FMR1_PONAB
ID FMR1_PONAB Reviewed; 594 AA.
AC Q5R9B4;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Fragile X messenger ribonucleoprotein 1 {ECO:0000250|UniProtKB:Q06787};
DE AltName: Full=Fragile X messenger ribonucleoprotein {ECO:0000250|UniProtKB:Q06787};
DE Short=FMRP {ECO:0000250|UniProtKB:Q06787};
GN Name=FMR1 {ECO:0000250|UniProtKB:Q06787};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Multifunctional polyribosome-associated RNA-binding protein
CC that plays a central role in neuronal development and synaptic
CC plasticity through the regulation of alternative mRNA splicing, mRNA
CC stability, mRNA dendritic transport and postsynaptic local protein
CC synthesis of a subset of mRNAs. Plays a role in the alternative
CC splicing of its own mRNA. Plays a role in mRNA nuclear export. Together
CC with export factor NXF2, is involved in the regulation of the NXF1 mRNA
CC stability in neurons. Stabilizes the scaffolding postsynaptic density
CC protein DLG4/PSD-95 and the myelin basic protein (MBP) mRNAs in
CC hippocampal neurons and glial cells, respectively; this stabilization
CC is further increased in response to metabotropic glutamate receptor
CC (mGluR) stimulation. Plays a role in selective delivery of a subset of
CC dendritic mRNAs to synaptic sites in response to mGluR activation in a
CC kinesin-dependent manner. Plays a role as a repressor of mRNA
CC translation during the transport of dendritic mRNAs to postsynaptic
CC dendritic spines. Component of the CYFIP1-EIF4E-FMR1 complex which
CC blocks cap-dependent mRNA translation initiation. Represses mRNA
CC translation by stalling ribosomal translocation during elongation.
CC Reports are contradictory with regards to its ability to mediate
CC translation inhibition of MBP mRNA in oligodendrocytes. Also involved
CC in the recruitment of the RNA helicase MOV10 to a subset of mRNAs and
CC hence regulates microRNA (miRNA)-mediated translational repression by
CC AGO2. Facilitates the assembly of miRNAs on specific target mRNAs. Also
CC plays a role as an activator of mRNA translation of a subset of
CC dendritic mRNAs at synapses. In response to mGluR stimulation, FMR1-
CC target mRNAs are rapidly derepressed, allowing for local translation at
CC synapses. Binds to a large subset of dendritic mRNAs that encode a
CC myriad of proteins involved in pre- and postsynaptic functions. Binds
CC to 5'-ACU[GU]-3' and/or 5'-[AU]GGA-3' RNA consensus sequences within
CC mRNA targets, mainly at coding sequence (CDS) and 3'-untranslated
CC region (UTR) and less frequently at 5'-UTR. Binds to intramolecular G-
CC quadruplex structures in the 5'- or 3'-UTRs of mRNA targets. Binds to
CC G-quadruplex structures in the 3'-UTR of its own mRNA. Binds also to
CC RNA ligands harboring a kissing complex (kc) structure; this binding
CC may mediate the association of FMR1 with polyribosomes. Binds mRNAs
CC containing U-rich target sequences. Binds to a triple stem-loop RNA
CC structure, called Sod1 stem loop interacting with FMRP (SoSLIP), in the
CC 5'-UTR region of superoxide dismutase SOD1 mRNA. Binds to the
CC dendritic, small non-coding brain cytoplasmic RNA 1 (BC1); which may
CC increase the association of the CYFIP1-EIF4E-FMR1 complex to FMR1
CC target mRNAs at synapses. Associates with export factor NXF1 mRNA-
CC containing ribonucleoprotein particles (mRNPs) in a NXF2-dependent
CC manner. Binds to a subset of miRNAs in the brain. May associate with
CC nascent transcripts in a nuclear protein NXF1-dependent manner. In
CC vitro, binds to RNA homomer; preferentially on poly(G) and to a lesser
CC extent on poly(U), but not on poly(A) or poly(C). Moreover, plays a
CC role in the modulation of the sodium-activated potassium channel KCNT1
CC gating activity. Negatively regulates the voltage-dependent calcium
CC channel current density in soma and presynaptic terminals of dorsal
CC root ganglion (DRG) neurons, and hence regulates synaptic vesicle
CC exocytosis. Modulates the voltage-dependent calcium channel CACNA1B
CC expression at the plasma membrane by targeting the channels for
CC proteosomal degradation. Plays a role in regulation of MAP1B-dependent
CC microtubule dynamics during neuronal development. Recently, has been
CC shown to play a translation-independent role in the modulation of
CC presynaptic action potential (AP) duration and neurotransmitter release
CC via large-conductance calcium-activated potassium (BK) channels in
CC hippocampal and cortical excitatory neurons. Finally, FMR1 may be
CC involved in the control of DNA damage response (DDR) mechanisms through
CC the regulation of ATR-dependent signaling pathways such as histone
CC H2AX/H2A.x and BRCA1 phosphorylations. {ECO:0000250|UniProtKB:P35922,
CC ECO:0000250|UniProtKB:Q06787, ECO:0000250|UniProtKB:Q80WE1}.
