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P35922

- FMR1_MOUSE

UniProt

P35922 - FMR1_MOUSE

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Protein

Fragile X mental retardation protein 1 homolog

Gene

Fmr1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

RNA-binding protein that plays a role in intracellular RNA transport and in the regulation of translation of target mRNAs. Associated with polysomes. May play a role in the transport of mRNA from the nucleus to the cytoplasm. Binds strongly to poly(G), binds moderately to poly(U) but shows very little binding to poly(A) or poly(C) (By similarity). Translation repressor. Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression. In the CYFIP1-EIF4E-FMR1 complex this subunit mediates translation repression.By similarity2 Publications

GO - Molecular functioni

  1. microtubule binding Source: MGI
  2. RNA binding Source: UniProtKB-KW

GO - Biological processi

  1. central nervous system development Source: MGI
  2. mRNA transport Source: UniProtKB-KW
  3. negative regulation of translational initiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

mRNA transport, Transport

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Fragile X mental retardation protein 1 homolog
Short name:
FMRP
Short name:
Protein FMR-1
Short name:
mFmr1p
Gene namesi
Name:Fmr1
Synonyms:Fmr-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:95564. Fmr1.

Subcellular locationi

Cytoplasm 1 Publication. Nucleusnucleolus By similarity

GO - Cellular componenti

  1. cell body Source: MGI
  2. cytoplasmic stress granule Source: MGI
  3. mRNA cap binding complex Source: UniProtKB
  4. neuronal ribonucleoprotein granule Source: MGI
  5. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Brain-region specific changes in the expression and/or localization of FAM206A/Simiate along with alterations in the appearance, distribution and volume of nuclear speckles (FMR1 was shown to associate with FAM206A mRNAs).1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi499 – 4991S → A: Loss of phosphorylation. 1 Publication
Mutagenesisi499 – 4991S → D: Leads to phosphorylation on other serine residues. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 614614Fragile X mental retardation protein 1 homologPRO_0000050103Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei336 – 3361PhosphoserineBy similarity
Modified residuei337 – 3371PhosphoserineBy similarity
Modified residuei349 – 3491PhosphoserineBy similarity
Modified residuei350 – 3501PhosphoserineBy similarity
Modified residuei369 – 3691PhosphoserineBy similarity
Modified residuei499 – 4991Phosphoserine1 Publication
Modified residuei543 – 5431Omega-N-methylated arginineBy similarity

Post-translational modificationi

Phosphorylated on several serine residues. Phosphorylation at Ser-499 is required for phosphorylation of other nearby serine residues. Phosphorylation has no effect on the binding of individual mRNA species, but may affect the interaction with polyribosomes.1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiP35922.
PaxDbiP35922.
PRIDEiP35922.

PTM databases

PhosphoSiteiP35922.

Expressioni

Tissue specificityi

In adults, expressed predominantly in the brain.1 Publication

Gene expression databases

CleanExiMM_FMR1.
GenevestigatoriP35922.

Interactioni

Subunit structurei

Homooligomer. Found in a RNP granule complex with IGF2BP1. Interacts with FXR1, FXR2, IGF2BP1 and RANBP9. Directly interacts with SMN and TDRD3 (By similarity). Component of the CYFIP1-EIF4E-FMR1 complex which is composed of CYFIP, EIF4E and FMR1. Interacts with CYFIP1 and CYFIP2. The interaction with brain cytoplasmic RNA 1 (BC1) increases binding affinity for the CYFIP1-EIF4E complex in the brain. Interacts with CYFIP1 and CYFIP2. Interacts with the SMN core complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Rcan1Q9JHG63EBI-645094,EBI-644061

Protein-protein interaction databases

IntActiP35922. 6 interactions.
MINTiMINT-111096.

