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Synaptic functional regulator FMR1 (Fragile X mental retardation syndrome-related protein 1) (dFMR1)

 FMR1_DROME              Reviewed;         684 AA.
Q9NFU0; A4V2M8; Q8INM7; Q8T0M0; Q8WQ60; Q95P21; Q9GSG3; Q9TVY4;
Q9VH27;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 159.
RecName: Full=Synaptic functional regulator FMR1 {ECO:0000305};
AltName: Full=Fragile X mental retardation syndrome-related protein 1 {ECO:0000250|UniProtKB:Q06787};
Short=dFMR1 {ECO:0000303|PubMed:11046149};
Name=Fmr1 {ECO:0000312|EMBL:AAF14639.1};
Synonyms=FXR {ECO:0000312|EMBL:CAB66340.1}; ORFNames=CG6203;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1] {ECO:0000305, ECO:0000312|EMBL:AAG22045.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), SUBUNIT, RNA-BINDING,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
MUTAGENESIS OF ILE-244 AND ILE-307.
TISSUE=Ovary {ECO:0000269|PubMed:11046149};
PubMed=11046149; DOI=10.1128/MCB.20.22.8536-8547.2000;
Wan L., Dockendorff T.C., Jongens T.A., Dreyfuss G.;
"Characterization of dFMR1, a Drosophila melanogaster homolog of the
fragile X mental retardation protein.";
Mol. Cell. Biol. 20:8536-8547(2000).
[2] {ECO:0000305, ECO:0000312|EMBL:CAB66340.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS A AND C), FUNCTION,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
STRAIN=Berkeley {ECO:0000269|PubMed:11733059};
TISSUE=Embryo {ECO:0000269|PubMed:11733059};
PubMed=11733059; DOI=10.1016/S0092-8674(01)00589-X;
Zhang Y.Q., Bailey A.M., Matthies H.J.G., Renden R.B., Smith M.A.,
Speese S.D., Rubin G.M., Broadie K.S.;
"Drosophila fragile X-related gene regulates the MAP1B homolog Futsch
to control synaptic structure and function.";
Cell 107:591-603(2001).
[3] {ECO:0000305, ECO:0000312|EMBL:CAD19444.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND C).
STRAIN=Berkeley {ECO:0000269|Ref.3};
TISSUE=Embryo {ECO:0000269|Ref.3}, Ovary {ECO:0000269|Ref.3}, and
Testis {ECO:0000312|EMBL:CAC88757.2};
Zhang Y.Q., Broadie K.S.;
"Modeling human fragile X syndrome in flies.";
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000312|EMBL:AAF54493.2}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[5] {ECO:0000305, ECO:0000312|EMBL:AAF54493.2}
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[6] {ECO:0000305, ECO:0000312|EMBL:CAD19444.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 105-684 (ISOFORMS C/E).
STRAIN=Berkeley {ECO:0000312|EMBL:AAL39327.2};
TISSUE=Embryo, and Head;
Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W.,
Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
George R.A., Gonzalez M., Guarin H., Kapadia B., Kronmiller B.,
Li P.W., Liao G., Miranda A., Mungall C.J., Nunoo J., Pacleb J.M.,
Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C.,
Lewis S.E., Rubin G.M., Celniker S.E.;
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
[7] {ECO:0000305}
FUNCTION, INTERACTION WITH AGO2; DCR-1; RM62; RPL5 AND RPL11, AND
ASSOCIATION WITH POLYRIBOSOME.
PubMed=12368261; DOI=10.1101/gad.1022002;
Ishizuka A., Siomi M.C., Siomi H.;
"A Drosophila fragile X protein interacts with components of RNAi and
ribosomal proteins.";
Genes Dev. 16:2497-2508(2002).
[8]
INTERACTION WITH SRA-1.
PubMed=12818175; DOI=10.1016/S0896-6273(03)00354-4;
Schenck A., Bardoni B., Langmann C., Harden N., Mandel J.-L.,
Giangrande A.;
"CYFIP/Sra-1 controls neuronal connectivity in Drosophila and links
the Rac1 GTPase pathway to the fragile X protein.";
Neuron 38:887-898(2003).
[9] {ECO:0000305}
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=15183715; DOI=10.1016/j.ydbio.2004.02.010;
Zhang Y.Q., Matthies H.J.G., Mancuso J., Andrews H.K.,
Woodruff E. III, Friedman D., Broadie K.S.;
"The Drosophila fragile X-related gene regulates axoneme
differentiation during spermatogenesis.";
Dev. Biol. 270:290-307(2004).