CC -!- SUBUNIT: Homodimer. Forms heterodimer with FXR1; heterodimerization
CC occurs in a methylation-dependent manner. Forms heterodimer with FXR2.
CC Homooligomer. Component of the CYFIP1-EIF4E-FMR1 complex at least
CC composed of CYFIP, EIF4E and FMR1; this mRNA cap binding complex
CC formation increases in presence of the brain cytoplasmic RNA BC1 and is
CC dynamically regulated in an activity-dependent manner to repress and
CC then possibly release dendritic mRNAs for translation in response to
CC mGluR stimulation. Associates with the SMN core complex that contains
CC SMN, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8
CC and STRAP/UNRIP. Part of a ribonucleoprotein complex with AGO2/EIF2C2
CC and miRNAs. Interacts with AGO2/EIF2C2. Interacts (via C-terminus) with
CC CACNA1B; this interaction induces a decrease in the number of
CC presynaptic functional CACNA1B channels at the cell surface. Interacts
CC with CYFIP1; this interaction recruits CYFIP1 to capped mRNA. Interacts
CC with CYFIP2. Interacts with EIF5; this interaction occurs in a RNA-
CC dependent manner. Interacts with dynein. Interacts with FXR1 and FXR2.
CC Interacts with methylated histone H3. Interacts with IGF2BP1; this
CC interaction allows to recruit IGF2BP1 to mRNA in a FMR1-dependent
CC manner. Interacts (via N-terminus) with KCNMB4. Interacts with KCNT1
CC (via C-terminus); this interaction alters gating properties of KCNT1.
CC Interacts (via phosphorylated form) with MCRS1 (via N-terminus).
CC Interacts with MOV10; this interaction is direct, occurs in an RNA-
CC dependent manner on polysomes and induces association of MOV10 with
CC RNAs. Interacts with MYO5A and PURA; these interactions occur in
CC association with polyribosome. Interacts with NCL. Interacts with
CC NUFIP1. Interacts (via N-terminus) with NUFIP2. Interacts with NXF1;
CC this interaction occurs in a mRNA-dependent and polyribosome-
CC independent manner in the nucleus. Interacts with NXF2 (via N-
CC terminus); this interaction is direct and occurs in a NXF1 mRNA-
CC containing mRNP complexes. Interacts with RANBP9 (via C-terminus); this
CC interaction is direct and inhibits binding of FMR1 to RNA homomer.
CC Interacts with RPLP0. Interacts (via C-terminus) with SMN (via C-
CC terminus); this interaction is direct and occurs in a RNA-independent
CC manner. Interacts with TDRD3 (via C-terminus); this interaction is
CC direct. Interacts with YBX1; this interaction occurs in association
CC with polyribosome. Interacts with nucleosome. Associates with
CC polyribosome; this association occurs in a mRNA-dependent manner.
