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

 FMR1_HUMAN              Reviewed;         632 AA.
Q06787; A6NNH4; D3DWT0; D3DWT1; D3DWT2; G8JL90; Q16578; Q5PQZ6;
Q99054;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
27-SEP-2017, entry version 191.
RecName: Full=Synaptic functional regulator FMR1 {ECO:0000305};
AltName: Full=Fragile X mental retardation protein 1 {ECO:0000312|HGNC:HGNC:3775};
Short=FMRP {ECO:0000303|PubMed:9659908};
Short=Protein FMR-1 {ECO:0000303|PubMed:1710175};
Name=FMR1 {ECO:0000312|HGNC:HGNC:3775};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING.
TISSUE=Fetal brain;
PubMed=1710175; DOI=10.1016/0092-8674(91)90397-H;
Verkerk A.J.M.H., Pieretti M., Sutcliffe J.S., Fu Y.H., Kuhl D.P.,
Pizzuti A., Reiner O., Richards S., Victoria M.F., Zhang F.,
Eussen B.E., van Ommen G.-J.B., Blonden L.A.J., Riggins G.J.,
Chastain J.L., Kunst C.B., Galjaard H., Caskey C.T., Nelson D.L.,
Oostra B.A., Warren S.T.;
"Identification of a gene (FMR-1) containing a CGG repeat coincident
with a breakpoint cluster region exhibiting length variation in
fragile X syndrome.";
Cell 65:905-914(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), AND TISSUE SPECIFICITY.
TISSUE=Fetal brain, and Liver;
PubMed=8504300; DOI=10.1093/hmg/2.4.399;
Verkerk A.J.M.H., de Graaff E., de Boulle K., Eichler E.E.,
Konecki D.S., Reyniers E., Manca A., Poustka A., Willems P.J.,
Nelson D.L., Oostra B.A.;
"Alternative splicing in the fragile X gene FMR1.";
Hum. Mol. Genet. 2:399-404(1993).
[3]
ERRATUM.
PubMed=8401531; DOI=10.1093/hmg/2.8.1348;
Verkerk A.J.H.M., de Graaff E., de Boulle K., Eichler E.E.,
Konecki D.S., Reyniers E., Manca A., Poustka A., Willems P.J.,
Nelson D.L., Oostra B.A.;
Hum. Mol. Genet. 2:1348-1348(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 9).
TISSUE=Fetal brain;
PubMed=24722188; DOI=10.1038/ncomms4650;
Corominas R., Yang X., Lin G.N., Kang S., Shen Y., Ghamsari L.,
Broly M., Rodriguez M., Tam S., Wanamaker S.A., Fan C., Yi S.,
Tasan M., Lemmens I., Kuang X., Zhao N., Malhotra D., Michaelson J.J.,
Vacic V., Calderwood M.A., Roth F.P., Tavernier J., Horvath S.,
Salehi-Ashtiani K., Korkin D., Sebat J., Hill D.E., Hao T., Vidal M.,
Iakoucheva L.M.;
"Protein interaction network of alternatively spliced isoforms from
brain links genetic risk factors for autism.";
Nat. Commun. 5:3650-3650(2014).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34; 36-139; 141-293; 295-490
AND 492-632.
PubMed=8401496; DOI=10.1093/hmg/2.8.1147;
Eichler E.E., Richards S., Gibbs R.A., Nelson D.L.;
"Fine structure of the human FMR1 gene.";
Hum. Mol. Genet. 2:1147-1153(1993).
[9]
ERRATUM.
PubMed=8069329;
Eichler E.E., Richards S., Gibbs R.A., Nelson D.L.;
Hum. Mol. Genet. 3:684-685(1994).
[10]
SEQUENCE REVISION TO 18-34.
Eichler E.E., Richards S., Gibbs R.A., Nelson D.L.;
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
PubMed=7825604; DOI=10.1002/ajmg.1320560115;
Hirst M., Grewal P., Flannery A., Slatter R., Maher E., Barton D.,
Fryns J.-P., Davies K.;
"Two new cases of FMR1 deletion associated with mental impairment.";
Am. J. Hum. Genet. 56:67-74(1995).
[12]
RNA-BINDING, AND INVOLVEMENT IN FRAX.
PubMed=7688265; DOI=10.1016/0092-8674(93)90420-U;
Siomi H., Siomi M.C., Nussbaum R.L., Dreyfuss G.;
"The protein product of the fragile X gene, FMR1, has characteristics
of an RNA-binding protein.";
Cell 74:291-298(1993).
[13]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=8515814; DOI=10.1038/363722a0;
Verheij C., Bakker C.E., de Graaff E., Keulemans J., Willemsen R.,
Verkerk A.J.M.H., Galjaard H., Reuser A.J.J., Hoogeveen A.T.,
Oostra B.A.;
"Characterization and localization of the FMR-1 gene product
associated with fragile X syndrome.";
Nature 363:722-724(1993).
[14]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INVOLVEMENT IN FRAX.
PubMed=8401578; DOI=10.1038/ng0893-335;
Devys D., Lutz Y., Rouyer N., Bellocq J.-P., Mandel J.-L.;
"The FMR-1 protein is cytoplasmic, most abundant in neurons and
appears normal in carriers of a fragile X premutation.";
Nat. Genet. 4:335-340(1993).
[15]
ASSOCIATION IN MRNP, AND RNA-BINDING.
PubMed=7692601; DOI=10.1126/science.7692601;
Ashley C.T. Jr., Wilkinson K.D., Reines D., Warren S.T.;
"FMR1 protein: conserved RNP family domains and selective RNA
binding.";
Science 262:563-566(1993).
[16]
RNA-BINDING, AND SUBCELLULAR LOCATION.
PubMed=7781595;
Siomi M.C., Siomi H., Sauer W.H., Srinivasan S., Nussbaum R.L.,
Dreyfuss G.;
"FXR1, an autosomal homolog of the fragile X mental retardation
gene.";
EMBO J. 14:2401-2408(1995).
[17]
SUBUNIT.
PubMed=7489725;
Zhang Y., O'Connor J.P., Siomi M.C., Srinivasan S., Dutra A.,
Nussbaum R.L., Dreyfuss G.;
"The fragile X mental retardation syndrome protein interacts with
novel homologs FXR1 and FXR2.";
EMBO J. 14:5358-5366(1995).
[18]
ALTERNATIVE SPLICING (ISOFORMS 6; 9; 10 AND 11), SUBCELLULAR LOCATION
(ISOFORMS 6; 9; 10 AND 11), AND DOMAIN.
PubMed=8789445; DOI=10.1093/hmg/5.1.95;
Sittler A., Devys D., Weber C., Mandel J.L.;
"Alternative splicing of exon 14 determines nuclear or cytoplasmic
localisation of fmr1 protein isoforms.";
Hum. Mol. Genet. 5:95-102(1996).
[19]
INTERACTION WITH FXR1 AND FXR2, AND ASSOCIATION WITH RIBOSOMES.
PubMed=8668200; DOI=10.1128/MCB.16.7.3825;
Siomi M.C., Zhang Y., Siomi H., Dreyfuss G.;
"Specific sequences in the fragile X syndrome protein FMR1 and the FXR
proteins mediate their binding to 60S ribosomal subunits and the
interactions among them.";
Mol. Cell. Biol. 16:3825-3832(1996).
[20]
SUBCELLULAR LOCATION, ASSOCIATION WITH POLYRIBOSOME AND MRNP, AND
CHARACTERIZATION OF VARIANT FRAX ASN-304.
PubMed=9659908; DOI=10.1016/S1097-2765(00)80012-X;
Feng Y., Absher D., Eberhart D.E., Brown V., Malter H.E., Warren S.T.;
"FMRP associates with polyribosomes as an mRNP, and the I304N mutation
of severe fragile X syndrome abolishes this association.";
Mol. Cell 1:109-118(1997).
[21]
INVOLVEMENT IN POF1.
PubMed=9719368; DOI=10.1136/jmg.35.8.637;
Murray A., Webb J., Grimley S., Conway G., Jacobs P.;
"Studies of FRAXA and FRAXE in women with premature ovarian failure.";
J. Med. Genet. 35:637-640(1998).
[22]
SUBCELLULAR LOCATION, NUCLEOCYTOPLASMIC SHUTTLING, AND
CHARACTERIZATION OF VARIANT FRAX ASN-304.
PubMed=10196376; DOI=10.1093/hmg/8.5.863;
Tamanini F., Bontekoe C., Bakker C.E., van Unen L., Anar B.,
Willemsen R., Yoshida M., Galjaard H., Oostra B.A., Hoogeveen A.T.;
"Different targets for the fragile X-related proteins revealed by
their distinct nuclear localizations.";
Hum. Mol. Genet. 8:863-869(1999).
