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Protein

Synaptic functional regulator FMR1

Gene

Fmr1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Multifunctional polyribosome-associated RNA-binding protein that plays a central role in neuronal development and synaptic plasticity through the regulation of alternative mRNA splicing, mRNA stability, mRNA dendritic transport and postsynaptic local protein synthesis of a subset of mRNAs (PubMed:11438589, PubMed:12032354, PubMed:15475576, PubMed:16631377, PubMed:16790844, PubMed:17417632, PubMed:17548835, PubMed:18539120, PubMed:18653529, PubMed:19640847, PubMed:19166269, PubMed:20159450, PubMed:21784246, PubMed:23235829, PubMed:24813610). Plays a role in the alternative splicing of its own mRNA (PubMed:18653529). Plays a role in mRNA nuclear export (PubMed:16790844). Together with export factor NXF2, is involved in the regulation of the NXF1 mRNA stability in neurons (PubMed:17548835). Stabilizes the scaffolding postsynaptic density protein DLG4/PSD-95 and the myelin basic protein MBP mRNAs in hippocampal neurons and glial cells, respectively; this stabilization is further increased in response to metabotropic glutamate receptor (mGluR) stimulation (PubMed:17417632). Plays a role in selective delivery of a subset of dendritic mRNAs to synaptic sites in response to mGluR activation in a kinesin-dependent manner (PubMed:18539120). Plays a role as a repressor of mRNA translation during the transport of dendritic mRNAs to postnyaptic dendritic spines (PubMed:11376146, PubMed:12581522, PubMed:14570712, PubMed:12927206, PubMed:15475576, PubMed:16908410, PubMed:18805096, PubMed:19640847, PubMed:21784246, PubMed:23235829). Component of the CYFIP1-EIF4E-FMR1 complex which blocks cap-dependent mRNA translation initiation (PubMed:18805096). Represses mRNA translation by stalling ribosomal translocation during elongation (PubMed:21784246). Reports are contradictory with regards to its ability to mediate translation inhibition of (MBP) mRNA in oligodendrocytes (PubMed:14613971, PubMed:23891804). Also involved in the recruitment of the RNA helicase MOV10 to a subset of mRNAs and hence regulates microRNA (miRNA)-mediated translational repression by AGO2 (PubMed:20159450, PubMed:25464849). Facilitates the assembly of miRNAs on specific target mRNAs (By similarity). Plays also a role as an activator of mRNA translation of a subset of dendritic mRNAs at synapses (PubMed:14614133, PubMed:14613971, PubMed:15548614, PubMed:19640847, PubMed:19166269, PubMed:21490210). In response to mGluR stimulation, FMR1-target mRNAs are rapidly derepressed, allowing for local translation at synapses (PubMed:16908410, PubMed:17507556, PubMed:19640847). Binds to a large subset of dendritic mRNAs that encode a myriad of proteins involved in pre- and postsynaptic functions (PubMed:11719188, PubMed:11376146, PubMed:14613971, PubMed:17507556, PubMed:21784246, PubMed:21490210, PubMed:24349419). Binds to 5'-ACU[GU]-3' and/or 5'-[AU]GGA-3' RNA consensus sequences within mRNA targets, mainly at coding sequence (CDS) and 3'-untranslated region (UTR) and less frequently at 5'-UTR (By similarity). Binds to intramolecular G-quadruplex structures in the 5'- or 3'-UTRs of mRNA targets (PubMed:25692235). Binds to G-quadruplex structures in the 3'-UTR of its own mRNA (By similarity). Binds also to RNA ligands harboring a kissing complex (kc) structure; this binding may mediate the association of FMR1 with polyribosomes (By similarity). Binds mRNAs containing U-rich target sequences (By similarity). Binds to a triple stem-loop RNA structure, called Sod1 stem loop interacting with FMRP (SoSLIP), in the 5'-UTR region of superoxide dismutase SOD1 mRNA (PubMed:19166269). Binds to the dendritic, small non-coding brain cytoplasmic RNA 1 (BC1); which may increase the association of the CYFIP1-EIF4E-FMR1 complex to FMR1 target mRNAs at synapses (PubMed:12581522, PubMed:18805096). Associates with export factor NXF1 mRNA-containing ribonucleoprotein particles (mRNPs) in a NXF2-dependent manner (PubMed:17548835). Binds to a subset of miRNAs in the brain (PubMed:20159450). May associate with nascent transcripts in a nuclear protein NXF1-dependent manner (By similarity). In vitro, binds to RNA homopolymer; preferentially on poly(G) and to a lesser extent on poly(U), but not on poly(A) or poly(C) (By similarity). Moreover, plays a role in the modulation of the sodium-activated potassium channel KCNT1 gating activity (PubMed:20512134). Negatively regulates the voltage-dependent calcium channel current density in soma and presynaptic terminals of dorsal root ganglion (DRG) neurons, and hence regulates synaptic vesicle exocytosis (By similarity). Modulates the voltage-dependent calcium channel CACNA1B expression at the plasma membrane by targeting the channels for proteosomal degradation (PubMed:24709664). Plays a role in regulation of MAP1B-dependent microtubule dynamics during neuronal development (PubMed:15475576). Recently, has been shown to play a translation-independent role in the modulation of presynaptic action potential (AP) duration and neurotransmitter release via large-conductance calcium-activated potassium (BK) channels in hippocampal and cortical excitatory neurons (PubMed:25561520). Finally, FMR1 may be involved in the control of DNA damage response (DDR) mechanisms through the regulation of ATR-dependent signaling pathways such as histone H2AFX/H2A.x and BRCA1 phosphorylations (PubMed:24813610).By similarity33 Publications

GO - Molecular functioni

  • chromatin binding Source: UniProtKB
  • dynein binding Source: UniProtKB
  • G-quadruplex RNA binding Source: UniProtKB
  • identical protein binding Source: MGI
  • methylated histone binding Source: UniProtKB
  • microtubule binding Source: UniProtKB
  • miRNA binding Source: UniProtKB
  • mRNA 3'-UTR binding Source: UniProtKB
  • mRNA 5'-UTR binding Source: UniProtKB
  • mRNA binding Source: UniProtKB
  • poly(A) RNA binding Source: MGI
  • poly(G) binding Source: UniProtKB
  • poly(U) RNA binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • ribosome binding Source: MGI
  • RNA binding Source: MGI
  • RNA stem-loop binding Source: UniProtKB
  • RNA strand annealing activity Source: UniProtKB
  • sequence-specific mRNA binding Source: UniProtKB
  • siRNA binding Source: UniProtKB
  • translation initiation factor binding Source: MGI
  • translation repressor activity Source: UniProtKB

