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P35922 (FMR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fragile X mental retardation protein 1 homolog
Short name=FMRP
Short name=Protein FMR-1
Short name=mFmr1p
Gene names
Name:Fmr1
Synonyms:Fmr-1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length614 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.6

Subunit structure

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. Ref.2 Ref.3 Ref.6 Ref.7

Subcellular location

Cytoplasm. Nucleus › nucleolus By similarity Ref.4.

Tissue specificity

In adults, expressed predominantly in the brain. Ref.5

Domain

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

Post-translational modification

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. Ref.4

Miscellaneous

RNA-binding activity is inhibited by RANBP9.

Sequence similarities

Belongs to the FMR1 family.

Contains 2 Agenet-like domains.

Contains 2 KH domains.

Alternative products

This entry describes 12 isoforms produced by alternative splicing. [Align] [Select]
Isoform ISO1 (identifier: P35922-1)

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.
Isoform ISO2 (identifier: P35922-2)

The sequence of this isoform differs from the canonical sequence as follows:
     490-501: Missing.
Isoform ISO3 (identifier: P35922-3)

The sequence of this isoform differs from the canonical sequence as follows:
     490-514: Missing.
Isoform ISO4 (identifier: P35922-4)

The sequence of this isoform differs from the canonical sequence as follows:
     425-448: EVDQLRLERLQIDEQLRQIGASSR → ELILKHQMLLKQNLTTETNSVIGH
     449-614: Missing.
Isoform ISO5 (identifier: P35922-5)

The sequence of this isoform differs from the canonical sequence as follows:
     425-436: EVDQLRLERLQI → NLTTETNSVIGH
     437-614: Missing.
Isoform ISO6 (identifier: P35922-6)

The sequence of this isoform differs from the canonical sequence as follows:
     425-512: EVDQLRLERL...SDHRDELSDW → LQQRKRGRAS...VTRRRKSQTA
     513-614: Missing.
Isoform ISO7 (identifier: P35922-7)

The sequence of this isoform differs from the canonical sequence as follows:
     375-395: Missing.
Isoform ISO8 (identifier: P35922-8)

The sequence of this isoform differs from the canonical sequence as follows:
     375-395: Missing.
     490-501: Missing.
Isoform ISO9 (identifier: P35922-9)

The sequence of this isoform differs from the canonical sequence as follows:
     375-395: Missing.
     490-514: Missing.
Isoform ISO10 (identifier: P35922-10)

The sequence of this isoform differs from the canonical sequence as follows:
     375-395: Missing.
     425-448: EVDQLRLERLQIDEQLRQIGASSR → ELILKHQMLLKQNLTTETNSVIGH
     449-614: Missing.
Isoform ISO11 (identifier: P35922-11)

The sequence of this isoform differs from the canonical sequence as follows:
     375-395: Missing.
     425-436: EVDQLRLERLQI → NLTTETNSVIGH
     437-614: Missing.
Isoform ISO12 (identifier: P35922-12)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 614614Fragile X mental retardation protein 1 homolog
PRO_0000050103

Regions

Domain4 – 5047Agenet-like 1
Domain63 – 11553Agenet-like 2
Domain222 – 25130KH 1
Domain285 – 31430KH 2
Region418 – 614197Interaction with RANBP9 By similarity
Region534 – 54714RNA-binding RGG-box

Amino acid modifications

Modified residue3691Phosphoserine By similarity
Modified residue4991Phosphoserine Ref.4
Modified residue5431Omega-N-methylated arginine By similarity

Natural variations

Alternative sequence375 – 39521Missing in isoform ISO7, isoform ISO8, isoform ISO9, isoform ISO10, isoform ISO11 and isoform ISO12.
VSP_002827
Alternative sequence425 – 51288EVDQL…ELSDW → LQQRKRGRASCAEETDGGVE EEEEDKEEEEEEEASKETTI IPEQIIVHVIQERLKEEQLM DPCRVPPVKGAGCARVKIVT RRRKSQTA in isoform ISO6 and isoform ISO12.
VSP_002834
Alternative sequence425 – 44824EVDQL…GASSR → ELILKHQMLLKQNLTTETNS VIGH in isoform ISO4 and isoform ISO10.
VSP_002831
Alternative sequence425 – 43612EVDQL…ERLQI → NLTTETNSVIGH in isoform ISO5 and isoform ISO11.
VSP_002832
Alternative sequence437 – 614178Missing in isoform ISO5 and isoform ISO11.
VSP_002833
Alternative sequence449 – 614166Missing in isoform ISO4 and isoform ISO10.
VSP_002830
Alternative sequence490 – 51425Missing in isoform ISO3 and isoform ISO9.
VSP_002829
Alternative sequence490 – 50112Missing in isoform ISO2 and isoform ISO8.
VSP_002828
Alternative sequence513 – 614102Missing in isoform ISO6 and isoform ISO12.
VSP_002835

