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Synaptic functional regulator FMR1 (Fragile X mental retardation protein 1 homolog) (FMRP) (Protein FMR-1) (mFmr1p)

 FMR1_MOUSE              Reviewed;         614 AA.
P35922;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
07-JUN-2017, entry version 155.
RecName: Full=Synaptic functional regulator FMR1 {ECO:0000305};
AltName: Full=Fragile X mental retardation protein 1 homolog {ECO:0000250|UniProtKB:Q06787};
Short=FMRP {ECO:0000303|PubMed:10567518};
Short=Protein FMR-1 {ECO:0000303|PubMed:8358432};
Short=mFmr1p;
Name=Fmr1 {ECO:0000312|MGI:MGI:95564};
Synonyms=Fmr-1 {ECO:0000303|PubMed:8358432};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=8358432; DOI=10.1038/ng0793-244;
Ashley C.T. Jr., Sutcliffe J.S., Kunst C.B., Leiner H.A.,
Eichler E.E., Nelson D.L., Warren S.T.;
"Human and murine FMR-1: alternative splicing and translational
initiation downstream of the CGG-repeat.";
Nat. Genet. 4:244-251(1993).
[2]
DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=8033209;
Bakker C.B., Verheij C., Willemsen R., van der Helm R., Oerlemans F.,
Vermey M., Bygrave A., Hoogeveen A.T., Oostra B.A.;
"Fmr1 knockout mice: a model to study fragile X mental retardation.";
Cell 78:23-33(1994).
[3]
SUBCELLULAR LOCATION, NUCLEOCYTOPLASMIC SHUTTLING, AND MUTAGENESIS OF
429-LEU--LEU-431.
PubMed=8895584;
Fridell R.A., Benson R.E., Hua J., Bogerd H.P., Cullen B.R.;
"A nuclear role for the Fragile X mental retardation protein.";
EMBO J. 15:5408-5414(1996).
[4]
SUBCELLULAR LOCATION, NUCLEOCYTOPLASMIC SHUTTLING, ASSOCIATION WITH
POLYRIBOSOME AND MRNP, AND MUTAGENESIS OF 429-LEU--LEU-434.
PubMed=8842725; DOI=10.1093/hmg/5.8.1083;
Eberhart D.E., Malter H.E., Feng Y., Warren S.T.;
"The fragile X mental retardation protein is a ribonucleoprotein
containing both nuclear localization and nuclear export signals.";
Hum. Mol. Genet. 5:1083-1091(1996).
[5]
SUBCELLULAR LOCATION, ASSOCIATION WITH POLYRIBOSOME, AND ASSOCIATION
WITH MRNP.
PubMed=9285783; DOI=10.1093/hmg/6.9.1465;
Corbin F., Bouillon M., Fortin A., Morin S., Rousseau F.,
Khandjian E.W.;
"The fragile X mental retardation protein is associated with poly(A)+
mRNA in actively translating polyribosomes.";
Hum. Mol. Genet. 6:1465-1472(1997).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=9144249; DOI=10.1073/pnas.94.10.5401;
Comery T.A., Harris J.B., Willems P.J., Oostra B.A., Irwin S.A.,
Weiler I.J., Greenough W.T.;
"Abnormal dendritic spines in fragile X knockout mice: maturation and
pruning deficits.";
Proc. Natl. Acad. Sci. U.S.A. 94:5401-5404(1997).
[7]
INTERACTION WITH NUFIP1.
PubMed=10556305; DOI=10.1093/hmg/8.13.2557;
Bardoni B., Schenck A., Mandel J.-L.;
"A novel RNA-binding nuclear protein that interacts with the fragile X
mental retardation (FMR1) protein.";
Hum. Mol. Genet. 8:2557-2566(1999).
[8]
INTERACTION WITH FXR1; FXR2 AND NCL.
PubMed=10567518; DOI=10.1128/MCB.19.12.7925;
Ceman S., Brown V., Warren S.T.;
"Isolation of an FMRP-associated messenger ribonucleoprotein particle
and identification of nucleolin and the fragile X-related proteins as
components of the complex.";
Mol. Cell. Biol. 19:7925-7932(1999).
[9]
INTERACTION WITH YBX1.
PubMed=11162447; DOI=10.1006/bbrc.2000.4035;
Ceman S., Nelson R., Warren S.T.;
"Identification of mouse YB1/p50 as a component of the FMRP-associated
mRNP particle.";
Biochem. Biophys. Res. Commun. 279:904-908(2000).
[10]
ASSOCIATION WITH MRNP, AND RNA-BINDING.
PubMed=11719188; DOI=10.1016/S0092-8674(01)00568-2;
Brown V., Jin P., Ceman S., Darnell J.C., O'Donnell W.T.,
Tenenbaum S.A., Jin X., Feng Y., Wilkinson K.D., Keene J.D.,
Darnell R.B., Warren S.T.;
"Microarray identification of FMRP-associated brain mRNAs and altered
mRNA translational profiles in fragile X syndrome.";
Cell 107:477-487(2001).
[11]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=11438589;
Nimchinsky E.A., Oberlander A.M., Svoboda K.;
"Abnormal development of dendritic spines in FMR1 knock-out mice.";
J. Neurosci. 21:5139-5146(2001).
[12]
FUNCTION, INTERACTION WITH FXR2, AND RNA-BINDING.
PubMed=11376146; DOI=10.1093/nar/29.11.2276;
Li Z., Zhang Y., Ku L., Wilkinson K.D., Warren S.T., Feng Y.;
"The fragile X mental retardation protein inhibits translation via
interacting with mRNA.";
Nucleic Acids Res. 29:2276-2283(2001).
[13]
INTERACTION WITH CYFIP1 AND CYFIP2, AND SUBCELLULAR LOCATION.
PubMed=11438699; DOI=10.1073/pnas.151231598;
Schenck A., Bardoni B., Moro A., Bagni C., Mandel J.-L.;
"A highly conserved protein family interacting with the fragile X
mental retardation protein (FMRP) and displaying selective
interactions with FMRP-related proteins FXR1P and FXR2P.";
Proc. Natl. Acad. Sci. U.S.A. 98:8844-8849(2001).
[14]
INTERACTION WITH MYO5A AND PURA.
PubMed=12147688; DOI=10.1074/jbc.M203608200;
Ohashi S., Koike K., Omori A., Ichinose S., Ohara S., Kobayashi S.,
Sato T.A., Anzai K.;
"Identification of mRNA/protein (mRNP) complexes containing Puralpha,
mStaufen, fragile X protein, and myosin Va and their association with
rough endoplasmic reticulum equipped with a kinesin motor.";
J. Biol. Chem. 277:37804-37810(2002).
[15]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12032354; DOI=10.1073/pnas.122205699;
Huber K.M., Gallagher S.M., Warren S.T., Bear M.F.;
"Altered synaptic plasticity in a mouse model of fragile X mental
retardation.";
Proc. Natl. Acad. Sci. U.S.A. 99:7746-7750(2002).