GO - Biological processi

  • cellular response to DNA damage stimulus Source: UniProtKB
  • cellular response to hydroxyurea Source: UniProtKB
  • cellular response to UV Source: UniProtKB
  • central nervous system development Source: MGI
  • dendritic spine development Source: MGI
  • glutamate receptor signaling pathway Source: UniProtKB
  • mRNA transport Source: UniProtKB
  • negative regulation of cytoplasmic translation Source: UniProtKB
  • negative regulation of gene expression Source: UniProtKB
  • negative regulation of long term synaptic depression Source: UniProtKB
  • negative regulation of synaptic vesicle exocytosis Source: UniProtKB
  • negative regulation of translation Source: UniProtKB
  • negative regulation of translational initiation Source: UniProtKB
  • negative regulation of voltage-gated calcium channel activity Source: UniProtKB
  • positive regulation of dendritic spine development Source: UniProtKB
  • positive regulation of filopodium assembly Source: UniProtKB
  • positive regulation of gene silencing by miRNA Source: UniProtKB
  • positive regulation of histone phosphorylation Source: UniProtKB
  • positive regulation of mRNA binding Source: UniProtKB
  • positive regulation of proteasomal protein catabolic process Source: UniProtKB
  • positive regulation of receptor internalization Source: UniProtKB
  • positive regulation of response to DNA damage stimulus Source: UniProtKB
  • positive regulation of translation Source: UniProtKB
  • regulation of alternative mRNA splicing, via spliceosome Source: UniProtKB
  • regulation of dendritic spine development Source: UniProtKB
  • regulation of filopodium assembly Source: UniProtKB
  • regulation of mRNA stability Source: UniProtKB
  • regulation of neuronal action potential Source: UniProtKB
  • regulation of neurotransmitter secretion Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor, Ribonucleoprotein

Keywords - Biological processi

DNA damage, mRNA processing, mRNA splicing, mRNA transport, Neurogenesis, RNA-mediated gene silencing, Translation regulation, Transport

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Synaptic functional regulator FMR1Curated
Alternative name(s):
Fragile X mental retardation protein 1 homologBy similarity
Short name:
FMRP1 Publication
Short name:
Protein FMR-11 Publication
Short name:
mFmr1p
Gene namesi
Name:Fmr1Imported
Synonyms:Fmr-11 Publication
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:95564. Fmr1.

Subcellular locationi

Isoform 4 :
  • Nucleus 1 Publication
  • Nucleusnucleoplasm 1 Publication

GO - Cellular componenti

  • axon Source: UniProtKB
  • axon terminus Source: UniProtKB
  • Cajal body Source: MGI
  • cell body Source: MGI
  • cell projection Source: MGI
  • chromocenter Source: UniProtKB
  • chromosome Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytoplasmic ribonucleoprotein granule Source: UniProtKB
  • cytoplasmic stress granule Source: MGI
  • dendrite Source: UniProtKB
  • dendritic filopodium Source: UniProtKB
  • dendritic spine Source: UniProtKB
  • extrinsic component of plasma membrane Source: UniProtKB
  • filopodium tip Source: UniProtKB
  • glial cell projection Source: UniProtKB
  • growth cone Source: UniProtKB
  • growth cone filopodium Source: UniProtKB
  • intracellular ribonucleoprotein complex Source: MGI
  • membrane Source: MGI
  • mRNA cap binding complex Source: UniProtKB
  • neuronal ribonucleoprotein granule Source: UniProtKB
  • neuron projection Source: MGI
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: MGI
  • perikaryon Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • polysome Source: UniProtKB
  • postsynapse Source: UniProtKB
  • postsynaptic density Source: UniProtKB
  • presynapse Source: UniProtKB
  • ribonucleoprotein complex Source: MGI
  • synapse Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Centromere, Chromosome, Cytoplasm, Membrane, Nucleus, Postsynaptic cell membrane, Synapse, Synaptosome