[10]
FUNCTION, AND INTERACTION WITH PIWI AND VAS.
PubMed=16949822; DOI=10.1016/j.cub.2006.08.051;
Megosh H.B., Cox D.N., Campbell C., Lin H.;
"The role of PIWI and the miRNA machinery in Drosophila germline
determination.";
Curr. Biol. 16:1884-1894(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403; SER-408; SER-409;
SER-413; SER-532; SER-533; SER-539 AND SER-541, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
-!- FUNCTION: Polyribosome-associated RNA-binding protein that plays a
role in neuronal development and synaptic plasticity through the
regulation of protein synthesis of mRNAs (PubMed:11046149,
PubMed:11733059, PubMed:12368261). Plays a role as a negative
translational regulator of specific mRNAs (PubMed:11733059).
Represses translation of the microtubule-associated protein futsch
mRNA to regulate microtubule-dependent synaptic growth and
function (PubMed:11733059). May also be involved in microRNA
(miRNA)-mediated translational suppression (PubMed:12368261).
Required for stability of the central pair of microtubules in the
spermatid axoneme (PubMed:15183715). Regulates photoreceptor
structure and neuromuscular junction (NMJ) neurotransmission in
the eye (PubMed:11733059). During embryogenesis, involved in
germline fate determination (PubMed:16949822).
{ECO:0000269|PubMed:11046149, ECO:0000269|PubMed:11733059,
ECO:0000269|PubMed:12368261, ECO:0000269|PubMed:15183715,
ECO:0000269|PubMed:16949822}.
-!- SUBUNIT: Homodimer (PubMed:11046149). Interacts with AGO2, Dcr-1,
Rm62, RpL5 and RpL11; these interactions form a messenger
ribonucleoprotein particle (RNP) complex involved in translation
regulation (PubMed:12368261). Interacts with piwi and vas; these
interactions occur in the polar granules (PubMed:16949822).
Interacts with Sra-1 (PubMed:12818175). Associates with
polyribosome (PubMed:12368261). {ECO:0000269|PubMed:11046149,
ECO:0000269|PubMed:12368261, ECO:0000269|PubMed:12818175,
ECO:0000269|PubMed:16949822}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-422631, EBI-422631;
Q9VUQ5:AGO2; NbExp=4; IntAct=EBI-422631, EBI-442476;
P19109:Rm62; NbExp=4; IntAct=EBI-422631, EBI-200734;
P46222:RpL11; NbExp=5; IntAct=EBI-422631, EBI-183104;
Q9NIU2:RpL5; NbExp=5; IntAct=EBI-422631, EBI-605695;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11046149}.
Perikaryon {ECO:0000269|PubMed:11733059}. Cell projection
{ECO:0000269|PubMed:11733059}. Cell junction, synapse
{ECO:0000269|PubMed:11733059}. Note=Localizes in the neuronal soma
and cell processes, and in pre- and postsynaptic neurons, as well
as in postsynaptic muscles (PubMed:11733059).
{ECO:0000269|PubMed:11733059}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=A {ECO:0000269|PubMed:11733059};
IsoId=Q9NFU0-1; Sequence=Displayed;
Name=B {ECO:0000269|Ref.3};
IsoId=Q9NFU0-4; Sequence=VSP_050785, VSP_050786, VSP_050787;
Name=C {ECO:0000269|PubMed:11733059}; Synonyms=D
{ECO:0000303|PubMed:10731132};
IsoId=Q9NFU0-2; Sequence=VSP_050784;
Name=E {ECO:0000303|PubMed:10731132};
IsoId=Q9NFU0-3; Sequence=VSP_050783, VSP_050784;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Highly expressed in testes in the early stages
of spermatogenesis before spermatid individualization (at protein
level) (PubMed:15183715). {ECO:0000269|PubMed:15183715}.
-!- DEVELOPMENTAL STAGE: Expressed during the embryonic development
(PubMed:11046149). Expressed both maternally and zygotically in
embryos (PubMed:11046149). Until early gastrulation, expression is
uniformly distributed in the embryo (PubMed:11046149). At mid-
gastrulation (stage 11), expressed everywhere with discernible
concentration in the mesoderm (PubMed:11046149). After
gastrulation (stage 14), expressed in the mesoderm, ventral nerve
cord, and brain (PubMed:11046149). At stage 16, elevated
expression is also seen in the muscle (PubMed:11046149). Highly
expressed in nervous system throughout later development (at
protein level) (PubMed:11046149, PubMed:11733059).
