FMR1
entrez
2332
canonical
uniprot
Q06787
canonical
ensembl
ENSG00000102081
resolver
ensp
ENSP00000218200
resolver
ensp
ENSP00000359502
resolver
ensp
ENSP00000359506
resolver
ensp
ENSP00000413764
resolver
ensp
ENSP00000649926
resolver
genesymbol
FMR1
resolver
hgnc
HGNC:3775
resolver
uniprot
A6NNH4
resolver
uniprot
D3DWT0
resolver
uniprot
D3DWT1
resolver
uniprot
D3DWT2
resolver
uniprot
G8JL90
resolver
uniprot
Q16578
resolver
uniprot
Q5PQZ6
resolver
uniprot
Q99054
resolver
uniprot_entry
FMR1_HUMAN
resolver
uniprot_sec
A6NNH4
resolver
uniprot_sec
D3DWT0
resolver
uniprot_sec
D3DWT1
resolver
uniprot_sec
D3DWT2
resolver
uniprot_sec
G8JL90
resolver
uniprot_sec
Q16578
resolver
uniprot_sec
Q5PQZ6
resolver
uniprot_sec
Q99054
resolver
amino_acid_sequence
MEELVVEVRGSNGAFYKAFVKDVHEDSITVAFENNWQPDRQIPFHDVRFPPPVGYNKDINESDEVEVYSRANEKEPCCWWLAKVRMIKGEFYVIEYAACDATYNEIVTIERLRSVNPNKPATKDTFHKIKLDVPEDLRQMCAKEAAHKDFKKAVGAFSVTYDPENYQLVILSINEVTSKRAHMLIDMHFRSLRTKLSLIMRNEEASKQLESSRQLASRFHEQFIVREDLMGLAIGTHGANIQQARKVPGVTAIDLDEDTCTFHIYGEDQDAVKKARSFLEFAEDVIQVPRNLVGKVIGKNGKLIQEIVDKSGVVRVRIEAENEKNVPQEEEIMPPNSLPSNNSRVGPNAPEEKKHLDIKENSTHFSQPNSTKVQRVLVASSVVAGESQKPELKAWQGMVPFVFVGTKDSIANATVLLDYHLNYLKEVDQLRLERLQIDEQLRQIGASSRPPPNRTDKEKSYVTDDGQGMGRGSRPYRNRGHGRRGPGYTSGTNSEASNASETESDHRDELSDWSLAPTEEERESFLRRGDGRRRGGGGRGQGGRGRGGGFKGNDDHSRTDNRPRNPREAKGRTTDGSLQIRVDCNNERSVHTKTLQNTSSEGSRLRTGKDRNQKKEKPDSVDGQQPLVNGVP
uniprot
proteins
disease_involvement
DISEASE: Fragile X syndrome (FXS) [MIM:300624]: An X-linked dominant disease characterized by moderate to severe intellectual disability, macroorchidism (enlargement of the testicles), large ears, prominent jaw, and high-pitched, jocular speech. The defect in most patients results from an amplification of a CGG repeat region in the FMR1 gene and abnormal methylation. {ECO:0000269|PubMed:10196376, ECO:0000269|PubMed:11157796, ECO:0000269|PubMed:15380484, ECO:0000269|PubMed:15805463, ECO:0000269|PubMed:17850748, ECO:0000269|PubMed:18093976, ECO:0000269|PubMed:18664458, ECO:0000269|PubMed:23235829, ECO:0000269|PubMed:24204304, ECO:0000269|PubMed:24448548, ECO:0000269|PubMed:24514761, ECO:0000269|PubMed:24813610, ECO:0000269|PubMed:25561520, ECO:0000269|PubMed:39106863, ECO:0000269|PubMed:7633450, ECO:0000269|PubMed:7688265, ECO:0000269|PubMed:8156595, ECO:0000269|PubMed:8401578, ECO:0000269|PubMed:8490650, ECO:0000269|PubMed:9659908}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Fragile X tremor/ataxia syndrome (FXTAS) [MIM:300623]: An X-linked neurodegenerative disorder characterized by late-onset, progressive cerebellar ataxia and intention tremor followed by cognitive decline. {ECO:0000269|PubMed:11445641}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Premature ovarian failure 1 (POF1) [MIM:311360]: An 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. {ECO:0000269|PubMed:9719368}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: 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 target mRNAs (PubMed:12417522, PubMed:16631377, PubMed:18653529, PubMed:19166269, PubMed:23235829, PubMed:25464849). Acts as an mRNA regulator by mediating formation of some phase-separated membraneless compartment: undergoes liquid-liquid phase separation upon binding to target mRNAs, leading to assemble mRNAs into cytoplasmic ribonucleoprotein granules that concentrate mRNAs with associated regulatory factors (PubMed:12417522, PubMed:30765518, PubMed:31439799). Plays a role in the alternative splicing of its own mRNA (PubMed:18653529). 