[23]
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).
[24]
ASSOCIATION WITH POLYRIBOSOME.
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).
[25]
RNA-BINDING, AND DOMAIN.
PubMed=11719189; DOI=10.1016/S0092-8674(01)00566-9;
Darnell J.C., Jensen K.B., Jin P., Brown V., Warren S.T.,
Darnell R.B.;
"Fragile X mental retardation protein targets G quartet mRNAs
important for neuronal function.";
Cell 107:489-499(2001).
[26]
FUNCTION, RNA-BINDING, AND DOMAIN.
PubMed=11532944; DOI=10.1093/emboj/20.17.4803;
Schaeffer C., Bardoni B., Mandel J.L., Ehresmann B., Ehresmann C.,
Moine H.;
"The fragile X mental retardation protein binds specifically to its
mRNA via a purine quartet motif.";
EMBO J. 20:4803-4813(2001).
[27]
FUNCTION, INTERACTION WITH FXR1 AND FXR2, SUBUNIT, RNA-BINDING, AND
CHARACTERIZATION OF VARIANT FRAX ASN-304.
PubMed=11157796; DOI=10.1093/hmg/10.4.329;
Laggerbauer B., Ostareck D., Keidel E.M., Ostareck-Lederer A.,
Fischer U.;
"Evidence that fragile X mental retardation protein is a negative
regulator of translation.";
Hum. Mol. Genet. 10:329-338(2001).
[28]
SUBCELLULAR LOCATION.
PubMed=12417734; DOI=10.1128/MCB.22.23.8332-8341.2002;
De Diego Otero Y., Severijnen L.A., van Cappellen G., Schrier M.,
Oostra B., Willemsen R.;
"Transport of fragile X mental retardation protein via granules in
neurites of PC12 cells.";
Mol. Cell. Biol. 22:8332-8341(2002).
[29]
PHOSPHORYLATION AT SER-500, AND MUTAGENESIS OF SER-500.
PubMed=12446764; DOI=10.1128/MCB.22.24.8438-8447.2002;
Siomi M.C., Higashijima K., Ishizuka A., Siomi H.;
"Casein kinase II phosphorylates the fragile X mental retardation
protein and modulates its biological properties.";
Mol. Cell. Biol. 22:8438-8447(2002).
[30]
SUBUNIT, RNA-BINDING, AND DOMAIN.
PubMed=12950170; DOI=10.1021/bi034909g;
Adinolfi S., Ramos A., Martin S.R., Dal Piaz F., Pucci P., Bardoni B.,
Mandel J.L., Pastore A.;
"The N-terminus of the fragile X mental retardation protein contains a
novel domain involved in dimerization and RNA binding.";
Biochemistry 42:10437-10444(2003).
[31]
INTERACTION WITH NUFIP2, AND SUBCELLULAR LOCATION.
PubMed=12837692; DOI=10.1093/hmg/ddg181;
Bardoni B., Castets M., Huot M.-E., Schenck A., Adinolfi S.,
Corbin F., Pastore A., Khandjian E.W., Mandel J.-L.;
"82-FIP, a novel FMRP (fragile X mental retardation protein)
interacting protein, shows a cell cycle-dependent intracellular
localization.";
Hum. Mol. Genet. 12:1689-1698(2003).
[32]
INTERACTION WITH FXR1, SUBCELLULAR LOCATION, PHOSPHORYLATION, DOMAIN,
AND MUTAGENESIS OF SER-500.
PubMed=14532325; DOI=10.1093/hmg/ddg335;
Mazroui R., Huot M.E., Tremblay S., Boilard N., Labelle Y.,
Khandjian E.W.;
"Fragile X Mental Retardation protein determinants required for its
association with polyribosomal mRNPs.";
Hum. Mol. Genet. 12:3087-3096(2003).
[33]
FUNCTION, RNA-BINDING, AND ASSOCIATION WITH POLYRIBOSOME.
PubMed=12594214; DOI=10.1074/jbc.M211117200;
Sung Y.J., Dolzhanskaya N., Nolin S.L., Brown T., Currie J.R.,
Denman R.B.;
"The fragile X mental retardation protein FMRP binds elongation factor
1A mRNA and negatively regulates its translation in vivo.";
J. Biol. Chem. 278:15669-15678(2003).
[34]
FUNCTION, 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).
[35]
RNA-BINDING.
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).
[36]
INTERACTION WITH IGF2BP1, AND RNA-BINDING.
PubMed=15282548; DOI=10.1038/sj.emboj.7600341;
Rackham O., Brown C.M.;
"Visualization of RNA-protein interactions in living cells: FMRP and
IMP1 interact on mRNAs.";
EMBO J. 23:3346-3355(2004).
[37]
RNA-BINDING, INTERACTION WITH RANBP9, SUBCELLULAR LOCATION, AND
DOMAIN.
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).
[38]
FUNCTION, ASSOCIATION WITH MICRORNA, AND INTERACTION WITH AGO2.
PubMed=14703574; DOI=10.1038/nn1174;
Jin P., Zarnescu D.C., Ceman S., Nakamoto M., Mowrey J., Jongens T.A.,
Nelson D.L., Moses K., Warren S.T.;
"Biochemical and genetic interaction between the fragile X mental
retardation protein and the microRNA pathway.";
Nat. Neurosci. 7:113-117(2004).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[40]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[41]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[42]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[43]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-500, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[44]
CHARACTERIZATION OF VARIANT FRAX ASN-304, RNA-BINDING, AND DOMAIN.
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).
[45]
METHYLATION AT ARG-544, AND MUTAGENESIS OF ARG-544 AND ARG-546.
PubMed=16922515; DOI=10.1021/bi0525019;
Dolzhanskaya N., Merz G., Denman R.B.;
"Alternative splicing modulates protein arginine methyltransferase-
dependent methylation of fragile X syndrome mental retardation
protein.";
Biochemistry 45:10385-10393(2006).
[46]
INTERACTION WITH MCRS1, ASSOCIATION WITH POLYRIBOSOME, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF SER-500.
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).
[47]
FUNCTION, RNA-BINDING, AND DOMAIN.
PubMed=17057366; DOI=10.1155/JBB/2006/64347;
Plante I., Davidovic L., Ouellet D.L., Gobeil L.A., Tremblay S.,
Khandjian E.W., Provost P.;
"Dicer-derived microRNAs are utilized by the fragile X mental
retardation protein for assembly on target RNAs.";
J. Biomed. Biotechnol. 2006:64347-64347(2006).
[48]
METHYLATION, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=16636078; DOI=10.1242/jcs.02882;
Dolzhanskaya N., Merz G., Aletta J.M., Denman R.B.;
"Methylation regulates the intracellular protein-protein and protein-
RNA interactions of FMRP.";
J. Cell Sci. 119:1933-1946(2006).
[49]
FUNCTION.
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).
[50]
RNA-BINDING.
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).
[51]
INTERACTION WITH TDRD3, AND SUBCELLULAR LOCATION.
PubMed=18632687; DOI=10.1093/hmg/ddn203;
Goulet I., Boisvenue S., Mokas S., Mazroui R., Cote J.;
"TDRD3, a novel Tudor domain-containing protein, localizes to
cytoplasmic stress granules.";
Hum. Mol. Genet. 17:3055-3074(2008).
[52]
SUBUNIT, INTERACTION WITH TDRD3, SUBCELLULAR LOCATION, AND
CHARACTERIZATION OF VARIANT FRAX ASN-304.
PubMed=18664458; DOI=10.1093/hmg/ddn219;
Linder B., Ploettner O., Kroiss M., Hartmann E., Laggerbauer B.,
Meister G., Keidel E., Fischer U.;
"Tdrd3 is a novel stress granule-associated protein interacting with
the Fragile-X syndrome protein FMRP.";
Hum. Mol. Genet. 17:3236-3246(2008).
[53]
INTERACTION WITH SMN, ASSOCIATION WITH THE SMN CORE COMPLEX,
SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANT FRAX ASN-304.
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).
[54]
FUNCTION, AND RNA-BINDING.
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).
[55]
RNA-BINDING, AND DOMAIN.
PubMed=18579868; DOI=10.1261/rna.1100708;
Menon L., Mader S.A., Mihailescu M.R.;
"Fragile X mental retardation protein interactions with the
microtubule associated protein 1B RNA.";
RNA 14:1644-1655(2008).
[56]
FUNCTION, RNA-BINDING, AND ASSOCIATION WITH POLYRIBOSOME AND MRNP.