[16]
FUNCTION, ASSOCIATION WITH POLYRIBOSOME AND MRNP, RNA-BINDING, AND
DISRUPTION PHENOTYPE.
PubMed=12581522; DOI=10.1016/S0092-8674(03)00079-5;
Zalfa F., Giorgi M., Primerano B., Moro A., Di Penta A., Reis S.,
Oostra B., Bagni C.;
"The fragile X syndrome protein FMRP associates with BC1 RNA and
regulates the translation of specific mRNAs at synapses.";
Cell 112:317-327(2003).
[17]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-499,
MUTAGENESIS OF SER-499, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=14570712; DOI=10.1093/hmg/ddg350;
Ceman S., O'Donnell W.T., Reed M., Patton S., Pohl J., Warren S.T.;
"Phosphorylation influences the translation state of FMRP-associated
polyribosomes.";
Hum. Mol. Genet. 12:3295-3305(2003).
[18]
FUNCTION, DISRUPTION PHENOTYPE, ASSOCIATION WITH POLYRIBOSOME, AND
ASSOCIATION WITH MRNP.
PubMed=12575950; DOI=10.1016/S0896-6273(03)00034-5;
Miyashiro K.Y., Beckel-Mitchener A., Purk T.P., Becker K.G.,
Barret T., Liu L., Carbonetto S., Weiler I.J., Greenough W.T.,
Eberwine J.;
"RNA cargoes associating with FMRP reveal deficits in cellular
functioning in Fmr1 null mice.";
Neuron 37:417-431(2003).
[19]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12927206; DOI=10.1016/S0306-4522(03)00406-8;
Chen L., Yun S.W., Seto J., Liu W., Toth M.;
"The fragile X mental retardation protein binds and regulates a novel
class of mRNAs containing U rich target sequences.";
Neuroscience 120:1005-1017(2003).
[20]
FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
PubMed=14614133; DOI=10.1073/pnas.2336265100;
Todd P.K., Mack K.J., Malter J.S.;
"The fragile X mental retardation protein is required for type-I
metabotropic glutamate receptor-dependent translation of PSD-95.";
Proc. Natl. Acad. Sci. U.S.A. 100:14374-14378(2003).
[21]
FUNCTION, ASSOCIATION WITH POLYRIBOSOME, RNA-BINDING, SUBCELLULAR
LOCATION, 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).
[22]
INTERACTION WITH RANBP9.
PubMed=15381419; DOI=10.1016/j.jmb.2004.08.024;
Menon R.P., Gibson T.J., Pastore A.;
"The C-terminus of fragile X mental retardation protein interacts with
the multi-domain Ran-binding protein in the microtubule-organising
centre.";
J. Mol. Biol. 343:43-53(2004).
[23]
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).
[24]
SUBCELLULAR LOCATION, AND ASSOCIATION WITH POLYRIBOSOME.
PubMed=15317853; DOI=10.1523/JNEUROSCI.2306-04.2004;
Stefani G., Fraser C.E., Darnell J.C., Darnell R.B.;
"Fragile X mental retardation protein is associated with translating
polyribosomes in neuronal cells.";
J. Neurosci. 24:7272-7276(2004).
[25]
SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=15312650; DOI=10.1016/j.neuron.2004.07.022;
Kanai Y., Dohmae N., Hirokawa N.;
"Kinesin transports RNA: isolation and characterization of an RNA-
transporting granule.";
Neuron 43:513-525(2004).
[26]
SUBCELLULAR LOCATION, AND ASSOCIATION WITH MRNP.
PubMed=15329415; DOI=10.1073/pnas.0405398101;
Khandjian E.W., Huot M.E., Tremblay S., Davidovic L., Mazroui R.,
Bardoni B.;
"Biochemical evidence for the association of fragile X mental
retardation protein with brain polyribosomal ribonucleoparticles.";
Proc. Natl. Acad. Sci. U.S.A. 101:13357-13362(2004).
[27]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=15475576; DOI=10.1073/pnas.0404995101;
Lu R., Wang H., Liang Z., Ku L., O'donnell W.T., Li W., Warren S.T.,
Feng Y.;
"The fragile X protein controls microtubule-associated protein 1B
translation and microtubule stability in brain neuron development.";
Proc. Natl. Acad. Sci. U.S.A. 101:15201-15206(2004).
[28]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15548614; DOI=10.1073/pnas.0407533101;
Weiler I.J., Spangler C.C., Klintsova A.Y., Grossman A.W., Kim S.H.,
Bertaina-Anglade V., Khaliq H., de Vries F.E., Lambers F.A., Hatia F.,
Base C.K., Greenough W.T.;
"Fragile X mental retardation protein is necessary for
neurotransmitter-activated protein translation at synapses.";
Proc. Natl. Acad. Sci. U.S.A. 101:17504-17509(2004).
[29]
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).
[30]
ASSOCIATION WITH POLYRIBOSOME.
PubMed=15805463; DOI=10.1101/gad.1276805;
Darnell J.C., Fraser C.E., Mostovetsky O., Stefani G., Jones T.A.,
Eddy S.R., Darnell R.B.;
"Kissing complex RNAs mediate interaction between the Fragile-X mental
retardation protein KH2 domain and brain polyribosomes.";
Genes Dev. 19:903-918(2005).
[31]
TISSUE SPECIFICITY.
PubMed=16000371; DOI=10.1091/mbc.E05-04-0304;
Huot M.-E., Bisson N., Davidovic L., Mazroui R., Labelle Y., Moss T.,
Khandjian E.W.;
"The RNA-binding protein Fragile X-related 1 regulates somite
formation in Xenopus laevis.";
Mol. Biol. Cell 16:4350-4361(2005).
[32]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=16631377; DOI=10.1016/j.mcn.2006.02.001;
Antar L.N., Li C., Zhang H., Carroll R.C., Bassell G.J.;
"Local functions for FMRP in axon growth cone motility and activity-
dependent regulation of filopodia and spine synapses.";
Mol. Cell. Neurosci. 32:37-48(2006).
[33]
FUNCTION, SUBCELLULAR LOCATION, PROTEOLYTIC DEGRADATION, INDUCTION,
AND DISRUPTION PHENOTYPE.
PubMed=16908410; DOI=10.1016/j.neuron.2006.07.005;
Hou L., Antion M.D., Hu D., Spencer C.M., Paylor R., Klann E.;
"Dynamic translational and proteasomal regulation of fragile X mental
retardation protein controls mGluR-dependent long-term depression.";
Neuron 51:441-454(2006).
