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Protein

Synaptic functional regulator FMR1

Gene

FMR1

Organism
Homo sapiens (Human)
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:16631377, PubMed:18653529, PubMed:19166269, PubMed:23235829, PubMed:25464849). Plays a role in the alternative splicing of its own mRNA (PubMed:18653529). Plays a role in mRNA nuclear export (By similarity). Together with export factor NXF2, is involved in the regulation of the NXF1 mRNA stability in neurons (By similarity). 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 (By similarity). 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 (By similarity). Plays a role as a repressor of mRNA translation during the transport of dendritic mRNAs to postnyaptic dendritic spines (PubMed:11532944, PubMed:11157796, PubMed:12594214, PubMed:23235829). Component of the CYFIP1-EIF4E-FMR1 complex which blocks cap-dependent mRNA translation initiation (By similarity). Represses mRNA translation by stalling ribosomal translocation during elongation (By similarity). Reports are contradictory with regards to its ability to mediate translation inhibition of MBP mRNA in oligodendrocytes (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:14703574, PubMed:17057366, PubMed:25464849). Facilitates the assembly of miRNAs on specific target mRNAs (PubMed:17057366). Plays also a role as an activator of mRNA translation of a subset of dendritic mRNAs at synapses (PubMed:19097999, PubMed:19166269). In response to mGluR stimulation, FMR1-target mRNAs are rapidly derepressed, allowing for local translation at synapses (By similarity). Binds to a large subset of dendritic mRNAs that encode a myriad of proteins involved in pre- and postsynaptic functions (PubMed:7692601, PubMed:11719189, PubMed:11157796, PubMed:12594214, PubMed:17417632, PubMed:23235829, PubMed:24448548). 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 (PubMed:23235829). Binds to intramolecular G-quadruplex structures in the 5'- or 3'-UTRs of mRNA targets (PubMed:11719189, PubMed:18579868, PubMed:25464849, PubMed:25692235). Binds to G-quadruplex structures in the 3'-UTR of its own mRNA (PubMed:7692601, PubMed:11532944, PubMed:12594214, PubMed:15282548, PubMed:18653529). Binds also to RNA ligands harboring a kissing complex (kc) structure; this binding may mediate the association of FMR1 with polyribosomes (PubMed:15805463). Binds mRNAs containing U-rich target sequences (PubMed:12927206). 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 (By similarity). Associates with export factor NXF1 mRNA-containing ribonucleoprotein particles (mRNPs) in a NXF2-dependent manner (By similarity). Binds to a subset of miRNAs in the brain (PubMed:14703574, PubMed:17057366). May associate with nascent transcripts in a nuclear protein NXF1-dependent manner (PubMed:18936162). 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) (PubMed:7688265, PubMed:7781595, PubMed:12950170, PubMed:15381419, PubMed:8156595). 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 (By similarity). Plays a role in regulation of MAP1B-dependent microtubule dynamics during neuronal development (By similarity). 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 similarity30 Publications
Isoform 10: binds to RNA homopolymer; preferentially on poly(G) and to a lesser extent on poly(U), but not on poly(A) or poly(C) (PubMed:24204304). May bind to RNA in Cajal bodies (PubMed:24204304).1 Publication
Isoform 6: binds to RNA homopolymer; preferentially on poly(G) and to a lesser extent on poly(U), but not on poly(A) or poly(C) (PubMed:24204304). May bind to RNA in Cajal bodies (PubMed:24204304).1 Publication
(Microbial infection) Acts as a positive regulator of influenza A virus (IAV) replication. Required for the assembly and nuclear export of the viral ribonucleoprotein (vRNP) components.1 Publication

GO - Molecular functioni

  • chromatin binding Source: UniProtKB
  • dynein binding Source: UniProtKB
  • G-quadruplex RNA binding Source: UniProtKB
  • identical protein binding Source: UniProtKB
  • ion channel binding Source: UniProtKB
  • 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: UniProtKB
  • poly(G) binding Source: UniProtKB
  • poly(U) RNA binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • ribosome binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • 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: UniProtKB
  • translation repressor activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor, Ribonucleoprotein

Keywords - Biological processi

DNA damage, Host-virus interaction, 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 1Imported
Short name:
FMRP1 Publication
Short name:
Protein FMR-11 Publication
Gene namesi
Name:FMR1Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:3775. FMR1.