CC Associates with cytoplasmic messenger ribonucleoprotein particles
CC (mRNPs). Associates with microtubules in a kinesin- and dynein-
CC dependent manner. Interacts with HABP4. {ECO:0000250|UniProtKB:P35922,
CC ECO:0000250|UniProtKB:Q06787}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q06787}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:Q06787}. Chromosome, centromere
CC {ECO:0000250|UniProtKB:P35922}. Chromosome
CC {ECO:0000250|UniProtKB:P35922}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q06787}. Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:Q06787}. Cytoplasm, Cytoplasmic
CC ribonucleoprotein granule {ECO:0000250|UniProtKB:Q06787}. Perikaryon
CC {ECO:0000250|UniProtKB:Q06787}. Cell projection, neuron projection
CC {ECO:0000250|UniProtKB:Q06787}. Cell projection, axon
CC {ECO:0000250|UniProtKB:P35922}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:P35922}. Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:P35922}. Synapse, synaptosome
CC {ECO:0000250|UniProtKB:P35922}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:Q06787}. Cell projection, filopodium tip
CC {ECO:0000250|UniProtKB:P35922}. Synapse {ECO:0000250|UniProtKB:P35922}.
CC Postsynaptic cell membrane {ECO:0000250|UniProtKB:P35922}. Presynaptic
CC cell membrane {ECO:0000250|UniProtKB:P35922}. Cell membrane
CC {ECO:0000250|UniProtKB:P35922}. Note=Colocalizes with H2AX/H2A.x in
CC pericentromeric heterochromatin in response to DNA damaging agents.
CC Localizes on meiotic pachytene-stage chromosomes. Forms nuclear foci
CC representing sites of ongoing DNA replication in response to DNA
CC damaging agents. Shuttles between nucleus and cytoplasm in a XPO1/CRM1-
CC dependent manner. Localizes to cytoplasmic granules, also referred to
CC as messenger ribonucleoprotein particles or mRNPs, along dendrites and
CC dendritic spines. FMR1-containing cytoplasmic granules colocalize to F-
CC actin-rich structures, including filopodium, spines and growth cone
CC during the development of hippocampal neurons. FMR1-containing
CC cytoplasmic granules are transported out of the soma along axon and
CC dendrite to synaptic contacts in a microtubule- and kinesin-dependent
CC manner. Colocalizes with CACNA1B in the cytoplasm and at the cell
CC membrane of neurons. Colocalizes with CYFIP1, CYFIP2, NXF2 and
CC ribosomes in the perinuclear region. Colocalizes with CYFIP1 and EIF4E
CC in dendrites and probably at synapses. Colocalizes with FXR1, kinesin,
CC 60S acidic ribosomal protein RPLP0 and SMN in cytoplasmic granules in
CC the soma and neurite cell processes. Colocalizes with FXR1 and FXR2 in
CC discrete granules, called fragile X granules (FXGs), along axon and
CC presynaptic compartments. Colocalizes with TDRD3 in cytoplasmic stress
CC granules (SGs) in response to various cellular stress.
CC {ECO:0000250|UniProtKB:P35922, ECO:0000250|UniProtKB:Q06787,
CC ECO:0000250|UniProtKB:Q80WE1}.
CC -!- DOMAIN: The N-terminal 134 amino acids are necessary for
CC homodimerization and RNA-binding. The N-terminal 298 amino acids are
CC sufficient to interact with KCNMB4 and to regulate presynaptic action
CC potential (AP) duration in neurons. The two agenet-like domains are
CC necessary for binding to histone H3 in a methylation-dependent manner.
CC The KH domains are necessary for mediating miRNA annealing to specific
CC RNA targets. The KH 2 domain is necessary for binding to kissing
CC complex (kc) RNA ligands. The RGG box domain is necessary for binding
CC to mRNA targets that contain G-quadruplex structures. The RGG-box
CC domain is necessary for binding to a triple stem-loop RNA structure,
CC called Sod1 stem loop interacting with FMRP (SoSLIP), in the superoxide
CC dismutase SOD1 mRNA. The RGG box domain is necessary for binding to its
CC own mRNA. The RGG-box domain is necessary for binding to homomer
CC poly(G). {ECO:0000250|UniProtKB:Q06787}.
CC -!- PTM: Phosphorylated. Phosphorylated on several serine residues.
CC Phosphorylation at Ser-479 is required for phosphorylation of other
CC nearby serine residues. Phosphorylation has no effect on the binding of
CC individual mRNA species, but may affect the association with
CC polyribosome. Unphosphorylated FMR1 is associated with actively
CC translating polyribosome, whereas a fraction of phosphorylated FMR1 is
CC associated with apparently stalled polyribosome. Dephosphorylation by
CC an activated phosphatase may release the FMR1-mediated translational
CC repression and allow synthesis of a locally required protein at
CC snypases. {ECO:0000250|UniProtKB:P35922, ECO:0000250|UniProtKB:Q06787}.
