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Protein

Synaptic functional regulator FMR1

Gene

Fmr1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).5 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • mRNA binding Source: FlyBase
  • protein self-association Source: FlyBase
  • RNA binding Source: FlyBase
  • translation regulator activity Source: CACAO

GO - Biological processi

  • axonal fasciculation Source: FlyBase
  • axon guidance Source: FlyBase
  • axonogenesis Source: FlyBase
  • brain development Source: FlyBase
  • cellularization Source: FlyBase
  • circadian rhythm Source: FlyBase
  • circadian sleep/wake cycle, sleep Source: FlyBase
  • dendrite morphogenesis Source: FlyBase
  • detection of mechanical stimulus involved in sensory perception of touch Source: FlyBase
  • gene silencing by RNA Source: UniProtKB-KW
  • germarium-derived oocyte fate determination Source: FlyBase
  • germ cell development Source: FlyBase
  • germ-line cyst formation Source: FlyBase
  • habituation Source: FlyBase
  • heterochromatin assembly Source: FlyBase
  • larval locomotory behavior Source: FlyBase
  • locomotion Source: FlyBase
  • locomotor rhythm Source: FlyBase
  • long-term memory Source: FlyBase
  • male courtship behavior Source: FlyBase
  • medium-term memory Source: FlyBase
  • mitotic cell cycle, embryonic Source: FlyBase
  • mRNA transport Source: FlyBase
  • mushroom body development Source: FlyBase
  • negative regulation of dendrite morphogenesis Source: FlyBase
  • negative regulation of imaginal disc growth Source: FlyBase
  • negative regulation of insulin receptor signaling pathway Source: FlyBase
  • negative regulation of synapse assembly Source: FlyBase
  • negative regulation of synaptic growth at neuromuscular junction Source: FlyBase
  • negative regulation of translation Source: FlyBase
  • neuromuscular junction development Source: FlyBase
  • neuron projection morphogenesis Source: FlyBase
  • olfactory learning Source: FlyBase
  • oocyte dorsal/ventral axis specification Source: FlyBase
  • pole cell formation Source: FlyBase
  • positive regulation of neuroblast proliferation Source: FlyBase
  • positive regulation of programmed cell death Source: FlyBase
  • regulation of cell proliferation Source: FlyBase
  • regulation of dendrite morphogenesis Source: FlyBase
  • regulation of mitotic cell cycle, embryonic Source: FlyBase
  • regulation of neuromuscular synaptic transmission Source: FlyBase
  • regulation of olfactory learning Source: FlyBase
  • regulation of synapse organization Source: FlyBase
  • regulation of synapse structural plasticity Source: FlyBase
  • regulation of translation Source: FlyBase
  • short-term memory Source: FlyBase
  • sperm axoneme assembly Source: FlyBase
  • synapse assembly Source: FlyBase
  • synapse organization Source: FlyBase
  • synaptic vesicle budding Source: FlyBase
  • synaptic vesicle clustering Source: FlyBase
  • visual perception Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor, Ribonucleoprotein

Keywords - Biological processi

Neurogenesis, RNA-mediated gene silencing, Sensory transduction, Translation regulation, Vision

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Synaptic functional regulator FMR1Curated
Alternative name(s):
Fragile X mental retardation syndrome-related protein 1By similarity
Short name:
dFMR11 Publication
Gene namesi
Name:Fmr1Imported
Synonyms:FXRImported
ORF Names:CG6203
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0028734. Fmr1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: FlyBase
  • cytosol Source: GOC
  • lipid particle Source: FlyBase
  • micro-ribonucleoprotein complex Source: FlyBase
  • nucleus Source: GO_Central
  • polysome Source: GO_Central
  • presynapse Source: GOC
  • RISC complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi244 – 2441I → N: Impairs RNA-binding. 1 Publication
Mutagenesisi307 – 3071I → N: Impairs RNA-binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 684684Synaptic functional regulator FMR1PRO_0000050109Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei403 – 4031Phosphoserine1 Publication
Modified residuei408 – 4081Phosphoserine1 Publication
Modified residuei409 – 4091Phosphoserine1 Publication
Modified residuei413 – 4131Phosphoserine1 Publication
Modified residuei532 – 5321Phosphoserine1 Publication
Modified residuei533 – 5331Phosphoserine1 Publication
Modified residuei539 – 5391Phosphoserine1 Publication
Modified residuei541 – 5411Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9NFU0.
PRIDEiQ9NFU0.

PTM databases

iPTMnetiQ9NFU0.