Subcellular locationi

Isoform 6 :
Isoform 9 :
Isoform 10 :
  • Nucleus 1 Publication
  • NucleusCajal body 1 Publication

  • Note: Colocalizes with Colin and SMN in Cajal bodies (PubMed:24204304).
Isoform 11 :
  • Nucleus 1 Publication
  • NucleusCajal body 1 Publication

GO - Cellular componenti

  • axon Source: UniProtKB
  • axon terminus Source: UniProtKB
  • Cajal body Source: UniProtKB
  • cell junction Source: UniProtKB-KW
  • cell projection Source: UniProtKB
  • chromocenter Source: UniProtKB
  • chromosome Source: UniProtKB
  • chromosome, centromeric region Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB
  • cytoplasmic ribonucleoprotein granule Source: UniProtKB
  • dendrite Source: UniProtKB
  • dendritic filopodium Source: UniProtKB
  • dendritic shaft Source: Ensembl
  • 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: UniProtKB
  • membrane Source: UniProtKB
  • mRNA cap binding complex Source: UniProtKB
  • neuronal ribonucleoprotein granule Source: UniProtKB
  • neuron projection Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
  • perikaryon Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • polysome Source: UniProtKB
  • postsynapse Source: UniProtKB
  • postsynaptic density Source: UniProtKB
  • postsynaptic membrane Source: UniProtKB-SubCell
  • presynapse Source: UniProtKB
  • presynaptic membrane Source: UniProtKB-SubCell
  • ribonucleoprotein complex Source: UniProtKB
  • synapse Source: UniProtKB
  • viral replication complex 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

Involvement in diseasei

Fragile X syndrome (FRAX)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionCommon genetic disease (has a prevalence of one in every 2000 children) which is characterized by moderate to severe mental retardation, macroorchidism (enlargement of the testicles), large ears, prominent jaw, and high-pitched, jocular speech. The defect in most fragile X syndrome patients results from an amplification of a CGG repeat region which is directly in front of the coding region.
See also OMIM:300624
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti138 – 1381R → Q in FRAX; rare variant found in a developmentally delayed male; inhibits nucleosome binding; reduces interaction with KCNMB4; inhibits presynaptic action potential (AP) broadening; does not alter postsynaptic RNA-binding and polyribosome association. 3 Publications
VAR_064507
Natural varianti266 – 2661G → E in FRAX; reduces association with polyribosome; reduces RNA-binding. 1 Publication
VAR_075977
Natural varianti304 – 3041I → N in FRAX; alters protein folding and stability; increases nucleocytoplasmic shuttling; reduces localization in Cajal bodies; reduces the association with cytoplasmic granules; reduces association with polyribosome; reduces RNA-binding; attenuates mRNA translation repression; impairs homooligomerization; reduces interaction with TDRD3; reduces interaction with viral influenza A nucleoprotein (NP); does not inhibit interaction with SMN1, FXR1 and FXR2. 14 Publications
VAR_005234
Fragile X tremor/ataxia syndrome (FXTAS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionIn FXTAS, the expanded repeats range in size from 55 to 200 repeats and are referred to as 'premutations'. Full repeat expansions with greater than 200 repeats results in fragile X mental retardation syndrome [MIM:300624]. Carriers of the premutation typically do not show the full fragile X syndrome phenotype, but comprise a subgroup that may have some physical features of fragile X syndrome or mild cognitive and emotional problems.
See also OMIM:300623
Premature ovarian failure 1 (POF1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn ovarian disorder defined as the cessation of ovarian function under the age of 40 years. It is characterized by oligomenorrhea or amenorrhea, in the presence of elevated levels of serum gonadotropins and low estradiol.
See also OMIM:311360

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi102 – 1021T → A: Reduces binding to nucleosome. 1 Publication
Mutagenesisi103 – 1031Y → L: Reduces binding to nucleosome. 1 Publication
Mutagenesisi125 – 1262TF → AA: Alters the structural integrity of the N-terminus and leads to aggregation. 1 Publication
Mutagenesisi500 – 5001S → A: Loss of phosphorylation. Does not affect interaction with MCRS1. Does not affect localization to cytoplasmic granules. Does not affect association with polyribosome. 3 Publications
Mutagenesisi500 – 5001S → D: Does not affect RNA-binding to G-quadruplex structure. 1 Publication
Mutagenesisi527 – 5348RRGDGRRR → EEGDGEEE: Reduces nucleolar localization. Strongly reduces nucleolar localization; when associated with 613-E--E-617. 1 Publication
Mutagenesisi544 – 5441R → K: Reduces arginine methylation by 80%. 1 Publication
Mutagenesisi546 – 5461R → K: Slightly reduced methylation. 1 Publication
Mutagenesisi613 – 6175QKKEK → EEEEE: Reduces nucleolar localization. Strongly reduces nucleolar localization; when associated with 527-E--E-534. 1 Publication

Keywords - Diseasei

Disease mutation, Mental retardation, Premature ovarian failure

Organism-specific databases

MalaCardsiFMR1.
MIMi300623. phenotype.
300624. phenotype.
311360. phenotype.
616034. phenotype.
Orphaneti908. Fragile X syndrome.
93256. Fragile X-associated tremor/ataxia syndrome.
619. Primary ovarian failure.
261483. Xq27.3q28 duplication syndrome.
PharmGKBiPA28191.

