566 AND SER-603, 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-603, AND IDENTIFICATION BY RP MASS 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192; SER-410; THR-411; RP SER-453; SER-566; SER-580; SER-601 AND SER-603, 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 [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-598 AND SER-601, 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 [24] 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 [25] RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 13-136, 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). CC -!- FUNCTION: mRNA-binding protein that acts as a regulator of mRNAs CC translation and/or stability, and which is required for adult CC hippocampal neurogenesis (By similarity). Specifically binds to AU-rich CC elements (AREs) in the 3'-UTR of target mRNAs (By similarity). Promotes CC formation of some phase-separated membraneless compartment by CC undergoing liquid-liquid phase separation upon binding to AREs- CC containing mRNAs: mRNAs storage into membraneless compartments CC regulates their translation and/or stability (By similarity). Acts as a CC regulator of adult hippocampal neurogenesis by regulating translation CC and/or stability of NOG mRNA, thereby preventing NOG protein expression CC in the dentate gyrus (By similarity). {ECO:0000250|UniProtKB:Q61584, CC ECO:0000250|UniProtKB:Q9WVR4}. CC -!- SUBUNIT: Interacts with FMR1 (PubMed:7489725, PubMed:8668200, CC PubMed:11157796). Interacts with FXR1 (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:Q9WVR4, 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-FXR2 CC complexes bind viral RNAs and probably orchestrate the assembly of CC viral replication complexes. {ECO:0000269|PubMed:27509095}. CC -!- INTERACTION: CC P51116; Q9BXS5: AP1M1; NbExp=7; IntAct=EBI-740459, EBI-541426; CC P51116; Q15041: ARL6IP1; NbExp=3; IntAct=EBI-740459, EBI-714543; CC P51116; Q9UIF8: BAZ2B; NbExp=3; IntAct=EBI-740459, EBI-741542; CC P51116; Q9UIF8-2: BAZ2B; NbExp=3; IntAct=EBI-740459, EBI-10321972; CC P51116; P51451: BLK; NbExp=3; IntAct=EBI-740459, EBI-2105445; CC P51116; Q13895: BYSL; NbExp=8; IntAct=EBI-740459, EBI-358049; CC P51116; Q5T681: C10orf62; NbExp=4; IntAct=EBI-740459, EBI-744052; CC P51116; Q13557: CAMK2D; NbExp=3; IntAct=EBI-740459, EBI-351018; CC P51116; P35520: CBS; NbExp=3; IntAct=EBI-740459, EBI-740135; CC P51116; Q8IVW4: CDKL3; NbExp=7; IntAct=EBI-740459, EBI-3919850; CC P51116; Q9C0F1: CEP44; NbExp=3; IntAct=EBI-740459, EBI-744115; CC P51116; Q53EZ4: CEP55; NbExp=3; IntAct=EBI-740459, EBI-747776; CC P51116; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-740459, EBI-5453285; CC P51116; Q04637-9: EIF4G1; NbExp=3; IntAct=EBI-740459, EBI-12012124; CC P51116; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-740459, EBI-6658203; CC P51116; P09467: FBP1; NbExp=3; IntAct=EBI-740459, EBI-712740; CC P51116; Q06787: FMR1; NbExp=3; IntAct=EBI-740459, EBI-366305; CC P51116; Q06787-8: FMR1; NbExp=3; IntAct=EBI-740459, EBI-10224470; CC P51116; Q8IXW7: FMR1; NbExp=4; IntAct=EBI-740459, EBI-11976595; CC P51116; P02794: FTH1; NbExp=3; IntAct=EBI-740459, EBI-713259; CC P51116; P51114: FXR1; NbExp=3; IntAct=EBI-740459, EBI-713291; CC P51116; P51116: FXR2; NbExp=3; IntAct=EBI-740459, EBI-740459; CC P51116; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-740459, EBI-2549423; CC P51116; Q6NT76-2: HMBOX1; NbExp=3; IntAct=EBI-740459, EBI-10212206; CC P51116; Q86VF2-5: IGFN1; NbExp=3; IntAct=EBI-740459, EBI-11955401; CC P51116; Q15735: INPP5J; NbExp=3; IntAct=EBI-740459, EBI-10236940; CC P51116; Q14847: LASP1; NbExp=3; IntAct=EBI-740459, EBI-742828; CC