[34]
FUNCTION, INTERACTION WITH NXF2, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=16790844; DOI=10.1261/rna.94306;
Lai D., Sakkas D., Huang Y.;
"The fragile X mental retardation protein interacts with a distinct
mRNA nuclear export factor NXF2.";
RNA 12:1446-1449(2006).
[35]
FUNCTION, ASSOCIATION WITH MRNA, AND DISRUPTION PHENOTYPE.
PubMed=17507556; DOI=10.1523/JNEUROSCI.0937-07.2007;
Muddashetty R.S., Kelic S., Gross C., Xu M., Bassell G.J.;
"Dysregulated metabotropic glutamate receptor-dependent translation of
AMPA receptor and postsynaptic density-95 mRNAs at synapses in a mouse
model of fragile X syndrome.";
J. Neurosci. 27:5338-5348(2007).
[36]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17417632; DOI=10.1038/nn1893;
Zalfa F., Eleuteri B., Dickson K.S., Mercaldo V., De Rubeis S.,
di Penta A., Tabolacci E., Chiurazzi P., Neri G., Grant S.G.,
Bagni C.;
"A new function for the fragile X mental retardation protein in
regulation of PSD-95 mRNA stability.";
Nat. Neurosci. 10:578-587(2007).
[37]
FUNCTION, INTERACTION WITH NXF2, AND TISSUE SPECIFICITY.
PubMed=17548835; DOI=10.1073/pnas.0700169104;
Zhang M., Wang Q., Huang Y.;
"Fragile X mental retardation protein FMRP and the RNA export factor
NXF2 associate with and destabilize Nxf1 mRNA in neuronal cells.";
Proc. Natl. Acad. Sci. U.S.A. 104:10057-10062(2007).
[38]
FUNCTION, INTERACTION WITH CYFIP1-EIF4E COMPLEX, ASSOCIATION WITH
MRNP, RNA-BINDING, AND SUBCELLULAR LOCATION.
PubMed=18805096; DOI=10.1016/j.cell.2008.07.031;
Napoli I., Mercaldo V., Boyl P.P., Eleuteri B., Zalfa F.,
De Rubeis S., Di Marino D., Mohr E., Massimi M., Falconi M., Witke W.,
Costa-Mattioli M., Sonenberg N., Achsel T., Bagni C.;
"The fragile X syndrome protein represses activity-dependent
translation through CYFIP1, a new 4E-BP.";
Cell 134:1042-1054(2008).
[39]
FUNCTION, INTERACTION WITH KIF5A, INTERACTION WITH DYNEIN, ASSOCIATION
WITH MICROTUBULES, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=18539120; DOI=10.1016/j.devcel.2008.04.003;
Dictenberg J.B., Swanger S.A., Antar L.N., Singer R.H., Bassell G.J.;
"A direct role for FMRP in activity-dependent dendritic mRNA transport
links filopodial-spine morphogenesis to fragile X syndrome.";
Dev. Cell 14:926-939(2008).
[40]
ASSOCIATION WITH THE SMN CORE COMPLEX.
PubMed=18093976; DOI=10.1074/jbc.M707304200;
Piazzon N., Rage F., Schlotter F., Moine H., Branlant C., Massenet S.;
"In vitro and in cellulo evidences for association of the survival of
motor neuron complex with the fragile X mental retardation protein.";
J. Biol. Chem. 283:5598-5610(2008).
[41]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18653529; DOI=10.1093/nar/gkn472;
Didiot M.C., Tian Z., Schaeffer C., Subramanian M., Mandel J.L.,
Moine H.;
"The G-quartet containing FMRP binding site in FMR1 mRNA is a potent
exonic splicing enhancer.";
Nucleic Acids Res. 36:4902-4912(2008).
[42]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=19640847; DOI=10.1074/jbc.M109.042663;
Schuett J., Falley K., Richter D., Kreienkamp H.J., Kindler S.;
"Fragile X mental retardation protein regulates the levels of scaffold
proteins and glutamate receptors in postsynaptic densities.";
J. Biol. Chem. 284:25479-25487(2009).
[43]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=19193898; DOI=10.1523/JNEUROSCI.3937-08.2009;
Christie S.B., Akins M.R., Schwob J.E., Fallon J.R.;
"The FXG: a presynaptic fragile X granule expressed in a subset of
developing brain circuits.";
J. Neurosci. 29:1514-1524(2009).
[44]
FUNCTION, RNA-BINDING, AND DISRUPTION PHENOTYPE.
PubMed=19166269; DOI=10.1371/journal.pbio.1000016;
Bechara E.G., Didiot M.C., Melko M., Davidovic L., Bensaid M.,
Martin P., Castets M., Pognonec P., Khandjian E.W., Moine H.,
Bardoni B.;
"A novel function for fragile X mental retardation protein in
translational activation.";
PLoS Biol. 7:E16-E16(2009).
[45]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-462 AND SER-602, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Kidney, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[46]
FUNCTION, AND 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).
[47]
FUNCTION, AND RNA-BINDING.
PubMed=20159450; DOI=10.1016/j.neuron.2010.01.005;
Edbauer D., Neilson J.R., Foster K.A., Wang C.F., Seeburg D.P.,
Batterton M.N., Tada T., Dolan B.M., Sharp P.A., Sheng M.;
"Regulation of synaptic structure and function by FMRP-associated
microRNAs miR-125b and miR-132.";
Neuron 65:373-384(2010).
[48]
FUNCTION, INTERACTION WITH RPLP0, RNA-BINDING, ASSOCIATION WITH
POLYRIBOSOME, AND DISRUPTION PHENOTYPE.
PubMed=21784246; DOI=10.1016/j.cell.2011.06.013;
Darnell J.C., Van Driesche S.J., Zhang C., Hung K.Y., Mele A.,
Fraser C.E., Stone E.F., Chen C., Fak J.J., Chi S.W., Licatalosi D.D.,
Richter J.D., Darnell R.B.;
"FMRP stalls ribosomal translocation on mRNAs linked to synaptic
function and autism.";
Cell 146:247-261(2011).
[49]
FUNCTION, RNA-BINDING, AND DISRUPTION PHENOTYPE.
PubMed=21490210; DOI=10.1523/JNEUROSCI.6661-10.2011;
Gross C., Yao X., Pong D.L., Jeromin A., Bassell G.J.;
"Fragile X mental retardation protein regulates protein expression and
mRNA translation of the potassium channel Kv4.2.";
J. Neurosci. 31:5693-5698(2011).
[50]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=23235829; DOI=10.1038/nature11737;
Ascano M. Jr., Mukherjee N., Bandaru P., Miller J.B., Nusbaum J.D.,
Corcoran D.L., Langlois C., Munschauer M., Dewell S., Hafner M.,
Williams Z., Ohler U., Tuschl T.;
"FMRP targets distinct mRNA sequence elements to regulate protein
expression.";
Nature 492:382-386(2012).
[51]
LACK OF FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
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).