Expressioni

Tissue specificityi

Highly expressed in testes in the early stages of spermatogenesis before spermatid individualization (at protein level) (PubMed:15183715).1 Publication

Developmental stagei

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).2 Publications

Gene expression databases

BgeeiQ9NFU0.
ExpressionAtlasiQ9NFU0. differential.
GenevisibleiQ9NFU0. DM.

Interactioni

Subunit structurei

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).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-422631,EBI-422631
AGO2Q9VUQ54EBI-422631,EBI-442476
Rm62P191094EBI-422631,EBI-200734
RpL11P462225EBI-422631,EBI-183104
RpL5Q9NIU25EBI-422631,EBI-605695

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein self-association Source: FlyBase

Protein-protein interaction databases

BioGridi63147. 21 interactions.
IntActiQ9NFU0. 22 interactions.
MINTiMINT-248306.
STRINGi7227.FBpp0300445.

Structurei

3D structure databases

ProteinModelPortaliQ9NFU0.
SMRiQ9NFU0. Positions 1-201, 224-367.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 4949Agenet-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini65 – 11753Agenet-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini221 – 28262KH 1PROSITE-ProRule annotationAdd
BLAST
Domaini284 – 35370KH 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni474 – 48916RNA-binding RGG-boxAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi419 – 49981Gly-richAdd
BLAST
Compositional biasi574 – 66996Gln-richAdd
BLAST

Sequence similaritiesi

Belongs to the FMR1 family.Sequence analysis
Contains 2 Agenet-like domains.PROSITE-ProRule annotation
Contains 2 KH domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IF9J. Eukaryota.
ENOG410ZDJG. LUCA.
GeneTreeiENSGT00390000017033.
InParanoidiQ9NFU0.
KOiK15516.
OrthoDBiEOG7NKKJT.
PhylomeDBiQ9NFU0.

Family and domain databases

Gene3Di3.30.1370.10. 2 hits.
InterProiIPR008395. Agenet-like_dom.
IPR022034. FXMRP1_C_core.
IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
[Graphical view]
PfamiPF12235. FXMRP1_C_core. 1 hit.
PF00013. KH_1. 2 hits.
[Graphical view]
SMARTiSM00322. KH. 2 hits.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 2 hits.
PROSITEiPS51641. AGENET_LIKE. 2 hits.
PS50084. KH_TYPE_1. 2 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A1 Publication (identifier: Q9NFU0-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEDLLVEVRL DNGAYYKGQV TAVADDGIFV DVDGVPESMK YPFVNVRLPP
60 70 80 90 100
EETVEVAAPI FEEGMEVEVF TRTNDRETCG WWVGIIKMRK AEIYAVAYIG
110 120 130 140 150
FETSYTEICE LGRLRAKNSN PPITAKTFYQ FTLPVPEELR EEAQKDGIHK
160 170 180 190 200
EFQRTIDAGV CNYSRDLDAL IVISKFEHTQ KRASMLKDMH FRNLSQKVML
210 220 230 240 250
LKRTEEAARQ LETTKLMSRG NYVEEFRVRD DLMGLAIGSH GSNIQAARTV
260 270 280 290 300
DGVTNIELEE KSCTFKISGE TEESVQRARA MLEYAEEFFQ VPRELVGKVI
310 320 330 340 350
GKNGRIIQEI VDKSGVFRIK VSAIAGDDEQ DQNIPRELAH VPFVFIGTVE
360 370 380 390 400
SIANAKVLLE YHLSHLKEVE QLRQEKMEID QQLRAIQESS MGSTQSFPVT
410 420 430 440 450
RRSERGYSSD IESVRSMRGG GGGQRGRVRG RGGGGPGGGN GLNQRYHNNR
460 470 480 490 500
RDEDDYNSRG DHQRDQQRGY NDRGGGDNTG SYRGGGGGAG GPGNNRRGGI
510 520 530 540 550
NRRPPRNDQQ NGRDYQHHNH TTEEVRETRE MSSVERADSN SSYEGSSRRR
560 570 580 590 600
RRQKNNNGPS NTNGAVANNN NKPQSAQQPQ QQQPPAPGNK AALNAGDASK
610 620 630 640 650
QNSGNANAAG GASKPKDASR NGDKQQAGTQ QQQPSQVQQQ QAAQQQQPKP
660 670 680
RRNKNRSNNH TDQPSGQQQL AENVKKEGLV NGTS
Length:684
Mass (Da):76,076
Last modified:October 1, 2000 - v1
Checksum:i973489A73B97F1FE
GO
Isoform B1 Publication (identifier: Q9NFU0-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     321-330: Missing.
     537-539: ADS → DTN
     540-684: Missing.