Polymorphism and mutation databases

BioMutaiFMR1.
DMDMi544328.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 632632Synaptic functional regulator FMR1PRO_0000050102Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei337 – 3371PhosphoserineBy similarity
Modified residuei370 – 3701PhosphoserineCombined sources
Modified residuei463 – 4631PhosphothreonineBy similarity
Modified residuei500 – 5001PhosphoserineCombined sources1 Publication
Modified residuei544 – 5441Omega-N-methylarginine1 Publication
Modified residuei620 – 6201PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated (PubMed:14532325). Phosphorylated on several serine residues. Phosphorylation at Ser-500 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).By similarity1 Publication
Monoubiquitinated. Polyubiquitinated. Ubiquitinated and targeted for proteasomal degradation after activation of metabotropic glutamate receptor (mGluR).By similarity
Methylated; methylation is necessary for heterodimerization with FXR1, association with polyribosomes, recruitment into stress granules and translation of FMR1 target mRNAs (PubMed:16636078). Methylated by PRMT1, PRMT3 and PRMT4, in vitro (PubMed:16922515).2 Publications
Isoform 10: Undergoes proteolytic cleavage; may be specifically cleaved by calpain-1/CAPN1 in cajal bodies (PubMed:24204304).1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ06787.
MaxQBiQ06787.
PaxDbiQ06787.
PeptideAtlasiQ06787.
PRIDEiQ06787.

PTM databases

iPTMnetiQ06787.
PhosphoSiteiQ06787.

Expressioni

Tissue specificityi

Expressed in the brain, cerebellum and testis (PubMed:8401578). Also expressed in epithelial tissues (PubMed:8401578). Expressed in mature oligodendrocytes (OLGs) (PubMed:23891804). Expressed in fibroblast (PubMed:24204304). Expressed in neurons, Purkinje cells and spermatogonias (at protein level) (PubMed:8401578). Expressed in brain, testis and placenta (PubMed:8504300). Expressed in neurons and lymphocytes (PubMed:8504300).4 Publications

Inductioni

(Microbial infection) Up-regulated in response to infection by influenza A virus.1 Publication

Gene expression databases

BgeeiENSG00000102081.
CleanExiHS_FMR1.
ExpressionAtlasiQ06787. baseline and differential.
GenevisibleiQ06787. HS.

Organism-specific databases

HPAiCAB012444.
HPA050118.
HPA056084.

