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Synaptic functional regulator FMR1 (Fragile X mental retardation protein 1 homolog) (FMRP) (Protein FMR-1)

 FMR1_RAT                Reviewed;         593 AA.
Q80WE1; P70568;
01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
01-JUL-2008, sequence version 2.
22-NOV-2017, entry version 108.
RecName: Full=Synaptic functional regulator FMR1 {ECO:0000305};
AltName: Full=Fragile X mental retardation protein 1 homolog {ECO:0000312|RGD:2623};
Short=FMRP {ECO:0000303|Ref.1};
Short=Protein FMR-1 {ECO:0000250|UniProtKB:Q06787};
Name=Fmr1 {ECO:0000312|RGD:2623};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=Sprague-Dawley;
Rackham O., Brown C.M.;
"Messenger RNA encoding FMRP isoform 18 from the rat hippocampus.";
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 42-587 (ISOFORM 1).
STRAIN=Wistar; TISSUE=Brain;
Huang T., Ji H., Sittler A., Shen Y., Mandel J., Wu G.;
"Cloning of rat FMR1 gene.";
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
[3]
SUBCELLULAR LOCATION, AND ASSOCIATION WITH POLYRIBOSOME.
PubMed=9030614;
Feng Y., Gutekunst C.A., Eberhart D.E., Yi H., Warren S.T.,
Hersch S.M.;
"Fragile X mental retardation protein: nucleocytoplasmic shuttling and
association with somatodendritic ribosomes.";
J. Neurosci. 17:1539-1547(1997).
[4]
FUNCTION, SUBCELLULAR LOCATION, ASSOCIATION WITH POLYRIBOSOME, AND
INDUCTION.
PubMed=9144248; DOI=10.1073/pnas.94.10.5395;
Weiler I.J., Irwin S.A., Klintsova A.Y., Spencer C.M., Brazelton A.D.,
Miyashiro K., Comery T.A., Patel B., Eberwine J., Greenough W.T.;
"Fragile X mental retardation protein is translated near synapses in
response to neurotransmitter activation.";
Proc. Natl. Acad. Sci. U.S.A. 94:5395-5400(1997).
[5]
SUBCELLULAR LOCATION, ASSOCIATION WITH POLYRIBOSOME, AND TISSUE
SPECIFICITY.
PubMed=14613971; DOI=10.1093/hmg/ddh009;
Wang H., Ku L., Osterhout D.J., Li W., Ahmadian A., Liang Z., Feng Y.;
"Developmentally-programmed FMRP expression in oligodendrocytes: a
potential role of FMRP in regulating translation in oligodendroglia
progenitors.";
Hum. Mol. Genet. 13:79-89(2004).
[6]
SUBCELLULAR LOCATION.
PubMed=15028757; DOI=10.1523/JNEUROSCI.0099-04.2004;
Antar L.N., Afroz R., Dictenberg J.B., Carroll R.C., Bassell G.J.;
"Metabotropic glutamate receptor activation regulates fragile x mental
retardation protein and FMR1 mRNA localization differentially in
dendrites and at synapses.";
J. Neurosci. 24:2648-2655(2004).
[7]
SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=15564573; DOI=10.1523/JNEUROSCI.2185-04.2004;
Gabel L.A., Won S., Kawai H., McKinney M., Tartakoff A.M.,
Fallon J.R.;
"Visual experience regulates transient expression and dendritic
localization of fragile X mental retardation protein.";
J. Neurosci. 24:10579-10583(2004).
[8]
SUBCELLULAR LOCATION.
PubMed=16098134; DOI=10.1111/j.1601-183X.2005.00128.x;
Antar L.N., Dictenberg J.B., Plociniak M., Afroz R., Bassell G.J.;
"Localization of FMRP-associated mRNA granules and requirement of
microtubules for activity-dependent trafficking in hippocampal
neurons.";
Genes Brain Behav. 4:350-359(2005).
[9]
SUBCELLULAR LOCATION, ASSOCIATION WITH POLYRIBOSOME, AND ASSOCIATION
WITH MRNP.