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). Undergoes liquid-liquid phase separation following phosphorylation and interaction with CAPRIN1, promoting formation of cytoplasmic ribonucleoprotein granules that concentrate mRNAs with factors that inhibit translation and mediate deadenylation of target mRNAs (PubMed:31439799). Acts as a repressor of mRNA translation in synaptic regions by mediating formation of neuronal ribonucleoprotein granules and promoting recruitmtent of EIF4EBP2 (PubMed:30765518). Plays a role as a repressor of mRNA translation during the transport of dendritic mRNAs to postsynaptic dendritic spines (PubMed:11157796, PubMed:11532944, 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). Also plays 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:11157796, PubMed:11719189, PubMed:12594214, PubMed:17417632, PubMed:23235829, PubMed:24448548, PubMed:7692601). 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:11532944, PubMed:12594214, PubMed:15282548, PubMed:18653529, PubMed:7692601). Also binds 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). Plays a role in mRNA nuclear export (PubMed:31753916). Specifically recognizes and binds a subset of N6-methyladenosine (m6A)-containing mRNAs, promoting their nuclear export in a XPO1/CRM1-dependent manner (PubMed:31753916). Together with export factor NXF2, is involved in the regulation of the NXF1 mRNA stability in neurons (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 homomer; preferentially on poly(G) and to a lesser extent on poly(U), but not on poly(A) or poly(C) (PubMed:12950170, PubMed:15381419, PubMed:7688265, PubMed:7781595, 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 proteasomal degradation (By similarity). Plays a role in regulation of MAP1B-dependent microtubule dynamics during neuronal development (By similarity). 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). 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 (PubMed:24813610). Forms a cytoplasmic messenger ribonucleoprotein (mRNP) network by packaging long mRNAs, serving as a scaffold that recruits proteins and signaling molecules. This network facilitates signaling reactions by maintaining proximity between kinases and substrates (PubMed:39106863). {ECO:0000250|UniProtKB:P35922, ECO:0000250|UniProtKB:Q80WE1, ECO:0000269|PubMed:11157796, ECO:0000269|PubMed:11532944, ECO:0000269|PubMed:11719189, ECO:0000269|PubMed:12417522, ECO:0000269|PubMed:12594214, ECO:0000269|PubMed:12927206, ECO:0000269|PubMed:12950170, ECO:0000269|PubMed:14703574, ECO:0000269|PubMed:15282548, ECO:0000269|PubMed:15381419, ECO:0000269|PubMed:15805463, ECO:0000269|PubMed:16631377, ECO:0000269|PubMed:17057366, ECO:0000269|PubMed:17417632, ECO:0000269|PubMed:18579868, ECO:0000269|PubMed:18653529, ECO:0000269|PubMed:18936162, ECO:0000269|PubMed:19097999, ECO:0000269|PubMed:19166269, ECO:0000269|PubMed:20512134, ECO:0000269|PubMed:23235829, ECO:0000269|PubMed:23891804, ECO:0000269|PubMed:24448548, ECO:0000269|PubMed:24813610, ECO:0000269|PubMed:25464849, ECO:0000269|PubMed:25561520, ECO:0000269|PubMed:25692235, ECO:0000269|PubMed:30765518, ECO:0000269|PubMed:31439799, ECO:0000269|PubMed:31753916, ECO:0000269|PubMed:39106863, ECO:0000269|PubMed:7688265, ECO:0000269|PubMed:7692601, ECO:0000269|PubMed:7781595, ECO:0000269|PubMed:8156595}.; FUNCTION: [Isoform 10]: Binds to RNA homomer; 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). {ECO:0000269|PubMed:24204304}.; FUNCTION: [Isoform 6]: Binds to RNA homomer; 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). {ECO:0000269|PubMed:24204304}.; FUNCTION: (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. {ECO:0000269|PubMed:24514761}.