Pathology & Biotechi

Disruption phenotypei

Show normal fertility (PubMed:8033209). Display enlarged testes and ovaries (PubMed:8033209, PubMed:23235829). Display learning deficits and hyperactivity, in the absence of gross pathological abnormalities of the brain (PubMed:8033209). Display immature neurons with excess of long, thin growth cone filopodia and dendritic filopodia and spine protrusions with less synaptic contacts (PubMed:9144249, PubMed:11438589, PubMed:16631377, PubMed:17417632, PubMed:18539120). Show no increase in the number of dendritic filopodia-spine protrusions in response to KCL-mediated depolarization (PubMed:16631377). Display alterations in the appearance, distribution and volume of nuclear speckles (PubMed:24349419). Display enhanced metabotropic glutamate receptor-dependent long-term depression (mGluR-LTD) in the hippocampus (PubMed:11438589, PubMed:16908410, PubMed:12032354). Leads to excessive presynaptic action potential (AP) broadening in hippocampal and cortical neurons (PubMed:25561520). Show alteration in the splicing pattern of its own FMR1 mRNA in the cortex (PubMed:18653529). Alters the abundance and subcellular distribution of a subset of mRNAs in the brain (PubMed:12575950, PubMed:17417632). Display a reduction in the recruitment of certain FMR1 target mRNAs in actively translating polyribosomes at synapses (PubMed:12575950, PubMed:17507556). Display decreased delivery of specific mRNAs into dendrites in mGluR-stimulated neurons (PubMed:18539120). Display a delayed MAPB1 protein expression decline in the developing hippocampus (PubMed:15475576). Show a relief of ribosome stalling on dendritic FMR1 target mRNAs (PubMed:21784246). Display enhanced postsynaptic protein synthesis of a subset of FMR1 target mRNAs (PubMed:12581522, PubMed:16908410, PubMed:19640847, PubMed:21784246). Unable to induce postsynaptic protein synthesis of a subset of FMR1 mRNA targets in response to mGluR activation (PubMed:16908410, PubMed:17507556). Display enhanced presynaptic protein synthesis of the voltage-dependent calcium channel CACNA1B (PubMed:24709664). Display also enhanced protein synthesis of a subset of FMR1 target mRNAs in ovaries (PubMed:23235829). Display reduced postsynaptic protein synthesis of a subset of FMR1 target mRNAs (PubMed:12927206, PubMed:14614133, PubMed:19640847, PubMed:19166269, PubMed:21490210). Display reduced general protein synthesis in synapses in response to mGluR activation (PubMed:15548614). Show brain-region specific reduction in the expression and/or localization of FAM206A/Simiate (PubMed:24349419). Display similar myelin basic protein (MBP) nexpression level in brain cerebrum than in wild-type mice (PubMed:23891804). Display an absence of nuclear foci on meiotic pachytene-stage chromosomes (PubMed:24813610). Show incomplete resolution of single-strand repair intermediates, crossing over and pairing of homologous chromosomes during meiotic prophase in a subset of spermatocytes (PubMed:24813610).26 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi429 – 4346LRLERL → ARAERA: Inhibits nuclear export. 1 Publication
Mutagenesisi429 – 4313LRL → ARA: Inhibits nuclear export. 1 Publication
Mutagenesisi499 – 4991S → A: Loss of phosphorylation. 1 Publication
Mutagenesisi499 – 4991S → D: Leads to phosphorylation on other serine residues. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 614614Synaptic functional regulator FMR1PRO_0000050103Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei336 – 3361PhosphoserineBy similarity
Modified residuei337 – 3371PhosphoserineBy similarity
Modified residuei349 – 3491PhosphoserineBy similarity
Modified residuei350 – 3501PhosphoserineBy similarity
Modified residuei369 – 3691PhosphoserineBy similarity
Modified residuei462 – 4621PhosphothreonineCombined sources
Modified residuei499 – 4991Phosphoserine1 Publication
Modified residuei543 – 5431Omega-N-methylarginine; alternateBy similarity
Modified residuei543 – 5431Omega-N-methylated arginine; alternateBy similarity
Modified residuei602 – 6021PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated on several serine residues (PubMed:14570712). Phosphorylation at Ser-499 is required for phosphorylation of other nearby serine residues (PubMed:14570712). Phosphorylation has no effect on the binding of individual mRNA species, but may affect the association with polyribosome (PubMed:14570712). Unphosphorylated FMR1 is associated with actively translating polyribosome, whereas a fraction of phosphorylated FMR1 is associated with apparently stalled polyribosome (PubMed:14570712). Dephosphorylation by an activated phosphatase may release the FMR1-mediated translational repression and allow synthesis of a locally required protein at snypases (PubMed:14570712).1 Publication
Monoubiquitinated (PubMed:16908410). Polyubiquitinated (PubMed:16908410). Ubiquitinated and targeted for proteasomal degradation after activation of metabotropic glutamate receptor (mGluR) (PubMed:16908410).1 Publication
Methylated; methylation is necessary for heterodimerization with FXR1, association with polyribosomes, recruitment into stress granules and translation of FMR1 target mRNAs. Methylated by PRMT1, PRMT3 and PRMT4, in vitro.By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP35922.
MaxQBiP35922.
PaxDbiP35922.
PeptideAtlasiP35922.
PRIDEiP35922.

PTM databases

iPTMnetiP35922.
PhosphoSiteiP35922.

Expressioni

Tissue specificityi

Expressed in brain (PubMed:8033209). Strongly expressed in the neonatal hippocampus (PubMed:15475576). Expressed in the brainstem (PubMed:14613971). Expressed in the cerebellum (PubMed:19193898). Expressed in neurons of hippocampal area CA3 (PubMed:17548835, PubMed:19193898). Expressed in neurons of the olfactory bulb including the granule, mitral, tufted and juxtaglomerular cells (PubMed:19193898). Expressed in both mature and immature olfactory sensory neurons (OSNs) (PubMed:19193898). Expressed in neurons in all layers and in all regions of cerebral cortex (PubMed:19193898). Expressed in mature oligodendrocytes (OLGs) (PubMed:23891804). Expressed in spermatogonia (at protein level) (PubMed:16790844). Expressed predominantly in the brain (PubMed:16000371). Expressed in testis (PubMed:8033209).8 Publications

Inductioni

Rapidly and transiently up-regulated in response to metabotropic glutamate receptor activation in a protein synthesis-dependent manner in neurons (at protein level).2 Publications

Gene expression databases

CleanExiMM_FMR1.

Interactioni

Subunit structurei

Homodimer (By similarity). Forms heterodimer with FXR1; heterodimerization occurs in a methylation-dependent manner (By similarity). Forms heterodimer with FXR2 (By similarity). Homooligomer (By similarity). Component of the CYFIP1-EIF4E-FMR1 complex at least composed of CYFIP, EIF4E and FMR1; this mRNA cap binding complex formation increases in presence of the brain cytoplasmic RNA BC1 and is dynamically regulated in an activity-dependent manner to repress and then possibly release dendritic mRNAs for translation in response to mGluR stimulation (PubMed:18805096). Associates with the SMN core complex that contains SMN, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP (PubMed:18093976). Part of a ribonucleoprotein complex with AGO2/EIF2C2 and miRNAs (By similarity). Interacts with AGO2/EIF2C2 (By similarity). Interacts (via C-terminus) with CACNA1B; this interaction induces a deacrease in the number of presynaptic functional CACNA1B channels at the cell surface (PubMed:24709664). Interacts with CYFIP1; this interaction recruits CYFIP1 to capped mRNA (PubMed:11438699, PubMed:18805096). Interacts with CYFIP2 (PubMed:11438699). Interacts with EIF5; this interaction occurs in a RNA-dependent manner (By similarity). Interacts with dynein (PubMed:18539120). Interacts with FXR1 and FXR2 (PubMed:10567518). Interacts with methylated histone H3 (By similarity). Interacts with IGF2BP1; this interaction allows to recruit IGF2BP1 to mRNA in a FMR1-dependent manner (By similarity). Interacts (via N-terminus) with KCNMB4 (PubMed:25561520). Interacts with KCNT1 (via C-terminus); this interaction alters gating properties of KCNT1 (PubMed:20512134). Interacts (via C-terminus) with KIF5A; this interaction is increased in a mGluR-dependent manner (PubMed:18539120). Interacts (via phosphorylated form) with MCRS1 (via N-terminus) (By similarity). Interacts with MOV10; this interaction is direct, occurs in an RNA-dependent manner on polysomes and induces association of MOV10 with RNAs (PubMed:25464849). Interacts with MYO5A and PURA; these interactions occur in association with polyribosome (PubMed:12147688). Interacts with NCL (PubMed:10567518). Interacts with NUFIP1 (PubMed:10556305). Interacts (via N-terminus) with NUFIP2 (By similarity). Interacts with NXF1; this interaction occurs in a mRNA-dependent and polyribosome-independent manner in the nucleus (By similarity). Interacts with NXF2 (via N-terminus); this interaction is direct and occurs in a NXF1 mRNA-containing mRNP complexes (PubMed:16790844, PubMed:17548835). Interacts with RANBP9; this interaction is direct and inhibits binding of FMR1 to RNA homopolymer (PubMed:15381419). Interacts with RPLP0 (PubMed:21784246). Interacts (via C-terminus) with SMN (via C-terminus); this interaction is direct and occurs in a RNA-independent manner (By similarity). Interacts with TDRD3 (via C-terminus); this interaction is direct (By similarity). Interacts with YBX1; this interaction occurs in association with polyribosome (PubMed:11162447). Interacts with nucleosome (By similarity). Associates with polyribosome; this association occurs in a mRNA-dependent manner (PubMed:8842725, PubMed:9285783, PubMed:12581522, PubMed:12575950, PubMed:14613971, PubMed:15317853, PubMed:15805463, PubMed:21784246). Associates with messenger ribonucleoprotein particles (mRNPs) (PubMed:8842725, PubMed:9285783, PubMed:11719188, PubMed:12581522, PubMed:12575950, PubMed:15329415, PubMed:18805096). Associates with microtubules in a kinesin- and dynein-dependent manner (PubMed:18539120).By similarity25 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Rcan1Q9JHG63EBI-645094,EBI-644061