Interactioni

Subunit structurei

Homodimer (PubMed:7489725, PubMed:12950170, PubMed:16636078). Forms heterodimer with FXR1; heterodimerization occurs in a methylation-dependent manner (PubMed:7489725, PubMed:11157796, PubMed:16636078). Forms heterodimer with FXR2 (PubMed:7489725, PubMed:11157796). Homooligomer (PubMed:11157796, PubMed:18664458). 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 (By similarity). 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 (PubMed:14703574). Interacts with AGO2/EIF2C2 (PubMed:14703574). Interacts (via C-terminus) with CACNA1B; this interaction induces a deacrease in the number of presynaptic functional CACNA1B channels at the cell surface (By similarity). Interacts with CYFIP1; this interaction recruits CYFIP1 to capped mRNA (By similarity). Interacts with CYFIP2 (By similarity). Interacts with EIF5; this interaction occurs in a RNA-dependent manner (By similarity). Interacts with dynein (By similarity). Interacts with FXR1 and FXR2 (PubMed:8668200, PubMed:14532325, PubMed:15380484). Interacts with methylated histone H3 (PubMed:24813610). Interacts with IGF2BP1; this interaction allows to recruit IGF2BP1 to mRNA in a FMR1-dependent manner (PubMed:15282548). 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 phosphorylated form) with MCRS1 (via N-terminus) (PubMed:16571602). 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 (By similarity). Interacts with NCL (By similarity). Interacts with NUFIP1 (PubMed:10556305). Interacts (via N-terminus) with NUFIP2 (PubMed:12837692, PubMed:16407062). Interacts with NXF1; this interaction occurs in a mRNA-dependent and polyribosome-independent manner in the nucleus (PubMed:18936162). Interacts with NXF2 (via N-terminus); this interaction is direct and occurs in a NXF1 mRNA-containing mRNP complexes (By similarity). Interacts with RANBP9 (via C-terminus); this interaction is direct and inhibits binding of FMR1 to RNA homopolymer (PubMed:15381419). Interacts with RPLP0 (PubMed:15380484). Interacts (via C-terminus) with SMN (via C-terminus); this interaction is direct and occurs in a RNA-independent manner (PubMed:18093976). Interacts with TDRD3 (via C-terminus); this interaction is direct (PubMed:18632687, PubMed:18664458). Interacts with YBX1; this interaction occurs in association with polyribosome (By similarity). Interacts with nucleosome (PubMed:24813610). Associates with polyribosome; this association occurs in a mRNA-dependent manner (PubMed:9659908, PubMed:11719188, PubMed:12594214, PubMed:19097999, PubMed:24448548). Associates with cytoplasmic messenger ribonucleoprotein particles (mRNPs) (PubMed:7692601, PubMed:9659908, PubMed:12575950, PubMed:19097999). Associates with microtubules in a kinesin- and dynein-dependent manner (By similarity). Isoform 6 interacts (via N-terminus) with NCL (via C-terminus) (PubMed:24658146). Isoform 6 interacts with CYFIP2; this interaction occurs in a RNA-dependent manner (PubMed:24658146). Isoform 6 interacts with EIF5; this interaction occurs in a RNA-dependent manner (PubMed:24658146). Isoform 6 interacts with RPLP0 (PubMed:24658146).By similarity30 Publications
(Microbial infection) Interacts (via KH 2 domain) with influenza A nucleoprotein (NP); this interaction occurs in a RNA-dependent manner and stimulates viral ribonucleoprotein (vRNP) assembly and subsequent RNA synthesis.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CYFIP1Q7L5764EBI-366305,EBI-1048143
CYFIP2Q96F072EBI-366305,EBI-2433893
FSD2A1L4K13EBI-10224470,EBI-5661036
FXR2P511163EBI-10224470,EBI-740459

GO - Molecular functioni

  • dynein binding Source: UniProtKB
  • identical protein binding Source: UniProtKB
  • ion channel binding Source: UniProtKB
  • methylated histone binding Source: UniProtKB
  • microtubule binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • translation initiation factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108619. 55 interactions.
DIPiDIP-29022N.
DIP-29509N.
IntActiQ06787. 41 interactions.
MINTiMINT-108156.
STRINGi9606.ENSP00000359506.

Structurei

Secondary structure

1
632
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 95Combined sources
Beta strandi15 – 239Combined sources
Beta strandi25 – 328Combined sources
Helixi33 – 353Combined sources
Beta strandi40 – 434Combined sources
Helixi44 – 463Combined sources
Beta strandi64 – 696Combined sources
Beta strandi71 – 755Combined sources
Beta strandi78 – 8811Combined sources
Beta strandi91 – 977Combined sources
Helixi100 – 1034Combined sources
Beta strandi104 – 1085Combined sources
Helixi109 – 1113Combined sources
Beta strandi112 – 1143Combined sources
Turni123 – 1253Combined sources
Beta strandi127 – 1326Combined sources
Turni135 – 1384Combined sources
Helixi139 – 1413Combined sources
Helixi144 – 1474Combined sources
Helixi148 – 1547Combined sources
Beta strandi157 – 1626Combined sources
Turni163 – 1664Combined sources
Beta strandi167 – 1737Combined sources
Helixi177 – 19822Combined sources
Beta strandi220 – 2245Combined sources
Helixi227 – 2293Combined sources
Helixi230 – 2345Combined sources
Helixi236 – 2383Combined sources
Helixi239 – 2457Combined sources
Beta strandi250 – 2567Combined sources
Turni257 – 2604Combined sources
Beta strandi261 – 2688Combined sources
Helixi269 – 27911Combined sources
Beta strandi281 – 2899Combined sources
Helixi290 – 2923Combined sources
Helixi293 – 2975Combined sources
Helixi299 – 3013Combined sources
Helixi302 – 31110Combined sources
Beta strandi314 – 3218Combined sources
Beta strandi398 – 4069Combined sources
Helixi407 – 42216Combined sources
Beta strandi535 – 5384Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BKDNMR-N1-134[»]
2FMRNMR-A216-280[»]
2LA5NMR-B527-541[»]
2QNDX-ray1.90A/B216-425[»]
4OVAX-ray3.00A/B/C/D1-209[»]
4QVZX-ray3.20A/B1-213[»]
4QW2X-ray2.99A/B1-213[»]
5DE5X-ray3.00B/D528-544[»]
5DE8X-ray3.10B/D528-544[»]
5DEAX-ray2.80B/D528-544[»]
DisProtiDP00134.
ProteinModelPortaliQ06787.
SMRiQ06787. Positions 1-200, 216-334, 369-425.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ06787.