uniprot
proteins
mass_dalton
71174
uniprot
proteins
mutagenesis
MUTAGEN 102; /note="T->A: Reduces binding to nucleosome."; /evidence="ECO:0000269|PubMed:24813610"; MUTAGEN 103; /note="Y->L: Reduces binding to nucleosome."; /evidence="ECO:0000269|PubMed:24813610"; MUTAGEN 125..126; /note="TF->AA: Alters the structural integrity of the N-terminus and leads to aggregation."; /evidence="ECO:0000269|PubMed:16407062"; MUTAGEN 500; /note="S->A: Loss of phosphorylation. Does not affect interaction with MCRS1. Does not affect localization to cytoplasmic granules. Does not affect association with polyribosome."; /evidence="ECO:0000269|PubMed:12446764, ECO:0000269|PubMed:14532325, ECO:0000269|PubMed:16571602"; MUTAGEN 500; /note="S->D: Does not affect RNA-binding to G-quadruplex structure."; /evidence="ECO:0000269|PubMed:25692235"; MUTAGEN 527..534; /note="RRGDGRRR->EEGDGEEE: Reduces nucleolar localization. Strongly reduces nucleolar localization; when associated with 613-E--E-617."; /evidence="ECO:0000269|PubMed:24658146"; MUTAGEN 544; /note="R->K: Reduces arginine methylation by 80%."; /evidence="ECO:0000269|PubMed:16922515"; MUTAGEN 546; /note="R->K: Slightly reduced methylation."; /evidence="ECO:0000269|PubMed:16922515"; MUTAGEN 613..617; /note="QKKEK->EEEEE: Reduces nucleolar localization. Strongly reduces nucleolar localization; when associated with 527-E--E-534."; /evidence="ECO:0000269|PubMed:24658146
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on several serine residues (PubMed:14532325). Phosphorylation by casein kinase II (CK2) promotes interaction with CAPRIN1 and liquid-liquid phase separation (LLPS) for the formation of a membraneless compartment that concentrates mRNAs with associated regulatory factors (PubMed:30765518, PubMed:31439799). Phosphorylation at Ser-500 by CK2 promotes secondary phosphorylation of other nearby serine residues (By similarity). Phosphorylation has no effect on the binding of individual mRNA species (By similarity). Unphosphorylated FMR1 is associated with actively translating polyribosome, whereas a fraction of phosphorylated FMR1 is associated with apparently stalled polyribosome (By similarity). Dephosphorylation by an activated phosphatase may release the FMR1-mediated translational repression and allow synthesis of a locally required protein at synapses (By similarity). {ECO:0000250|UniProtKB:P35922, ECO:0000269|PubMed:14532325, ECO:0000269|PubMed:30765518, ECO:0000269|PubMed:31439799}.; PTM: Monoubiquitinated. Polyubiquitinated. Ubiquitinated and targeted for proteasomal degradation after activation of metabotropic glutamate receptor (mGluR). {ECO:0000250|UniProtKB:P35922}.; PTM: Monomethylated and asymmetrically dimethylated by PRMT1, PRMT3 and PRMT4 at four arginine residues of the arginine-glycine-glycine box (PubMed:16922515, PubMed:30765518). Methylation decreases ability to undergo liquid-liquid phase separation (LLPS) for the formation of a membraneless compartment (PubMed:30765518). Methylation does not affect mRNA-binding (PubMed:30765518). Methylation is necessary for heterodimerization with FXR1, association with polyribosomes, recruitment into stress granules and translation of FMR1 target mRNAs (PubMed:16636078). {ECO:0000269|PubMed:16636078, ECO:0000269|PubMed:16922515, ECO:0000269|PubMed:30765518}.; PTM: [Isoform 10]: Undergoes proteolytic cleavage; may be specifically cleaved by calpain-1/CAPN1 in cajal bodies (PubMed:24204304). {ECO:0000269|PubMed:24204304}.