{ECO:0000269|PubMed:11046149, ECO:0000269|PubMed:11733059}.
-!- SIMILARITY: Belongs to the FMR1 family. {ECO:0000255}.
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EMBL; AF305881; AAG22045.1; -; mRNA.
EMBL; AF205596; AAF14639.1; -; mRNA.
EMBL; AF205597; AAF14640.1; -; Genomic_DNA.
EMBL; AJ271221; CAB66340.1; -; mRNA.
EMBL; AJ413217; CAC88757.2; -; mRNA.
EMBL; AJ422082; CAD19443.1; -; mRNA.
EMBL; AJ422083; CAD19444.1; -; mRNA.
EMBL; AE014297; AAF54493.2; -; Genomic_DNA.
EMBL; AE014297; AAN13451.1; -; Genomic_DNA.
EMBL; AE014297; AAN13452.1; -; Genomic_DNA.
EMBL; AE014297; AAN13453.1; -; Genomic_DNA.
EMBL; AE014297; AAN13454.1; -; Genomic_DNA.
EMBL; AY069182; AAL39327.2; -; mRNA.
EMBL; BT031124; ABX00746.1; -; mRNA.
RefSeq; NP_001303443.1; NM_001316514.1. [Q9NFU0-2]
RefSeq; NP_001303444.1; NM_001316515.1. [Q9NFU0-2]
RefSeq; NP_611645.1; NM_137801.4. [Q9NFU0-1]
RefSeq; NP_731443.1; NM_169324.2. [Q9NFU0-2]
RefSeq; NP_731444.1; NM_169325.3. [Q9NFU0-2]
RefSeq; NP_731445.1; NM_169326.3. [Q9NFU0-3]
RefSeq; NP_731446.1; NM_169327.2. [Q9NFU0-4]
UniGene; Dm.5279; -.
ProteinModelPortal; Q9NFU0; -.
SMR; Q9NFU0; -.
BioGrid; 63147; 100.
IntAct; Q9NFU0; 22.
MINT; MINT-248306; -.
STRING; 7227.FBpp0300445; -.
iPTMnet; Q9NFU0; -.
PaxDb; Q9NFU0; -.
PRIDE; Q9NFU0; -.
EnsemblMetazoa; FBtr0082196; FBpp0081674; FBgn0028734. [Q9NFU0-4]
EnsemblMetazoa; FBtr0082197; FBpp0081675; FBgn0028734. [Q9NFU0-1]
EnsemblMetazoa; FBtr0082198; FBpp0081676; FBgn0028734. [Q9NFU0-2]
EnsemblMetazoa; FBtr0082199; FBpp0081677; FBgn0028734. [Q9NFU0-2]
EnsemblMetazoa; FBtr0082200; FBpp0081678; FBgn0028734. [Q9NFU0-3]
EnsemblMetazoa; FBtr0347104; FBpp0312465; FBgn0028734. [Q9NFU0-2]
EnsemblMetazoa; FBtr0347105; FBpp0312466; FBgn0028734. [Q9NFU0-2]
GeneID; 37528; -.
KEGG; dme:Dmel_CG6203; -.
UCSC; CG6203-RD; d. melanogaster.
CTD; 2332; -.
FlyBase; FBgn0028734; Fmr1.
eggNOG; ENOG410IF9J; Eukaryota.
eggNOG; ENOG410ZDJG; LUCA.
GeneTree; ENSGT00390000017033; -.
InParanoid; Q9NFU0; -.
KO; K15516; -.
OrthoDB; EOG091G08EZ; -.
PhylomeDB; Q9NFU0; -.
ChiTaRS; Fmr1; fly.
GenomeRNAi; 37528; -.
PRO; PR:Q9NFU0; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0028734; -.
ExpressionAtlas; Q9NFU0; differential.
Genevisible; Q9NFU0; DM.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:0035068; C:micro-ribonucleoprotein complex; TAS:FlyBase.
GO; GO:0071598; C:neuronal ribonucleoprotein granule; IDA:FlyBase.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0043186; C:P granule; IDA:FlyBase.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0005844; C:polysome; IBA:GO_Central.
GO; GO:0098793; C:presynapse; IEA:GOC.
GO; GO:0016442; C:RISC complex; IPI:FlyBase.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
GO; GO:0043621; F:protein self-association; IDA:FlyBase.
GO; GO:0003723; F:RNA binding; IDA:FlyBase.
