ID A0A0G2JEP0_MOUSE Unreviewed; 568 AA. AC A0A0G2JEP0; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 29-MAY-2024, entry version 57. DE RecName: Full=RNA-binding protein FXR1 {ECO:0000256|ARBA:ARBA00034847}; GN Name=Fxr1 {ECO:0000313|Ensembl:ENSMUSP00000142847.2, GN ECO:0000313|MGI:MGI:104860}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000142847.2, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0007829|PubMed:15592455} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [2] {ECO:0007829|PubMed:16452087} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200; RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.; RT "Comprehensive identification of phosphorylation sites in postsynaptic RT density preparations."; RL Mol. Cell. Proteomics 5:914-922(2006). RN [3] {ECO:0007829|PubMed:17947660} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17947660; RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., RA Kawakami T., Salomon A.R.; RT "Quantitative time-resolved phosphoproteomic analysis of mast cell RT signaling."; RL J. Immunol. 179:5864-5876(2007). RN [4] {ECO:0007829|PubMed:17242355} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [5] {ECO:0000313|Ensembl:ENSMUSP00000142847.2, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000142847.2, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [6] {ECO:0007829|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [7] {ECO:0000313|Ensembl:ENSMUSP00000142847.2} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000142847.2}; RG Ensembl; RL Submitted (FEB-2024) to UniProtKB. CC -!- SUBCELLULAR LOCATION: Cell projection, dendritic spine CC {ECO:0000256|ARBA:ARBA00004552}. Cytoplasm, Cytoplasmic CC ribonucleoprotein granule {ECO:0000256|ARBA:ARBA00004331}. Postsynapse CC {ECO:0000256|ARBA:ARBA00034110}. Synapse CC {ECO:0000256|ARBA:ARBA00034103}. CC -!- SIMILARITY: Belongs to the FMR1 family. CC {ECO:0000256|ARBA:ARBA00006633}. 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 RefSeq; XP_006535465.1; XM_006535402.1. DR AlphaFoldDB; A0A0G2JEP0; -. DR SMR; A0A0G2JEP0; -. DR jPOST; A0A0G2JEP0; -. DR ProteomicsDB; 345372; -. DR Antibodypedia; 18845; 387 antibodies from 39 providers. DR DNASU; 14359; -. DR Ensembl; ENSMUST00000198051.5; ENSMUSP00000142847.2; ENSMUSG00000027680.16. DR GeneID; 14359; -. DR AGR; MGI:104860; -. DR CTD; 8087; -. DR MGI; MGI:104860; Fxr1. DR VEuPathDB; HostDB:ENSMUSG00000027680; -. DR GeneTree; ENSGT00950000183189; -. DR OrthoDB; 2995592at2759; -. DR BioGRID-ORCS; 14359; 0 hits in 78 CRISPR screens. DR Proteomes; UP000000589; Chromosome 3. DR Bgee; ENSMUSG00000027680; Expressed in seminiferous tubule of testis and 256 other cell types or tissues. DR ExpressionAtlas; A0A0G2JEP0; baseline and differential. DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IEA:UniProtKB-SubCell. DR GO; GO:1902737; C:dendritic filopodium; IEA:TreeGrafter. DR GO; GO:0044326; C:dendritic spine neck; IEA:TreeGrafter. DR GO; GO:0030426; C:growth cone; IEA:TreeGrafter. DR GO; GO:0016020; C:membrane; IEA:TreeGrafter. DR GO; GO:0043025; C:neuronal cell body; IEA:TreeGrafter. DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter. DR GO; GO:0014069; C:postsynaptic density; IEA:TreeGrafter. DR GO; GO:0098793; C:presynapse; IEA:TreeGrafter. DR GO; GO:0003730; F:mRNA 3'-UTR binding; IEA:TreeGrafter. DR GO; GO:0042803; F:protein homodimerization activity; IEA:TreeGrafter. DR GO; GO:0045182; F:translation regulator activity; IEA:TreeGrafter. DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW. DR GO; GO:0017148; P:negative regulation of translation; IEA:TreeGrafter. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:TreeGrafter. DR GO; GO:0045727; P:positive regulation of translation; IEA:TreeGrafter. DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IEA:TreeGrafter. DR GO; GO:0051489; P:regulation of filopodium assembly; IEA:TreeGrafter. DR GO; GO:0043488; P:regulation of mRNA stability; IEA:TreeGrafter. 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; 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; 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. PE 1: Evidence at protein level; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Myogenesis {ECO:0000256|ARBA:ARBA00022541}; KW Proteomics identification {ECO:0007829|EPD:A0A0G2JEP0, KW ECO:0007829|MaxQB:A0A0G2JEP0}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE- KW ProRule:PRU00117}. FT DOMAIN 4..50 FT /note="Agenet-like" FT /evidence="ECO:0000259|PROSITE:PS51641" FT DOMAIN 63..115 FT /note="Agenet-like" FT /evidence="ECO:0000259|PROSITE:PS51641" FT REGION 380..568 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 438..473 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 496..518 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 568 AA; 63915 MW; 2087AA7D0C7AAFD6 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 TFRIYGESAE AVKKARGFLE FVEDFIQVPR NLVGKVIGKN GKVIQEIVDK SGVVRVRIEG DNENKLPRED GMVPFVFVGT KESIGNVQVL LEYHIAYLKE VEQLRMERLQ IDEQLRQIGM GFRPSSTRGP EREKGYATDE STVSSVQGSR SYSGRGRGRR GPNYTSGYGT NSELSNPSET ESERKDELSD WSLAGEDDRE TRHQRDSRRR PGGRGRSVSG GRGRGGPRGG KSSISSVLKD PDSNPYSLLD NTESDQTADT DASESHHSTN RRRRSRRRRT DEDAVLMDGL TESDTASVNE NGLGKRCD //