[52]
DISRUPTION PHENOTYPE, AND RNA-BINDING.
PubMed=24349419; DOI=10.1371/journal.pone.0083007;
Derlig K., Giessl A., Brandstatter J.H., Enz R., Dahlhaus R.;
"Identification and characterisation of Simiate, a novel protein
linked to the fragile X syndrome.";
PLoS ONE 8:E83007-E83007(2013).
[53]
FUNCTION, CHROMATIN BINDING, SUBCELLULAR LOCATION, AND DISRUPTION
PHENOTYPE.
PubMed=24813610; DOI=10.1016/j.cell.2014.03.040;
Alpatov R., Lesch B.J., Nakamoto-Kinoshita M., Blanco A., Chen S.,
Stuetzer A., Armache K.J., Simon M.D., Xu C., Ali M., Murn J.,
Prisic S., Kutateladze T.G., Vakoc C.R., Min J., Kingston R.E.,
Fischle W., Warren S.T., Page D.C., Shi Y.;
"A chromatin-dependent role of the fragile X mental retardation
protein FMRP in the DNA damage response.";
Cell 157:869-881(2014).
[54]
INTERACTION WITH MOV10.
PubMed=25464849; DOI=10.1016/j.celrep.2014.10.054;
Kenny P.J., Zhou H., Kim M., Skariah G., Khetani R.S., Drnevich J.,
Arcila M.L., Kosik K.S., Ceman S.;
"MOV10 and FMRP regulate AGO2 association with microRNA recognition
elements.";
Cell Rep. 9:1729-1741(2014).
[55]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-470, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[56]
FUNCTION, INTERACTION WITH CACNA1B, SUBCELLULAR LOCATION, AND
DISRUPTION PHENOTYPE.
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).
[57]
RNA-BINDING.
PubMed=25692235; DOI=10.1080/15476286.2014.996464;
Zhang Y., Gaetano C.M., Williams K.R., Bassell G.J., Mihailescu M.R.;
"FMRP interacts with G-quadruplex structures in the 3'-UTR of its
dendritic target Shank1 mRNA.";
RNA Biol. 11:1364-1374(2014).
[58]
FUNCTION, INTERACTION WITH KCNMB4, AND DISRUPTION PHENOTYPE.
PubMed=25561520; DOI=10.1073/pnas.1423094112;
Myrick L.K., Deng P.Y., Hashimoto H., Oh Y.M., Cho Y., Poidevin M.J.,
Suhl J.A., Visootsak J., Cavalli V., Jin P., Cheng X., Warren S.T.,
Klyachko V.A.;
"Independent role for presynaptic FMRP revealed by an FMR1 missense
mutation associated with intellectual disability and seizures.";
Proc. Natl. Acad. Sci. U.S.A. 112:949-956(2015).
-!- 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:11438589, PubMed:12032354, PubMed:15475576,
PubMed:16631377, PubMed:16790844, PubMed:17417632,
PubMed:17548835, PubMed:18539120, PubMed:18653529,
PubMed:19640847, PubMed:19166269, PubMed:20159450,
PubMed:21784246, PubMed:23235829, PubMed:24813610). Plays a role
in the alternative splicing of its own mRNA (PubMed:18653529).
Plays a role in mRNA nuclear export (PubMed:16790844). Together
with export factor NXF2, is involved in the regulation of the NXF1
mRNA stability in neurons (PubMed:17548835). 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
(PubMed:17417632). 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 (PubMed:18539120). Plays
a role as a repressor of mRNA translation during the transport of
dendritic mRNAs to postnyaptic dendritic spines (PubMed:11376146,
PubMed:12581522, PubMed:14570712, PubMed:12927206,
PubMed:15475576, PubMed:16908410, PubMed:18805096,
PubMed:19640847, PubMed:21784246, PubMed:23235829). Component of
the CYFIP1-EIF4E-FMR1 complex which blocks cap-dependent mRNA
translation initiation (PubMed:18805096). Represses mRNA
translation by stalling ribosomal translocation during elongation
(PubMed:21784246). Reports are contradictory with regards to its
ability to mediate translation inhibition of (MBP) mRNA in
oligodendrocytes (PubMed:14613971, 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:20159450, PubMed:25464849). 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 (PubMed:14614133, PubMed:14613971,
PubMed:15548614, PubMed:19640847, PubMed:19166269,
PubMed:21490210). In response to mGluR stimulation, FMR1-target
mRNAs are rapidly derepressed, allowing for local translation at
synapses (PubMed:16908410, PubMed:17507556, PubMed:19640847).
Binds to a large subset of dendritic mRNAs that encode a myriad of
proteins involved in pre- and postsynaptic functions
(PubMed:11719188, PubMed:11376146, PubMed:14613971,
PubMed:17507556, PubMed:21784246, PubMed:21490210,
PubMed:24349419). 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
(PubMed:25692235). 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 (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 (PubMed:12581522,
PubMed:18805096). Associates with export factor NXF1 mRNA-
containing ribonucleoprotein particles (mRNPs) in a NXF2-dependent
manner (PubMed:17548835). Binds to a subset of miRNAs in the brain
(PubMed:20159450). 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
(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
(PubMed:24709664). Plays a role in regulation of MAP1B-dependent
microtubule dynamics during neuronal development
(PubMed:15475576). 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).
{ECO:0000250|UniProtKB:Q06787, ECO:0000250|UniProtKB:Q80WE1,
ECO:0000269|PubMed:11376146, ECO:0000269|PubMed:11438589,
ECO:0000269|PubMed:11719188, ECO:0000269|PubMed:12032354,
ECO:0000269|PubMed:12581522, ECO:0000269|PubMed:12927206,
ECO:0000269|PubMed:14570712, ECO:0000269|PubMed:14613971,
ECO:0000269|PubMed:14614133, ECO:0000269|PubMed:15475576,
ECO:0000269|PubMed:15548614, ECO:0000269|PubMed:16631377,
ECO:0000269|PubMed:16790844, ECO:0000269|PubMed:16908410,
ECO:0000269|PubMed:17417632, ECO:0000269|PubMed:17507556,
ECO:0000269|PubMed:17548835, ECO:0000269|PubMed:18539120,
ECO:0000269|PubMed:18653529, ECO:0000269|PubMed:18805096,
ECO:0000269|PubMed:19166269, ECO:0000269|PubMed:19640847,
ECO:0000269|PubMed:20159450, ECO:0000269|PubMed:20512134,
ECO:0000269|PubMed:21490210, ECO:0000269|PubMed:21784246,
ECO:0000269|PubMed:23235829, ECO:0000269|PubMed:23891804,
ECO:0000269|PubMed:24349419, ECO:0000269|PubMed:24709664,
ECO:0000269|PubMed:24813610, ECO:0000269|PubMed:25561520,
ECO:0000269|PubMed:25692235}.
