FXR1_MOUSE
ID FXR1_MOUSE Reviewed; 677 AA.
AC Q61584; Q8VCU4; Q9R1E2; Q9R1E3; Q9R1E4; Q9R1E5; Q9WUA7; Q9WUA8; Q9WUA9;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=RNA-binding protein FXR1 {ECO:0000305};
DE AltName: Full=mFxr1p;
GN Name=Fxr1; Synonyms=Fxr1h;
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 [MRNA] (ISOFORM A).
RC TISSUE=Fetal brain;
RX PubMed=8634689; DOI=10.1093/hmg/4.12.2209;
RA Coy J.F., Sedlacek Z., Baechner D., Hameister H., Joos S., Lichter P.,
RA Delius H., Poustka A.;
RT "Highly conserved 3' UTR and expression pattern of FXR1 points to a
RT divergent gene regulation of FXR1 and FMR1.";
RL Hum. Mol. Genet. 4:2209-2218(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS A; B; C; D; E; F AND G),
RP AND TISSUE SPECIFICITY.
RX PubMed=10409431; DOI=10.1006/geno.1999.5868;
RA Kirkpatrick L.L., McIlwain K.A., Nelson D.L.;
RT "Alternative splicing in the murine and human FXR1 genes.";
RL Genomics 59:193-202(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC TISSUE=Kidney;
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 [4]
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15128702; DOI=10.1093/hmg/ddh150;
RA Mientjes E.J., Willemsen R., Kirkpatrick L.L., Nieuwenhuizen I.M.,
RA Hoogeveen-Westerveld M., Verweij M., Reis S., Bardoni B., Hoogeveen A.T.,
RA Oostra B.A., Nelson D.L.;
RT "Fxr1 knockout mice show a striated muscle phenotype: implications for
RT Fxr1p function in vivo.";
RL Hum. Mol. Genet. 13:1291-1302(2004).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=16000371; DOI=10.1091/mbc.e05-04-0304;
RA Huot M.-E., Bisson N., Davidovic L., Mazroui R., Labelle Y., Moss T.,
RA Khandjian E.W.;
RT "The RNA-binding protein Fragile X-related 1 regulates somite formation in
RT Xenopus laevis.";
RL Mol. Biol. Cell 16:4350-4361(2005).
RN [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-68, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435 AND SER-449, AND
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435; SER-438; THR-512 AND
RP SER-643, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
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 expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=30770808; DOI=10.1038/s41467-019-08548-9;
RA Estan M.C., Fernandez-Nunez E., Zaki M.S., Esteban M.I., Donkervoort S.,
RA Hawkins C., Caparros-Martin J.A., Saade D., Hu Y., Bolduc V., Chao K.R.,
RA Nevado J., Lamuedra A., Largo R., Herrero-Beaumont G., Regadera J.,
RA Hernandez-Chico C., Tizzano E.F., Martinez-Glez V., Carvajal J.J., Zong R.,
RA Nelson D.L., Otaify G.A., Temtamy S., Aglan M., Issa M., Boennemann C.G.,
RA Lapunzina P., Yoon G., Ruiz-Perez V.L.;
RT "Recessive mutations in muscle-specific isoforms of FXR1 cause congenital
RT multi-minicore myopathy.";
RL Nat. Commun. 10:797-797(2019).
CC -!- FUNCTION: RNA-binding protein required for embryonic and postnatal
CC development of muscle tissue. May regulate intracellular transport and
CC local translation of certain mRNAs. {ECO:0000269|PubMed:15128702}.
CC -!- SUBUNIT: Interacts with FMR1 (By similarity). Interacts with FRX2 (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:P51114,
CC ECO:0000269|PubMed:11438699}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:30770808}.
