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Entry version 97 (02 Jun 2021)
Sequence version 1 (21 Dec 2004)
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Synaptic functional regulator FMR1



Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at transcript leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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. Plays a role in the alternative splicing of its own mRNA. Plays a role in mRNA nuclear export. Together with export factor NXF2, is involved in the regulation of the NXF1 mRNA stability in neurons. 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. 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. Plays a role as a repressor of mRNA translation during the transport of dendritic mRNAs to postsynaptic dendritic spines. Component of the CYFIP1-EIF4E-FMR1 complex which blocks cap-dependent mRNA translation initiation. Represses mRNA translation by stalling ribosomal translocation during elongation. Reports are contradictory with regards to its ability to mediate translation inhibition of MBP mRNA in oligodendrocytes. 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. Facilitates the assembly of miRNAs on specific target mRNAs. Plays also a role as an activator of mRNA translation of a subset of dendritic mRNAs at synapses. In response to mGluR stimulation, FMR1-target mRNAs are rapidly derepressed, allowing for local translation at synapses. Binds to a large subset of dendritic mRNAs that encode a myriad of proteins involved in pre- and postsynaptic functions. 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. Binds to intramolecular G-quadruplex structures in the 5'- or 3'-UTRs of mRNA targets. Binds to G-quadruplex structures in the 3'-UTR of its own mRNA. Binds also to RNA ligands harboring a kissing complex (kc) structure; this binding may mediate the association of FMR1 with polyribosomes. Binds mRNAs containing U-rich target sequences. 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. 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. Associates with export factor NXF1 mRNA-containing ribonucleoprotein particles (mRNPs) in a NXF2-dependent manner. Binds to a subset of miRNAs in the brain. May associate with nascent transcripts in a nuclear protein NXF1-dependent manner. In vitro, binds to RNA homomer; preferentially on poly(G) and to a lesser extent on poly(U), but not on poly(A) or poly(C). Moreover, plays a role in the modulation of the sodium-activated potassium channel KCNT1 gating activity. 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. Modulates the voltage-dependent calcium channel CACNA1B expression at the plasma membrane by targeting the channels for proteosomal degradation. Plays a role in regulation of MAP1B-dependent microtubule dynamics during neuronal development. 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. 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 H2AX/H2A.x and BRCA1 phosphorylations.

By similarity

<p>The <a href="">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, Repressor, Ribonucleoprotein, RNA-binding
Biological processDNA damage, mRNA processing, mRNA splicing, mRNA transport, Neurogenesis, RNA-mediated gene silencing, Translation regulation, Transport

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Synaptic functional regulator FMR1Curated
Alternative name(s):
Fragile X mental retardation protein 1 homologBy similarity
Short name:
FMRPBy similarity
Short name:
Protein FMR-1By similarity
<p>This subsection of the <a href="">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:FMR1By similarity
<p>This subsection of the <a href="">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
<p>This subsection of the <a href="">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9601 [NCBI]
<p>This subsection of the <a href="">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
<p>This subsection of the <a href="">Names and taxonomy</a> section is present for entries that are part of a <a href="">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001595 <p>A UniProt <a href="">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003421841 – 594Synaptic functional regulator FMR1Add BLAST594

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="">lipids</a>, <a href="">glycans</a> and <a href="">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-acetylmethionineBy similarity1
Modified residuei337PhosphoserineBy similarity1
Modified residuei370PhosphoserineBy similarity1
Modified residuei442PhosphothreonineBy similarity1
Modified residuei450Omega-N-methylarginineBy similarity1
Modified residuei479PhosphoserineBy similarity1
Modified residuei513Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei513Omega-N-methylarginine; alternateBy similarity1
Modified residuei518Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei518Omega-N-methylarginine; alternateBy similarity1
Modified residuei523Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei523Omega-N-methylarginine; alternateBy similarity1
Modified residuei525Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei525Omega-N-methylarginine; alternateBy similarity1
Modified residuei582PhosphoserineBy similarity1