Structurei

3D structure databases

ProteinModelPortaliP35922.
SMRiP35922. Positions 1-134, 216-334, 395-424.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 5047Agenet-like 1Add
BLAST
Domaini63 – 11553Agenet-like 2Add
BLAST
Domaini222 – 25130KH 1PROSITE-ProRule annotationAdd
BLAST
Domaini285 – 31430KH 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni418 – 614197Interaction with RANBP9By similarityAdd
BLAST
Regioni534 – 54714RNA-binding RGG-boxAdd
BLAST

Domaini

The tandem Tudor domains preferentially recognize trimethylated histone peptides.By similarity

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG75351.
HOGENOMiHOG000293377.
HOVERGENiHBG005739.
InParanoidiP35922.
PhylomeDBiP35922.

Family and domain databases

Gene3Di3.30.1370.10. 3 hits.
InterProiIPR008395. Agenet-like_dom.
IPR022034. Frag_X_MRP_fam.
IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
[Graphical view]
PfamiPF05641. Agenet. 1 hit.
PF12235. FXR1P_C. 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 (12)i

Sequence statusi: Complete.

This entry describes 12 isoformsi produced by alternative splicing. Align

Isoform ISO1 (identifier: P35922-1) [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
MEELVVEVRG SNGAFYKAFV KDVHEDSITV AFENNWQPER QIPFHDVRFP
60 70 80 90 100
PPVGYNKDIN ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD
110 120 130 140 150
ATYNEIVTIE RLRSVNPNKP ATKDTFHKIK LEVPEDLRQM CAKESAHKDF
160 170 180 190 200
KKAVGAFSVT YDPENYQLVI LSINEVTSKR AHMLIDMHFR SLRTKLSLIL
210 220 230 240 250
RNEEASKQLE SSRQLASRFH EQFIVREDLM GLAIGTHGAN IQQARKVPGV
260 270 280 290 300
TAIDLDEDTC TFHIYGEDQD AVKKARSFLE FAEDVIQVPR NLVGKVIGKN
310 320 330 340 350
GKLIQEIVDK SGVVRVRIEA ENEKSVPQEE EIMPPSSLPS NNSRVGPNSS
360 370 380 390 400
EEKKHLDTKE NTHFSQPNST KVQRVLVVSS IVAGGPQKPE PKAWQGMVPF
410 420 430 440 450
VFVGTKDSIA NATVLLDYHL NYLKEVDQLR LERLQIDEQL RQIGASSRPP
460 470 480 490 500
PNRTDKEKGY VTDDGQGMGR GSRPYRNRGH GRRGPGYTSG TNSEASNASE
510 520 530 540 550
TESDHRDELS DWSLAPTEEE RESFLRRGDG RRRRGGGRGQ GGRGRGGGFK
560 570 580 590 600
GNDDHSRTDN RPRNPREAKG RTADGSLQSA SSEGSRLRTG KDRNQKKEKP
610
DSVDGLQPLV NGVP
Length:614
Mass (Da):68,989
Last modified:June 1, 1994 - v1
Checksum:i093DD90D589ED066
GO
Isoform ISO2 (identifier: P35922-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     490-501: Missing.

Show »
Length:602
Mass (Da):67,840
Checksum:i731A506F0359F0E5
GO
Isoform ISO3 (identifier: P35922-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     490-514: Missing.

Show »
Length:589
Mass (Da):66,269
Checksum:i9462AD5A666E906A
GO
Isoform ISO4 (identifier: P35922-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     425-448: EVDQLRLERLQIDEQLRQIGASSR → ELILKHQMLLKQNLTTETNSVIGH
     449-614: Missing.

Show »
Length:448
Mass (Da):50,829
Checksum:i0F25006E964AD90C
GO
Isoform ISO5 (identifier: P35922-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     425-436: EVDQLRLERLQI → NLTTETNSVIGH
     437-614: Missing.

Show »
Length:436
Mass (Da):49,353
Checksum:i5AB0A796CC0CF180
GO
Isoform ISO6 (identifier: P35922-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     425-512: EVDQLRLERL...SDHRDELSDW → LQQRKRGRAS...VTRRRKSQTA
     513-614: Missing.

Show »
Length:512
Mass (Da):58,113
Checksum:i093A5C6493C61131
GO
Isoform ISO7 (identifier: P35922-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     375-395: Missing.

