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P35922

- FMR1_MOUSE

UniProt

P35922 - FMR1_MOUSE

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
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    3. 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

    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. nucleolus Source: UniProtKB-SubCell
    6. nucleus Source: MGI

    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.
    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

    MEELVVEVRG SNGAFYKAFV KDVHEDSITV AFENNWQPER QIPFHDVRFP    50
    PPVGYNKDIN ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD 100
    ATYNEIVTIE RLRSVNPNKP ATKDTFHKIK LEVPEDLRQM CAKESAHKDF 150
    KKAVGAFSVT YDPENYQLVI LSINEVTSKR AHMLIDMHFR SLRTKLSLIL 200
    RNEEASKQLE SSRQLASRFH EQFIVREDLM GLAIGTHGAN IQQARKVPGV 250
    TAIDLDEDTC TFHIYGEDQD AVKKARSFLE FAEDVIQVPR NLVGKVIGKN 300
    GKLIQEIVDK SGVVRVRIEA ENEKSVPQEE EIMPPSSLPS NNSRVGPNSS 350
    EEKKHLDTKE NTHFSQPNST KVQRVLVVSS IVAGGPQKPE PKAWQGMVPF 400
    VFVGTKDSIA NATVLLDYHL NYLKEVDQLR LERLQIDEQL RQIGASSRPP 450
    PNRTDKEKGY VTDDGQGMGR GSRPYRNRGH GRRGPGYTSG TNSEASNASE 500
    TESDHRDELS DWSLAPTEEE RESFLRRGDG RRRRGGGRGQ GGRGRGGGFK 550
    GNDDHSRTDN RPRNPREAKG RTADGSLQSA SSEGSRLRTG KDRNQKKEKP 600
    DSVDGLQPLV NGVP 614
    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.
    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 1, 2014
    This is version 130 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