GO; GO:0045182; F:translation regulator activity; IMP:CACAO.
GO; GO:0008344; P:adult locomotory behavior; IMP:FlyBase.
GO; GO:0008306; P:associative learning; IMP:FlyBase.
GO; GO:0007411; P:axon guidance; IMP:FlyBase.
GO; GO:0007413; P:axonal fasciculation; IMP:FlyBase.
GO; GO:0007409; P:axonogenesis; IMP:FlyBase.
GO; GO:0007420; P:brain development; IMP:FlyBase.
GO; GO:0007349; P:cellularization; IDA:FlyBase.
GO; GO:0007623; P:circadian rhythm; IMP:FlyBase.
GO; GO:0050802; P:circadian sleep/wake cycle, sleep; IMP:FlyBase.
GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
GO; GO:0050976; P:detection of mechanical stimulus involved in sensory perception of touch; IMP:FlyBase.
GO; GO:0031047; P:gene silencing by RNA; IMP:FlyBase.
GO; GO:0007281; P:germ cell development; IMP:FlyBase.
GO; GO:0048134; P:germ-line cyst formation; IMP:FlyBase.
GO; GO:0007294; P:germarium-derived oocyte fate determination; IMP:FlyBase.
GO; GO:0007625; P:grooming behavior; IMP:FlyBase.
GO; GO:0046959; P:habituation; IMP:FlyBase.
GO; GO:0031507; P:heterochromatin assembly; IMP:FlyBase.
GO; GO:0008345; P:larval locomotory behavior; IMP:FlyBase.
GO; GO:0040011; P:locomotion; TAS:FlyBase.
GO; GO:0045475; P:locomotor rhythm; IMP:FlyBase.
GO; GO:0007616; P:long-term memory; IMP:FlyBase.
GO; GO:0008049; P:male courtship behavior; IMP:FlyBase.
GO; GO:0072375; P:medium-term memory; IMP:FlyBase.
GO; GO:0045448; P:mitotic cell cycle, embryonic; IMP:FlyBase.
GO; GO:0051028; P:mRNA transport; IMP:FlyBase.
GO; GO:0016319; P:mushroom body development; IMP:FlyBase.
GO; GO:0050774; P:negative regulation of dendrite morphogenesis; IMP:FlyBase.
GO; GO:0045571; P:negative regulation of imaginal disc growth; IGI:FlyBase.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IMP:FlyBase.
GO; GO:0051964; P:negative regulation of synapse assembly; IMP:FlyBase.
GO; GO:0045886; P:negative regulation of synaptic growth at neuromuscular junction; IMP:FlyBase.
GO; GO:0017148; P:negative regulation of translation; IDA:FlyBase.
GO; GO:0007528; P:neuromuscular junction development; IMP:FlyBase.
GO; GO:0048812; P:neuron projection morphogenesis; IMP:FlyBase.
GO; GO:0008355; P:olfactory learning; IMP:FlyBase.
GO; GO:0007310; P:oocyte dorsal/ventral axis specification; IGI:FlyBase.
GO; GO:0007279; P:pole cell formation; IMP:FlyBase.
GO; GO:0002052; P:positive regulation of neuroblast proliferation; IMP:FlyBase.
GO; GO:0043068; P:positive regulation of programmed cell death; IMP:FlyBase.
GO; GO:0042127; P:regulation of cell proliferation; IMP:FlyBase.
GO; GO:0048814; P:regulation of dendrite morphogenesis; IMP:FlyBase.
GO; GO:0009794; P:regulation of mitotic cell cycle, embryonic; IGI:FlyBase.
GO; GO:1900073; P:regulation of neuromuscular synaptic transmission; IMP:FlyBase.
GO; GO:0090328; P:regulation of olfactory learning; IMP:FlyBase.
GO; GO:0050807; P:regulation of synapse organization; IMP:FlyBase.
GO; GO:0051823; P:regulation of synapse structural plasticity; IMP:FlyBase.
GO; GO:0006417; P:regulation of translation; IMP:FlyBase.
GO; GO:0007614; P:short-term memory; IMP:FlyBase.
GO; GO:0035176; P:social behavior; IMP:FlyBase.
GO; GO:0007288; P:sperm axoneme assembly; IMP:FlyBase.
GO; GO:0007416; P:synapse assembly; NAS:FlyBase.
GO; GO:0050808; P:synapse organization; IMP:FlyBase.
GO; GO:0070142; P:synaptic vesicle budding; IMP:FlyBase.
GO; GO:0097091; P:synaptic vesicle clustering; IMP:FlyBase.