GO - Molecular functioni

Protein-protein interaction databases

IntActiP35922. 7 interactions.
MINTiMINT-111096.
STRINGi10090.ENSMUSP00000085906.

Structurei

3D structure databases

ProteinModelPortaliP35922.
SMRiP35922. Positions 1-200, 216-334, 395-424.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 5047Agenet-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini63 – 11553Agenet-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini222 – 25130KH 1PROSITE-ProRule annotationAdd
BLAST
Domaini285 – 31430KH 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 184184Required for nuclear localization1 PublicationAdd
BLAST
Regioni172 – 21140Necessary for interaction with CYFIP1, CYFIP2, FXR1 and FXR2By similarity1 PublicationAdd
BLAST
Regioni396 – 49095Required for nuclear exportBy similarityAdd
BLAST
Regioni418 – 614197Interaction with RANBP9By similarityAdd
BLAST
Regioni534 – 54714RNA-binding RGG-boxAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi423 – 44220Nuclear export signal1 PublicationAdd
BLAST
Motifi526 – 5338Nucleolar localization signal 1By similarity
Motifi595 – 5995Nucleolar localization signal 2By similarity

Domaini

The N-terminal 134 amino acids are necessary for homodimerization and RNA-binding. The N-terminal 298 amino acids are sufficient to interact with KCNMB4 and to regulate presynaptic action potential (AP) duration in neurons. The two agenet-like domains are necessary for binding to histone H3 in a methylation-dependent manner. The KH domains are necessary for mediating miRNA annealing to specific RNA targets. The KH 2 domain is necessary for binding to kissing complex (kc) RNA ligands. The RGG box domain is necessary for binding to mRNA targets that contain G-quadruplex structures. The RGG-box domain is necessary for binding to a triple stem-loop RNA structure, called Sod1 stem loop interacting with FMRP (SoSLIP), in the superoxide dismutase SOD1 mRNA. The RGG box domain is necessary for binding to its own mRNA. The RGG-box domain is necessary for binding to homopolymer poly(G).By similarity

Sequence similaritiesi

Belongs to the FMR1 family.Curated
Contains 2 Agenet-like domains.PROSITE-ProRule annotation
Contains 2 KH domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IF9J. Eukaryota.
ENOG410ZDJG. LUCA.
HOGENOMiHOG000293377.
HOVERGENiHBG005739.
InParanoidiP35922.
PhylomeDBiP35922.

Family and domain databases

Gene3Di3.30.1370.10. 3 hits.
InterProiIPR008395. Agenet-like_dom.
IPR032196. FXMR_C2.
IPR022034. FXMRP1_C_core.
IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
[Graphical view]
PfamiPF05641. Agenet. 1 hit.
PF16098. FXMR_C2. 2 hits.
PF12235. FXMRP1_C_core. 1 hit.
PF00013. KH_1. 2 hits.
[Graphical view]
SMARTiSM00322. KH. 2 hits.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 2 hits.
PROSITEiPS51641. AGENET_LIKE. 2 hits.
PS50084. KH_TYPE_1. 2 hits.
[Graphical view]

Sequences (12)i

Sequence statusi: Complete.

This entry describes 12 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P35922-1) [UniParc]FASTAAdd to basket

Also known as: ISO1

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEELVVEVRG SNGAFYKAFV KDVHEDSITV AFENNWQPER QIPFHDVRFP
60 70 80 90 100
PPVGYNKDIN ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD
110 120 130 140 150
ATYNEIVTIE RLRSVNPNKP ATKDTFHKIK LEVPEDLRQM CAKESAHKDF
160 170 180 190 200
KKAVGAFSVT YDPENYQLVI LSINEVTSKR AHMLIDMHFR SLRTKLSLIL
210 220 230 240 250
RNEEASKQLE SSRQLASRFH EQFIVREDLM GLAIGTHGAN IQQARKVPGV
260 270 280 290 300
TAIDLDEDTC TFHIYGEDQD AVKKARSFLE FAEDVIQVPR NLVGKVIGKN
310 320 330 340 350
GKLIQEIVDK SGVVRVRIEA ENEKSVPQEE EIMPPSSLPS NNSRVGPNSS
360 370 380 390 400
EEKKHLDTKE NTHFSQPNST KVQRVLVVSS IVAGGPQKPE PKAWQGMVPF
410 420 430 440 450
VFVGTKDSIA NATVLLDYHL NYLKEVDQLR LERLQIDEQL RQIGASSRPP
460 470 480 490 500
PNRTDKEKGY VTDDGQGMGR GSRPYRNRGH GRRGPGYTSG TNSEASNASE
510 520 530 540 550
TESDHRDELS DWSLAPTEEE RESFLRRGDG RRRRGGGRGQ GGRGRGGGFK
560 570 580 590 600
GNDDHSRTDN RPRNPREAKG RTADGSLQSA SSEGSRLRTG KDRNQKKEKP
610
DSVDGLQPLV NGVP
Length:614
Mass (Da):68,989
Last modified:June 1, 1994 - v1
Checksum:i093DD90D589ED066
GO
Isoform 2 (identifier: P35922-2) [UniParc]FASTAAdd to basket

Also known as: ISO2

The sequence of this isoform differs from the canonical sequence as follows:
     490-501: Missing.