CC -!- PTM: Monoubiquitinated. Polyubiquitinated. Ubiquitinated and targeted
CC for proteasomal degradation after activation of metabotropic glutamate
CC receptor (mGluR). {ECO:0000250|UniProtKB:P35922}.
CC -!- PTM: Monomethylated and asymmetrically dimethylated at four arginine
CC residues of the arginine-glycine-glycine box. Methylation disrupts the
CC binding of FMRP to RNAs through its RGG box. Methylation is necessary
CC for heterodimerization with FXR1, association with polyribosomes,
CC recruitment into stress granules and translation of FMR1 target mRNAs.
CC Methylated by PRMT1, PRMT3 and PRMT4, in vitro.
CC {ECO:0000250|UniProtKB:P35922, ECO:0000250|UniProtKB:Q06787}.
CC -!- SIMILARITY: Belongs to the FMR1 family. {ECO:0000305}.
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DR EMBL; CR859475; CAH91646.1; -; mRNA.
DR RefSeq; NP_001125966.1; NM_001132494.1.
DR AlphaFoldDB; Q5R9B4; -.
DR SMR; Q5R9B4; -.
DR STRING; 9601.ENSPPYP00000023279; -.
DR GeneID; 100172902; -.
DR KEGG; pon:100172902; -.
DR CTD; 2332; -.
DR eggNOG; ENOG502QPKJ; Eukaryota.
DR InParanoid; Q5R9B4; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
DR GO; GO:0042995; C:cell projection; ISS:UniProtKB.
DR GO; GO:0010369; C:chromocenter; ISS:UniProtKB.
DR GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISS:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:1902737; C:dendritic filopodium; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0032433; C:filopodium tip; ISS:UniProtKB.
DR GO; GO:0097386; C:glial cell projection; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:1990812; C:growth cone filopodium; ISS:UniProtKB.
DR GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0071598; C:neuronal ribonucleoprotein granule; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005844; C:polysome; ISS:UniProtKB.
DR GO; GO:0098794; C:postsynapse; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; ISS:UniProtKB.
DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0070840; F:dynein complex binding; ISS:UniProtKB.
DR GO; GO:0002151; F:G-quadruplex RNA binding; ISS:UniProtKB.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0034046; F:poly(G) binding; ISS:UniProtKB.
DR GO; GO:0008266; F:poly(U) RNA binding; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0035613; F:RNA stem-loop binding; ISS:UniProtKB.
DR GO; GO:0033592; F:RNA strand annealing activity; ISS:UniProtKB.
DR GO; GO:1990825; F:sequence-specific mRNA binding; ISS:UniProtKB.
DR GO; GO:0035197; F:siRNA binding; ISS:UniProtKB.
DR GO; GO:0030371; F:translation repressor activity; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0007215; P:glutamate receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; ISS:UniProtKB.
DR GO; GO:2000766; P:negative regulation of cytoplasmic translation; ISS:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; ISS:UniProtKB.
DR GO; GO:1900453; P:negative regulation of long-term synaptic depression; ISS:UniProtKB.
DR GO; GO:2000301; P:negative regulation of synaptic vesicle exocytosis; ISS:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR GO; GO:0045947; P:negative regulation of translational initiation; ISS:UniProtKB.
DR GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; ISS:UniProtKB.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; ISS:UniProtKB.
DR GO; GO:2000637; P:positive regulation of miRNA-mediated gene silencing; ISS:UniProtKB.
DR GO; GO:1902416; P:positive regulation of mRNA binding; ISS:UniProtKB.
DR GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; ISS:UniProtKB.
DR GO; GO:0002092; P:positive regulation of receptor internalization; ISS:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0060998; P:regulation of dendritic spine development; ISS:UniProtKB.
DR GO; GO:0051489; P:regulation of filopodium assembly; ISS:UniProtKB.
DR GO; GO:0060964; P:regulation of miRNA-mediated gene silencing; ISS:UniProtKB.