PubMed=16571602; DOI=10.1093/hmg/ddl074;
Davidovic L., Bechara E., Gravel M., Jaglin X.H., Tremblay S., Sik A.,
Bardoni B., Khandjian E.W.;
"The nuclear microspherule protein 58 is a novel RNA-binding protein
that interacts with fragile X mental retardation protein in
polyribosomal mRNPs from neurons.";
Hum. Mol. Genet. 15:1525-1538(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336; SER-337; SER-347;
SER-349 AND SER-350, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=16641100; DOI=10.1073/pnas.0600895103;
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
regulation of aquaporin-2 phosphorylation at two sites.";
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
[11]
INTERACTION WITH KCNT1.
PubMed=20512134; DOI=10.1038/nn.2563;
Brown M.R., Kronengold J., Gazula V.R., Chen Y., Strumbos J.G.,
Sigworth F.J., Navaratnam D., Kaczmarek L.K.;
"Fragile X mental retardation protein controls gating of the sodium-
activated potassium channel Slack.";
Nat. Neurosci. 13:819-821(2010).
[12]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=23891804; DOI=10.1016/j.mcn.2013.07.009;
Giampetruzzi A., Carson J.H., Barbarese E.;
"FMRP and myelin protein expression in oligodendrocytes.";
Mol. Cell. Neurosci. 56:333-341(2013).
[13]
FUNCTION, INTERACTION WITH CACNA1B, AND SUBCELLULAR LOCATION.
PubMed=24709664; DOI=10.1038/ncomms4628;
Ferron L., Nieto-Rostro M., Cassidy J.S., Dolphin A.C.;
"Fragile X mental retardation protein controls synaptic vesicle
exocytosis by modulating N-type calcium channel density.";
Nat. Commun. 5:3628-3628(2014).
-!- 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 a subset of mRNAs
(PubMed:9144248). Plays a role in the alternative splicing of its
own mRNA (By similarity). 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:9144248).
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 (By similarity). 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 (By
similarity). Facilitates the assembly of miRNAs on specific target
mRNAs (By similarity). Plays also a role as an activator of mRNA
translation of a subset of dendritic mRNAs at synapses (By
similarity). 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 (By similarity). Binds to 5'-ACU[GU]-3'
and/or 5'-[AU]GGA-3' RNA consensus sequences within mRNA targets,
mainly at coding sequence (CDS) and 3'-untranslated region (UTR)
and less frequently at 5'-UTR (By similarity). Binds to
intramolecular G-quadruplex structures in the 5'- or 3'-UTRs of
mRNA targets (By similarity). Binds to G-quadruplex structures in
the 3'-UTR of its own mRNA (By similarity). Binds also to RNA
ligands harboring a kissing complex (kc) structure; this binding
may mediate the association of FMR1 with polyribosomes (By
similarity). Binds mRNAs containing U-rich target sequences (By
similarity). Binds to a triple stem-loop RNA structure, called
Sod1 stem loop interacting with FMRP (SoSLIP), in the 5'-UTR
region of superoxide dismutase SOD1 mRNA (By similarity). 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 (By
similarity). May associate with nascent transcripts in a nuclear
protein NXF1-dependent manner (By similarity). In vitro, binds to
RNA homopolymer; preferentially on poly(G) and to a lesser extent
on poly(U), but not on poly(A) or poly(C) (By similarity).
Moreover, plays a role in the modulation of the sodium-activated
potassium channel KCNT1 gating activity (By similarity).
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
(PubMed:24709664). 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 (By
similarity). 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 (By similarity). {ECO:0000250|UniProtKB:P35922,
ECO:0000250|UniProtKB:Q06787, ECO:0000269|PubMed:24709664,
ECO:0000269|PubMed:9144248}.
-!- SUBUNIT: Homodimer (By similarity). Forms heterodimer with FXR1;
heterodimerization occurs in a methylation-dependent manner (By
similarity). Forms heterodimer with FXR2 (By similarity).