PubMed=19097999; DOI=10.1074/jbc.M807354200;
Faehling M., Mrowka R., Steege A., Kirschner K.M., Benko E.,
Foerstera B., Persson P.B., Thiele B.J., Meier J.C., Scholz H.;
"Translational regulation of the human achaete-scute homologue-1 by
fragile X mental retardation protein.";
J. Biol. Chem. 284:4255-4266(2009).
[57]
INTERACTION WITH NXF1, RNA-BINDING, AND SUBCELLULAR LOCATION.
PubMed=18936162; DOI=10.1128/MCB.01377-08;
Kim M., Bellini M., Ceman S.;
"Fragile X mental retardation protein FMRP binds mRNAs in the
nucleus.";
Mol. Cell. Biol. 29:214-228(2009).
[58]
FUNCTION, RNA-BINDING, AND DOMAIN.
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).
[59]
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).
[60]
FUNCTION, RNA-BINDING, AND CHARACTERIZATION OF VARIANT FRAX ASN-304.
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).
[61]
LACK OF FUNCTION, 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).
[62]
FUNCTION (ISOFORMS 6 AND 10), SUBCELLULAR LOCATION (ISOFORMS 6; 9; 10
AND 11), PROTEOLYTIC PROCESSING (ISOFORM 10), RNA-BINDING (ISOFORMS 6
AND 10), DOMAIN (ISOFORM 10), TISSUE SPECIFICITY, AND CHARACTERIZATION
OF VARIANT FRAX ASN-304 (ISOFORM 10).
PubMed=24204304; DOI=10.1371/journal.pgen.1003890;
Dury A.Y., El Fatimy R., Tremblay S., Rose T.M., Cote J.,
De Koninck P., Khandjian E.W.;
"Nuclear Fragile X Mental Retardation Protein is localized to Cajal
bodies.";
PLoS Genet. 9:E1003890-E1003890(2013).
[63]
FUNCTION, INTERACTION WITH METHYLATED HISTONE H3, DOMAIN,
CHARACTERIZATION OF VARIANT FRAX GLN-138, AND MUTAGENESIS OF THR-102
AND TYR-103.
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).
[64]
FUNCTION, INTERACTION WITH MOV10, AND RNA-BINDING.
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).
[65]
FUNCTION (MICROBIAL INFECTION), INTERACTION WITH INFLUENZA A NP
(MICROBIAL INFECTION), CHARACTERIZATION OF VARIANT FRAX ASN-304
(MICROBIAL INFECTION), AND INDUCTION (MICROBIAL INFECTION).
PubMed=24514761; DOI=10.1038/ncomms4259;
Zhou Z., Cao M., Guo Y., Zhao L., Wang J., Jia X., Li J., Wang C.,
Gabriel G., Xue Q., Yi Y., Cui S., Jin Q., Wang J., Deng T.;
"Fragile X mental retardation protein stimulates ribonucleoprotein
assembly of influenza A virus.";
Nat. Commun. 5:3259-3259(2014).
[66]
INTERACTION WITH CYFIP2; EIF5; NCL AND RPLP0 (ISOFORM 6), SUBCELLULAR
LOCATION, DOMAIN, AND MUTAGENESIS OF 527-ARG--ARG-534 AND
613-GLN--LYS-617.
PubMed=24658146; DOI=10.1371/journal.pone.0091465;
Taha M.S., Nouri K., Milroy L.G., Moll J.M., Herrmann C.,
Brunsveld L., Piekorz R.P., Ahmadian M.R.;
"Subcellular fractionation and localization studies reveal a direct
interaction of the fragile X mental retardation protein (FMRP) with
nucleolin.";
PLoS ONE 9:E91465-E91465(2014).
[67]
RNA-BINDING, DOMAIN, AND MUTAGENESIS OF SER-500.
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).
[68]
STRUCTURE BY NMR OF 216-280.
PubMed=9302998; DOI=10.1038/nsb0997-712;
Musco G., Kharrat A., Stier G., Fraternali F., Gibson T.J., Nilges M.,
Pastore A.;
"The solution structure of the first KH domain of FMR1, the protein
responsible for the fragile X syndrome.";
Nat. Struct. Biol. 4:712-716(1997).
[69]
STRUCTURE BY NMR OF 1-134, MUTAGENESIS OF 125-THR-PHE-126, SUBCELLULAR
LOCATION, AND INTERACTION WITH NUFIP2.
PubMed=16407062; DOI=10.1016/j.str.2005.09.018;
Ramos A., Hollingworth D., Adinolfi S., Castets M., Kelly G.,
Frenkiel T.A., Bardoni B., Pastore A.;
"The structure of the N-terminal domain of the fragile X mental
retardation protein: a platform for protein-protein interaction.";
Structure 14:21-31(2006).
[70]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 397-425, AND CHARACTERIZATION
OF VARIANT FRAX ASN-304.
PubMed=17850748; DOI=10.1016/j.str.2007.06.022;
Valverde R., Pozdnyakova I., Kajander T., Venkatraman J., Regan L.;
"Fragile X mental retardation syndrome: structure of the KH1-KH2
domains of fragile X mental retardation protein.";
Structure 15:1090-1098(2007).
[71]
VARIANT FRAX ASN-304.
PubMed=8490650; DOI=10.1038/ng0193-31;
de Boulle K., Verkerk A.J.M.H., Reyniers E., Vits L., Hendrickx J.,
van Roy B., van den Bos F., de Graaff E., Oostra B.A., Willems P.J.;
"A point mutation in the FMR-1 gene associated with fragile X mental
retardation.";
Nat. Genet. 3:31-35(1993).
[72]
CHARACTERIZATION OF VARIANT FRAX ASN-304, AND RNA-BINDING.
PubMed=8156595; DOI=10.1016/0092-8674(94)90232-1;
Siomi H., Choi M., Siomi M.C., Nussbaum R.L., Dreyfuss G.;
"Essential role for KH domains in RNA binding: impaired RNA binding by
a mutation in the KH domain of FMR1 that causes fragile X syndrome.";
Cell 77:33-39(1994).
[73]
CHARACTERIZATION OF VARIANT FRAX ASN-304.
PubMed=7633450; DOI=10.1093/hmg/4.5.895;
Verheij C., de Graaff E., Bakker C.E., Willemsen R., Willems P.J.,
Meijer N., Galjaard H., Reuser A.J.J., Oostra B.A., Hoogeveen A.T.;
"Characterization of FMR1 proteins isolated from different tissues.";
Hum. Mol. Genet. 4:895-901(1995).
[74]
VARIANT HIS-546.
PubMed=9375856;
DOI=10.1002/(SICI)1098-1004(1997)10:5<393::AID-HUMU10>3.0.CO;2-V;
Wang Y.-C., Lin M.-L., Lin S.J., Li Y.-C., Li S.-Y.;
"Novel point mutation within intron 10 of FMR-1 gene causing fragile X
syndrome.";
Hum. Mutat. 10:393-399(1997).
[75]
INVOLVEMENT IN FXTAS.
PubMed=11445641; DOI=10.1212/WNL.57.1.127;
Hagerman R.J., Leehey M., Heinrichs W., Tassone F., Wilson R.,
Hills J., Grigsby J., Gage B., Hagerman P.J.;
"Intention tremor, parkinsonism, and generalized brain atrophy in male
carriers of fragile X.";
Neurology 57:127-130(2001).
[76]
CHARACTERIZATION OF VARIANT FRAX ASN-304, INTERACTION WITH FXR1 AND
RPLP0, AND SUBCELLULAR LOCATION.
PubMed=15380484; DOI=10.1016/j.expneurol.2004.05.039;
Schrier M., Severijnen L.A., Reis S., Rife M., van't Padje S.,
van Cappellen G., Oostra B.A., Willemsen R.;
"Transport kinetics of FMRP containing the I304N mutation of severe
fragile X syndrome in neurites of living rat PC12 cells.";
Exp. Neurol. 189:343-353(2004).
[77]
VARIANT GLN-138.
PubMed=20799337; DOI=10.1002/ajmg.a.33626;
Collins S.C., Bray S.M., Suhl J.A., Cutler D.J., Coffee B.,
Zwick M.E., Warren S.T.;
"Identification of novel FMR1 variants by massively parallel
sequencing in developmentally delayed males.";
Am. J. Med. Genet. A 152:2512-2520(2010).
[78]
VARIANT FRAX GLU-266, CHARACTERIZATION OF VARIANT FRAX GLU-266,
RNA-BINGING, AND ASSOCIATION WITH POLYRIBOSOME.
PubMed=24448548; DOI=10.1038/ejhg.2013.311;
Myrick L.K., Nakamoto-Kinoshita M., Lindor N.M., Kirmani S., Cheng X.,
Warren S.T.;
"Fragile X syndrome due to a missense mutation.";
Eur. J. Hum. Genet. 22:1185-1189(2014).