Show »
Length:593
Mass (Da):66,817
Checksum:iA5775ADA3613D93D
GO
Isoform ISO8 (identifier: P35922-8) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     375-395: Missing.
     490-501: Missing.

Show »
Length:581
Mass (Da):65,667
Checksum:i64ED438071325D40
GO
Isoform ISO9 (identifier: P35922-9) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     375-395: Missing.
     490-514: Missing.

Show »
Length:568
Mass (Da):64,097
Checksum:i94B1FEC72A1C7D1D
GO
Isoform ISO10 (identifier: P35922-10) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     375-395: Missing.
     425-448: EVDQLRLERLQIDEQLRQIGASSR → ELILKHQMLLKQNLTTETNSVIGH
     449-614: Missing.

Show »
Length:427
Mass (Da):48,656
Checksum:i8F1236A4CBBAE6FA
GO
Isoform ISO11 (identifier: P35922-11) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     375-395: Missing.
     425-436: EVDQLRLERLQI → NLTTETNSVIGH
     437-614: Missing.

Show »
Length:415
Mass (Da):47,180
Checksum:i8F5306E3316AAFF1
GO
Isoform ISO12 (identifier: P35922-12) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     375-395: Missing.
     425-512: EVDQLRLERL...SDHRDELSDW → LQQRKRGRAS...VTRRRKSQTA
     513-614: Missing.

Show »
Length:491
Mass (Da):55,940
Checksum:iF16075B4136A226F
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei375 – 39521Missing in isoform ISO7, isoform ISO8, isoform ISO9, isoform ISO10, isoform ISO11 and isoform ISO12. CuratedVSP_002827Add
BLAST
Alternative sequencei425 – 51288EVDQL…ELSDW → LQQRKRGRASCAEETDGGVE EEEEDKEEEEEEEASKETTI IPEQIIVHVIQERLKEEQLM DPCRVPPVKGAGCARVKIVT RRRKSQTA in isoform ISO6 and isoform ISO12. CuratedVSP_002834Add
BLAST
Alternative sequencei425 – 44824EVDQL…GASSR → ELILKHQMLLKQNLTTETNS VIGH in isoform ISO4 and isoform ISO10. CuratedVSP_002831Add
BLAST
Alternative sequencei425 – 43612EVDQL…ERLQI → NLTTETNSVIGH in isoform ISO5 and isoform ISO11. CuratedVSP_002832Add
BLAST
Alternative sequencei437 – 614178Missing in isoform ISO5 and isoform ISO11. CuratedVSP_002833Add
BLAST
Alternative sequencei449 – 614166Missing in isoform ISO4 and isoform ISO10. CuratedVSP_002830Add
BLAST
Alternative sequencei490 – 51425Missing in isoform ISO3 and isoform ISO9. CuratedVSP_002829Add
BLAST
Alternative sequencei490 – 50112Missing in isoform ISO2 and isoform ISO8. CuratedVSP_002828Add
BLAST
Alternative sequencei513 – 614102Missing in isoform ISO6 and isoform ISO12. CuratedVSP_002835Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L23971 mRNA. Translation: AAA37635.1.
CCDSiCCDS30171.1. [P35922-1]
CCDS72385.1. [P35922-3]
PIRiS36173.
UniGeneiMm.3451.

Genome annotation databases

UCSCiuc009tiu.1. mouse. [P35922-1]
uc009tiv.1. mouse. [P35922-11]
uc009tiy.1. mouse. [P35922-5]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L23971 mRNA. Translation: AAA37635.1 .
CCDSi CCDS30171.1. [P35922-1 ]
CCDS72385.1. [P35922-3 ]
PIRi S36173.
UniGenei Mm.3451.

3D structure databases

ProteinModelPortali P35922.
SMRi P35922. Positions 1-134, 216-334, 395-424.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P35922. 6 interactions.
MINTi MINT-111096.

PTM databases

PhosphoSitei P35922.

