ID FXR2_MOUSE Reviewed; 673 AA. AC Q9WVR4; Q9WVR5; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 03-AUG-2022, entry version 136. DE RecName: Full=RNA-binding protein FXR2 {ECO:0000305}; GN Name=Fxr2 {ECO:0000312|MGI:MGI:1346074}; Synonyms=Fxr2h; 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; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC STRAIN=129; RX PubMed=10524236; DOI=10.1016/s0378-1119(99)00301-7; RA Miyashita A., Shimizu N., Endo N., Hanyuu T., Ishii N., Ito K., Itoh Y., RA Shirai M., Nakajima T., Odani S., Kuwano R.; RT "Five different genes, Eif4a1, Cd68, Supl15h, Sox15 and Fxr2h, are RT clustered in a 40 kb region of mouse chromosome 11."; RL Gene 237:53-60(1999). RN [2] RP INTERACTION WITH CYFIP2. RX PubMed=11438699; DOI=10.1073/pnas.151231598; RA Schenck A., Bardoni B., Moro A., Bagni C., Mandel J.-L.; RT "A highly conserved protein family interacting with the fragile X mental RT retardation protein (FMRP) and displaying selective interactions with FMRP- RT related proteins FXR1P and FXR2P."; RL Proc. Natl. Acad. Sci. U.S.A. 98:8844-8849(2001). RN [3] 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 [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; 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] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200; RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; RT "Large scale localization of protein phosphorylation by use of electron RT capture dissociation mass spectrometry."; RL Mol. Cell. Proteomics 8:904-912(2009). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-413; SER-602 AND SER-604, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and RC Testis; 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). CC -!- FUNCTION: RNA-binding protein. {ECO:0000250}. CC -!- SUBUNIT: Interacts with FMR1 (By similarity). Interacts with FXR1 (By CC similarity). Interacts with TDRD3 (By similarity). Interacts with HABP4 CC (By similarity). Interacts with CYFIP2 but not with CYFIP1 CC (PubMed:11438699). {ECO:0000250|UniProtKB:P51116, CC ECO:0000269|PubMed:11438699}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- DOMAIN: The tandem Agenet-like domains preferentially recognize CC trimethylated histone peptides. {ECO:0000250}. 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; AB025269; BAA82147.1; -; mRNA. DR EMBL; AB025311; BAA82249.1; -; Genomic_DNA. DR AlphaFoldDB; Q9WVR4; -. DR SMR; Q9WVR4; -. DR IntAct; Q9WVR4; 7. DR MINT; Q9WVR4; -. DR STRING; 10090.ENSMUSP00000018909; -. DR iPTMnet; Q9WVR4; -. DR PhosphoSitePlus; Q9WVR4; -. DR EPD; Q9WVR4; -. DR jPOST; Q9WVR4; -. DR MaxQB; Q9WVR4; -. DR PaxDb; Q9WVR4; -. DR PeptideAtlas; Q9WVR4; -. DR PRIDE; Q9WVR4; -. DR ProteomicsDB; 266892; -. DR MGI; MGI:1346074; Fxr2. DR eggNOG; ENOG502QPKJ; Eukaryota. DR InParanoid; Q9WVR4; -. DR ChiTaRS; Fxr2; mouse. DR PRO; PR:Q9WVR4; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; Q9WVR4; protein. DR GO; GO:0030424; C:axon; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0030425; C:dendrite; IDA:MGI. 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; IDA:SynGO. DR GO; GO:0030426; C:growth cone; IBA:GO_Central. DR GO; GO:0016020; C:membrane; IBA:GO_Central. 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; IDA:MGI. DR GO; GO:0098794; C:postsynapse; IDA:SynGO. 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; ISO:MGI. DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central. DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; ISS: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 Cytoplasm; Phosphoprotein; Reference proteome; Repeat; RNA-binding. FT CHAIN 1..673 FT /note="RNA-binding protein FXR2" FT /id="PRO_0000050111" 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 228..276 FT /note="KH 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117" FT DOMAIN 291..340 FT /note="KH 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117" FT REGION 388..673 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 409..427 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 455..488 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 501..524 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 615..644 FT /note="Polar 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:0000250|UniProtKB:P51116" FT MOD_RES 413 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 452 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q61584" FT MOD_RES 455 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P51116" FT MOD_RES 465 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q61584" FT MOD_RES 534 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P51116" FT MOD_RES 567 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P51116" FT MOD_RES 581 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P51116" FT MOD_RES 599 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P51116" FT MOD_RES 602 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 604 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" SQ SEQUENCE 673 AA; 73743 MW; 01F6814D4C3B5654 CRC64; MGGLASGGDV EPGLPVEVRG SNGAFYKGFV KDVHEDSVTI FFENNWQSER QIPFGDVRLP PPADYNKEIT EGDEVEVYSR ANEQEPCGWC LARVRMMKGD FYVIEYAACD ATYNEIVTLE RLRPVNSSSL ATKGSFFKVT MAVPEDLREA CSNENVHKEF KKALGANCIF LNITNSELFI LSTTEAPVKR ASLLGDMHFR SLRTKLLLMS RNEEATKHLE TSKQLAAAFQ EEFTVREDLM GLAIGTHGAN IQQARKVPGV TAIELGEETC TFRIYGETPE ACRQARSYLE FSEDSVQVPR DLVGKVTGKT GKVIQGIVDK SGVVRVRVEG DNDKKNPKEG GMVPFIFVGT RENISNAQAL LEYHLSYLQE VETLRLERLQ IDEQLRQIGA GFRPPGSGRG GSGGGSDKAG YTTDESSSSS LHTTRTYGGS YGGRGRGRRT GGPAYGPSSD PSTASETESE KREESNRAGP GDRDPPSRGE ESRRRRLGPG KGPPPVPRPT SRYNSSSISS VLKDPDSNPY SLLDTSEPEP PVDSEPGEPP PASARRRRSR RRRTDEDRTV MDGALESDGP NMTENGLEDE SRPQRRNRSR RRRNRGNRTD GSISGDRQPV TVADYISRAE SQSRQRPLGR TEPSEDSLSG QKGDSVSKLP KGPSENGELS APLELGSLVN GVS //