Show »
Length:602
Mass (Da):67,840
Checksum:i731A506F0359F0E5
GO
Isoform 3 (identifier: P35922-3) [UniParc]FASTAAdd to basket

Also known as: ISO3

The sequence of this isoform differs from the canonical sequence as follows:
     490-514: Missing.

Show »
Length:589
Mass (Da):66,269
Checksum:i9462AD5A666E906A
GO
Isoform 4 (identifier: P35922-4) [UniParc]FASTAAdd to basket

Also known as: ISO4

The sequence of this isoform differs from the canonical sequence as follows:
     425-448: EVDQLRLERLQIDEQLRQIGASSR → ELILKHQMLLKQNLTTETNSVIGH
     449-614: Missing.

Show »
Length:448
Mass (Da):50,829
Checksum:i0F25006E964AD90C
GO
Isoform 5 (identifier: P35922-5) [UniParc]FASTAAdd to basket

Also known as: ISO5

The sequence of this isoform differs from the canonical sequence as follows:
     425-436: EVDQLRLERLQI → NLTTETNSVIGH
     437-614: Missing.

Show »
Length:436
Mass (Da):49,353
Checksum:i5AB0A796CC0CF180
GO
Isoform 6 (identifier: P35922-6) [UniParc]FASTAAdd to basket

Also known as: ISO6

The sequence of this isoform differs from the canonical sequence as follows:
     425-512: EVDQLRLERL...SDHRDELSDW → LQQRKRGRAS...VTRRRKSQTA
     513-614: Missing.

Show »
Length:512
Mass (Da):58,113
Checksum:i093A5C6493C61131
GO
Isoform 7 (identifier: P35922-7) [UniParc]FASTAAdd to basket

Also known as: ISO7

The sequence of this isoform differs from the canonical sequence as follows:
     375-395: Missing.

Show »
Length:593
Mass (Da):66,817
Checksum:iA5775ADA3613D93D
GO
Isoform 8 (identifier: P35922-8) [UniParc]FASTAAdd to basket

Also known as: ISO8

The sequence of this isoform differs from the canonical sequence as follows:
     375-395: Missing.
     490-501: Missing.

Show »
Length:581
Mass (Da):65,667
Checksum:i64ED438071325D40
GO
Isoform 9 (identifier: P35922-9) [UniParc]FASTAAdd to basket

Also known as: ISO9

The sequence of this isoform differs from the canonical sequence as follows:
     375-395: Missing.
     490-514: Missing.

Show »
Length:568
Mass (Da):64,097
Checksum:i94B1FEC72A1C7D1D
GO
Isoform 10 (identifier: P35922-10) [UniParc]FASTAAdd to basket

Also known as: ISO10

The sequence of this isoform differs from the canonical sequence as follows:
     375-395: Missing.
     425-448: EVDQLRLERLQIDEQLRQIGASSR → ELILKHQMLLKQNLTTETNSVIGH
     449-614: Missing.

Show »
Length:427
Mass (Da):48,656
Checksum:i8F1236A4CBBAE6FA
GO
Isoform 11 (identifier: P35922-11) [UniParc]FASTAAdd to basket

Also known as: ISO11

The sequence of this isoform differs from the canonical sequence as follows:
     375-395: Missing.
     425-436: EVDQLRLERLQI → NLTTETNSVIGH
     437-614: Missing.

Show »
Length:415
Mass (Da):47,180
Checksum:i8F5306E3316AAFF1
GO
Isoform 12 (identifier: P35922-12) [UniParc]FASTAAdd to basket

Also known as: ISO12

The sequence of this isoform differs from the canonical sequence as follows:
     375-395: Missing.
     425-512: EVDQLRLERL...SDHRDELSDW → LQQRKRGRAS...VTRRRKSQTA
     513-614: Missing.

Show »
Length:491
Mass (Da):55,940
Checksum:iF16075B4136A226F
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei375 – 39521Missing in isoform 7, isoform 8, isoform 9, isoform 10, isoform 11 and isoform 12. CuratedVSP_002827Add
BLAST
Alternative sequencei425 – 51288EVDQL…ELSDW → LQQRKRGRASCAEETDGGVE EEEEDKEEEEEEEASKETTI IPEQIIVHVIQERLKEEQLM DPCRVPPVKGAGCARVKIVT RRRKSQTA in isoform 6 and isoform 12. CuratedVSP_002834Add
BLAST
Alternative sequencei425 – 44824EVDQL…GASSR → ELILKHQMLLKQNLTTETNS VIGH in isoform 4 and isoform 10. CuratedVSP_002831Add
BLAST
Alternative sequencei425 – 43612EVDQL…ERLQI → NLTTETNSVIGH in isoform 5 and isoform 11. CuratedVSP_002832Add
BLAST
Alternative sequencei437 – 614178Missing in isoform 5 and isoform 11. CuratedVSP_002833Add
BLAST
Alternative sequencei449 – 614166Missing in isoform 4 and isoform 10. CuratedVSP_002830Add
BLAST
Alternative sequencei490 – 51425Missing in isoform 3 and isoform 9. CuratedVSP_002829Add
BLAST
Alternative sequencei490 – 50112Missing in isoform 2 and isoform 8. CuratedVSP_002828Add
BLAST
Alternative sequencei513 – 614102Missing in isoform 6 and isoform 12. CuratedVSP_002835Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L23971 mRNA. Translation: AAA37635.1.
CCDSiCCDS30171.1. [P35922-1]
CCDS72385.1. [P35922-3]
PIRiS36173.
UniGeneiMm.3451.

Genome annotation databases

UCSCiuc009tiu.2. mouse. [P35922-1]
uc009tiv.2. mouse. [P35922-11]
uc009tiy.1. mouse. [P35922-5]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L23971 mRNA. Translation: AAA37635.1.
CCDSiCCDS30171.1. [P35922-1]
CCDS72385.1. [P35922-3]
PIRiS36173.
UniGeneiMm.3451.