[79]
VARIANT FRAX GLN-138, CHARACTERIZATION OF VARIANT FRAX GLN-138,
FUNCTION, INTERACTION WITH KCNMB4, AND DOMAIN.
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:16631377, PubMed:18653529, PubMed:19166269,
PubMed:23235829, PubMed:25464849). Plays a role in the alternative
splicing of its own mRNA (PubMed:18653529). Plays a role in mRNA
nuclear export (By similarity). Together with export factor NXF2,
is involved in the regulation of the NXF1 mRNA stability in
neurons (By similarity). Stabilizes the scaffolding postsynaptic
density protein DLG4/PSD-95 and the myelin basic protein (MBP)
mRNAs in hippocampal neurons and glial cells, respectively; this
stabilization is further increased in response to metabotropic
glutamate receptor (mGluR) stimulation (By similarity). Plays a
role in selective delivery of a subset of dendritic mRNAs to
synaptic sites in response to mGluR activation in a kinesin-
dependent manner (By similarity). Plays a role as a repressor of
mRNA translation during the transport of dendritic mRNAs to
postnyaptic dendritic spines (PubMed:11532944, PubMed:11157796,
PubMed:12594214, PubMed:23235829). Component of the CYFIP1-EIF4E-
FMR1 complex which blocks cap-dependent mRNA translation
initiation (By similarity). Represses mRNA translation by stalling
ribosomal translocation during elongation (By similarity). Reports
are contradictory with regards to its ability to mediate
translation inhibition of MBP mRNA in oligodendrocytes
(PubMed:23891804). Also involved in the recruitment of the RNA
helicase MOV10 to a subset of mRNAs and hence regulates microRNA
(miRNA)-mediated translational repression by AGO2
(PubMed:14703574, PubMed:17057366, PubMed:25464849). Facilitates
the assembly of miRNAs on specific target mRNAs (PubMed:17057366).
Plays also a role as an activator of mRNA translation of a subset
of dendritic mRNAs at synapses (PubMed:19097999, PubMed:19166269).
In response to mGluR stimulation, FMR1-target mRNAs are rapidly
derepressed, allowing for local translation at synapses (By
similarity). Binds to a large subset of dendritic mRNAs that
encode a myriad of proteins involved in pre- and postsynaptic
functions (PubMed:7692601, PubMed:11719189, PubMed:11157796,
PubMed:12594214, PubMed:17417632, PubMed:23235829,
PubMed:24448548). Binds to 5'-ACU[GU]-3' and/or 5'-[AU]GGA-3' RNA
consensus sequences within mRNA targets, mainly at coding sequence
(CDS) and 3'-untranslated region (UTR) and less frequently at 5'-
UTR (PubMed:23235829). Binds to intramolecular G-quadruplex
structures in the 5'- or 3'-UTRs of mRNA targets (PubMed:11719189,
PubMed:18579868, PubMed:25464849, PubMed:25692235). Binds to G-
quadruplex structures in the 3'-UTR of its own mRNA
(PubMed:7692601, PubMed:11532944, PubMed:12594214,
PubMed:15282548, PubMed:18653529). Binds also to RNA ligands
harboring a kissing complex (kc) structure; this binding may
mediate the association of FMR1 with polyribosomes
(PubMed:15805463). Binds mRNAs containing U-rich target sequences
(PubMed:12927206). Binds to a triple stem-loop RNA structure,
called Sod1 stem loop interacting with FMRP (SoSLIP), in the 5'-
UTR region of superoxide dismutase SOD1 mRNA (PubMed:19166269).
Binds to the dendritic, small non-coding brain cytoplasmic RNA 1
(BC1); which may increase the association of the CYFIP1-EIF4E-FMR1
complex to FMR1 target mRNAs at synapses (By similarity).
Associates with export factor NXF1 mRNA-containing
ribonucleoprotein particles (mRNPs) in a NXF2-dependent manner (By
similarity). Binds to a subset of miRNAs in the brain
(PubMed:14703574, PubMed:17057366). May associate with nascent
transcripts in a nuclear protein NXF1-dependent manner
(PubMed:18936162). In vitro, binds to RNA homopolymer;
preferentially on poly(G) and to a lesser extent on poly(U), but
not on poly(A) or poly(C) (PubMed:7688265, PubMed:7781595,
PubMed:12950170, PubMed:15381419, PubMed:8156595). Moreover, plays
a role in the modulation of the sodium-activated potassium channel
KCNT1 gating activity (PubMed:20512134). Negatively regulates the
voltage-dependent calcium channel current density in soma and
presynaptic terminals of dorsal root ganglion (DRG) neurons, and
hence regulates synaptic vesicle exocytosis (By similarity).
Modulates the voltage-dependent calcium channel CACNA1B expression
at the plasma membrane by targeting the channels for proteosomal
degradation (By similarity). Plays a role in regulation of MAP1B-
dependent microtubule dynamics during neuronal development (By
similarity). Recently, has been shown to play a translation-
independent role in the modulation of presynaptic action potential
(AP) duration and neurotransmitter release via large-conductance
calcium-activated potassium (BK) channels in hippocampal and
cortical excitatory neurons (PubMed:25561520). Finally, FMR1 may
be involved in the control of DNA damage response (DDR) mechanisms
through the regulation of ATR-dependent signaling pathways such as
histone H2AFX/H2A.x and BRCA1 phosphorylations (PubMed:24813610).
{ECO:0000250|UniProtKB:P35922, ECO:0000250|UniProtKB:Q80WE1,
ECO:0000269|PubMed:11157796, ECO:0000269|PubMed:11532944,
ECO:0000269|PubMed:11719189, 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:7688265, ECO:0000269|PubMed:7692601,
ECO:0000269|PubMed:7781595, ECO:0000269|PubMed:8156595}.
-!- FUNCTION: Isoform 10: binds to RNA homopolymer; preferentially on
poly(G) and to a lesser extent on poly(U), but not on poly(A) or
poly(C) (PubMed:24204304). May bind to RNA in Cajal bodies
(PubMed:24204304). {ECO:0000269|PubMed:24204304}.
-!- FUNCTION: Isoform 6: binds to RNA homopolymer; preferentially on
poly(G) and to a lesser extent on poly(U), but not on poly(A) or
poly(C) (PubMed:24204304). May bind to RNA in Cajal bodies
(PubMed:24204304). {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}.
-!- SUBUNIT: Homodimer (PubMed:7489725, PubMed:12950170,
PubMed:16636078). Forms heterodimer with FXR1; heterodimerization
occurs in a methylation-dependent manner (PubMed:7489725,
PubMed:11157796, PubMed:16636078). Forms heterodimer with FXR2
(PubMed:7489725, PubMed:11157796). Homooligomer (PubMed:11157796,
PubMed:18664458). Component of the CYFIP1-EIF4E-FMR1 complex at
least composed of CYFIP, EIF4E and FMR1; this mRNA cap binding
complex formation increases in presence of the brain cytoplasmic
RNA BC1 and is dynamically regulated in an activity-dependent
manner to repress and then possibly release dendritic mRNAs for
translation in response to mGluR stimulation (By similarity).
Associates with the SMN core complex that contains SMN,
GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8
and STRAP/UNRIP (PubMed:18093976). Part of a ribonucleoprotein
complex with AGO2/EIF2C2 and miRNAs (PubMed:14703574). Interacts
with AGO2/EIF2C2 (PubMed:14703574). Interacts (via C-terminus)
with CACNA1B; this interaction induces a deacrease in the number
of presynaptic functional CACNA1B channels at the cell surface (By
similarity). Interacts with CYFIP1; this interaction recruits
CYFIP1 to capped mRNA (By similarity). Interacts with CYFIP2 (By
similarity). Interacts with EIF5; this interaction occurs in a
RNA-dependent manner (By similarity). Interacts with dynein (By
similarity). Interacts with FXR1 and FXR2 (PubMed:8668200,
PubMed:14532325, PubMed:15380484). Interacts with methylated
histone H3 (PubMed:24813610). Interacts with IGF2BP1; this
interaction allows to recruit IGF2BP1 to mRNA in a FMR1-dependent
manner (PubMed:15282548). Interacts (via N-terminus) with KCNMB4
(PubMed:25561520). Interacts with KCNT1 (via C-terminus); this
interaction alters gating properties of KCNT1 (PubMed:20512134).
Interacts (via phosphorylated form) with MCRS1 (via N-terminus)
(PubMed:16571602). Interacts with MOV10; this interaction is
direct, occurs in an RNA-dependent manner on polysomes and induces
association of MOV10 with RNAs (PubMed:25464849). Interacts with
MYO5A and PURA; these interactions occur in association with
polyribosome (By similarity). Interacts with NCL (By similarity).