-!- 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
(PubMed:18805096). 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 (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 (PubMed:11438699,
PubMed:18805096). Interacts with CYFIP2 (PubMed:11438699).
Interacts with EIF5; this interaction occurs in a RNA-dependent
manner (By similarity). Interacts with dynein (PubMed:18539120).
Interacts with FXR1 and FXR2 (PubMed:10567518). 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 (PubMed:25561520). 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
(PubMed:18539120). 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
(PubMed:25464849). Interacts with MYO5A and PURA; these
interactions occur in association with polyribosome
(PubMed:12147688). Interacts with NCL (PubMed:10567518). Interacts
with NUFIP1 (PubMed:10556305). 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 (PubMed:16790844, PubMed:17548835). Interacts with
RANBP9; this interaction is direct and inhibits binding of FMR1 to
RNA homopolymer (PubMed:15381419). Interacts with RPLP0
(PubMed:21784246). 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 (PubMed:11162447). Interacts with nucleosome (By
similarity). Associates with polyribosome; this association occurs
in a mRNA-dependent manner (PubMed:8842725, PubMed:9285783,
PubMed:12581522, PubMed:12575950, PubMed:14613971,
PubMed:15317853, PubMed:15805463, PubMed:21784246). Associates
with messenger ribonucleoprotein particles (mRNPs)
(PubMed:8842725, PubMed:9285783, PubMed:11719188, PubMed:12581522,
PubMed:12575950, PubMed:15329415, PubMed:18805096). Associates
with microtubules in a kinesin- and dynein-dependent manner
(PubMed:18539120). {ECO:0000250|UniProtKB:Q06787,
ECO:0000269|PubMed:10556305, ECO:0000269|PubMed:10567518,
ECO:0000269|PubMed:11162447, ECO:0000269|PubMed:11438699,
ECO:0000269|PubMed:11719188, ECO:0000269|PubMed:12147688,
ECO:0000269|PubMed:12575950, ECO:0000269|PubMed:12581522,
ECO:0000269|PubMed:14613971, ECO:0000269|PubMed:15317853,
ECO:0000269|PubMed:15329415, ECO:0000269|PubMed:15381419,
ECO:0000269|PubMed:15805463, ECO:0000269|PubMed:16790844,
ECO:0000269|PubMed:17548835, ECO:0000269|PubMed:18093976,
ECO:0000269|PubMed:18539120, ECO:0000269|PubMed:18805096,
ECO:0000269|PubMed:20512134, ECO:0000269|PubMed:21784246,
ECO:0000269|PubMed:24709664, ECO:0000269|PubMed:25464849,
ECO:0000269|PubMed:25561520, ECO:0000269|PubMed:8842725,
ECO:0000269|PubMed:9285783}.
-!- INTERACTION:
Q9JHG6:Rcan1; NbExp=3; IntAct=EBI-645094, EBI-644061;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16908410,
ECO:0000269|PubMed:8842725, ECO:0000269|PubMed:8895584}. Nucleus,
nucleolus {ECO:0000250|UniProtKB:Q06787}. Chromosome, centromere
{ECO:0000269|PubMed:24813610}. Chromosome
{ECO:0000269|PubMed:24813610}. Cytoplasm
{ECO:0000269|PubMed:11438699, ECO:0000269|PubMed:14570712,
ECO:0000269|PubMed:15317853, ECO:0000269|PubMed:15329415,
ECO:0000269|PubMed:16790844, ECO:0000269|PubMed:24709664,
ECO:0000269|PubMed:8842725, ECO:0000269|PubMed:8895584}.
Cytoplasm, perinuclear region {ECO:0000269|PubMed:11438699,
ECO:0000269|PubMed:16790844, ECO:0000269|PubMed:8842725,
ECO:0000269|PubMed:9285783}. Cytoplasmic granule
{ECO:0000269|PubMed:15028757, ECO:0000269|PubMed:15312650,
ECO:0000269|PubMed:16098134, ECO:0000269|PubMed:18539120,
ECO:0000269|PubMed:9285783}. Perikaryon
{ECO:0000269|PubMed:14613971, ECO:0000269|PubMed:16908410,
ECO:0000269|PubMed:18805096, ECO:0000269|PubMed:19193898}. Cell
projection {ECO:0000250|UniProtKB:Q06787}. Cell projection, axon
{ECO:0000269|PubMed:16631377, ECO:0000269|PubMed:19193898}. Cell
projection, dendrite {ECO:0000269|PubMed:15028757,
ECO:0000269|PubMed:16631377, ECO:0000269|PubMed:16908410,
ECO:0000269|PubMed:18539120, ECO:0000269|PubMed:18805096,
ECO:0000269|PubMed:19193898}. Cell projection, dendritic spine
{ECO:0000269|PubMed:15028757, ECO:0000269|PubMed:16631377}. Cell
junction, synapse, synaptosome {ECO:0000269|PubMed:18805096}. Cell
projection, filopodium {ECO:0000269|PubMed:16631377}. Cell
projection, growth cone {ECO:0000269|PubMed:16631377}. Cell
projection, filopodium tip {ECO:0000269|PubMed:16631377}. Cell
junction, synapse {ECO:0000269|PubMed:16631377}. Cell junction,
synapse, postsynaptic cell membrane {ECO:0000269|PubMed:19193898}.
Cell junction, synapse, presynaptic cell membrane
{ECO:0000269|PubMed:19193898}. Cell membrane
{ECO:0000269|PubMed:24709664}. Note=Colocalizes with H2AFX/H2A.x
in pericentromeric heterochromatin in response to DNA damaging
agents (PubMed:24813610). Localizes on meiotic pachytene-stage
chromosomes (PubMed:24813610). Forms nuclear foci representing
sites of ongoing DNA replication in response to DNA damaging
agents (PubMed:24813610). Shuttles between nucleus and cytoplasm
in a XPO1/CRM1-dependent manner (PubMed:8895584, PubMed:8842725).
Localizes to cytoplasmic granules, also referred to as messenger
ribonucleoprotein particles or mRNPs, along dendrites and
dendritic spines (PubMed:15028757, PubMed:16631377). 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:15312650, PubMed:16098134,
PubMed:18539120). Colocalizes with CACNA1B in the cytoplasm and at
the cell membrane of neurons (PubMed:24709664). Colocalizes with
CYFIP1, CYFIP2, NXF2 and ribosomes in the perinuclear region
(PubMed:11438699, PubMed:16790844). Colocalizes with CYFIP1 and
EIF4E in dendrites and probably at synapses (PubMed:18805096).