Homooligomer (By similarity). Component of the CYFIP1-EIF4E-FMR1
complex at least composed of CYFIP, EIF4E and FMR1; this mRNA cap
binding complex formation increases in presence of the brain
cytoplasmic RNA BC1 and is dynamically regulated in an activity-
dependent manner to repress and then possibly release dendritic
mRNAs for translation in response to mGluR stimulation (By
similarity). Associates with the SMN core complex that contains
SMN, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7,
GEMIN8 and STRAP/UNRIP (By similarity). Part of a
ribonucleoprotein complex with AGO2/EIF2C2 and miRNAs (By
similarity). Interacts with AGO2/EIF2C2 (By similarity). Interacts
(via C-terminus) with CACNA1B; this interaction induces a
deacrease in the number of presynaptic functional CACNA1B channels
at the cell surface (PubMed:24709664). Interacts with CYFIP1; this
interaction recruits CYFIP1 to capped mRNA. 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 (By similarity).
Interacts with methylated histone H3 (By similarity). Interacts
with IGF2BP1; this interaction allows to recruit IGF2BP1 to mRNA
in a FMR1-dependent manner (By similarity). Interacts (via N-
terminus) with KCNMB4 (By similarity). Interacts with KCNT1 (via
C-terminus); this interaction alters gating properties of KCNT1
(PubMed:20512134). Interacts (via C-terminus) with KIF5A; this
interaction is increased in a mGluR-dependent manner (By
similarity). Interacts (via phosphorylated form) with MCRS1 (via
N-terminus) (By similarity). Interacts with MOV10; this
interaction is direct, occurs in an RNA-dependent manner on
polysomes and induces association of MOV10 with RNAs (By
similarity). Interacts with MYO5A and PURA; these interactions
occur in association with polyribosome (By similarity). Interacts
with NCL (By similarity). Interacts with NUFIP1 (By similarity).
Interacts (via N-terminus) with NUFIP2 (By similarity). Interacts
with NXF1; this interaction occurs in a mRNA-dependent and
polyribosome-independent manner in the nucleus (By similarity).
Interacts with NXF2 (via N-terminus); this interaction is direct
and occurs in a NXF1 mRNA-containing mRNP complexes (By
similarity). Interacts with RANBP9; this interaction is direct and
inhibits binding of FMR1 to RNA homopolymer (By similarity).
Interacts with RPLP0 (By similarity). Interacts (via C-terminus)
with SMN (via C-terminus); this interaction is direct and occurs
in a RNA-independent manner (By similarity). Interacts with TDRD3
(via C-terminus); this interaction is direct (By similarity).
Interacts with YBX1; this interaction occurs in association with
polyribosome (By similarity). Interacts with nucleosome (By
similarity). Associates with polyribosome; this association occurs
in a mRNA-dependent manner (PubMed:9030614, PubMed:9144248,
PubMed:14613971, PubMed:16571602). Associates with messenger
ribonucleoprotein particles (mRNPs) (PubMed:16571602). Associates
with microtubules in a kinesin- and dynein-dependent manner (By
similarity). Interacts with HABP4 (By similarity).
{ECO:0000250|UniProtKB:P35922, ECO:0000250|UniProtKB:Q06787,
ECO:0000269|PubMed:14613971, ECO:0000269|PubMed:16571602,
ECO:0000269|PubMed:20512134, ECO:0000269|PubMed:24709664,
ECO:0000269|PubMed:9030614, ECO:0000269|PubMed:9144248}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9030614}.