3D structure databases

ProteinModelPortaliP35922.
SMRiP35922. Positions 1-200, 216-334, 395-424.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP35922. 7 interactions.
MINTiMINT-111096.
STRINGi10090.ENSMUSP00000085906.

PTM databases

iPTMnetiP35922.
PhosphoSiteiP35922.

Proteomic databases

EPDiP35922.
MaxQBiP35922.
PaxDbiP35922.
PeptideAtlasiP35922.
PRIDEiP35922.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiuc009tiu.2. mouse. [P35922-1]
uc009tiv.2. mouse. [P35922-11]
uc009tiy.1. mouse. [P35922-5]

Organism-specific databases

MGIiMGI:95564. Fmr1.

Phylogenomic databases

eggNOGiENOG410IF9J. Eukaryota.
ENOG410ZDJG. LUCA.
HOGENOMiHOG000293377.
HOVERGENiHBG005739.
InParanoidiP35922.
PhylomeDBiP35922.

Miscellaneous databases

ChiTaRSiFmr1. mouse.
PROiP35922.
SOURCEiSearch...

Gene expression databases

CleanExiMM_FMR1.

Family and domain databases

Gene3Di3.30.1370.10. 3 hits.
InterProiIPR008395. Agenet-like_dom.
IPR032196. FXMR_C2.
IPR022034. FXMRP1_C_core.
IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
[Graphical view]
PfamiPF05641. Agenet. 1 hit.
PF16098. FXMR_C2. 2 hits.
PF12235. FXMRP1_C_core. 1 hit.
PF00013. KH_1. 2 hits.
[Graphical view]
SMARTiSM00322. KH. 2 hits.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 2 hits.
PROSITEiPS51641. AGENET_LIKE. 2 hits.
PS50084. KH_TYPE_1. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human and murine FMR-1: alternative splicing and translational initiation downstream of the CGG-repeat."
    Ashley C.T. Jr., Sutcliffe J.S., Kunst C.B., Leiner H.A., Eichler E.E., Nelson D.L., Warren S.T.
    Nat. Genet. 4:244-251(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
    Strain: BALB/cJ.
    Tissue: Brain.
  2. "Fmr1 knockout mice: a model to study fragile X mental retardation."
    Bakker C.B., Verheij C., Willemsen R., van der Helm R., Oerlemans F., Vermey M., Bygrave A., Hoogeveen A.T., Oostra B.A.
    Cell 78:23-33(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  3. "A nuclear role for the Fragile X mental retardation protein."
    Fridell R.A., Benson R.E., Hua J., Bogerd H.P., Cullen B.R.
    EMBO J. 15:5408-5414(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, NUCLEOCYTOPLASMIC SHUTTLING, MUTAGENESIS OF 429-LEU--LEU-431.
  4. "The fragile X mental retardation protein is a ribonucleoprotein containing both nuclear localization and nuclear export signals."
    Eberhart D.E., Malter H.E., Feng Y., Warren S.T.
    Hum. Mol. Genet. 5:1083-1091(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, NUCLEOCYTOPLASMIC SHUTTLING, ASSOCIATION WITH POLYRIBOSOME AND MRNP, MUTAGENESIS OF 429-LEU--LEU-434.
  5. "The fragile X mental retardation protein is associated with poly(A)+ mRNA in actively translating polyribosomes."
    Corbin F., Bouillon M., Fortin A., Morin S., Rousseau F., Khandjian E.W.
    Hum. Mol. Genet. 6:1465-1472(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, ASSOCIATION WITH POLYRIBOSOME, ASSOCIATION WITH MRNP.
  6. "Abnormal dendritic spines in fragile X knockout mice: maturation and pruning deficits."
    Comery T.A., Harris J.B., Willems P.J., Oostra B.A., Irwin S.A., Weiler I.J., Greenough W.T.
    Proc. Natl. Acad. Sci. U.S.A. 94:5401-5404(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  7. "A novel RNA-binding nuclear protein that interacts with the fragile X mental retardation (FMR1) protein."
    Bardoni B., Schenck A., Mandel J.-L.
    Hum. Mol. Genet. 8:2557-2566(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NUFIP1.
  8. "Isolation of an FMRP-associated messenger ribonucleoprotein particle and identification of nucleolin and the fragile X-related proteins as components of the complex."
    Ceman S., Brown V., Warren S.T.
    Mol. Cell. Biol. 19:7925-7932(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FXR1; FXR2 AND NCL.
  9. "Identification of mouse YB1/p50 as a component of the FMRP-associated mRNP particle."
    Ceman S., Nelson R., Warren S.T.
    Biochem. Biophys. Res. Commun. 279:904-908(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH YBX1.
  10. "Microarray identification of FMRP-associated brain mRNAs and altered mRNA translational profiles in fragile X syndrome."
    Brown V., Jin P., Ceman S., Darnell J.C., O'Donnell W.T., Tenenbaum S.A., Jin X., Feng Y., Wilkinson K.D., Keene J.D., Darnell R.B., Warren S.T.
    Cell 107:477-487(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH MRNP, RNA-BINDING.
  11. "Abnormal development of dendritic spines in FMR1 knock-out mice."
    Nimchinsky E.A., Oberlander A.M., Svoboda K.
    J. Neurosci. 21:5139-5146(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  12. "The fragile X mental retardation protein inhibits translation via interacting with mRNA."
    Li Z., Zhang Y., Ku L., Wilkinson K.D., Warren S.T., Feng Y.
    Nucleic Acids Res. 29:2276-2283(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FXR2, RNA-BINDING.
  13. "A highly conserved protein family interacting with the fragile X mental retardation protein (FMRP) and displaying selective interactions with FMRP-related proteins FXR1P and FXR2P."
    Schenck A., Bardoni B., Moro A., Bagni C., Mandel J.-L.
    Proc. Natl. Acad. Sci. U.S.A. 98:8844-8849(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CYFIP1 AND CYFIP2, SUBCELLULAR LOCATION.
  14. "Identification of mRNA/protein (mRNP) complexes containing Puralpha, mStaufen, fragile X protein, and myosin Va and their association with rough endoplasmic reticulum equipped with a kinesin motor."
    Ohashi S., Koike K., Omori A., Ichinose S., Ohara S., Kobayashi S., Sato T.A., Anzai K.
    J. Biol. Chem. 277:37804-37810(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MYO5A AND PURA.
  15. "Altered synaptic plasticity in a mouse model of fragile X mental retardation."
    Huber K.M., Gallagher S.M., Warren S.T., Bear M.F.
    Proc. Natl. Acad. Sci. U.S.A. 99:7746-7750(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  16. "The fragile X syndrome protein FMRP associates with BC1 RNA and regulates the translation of specific mRNAs at synapses."
    Zalfa F., Giorgi M., Primerano B., Moro A., Di Penta A., Reis S., Oostra B., Bagni C.