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 localizationBy similarityAdd
BLAST
Regioni172 – 21140Necessary for interaction with CYFIP1, CYFIP2, FXR1 and FXR2By similarity2 PublicationsAdd
BLAST
Regioni397 – 49195Required for nuclear export2 PublicationsAdd
BLAST
Regioni419 – 632214Interaction with RANBP91 PublicationAdd
BLAST
Regioni534 – 54815RNA-binding RGG-boxAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi424 – 44320Nuclear export signalBy similarityAdd
BLAST
Motifi527 – 5348Nucleolar localization signal 11 Publication
Motifi613 – 6175Nucleolar localization signal 21 Publication

Domaini

The N-terminal 134 amino acids are necessary for homodimerization and RNA-binding (PubMed:12950170). The N-terminal 298 amino acids are sufficient to interact with KCNMB4 and to regulate presynaptic action potential (AP) duration in neurons (PubMed:25561520). The two agenet-like domains are necessary for binding to histone H3 in a methylation-dependent manner (PubMed:24813610). The KH domains are necessary for mediating miRNA annealing to specific RNA targets (PubMed:17057366). The KH 2 domain is necessary for binding to kissing complex (kc) RNA ligands (PubMed:15805463). The RGG box domain is necessary for binding to mRNA targets that contain G-quadruplex structures (PubMed:11719189, PubMed:18579868, PubMed:25692235). 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 (PubMed:19166269). The RGG box domain is necessary for binding to its own mRNA (PubMed:11532944). The RGG-box domain is necessary for binding to homopolymer poly(G) (PubMed:14532325).11 Publications
Isoform 10: The C-terminal region contains a Cajal body localization signal at positions 490 through 506 (PubMed:24204304).1 Publication

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.
GeneTreeiENSGT00390000017033.
HOVERGENiHBG005739.
InParanoidiQ06787.
KOiK15516.
OMAiTKRANMM.
OrthoDBiEOG091G08EZ.
PhylomeDBiQ06787.
TreeFamiTF105427.

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. 1 hit.
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 (11)i

Sequence statusi: Complete.

This entry describes 11 isoformsi produced by alternative splicing. AlignAdd to basket

Note: At least 12 different isoforms are produced.
Isoform 6 (identifier: Q06787-1) [UniParc]FASTAAdd to basket

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 AFENNWQPDR QIPFHDVRFP
60 70 80 90 100
PPVGYNKDIN ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD
110 120 130 140 150
ATYNEIVTIE RLRSVNPNKP ATKDTFHKIK LDVPEDLRQM CAKEAAHKDF
160 170 180 190 200
KKAVGAFSVT YDPENYQLVI LSINEVTSKR AHMLIDMHFR SLRTKLSLIM
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 ENEKNVPQEE EIMPPNSLPS NNSRVGPNAP
360 370 380 390 400
EEKKHLDIKE NSTHFSQPNS TKVQRVLVAS SVVAGESQKP ELKAWQGMVP
410 420 430 440 450
FVFVGTKDSI ANATVLLDYH LNYLKEVDQL RLERLQIDEQ LRQIGASSRP
460 470 480 490 500
PPNRTDKEKS YVTDDGQGMG RGSRPYRNRG HGRRGPGYTS GTNSEASNAS
510 520 530 540 550
ETESDHRDEL SDWSLAPTEE ERESFLRRGD GRRRGGGGRG QGGRGRGGGF
560 570 580 590 600
KGNDDHSRTD NRPRNPREAK GRTTDGSLQI RVDCNNERSV HTKTLQNTSS
610 620 630
EGSRLRTGKD RNQKKEKPDS VDGQQPLVNG VP
Length:632
Mass (Da):71,174
Last modified:June 1, 1994 - v1
Checksum:iF853D6C82E3489B9
GO
Isoform 1 (identifier: Q06787-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     376-396: Missing.
     580-596: Missing.

Show »
Length:594
Mass (Da):66,971
Checksum:iBC65C14768EB268C
GO
Isoform 2 (identifier: Q06787-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     491-502: Missing.

Show »
Length:620
Mass (Da):70,025
Checksum:i8C8BC3876E1D92CA
GO
Isoform 3 (identifier: Q06787-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     491-502: Missing.
     580-596: Missing.

Show »
Length:603
Mass (Da):68,030
Checksum:iB8F3364E88A3489B
GO
Isoform 4 (identifier: Q06787-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     491-515: Missing.

Show »
Length:607
Mass (Da):68,455
Checksum:i561113CBB00CCAD0
GO
Isoform 5 (identifier: Q06787-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     491-515: Missing.
     580-596: Missing.