CC Note=Adjacent to Z-lines in muscles. {ECO:0000269|PubMed:30770808}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=E;
CC IsoId=Q61584-1; Sequence=Displayed;
CC Name=A;
CC IsoId=Q61584-2; Sequence=VSP_002836, VSP_002838, VSP_002840;
CC Name=B;
CC IsoId=Q61584-3; Sequence=VSP_002838;
CC Name=C;
CC IsoId=Q61584-4; Sequence=VSP_002839;
CC Name=D;
CC IsoId=Q61584-5; Sequence=VSP_002836, VSP_002839;
CC Name=F;
CC IsoId=Q61584-6; Sequence=VSP_002836;
CC Name=G;
CC IsoId=Q61584-7; Sequence=VSP_002837;
CC -!- TISSUE SPECIFICITY: In early embryogenesis, highest expression in
CC somites and central nervous system. Also expressed in spinal cord,
CC surrounding mesenchymal tissue and undifferentiated gonad. In mid-
CC embryogenesis, most prominent in gonad and muscle tissue. Also
CC expressed in liver, retina, telencephalon and mesencephalon. In late
CC embryogenesis, restricted to skeletal muscle and proliferative active
CC layers of brain. After birth, highly expressed in postmeiotic
CC spermatids. Intermediate levels are found in heart, liver and kidney
CC with lower levels in brain and skeletal muscle. Isoform(s) containing
CC the 27 amino acid pocket (residues 564-590) are present in adult heart
CC and muscle. {ECO:0000269|PubMed:10409431, ECO:0000269|PubMed:16000371}.
CC -!- DOMAIN: The tandem Agenet-like domains preferentially recognize
CC trimethylated histone peptides. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Death shortly after birth. Mice expressing low
CC levels of Fxr1 show postnatal growth retardation with reduced increase
CC in muscle mass and strength. They die within 3 weeks of birth.
CC {ECO:0000269|PubMed:15128702}.
CC -!- SIMILARITY: Belongs to the FMR1 family. {ECO:0000305}.
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DR EMBL; X90875; CAA62383.1; -; mRNA.
DR EMBL; AF124385; AAD30211.1; -; mRNA.
DR EMBL; AF124394; AAD30212.1; -; Genomic_DNA.
DR EMBL; AF124386; AAD30212.1; JOINED; Genomic_DNA.
DR EMBL; AF124387; AAD30212.1; JOINED; Genomic_DNA.
DR EMBL; AF124388; AAD30212.1; JOINED; Genomic_DNA.
DR EMBL; AF124389; AAD30212.1; JOINED; Genomic_DNA.
DR EMBL; AF124390; AAD30212.1; JOINED; Genomic_DNA.
DR EMBL; AF124391; AAD30212.1; JOINED; Genomic_DNA.
DR EMBL; AF124392; AAD30212.1; JOINED; Genomic_DNA.
DR EMBL; AF124393; AAD30212.1; JOINED; Genomic_DNA.
DR EMBL; AF124394; AAD30213.1; -; Genomic_DNA.
DR EMBL; AF124386; AAD30213.1; JOINED; Genomic_DNA.
DR EMBL; AF124387; AAD30213.1; JOINED; Genomic_DNA.
DR EMBL; AF124388; AAD30213.1; JOINED; Genomic_DNA.
DR EMBL; AF124389; AAD30213.1; JOINED; Genomic_DNA.
DR EMBL; AF124390; AAD30213.1; JOINED; Genomic_DNA.
DR EMBL; AF124391; AAD30213.1; JOINED; Genomic_DNA.
DR EMBL; AF124392; AAD30213.1; JOINED; Genomic_DNA.
DR EMBL; AF124393; AAD30213.1; JOINED; Genomic_DNA.
DR EMBL; AF124394; AAD30214.1; -; Genomic_DNA.
DR EMBL; AF124386; AAD30214.1; JOINED; Genomic_DNA.
DR EMBL; AF124387; AAD30214.1; JOINED; Genomic_DNA.
DR EMBL; AF124388; AAD30214.1; JOINED; Genomic_DNA.
DR EMBL; AF124389; AAD30214.1; JOINED; Genomic_DNA.
DR EMBL; AF124390; AAD30214.1; JOINED; Genomic_DNA.
DR EMBL; AF124391; AAD30214.1; JOINED; Genomic_DNA.
DR EMBL; AF124392; AAD30214.1; JOINED; Genomic_DNA.
DR EMBL; AF124393; AAD30214.1; JOINED; Genomic_DNA.
DR EMBL; AF124394; AAD30215.1; -; Genomic_DNA.
DR EMBL; AF124386; AAD30215.1; JOINED; Genomic_DNA.
DR EMBL; AF124387; AAD30215.1; JOINED; Genomic_DNA.
DR EMBL; AF124388; AAD30215.1; JOINED; Genomic_DNA.
DR EMBL; AF124389; AAD30215.1; JOINED; Genomic_DNA.
DR EMBL; AF124390; AAD30215.1; JOINED; Genomic_DNA.
DR EMBL; AF124391; AAD30215.1; JOINED; Genomic_DNA.
DR EMBL; AF124392; AAD30215.1; JOINED; Genomic_DNA.