GO; GO:0072553; P:terminal button organization; IMP:FlyBase.
GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
Gene3D; 3.30.1370.10; -; 2.
Gene3D; 3.30.300.20; -; 1.
InterPro; IPR008395; Agenet-like_dom.
InterPro; IPR022034; FXMRP1_C_core.
InterPro; IPR004087; KH_dom.
InterPro; IPR015946; KH_dom-like_a/b.
InterPro; IPR004088; KH_dom_type_1.
InterPro; IPR036612; KH_dom_type_1_sf.
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;
Alternative splicing; Cell junction; Cell projection;
Complete proteome; Cytoplasm; Neurogenesis; Phosphoprotein;
Reference proteome; Repeat; Repressor; Ribonucleoprotein; RNA-binding;
RNA-mediated gene silencing; Sensory transduction; Synapse;
Translation regulation; Vision.
CHAIN 1 684 Synaptic functional regulator FMR1.
/FTId=PRO_0000050109.
DOMAIN 1 49 Agenet-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00973}.
DOMAIN 65 117 Agenet-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00973}.
DOMAIN 221 282 KH 1. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 284 353 KH 2. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
REGION 474 489 RNA-binding RGG-box.
COMPBIAS 419 499 Gly-rich.
COMPBIAS 574 669 Gln-rich.
MOD_RES 403 403 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 408 408 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 409 409 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 413 413 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 532 532 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 533 533 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 539 539 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 541 541 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
VAR_SEQ 1 38 Missing (in isoform E).
{ECO:0000303|PubMed:10731132}.
/FTId=VSP_050783.
VAR_SEQ 321 330 Missing (in isoform B).
{ECO:0000303|Ref.3}.
/FTId=VSP_050785.
VAR_SEQ 321 323 Missing (in isoform C and isoform E).
{ECO:0000303|PubMed:10731132,
ECO:0000303|PubMed:11046149,
ECO:0000303|PubMed:11733059,
ECO:0000303|Ref.3, ECO:0000303|Ref.6}.
/FTId=VSP_050784.
VAR_SEQ 537 539 ADS -> DTN (in isoform B).
{ECO:0000303|Ref.3}.
/FTId=VSP_050786.
VAR_SEQ 540 684 Missing (in isoform B).
{ECO:0000303|Ref.3}.
/FTId=VSP_050787.
MUTAGEN 244 244 I->N: Impairs RNA-binding.
{ECO:0000269|PubMed:11046149}.
MUTAGEN 307 307 I->N: Impairs RNA-binding.
{ECO:0000269|PubMed:11046149}.
CONFLICT 343 343 F -> L (in Ref. 1; AAG22045).
{ECO:0000305}.
SEQUENCE 684 AA; 76076 MW; 973489A73B97F1FE CRC64;
MEDLLVEVRL DNGAYYKGQV TAVADDGIFV DVDGVPESMK YPFVNVRLPP EETVEVAAPI
FEEGMEVEVF TRTNDRETCG WWVGIIKMRK AEIYAVAYIG FETSYTEICE LGRLRAKNSN
PPITAKTFYQ FTLPVPEELR EEAQKDGIHK EFQRTIDAGV CNYSRDLDAL IVISKFEHTQ
KRASMLKDMH FRNLSQKVML LKRTEEAARQ LETTKLMSRG NYVEEFRVRD DLMGLAIGSH
GSNIQAARTV DGVTNIELEE KSCTFKISGE TEESVQRARA MLEYAEEFFQ VPRELVGKVI
GKNGRIIQEI VDKSGVFRIK VSAIAGDDEQ DQNIPRELAH VPFVFIGTVE SIANAKVLLE
YHLSHLKEVE QLRQEKMEID QQLRAIQESS MGSTQSFPVT RRSERGYSSD IESVRSMRGG
GGGQRGRVRG RGGGGPGGGN GLNQRYHNNR RDEDDYNSRG DHQRDQQRGY NDRGGGDNTG
SYRGGGGGAG GPGNNRRGGI NRRPPRNDQQ NGRDYQHHNH TTEEVRETRE MSSVERADSN
SSYEGSSRRR RRQKNNNGPS NTNGAVANNN NKPQSAQQPQ QQQPPAPGNK AALNAGDASK
QNSGNANAAG GASKPKDASR NGDKQQAGTQ QQQPSQVQQQ QAAQQQQPKP RRNKNRSNNH
TDQPSGQQQL AENVKKEGLV NGTS


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