<p>This subsection of the <a href="">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated. Phosphorylated on several serine residues. Phosphorylation at Ser-479 is required for phosphorylation of other nearby serine residues. Phosphorylation has no effect on the binding of individual mRNA species, but may affect the association with polyribosome. Unphosphorylated FMR1 is associated with actively translating polyribosome, whereas a fraction of phosphorylated FMR1 is associated with apparently stalled polyribosome. Dephosphorylation by an activated phosphatase may release the FMR1-mediated translational repression and allow synthesis of a locally required protein at snypases.By similarity
Monoubiquitinated. Polyubiquitinated. Ubiquitinated and targeted for proteasomal degradation after activation of metabotropic glutamate receptor (mGluR).By similarity
Monomethylated and asymmetrically dimethylated at four arginine residues of the arginine-glycine-glycine box. Methylation disrupts the binding of FMRP to RNAs through its RGG box. 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

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer. Forms heterodimer with FXR1; heterodimerization occurs in a methylation-dependent manner. Forms heterodimer with FXR2. Homooligomer.

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. Associates with the SMN core complex that contains SMN, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP.

Part of a ribonucleoprotein complex with AGO2/EIF2C2 and miRNAs.

Interacts with AGO2/EIF2C2.

Interacts (via C-terminus) with CACNA1B; this interaction induces a decrease in the number of presynaptic functional CACNA1B channels at the cell surface.

Interacts with CYFIP1; this interaction recruits CYFIP1 to capped mRNA.

Interacts with CYFIP2.

Interacts with EIF5; this interaction occurs in a RNA-dependent manner.

Interacts with dynein.

Interacts with FXR1 and FXR2.

Interacts with methylated histone H3.

Interacts with IGF2BP1; this interaction allows to recruit IGF2BP1 to mRNA in a FMR1-dependent manner.

Interacts (via N-terminus) with KCNMB4.

Interacts with KCNT1 (via C-terminus); this interaction alters gating properties of KCNT1.

Interacts (via phosphorylated form) with MCRS1 (via N-terminus).

Interacts with MOV10; this interaction is direct, occurs in an RNA-dependent manner on polysomes and induces association of MOV10 with RNAs.

Interacts with MYO5A and PURA; these interactions occur in association with polyribosome.

Interacts with NCL.

Interacts with NUFIP1.

Interacts (via N-terminus) with NUFIP2.

Interacts with NXF1; this interaction occurs in a mRNA-dependent and polyribosome-independent manner in the nucleus.

Interacts with NXF2 (via N-terminus); this interaction is direct and occurs in a NXF1 mRNA-containing mRNP complexes.

Interacts with RANBP9 (via C-terminus); this interaction is direct and inhibits binding of FMR1 to RNA homomer.

Interacts with RPLP0.

Interacts (via C-terminus) with SMN (via C-terminus); this interaction is direct and occurs in a RNA-independent manner.

Interacts with TDRD3 (via C-terminus); this interaction is direct.

Interacts with YBX1; this interaction occurs in association with polyribosome.

Interacts with nucleosome. Associates with polyribosome; this association occurs in a mRNA-dependent manner. Associates with cytoplasmic messenger ribonucleoprotein particles (mRNPs). Associates with microtubules in a kinesin- and dynein-dependent manner.

Interacts with HABP4.

By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks


<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models


Database of comparative protein structure models


<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini4 – 50Agenet-like 1PROSITE-ProRule annotationAdd BLAST47
Domaini63 – 115Agenet-like 2PROSITE-ProRule annotationAdd BLAST53
Domaini218 – 279KH 1PROSITE-ProRule annotationAdd BLAST62
Domaini281 – 348KH 2PROSITE-ProRule annotationAdd BLAST68


Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 184Required for nuclear localizationBy similarityAdd BLAST184
Regioni172 – 211Necessary for interaction with CYFIP1, CYFIP2, FXR1 and FXR2By similarityAdd BLAST40
Regioni325 – 349DisorderedSequence analysisAdd BLAST25
Regioni376 – 470Required for nuclear exportBy similarityAdd BLAST95
Regioni398 – 594Interaction with RANBP9By similarityAdd BLAST197
Regioni422 – 594DisorderedSequence analysisAdd BLAST173
Regioni513 – 527RNA-binding RGG-boxBy similarityAdd BLAST15


Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi403 – 422Nuclear export signalBy similarityAdd BLAST20
Motifi506 – 513Nucleolar localization signal 1By similarity8
Motifi575 – 579Nucleolar localization signal 2By similarity5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi479 – 516Basic and acidic residuesSequence analysisAdd BLAST38
Compositional biasi528 – 550Basic and acidic residuesSequence analysisAdd BLAST23
Compositional biasi551 – 565Polar residuesSequence analysisAdd BLAST15
Compositional biasi566 – 583Basic and acidic residuesSequence analysisAdd BLAST18

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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 homomer poly(G).By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the FMR1 family.Curated

Keywords - Domaini


Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

ENOG502QPKJ, Eukaryota

InParanoid: Eukaryotic Ortholog Groups


Identification of Orthologs from Complete Genome Data


Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

3.30.1370.10, 1 hit

Integrated resource of protein families, domains and functional sites

View protein in InterPro
IPR008395, Agenet-like_dom
IPR040148, FMR1
IPR040472, FMRP_KH0
IPR032196, FXMR_C2
IPR022034, FXMRP1_C_core
IPR004087, KH_dom
IPR004088, KH_dom_type_1
IPR036612, KH_dom_type_1_sf
IPR041560, Tudor_FRX1

The PANTHER Classification System

PTHR10603, PTHR10603, 1 hit

Pfam protein domain database

View protein in Pfam
PF05641, Agenet, 1 hit
PF16098, FXMR_C2, 1 hit
PF12235, FXMRP1_C_core, 1 hit
PF00013, KH_1, 2 hits
PF17904, KH_9, 1 hit
PF18336, Tudor_FRX1, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

View protein in SMART
SM00322, KH, 2 hits

Superfamily database of structural and functional annotation

SSF54791, SSF54791, 2 hits

PROSITE; a protein domain and family database

View protein in PROSITE
PS51641, AGENET_LIKE, 2 hits
PS50084, KH_TYPE_1, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="">length</a> and <a href="">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="">Sequence</a> section indicates if the <a href="">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q5R9B4-1 [UniParc]FASTAAdd to basket
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Mass (Da):67,057
Last modified:December 21, 2004 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iC465B5790C6BEB0D

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database


GenBank nucleotide sequence database


DNA Data Bank of Japan; a nucleotide sequence database

Links Updated
CR859475 mRNA Translation: CAH91646.1

NCBI Reference Sequences

NP_001125966.1, NM_001132494.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes


KEGG: Kyoto Encyclopedia of Genes and Genomes


<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
Links Updated
CR859475 mRNA Translation: CAH91646.1
RefSeqiNP_001125966.1, NM_001132494.1

3D structure databases


Protein-protein interaction databases


Genome annotation databases


Organism-specific databases

Comparative Toxicogenomics Database


Phylogenomic databases

eggNOGiENOG502QPKJ, Eukaryota

Family and domain databases

Gene3Di3.30.1370.10, 1 hit
InterProiView protein in InterPro
IPR008395, Agenet-like_dom
IPR040148, FMR1
IPR040472, FMRP_KH0
IPR032196, FXMR_C2
IPR022034, FXMRP1_C_core
IPR004087, KH_dom
IPR004088, KH_dom_type_1
IPR036612, KH_dom_type_1_sf
IPR041560, Tudor_FRX1
PANTHERiPTHR10603, PTHR10603, 1 hit
PfamiView protein in Pfam
PF05641, Agenet, 1 hit
PF16098, FXMR_C2, 1 hit
PF12235, FXMRP1_C_core, 1 hit
PF00013, KH_1, 2 hits
PF17904, KH_9, 1 hit
PF18336, Tudor_FRX1, 1 hit
SMARTiView protein in SMART
SM00322, KH, 2 hits
SUPFAMiSSF54791, SSF54791, 2 hits
PROSITEiView protein in PROSITE
PS51641, AGENET_LIKE, 2 hits
PS50084, KH_TYPE_1, 2 hits

MobiDB: a database of protein disorder and mobility annotations


<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFMR1_PONAB
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q5R9B4
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: December 21, 2004
Last modified: June 2, 2021
This is version 97 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome


  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
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