Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Different targets for the fragile X-related proteins revealed by their distinct nuclear localizations.
Dissecting FMR1, the protein responsible for fragile X syndrome, in its structural and functional domains.
A novel RNA-binding nuclear protein that interacts with the fragile X mental retardation (FMR1) protein.
The fragile X-related proteins FXR1P and FXR2P contain a functional nucleolar-targeting signal equivalent to the HIV-1 regulatory proteins.
Evidence that fragile X mental retardation protein is a negative regulator of translation.
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.
Trapping of messenger RNA by Fragile X Mental Retardation protein into cytoplasmic granules induces translation repression.
Transport of fragile X mental retardation protein via granules in neurites of PC12 cells.
82-FIP, a novel FMRP (fragile X mental retardation protein) interacting protein, shows a cell cycle-dependent intracellular localization.
The fragile X mental retardation protein binds and regulates a novel class of mRNAs containing U rich target sequences.
The composition of Staufen-containing RNA granules from human cells indicates their role in the regulated transport and translation of messenger RNAs.
Transport kinetics of FMRP containing the I304N mutation of severe fragile X syndrome in neurites of living rat PC12 cells.
The C terminus of fragile X mental retardation protein interacts with the multi-domain Ran-binding protein in the microtubule-organising centre.
Kissing complex RNAs mediate interaction between the Fragile-X mental retardation protein KH2 domain and brain polyribosomes.
The structure of the N-terminal domain of the fragile X mental retardation protein: a platform for protein-protein interaction.
The nuclear microspherule protein 58 is a novel RNA-binding protein that interacts with fragile X mental retardation protein in polyribosomal mRNPs from neurons.
Local functions for FMRP in axon growth cone motility and activity-dependent regulation of filopodia and spine synapses.
Dicer-derived microRNAs are utilized by the fragile X mental retardation protein for assembly on target RNAs.
A new function for the fragile X mental retardation protein in regulation of PSD-95 mRNA stability.
Fragile X mental retardation syndrome: structure of the KH1-KH2 domains of fragile X mental retardation protein.
In vitro and in cellulo evidences for association of the survival of motor neuron complex with the fragile X mental retardation protein.
The G-quartet containing FMRP binding site in FMR1 mRNA is a potent exonic splicing enhancer.
Tdrd3 is a novel stress granule-associated protein interacting with the Fragile-X syndrome protein FMRP.
The fragile X syndrome protein represses activity-dependent translation through CYFIP1, a new 4E-BP.
Fragile X mental retardation protein FMRP binds mRNAs in the nucleus.
Translational regulation of the human achaete-scute homologue-1 by fragile X mental retardation protein.
-
Selected human-cell experiments support positive regulation of ASCL1 translation by FMRP, using endogenous depletion and polysome or untranslated-region reporter measurements. The tested RNA element and protein constructs constrain the result; target recognition does not require repression of every bound mRNA.
A novel function for fragile X mental retardation protein in translational activation.
Defining the membrane proteome of NK cells.
On the aggregation properties of FMRP--a link with the FXTAS syndrome?
Structure-function studies of FMRP RGG peptide recognition of an RNA duplex-quadruplex junction.
Protein interactome reveals converging molecular pathways among autism disorders.
Evidence for the association of the human regulatory protein Ki-1/57 with the translational machinery.
Insights into RNA biology from an atlas of mammalian mRNA-binding proteins.
The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts.
FMRP targets distinct mRNA sequence elements to regulate protein expression.
Nuclear Fragile X Mental Retardation Protein is localized to Cajal bodies.
Fragile X mental retardation protein stimulates ribonucleoprotein assembly of influenza A virus.
Subcellular fractionation and localization studies reveal a direct interaction of the fragile X mental retardation protein (FMRP) with nucleolin.
A chromatin-dependent role of the fragile X mental retardation protein FMRP in the DNA damage response.
Human-chromatin-related protein interactions identify a demethylase complex required for chromosome segregation.
MOV10 and FMRP regulate AGO2 association with microRNA recognition elements.
Independent role for presynaptic FMRP revealed by an FMR1 missense mutation associated with intellectual disability and seizures.
Crystal structure reveals specific recognition of a G-quadruplex RNA by a β-turn in the RGG motif of FMRP.
Identification of Human Neuronal Protein Complexes Reveals Biochemical Activities and Convergent Mechanisms of Action in Autism Spectrum Disorders.