    Cell 112:317-327(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ASSOCIATION WITH POLYRIBOSOME AND MRNP, RNA-BINDING, DISRUPTION PHENOTYPE.
  17. "Phosphorylation influences the translation state of FMRP-associated polyribosomes."
    Ceman S., O'Donnell W.T., Reed M., Patton S., Pohl J., Warren S.T.
    Hum. Mol. Genet. 12:3295-3305(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-499, MUTAGENESIS OF SER-499, IDENTIFICATION BY MASS SPECTROMETRY.
  18. "RNA cargoes associating with FMRP reveal deficits in cellular functioning in Fmr1 null mice."
    Miyashiro K.Y., Beckel-Mitchener A., Purk T.P., Becker K.G., Barret T., Liu L., Carbonetto S., Weiler I.J., Greenough W.T., Eberwine J.
    Neuron 37:417-431(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, ASSOCIATION WITH POLYRIBOSOME, ASSOCIATION WITH MRNP.
  19. "The fragile X mental retardation protein binds and regulates a novel class of mRNAs containing U rich target sequences."
    Chen L., Yun S.W., Seto J., Liu W., Toth M.
    Neuroscience 120:1005-1017(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  20. "The fragile X mental retardation protein is required for type-I metabotropic glutamate receptor-dependent translation of PSD-95."
    Todd P.K., Mack K.J., Malter J.S.
    Proc. Natl. Acad. Sci. U.S.A. 100:14374-14378(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, INDUCTION.
  21. "Developmentally-programmed FMRP expression in oligodendrocytes: a potential role of FMRP in regulating translation in oligodendroglia progenitors."
    Wang H., Ku L., Osterhout D.J., Li W., Ahmadian A., Liang Z., Feng Y.
    Hum. Mol. Genet. 13:79-89(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ASSOCIATION WITH POLYRIBOSOME, RNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  22. "The C-terminus of fragile X mental retardation protein interacts with the multi-domain Ran-binding protein in the microtubule-organising centre."
    Menon R.P., Gibson T.J., Pastore A.
    J. Mol. Biol. 343:43-53(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RANBP9.
  23. "Metabotropic glutamate receptor activation regulates fragile x mental retardation protein and FMR1 mRNA localization differentially in dendrites and at synapses."
    Antar L.N., Afroz R., Dictenberg J.B., Carroll R.C., Bassell G.J.
    J. Neurosci. 24:2648-2655(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  24. "Fragile X mental retardation protein is associated with translating polyribosomes in neuronal cells."
    Stefani G., Fraser C.E., Darnell J.C., Darnell R.B.
    J. Neurosci. 24:7272-7276(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, ASSOCIATION WITH POLYRIBOSOME.
  25. "Kinesin transports RNA: isolation and characterization of an RNA-transporting granule."
    Kanai Y., Dohmae N., Hirokawa N.
    Neuron 43:513-525(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  26. "Biochemical evidence for the association of fragile X mental retardation protein with brain polyribosomal ribonucleoparticles."
    Khandjian E.W., Huot M.E., Tremblay S., Davidovic L., Mazroui R., Bardoni B.
    Proc. Natl. Acad. Sci. U.S.A. 101:13357-13362(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, ASSOCIATION WITH MRNP.
  27. "The fragile X protein controls microtubule-associated protein 1B translation and microtubule stability in brain neuron development."
    Lu R., Wang H., Liang Z., Ku L., O'donnell W.T., Li W., Warren S.T., Feng Y.
    Proc. Natl. Acad. Sci. U.S.A. 101:15201-15206(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  28. "Fragile X mental retardation protein is necessary for neurotransmitter-activated protein translation at synapses."
    Weiler I.J., Spangler C.C., Klintsova A.Y., Grossman A.W., Kim S.H., Bertaina-Anglade V., Khaliq H., de Vries F.E., Lambers F.A., Hatia F., Base C.K., Greenough W.T.
    Proc. Natl. Acad. Sci. U.S.A. 101:17504-17509(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  29. "Localization of FMRP-associated mRNA granules and requirement of microtubules for activity-dependent trafficking in hippocampal neurons."
    Antar L.N., Dictenberg J.B., Plociniak M., Afroz R., Bassell G.J.
    Genes Brain Behav. 4:350-359(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  30. "Kissing complex RNAs mediate interaction between the Fragile-X mental retardation protein KH2 domain and brain polyribosomes."
    Darnell J.C., Fraser C.E., Mostovetsky O., Stefani G., Jones T.A., Eddy S.R., Darnell R.B.
    Genes Dev. 19:903-918(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH POLYRIBOSOME.
  31. "The RNA-binding protein Fragile X-related 1 regulates somite formation in Xenopus laevis."
    Huot M.-E., Bisson N., Davidovic L., Mazroui R., Labelle Y., Moss T., Khandjian E.W.
    Mol. Biol. Cell 16:4350-4361(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  32. "Local functions for FMRP in axon growth cone motility and activity-dependent regulation of filopodia and spine synapses."
    Antar L.N., Li C., Zhang H., Carroll R.C., Bassell G.J.
    Mol. Cell. Neurosci. 32:37-48(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  33. "Dynamic translational and proteasomal regulation of fragile X mental retardation protein controls mGluR-dependent long-term depression."
    Hou L., Antion M.D., Hu D., Spencer C.M., Paylor R., Klann E.
    Neuron 51:441-454(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PROTEOLYTIC DEGRADATION, INDUCTION, DISRUPTION PHENOTYPE.
  34. "The fragile X mental retardation protein interacts with a distinct mRNA nuclear export factor NXF2."
    Lai D., Sakkas D., Huang Y.
    RNA 12:1446-1449(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NXF2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  35. "Dysregulated metabotropic glutamate receptor-dependent translation of AMPA receptor and postsynaptic density-95 mRNAs at synapses in a mouse model of fragile X syndrome."
    Muddashetty R.S., Kelic S., Gross C., Xu M., Bassell G.J.
    J. Neurosci. 27:5338-5348(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ASSOCIATION WITH MRNA, DISRUPTION PHENOTYPE.
  36. "A new function for the fragile X mental retardation protein in regulation of PSD-95 mRNA stability."