DR EMBL; AF124393; AAD30215.1; JOINED; Genomic_DNA.
DR EMBL; AF124394; AAD30216.1; -; Genomic_DNA.
DR EMBL; AF124386; AAD30216.1; JOINED; Genomic_DNA.
DR EMBL; AF124387; AAD30216.1; JOINED; Genomic_DNA.
DR EMBL; AF124388; AAD30216.1; JOINED; Genomic_DNA.
DR EMBL; AF124389; AAD30216.1; JOINED; Genomic_DNA.
DR EMBL; AF124390; AAD30216.1; JOINED; Genomic_DNA.
DR EMBL; AF124391; AAD30216.1; JOINED; Genomic_DNA.
DR EMBL; AF124392; AAD30216.1; JOINED; Genomic_DNA.
DR EMBL; AF124393; AAD30216.1; JOINED; Genomic_DNA.
DR EMBL; AF124394; AAD30217.1; -; Genomic_DNA.
DR EMBL; AF124386; AAD30217.1; JOINED; Genomic_DNA.
DR EMBL; AF124387; AAD30217.1; JOINED; Genomic_DNA.
DR EMBL; AF124388; AAD30217.1; JOINED; Genomic_DNA.
DR EMBL; AF124389; AAD30217.1; JOINED; Genomic_DNA.
DR EMBL; AF124390; AAD30217.1; JOINED; Genomic_DNA.
DR EMBL; AF124391; AAD30217.1; JOINED; Genomic_DNA.
DR EMBL; AF124392; AAD30217.1; JOINED; Genomic_DNA.
DR EMBL; AF124393; AAD30217.1; JOINED; Genomic_DNA.
DR EMBL; AF124394; AAD30218.1; -; Genomic_DNA.
DR EMBL; AF124386; AAD30218.1; JOINED; Genomic_DNA.
DR EMBL; AF124387; AAD30218.1; JOINED; Genomic_DNA.
DR EMBL; AF124388; AAD30218.1; JOINED; Genomic_DNA.
DR EMBL; AF124389; AAD30218.1; JOINED; Genomic_DNA.
DR EMBL; AF124390; AAD30218.1; JOINED; Genomic_DNA.
DR EMBL; AF124391; AAD30218.1; JOINED; Genomic_DNA.
DR EMBL; AF124392; AAD30218.1; JOINED; Genomic_DNA.
DR EMBL; AF124393; AAD30218.1; JOINED; Genomic_DNA.
DR EMBL; BC019139; AAH19139.1; -; mRNA.
DR CCDS; CCDS50890.1; -. [Q61584-2]
DR CCDS; CCDS50891.1; -. [Q61584-1]
DR CCDS; CCDS79896.1; -. [Q61584-5]
DR RefSeq; NP_001106659.1; NM_001113188.1. [Q61584-1]
DR RefSeq; NP_001106660.1; NM_001113189.1. [Q61584-5]
DR RefSeq; NP_032079.1; NM_008053.2. [Q61584-2]
DR RefSeq; XP_006535463.1; XM_006535400.1. [Q61584-4]
DR RefSeq; XP_006535464.1; XM_006535401.1. [Q61584-6]
DR RefSeq; XP_006535465.1; XM_006535402.1.
DR AlphaFoldDB; Q61584; -.
DR SMR; Q61584; -.
DR BioGRID; 199772; 180.
DR IntAct; Q61584; 156.
DR MINT; Q61584; -.
DR STRING; 10090.ENSMUSP00000001620; -.
DR BindingDB; Q61584; -.
DR iPTMnet; Q61584; -.
DR PhosphoSitePlus; Q61584; -.
DR SwissPalm; Q61584; -.
DR EPD; Q61584; -.
DR jPOST; Q61584; -.
DR MaxQB; Q61584; -.
DR PaxDb; Q61584; -.
DR PeptideAtlas; Q61584; -.
DR PRIDE; Q61584; -.
DR ProteomicsDB; 267540; -. [Q61584-1]
DR ProteomicsDB; 267541; -. [Q61584-2]
DR ProteomicsDB; 267542; -. [Q61584-3]
DR ProteomicsDB; 267543; -. [Q61584-4]
DR ProteomicsDB; 267544; -. [Q61584-5]
DR ProteomicsDB; 267545; -. [Q61584-6]
DR ProteomicsDB; 267546; -. [Q61584-7]
DR Antibodypedia; 18845; 353 antibodies from 39 providers.
DR DNASU; 14359; -.