Nucleus, nucleolus {ECO:0000250|UniProtKB:Q06787}. Chromosome,
centromere {ECO:0000250|UniProtKB:P35922}. Chromosome
{ECO:0000250|UniProtKB:P35922}. Cytoplasm
{ECO:0000250|UniProtKB:P35922}. Cytoplasm, perinuclear region
{ECO:0000250|UniProtKB:P35922}. Perikaryon
{ECO:0000269|PubMed:14613971, ECO:0000269|PubMed:15028757,
ECO:0000269|PubMed:15564573, ECO:0000269|PubMed:16571602,
ECO:0000269|PubMed:24709664, ECO:0000269|PubMed:9030614,
ECO:0000269|PubMed:9144248}. Cytoplasmic granule
{ECO:0000269|PubMed:15028757, ECO:0000269|PubMed:16098134,
ECO:0000269|PubMed:23891804}. Cell projection
{ECO:0000269|PubMed:14613971, ECO:0000269|PubMed:24709664}. Cell
projection, dendrite {ECO:0000269|PubMed:15028757,
ECO:0000269|PubMed:15564573, ECO:0000269|PubMed:16571602,
ECO:0000269|PubMed:9030614, ECO:0000269|PubMed:9144248}. Cell
projection, dendritic spine {ECO:0000269|PubMed:15028757,
ECO:0000269|PubMed:16098134, ECO:0000269|PubMed:9030614,
ECO:0000269|PubMed:9144248}. Cell projection, growth cone
{ECO:0000269|PubMed:16098134}. Cell projection, filopodium
{ECO:0000269|PubMed:16098134}. Cell projection, filopodium tip
{ECO:0000250|UniProtKB:P35922}. Cell projection, axon
{ECO:0000269|PubMed:9030614}. Cell junction, synapse
{ECO:0000269|PubMed:15028757}. Cell junction, synapse, synaptosome
{ECO:0000269|PubMed:15564573, ECO:0000269|PubMed:9030614,
ECO:0000269|PubMed:9144248}. Cell junction, synapse, postsynaptic
cell membrane, postsynaptic density {ECO:0000269|PubMed:9144248}.
Cell junction, synapse, presynaptic cell membrane
{ECO:0000250|UniProtKB:P35922}. Cell membrane
{ECO:0000250|UniProtKB:P35922}. Note=Colocalizes with H2AFX/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 (By similarity). Localizes to
cytoplasmic granules, also referred to as messenger
ribonucleoprotein particles or mRNPs, along dendrites and
dendritic spines (PubMed:15028757, PubMed:23891804). FMR1-
containing cytoplasmic granules colocalize to F-actin-rich
structures, including filopodium, spines and growth cone during
the development of hippocampal neurons (PubMed:16098134). 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:16098134). 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).
Colocalizes with FXR1, kinesin, 60S acidic ribosomal protein RPLP0
and SMN in cytoplasmic granules in the soma and neurite cell
processes (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:P35922,
ECO:0000250|UniProtKB:Q06787, ECO:0000269|PubMed:15028757,
ECO:0000269|PubMed:16098134, ECO:0000269|PubMed:23891804}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q80WE1-1; Sequence=Displayed;
Name=2; Synonyms=18;
IsoId=Q80WE1-2; Sequence=VSP_034393;
-!- TISSUE SPECIFICITY: Expressed in brain (PubMed:9030614). Expressed
in neurons (PubMed:9030614). Expressed in mature oligodendrocytes
(OLGs) (PubMed:23891804). Expressed in oligodendroglia progenitor
cells (OPCs) and immature oligodendrocytes (OLGs) in the neonatal
brain (at protein level) (PubMed:14613971).
{ECO:0000269|PubMed:14613971, ECO:0000269|PubMed:23891804,
ECO:0000269|PubMed:9030614}.
-!- INDUCTION: Up-regulated in response to the activation of group I
metabotropic glutamate receptors at synapses (PubMed:9144248).
Rapidly and transiently up-regulated in response to light exposure
in the cell bodies and dendrites of visual cortical neurons (at
protein level) (PubMed:15564573). {ECO:0000269|PubMed:15564573,
ECO:0000269|PubMed:9144248}.
-!- DOMAIN: The N-terminal 134 amino acids are necessary for
homodimerization and RNA-binding. The N-terminal 298 amino acids
are sufficient to interact with KCNMB4 and to regulate presynaptic
action potential (AP) duration in neurons. The two agenet-like
domains are necessary for binding to histone H3 in a methylation-
dependent manner. The KH domains are necessary for mediating miRNA
annealing to specific RNA targets. The KH 2 domain is necessary
for binding to kissing complex (kc) RNA ligands. The RGG box
domain is necessary for binding to mRNA targets that contain G-
quadruplex structures. The RGG-box domain is necessary for binding
to a triple stem-loop RNA structure, called Sod1 stem loop
interacting with FMRP (SoSLIP), in the superoxide dismutase SOD1
mRNA. The RGG box domain is necessary for binding to its own mRNA.