uniprot
proteins
protein_family
FMR1 family
uniprot
proteins
pubmed
10196376
uniprot
proteins
pubmed
10556305
uniprot
proteins
pubmed
11157796
uniprot
proteins
pubmed
11445641
uniprot
proteins
pubmed
11532944
uniprot
proteins
pubmed
11719188
uniprot
proteins
pubmed
11719189
uniprot
proteins
pubmed
12417522
uniprot
proteins
pubmed
12417734
uniprot
proteins
pubmed
12446764
uniprot
proteins
pubmed
12575950
uniprot
proteins
pubmed
12594214
uniprot
proteins
pubmed
12837692
uniprot
proteins
pubmed
12927206
uniprot
proteins
pubmed
12950170
uniprot
proteins
pubmed
14508492
uniprot
proteins
pubmed
14532325
uniprot
proteins
pubmed
14703574
uniprot
proteins
pubmed
15282548
uniprot
proteins
pubmed
15380484
uniprot
proteins
pubmed
15381419
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
15805463
uniprot
proteins
pubmed
16407062
uniprot
proteins
pubmed
16571602
uniprot
proteins
pubmed
16631377
uniprot
proteins
pubmed
16636078
uniprot
proteins
pubmed
16922515
uniprot
proteins
pubmed
17057366
uniprot
proteins
pubmed
1710175
uniprot
proteins
pubmed
17417632
uniprot
proteins
pubmed
17850748
uniprot
proteins
pubmed
18093976
uniprot
proteins
pubmed
18579868
uniprot
proteins
pubmed
18632687
uniprot
proteins
pubmed
18653529
uniprot
proteins
pubmed
18664458
uniprot
proteins
pubmed
18936162
uniprot
proteins
pubmed
19097999
uniprot
proteins
pubmed
19166269
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20512134
uniprot
proteins
pubmed
20799337
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21771594
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23235829
uniprot
proteins
pubmed
23891804
uniprot
proteins
pubmed
24204304
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24448548
uniprot
proteins
pubmed
24514761
uniprot
proteins
pubmed
24658146
uniprot
proteins
pubmed
24722188
uniprot
proteins
pubmed
24813610
uniprot
proteins
pubmed
25464849
uniprot
proteins
pubmed
25561520
uniprot
proteins
pubmed
25692235
uniprot
proteins
pubmed
27509095
uniprot
proteins
pubmed
30765518
uniprot
proteins
pubmed
31439799
uniprot
proteins
pubmed
31753916
uniprot
proteins
pubmed
39106863
uniprot
proteins
pubmed
7489725
uniprot
proteins
pubmed
7633450
uniprot
proteins
pubmed
7688265
uniprot
proteins
pubmed
7692601
uniprot
proteins
pubmed
7781595
uniprot
proteins
pubmed
7825604
uniprot
proteins
pubmed
8069329
uniprot
proteins
pubmed
8156595
uniprot
proteins
pubmed
8401496
uniprot
proteins
pubmed
8401531
uniprot
proteins
pubmed
8401578
uniprot
proteins
pubmed
8490650
uniprot
proteins
pubmed
8504300
uniprot
proteins
pubmed
8515814
uniprot
proteins
pubmed
8668200
uniprot
proteins
pubmed
8789445
uniprot
proteins
pubmed
9259278
uniprot
proteins
pubmed
9302998
uniprot
proteins
pubmed
9375856
uniprot
proteins
pubmed
9659908
uniprot
proteins
pubmed
9719368
uniprot
proteins
sequence_length
632
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:12417734, ECO:0000269|PubMed:14532325, ECO:0000269|PubMed:15380484, ECO:0000269|PubMed:16636078, ECO:0000269|PubMed:18093976, ECO:0000269|PubMed:30765518, ECO:0000269|PubMed:31439799, ECO:0000269|PubMed:39106863, ECO:0000269|PubMed:9659908}. Cytoplasm, Stress granule {ECO:0000269|PubMed:12417522, ECO:0000269|PubMed:16636078, ECO:0000269|PubMed:18632687, ECO:0000269|PubMed:18664458}. Cytoplasm {ECO:0000269|PubMed:10196376, ECO:0000269|PubMed:12837692, ECO:0000269|PubMed:18664458, ECO:0000269|PubMed:18936162, ECO:0000269|PubMed:7781595, ECO:0000269|PubMed:8401578, ECO:0000269|PubMed:8515814, ECO:0000269|PubMed:9259278}. Perikaryon {ECO:0000269|PubMed:12417734, ECO:0000269|PubMed:15380484, ECO:0000269|PubMed:18093976}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:24658146}. Cell projection, neuron projection {ECO:0000269|PubMed:12417734, ECO:0000269|PubMed:15380484, ECO:0000269|PubMed:18093976}. Cell