DR Ensembl; ENSMUST00000001620; ENSMUSP00000001620; ENSMUSG00000027680. [Q61584-1]
DR Ensembl; ENSMUST00000197694; ENSMUSP00000142441; ENSMUSG00000027680. [Q61584-5]
DR Ensembl; ENSMUST00000200392; ENSMUSP00000143392; ENSMUSG00000027680. [Q61584-2]
DR GeneID; 14359; -.
DR KEGG; mmu:14359; -.
DR UCSC; uc008oxk.2; mouse. [Q61584-2]
DR UCSC; uc008oxl.2; mouse. [Q61584-5]
DR UCSC; uc008oxn.2; mouse. [Q61584-1]
DR CTD; 8087; -.
DR MGI; MGI:104860; Fxr1.
DR VEuPathDB; HostDB:ENSMUSG00000027680; -.
DR eggNOG; ENOG502QPKJ; Eukaryota.
DR GeneTree; ENSGT00950000183189; -.
DR InParanoid; Q61584; -.
DR OMA; DQQQRGY; -.
DR OrthoDB; 374073at2759; -.
DR PhylomeDB; Q61584; -.
DR TreeFam; TF105427; -.
DR BioGRID-ORCS; 14359; 0 hits in 73 CRISPR screens.
DR PRO; PR:Q61584; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q61584; protein.
DR Bgee; ENSMUSG00000027680; Expressed in seminiferous tubule of testis and 253 other tissues.
DR ExpressionAtlas; Q61584; baseline and differential.
DR Genevisible; Q61584; MM.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0043034; C:costamere; IDA:MGI.
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; IDA:UniProtKB.
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; IDA:MGI.
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; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
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:0035770; C:ribonucleoprotein granule; IDA: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:0033592; F:RNA strand annealing activity; ISS:UniProtKB.
DR GO; GO:0045182; F:translation regulator activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007517; P:muscle organ development; IMP:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central.
DR GO; GO:2000637; P:positive regulation of miRNA-mediated gene silencing; ISS:UniProtKB.
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 GO; GO:0060538; P:skeletal muscle organ development; IDA:UniProtKB.
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; IPR032177; FXR_C3.
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; PF16097; FXR_C3; 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 Acetylation; Alternative splicing; Cytoplasm; Developmental protein;
KW Differentiation; Isopeptide bond; Methylation; Myogenesis; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P51114"
FT CHAIN 2..677
FT /note="RNA-binding protein FXR1"
FT /id="PRO_0000050107"
FT DOMAIN 4..50
FT /note="Agenet-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00973"
FT DOMAIN 63..115
FT /note="Agenet-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00973"
FT DOMAIN 222..251
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 285..314
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 380..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..486
FT /note="RNA-binding RGG-box"
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"
FT COMPBIAS 596..610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..631
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..665
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P51114"
FT MOD_RES 68
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 398
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5XI81"
FT MOD_RES 430
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P51114"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5XI81"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51114"
FT MOD_RES 476
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 476
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 482
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 482
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 484
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 484
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 512
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51114"
FT MOD_RES 553
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51116"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 667
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P51114"
FT CROSSLNK 56
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P51114"
FT VAR_SEQ 380..408
FT /note="Missing (in isoform A, isoform D and isoform F)"
FT /evidence="ECO:0000303|PubMed:10409431,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8634689"
FT /id="VSP_002836"
FT VAR_SEQ 430..455
FT /note="Missing (in isoform G)"
FT /evidence="ECO:0000303|PubMed:10409431"
FT /id="VSP_002837"
FT VAR_SEQ 564..590
FT /note="Missing (in isoform C and isoform D)"
FT /evidence="ECO:0000303|PubMed:10409431"
FT /id="VSP_002839"
FT VAR_SEQ 564..568
FT /note="DDSEK -> GKRCD (in isoform A and isoform B)"
FT /evidence="ECO:0000303|PubMed:10409431,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8634689"
FT /id="VSP_002838"
FT VAR_SEQ 569..677
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:10409431,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8634689"
FT /id="VSP_002840"
FT CONFLICT 136
FT /note="D -> H (in Ref. 3; AAH19139)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 677 AA; 76222 MW; 908104FC95431A11 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 NGLDDSEKKP QRRNRSRRRR FRGQAEDRQP VTVADYISRA
ESQSRQRNLP RETLAKNKKE MAKDVIEEHG PSEKAINGPT SASGDEIPKL PRTLGEEKTK
TLKEDSTQEA AVLNGVS