DR GO; GO:0043488; P:regulation of mRNA stability; ISS:UniProtKB.
DR GO; GO:0098908; P:regulation of neuronal action potential; ISS:UniProtKB.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0060538; P:skeletal muscle organ development; ISS:UniProtKB.
DR Gene3D; 3.30.1370.10; -; 3.
DR InterPro; IPR008395; Agenet-like_dom.
DR InterPro; IPR040148; FMR1.
DR InterPro; IPR040472; FMRP_KH0.
DR InterPro; IPR032196; FXMR_C2.
DR InterPro; IPR022034; FXMRP1_C_core.
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; PF16098; FXMR_C2; 1.
DR Pfam; PF12235; FXMRP1_C_core; 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 2: Evidence at transcript level;
KW Acetylation; Activator; Cell membrane; Cell projection; Centromere;
KW Chromosome; Cytoplasm; DNA damage; Membrane; Methylation; mRNA processing;
KW mRNA splicing; mRNA transport; Neurogenesis; Nucleus; Phosphoprotein;
KW Postsynaptic cell membrane; Reference proteome; Repeat; Repressor;
KW Ribonucleoprotein; RNA-binding; RNA-mediated gene silencing; Synapse;
KW Synaptosome; Translation regulation; Transport; Ubl conjugation.
FT CHAIN 1..594
FT /note="Fragile X messenger ribonucleoprotein 1"
FT /id="PRO_0000342184"
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 218..279
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 281..348
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 1..184
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT REGION 172..211
FT /note="Necessary for interaction with CYFIP1, CYFIP2, FXR1
FT and FXR2"
FT /evidence="ECO:0000250|UniProtKB:P35922,
FT ECO:0000250|UniProtKB:Q06787"
FT REGION 325..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..470
FT /note="Required for nuclear export"
FT /evidence="ECO:0000250|UniProtKB:Q06787"
FT REGION 398..594
FT /note="Interaction with RANBP9"
FT /evidence="ECO:0000250|UniProtKB:Q06787"
FT REGION 422..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..527
FT /note="RNA-binding RGG-box"
FT /evidence="ECO:0000250"
FT MOTIF 403..422
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOTIF 506..513
FT /note="Nucleolar localization signal 1"
FT /evidence="ECO:0000250|UniProtKB:Q06787"
FT MOTIF 575..579
FT /note="Nucleolar localization signal 2"
FT /evidence="ECO:0000250|UniProtKB:Q06787"
FT COMPBIAS 479..516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q06787"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80WE1"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06787"
FT MOD_RES 442
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 450
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 479
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06787"
FT MOD_RES 513
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 513
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 518
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 518
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 523
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 523
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 525
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 525
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P35922"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35922"
SQ SEQUENCE 594 AA; 67057 MW; C465B5790C6BEB0D CRC64;
MEELVVEVRG SNGAFYKAFV KDVHEDSITV AFENNWQPDR QIPFHDVRFP PPVGYNKDIN
ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD ATYNEIVTIE RLRSVNPNKP
ATKDTFHKIK LDVPEDLRQM CAKESAHKDF KKAVGAFSVT YDPENYQLVI LSINEVTSKR
AHMLIDMHFR SLRTKLSLIM RNEEASKQLE SSRQLASRFH EQFIVREDLM GLAIGTHGAN
IQQARKVPGV TAIDLDEDTC TFHIYGEDQD AVKKARSFLE FAEDVIQVPR NLVGKVIGKN
GKLIQEIVDK SGVVRVRIEA ENEKNVPQEE EIMPPNSLPS NNSRVGPNAP EEKKHLEIKE
NSTHFSQPNS TKVQRGMVPF VFVGTKDSIA NATVLLDYHL NYLKEVDQLR LERLQIDEQL
RQIGASSRPP PNRTDKEKSY VTDDGQGMGR GSRPYRNRGH GRRGPGYTSG TNSEASNASE
TESDHRDELS DWSLAPTEEE RESFLRRGDG RRRGGGGRGQ GGRGRGGGFE GNDDHSRTDN
RPRNPREAKG RTTDGSLQNT SSEGNRLRTG KDRNRKKEKP DSVDGQQPLV NGVP