Show »
Length:529
Mass (Da):59,708
Checksum:i44A6AB3CEC9C4B91
GO
Isoform C1 Publication (identifier: Q9NFU0-2) [UniParc]FASTAAdd to basket

Also known as: D1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     321-323: Missing.

Show »
Length:681
Mass (Da):75,819
Checksum:i570C388A0A3134C2
GO
Isoform E1 Publication (identifier: Q9NFU0-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-38: Missing.
     321-323: Missing.

Note: No experimental confirmation available.Curated
Show »
Length:643
Mass (Da):71,736
Checksum:i944F771C9E7B9A5C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti343 – 3431F → L in AAG22045 (PubMed:11046149).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3838Missing in isoform E. 1 PublicationVSP_050783Add
BLAST
Alternative sequencei321 – 33010Missing in isoform B. 1 PublicationVSP_050785
Alternative sequencei321 – 3233Missing in isoform C and isoform E. 5 PublicationsVSP_050784
Alternative sequencei537 – 5393ADS → DTN in isoform B. 1 PublicationVSP_050786
Alternative sequencei540 – 684145Missing in isoform B. 1 PublicationVSP_050787Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF305881 mRNA. Translation: AAG22045.1.
AF205596 mRNA. Translation: AAF14639.1.
AF205597 Genomic DNA. Translation: AAF14640.1.
AJ271221 mRNA. Translation: CAB66340.1.
AJ413217 mRNA. Translation: CAC88757.2.
AJ422082 mRNA. Translation: CAD19443.1.
AJ422083 mRNA. Translation: CAD19444.1.
AE014297 Genomic DNA. Translation: AAF54493.2.
AE014297 Genomic DNA. Translation: AAN13451.1.
AE014297 Genomic DNA. Translation: AAN13452.1.
AE014297 Genomic DNA. Translation: AAN13453.1.
AE014297 Genomic DNA. Translation: AAN13454.1.
AY069182 mRNA. Translation: AAL39327.2.
BT031124 mRNA. Translation: ABX00746.1.
RefSeqiNP_001303443.1. NM_001316514.1. [Q9NFU0-2]
NP_001303444.1. NM_001316515.1. [Q9NFU0-2]
NP_611645.1. NM_137801.4. [Q9NFU0-1]
NP_731443.1. NM_169324.2. [Q9NFU0-2]
NP_731444.1. NM_169325.3. [Q9NFU0-2]
NP_731445.1. NM_169326.3. [Q9NFU0-3]
NP_731446.1. NM_169327.2. [Q9NFU0-4]
UniGeneiDm.5279.

Genome annotation databases

EnsemblMetazoaiFBtr0082197; FBpp0081675; FBgn0028734. [Q9NFU0-1]
GeneIDi37528.
KEGGidme:Dmel_CG6203.
UCSCiCG6203-RD. d. melanogaster.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF305881 mRNA. Translation: AAG22045.1.
AF205596 mRNA. Translation: AAF14639.1.
AF205597 Genomic DNA. Translation: AAF14640.1.
AJ271221 mRNA. Translation: CAB66340.1.
AJ413217 mRNA. Translation: CAC88757.2.
AJ422082 mRNA. Translation: CAD19443.1.
AJ422083 mRNA. Translation: CAD19444.1.
AE014297 Genomic DNA. Translation: AAF54493.2.
AE014297 Genomic DNA. Translation: AAN13451.1.
AE014297 Genomic DNA. Translation: AAN13452.1.
AE014297 Genomic DNA. Translation: AAN13453.1.
AE014297 Genomic DNA. Translation: AAN13454.1.
AY069182 mRNA. Translation: AAL39327.2.
BT031124 mRNA. Translation: ABX00746.1.
RefSeqiNP_001303443.1. NM_001316514.1. [Q9NFU0-2]
NP_001303444.1. NM_001316515.1. [Q9NFU0-2]
NP_611645.1. NM_137801.4. [Q9NFU0-1]
NP_731443.1. NM_169324.2. [Q9NFU0-2]
NP_731444.1. NM_169325.3. [Q9NFU0-2]
NP_731445.1. NM_169326.3. [Q9NFU0-3]
NP_731446.1. NM_169327.2. [Q9NFU0-4]
UniGeneiDm.5279.

