FXR2_HUMAN
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 03-AUG-2022, entry version 195.
DE RecName: Full=RNA-binding protein FXR2 {ECO:0000305};
DE AltName: Full=FMR1 autosomal homolog 2 {ECO:0000312|HGNC:HGNC:4024};
GN Name=FXR2 {ECO:0000312|HGNC:HGNC:4024}; 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 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 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 [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 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 [13]
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 [14]
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 [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 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 [17]
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 [18]
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 [19]
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 [20]
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 [21]
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 [22]
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 [23]
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 [24]
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: RNA-binding protein.
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; A0A0A0MR97: BAZ2B; NbExp=3; IntAct=EBI-740459, EBI-11985607;
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=4; IntAct=EBI-740459, EBI-25492388;
CC P51116; PRO_0000449627 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-740459, EBI-25475877;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: The tandem Agenet-like domains preferentially recognize
CC trimethylated histone peptides. {ECO:0000269|PubMed:21072162}.
CC -!- SIMILARITY: Belongs to the FMR1 family. {ECO:0000305}.
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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; 408.
DR IntAct; P51116; 237.
DR MINT; P51116; -.
DR STRING; 9606.ENSP00000250113; -.
DR CarbonylDB; P51116; -.
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; P51116; -.
DR PeptideAtlas; P51116; -.
DR PRIDE; P51116; -.
DR ProteomicsDB; 56281; -.
DR ABCD; P51116; 5 sequenced antibodies.
DR Antibodypedia; 4407; 346 antibodies from 34 providers.
DR DNASU; 9513; -.
DR Ensembl; ENST00000250113.12; ENSP00000250113.7; ENSG00000129245.12.
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 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; 374073at2759; -.
DR PhylomeDB; P51116; -.
DR TreeFam; TF105427; -.
DR PathwayCommons; P51116; -.
DR SignaLink; P51116; -.
DR BioGRID-ORCS; 9513; 12 hits in 1083 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 204 other tissues.
DR ExpressionAtlas; P51116; baseline and differential.
DR Genevisible; P51116; HS.
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:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; TAS:ProtInc.
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: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: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 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; 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; 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; SSF54791; 2.
DR PROSITE; PS51641; AGENET_LIKE; 2.
DR PROSITE; PS50084; KH_TYPE_1; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding.
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