Proteomic databases

MaxQBi P35922.
PaxDbi P35922.
PRIDEi P35922.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

UCSCi uc009tiu.1. mouse. [P35922-1 ]
uc009tiv.1. mouse. [P35922-11 ]
uc009tiy.1. mouse. [P35922-5 ]

Organism-specific databases

MGIi MGI:95564. Fmr1.

Phylogenomic databases

eggNOGi NOG75351.
HOGENOMi HOG000293377.
HOVERGENi HBG005739.
InParanoidi P35922.
PhylomeDBi P35922.

Miscellaneous databases

ChiTaRSi FMR1. mouse.
PROi P35922.
SOURCEi Search...

Gene expression databases

CleanExi MM_FMR1.
Genevestigatori P35922.

Family and domain databases

Gene3Di 3.30.1370.10. 3 hits.
InterProi IPR008395. Agenet-like_dom.
IPR022034. Frag_X_MRP_fam.
IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
[Graphical view ]
Pfami PF05641. Agenet. 1 hit.
PF12235. FXR1P_C. 1 hit.
PF00013. KH_1. 2 hits.
[Graphical view ]
SMARTi SM00322. KH. 2 hits.
[Graphical view ]
SUPFAMi SSF54791. SSF54791. 2 hits.
PROSITEi PS51641. AGENET_LIKE. 2 hits.
PS50084. KH_TYPE_1. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Human and murine FMR-1: alternative splicing and translational initiation downstream of the CGG-repeat."
    Ashley C.T. Jr., Sutcliffe J.S., Kunst C.B., Leiner H.A., Eichler E.E., Nelson D.L., Warren S.T.
    Nat. Genet. 4:244-251(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
    Strain: BALB/c.
    Tissue: Brain.
  2. "A novel RNA-binding nuclear protein that interacts with the fragile X mental retardation (FMR1) protein."
    Bardoni B., Schenck A., Mandel J.-L.
    Hum. Mol. Genet. 8:2557-2566(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NUFIP1.
  3. "A highly conserved protein family interacting with the fragile X mental retardation protein (FMRP) and displaying selective interactions with FMRP-related proteins FXR1P and FXR2P."
    Schenck A., Bardoni B., Moro A., Bagni C., Mandel J.-L.
    Proc. Natl. Acad. Sci. U.S.A. 98:8844-8849(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CYFIP1 AND CYFIP2.
  4. "Phosphorylation influences the translation state of FMRP-associated polyribosomes."
    Ceman S., O'Donnell W.T., Reed M., Patton S., Pohl J., Warren S.T.
    Hum. Mol. Genet. 12:3295-3305(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-499, MUTAGENESIS OF SER-499, IDENTIFICATION BY MASS SPECTROMETRY.
  5. "The RNA-binding protein Fragile X-related 1 regulates somite formation in Xenopus laevis."
    Huot M.-E., Bisson N., Davidovic L., Mazroui R., Labelle Y., Moss T., Khandjian E.W.
    Mol. Biol. Cell 16:4350-4361(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. "The fragile X syndrome protein represses activity-dependent translation through CYFIP1, a new 4E-BP."
    Napoli I., Mercaldo V., Boyl P.P., Eleuteri B., Zalfa F., De Rubeis S., Di Marino D., Mohr E., Massimi M., Falconi M., Witke W., Costa-Mattioli M., Sonenberg N., Achsel T., Bagni C.
    Cell 134:1042-1054(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CYFIP1-EIF4E COMPLEX, BC1 RNA-BINDING.
  7. "In vitro and in cellulo evidences for association of the survival of motor neuron complex with the fragile X mental retardation protein."
    Piazzon N., Rage F., Schlotter F., Moine H., Branlant C., Massenet S.
    J. Biol. Chem. 283:5598-5610(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THE SMN CORE COMPLEX.
  8. "Identification and characterisation of Simiate, a novel protein linked to the fragile X syndrome."
    Derlig K., Giessl A., Brandstatter J.H., Enz R., Dahlhaus R.
    PLoS ONE 8:E83007-E83007(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiFMR1_MOUSE
AccessioniPrimary (citable) accession number: P35922
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: October 29, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

RNA-binding activity is inhibited by RANBP9.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3