3D structure databases

ProteinModelPortaliQ9NFU0.
SMRiQ9NFU0. Positions 1-201, 224-367.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi63147. 21 interactions.
IntActiQ9NFU0. 22 interactions.
MINTiMINT-248306.
STRINGi7227.FBpp0300445.

PTM databases

iPTMnetiQ9NFU0.

Proteomic databases

PaxDbiQ9NFU0.
PRIDEiQ9NFU0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0082197; FBpp0081675; FBgn0028734. [Q9NFU0-1]
GeneIDi37528.
KEGGidme:Dmel_CG6203.
UCSCiCG6203-RD. d. melanogaster.

Organism-specific databases

CTDi2332.
FlyBaseiFBgn0028734. Fmr1.

Phylogenomic databases

eggNOGiENOG410IF9J. Eukaryota.
ENOG410ZDJG. LUCA.
GeneTreeiENSGT00390000017033.
InParanoidiQ9NFU0.
KOiK15516.
OrthoDBiEOG7NKKJT.
PhylomeDBiQ9NFU0.

Miscellaneous databases

ChiTaRSiFmr1. fly.
GenomeRNAii37528.
PROiQ9NFU0.

Gene expression databases

BgeeiQ9NFU0.
ExpressionAtlasiQ9NFU0. differential.
GenevisibleiQ9NFU0. DM.

Family and domain databases

Gene3Di3.30.1370.10. 2 hits.
InterProiIPR008395. Agenet-like_dom.
IPR022034. FXMRP1_C_core.
IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
[Graphical view]
PfamiPF12235. FXMRP1_C_core. 1 hit.
PF00013. KH_1. 2 hits.
[Graphical view]
SMARTiSM00322. KH. 2 hits.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 2 hits.
PROSITEiPS51641. AGENET_LIKE. 2 hits.
PS50084. KH_TYPE_1. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of dFMR1, a Drosophila melanogaster homolog of the fragile X mental retardation protein."
    Wan L., Dockendorff T.C., Jongens T.A., Dreyfuss G.
    Mol. Cell. Biol. 20:8536-8547(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), SUBUNIT, RNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF ILE-244 AND ILE-307.
    Tissue: Ovary1 Publication.
  2. "Drosophila fragile X-related gene regulates the MAP1B homolog Futsch to control synaptic structure and function."
    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.
    Cell 107:591-603(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS A AND C), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: Berkeley1 Publication.
    Tissue: Embryo1 Publication.
  3. "Modeling human fragile X syndrome in flies."
    Zhang Y.Q., Broadie K.S.
    Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND C).
    Strain: Berkeley1 Publication.
    Tissue: Embryo1 Publication, Ovary1 Publication and TestisImported.
  4. "The genome sequence of Drosophila melanogaster."
    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.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley1 Publication.
  5. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 105-684 (ISOFORMS C/E).
    Strain: BerkeleyImported.
    Tissue: Embryo and Head.
  7. "A Drosophila fragile X protein interacts with components of RNAi and ribosomal proteins."
    Ishizuka A., Siomi M.C., Siomi H.
    Genes Dev. 16:2497-2508(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH AGO2; DCR-1; RM62; RPL5 AND RPL11, ASSOCIATION WITH POLYRIBOSOME.
  8. "CYFIP/Sra-1 controls neuronal connectivity in Drosophila and links the Rac1 GTPase pathway to the fragile X protein."
    Schenck A., Bardoni B., Langmann C., Harden N., Mandel J.-L., Giangrande A.
    Neuron 38:887-898(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRA-1.
  9. "The Drosophila fragile X-related gene regulates axoneme differentiation during spermatogenesis."
    Zhang Y.Q., Matthies H.J.G., Mancuso J., Andrews H.K., Woodruff E. III, Friedman D., Broadie K.S.
    Dev. Biol. 270:290-307(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  10. "The role of PIWI and the miRNA machinery in Drosophila germline determination."
    Megosh H.B., Cox D.N., Campbell C., Lin H.
    Curr. Biol. 16:1884-1894(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PIWI AND VAS.
  11. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403; SER-408; SER-409; SER-413; SER-532; SER-533; SER-539 AND SER-541, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiFMR1_DROME
AccessioniPrimary (citable) accession number: Q9NFU0
Secondary accession number(s): A4V2M8
, Q8INM7, Q8T0M0, Q8WQ60, Q95P21, Q9GSG3, Q9TVY4, Q9VH27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: October 1, 2000
Last modified: July 6, 2016
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.