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 (PubMed:19193898). Colocalizes with
TDRD3 in cytoplasmic stress granules (SGs) in response to various
cellular stress (By similarity). {ECO:0000250|UniProtKB:Q06787,
ECO:0000250|UniProtKB:Q80WE1, ECO:0000269|PubMed:11438699,
ECO:0000269|PubMed:15028757, ECO:0000269|PubMed:15312650,
ECO:0000269|PubMed:16098134, ECO:0000269|PubMed:16631377,
ECO:0000269|PubMed:16790844, ECO:0000269|PubMed:18539120,
ECO:0000269|PubMed:18805096, ECO:0000269|PubMed:19193898,
ECO:0000269|PubMed:24709664, ECO:0000269|PubMed:24813610,
ECO:0000269|PubMed:8842725, ECO:0000269|PubMed:8895584}.
-!- SUBCELLULAR LOCATION: Isoform 4: Nucleus
{ECO:0000269|PubMed:8842725}. Nucleus, nucleoplasm
{ECO:0000269|PubMed:8842725}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=12;
Name=1; Synonyms=ISO1;
IsoId=P35922-1; Sequence=Displayed;
Name=2; Synonyms=ISO2;
IsoId=P35922-2; Sequence=VSP_002828;
Name=3; Synonyms=ISO3;
IsoId=P35922-3; Sequence=VSP_002829;
Name=4; Synonyms=ISO4;
IsoId=P35922-4; Sequence=VSP_002831, VSP_002830;
Name=5; Synonyms=ISO5;
IsoId=P35922-5; Sequence=VSP_002832, VSP_002833;
Name=6; Synonyms=ISO6;
IsoId=P35922-6; Sequence=VSP_002834, VSP_002835;
Name=7; Synonyms=ISO7;
IsoId=P35922-7; Sequence=VSP_002827;
Name=8; Synonyms=ISO8;
IsoId=P35922-8; Sequence=VSP_002827, VSP_002828;
Name=9; Synonyms=ISO9;
IsoId=P35922-9; Sequence=VSP_002827, VSP_002829;
Name=10; Synonyms=ISO10;
IsoId=P35922-10; Sequence=VSP_002827, VSP_002831, VSP_002830;
Name=11; Synonyms=ISO11;
IsoId=P35922-11; Sequence=VSP_002827, VSP_002832, VSP_002833;
Name=12; Synonyms=ISO12;
IsoId=P35922-12; Sequence=VSP_002827, VSP_002834, VSP_002835;
-!- TISSUE SPECIFICITY: Expressed in brain (PubMed:8033209). Strongly
expressed in the neonatal hippocampus (PubMed:15475576). Expressed
in the brainstem (PubMed:14613971). Expressed in the cerebellum
(PubMed:19193898). Expressed in neurons of hippocampal area CA3
(PubMed:17548835, PubMed:19193898). Expressed in neurons of the
olfactory bulb including the granule, mitral, tufted and
juxtaglomerular cells (PubMed:19193898). Expressed in both mature
and immature olfactory sensory neurons (OSNs) (PubMed:19193898).
Expressed in neurons in all layers and in all regions of cerebral
cortex (PubMed:19193898). Expressed in mature oligodendrocytes
(OLGs) (PubMed:23891804). Expressed in spermatogonia (at protein
level) (PubMed:16790844). Expressed predominantly in the brain
(PubMed:16000371). Expressed in testis (PubMed:8033209).
{ECO:0000269|PubMed:14613971, ECO:0000269|PubMed:15475576,
ECO:0000269|PubMed:16000371, ECO:0000269|PubMed:16790844,
ECO:0000269|PubMed:17548835, ECO:0000269|PubMed:19193898,
ECO:0000269|PubMed:23891804, ECO:0000269|PubMed:8033209}.
-!- INDUCTION: Rapidly and transiently up-regulated in response to
metabotropic glutamate receptor activation in a protein synthesis-
dependent manner in neurons (at protein level).
{ECO:0000269|PubMed:14614133, ECO:0000269|PubMed:16908410}.
-!- 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 (PubMed:14570712).
Phosphorylation at Ser-499 is required for phosphorylation of
other nearby serine residues (PubMed:14570712). Phosphorylation
has no effect on the binding of individual mRNA species, but may
affect the association with polyribosome (PubMed:14570712).
Unphosphorylated FMR1 is associated with actively translating
polyribosome, whereas a fraction of phosphorylated FMR1 is
associated with apparently stalled polyribosome (PubMed:14570712).
Dephosphorylation by an activated phosphatase may release the
FMR1-mediated translational repression and allow synthesis of a
locally required protein at snypases (PubMed:14570712).
{ECO:0000269|PubMed:14570712}.
-!- PTM: Monoubiquitinated (PubMed:16908410). Polyubiquitinated
(PubMed:16908410). Ubiquitinated and targeted for proteasomal
degradation after activation of metabotropic glutamate receptor
(mGluR) (PubMed:16908410). {ECO:0000269|PubMed:16908410}.
-!- 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}.
-!- DISRUPTION PHENOTYPE: Show normal fertility (PubMed:8033209).
Display enlarged testes and ovaries (PubMed:8033209,
PubMed:23235829). Display learning deficits and hyperactivity, in
the absence of gross pathological abnormalities of the brain
(PubMed:8033209). Display immature neurons with excess of long,
thin growth cone filopodia and dendritic filopodia and spine
protrusions with less synaptic contacts (PubMed:9144249,
PubMed:11438589, PubMed:16631377, PubMed:17417632,
PubMed:18539120). Show no increase in the number of dendritic
filopodia-spine protrusions in response to KCL-mediated
depolarization (PubMed:16631377). Display alterations in the
appearance, distribution and volume of nuclear speckles
(PubMed:24349419). Display enhanced metabotropic glutamate
receptor-dependent long-term depression (mGluR-LTD) in the
hippocampus (PubMed:11438589, PubMed:16908410, PubMed:12032354).
Leads to excessive presynaptic action potential (AP) broadening in
hippocampal and cortical neurons (PubMed:25561520). Show
alteration in the splicing pattern of its own FMR1 mRNA in the
cortex (PubMed:18653529). Alters the abundance and subcellular
distribution of a subset of mRNAs in the brain (PubMed:12575950,
PubMed:17417632). Display a reduction in the recruitment of
certain FMR1 target mRNAs in actively translating polyribosomes at
synapses (PubMed:12575950, PubMed:17507556). Display decreased
delivery of specific mRNAs into dendrites in mGluR-stimulated
neurons (PubMed:18539120). Display a delayed MAPB1 protein
expression decline in the developing hippocampus
(PubMed:15475576). Show a relief of ribosome stalling on dendritic
FMR1 target mRNAs (PubMed:21784246). Display enhanced postsynaptic
protein synthesis of a subset of FMR1 target mRNAs
(PubMed:12581522, PubMed:16908410, PubMed:19640847,
PubMed:21784246). Unable to induce postsynaptic protein synthesis
of a subset of FMR1 mRNA targets in response to mGluR activation
(PubMed:16908410, PubMed:17507556). Display enhanced presynaptic
protein synthesis of the voltage-dependent calcium channel CACNA1B
(PubMed:24709664). Display also enhanced protein synthesis of a
subset of FMR1 target mRNAs in ovaries (PubMed:23235829). Display
reduced postsynaptic protein synthesis of a subset of FMR1 target
mRNAs (PubMed:12927206, PubMed:14614133, PubMed:19640847,
PubMed:19166269, PubMed:21490210). Display reduced general protein
synthesis in synapses in response to mGluR activation
(PubMed:15548614). Show brain-region specific reduction in the
expression and/or localization of FAM206A/Simiate
(PubMed:24349419). Display similar myelin basic protein (MBP)
nexpression level in brain cerebrum than in wild-type mice
(PubMed:23891804). Display an absence of nuclear foci on meiotic
pachytene-stage chromosomes (PubMed:24813610). Show incomplete
resolution of single-strand repair intermediates, crossing over
and pairing of homologous chromosomes during meiotic prophase in a
subset of spermatocytes (PubMed:24813610).