The RGG-box domain is necessary for binding to homopolymer
poly(G). {ECO:0000250|UniProtKB:Q06787}.
-!- PTM: Phosphorylated on several serine residues. Phosphorylation at
Ser-478 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.
{ECO:0000250|UniProtKB:P35922}.
-!- PTM: Monoubiquitinated. Polyubiquitinated. Ubiquitinated and
targeted for proteasomal degradation after activation of
metabotropic glutamate receptor (mGluR).
{ECO:0000250|UniProtKB:P35922}.
-!- PTM: Methylated; methylation is necessary for heterodimerization
with FXR1, association with polyribosomes, recruitment into stress
granules and translation of FMR1 target mRNAs. Methylated by
PRMT1, PRMT3 and PRMT4, in vitro. {ECO:0000250|UniProtKB:Q06787}.
-!- SIMILARITY: Belongs to the FMR1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB07073.1; Type=Miscellaneous discrepancy; Note=N-ter sequencing errors.; Evidence={ECO:0000305};
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EMBL; AY240947; AAP15341.1; -; mRNA.
EMBL; U60145; AAB07073.1; ALT_SEQ; mRNA.
RefSeq; NP_434691.1; NM_052804.1. [Q80WE1-2]
RefSeq; XP_006229594.1; XM_006229532.3. [Q80WE1-1]
UniGene; Rn.40595; -.
ProteinModelPortal; Q80WE1; -.
SMR; Q80WE1; -.
BioGrid; 247050; 1.
IntAct; Q80WE1; 1.
STRING; 10116.ENSRNOP00000016227; -.
iPTMnet; Q80WE1; -.
PhosphoSitePlus; Q80WE1; -.
PaxDb; Q80WE1; -.
PRIDE; Q80WE1; -.
Ensembl; ENSRNOT00000087893; ENSRNOP00000074033; ENSRNOG00000057464. [Q80WE1-2]
GeneID; 24948; -.
KEGG; rno:24948; -.
CTD; 2332; -.
RGD; 2623; Fmr1.
eggNOG; ENOG410IF9J; Eukaryota.
eggNOG; ENOG410ZDJG; LUCA.
GeneTree; ENSGT00390000017033; -.
HOGENOM; HOG000293377; -.
HOVERGEN; HBG005739; -.
InParanoid; Q80WE1; -.
KO; K15516; -.
PhylomeDB; Q80WE1; -.
PRO; PR:Q80WE1; -.
Proteomes; UP000002494; Chromosome X.
Bgee; ENSRNOG00000057464; -.
ExpressionAtlas; Q80WE1; differential.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0043679; C:axon terminus; IDA:UniProtKB.
GO; GO:0044295; C:axonal growth cone; IDA:RGD.
GO; GO:0015030; C:Cajal body; ISO:RGD.
GO; GO:0044297; C:cell body; IDA:MGI.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0042995; C:cell projection; ISO:RGD.
GO; GO:0010369; C:chromocenter; ISS:UniProtKB.
GO; GO:0005694; C:chromosome; ISS:UniProtKB.
GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; ISO:RGD.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:UniProtKB.
GO; GO:0010494; C:cytoplasmic stress granule; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0030425; C:dendrite; IDA:UniProtKB.
GO; GO:1902737; C:dendritic filopodium; IDA:UniProtKB.
GO; GO:0044294; C:dendritic growth cone; IDA:RGD.
GO; GO:0043198; C:dendritic shaft; IDA:RGD.
GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
GO; GO:0044327; C:dendritic spine head; IDA:RGD.
GO; GO:0044326; C:dendritic spine neck; IDA:RGD.
GO; GO:0019897; C:extrinsic component of plasma membrane; ISS:UniProtKB.