Interacts with NUFIP1 (PubMed:10556305). Interacts (via N-
terminus) with NUFIP2 (PubMed:12837692, PubMed:16407062).
Interacts with NXF1; this interaction occurs in a mRNA-dependent
and polyribosome-independent manner in the nucleus
(PubMed:18936162). Interacts with NXF2 (via N-terminus); this
interaction is direct and occurs in a NXF1 mRNA-containing mRNP
complexes (By similarity). Interacts with RANBP9 (via C-terminus);
this interaction is direct and inhibits binding of FMR1 to RNA
homopolymer (PubMed:15381419). Interacts with RPLP0
(PubMed:15380484). Interacts (via C-terminus) with SMN (via C-
terminus); this interaction is direct and occurs in a RNA-
independent manner (PubMed:18093976). Interacts with TDRD3 (via C-
terminus); this interaction is direct (PubMed:18632687,
PubMed:18664458). Interacts with YBX1; this interaction occurs in
association with polyribosome (By similarity). Interacts with
nucleosome (PubMed:24813610). Associates with polyribosome; this
association occurs in a mRNA-dependent manner (PubMed:9659908,
PubMed:11719188, PubMed:12594214, PubMed:19097999,
PubMed:24448548). Associates with cytoplasmic messenger
ribonucleoprotein particles (mRNPs) (PubMed:7692601,
PubMed:9659908, PubMed:12575950, PubMed:19097999). Associates with
microtubules in a kinesin- and dynein-dependent manner (By
similarity). Isoform 6 interacts (via N-terminus) with NCL (via C-
terminus) (PubMed:24658146). Isoform 6 interacts with CYFIP2; this
interaction occurs in a RNA-dependent manner (PubMed:24658146).
Isoform 6 interacts with EIF5; this interaction occurs in a RNA-
dependent manner (PubMed:24658146). Isoform 6 interacts with RPLP0
(PubMed:24658146). {ECO:0000250|UniProtKB:P35922,
ECO:0000269|PubMed:10556305, ECO:0000269|PubMed:11157796,
ECO:0000269|PubMed:11719188, ECO:0000269|PubMed:12575950,
ECO:0000269|PubMed:12594214, ECO:0000269|PubMed:12837692,
ECO:0000269|PubMed:12950170, ECO:0000269|PubMed:14532325,
ECO:0000269|PubMed:14703574, ECO:0000269|PubMed:15282548,
ECO:0000269|PubMed:15380484, ECO:0000269|PubMed:15381419,
ECO:0000269|PubMed:16407062, ECO:0000269|PubMed:16571602,
ECO:0000269|PubMed:16636078, ECO:0000269|PubMed:18093976,
ECO:0000269|PubMed:18632687, ECO:0000269|PubMed:18664458,
ECO:0000269|PubMed:18936162, ECO:0000269|PubMed:19097999,
ECO:0000269|PubMed:20512134, ECO:0000269|PubMed:24448548,
ECO:0000269|PubMed:24658146, ECO:0000269|PubMed:24813610,
ECO:0000269|PubMed:25464849, ECO:0000269|PubMed:25561520,
ECO:0000269|PubMed:7489725, ECO:0000269|PubMed:7692601,
ECO:0000269|PubMed:8668200, ECO:0000269|PubMed:9659908}.
-!- SUBUNIT: (Microbial infection) Interacts (via KH 2 domain) with
influenza A nucleoprotein (NP); this interaction occurs in a RNA-
dependent manner and stimulates viral ribonucleoprotein (vRNP)
assembly and subsequent RNA synthesis.
{ECO:0000269|PubMed:24514761}.
-!- INTERACTION:
Q7L576:CYFIP1; NbExp=4; IntAct=EBI-366305, EBI-1048143;
Q96F07:CYFIP2; NbExp=2; IntAct=EBI-366305, EBI-2433893;
A1L4K1:FSD2; NbExp=3; IntAct=EBI-10224470, EBI-5661036;
P51116:FXR2; NbExp=3; IntAct=EBI-10224470, EBI-740459;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10196376,
ECO:0000269|PubMed:16571602, ECO:0000269|PubMed:18936162}.
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}. 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:9659908}.
Cytoplasm, perinuclear region {ECO:0000269|PubMed:24658146}.
Cytoplasmic granule {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}.
Perikaryon {ECO:0000269|PubMed:12417734,
ECO:0000269|PubMed:15380484, ECO:0000269|PubMed:18093976}. Cell
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}. Cell junction,
synapse, synaptosome {ECO:0000250|UniProtKB:P35922}. Cell
projection, growth cone {ECO:0000269|PubMed:15380484}. Cell
projection, filopodium tip {ECO:0000250|UniProtKB:P35922}. Cell
junction, synapse {ECO:0000250|UniProtKB:P35922}. Cell junction,
synapse, postsynaptic cell membrane
{ECO:0000250|UniProtKB:P35922}. 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 (PubMed:10196376). Localizes to
cytoplasmic granules, also referred to as messenger
ribonucleoprotein particles or mRNPs, along dendrites and
dendritic spines (PubMed:9659908, PubMed:14532325). 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 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 (PubMed:12417734,
PubMed:18093976, PubMed:16636078). 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:18632687, PubMed:18664458,
PubMed:16636078). {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: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}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=11;
Comment=At least 12 different isoforms are produced.;
Name=6;
IsoId=Q06787-1; Sequence=Displayed;
Name=1;
IsoId=Q06787-2; Sequence=VSP_002823, VSP_002826;
Name=2;
IsoId=Q06787-3; Sequence=VSP_002824;
Name=3;
IsoId=Q06787-4; Sequence=VSP_002824, VSP_002826;
Name=4;
IsoId=Q06787-5; Sequence=VSP_002825;
Name=5;
IsoId=Q06787-6; Sequence=VSP_002825, VSP_002826;
Name=7;
IsoId=Q06787-7; Sequence=VSP_002826;
Name=8;
IsoId=Q06787-8; Sequence=VSP_002823, VSP_002825;
Name=9; Synonyms=B;
IsoId=Q06787-9; Sequence=VSP_002823;
Name=10; Synonyms=ISO6 {ECO:0000303|PubMed:8789445};
IsoId=Q06787-10; Sequence=VSP_058423;
Name=11; Synonyms=ISO12 {ECO:0000303|PubMed:8789445};
IsoId=Q06787-11; Sequence=VSP_002823, VSP_058423;
-!- TISSUE SPECIFICITY: Expressed in the brain, cerebellum and testis
(PubMed:8401578). Also expressed in epithelial tissues
(PubMed:8401578). Expressed in mature oligodendrocytes (OLGs)
(PubMed:23891804). Expressed in fibroblast (PubMed:24204304).
Expressed in neurons, Purkinje cells and spermatogonias (at
protein level) (PubMed:8401578). Expressed in brain, testis and
placenta (PubMed:8504300). Expressed in neurons and lymphocytes
(PubMed:8504300). {ECO:0000269|PubMed:23891804,
ECO:0000269|PubMed:24204304, ECO:0000269|PubMed:8401578,
ECO:0000269|PubMed:8504300}.
-!- INDUCTION: (Microbial infection) Up-regulated in response to
infection by influenza A virus. {ECO:0000269|PubMed:24514761}.
-!- DOMAIN: The N-terminal 134 amino acids are necessary for
homodimerization and RNA-binding (PubMed:12950170). The N-terminal
298 amino acids are sufficient to interact with KCNMB4 and to
regulate presynaptic action potential (AP) duration in neurons
(PubMed:25561520). The two agenet-like domains are necessary for
binding to histone H3 in a methylation-dependent manner
(PubMed:24813610). The KH domains are necessary for mediating
miRNA annealing to specific RNA targets (PubMed:17057366). The KH
2 domain is necessary for binding to kissing complex (kc) RNA
ligands (PubMed:15805463). The RGG box domain is necessary for
binding to mRNA targets that contain G-quadruplex structures
(PubMed:11719189, PubMed:18579868, PubMed:25692235). The RGG-box
domain is necessary for binding to a triple stem-loop RNA
structure, called Sod1 stem loop interacting with FMRP (SoSLIP),
in the superoxide dismutase SOD1 mRNA (PubMed:19166269). The RGG
box domain is necessary for binding to its own mRNA
(PubMed:11532944). The RGG-box domain is necessary for binding to
homopolymer poly(G) (PubMed:14532325).