Show »
Length:590
Mass (Da):66,460
Checksum:i643FA1A3826879A3
GO
Isoform 7 (identifier: Q06787-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     580-596: Missing.

Show »
Length:615
Mass (Da):69,179
Checksum:iFE061178DA0A7ABB
GO
Isoform 8 (identifier: Q06787-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     376-396: Missing.
     491-515: Missing.

Show »
Length:586
Mass (Da):66,246
Checksum:iB413D4F8FA0D697F
GO
Isoform 9 (identifier: Q06787-9) [UniParc]FASTAAdd to basket
Also known as: B

The sequence of this isoform differs from the canonical sequence as follows:
     376-396: Missing.

Show »
Length:611
Mass (Da):68,966
Checksum:iE69936008EABA9D6
GO
Isoform 10 (identifier: Q06787-10) [UniParc]FASTAAdd to basket
Also known as: ISO61 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     426-632: EVDQLRLERL...GQQPLVNGVP → LQQRKRGRAS...QTAWMVSNHS

Show »
Length:537
Mass (Da):61,043
Checksum:i5E1324A8B0C34C26
GO
Isoform 11 (identifier: Q06787-11) [UniParc]FASTAAdd to basket
Also known as: ISO121 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     376-396: Missing.
     426-632: EVDQLRLERL...GQQPLVNGVP → LQQRKRGRAS...QTAWMVSNHS

Show »
Length:516
Mass (Da):58,835
Checksum:i3E95B836A3811D3C
GO

Sequence cautioni

The sequence AAA52458 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAA62466 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAA62467 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti294 – 2952Missing in AAA52458 (PubMed:1710175).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti138 – 1381R → Q in FRAX; rare variant found in a developmentally delayed male; inhibits nucleosome binding; reduces interaction with KCNMB4; inhibits presynaptic action potential (AP) broadening; does not alter postsynaptic RNA-binding and polyribosome association. 3 Publications
VAR_064507
Natural varianti145 – 1451A → S.
Corresponds to variant rs29281 [ dbSNP | Ensembl ].
VAR_029278
Natural varianti266 – 2661G → E in FRAX; reduces association with polyribosome; reduces RNA-binding. 1 Publication
VAR_075977
Natural varianti304 – 3041I → N in FRAX; alters protein folding and stability; increases nucleocytoplasmic shuttling; reduces localization in Cajal bodies; reduces the association with cytoplasmic granules; reduces association with polyribosome; reduces RNA-binding; attenuates mRNA translation repression; impairs homooligomerization; reduces interaction with TDRD3; reduces interaction with viral influenza A nucleoprotein (NP); does not inhibit interaction with SMN1, FXR1 and FXR2. 14 Publications
VAR_005234
Natural varianti546 – 5461R → H.1 Publication
VAR_005235