Phosphoregulated FMRP phase separation models activity-dependent translation through bidirectional control of mRNA granule formation.
-
Recombinant human FMRP C-terminal low-complexity fragments form RNA-containing condensates and repress a luciferase translation readout in rabbit reticulocyte lysate, with phosphorylation and arginine-methylation effects. This supports a link between assembly and repression in the reconstituted system, without establishing a universal neuronal-granule mechanism.
HENA, heterogeneous network-based data set for Alzheimer's disease.
Phospho-dependent phase separation of FMRP and CAPRIN1 recapitulates regulation of translation and deadenylation.
-
Human FMRP and CAPRIN1 low-complexity regions support phosphorylation-sensitive condensate organization and RNA partitioning, with translation and CNOT7-dependent deadenylation readouts. The experimentally established binding and scaffold capacities are distinct from the proposed integration of cellular signaling pathways, whose precise causal annotation remains unresolved.
The RNA-binding protein FMRP facilitates the nuclear export of N(6)-methyladenosine-containing mRNAs.
Novel FMRP interaction networks linked to cellular stress.
Fragile X-related protein family: a double-edged sword in neurodevelopmental disorders and cancer.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Protein interaction studies in human induced neurons indicate convergent biology underlying autism spectrum disorders.
Using brain cell-type-specific protein interactomes to interpret neurodevelopmental genetic signals in schizophrenia.
Systematic identification of post-transcriptional regulatory modules.
Multimodal cell maps as a foundation for structural and functional genomics.
The fragile X mental retardation syndrome protein interacts with novel homologs FXR1 and FXR2.
The protein product of the fragile X gene, FMR1, has characteristics of an RNA-binding protein.
FMR1 protein: conserved RNP family domains and selective RNA binding.
FXR1, an autosomal homolog of the fragile X mental retardation gene.
Essential role for KH domains in RNA binding: impaired RNA binding by a mutation in the KH domain of FMR1 that causes fragile X syndrome.
The FMR-1 protein is cytoplasmic, most abundant in neurons and appears normal in carriers of a fragile X premutation.
Characterization and localization of the FMR-1 gene product associated with fragile X syndrome.
Alternative splicing of exon 14 determines nuclear or cytoplasmic localisation of fmr1 protein isoforms.
Differential expression of FMR1, FXR1 and FXR2 proteins in human brain and testis.
FMRP associates with polyribosomes as an mRNP, and the I304N mutation of severe fragile X syndrome abolishes this association.
Fragile X mental retardation protein: nucleocytoplasmic shuttling and association with somatodendritic ribosomes.
Fragile X mental retardation protein is translated near synapses in response to neurotransmitter activation.
The fragile X mental retardation protein inhibits translation via interacting with mRNA.
Abnormal development of dendritic spines in FMR1 knock-out mice.
The N-terminus of the fragile X mental retardation protein contains a novel domain involved in dimerization and RNA binding.
Developmentally-programmed FMRP expression in oligodendrocytes: a potential role of FMRP in regulating translation in oligodendroglia progenitors.
Metabotropic glutamate receptor activation regulates fragile x mental retardation protein and FMR1 mRNA localization differentially in dendrites and at synapses.
Localization of FMRP-associated mRNA granules and requirement of microtubules for activity-dependent trafficking in hippocampal neurons.
Methylation regulates the intracellular protein-protein and protein-RNA interactions of FMRP.
A direct role for FMRP in activity-dependent dendritic mRNA transport links filopodial-spine morphogenesis to fragile X syndrome.
Cells lacking the fragile X mental retardation protein (FMRP) have normal RISC activity but exhibit altered stress granule assembly.
The FXG: a presynaptic fragile X granule expressed in a subset of developing brain circuits.
Fragile X mental retardation protein controls synaptic vesicle exocytosis by modulating N-type calcium channel density.
Sub-synaptic, multiplexed analysis of proteins reveals Fragile X related protein 2 is mislocalized in Fmr1 KO synapses.
N(6)-methyladenosine (m(6)A) recruits and repels proteins to regulate mRNA homeostasis.
Loss of FMRP Impaired Hippocampal Long-Term Plasticity and Spatial Learning in Rats.
The FXR1 network acts as a signaling scaffold for actomyosin remodeling.
FMR1 source access, assay scope and review decisions
FMR1 original annotation contexts, products and source provenance