{ECO:0000269|PubMed:11532944, ECO:0000269|PubMed:11719189,
ECO:0000269|PubMed:12950170, ECO:0000269|PubMed:14532325,
ECO:0000269|PubMed:15805463, ECO:0000269|PubMed:17057366,
ECO:0000269|PubMed:18579868, ECO:0000269|PubMed:19166269,
ECO:0000269|PubMed:24813610, ECO:0000269|PubMed:25561520,
ECO:0000269|PubMed:25692235}.
-!- DOMAIN: Isoform 10: The C-terminal region contains a Cajal body
localization signal at positions 490 through 506
(PubMed:24204304). {ECO:0000269|PubMed:24204304}.
-!- PTM: Phosphorylated (PubMed:14532325). Phosphorylated on several
serine residues. Phosphorylation at Ser-500 is required for
phosphorylation of other nearby serine residues. Phosphorylation
has no effect on the binding of individual mRNA species, but may
affect the association with polyribosome. Unphosphorylated FMR1 is
associated with actively translating polyribosome, whereas a
fraction of phosphorylated FMR1 is associated with apparently
stalled polyribosome. Dephosphorylation by an activated
phosphatase may release the FMR1-mediated translational repression
and allow synthesis of a locally required protein at snypases (By
similarity). {ECO:0000250|UniProtKB:P35922,
ECO:0000269|PubMed:14532325}.
-!- 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 (PubMed:16636078).
Methylated by PRMT1, PRMT3 and PRMT4, in vitro (PubMed:16922515).
{ECO:0000269|PubMed:16636078, ECO:0000269|PubMed:16922515}.
-!- PTM: Isoform 10: Undergoes proteolytic cleavage; may be
specifically cleaved by calpain-1/CAPN1 in cajal bodies
(PubMed:24204304). {ECO:0000269|PubMed:24204304}.
-!- DISEASE: Fragile X syndrome (FRAX) [MIM:300624]: Common genetic
disease (has a prevalence of one in every 2000 children) which is
characterized by moderate to severe mental retardation,
macroorchidism (enlargement of the testicles), large ears,
prominent jaw, and high-pitched, jocular speech. The defect in
most fragile X syndrome patients results from an amplification of
a CGG repeat region which is directly in front of the coding
region. {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: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
mutations affecting the gene represented in this entry.
-!- DISEASE: Fragile X tremor/ataxia syndrome (FXTAS) [MIM:300623]: In
FXTAS, the expanded repeats range in size from 55 to 200 repeats
and are referred to as 'premutations'. Full repeat expansions with
greater than 200 repeats results in fragile X mental retardation
syndrome [MIM:300624]. Carriers of the premutation typically do
not show the full fragile X syndrome phenotype, but comprise a
subgroup that may have some physical features of fragile X
syndrome or mild cognitive and emotional problems.
{ECO:0000269|PubMed:11445641}. Note=The disease is caused by
mutations 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 mutations affecting the gene
represented in this entry.
-!- MISCELLANEOUS: The mechanism of the severe phenotype in the Asn-
304 patient lies in the sequestration of bound mRNAs in
nontranslatable mRNP particles. In the absence of FMRP, these same
mRNAs may be partially translated via alternate mRNPs, although
perhaps abnormally localized or regulated, resulting in typical
fragile X syndrome. Asn-304 mutation maps to a position within the
second KH domain of FMRP that is critical for stabilizing
sequence-specific RNA-protein interactions. Asn-304 mutation
abrogates the association of the FMRP KH 2 domain with its target,
kissing complex RNA.
-!- SIMILARITY: Belongs to the FMR1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA52458.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAA62466.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAA62467.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; L29074; AAB18828.1; -; Genomic_DNA.
EMBL; L29074; AAB18829.1; -; Genomic_DNA.
EMBL; L29074; AAB18830.1; -; Genomic_DNA.
EMBL; L29074; AAB18831.1; -; Genomic_DNA.
EMBL; L29074; AAB18832.1; -; Genomic_DNA.
EMBL; L29074; AAB18833.1; -; Genomic_DNA.
EMBL; KJ534836; AHW56476.1; -; mRNA.
EMBL; CH471171; EAW61294.1; -; Genomic_DNA.
EMBL; CH471171; EAW61296.1; -; Genomic_DNA.
EMBL; CH471171; EAW61298.1; -; Genomic_DNA.
EMBL; CH471171; EAW61301.1; -; Genomic_DNA.
EMBL; CH471171; EAW61302.1; -; Genomic_DNA.
EMBL; CH471171; EAW61303.1; -; Genomic_DNA.
EMBL; BC086957; AAH86957.1; -; mRNA.
EMBL; M67468; AAA52458.1; ALT_INIT; mRNA.
EMBL; X69962; CAA49586.1; -; mRNA.
EMBL; S65791; AAB28395.2; -; mRNA.
EMBL; L19476; AAA62452.2; -; Genomic_DNA.
EMBL; L19477; AAA62453.1; -; Genomic_DNA.
EMBL; L19478; AAA62454.1; -; Genomic_DNA.
EMBL; L19479; AAA62455.1; -; Genomic_DNA.
EMBL; L19480; AAA62456.1; -; Genomic_DNA.
EMBL; L19481; AAA62457.1; -; Genomic_DNA.
EMBL; L19482; AAA62458.1; -; Genomic_DNA.
EMBL; L19483; AAA62459.1; -; Genomic_DNA.
EMBL; L19484; AAA62460.1; -; Genomic_DNA.
EMBL; L19485; AAA62461.1; -; Genomic_DNA.
EMBL; L19486; AAA62462.1; -; Genomic_DNA.
EMBL; L19487; AAA62463.1; -; Genomic_DNA.
EMBL; L19488; AAA62464.1; -; Genomic_DNA.
EMBL; L19489; AAA62465.1; -; Genomic_DNA.
EMBL; L19490; AAA62466.1; ALT_SEQ; Genomic_DNA.
EMBL; L19491; AAA62467.1; ALT_SEQ; Genomic_DNA.
EMBL; L19492; AAA62468.1; -; Genomic_DNA.
EMBL; L19493; AAA62469.1; -; Genomic_DNA.
EMBL; S76590; AAD14228.1; -; Genomic_DNA.
CCDS; CCDS14682.1; -. [Q06787-1]
CCDS; CCDS55518.1; -. [Q06787-10]
CCDS; CCDS55519.1; -. [Q06787-9]
CCDS; CCDS76039.1; -. [Q06787-8]
PIR; I68614; I68614.
PIR; S45243; A40724.
RefSeq; NP_001172004.1; NM_001185075.1. [Q06787-10]
RefSeq; NP_001172005.1; NM_001185076.1. [Q06787-9]
RefSeq; NP_001172010.1; NM_001185081.1. [Q06787-11]
RefSeq; NP_001172011.1; NM_001185082.1. [Q06787-8]
RefSeq; NP_002015.1; NM_002024.5. [Q06787-1]
UniGene; Hs.103183; -.
PDB; 2BKD; NMR; -; N=1-134.
PDB; 2FMR; NMR; -; A=216-280.
PDB; 2LA5; NMR; -; B=527-541.
PDB; 2QND; X-ray; 1.90 A; A/B=216-425.
PDB; 4OVA; X-ray; 3.00 A; A/B/C/D=1-209.
PDB; 4QVZ; X-ray; 3.20 A; A/B=1-213.
PDB; 4QW2; X-ray; 2.99 A; A/B=1-213.
PDB; 5DE5; X-ray; 3.00 A; B/D=528-544.
PDB; 5DE8; X-ray; 3.10 A; B/D=528-544.
PDB; 5DEA; X-ray; 2.80 A; B/D=528-544.
PDB; 5UWJ; X-ray; 2.22 A; D=423-437.
PDB; 5UWO; X-ray; 2.35 A; D=422-438.
PDBsum; 2BKD; -.
PDBsum; 2FMR; -.
PDBsum; 2LA5; -.
PDBsum; 2QND; -.
PDBsum; 4OVA; -.
PDBsum; 4QVZ; -.
PDBsum; 4QW2; -.
PDBsum; 5DE5; -.
PDBsum; 5DE8; -.
PDBsum; 5DEA; -.
PDBsum; 5UWJ; -.
PDBsum; 5UWO; -.
DisProt; DP00134; -.
ProteinModelPortal; Q06787; -.
SMR; Q06787; -.
BioGrid; 108619; 59.
DIP; DIP-29509N; -.
IntAct; Q06787; 44.
MINT; MINT-108156; -.
STRING; 9606.ENSP00000359506; -.
iPTMnet; Q06787; -.
PhosphoSitePlus; Q06787; -.
BioMuta; FMR1; -.
DMDM; 544328; -.
EPD; Q06787; -.
MaxQB; Q06787; -.
PaxDb; Q06787; -.