GO; GO:0032433; C:filopodium tip; ISS:UniProtKB.
GO; GO:0097386; C:glial cell projection; IDA:UniProtKB.
GO; GO:0030426; C:growth cone; IDA:UniProtKB.
GO; GO:1990812; C:growth cone filopodium; ISS:UniProtKB.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; ISO:RGD.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:1990124; C:messenger ribonucleoprotein complex; ISO:RGD.
GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB.
GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0071598; C:neuronal ribonucleoprotein granule; IDA:MGI.
GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0005844; C:polysome; IDA:UniProtKB.
GO; GO:0098794; C:postsynapse; ISO:RGD.
GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0098793; C:presynapse; ISS:UniProtKB.
GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:1990635; C:proximal dendrite; IDA:RGD.
GO; GO:1990904; C:ribonucleoprotein complex; ISO:RGD.
GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
GO; GO:0005790; C:smooth endoplasmic reticulum; IDA:RGD.
GO; GO:0097444; C:spine apparatus; IDA:RGD.
GO; GO:0045202; C:synapse; IDA:RGD.
GO; GO:0043195; C:terminal bouton; IDA:RGD.
GO; GO:0019034; C:viral replication complex; ISO:RGD.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0070840; F:dynein complex binding; ISS:UniProtKB.
GO; GO:0002151; F:G-quadruplex RNA binding; ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; ISO:RGD.
GO; GO:0044325; F:ion channel binding; ISO:RGD.
GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
GO; GO:0048027; F:mRNA 5'-UTR binding; ISS:UniProtKB.
GO; GO:0003729; F:mRNA binding; IPI:RGD.
GO; GO:0034046; F:poly(G) binding; ISS:UniProtKB.
GO; GO:0008266; F:poly(U) RNA binding; ISS:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IDA:RGD.
GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:RGD.
GO; GO:0019903; F:protein phosphatase binding; IDA:RGD.
GO; GO:0043022; F:ribosome binding; ISO:RGD.
GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IDA:RGD.
GO; GO:0003723; F:RNA binding; IDA:RGD.
GO; GO:0035613; F:RNA stem-loop binding; ISS:UniProtKB.
GO; GO:0033592; F:RNA strand annealing activity; ISS:UniProtKB.
GO; GO:1990825; F:sequence-specific mRNA binding; ISS:UniProtKB.
GO; GO:0035197; F:siRNA binding; ISS:UniProtKB.
GO; GO:0031369; F:translation initiation factor binding; ISO:RGD.
GO; GO:0030371; F:translation repressor activity; ISS:UniProtKB.
GO; GO:0008089; P:anterograde axonal transport; ISO:RGD.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0072711; P:cellular response to hydroxyurea; ISS:UniProtKB.
GO; GO:1904009; P:cellular response to monosodium glutamate; IEP:RGD.
GO; GO:0035865; P:cellular response to potassium ion; IEP:RGD.
GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB.
GO; GO:0098586; P:cellular response to virus; ISO:RGD.
GO; GO:0007417; P:central nervous system development; ISO:RGD.
GO; GO:0060996; P:dendritic spine development; ISO:RGD.
GO; GO:0050974; P:detection of mechanical stimulus involved in sensory perception; IEP:RGD.
GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
GO; GO:0007215; P:glutamate receptor signaling pathway; IDA:UniProtKB.
GO; GO:0044830; P:modulation by host of viral RNA genome replication; ISO:RGD.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0051028; P:mRNA transport; ISS:UniProtKB.
GO; GO:2000766; P:negative regulation of cytoplasmic translation; ISS:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; IMP:RGD.
GO; GO:1900453; P:negative regulation of long term synaptic depression; ISS:UniProtKB.
GO; GO:1902373; P:negative regulation of mRNA catabolic process; ISO:RGD.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:RGD.
GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:RGD.
GO; GO:0010955; P:negative regulation of protein processing; IMP:RGD.
GO; GO:0002091; P:negative regulation of receptor internalization; IMP:RGD.
GO; GO:2000301; P:negative regulation of synaptic vesicle exocytosis; IMP:UniProtKB.
GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
GO; GO:0045947; P:negative regulation of translational initiation; ISS:UniProtKB.
GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; IMP:UniProtKB.
GO; GO:0048666; P:neuron development; IEP:RGD.
GO; GO:0001541; P:ovarian follicle development; IEP:RGD.
GO; GO:0060999; P:positive regulation of dendritic spine development; ISS:UniProtKB.
GO; GO:0051491; P:positive regulation of filopodium assembly; ISS:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD.
GO; GO:2000637; P:positive regulation of gene silencing by miRNA; ISS:UniProtKB.
GO; GO:0033129; P:positive regulation of histone phosphorylation; ISS:UniProtKB.
GO; GO:1901254; P:positive regulation of intracellular transport of viral material; ISO:RGD.
GO; GO:1902416; P:positive regulation of mRNA binding; ISS:UniProtKB.
GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; ISS:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:RGD.
GO; GO:0002092; P:positive regulation of receptor internalization; ISS:UniProtKB.
GO; GO:2001022; P:positive regulation of response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
GO; GO:0060998; P:regulation of dendritic spine development; ISS:UniProtKB.
GO; GO:0051489; P:regulation of filopodium assembly; ISS:UniProtKB.
GO; GO:0060964; P:regulation of gene silencing by miRNA; ISS:UniProtKB.
GO; GO:1905244; P:regulation of modification of synaptic structure; ISO:RGD.
GO; GO:0043488; P:regulation of mRNA stability; ISS:UniProtKB.
GO; GO:0098908; P:regulation of neuronal action potential; ISS:UniProtKB.
GO; GO:0046928; P:regulation of neurotransmitter secretion; IMP:UniProtKB.
GO; GO:0006417; P:regulation of translation; TAS:RGD.
GO; GO:0099578; P:regulation of translation at postsynapse, modulating synaptic transmission; ISO:RGD.
GO; GO:0014823; P:response to activity; IEP:RGD.
GO; GO:0042220; P:response to cocaine; IEP:RGD.
GO; GO:0051602; P:response to electrical stimulus; IEP:RGD.
GO; GO:0034698; P:response to gonadotropin; IEP:RGD.
GO; GO:0070555; P:response to interleukin-1; IEP:RGD.
GO; GO:0009416; P:response to light stimulus; IEP:RGD.
GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
Gene3D; 3.30.1370.10; -; 2.
InterPro; IPR008395; Agenet-like_dom.
InterPro; IPR032196; FXMR_C2.
InterPro; IPR022034; FXMRP1_C_core.
InterPro; IPR004087; KH_dom.
InterPro; IPR004088; KH_dom_type_1.
InterPro; IPR036612; KH_dom_type_1_sf.
Pfam; PF05641; Agenet; 1.
Pfam; PF16098; FXMR_C2; 2.
Pfam; PF12235; FXMRP1_C_core; 1.
Pfam; PF00013; KH_1; 2.
SMART; SM00322; KH; 2.
SUPFAM; SSF54791; SSF54791; 2.
PROSITE; PS51641; AGENET_LIKE; 2.
PROSITE; PS50084; KH_TYPE_1; 2.
1: Evidence at protein level;
Acetylation; Activator; Alternative splicing; Cell junction;
Cell membrane; Cell projection; Centromere; Chromosome;
Complete proteome; Cytoplasm; DNA damage; Membrane; Methylation;
mRNA processing; mRNA splicing; mRNA transport; Neurogenesis; Nucleus;
Phosphoprotein; Postsynaptic cell membrane; Reference proteome;
Repeat; Repressor; Ribonucleoprotein; RNA-binding;
RNA-mediated gene silencing; Synapse; Synaptosome;
Translation regulation; Transport; Ubl conjugation.
CHAIN 1 593 Synaptic functional regulator FMR1.
/FTId=PRO_0000342185.
DOMAIN 4 50 Agenet-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00973}.
DOMAIN 63 115 Agenet-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00973}.
DOMAIN 218 279 KH 1. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 281 348 KH 2. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
REGION 1 184 Required for nuclear localization.