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei376 – 39621Missing in isoform 1, isoform 8, isoform 9 and isoform 11. 3 PublicationsVSP_002823Add
BLAST
Alternative sequencei426 – 632207EVDQL…VNGVP → LQQRKRGRASCAEETDGGVE GEEEDKEEEDVEEASKETTI TPEQIIVHVIQERLKEEQQM DPFRSELTAIMKGVSTLKHY RIPPVKVVGCARVKIVTRRK RSQTAWMVSNHS in isoform 10 and isoform 11. 1 PublicationVSP_058423Add
BLAST
Alternative sequencei491 – 51525Missing in isoform 4, isoform 5 and isoform 8. 1 PublicationVSP_002825Add
BLAST
Alternative sequencei491 – 50212Missing in isoform 2 and isoform 3. CuratedVSP_002824Add
BLAST
Alternative sequencei580 – 59617Missing in isoform 1, isoform 3, isoform 5 and isoform 7. CuratedVSP_002826Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L29074 Genomic DNA. Translation: AAB18828.1.
L29074 Genomic DNA. Translation: AAB18829.1.
L29074 Genomic DNA. Translation: AAB18830.1.
L29074 Genomic DNA. Translation: AAB18831.1.
L29074 Genomic DNA. Translation: AAB18832.1.
L29074 Genomic DNA. Translation: AAB18833.1.
KJ534836 mRNA. Translation: AHW56476.1.
CH471171 Genomic DNA. Translation: EAW61294.1.
CH471171 Genomic DNA. Translation: EAW61296.1.
CH471171 Genomic DNA. Translation: EAW61298.1.
CH471171 Genomic DNA. Translation: EAW61301.1.
CH471171 Genomic DNA. Translation: EAW61302.1.
CH471171 Genomic DNA. Translation: EAW61303.1.
BC086957 mRNA. Translation: AAH86957.1.
M67468 mRNA. Translation: AAA52458.1. Different initiation.
X69962 mRNA. Translation: CAA49586.1.
S65791 mRNA. Translation: AAB28395.2.
L19476 Genomic DNA. Translation: AAA62452.2.
L19477 Genomic DNA. Translation: AAA62453.1.
L19478 Genomic DNA. Translation: AAA62454.1.
L19479 Genomic DNA. Translation: AAA62455.1.
L19480 Genomic DNA. Translation: AAA62456.1.
L19481 Genomic DNA. Translation: AAA62457.1.
L19482 Genomic DNA. Translation: AAA62458.1.
L19483 Genomic DNA. Translation: AAA62459.1.
L19484 Genomic DNA. Translation: AAA62460.1.
L19485 Genomic DNA. Translation: AAA62461.1.
L19486 Genomic DNA. Translation: AAA62462.1.
L19487 Genomic DNA. Translation: AAA62463.1.
L19488 Genomic DNA. Translation: AAA62464.1.
L19489 Genomic DNA. Translation: AAA62465.1.
L19490 Genomic DNA. Translation: AAA62466.1. Sequence problems.
L19491 Genomic DNA. Translation: AAA62467.1. Sequence problems.
L19492 Genomic DNA. Translation: AAA62468.1.
L19493 Genomic DNA. Translation: AAA62469.1.
S76590 Genomic DNA. Translation: AAD14228.1.
CCDSiCCDS14682.1. [Q06787-1]
CCDS55519.1. [Q06787-9]
CCDS76039.1. [Q06787-8]
PIRiI68614.
S45243. A40724.
RefSeqiNP_001172004.1. NM_001185075.1.
NP_001172005.1. NM_001185076.1. [Q06787-9]
NP_001172010.1. NM_001185081.1.
NP_001172011.1. NM_001185082.1. [Q06787-8]
NP_002015.1. NM_002024.5. [Q06787-1]
UniGeneiHs.103183.

Genome annotation databases

EnsembliENST00000218200; ENSP00000218200; ENSG00000102081. [Q06787-9]
ENST00000370470; ENSP00000359501; ENSG00000102081. [Q06787-6]
ENST00000370471; ENSP00000359502; ENSG00000102081. [Q06787-10]
ENST00000370475; ENSP00000359506; ENSG00000102081. [Q06787-1]
ENST00000440235; ENSP00000413764; ENSG00000102081. [Q06787-8]
GeneIDi2332.
KEGGihsa:2332.
UCSCiuc004fck.5. human. [Q06787-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L29074 Genomic DNA. Translation: AAB18828.1.
L29074 Genomic DNA. Translation: AAB18829.1.
L29074 Genomic DNA. Translation: AAB18830.1.
L29074 Genomic DNA. Translation: AAB18831.1.
L29074 Genomic DNA. Translation: AAB18832.1.
L29074 Genomic DNA. Translation: AAB18833.1.
KJ534836 mRNA. Translation: AHW56476.1.
CH471171 Genomic DNA. Translation: EAW61294.1.
CH471171 Genomic DNA. Translation: EAW61296.1.
CH471171 Genomic DNA. Translation: EAW61298.1.
CH471171 Genomic DNA. Translation: EAW61301.1.
CH471171 Genomic DNA. Translation: EAW61302.1.
CH471171 Genomic DNA. Translation: EAW61303.1.
BC086957 mRNA. Translation: AAH86957.1.
M67468 mRNA. Translation: AAA52458.1. Different initiation.
X69962 mRNA. Translation: CAA49586.1.
S65791 mRNA. Translation: AAB28395.2.
L19476 Genomic DNA. Translation: AAA62452.2.
L19477 Genomic DNA. Translation: AAA62453.1.
L19478 Genomic DNA. Translation: AAA62454.1.
L19479 Genomic DNA. Translation: AAA62455.1.
L19480 Genomic DNA. Translation: AAA62456.1.
L19481 Genomic DNA. Translation: AAA62457.1.
L19482 Genomic DNA. Translation: AAA62458.1.
L19483 Genomic DNA. Translation: AAA62459.1.
L19484 Genomic DNA. Translation: AAA62460.1.
L19485 Genomic DNA. Translation: AAA62461.1.
L19486 Genomic DNA. Translation: AAA62462.1.
L19487 Genomic DNA. Translation: AAA62463.1.
L19488 Genomic DNA. Translation: AAA62464.1.
L19489 Genomic DNA. Translation: AAA62465.1.
L19490 Genomic DNA. Translation: AAA62466.1. Sequence problems.
L19491 Genomic DNA. Translation: AAA62467.1. Sequence problems.
L19492 Genomic DNA. Translation: AAA62468.1.
L19493 Genomic DNA. Translation: AAA62469.1.
S76590 Genomic DNA. Translation: AAD14228.1.
CCDSiCCDS14682.1. [Q06787-1]
CCDS55519.1. [Q06787-9]
CCDS76039.1. [Q06787-8]
PIRiI68614.
S45243. A40724.
RefSeqiNP_001172004.1. NM_001185075.1.
NP_001172005.1. NM_001185076.1. [Q06787-9]
NP_001172010.1. NM_001185081.1.
NP_001172011.1. NM_001185082.1. [Q06787-8]
NP_002015.1. NM_002024.5. [Q06787-1]
UniGeneiHs.103183.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BKDNMR-N1-134[»]
2FMRNMR-A216-280[»]
2LA5NMR-B527-541[»]
2QNDX-ray1.90A/B216-425[»]
4OVAX-ray3.00A/B/C/D1-209[»]
4QVZX-ray3.20A/B1-213[»]
4QW2X-ray2.99A/B1-213[»]
5DE5X-ray3.00B/D528-544[»]
5DE8X-ray3.10B/D528-544[»]
5DEAX-ray2.80B/D528-544[»]
DisProtiDP00134.
ProteinModelPortaliQ06787.
SMRiQ06787. Positions 1-200, 216-334, 369-425.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108619. 55 interactions.
DIPiDIP-29022N.
DIP-29509N.
IntActiQ06787. 41 interactions.
MINTiMINT-108156.
STRINGi9606.ENSP00000359506.