{ECO:0000269|PubMed:11438589, ECO:0000269|PubMed:12032354,
ECO:0000269|PubMed:12575950, ECO:0000269|PubMed:12581522,
ECO:0000269|PubMed:12927206, ECO:0000269|PubMed:14614133,
ECO:0000269|PubMed:15475576, ECO:0000269|PubMed:15548614,
ECO:0000269|PubMed:16631377, ECO:0000269|PubMed:16908410,
ECO:0000269|PubMed:17417632, ECO:0000269|PubMed:17507556,
ECO:0000269|PubMed:18539120, ECO:0000269|PubMed:18653529,
ECO:0000269|PubMed:19166269, ECO:0000269|PubMed:19640847,
ECO:0000269|PubMed:21490210, ECO:0000269|PubMed:21784246,
ECO:0000269|PubMed:23235829, ECO:0000269|PubMed:23891804,
ECO:0000269|PubMed:24349419, ECO:0000269|PubMed:24709664,
ECO:0000269|PubMed:24813610, ECO:0000269|PubMed:25561520,
ECO:0000269|PubMed:8033209, ECO:0000269|PubMed:9144249}.
-!- SIMILARITY: Belongs to the FMR1 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L23971; AAA37635.1; -; mRNA.
CCDS; CCDS30171.1; -. [P35922-1]
CCDS; CCDS72385.1; -. [P35922-3]
PIR; S36173; S36173.
UniGene; Mm.3451; -.
ProteinModelPortal; P35922; -.
SMR; P35922; -.
IntAct; P35922; 7.
MINT; MINT-111096; -.
STRING; 10090.ENSMUSP00000085906; -.
iPTMnet; P35922; -.
PhosphoSitePlus; P35922; -.
MaxQB; P35922; -.
PaxDb; P35922; -.
PeptideAtlas; P35922; -.
PRIDE; P35922; -.
UCSC; uc009tiu.2; mouse. [P35922-1]
UCSC; uc009tiv.2; mouse. [P35922-11]
UCSC; uc009tiy.1; mouse. [P35922-5]
MGI; MGI:95564; Fmr1.
eggNOG; ENOG410IF9J; Eukaryota.
eggNOG; ENOG410ZDJG; LUCA.
HOGENOM; HOG000293377; -.
HOVERGEN; HBG005739; -.
InParanoid; P35922; -.
PhylomeDB; P35922; -.
ChiTaRS; Fmr1; mouse.
PRO; PR:P35922; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_FMR1; -.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
GO; GO:0015030; C:Cajal body; ISO:MGI.
GO; GO:0044297; C:cell body; ISO:MGI.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0042995; C:cell projection; ISO:MGI.
GO; GO:0010369; C:chromocenter; IDA:UniProtKB.
GO; GO:0005694; C:chromosome; IDA:UniProtKB.
GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:UniProtKB.
GO; GO:0010494; C:cytoplasmic stress granule; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0030425; C:dendrite; IDA:UniProtKB.
GO; GO:1902737; C:dendritic filopodium; IDA:UniProtKB.
GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:UniProtKB.
GO; GO:0032433; C:filopodium tip; IDA:UniProtKB.
GO; GO:0097386; C:glial cell projection; ISS:UniProtKB.
GO; GO:0030426; C:growth cone; ISS:UniProtKB.
GO; GO:1990812; C:growth cone filopodium; IDA:UniProtKB.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; ISO:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:1990124; C:messenger ribonucleoprotein complex; ISO:MGI.
GO; GO:0005845; C:mRNA cap binding complex; IDA:UniProtKB.
GO; GO:0043005; C:neuron projection; ISO:MGI.
GO; GO:0071598; C:neuronal ribonucleoprotein granule; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005844; C:polysome; IDA:UniProtKB.
GO; GO:0098794; C:postsynapse; IDA:UniProtKB.
GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0098793; C:presynapse; IDA:UniProtKB.
GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI.
GO; GO:0045202; C:synapse; IDA:UniProtKB.
GO; GO:0019034; C:viral replication complex; ISO:MGI.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0070840; F:dynein complex binding; IDA:UniProtKB.
GO; GO:0002151; F:G-quadruplex RNA binding; ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0044325; F:ion channel binding; ISO:MGI.
GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
GO; GO:0035198; F:miRNA binding; IDA:UniProtKB.
GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
GO; GO:0048027; F:mRNA 5'-UTR binding; ISS:UniProtKB.
GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
GO; GO:0034046; F:poly(G) binding; ISS:UniProtKB.
GO; GO:0008266; F:poly(U) RNA binding; ISS:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0043022; F:ribosome binding; ISO:MGI.
GO; GO:0003723; F:RNA binding; IDA:MGI.
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:MGI.
GO; GO:0030371; F:translation repressor activity; IDA:UniProtKB.
GO; GO:0008089; P:anterograde axonal transport; IMP:SynGO.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0072711; P:cellular response to hydroxyurea; IDA:UniProtKB.
GO; GO:0034644; P:cellular response to UV; IDA:UniProtKB.
GO; GO:0098586; P:cellular response to virus; ISO:MGI.
GO; GO:0007417; P:central nervous system development; IMP:MGI.
GO; GO:0060996; P:dendritic spine development; IGI:MGI.
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:MGI.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0051028; P:mRNA transport; IDA:UniProtKB.
GO; GO:2000766; P:negative regulation of cytoplasmic translation; IDA:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
GO; GO:1900453; P:negative regulation of long term synaptic depression; IMP:UniProtKB.
GO; GO:1902373; P:negative regulation of mRNA catabolic process; ISO:MGI.
GO; GO:2000301; P:negative regulation of synaptic vesicle exocytosis; ISS:UniProtKB.
GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
GO; GO:0045947; P:negative regulation of translational initiation; IDA:UniProtKB.
GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; ISS:UniProtKB.