P51116; Q9UIC8: LCMT1; NbExp=2; IntAct=EBI-740459, EBI-747632; CC P51116; Q13094: LCP2; NbExp=7; IntAct=EBI-740459, EBI-346946; CC P51116; O95751: LDOC1; NbExp=3; IntAct=EBI-740459, EBI-740738; CC P51116; Q9NS73: MBIP; NbExp=3; IntAct=EBI-740459, EBI-741953; CC P51116; Q96EZ8: MCRS1; NbExp=4; IntAct=EBI-740459, EBI-348259; CC P51116; Q9HAF1: MEAF6; NbExp=3; IntAct=EBI-740459, EBI-399266; CC P51116; P55081: MFAP1; NbExp=6; IntAct=EBI-740459, EBI-1048159; CC P51116; Q5JRA6-2: MIA3; NbExp=3; IntAct=EBI-740459, EBI-10244342; CC P51116; Q9BU76: MMTAG2; NbExp=6; IntAct=EBI-740459, EBI-742459; CC P51116; Q9UBU8: MORF4L1; NbExp=3; IntAct=EBI-740459, EBI-399246; CC P51116; Q9UBU8-2: MORF4L1; NbExp=3; IntAct=EBI-740459, EBI-10288852; CC P51116; Q8N983: MRPL43; NbExp=3; IntAct=EBI-740459, EBI-1043145; CC P51116; Q0ZGT2-4: NEXN; NbExp=3; IntAct=EBI-740459, EBI-10977819; CC P51116; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-740459, EBI-740897; CC P51116; P15531: NME1; NbExp=4; IntAct=EBI-740459, EBI-741141; CC P51116; P49902: NT5C2; NbExp=3; IntAct=EBI-740459, EBI-742084; CC P51116; Q96CV9: OPTN; NbExp=3; IntAct=EBI-740459, EBI-748974; CC P51116; Q8N7H5: PAF1; NbExp=4; IntAct=EBI-740459, EBI-2607770; CC P51116; P22234: PAICS; NbExp=4; IntAct=EBI-740459, EBI-712261; CC P51116; P61457: PCBD1; NbExp=6; IntAct=EBI-740459, EBI-740475; CC P51116; P11309: PIM1; NbExp=3; IntAct=EBI-740459, EBI-696621; CC P51116; Q96HA1: POM121; NbExp=4; IntAct=EBI-740459, EBI-739990; CC P51116; Q96QH2: PRAM1; NbExp=7; IntAct=EBI-740459, EBI-2860740; CC P51116; Q03393: PTS; NbExp=4; IntAct=EBI-740459, EBI-712344; CC P51116; Q9UI14: RABAC1; NbExp=3; IntAct=EBI-740459, EBI-712367; CC P51116; O95171: SCEL; NbExp=4; IntAct=EBI-740459, EBI-7543896; CC P51116; P78362: SRPK2; NbExp=4; IntAct=EBI-740459, EBI-593303; CC P51116; Q5T7P8-2: SYT6; NbExp=6; IntAct=EBI-740459, EBI-10246152; CC P51116; Q96C24: SYTL4; NbExp=6; IntAct=EBI-740459, EBI-747142; CC P51116; Q9NU19: TBC1D22B; NbExp=5; IntAct=EBI-740459, EBI-8787464; CC P51116; Q14157: UBAP2L; NbExp=4; IntAct=EBI-740459, EBI-347762; CC P51116; P07947: YES1; NbExp=6; IntAct=EBI-740459, EBI-515331; CC P51116; O15209: ZBTB22; NbExp=3; IntAct=EBI-740459, EBI-723574; CC P51116; Q96NC0: ZMAT2; NbExp=6; IntAct=EBI-740459, EBI-2682299; CC P51116; Q9UNY5: ZNF232; NbExp=3; IntAct=EBI-740459, EBI-749023; CC P51116; PRO_0000449621 [P0DTD1]: rep; Xeno; NbExp=5; IntAct=EBI-740459, EBI-25492388; CC P51116; PRO_0000449627 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-740459, EBI-25475877; CC -!- SUBCELLULAR LOCATION: Cytoplasm, Cytoplasmic ribonucleoprotein granule CC {ECO:0000250|UniProtKB:Q61584}. Cytoplasm {ECO:0000269|PubMed:9259278}. CC Postsynapse {ECO:0000250|UniProtKB:Q9WVR4}. Note=Specifically localizes CC to cytoplasmic ribonucleoprotein membraneless compartments (By CC similarity). Localization to the post-synaptic region is dependent on CC FMR1 (By similarity). {ECO:0000250|UniProtKB:Q61584, CC ECO:0000250|UniProtKB:Q9WVR4}. CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined including heart, CC brain, kidney and testis (PubMed:9259278). In brain, present at high CC level in neurons and especially in the Purkinje cells at the interface CC between the granular layer and the molecular layer (at protein level) CC (PubMed:9259278). {ECO:0000269|PubMed:9259278}. 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 -!