projection, axon {ECO:0000250|UniProtKB:P35922}. Cell projection, dendrite {ECO:0000250|UniProtKB:P35922}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:P35922}. Synapse, synaptosome {ECO:0000250|UniProtKB:P35922}. Cell projection, growth cone {ECO:0000269|PubMed:15380484}. Cell projection, filopodium tip {ECO:0000250|UniProtKB:P35922}. Synapse {ECO:0000250|UniProtKB:P35922}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P35922}. Presynaptic cell membrane {ECO:0000250|UniProtKB:P35922}. Nucleus {ECO:0000269|PubMed:10196376, ECO:0000269|PubMed:16571602, ECO:0000269|PubMed:18936162, ECO:0000269|PubMed:31753916}. Nucleus, nucleolus {ECO:0000269|PubMed:12837692, ECO:0000269|PubMed:16407062, ECO:0000269|PubMed:16571602, ECO:0000269|PubMed:24658146}. Chromosome, centromere {ECO:0000250|UniProtKB:P35922}. Chromosome {ECO:0000250|UniProtKB:P35922}. Cell membrane {ECO:0000250|UniProtKB:P35922}. Note=Mediates formation and localizes to cytoplasmic ribonucleoprotein membraneless compartments (PubMed:30765518, PubMed:31439799). Localizes to cytoplasmic ribonucleoprotein granules, also referred to as messenger ribonucleoprotein particles or mRNPs, along dendrites and dendritic spines (PubMed:14532325, PubMed:9659908). FMR1-containing cytoplasmic granules colocalize to F-actin-rich structures, including filopodium, spines and growth cone during the development of hippocampal neurons (By similarity). FMR1-containing cytoplasmic granules are transported out of the soma along axon and dendrite to synaptic contacts in a microtubule- and kinesin-dependent manner (PubMed:12417734, PubMed:15380484). Colocalizes with FXR1 and FXR2 in discrete granules, called fragile X granules (FXGs), along axon and presynaptic compartments (By similarity). Colocalizes with TDRD3 in cytoplasmic stress granules (SGs) in response to various cellular stress (PubMed:16636078, PubMed:18632687, PubMed:18664458). Colocalizes with FXR1, kinesin, 60S acidic ribosomal protein RPLP0 and SMN in cytoplasmic granules in the soma and neurite cell processes (PubMed:12417734, PubMed:16636078, PubMed:18093976). Colocalizes with H2AX/H2A.x in pericentromeric heterochromatin in response to DNA damaging agents (By similarity). Localizes on meiotic pachytene-stage chromosomes (By similarity). Forms nuclear foci representing sites of ongoing DNA replication in response to DNA damaging agents (By similarity). Shuttles between nucleus and cytoplasm in a XPO1/CRM1-dependent manner (PubMed:10196376). Colocalizes with CACNA1B in the cytoplasm and at the cell membrane of neurons (By similarity). Colocalizes with CYFIP1, CYFIP2, NXF2 and ribosomes in the perinuclear region (By similarity). Colocalizes with CYFIP1 and EIF4E in dendrites and probably at synapses (By similarity). {ECO:0000250|UniProtKB:P35922, ECO:0000250|UniProtKB:Q80WE1, ECO:0000269|PubMed:10196376, ECO:0000269|PubMed:12417734, ECO:0000269|PubMed:14532325, ECO:0000269|PubMed:15380484, ECO:0000269|PubMed:16636078, ECO:0000269|PubMed:18093976, ECO:0000269|PubMed:18632687, ECO:0000269|PubMed:18664458, ECO:0000269|PubMed:30765518, ECO:0000269|PubMed:31439799, ECO:0000269|PubMed:9659908}.; SUBCELLULAR LOCATION: [Isoform 6]: Cytoplasm {ECO:0000269|PubMed:24204304, ECO:0000269|PubMed:8789445}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:24204304}.; SUBCELLULAR LOCATION: [Isoform 9]: Cytoplasm {ECO:0000269|PubMed:24204304, ECO:0000269|PubMed:8789445}.; SUBCELLULAR LOCATION: [Isoform 10]: Nucleus {ECO:0000269|PubMed:8789445}. Nucleus, Cajal body {ECO:0000269|PubMed:24204304}. Note=Colocalizes with Colin and SMN in Cajal bodies (PubMed:24204304).; SUBCELLULAR LOCATION: [Isoform 11]: Nucleus {ECO:0000269|PubMed:8789445}. Nucleus, Cajal body {ECO:0000269|PubMed:24204304}.
uniprot
proteins