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 28-MAR-2018, entry version 120. DE RecName: Full=Fragile X mental retardation syndrome-related protein 2; GN Name=Fxr2; Synonyms=Fxr2h; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; 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., RA Itoh Y., 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 RT mental retardation protein (FMRP) and displaying selective RT interactions with FMRP-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 RT 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 RT electron 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 RP SER-604, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Spleen, and 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 RT expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: RNA-binding protein. {ECO:0000250}. CC -!- SUBUNIT: Interacts with FMR1 (By similarity). Interacts with FXR1 CC (By similarity). Interacts with TDRD3 (By similarity). Interacts CC with HABP4 (By similarity). Interacts with CYFIP2 but not with CC CYFIP1 (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 UniGene; Mm.41930; -. DR ProteinModelPortal; 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 MaxQB; Q9WVR4; -. DR PaxDb; Q9WVR4; -. DR PeptideAtlas; Q9WVR4; -. DR PRIDE; Q9WVR4; -. DR MGI; MGI:1346074; Fxr2. DR eggNOG; ENOG410IF9J; Eukaryota. DR eggNOG; ENOG410ZDJG; LUCA. DR HOVERGEN; HBG005739; -. DR InParanoid; Q9WVR4; -. DR ChiTaRS; Fxr2; mouse. DR PRO; PR:Q9WVR4; -. DR Proteomes; UP000000589; Unplaced. DR CleanEx; MM_FXR2; -. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0030425; C:dendrite; IDA:MGI. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005844; C:polysome; IDA:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0003729; F:mRNA 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:0017148; P:negative regulation of translation; IBA:GO_Central. DR Gene3D; 3.30.1370.10; -; 2. DR InterPro; IPR008395; Agenet-like_dom. 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 Pfam; PF05641; Agenet; 1. DR Pfam; PF12235; FXMRP1_C_core; 1. DR Pfam; PF16096; FXR_C1; 1. DR Pfam; PF00013; KH_1; 2. 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 Complete proteome; Cytoplasm; Phosphoprotein; Reference proteome; KW Repeat; RNA-binding. FT CHAIN 1 673 Fragile X mental retardation syndrome- FT related protein 2. FT /FTId=PRO_0000050111. FT DOMAIN 14 60 Agenet-like 1. {ECO:0000255|PROSITE- FT ProRule:PRU00973}. FT DOMAIN 73 125 Agenet-like 2. {ECO:0000255|PROSITE- FT ProRule:PRU00973}. FT DOMAIN 228 276 KH 1. {ECO:0000255|PROSITE- FT ProRule:PRU00117}. FT DOMAIN 291 340 KH 2. {ECO:0000255|PROSITE- FT ProRule:PRU00117}. FT COMPBIAS 416 420 Poly-Ser. FT COMPBIAS 483 486 Poly-Arg. FT COMPBIAS 545 553 Poly-Arg. FT COMPBIAS 585 595 Poly-Arg. FT MOD_RES 78 78 Phosphotyrosine. FT {ECO:0000250|UniProtKB:Q61584}. FT MOD_RES 192 192 Phosphoserine. FT {ECO:0000250|UniProtKB:P51116}. FT MOD_RES 413 413 Phosphothreonine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 452 452 Phosphoserine. FT {ECO:0000250|UniProtKB:Q61584}. FT MOD_RES 455 455 Phosphoserine. FT {ECO:0000250|UniProtKB:P51116}. FT MOD_RES 465 465 Phosphoserine. FT {ECO:0000250|UniProtKB:Q61584}. FT MOD_RES 534 534 Phosphoserine. FT {ECO:0000250|UniProtKB:P51116}. FT MOD_RES 567 567 Phosphoserine. FT {ECO:0000250|UniProtKB:P51116}. FT MOD_RES 581 581 Phosphoserine. FT {ECO:0000250|UniProtKB:P51116}. FT MOD_RES 599 599 Phosphothreonine. FT {ECO:0000250|UniProtKB:P51116}. FT MOD_RES 602 602 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 604 604 Phosphoserine. FT {ECO:0000244|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 //