- 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; U31501; AAC50292.1; -; mRNA. DR EMBL; BT009817; AAP88819.1; -; mRNA. DR EMBL; AK313836; BAG36569.1; -; mRNA. DR EMBL; CH471108; EAW90154.1; -; Genomic_DNA. DR EMBL; CH471108; EAW90155.1; -; Genomic_DNA. DR EMBL; BC020090; AAH20090.1; -; mRNA. DR EMBL; BC051907; AAH51907.1; -; mRNA. DR EMBL; BC067272; AAH67272.1; -; mRNA. DR EMBL; AF044263; AAC03357.1; -; Genomic_DNA. DR CCDS; CCDS45604.1; -. DR PIR; S60173; S60173. DR RefSeq; NP_004851.2; NM_004860.3. DR PDB; 3H8Z; X-ray; 1.92 A; A=13-136. DR PDBsum; 3H8Z; -. DR AlphaFoldDB; P51116; -. DR SMR; P51116; -. DR BioGRID; 114890; 443. DR IntAct; P51116; 252. DR MINT; P51116; -. DR STRING; 9606.ENSP00000250113; -. DR BindingDB; P51116; -. DR ChEMBL; CHEMBL5169136; -. DR CarbonylDB; P51116; -. DR GlyCosmos; P51116; 1 site, 1 glycan. DR GlyGen; P51116; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P51116; -. DR MetOSite; P51116; -. DR PhosphoSitePlus; P51116; -. DR SwissPalm; P51116; -. DR BioMuta; FXR2; -. DR DMDM; 90177782; -. DR EPD; P51116; -. DR jPOST; P51116; -. DR MassIVE; P51116; -. DR MaxQB; P51116; -. DR PaxDb; 9606-ENSP00000250113; -. DR PeptideAtlas; P51116; -. DR ProteomicsDB; 56281; -. DR Pumba; P51116; -. DR ABCD; P51116; 5 sequenced antibodies. DR Antibodypedia; 4407; 376 antibodies from 34 providers. DR DNASU; 9513; -. DR Ensembl; ENST00000250113.12; ENSP00000250113.7; ENSG00000129245.13. DR GeneID; 9513; -. DR KEGG; hsa:9513; -. DR MANE-Select; ENST00000250113.12; ENSP00000250113.7; NM_004860.4; NP_004851.2. DR UCSC; uc002gia.3; human. DR AGR; HGNC:4024; -. DR CTD; 9513; -. DR DisGeNET; 9513; -. DR GeneCards; FXR2; -. DR HGNC; HGNC:4024; FXR2. DR HPA; ENSG00000129245; Tissue enhanced (skeletal). DR MIM; 605339; gene. DR neXtProt; NX_P51116; -. DR OpenTargets; ENSG00000129245; -. DR PharmGKB; PA28440; -. DR VEuPathDB; HostDB:ENSG00000129245; -. DR eggNOG; ENOG502QPKJ; Eukaryota. DR GeneTree; ENSGT00950000183189; -. DR HOGENOM; CLU_020699_3_0_1; -. DR InParanoid; P51116; -. DR OMA; EDRTIMD; -. DR OrthoDB; 2995592at2759; -. DR PhylomeDB; P51116; -. DR TreeFam; TF105427; -. DR PathwayCommons; P51116; -. DR SignaLink; P51116; -. DR BioGRID-ORCS; 9513; 12 hits in 1161 CRISPR screens. DR ChiTaRS; FXR2; human. DR EvolutionaryTrace; P51116; -. DR GeneWiki; FXR2; -. DR GenomeRNAi; 9513; -. DR Pharos; P51116; Tbio. DR PRO; PR:P51116; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P51116; Protein. DR Bgee; ENSG00000129245; Expressed in apex of heart and 206 other cell types or tissues. DR ExpressionAtlas; P51116; baseline and differential. DR GO; GO:0030424; C:axon; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; IDA:CACAO. DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IBA:GO_Central. 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: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:0005634; C:nucleus; IBA:GO_Central. 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:0042802; F:identical protein binding; IPI:IntAct. 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:0045182; F:translation regulator activity; IBA:GO_Central. DR GO; GO:0021542; P:dentate gyrus development; ISS:UniProtKB. DR GO; GO:0061157; P:mRNA destabilization; ISS:UniProtKB. DR GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; 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 CDD; cd22505; KH_I_FXR2_rpt1; 1. DR CDD; cd22508; KH_I_FXR2_rpt2; 1. DR CDD; cd22511; KH_I_FXR2_rpt3; 1. DR CDD; cd20473; Tudor_Agenet_FXR2_rpt1; 1. DR CDD; cd20476; Tudor_Agenet_FXR2_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; IPR004087; KH_dom. DR InterPro; IPR004088; KH_dom_type_1. DR InterPro; IPR036612; KH_dom_type_1_sf. DR InterPro; IPR047422; KH_I_FXR2_rpt1. DR InterPro; IPR047424; KH_I_FXR2_rpt2. DR InterPro; IPR047421; Tudor_Agenet_FXR2_rpt1. DR InterPro; IPR047420; Tudor_Agenet_FXR2_rpt2. DR InterPro; IPR041560; Tudor_FRM1. DR PANTHER; PTHR10603; FRAGILE X MENTAL RETARDATION SYNDROME-RELATED PROTEIN; 1. DR PANTHER; PTHR10603:SF3; FRAGILE X MENTAL RETARDATION SYNDROME-RELATED PROTEIN 2; 1. DR Pfam; PF05641; Agenet; 1. DR Pfam; PF12235; FXMRP1_C_core; 1. DR Pfam; PF16096; FXR_C1; 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; P51116; HS. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Phosphoprotein; Reference proteome; Repeat; KW RNA-binding; Synapse. FT CHAIN 1..673 FT /note="RNA-binding protein FXR2" FT /id="PRO_0000050110" FT DOMAIN 14..60 FT /note="Agenet-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00973" FT DOMAIN 73..125 FT /note="Agenet-like 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00973" FT DOMAIN 232..261 FT /note="KH 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117" FT DOMAIN 295..324 FT /note="KH 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117" FT REGION 389..673 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 407..424 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 453..486 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 500..523 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 623..637 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 78 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q61584" FT MOD_RES 192 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 410 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 411 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 450 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q61584" FT MOD_RES 453 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 533 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 566 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 580 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 598 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:24275569" FT MOD_RES 601 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 603 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT VARIANT 252 FT /note="Q -> H (in dbSNP:rs17854734)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_067039" FT VARIANT 591 FT /note="R -> P (in dbSNP:rs36013555)" FT /id="VAR_055979" FT CONFLICT 625..626 FT /note="RP -> SA (in Ref. 1; AAC50292)" FT /evidence="ECO:0000305" FT STRAND 15..19 FT /evidence="ECO:0007829|PDB:3H8Z" FT STRAND 25..33 FT /evidence="ECO:0007829|PDB:3H8Z" FT STRAND 35..42 FT /evidence="ECO:0007829|PDB:3H8Z" FT STRAND 50..53 FT /evidence="ECO:0007829|PDB:3H8Z" FT HELIX 54..56 FT /evidence="ECO:0007829|PDB:3H8Z" FT STRAND 74..79 FT /evidence="ECO:0007829|PDB:3H8Z" FT STRAND 88..98 FT /evidence="ECO:0007829|PDB:3H8Z" FT STRAND 101..106 FT /evidence="ECO:0007829|PDB:3H8Z" FT STRAND 115..117 FT /evidence="ECO:0007829|PDB:3H8Z" FT HELIX 119..121 FT /evidence="ECO:0007829|PDB:3H8Z" FT STRAND 122..124 FT /evidence="ECO:0007829|PDB:3H8Z" SQ SEQUENCE 673 AA; 74223 MW; B8A498C3F634D41F CRC64; MGGLASGGDV EPGLPVEVRG SNGAFYKGFV KDVHEDSVTI FFENNWQSER QIPFGDVRLP PPADYNKEIT EGDEVEVYSR ANEQEPCGWW LARVRMMKGD FYVIEYAACD ATYNEIVTLE RLRPVNPNPL ATKGSFFKVT MAVPEDLREA CSNENVHKEF KKALGANCIF LNITNSELFI LSTTEAPVKR ASLLGDMHFR SLRTKLLLMS RNEEATKHLE TSKQLAAAFQ EEFTVREDLM GLAIGTHGAN IQQARKVPGV TAIELGEETC TFRIYGETPE ACRQARSYLE FSEDSVQVPR NLVGKVIGKN GKVIQEIVDK SGVVRVRVEG DNDKKNPREE GMVPFIFVGT RENISNAQAL LEYHLSYLQE VEQLRLERLQ IDEQLRQIGL GFRPPGSGRG SGGSDKAGYS TDESSSSSLH ATRTYGGSYG GRGRGRRTGG PAYGPSSDVS TASETESEKR EEPNRAGPGD RDPPTRGEES RRRPTGGRGR GPPPAPRPTS RYNSSSISSV LKDPDSNPYS LLDTSEPEPP VDSEPGEPPP ASARRRRSRR RRTDEDRTVM DGGLESDGPN MTENGLEDES RPQRRNRSRR RRNRGNRTDG SISGDRQPVT VADYISRAES QSRQRPPLER TKPSEDSLSG QKGDSVSKLP KGPSENGELS APLELGSMVN GVS //