PeptideAtlas; Q06787; -.
PRIDE; Q06787; -.
Ensembl; ENST00000218200; ENSP00000218200; ENSG00000102081. [Q06787-9]
Ensembl; ENST00000370470; ENSP00000359501; ENSG00000102081. [Q06787-6]
Ensembl; ENST00000370471; ENSP00000359502; ENSG00000102081. [Q06787-10]
Ensembl; ENST00000370475; ENSP00000359506; ENSG00000102081. [Q06787-1]
Ensembl; ENST00000440235; ENSP00000413764; ENSG00000102081. [Q06787-8]
GeneID; 2332; -.
KEGG; hsa:2332; -.
UCSC; uc004fck.5; human. [Q06787-1]
CTD; 2332; -.
DisGeNET; 2332; -.
EuPathDB; HostDB:ENSG00000102081.13; -.
GeneCards; FMR1; -.
GeneReviews; FMR1; -.
HGNC; HGNC:3775; FMR1.
HPA; CAB012444; -.
HPA; HPA050118; -.
HPA; HPA056084; -.
MalaCards; FMR1; -.
MIM; 300623; phenotype.
MIM; 300624; phenotype.
MIM; 309550; gene.
MIM; 311360; phenotype.
MIM; 616034; phenotype.
neXtProt; NX_Q06787; -.
OpenTargets; ENSG00000102081; -.
Orphanet; 908; Fragile X syndrome.
Orphanet; 93256; Fragile X-associated tremor/ataxia syndrome.
Orphanet; 619; Primary ovarian failure.
Orphanet; 261483; Xq27.3q28 duplication syndrome.
PharmGKB; PA28191; -.
eggNOG; ENOG410IF9J; Eukaryota.
eggNOG; ENOG410ZDJG; LUCA.
GeneTree; ENSGT00390000017033; -.
HOVERGEN; HBG005739; -.
InParanoid; Q06787; -.
KO; K15516; -.
OMA; RETCGWW; -.
OrthoDB; EOG091G08EZ; -.
PhylomeDB; Q06787; -.
TreeFam; TF105427; -.
ChiTaRS; FMR1; human.
EvolutionaryTrace; Q06787; -.
GeneWiki; FMR1; -.
GenomeRNAi; 2332; -.
PRO; PR:Q06787; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000102081; -.
CleanEx; HS_FMR1; -.
ExpressionAtlas; Q06787; baseline and differential.
Genevisible; Q06787; HS.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
GO; GO:0015030; C:Cajal body; IDA:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0042995; C:cell projection; IDA:UniProtKB.
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; IDA:UniProtKB.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:1902737; C:dendritic filopodium; ISS:UniProtKB.
GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
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; ISS: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; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:1990124; C:messenger ribonucleoprotein complex; IDA:CAFA.
GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB.
GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
GO; GO:0071598; C:neuronal ribonucleoprotein granule; ISS:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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; ISS:UniProtKB.
GO; GO:0014069; C:postsynaptic density of dendrite; ISS:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0098793; C:presynapse; ISS:UniProtKB.
GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0045202; C:synapse; ISS:UniProtKB.
GO; GO:0019034; C:viral replication complex; IDA:UniProtKB.
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; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
GO; GO:0044325; F:ion channel binding; IPI:UniProtKB.
GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
GO; GO:0008017; F:microtubule binding; ISS: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; IDA:UniProtKB.
GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
GO; GO:0034046; F:poly(G) binding; IDA:UniProtKB.
GO; GO:0008266; F:poly(U) RNA binding; IDA:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0043022; F:ribosome binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0035613; F:RNA stem-loop binding; IDA:UniProtKB.
GO; GO:0033592; F:RNA strand annealing activity; IDA:UniProtKB.
GO; GO:1990825; F:sequence-specific mRNA binding; IDA:UniProtKB.
GO; GO:0035197; F:siRNA binding; IDA:UniProtKB.
GO; GO:0031369; F:translation initiation factor binding; IPI:UniProtKB.
GO; GO:0030371; F:translation repressor activity; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0072711; P:cellular response to hydroxyurea; ISS:UniProtKB.
GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB.
GO; GO:0098586; P:cellular response to virus; IDA:UniProtKB.
GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
GO; GO:0007215; P:glutamate receptor signaling pathway; ISS:UniProtKB.
GO; GO:0044830; P:modulation by host of viral RNA genome replication; IMP:UniProtKB.
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:1900453; P:negative regulation of long term synaptic depression; ISS:UniProtKB.
GO; GO:1902373; P:negative regulation of mRNA catabolic process; IMP:CAFA.
GO; GO:2000301; P:negative regulation of synaptic vesicle exocytosis; 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; ISS:UniProtKB.
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: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; IMP:UniProtKB.
GO; GO:1902416; P:positive regulation of mRNA binding; IDA:UniProtKB.
GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; ISS:UniProtKB.
GO; GO:0002092; P:positive regulation of receptor internalization; IDA:UniProtKB.
GO; GO:2001022; P:positive regulation of response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0045727; P:positive regulation of translation; IDA:UniProtKB.
GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB.
GO; GO:0060998; P:regulation of dendritic spine development; IDA:UniProtKB.
GO; GO:0051489; P:regulation of filopodium assembly; IDA:UniProtKB.
GO; GO:0060964; P:regulation of gene silencing by miRNA; IMP:UniProtKB.
GO; GO:0043488; P:regulation of mRNA stability; ISS:UniProtKB.
GO; GO:0098908; P:regulation of neuronal action potential; IDA:UniProtKB.
GO; GO:0046928; P:regulation of neurotransmitter secretion; ISS:UniProtKB.
GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
GO; GO:0016032; P:viral process; 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; 1.
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;
3D-structure; Acetylation; Activator; Alternative splicing;
Cell junction; Cell membrane; Cell projection; Centromere; Chromosome;
Complete proteome; Cytoplasm; Disease mutation; DNA damage;
Host-virus interaction; Membrane; Mental retardation; Methylation;
mRNA processing; mRNA splicing; mRNA transport; Neurogenesis; Nucleus;
Phosphoprotein; Polymorphism; Postsynaptic cell membrane;
Premature ovarian failure; Reference proteome; Repeat; Repressor;
Ribonucleoprotein; RNA-binding; RNA-mediated gene silencing; Synapse;
Synaptosome; Translation regulation; Transport; Ubl conjugation.
CHAIN 1 632 Synaptic functional regulator FMR1.
/FTId=PRO_0000050102.
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:0000250|UniProtKB:P35922}.
REGION 172 211 Necessary for interaction with CYFIP1,
CYFIP2, FXR1 and FXR2.
{ECO:0000250|UniProtKB:P35922,
ECO:0000269|PubMed:14532325,
ECO:0000269|PubMed:8668200}.
REGION 397 491 Required for nuclear export.
{ECO:0000269|PubMed:18936162,
ECO:0000269|PubMed:8789445}.
REGION 419 632 Interaction with RANBP9.
{ECO:0000269|PubMed:15381419}.
REGION 534 548 RNA-binding RGG-box.
MOTIF 424 443 Nuclear export signal.
{ECO:0000250|UniProtKB:P35922}.
MOTIF 527 534 Nucleolar localization signal 1.
{ECO:0000269|PubMed:24658146}.
MOTIF 613 617 Nucleolar localization signal 2.
{ECO:0000269|PubMed:24658146}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 337 337 Phosphoserine.
{ECO:0000250|UniProtKB:Q80WE1}.
MOD_RES 370 370 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 463 463 Phosphothreonine.
{ECO:0000250|UniProtKB:P35922}.
MOD_RES 471 471 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P35922}.
MOD_RES 500 500 Phosphoserine.
{ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:12446764}.
MOD_RES 544 544 Omega-N-methylarginine.
{ECO:0000269|PubMed:16922515}.
MOD_RES 620 620 Phosphoserine.
{ECO:0000250|UniProtKB:P35922}.
VAR_SEQ 376 396 Missing (in isoform 1, isoform 8, isoform
9 and isoform 11).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:24722188,
ECO:0000303|PubMed:8789445}.
/FTId=VSP_002823.
VAR_SEQ 426 632 EVDQLRLERLQIDEQLRQIGASSRPPPNRTDKEKSYVTDDG
QGMGRGSRPYRNRGHGRRGPGYTSGTNSEASNASETESDHR
DELSDWSLAPTEEERESFLRRGDGRRRGGGGRGQGGRGRGG
GFKGNDDHSRTDNRPRNPREAKGRTTDGSLQIRVDCNNERS
VHTKTLQNTSSEGSRLRTGKDRNQKKEKPDSVDGQQPLVNG
VP -> LQQRKRGRASCAEETDGGVEGEEEDKEEEDVEEAS
KETTITPEQIIVHVIQERLKEEQQMDPFRSELTAIMKGVST
LKHYRIPPVKVVGCARVKIVTRRKRSQTAWMVSNHS (in
isoform 10 and isoform 11).