GO; GO:0060999; P:positive regulation of dendritic spine development; IDA:UniProtKB.
GO; GO:0051491; P:positive regulation of filopodium assembly; IDA:UniProtKB.
GO; GO:2000637; P:positive regulation of gene silencing by miRNA; IDA:UniProtKB.
GO; GO:0033129; P:positive regulation of histone phosphorylation; IDA:UniProtKB.
GO; GO:1901254; P:positive regulation of intracellular transport of viral material; ISO:MGI.
GO; GO:1902416; P:positive regulation of mRNA binding; ISS:UniProtKB.
GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IDA:UniProtKB.
GO; GO:0002092; P:positive regulation of receptor internalization; ISS:UniProtKB.
GO; GO:2001022; P:positive regulation of response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0045727; P:positive regulation of translation; IMP:CACAO.
GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB.
GO; GO:0060998; P:regulation of dendritic spine development; IMP:UniProtKB.
GO; GO:0051489; P:regulation of filopodium assembly; IMP:UniProtKB.
GO; GO:0060964; P:regulation of gene silencing by miRNA; ISO:MGI.
GO; GO:1905244; P:regulation of modification of synaptic structure; IMP:SynGO.
GO; GO:0043488; P:regulation of mRNA stability; IMP:UniProtKB.
GO; GO:0098908; P:regulation of neuronal action potential; ISS:UniProtKB.
GO; GO:0046928; P:regulation of neurotransmitter secretion; ISS:UniProtKB.
GO; GO:0099578; P:regulation of translation at postsynapse, modulating synaptic transmission; IMP:SynGO.
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.
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 1 614 Synaptic functional regulator FMR1.
/FTId=PRO_0000050103.
DOMAIN 4 50 Agenet-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00973}.
DOMAIN 63 115 Agenet-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00973}.
DOMAIN 222 251 KH 1. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 285 314 KH 2. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
REGION 1 184 Required for nuclear localization.
{ECO:0000269|PubMed:8842725}.
REGION 172 211 Necessary for interaction with CYFIP1,
CYFIP2, FXR1 and FXR2.
{ECO:0000250|UniProtKB:Q06787,
ECO:0000269|PubMed:11438699}.
REGION 396 490 Required for nuclear export.
{ECO:0000250|UniProtKB:Q06787}.
REGION 418 614 Interaction with RANBP9.
{ECO:0000250|UniProtKB:Q06787}.
REGION 534 547 RNA-binding RGG-box.
MOTIF 423 442 Nuclear export signal.
{ECO:0000269|PubMed:8842725}.
MOTIF 526 533 Nucleolar localization signal 1.
{ECO:0000250|UniProtKB:Q06787}.
MOTIF 595 599 Nucleolar localization signal 2.
{ECO:0000250|UniProtKB:Q06787}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q06787}.
MOD_RES 336 336 Phosphoserine.
{ECO:0000250|UniProtKB:Q80WE1}.
MOD_RES 337 337 Phosphoserine.
{ECO:0000250|UniProtKB:Q80WE1}.
MOD_RES 349 349 Phosphoserine.
{ECO:0000250|UniProtKB:Q80WE1}.
MOD_RES 350 350 Phosphoserine.
{ECO:0000250|UniProtKB:Q80WE1}.
MOD_RES 369 369 Phosphoserine.
{ECO:0000250|UniProtKB:Q06787}.
MOD_RES 462 462 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 470 470 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 499 499 Phosphoserine.
{ECO:0000269|PubMed:14570712}.
MOD_RES 543 543 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:Q06787}.
MOD_RES 543 543 Omega-N-methylated arginine; alternate.
{ECO:0000250}.
MOD_RES 602 602 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 375 395 Missing (in isoform 7, isoform 8, isoform
9, isoform 10, isoform 11 and isoform
12). {ECO:0000305}.
/FTId=VSP_002827.
VAR_SEQ 425 512 EVDQLRLERLQIDEQLRQIGASSRPPPNRTDKEKGYVTDDG
QGMGRGSRPYRNRGHGRRGPGYTSGTNSEASNASETESDHR
DELSDW -> LQQRKRGRASCAEETDGGVEEEEEDKEEEEE
EEASKETTIIPEQIIVHVIQERLKEEQLMDPCRVPPVKGAG
CARVKIVTRRRKSQTA (in isoform 6 and
isoform 12). {ECO:0000305}.
/FTId=VSP_002834.
VAR_SEQ 425 448 EVDQLRLERLQIDEQLRQIGASSR -> ELILKHQMLLKQN
LTTETNSVIGH (in isoform 4 and isoform
10). {ECO:0000305}.
/FTId=VSP_002831.
VAR_SEQ 425 436 EVDQLRLERLQI -> NLTTETNSVIGH (in isoform
5 and isoform 11). {ECO:0000305}.
/FTId=VSP_002832.
VAR_SEQ 437 614 Missing (in isoform 5 and isoform 11).
{ECO:0000305}.
/FTId=VSP_002833.
VAR_SEQ 449 614 Missing (in isoform 4 and isoform 10).
{ECO:0000305}.
/FTId=VSP_002830.
VAR_SEQ 490 514 Missing (in isoform 3 and isoform 9).
{ECO:0000305}.
/FTId=VSP_002829.
VAR_SEQ 490 501 Missing (in isoform 2 and isoform 8).
{ECO:0000305}.
/FTId=VSP_002828.
VAR_SEQ 513 614 Missing (in isoform 6 and isoform 12).
{ECO:0000305}.
/FTId=VSP_002835.
MUTAGEN 429 434 LRLERL->ARAERA: Inhibits nuclear export.
{ECO:0000269|PubMed:8842725}.
MUTAGEN 429 431 LRL->ARA: Inhibits nuclear export.
{ECO:0000269|PubMed:8895584}.
MUTAGEN 499 499 S->A: Loss of phosphorylation.
{ECO:0000269|PubMed:14570712}.
MUTAGEN 499 499 S->D: Leads to phosphorylation on other
serine residues.
{ECO:0000269|PubMed:14570712}.
SEQUENCE 614 AA; 68989 MW; 093DD90D589ED066 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 EIMPPSSLPS NNSRVGPNSS EEKKHLDTKE
NTHFSQPNST KVQRVLVVSS IVAGGPQKPE PKAWQGMVPF VFVGTKDSIA NATVLLDYHL
NYLKEVDQLR LERLQIDEQL RQIGASSRPP PNRTDKEKGY VTDDGQGMGR GSRPYRNRGH
GRRGPGYTSG TNSEASNASE TESDHRDELS DWSLAPTEEE RESFLRRGDG RRRRGGGRGQ
GGRGRGGGFK GNDDHSRTDN RPRNPREAKG RTADGSLQSA SSEGSRLRTG KDRNQKKEKP
DSVDGLQPLV NGVP


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