PTM databases

iPTMnetiQ06787.
PhosphoSiteiQ06787.

Polymorphism and mutation databases

BioMutaiFMR1.
DMDMi544328.

Proteomic databases

EPDiQ06787.
MaxQBiQ06787.
PaxDbiQ06787.
PeptideAtlasiQ06787.
PRIDEiQ06787.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000218200; ENSP00000218200; ENSG00000102081. [Q06787-9]
ENST00000370470; ENSP00000359501; ENSG00000102081. [Q06787-6]
ENST00000370471; ENSP00000359502; ENSG00000102081. [Q06787-10]
ENST00000370475; ENSP00000359506; ENSG00000102081. [Q06787-1]
ENST00000440235; ENSP00000413764; ENSG00000102081. [Q06787-8]
GeneIDi2332.
KEGGihsa:2332.
UCSCiuc004fck.5. human. [Q06787-1]

Organism-specific databases

CTDi2332.
GeneCardsiFMR1.
GeneReviewsiFMR1.
HGNCiHGNC:3775. FMR1.
HPAiCAB012444.
HPA050118.
HPA056084.
MalaCardsiFMR1.
MIMi300623. phenotype.
300624. phenotype.
309550. gene.
311360. phenotype.
616034. phenotype.
neXtProtiNX_Q06787.
Orphaneti908. Fragile X syndrome.
93256. Fragile X-associated tremor/ataxia syndrome.
619. Primary ovarian failure.
261483. Xq27.3q28 duplication syndrome.
PharmGKBiPA28191.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IF9J. Eukaryota.
ENOG410ZDJG. LUCA.
GeneTreeiENSGT00390000017033.
HOVERGENiHBG005739.
InParanoidiQ06787.
KOiK15516.
OMAiTKRANMM.
OrthoDBiEOG091G08EZ.
PhylomeDBiQ06787.
TreeFamiTF105427.

Miscellaneous databases

ChiTaRSiFMR1. human.
EvolutionaryTraceiQ06787.
GeneWikiiFMR1.
GenomeRNAii2332.
PROiQ06787.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000102081.
CleanExiHS_FMR1.
ExpressionAtlasiQ06787. baseline and differential.
GenevisibleiQ06787. HS.

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. 1 hit.
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...

Entry informationi

Entry nameiFMR1_HUMAN
AccessioniPrimary (citable) accession number: Q06787
Secondary accession number(s): A6NNH4
, D3DWT0, D3DWT1, D3DWT2, G8JL90, Q16578, Q5PQZ6, Q99054
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: September 7, 2016
This is version 180 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

The mechanism of the severe phenotype in the Asn-304 patient lies in the sequestration of bound mRNAs in nontranslatable mRNP particles. In the absence of FMRP, these same mRNAs may be partially translated via alternate mRNPs, although perhaps abnormally localized or regulated, resulting in typical fragile X syndrome. Asn-304 mutation maps to a position within the second KH domain of FMRP that is critical for stabilizing sequence-specific RNA-protein interactions. Asn-304 mutation abrogates the association of the FMRP KH 2 domain with its target, kissing complex RNA.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.