    Zalfa F., Eleuteri B., Dickson K.S., Mercaldo V., De Rubeis S., di Penta A., Tabolacci E., Chiurazzi P., Neri G., Grant S.G., Bagni C.
    Nat. Neurosci. 10:578-587(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  37. "Fragile X mental retardation protein FMRP and the RNA export factor NXF2 associate with and destabilize Nxf1 mRNA in neuronal cells."
    Zhang M., Wang Q., Huang Y.
    Proc. Natl. Acad. Sci. U.S.A. 104:10057-10062(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NXF2, TISSUE SPECIFICITY.
  38. "The fragile X syndrome protein represses activity-dependent translation through CYFIP1, a new 4E-BP."
    Napoli I., Mercaldo V., Boyl P.P., Eleuteri B., Zalfa F., De Rubeis S., Di Marino D., Mohr E., Massimi M., Falconi M., Witke W., Costa-Mattioli M., Sonenberg N., Achsel T., Bagni C.
    Cell 134:1042-1054(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CYFIP1-EIF4E COMPLEX, ASSOCIATION WITH MRNP, RNA-BINDING, SUBCELLULAR LOCATION.
  39. "A direct role for FMRP in activity-dependent dendritic mRNA transport links filopodial-spine morphogenesis to fragile X syndrome."
    Dictenberg J.B., Swanger S.A., Antar L.N., Singer R.H., Bassell G.J.
    Dev. Cell 14:926-939(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH KIF5A, INTERACTION WITH DYNEIN, ASSOCIATION WITH MICROTUBULES, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  40. "In vitro and in cellulo evidences for association of the survival of motor neuron complex with the fragile X mental retardation protein."
    Piazzon N., Rage F., Schlotter F., Moine H., Branlant C., Massenet S.
    J. Biol. Chem. 283:5598-5610(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH THE SMN CORE COMPLEX.
  41. "The G-quartet containing FMRP binding site in FMR1 mRNA is a potent exonic splicing enhancer."
    Didiot M.C., Tian Z., Schaeffer C., Subramanian M., Mandel J.L., Moine H.
    Nucleic Acids Res. 36:4902-4912(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  42. "Fragile X mental retardation protein regulates the levels of scaffold proteins and glutamate receptors in postsynaptic densities."
    Schuett J., Falley K., Richter D., Kreienkamp H.J., Kindler S.
    J. Biol. Chem. 284:25479-25487(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  43. "The FXG: a presynaptic fragile X granule expressed in a subset of developing brain circuits."
    Christie S.B., Akins M.R., Schwob J.E., Fallon J.R.
    J. Neurosci. 29:1514-1524(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  44. "A novel function for fragile X mental retardation protein in translational activation."
    Bechara E.G., Didiot M.C., Melko M., Davidovic L., Bensaid M., Martin P., Castets M., Pognonec P., Khandjian E.W., Moine H., Bardoni B.
    PLoS Biol. 7:E16-E16(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING, DISRUPTION PHENOTYPE.
  45. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-462 AND SER-602, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney, Lung, Spleen and Testis.
  46. "Fragile X mental retardation protein controls gating of the sodium-activated potassium channel Slack."
    Brown M.R., Kronengold J., Gazula V.R., Chen Y., Strumbos J.G., Sigworth F.J., Navaratnam D., Kaczmarek L.K.
    Nat. Neurosci. 13:819-821(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH KCNT1.
  47. "Regulation of synaptic structure and function by FMRP-associated microRNAs miR-125b and miR-132."
    Edbauer D., Neilson J.R., Foster K.A., Wang C.F., Seeburg D.P., Batterton M.N., Tada T., Dolan B.M., Sharp P.A., Sheng M.
    Neuron 65:373-384(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING.
  48. Cited for: FUNCTION, INTERACTION WITH RPLP0, RNA-BINDING, ASSOCIATION WITH POLYRIBOSOME, DISRUPTION PHENOTYPE.
  49. "Fragile X mental retardation protein regulates protein expression and mRNA translation of the potassium channel Kv4.2."
    Gross C., Yao X., Pong D.L., Jeromin A., Bassell G.J.
    J. Neurosci. 31:5693-5698(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING, DISRUPTION PHENOTYPE.
  50. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  51. "FMRP and myelin protein expression in oligodendrocytes."
    Giampetruzzi A., Carson J.H., Barbarese E.
    Mol. Cell. Neurosci. 56:333-341(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: LACK OF FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  52. "Identification and characterisation of Simiate, a novel protein linked to the fragile X syndrome."
    Derlig K., Giessl A., Brandstatter J.H., Enz R., Dahlhaus R.
    PLoS ONE 8:E83007-E83007(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, RNA-BINDING.
  53. Cited for: FUNCTION, CHROMATIN BINDING, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  54. "MOV10 and FMRP regulate AGO2 association with microRNA recognition elements."
    Kenny P.J., Zhou H., Kim M., Skariah G., Khetani R.S., Drnevich J., Arcila M.L., Kosik K.S., Ceman S.
    Cell Rep. 9:1729-1741(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MOV10.
  55. "Fragile X mental retardation protein controls synaptic vesicle exocytosis by modulating N-type calcium channel density."
    Ferron L., Nieto-Rostro M., Cassidy J.S., Dolphin A.C.
    Nat. Commun. 5:3628-3628(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CACNA1B, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  56. "FMRP interacts with G-quadruplex structures in the 3'-UTR of its dendritic target Shank1 mRNA."
    Zhang Y., Gaetano C.M., Williams K.R., Bassell G.J., Mihailescu M.R.
    RNA Biol. 11:1364-1374(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA-BINDING.
  57. "Independent role for presynaptic FMRP revealed by an FMR1 missense mutation associated with intellectual disability and seizures."
    Myrick L.K., Deng P.Y., Hashimoto H., Oh Y.M., Cho Y., Poidevin M.J., Suhl J.A., Visootsak J., Cavalli V., Jin P., Cheng X., Warren S.T., Klyachko V.A.
    Proc. Natl. Acad. Sci. U.S.A. 112:949-956(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH KCNMB4, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiFMR1_MOUSE
AccessioniPrimary (citable) accession number: P35922
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: July 6, 2016
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.