{ECO:0000250|UniProtKB:P35922}.
REGION 172 211 Necessary for interaction with CYFIP1,
CYFIP2, FXR1 and FXR2.
{ECO:0000250|UniProtKB:P35922,
ECO:0000250|UniProtKB:Q06787}.
REGION 375 469 Required for nuclear export.
{ECO:0000250|UniProtKB:Q06787}.
REGION 397 593 Interaction with RANBP9.
{ECO:0000250|UniProtKB:Q06787}.
REGION 512 526 RNA-binding RGG-box. {ECO:0000250}.
MOTIF 402 421 Nuclear export signal.
{ECO:0000250|UniProtKB:P35922}.
MOTIF 505 512 Nucleolar localization signal 1.
{ECO:0000250|UniProtKB:Q06787}.
MOTIF 574 578 Nucleolar localization signal 2.
{ECO:0000250|UniProtKB:Q06787}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q06787}.
MOD_RES 336 336 Phosphoserine.
{ECO:0000244|PubMed:16641100}.
MOD_RES 337 337 Phosphoserine.
{ECO:0000244|PubMed:16641100}.
MOD_RES 347 347 Phosphoserine.
{ECO:0000244|PubMed:16641100}.
MOD_RES 349 349 Phosphoserine.
{ECO:0000244|PubMed:16641100}.
MOD_RES 350 350 Phosphoserine.
{ECO:0000244|PubMed:16641100}.
MOD_RES 369 369 Phosphoserine.
{ECO:0000250|UniProtKB:Q06787}.
MOD_RES 441 441 Phosphothreonine.
{ECO:0000250|UniProtKB:P35922}.
MOD_RES 449 449 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P35922}.
MOD_RES 478 478 Phosphoserine.
{ECO:0000250|UniProtKB:Q06787}.
MOD_RES 522 522 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:Q06787}.
MOD_RES 522 522 Omega-N-methylated arginine; alternate.
{ECO:0000250}.
MOD_RES 581 581 Phosphoserine.
{ECO:0000250|UniProtKB:P35922}.
VAR_SEQ 469 480 Missing (in isoform 2).
{ECO:0000303|Ref.1}.
/FTId=VSP_034393.
CONFLICT 110 110 E -> D (in Ref. 2; AAB07073).
{ECO:0000305}.
CONFLICT 184 184 L -> S (in Ref. 2; AAB07073).
{ECO:0000305}.
CONFLICT 424 424 A -> V (in Ref. 2; AAB07073).
{ECO:0000305}.
SEQUENCE 593 AA; 66780 MW; 8EFBEC47E6B818F4 CRC64;
MEELVVEVRG SNGAFYKAFV KDVHEDSITV AFENNWQPER QIPFHDVRFP PPVGYNKDIN
ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD ATYNEIVTIE RLRSVNPNKP
ATKDTFHKIK LEVPEDLRQM CAKESAHKDF KKAVGAFSVT YDPENYQLVI LSINEVTSKR
AHMLIDMHFR SLRTKLSLIL RNEEASKQLE SSRQLASRFH EQFIVREDLM GLAIGTHGAN
IQQARKVPGV TAIDLDEDTC TFHIYGEDQD AVKKARSFLE FAEDVIQVPR NLVGKVIGKN
GKLIQEIVDK SGVVRVRIEA ENEKSVPQEE ENLPPSSLPS NNSRVGSNSS EEKKHLDTKE
NTHFSQPNST KVQRGMVPFV FVGTKDSIAN ATVLLDYHLN YLKEVDQLRL ERLQIDEQLR
QIGASSRPPP NRTDKEKGYV TDDGQGMGRG SRPYRNRGHG RRGPGYTSGT NSEASNASET
ESDHRDELSD WSLAPTEEER ESFLRRGDGR RRGGGGRGQG GRGRGGGFKG NDDHSRTDNR
PRNPRETKGR TTDGSLQSTS SEGSRLRTGK DRNQKKEKPD SVDGLQPLVN GVP


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