{ECO:0000303|PubMed:8789445}.
/FTId=VSP_058423.
VAR_SEQ 491 515 Missing (in isoform 4, isoform 5 and
isoform 8).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_002825.
VAR_SEQ 491 502 Missing (in isoform 2 and isoform 3).
{ECO:0000305}.
/FTId=VSP_002824.
VAR_SEQ 580 596 Missing (in isoform 1, isoform 3, isoform
5 and isoform 7). {ECO:0000305}.
/FTId=VSP_002826.
VARIANT 138 138 R -> Q (in FRAX; rare variant found in a
developmentally delayed male; inhibits
nucleosome binding; reduces interaction
with KCNMB4; inhibits presynaptic action
potential (AP) broadening; does not alter
postsynaptic RNA-binding and polyribosome
association; dbSNP:rs200163413).
{ECO:0000269|PubMed:20799337,
ECO:0000269|PubMed:24813610,
ECO:0000269|PubMed:25561520}.
/FTId=VAR_064507.
VARIANT 145 145 A -> S (in dbSNP:rs29281).
/FTId=VAR_029278.
VARIANT 266 266 G -> E (in FRAX; reduces association with
polyribosome; reduces RNA-binding).
{ECO:0000269|PubMed:24448548}.
/FTId=VAR_075977.
VARIANT 304 304 I -> N (in FRAX; alters protein folding
and stability; increases
nucleocytoplasmic shuttling; reduces
localization in Cajal bodies; reduces the
association with cytoplasmic granules;
reduces association with polyribosome;
reduces RNA-binding; attenuates mRNA
translation repression; impairs
homooligomerization; reduces interaction
with TDRD3; reduces interaction with
viral influenza A nucleoprotein (NP);
does not inhibit interaction with SMN1,
FXR1 and FXR2; dbSNP:rs121434622).
{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:24514761,
ECO:0000269|PubMed:7633450,
ECO:0000269|PubMed:8156595,
ECO:0000269|PubMed:8490650,
ECO:0000269|PubMed:9659908}.
/FTId=VAR_005234.
VARIANT 546 546 R -> H (in dbSNP:rs782651077).
{ECO:0000269|PubMed:9375856}.
/FTId=VAR_005235.
MUTAGEN 102 102 T->A: Reduces binding to nucleosome.
{ECO:0000269|PubMed:24813610}.
MUTAGEN 103 103 Y->L: Reduces binding to nucleosome.
{ECO:0000269|PubMed:24813610}.
MUTAGEN 125 126 TF->AA: Alters the structural integrity
of the N-terminus and leads to
aggregation.
{ECO:0000269|PubMed:16407062}.
MUTAGEN 500 500 S->A: Loss of phosphorylation. Does not
affect interaction with MCRS1. Does not
affect localization to cytoplasmic
granules. Does not affect association
with polyribosome.
{ECO:0000269|PubMed:12446764,
ECO:0000269|PubMed:14532325,
ECO:0000269|PubMed:16571602}.
MUTAGEN 500 500 S->D: Does not affect RNA-binding to G-
quadruplex structure.
{ECO:0000269|PubMed:25692235}.
MUTAGEN 527 534 RRGDGRRR->EEGDGEEE: Reduces nucleolar
localization. Strongly reduces nucleolar
localization; when associated with 613-
E--E-617. {ECO:0000269|PubMed:24658146}.
MUTAGEN 544 544 R->K: Reduces arginine methylation by
80%. {ECO:0000269|PubMed:16922515}.
MUTAGEN 546 546 R->K: Slightly reduced methylation.
{ECO:0000269|PubMed:16922515}.
MUTAGEN 613 617 QKKEK->EEEEE: Reduces nucleolar
localization. Strongly reduces nucleolar
localization; when associated with 527-
E--E-534. {ECO:0000269|PubMed:24658146}.
CONFLICT 294 295 Missing (in Ref. 1; AAA52458).
{ECO:0000305}.
STRAND 5 9 {ECO:0000244|PDB:4QW2}.
STRAND 15 23 {ECO:0000244|PDB:4QW2}.
STRAND 25 32 {ECO:0000244|PDB:4QW2}.
HELIX 33 35 {ECO:0000244|PDB:4QW2}.
STRAND 40 43 {ECO:0000244|PDB:4QW2}.
HELIX 44 46 {ECO:0000244|PDB:4QW2}.
STRAND 64 69 {ECO:0000244|PDB:4QW2}.
STRAND 71 75 {ECO:0000244|PDB:4QW2}.
STRAND 78 88 {ECO:0000244|PDB:4QW2}.
STRAND 91 97 {ECO:0000244|PDB:4QW2}.
HELIX 100 103 {ECO:0000244|PDB:4OVA}.
STRAND 104 108 {ECO:0000244|PDB:4QW2}.
HELIX 109 111 {ECO:0000244|PDB:4QW2}.
STRAND 112 114 {ECO:0000244|PDB:4QW2}.
TURN 123 125 {ECO:0000244|PDB:4QW2}.
STRAND 127 132 {ECO:0000244|PDB:4QW2}.
TURN 135 138 {ECO:0000244|PDB:4QW2}.
HELIX 139 141 {ECO:0000244|PDB:4QW2}.
HELIX 144 147 {ECO:0000244|PDB:4QW2}.
HELIX 148 154 {ECO:0000244|PDB:4QW2}.
STRAND 157 162 {ECO:0000244|PDB:4QW2}.
TURN 163 166 {ECO:0000244|PDB:4QW2}.
STRAND 167 173 {ECO:0000244|PDB:4QW2}.
HELIX 177 198 {ECO:0000244|PDB:4QW2}.
STRAND 220 224 {ECO:0000244|PDB:2QND}.
HELIX 227 229 {ECO:0000244|PDB:2QND}.
HELIX 230 234 {ECO:0000244|PDB:2QND}.
HELIX 236 238 {ECO:0000244|PDB:2QND}.
HELIX 239 245 {ECO:0000244|PDB:2QND}.
STRAND 250 256 {ECO:0000244|PDB:2QND}.
TURN 257 260 {ECO:0000244|PDB:2QND}.
STRAND 261 268 {ECO:0000244|PDB:2QND}.
HELIX 269 279 {ECO:0000244|PDB:2QND}.
STRAND 281 289 {ECO:0000244|PDB:2QND}.
HELIX 290 292 {ECO:0000244|PDB:2QND}.
HELIX 293 297 {ECO:0000244|PDB:2QND}.
HELIX 299 301 {ECO:0000244|PDB:2QND}.
HELIX 302 311 {ECO:0000244|PDB:2QND}.
STRAND 314 321 {ECO:0000244|PDB:2QND}.
STRAND 398 406 {ECO:0000244|PDB:2QND}.
HELIX 407 422 {ECO:0000244|PDB:2QND}.
STRAND 535 538 {ECO:0000244|PDB:2LA5}.
SEQUENCE 632 AA; 71174 MW; F853D6C82E3489B9 CRC64;
MEELVVEVRG SNGAFYKAFV KDVHEDSITV AFENNWQPDR QIPFHDVRFP PPVGYNKDIN
ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD ATYNEIVTIE RLRSVNPNKP
ATKDTFHKIK LDVPEDLRQM CAKEAAHKDF KKAVGAFSVT YDPENYQLVI LSINEVTSKR
AHMLIDMHFR SLRTKLSLIM RNEEASKQLE SSRQLASRFH EQFIVREDLM GLAIGTHGAN
IQQARKVPGV TAIDLDEDTC TFHIYGEDQD AVKKARSFLE FAEDVIQVPR NLVGKVIGKN
GKLIQEIVDK SGVVRVRIEA ENEKNVPQEE EIMPPNSLPS NNSRVGPNAP EEKKHLDIKE
NSTHFSQPNS TKVQRVLVAS SVVAGESQKP ELKAWQGMVP FVFVGTKDSI ANATVLLDYH
LNYLKEVDQL RLERLQIDEQ LRQIGASSRP PPNRTDKEKS YVTDDGQGMG RGSRPYRNRG
HGRRGPGYTS GTNSEASNAS ETESDHRDEL SDWSLAPTEE ERESFLRRGD GRRRGGGGRG
QGGRGRGGGF KGNDDHSRTD NRPRNPREAK GRTTDGSLQI RVDCNNERSV HTKTLQNTSS
EGSRLRTGKD RNQKKEKPDS VDGQQPLVNG VP


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