Experimental info

Mutagenesis4991S → A: Loss of phosphorylation. Ref.4
Mutagenesis4991S → D: Leads to phosphorylation on other serine residues. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform ISO1 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 093DD90D589ED066

FASTA61468,989
        10         20         30         40         50         60 
MEELVVEVRG SNGAFYKAFV KDVHEDSITV AFENNWQPER QIPFHDVRFP PPVGYNKDIN 

        70         80         90        100        110        120 
ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD ATYNEIVTIE RLRSVNPNKP 

       130        140        150        160        170        180 
ATKDTFHKIK LEVPEDLRQM CAKESAHKDF KKAVGAFSVT YDPENYQLVI LSINEVTSKR 

       190        200        210        220        230        240 
AHMLIDMHFR SLRTKLSLIL RNEEASKQLE SSRQLASRFH EQFIVREDLM GLAIGTHGAN 

       250        260        270        280        290        300 
IQQARKVPGV TAIDLDEDTC TFHIYGEDQD AVKKARSFLE FAEDVIQVPR NLVGKVIGKN 

       310        320        330        340        350        360 
GKLIQEIVDK SGVVRVRIEA ENEKSVPQEE EIMPPSSLPS NNSRVGPNSS EEKKHLDTKE 

       370        380        390        400        410        420 
NTHFSQPNST KVQRVLVVSS IVAGGPQKPE PKAWQGMVPF VFVGTKDSIA NATVLLDYHL 

       430        440        450        460        470        480 
NYLKEVDQLR LERLQIDEQL RQIGASSRPP PNRTDKEKGY VTDDGQGMGR GSRPYRNRGH 

       490        500        510        520        530        540 
GRRGPGYTSG TNSEASNASE TESDHRDELS DWSLAPTEEE RESFLRRGDG RRRRGGGRGQ 

       550        560        570        580        590        600 
GGRGRGGGFK GNDDHSRTDN RPRNPREAKG RTADGSLQSA SSEGSRLRTG KDRNQKKEKP 

       610 
DSVDGLQPLV NGVP

« Hide

Isoform ISO2 [UniParc].

Checksum: 731A506F0359F0E5
Show »

FASTA60267,840
Isoform ISO3 [UniParc].

Checksum: 9462AD5A666E906A
Show »

FASTA58966,269
Isoform ISO4 [UniParc].

Checksum: 0F25006E964AD90C
Show »

FASTA44850,829
Isoform ISO5 [UniParc].

Checksum: 5AB0A796CC0CF180
Show »

FASTA43649,353
Isoform ISO6 [UniParc].

Checksum: 093A5C6493C61131
Show »

FASTA51258,113
Isoform ISO7 [UniParc].

Checksum: A5775ADA3613D93D
Show »

FASTA59366,817
Isoform ISO8 [UniParc].

Checksum: 64ED438071325D40
Show »

FASTA58165,667
Isoform ISO9 [UniParc].

Checksum: 94B1FEC72A1C7D1D
Show »

FASTA56864,097
Isoform ISO10 [UniParc].

Checksum: 8F1236A4CBBAE6FA
Show »

FASTA42748,656
Isoform ISO11 [UniParc].

Checksum: 8F5306E3316AAFF1
Show »

FASTA41547,180
Isoform ISO12 [UniParc].

Checksum: F16075B4136A226F
Show »

FASTA49155,940

References

[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, 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L23971 mRNA. Translation: AAA37635.1.
IPIIPI00227005.
IPI00227006.
IPI00227007.
IPI00227008.
IPI00227013.
IPI00230029.
IPI00230030.
IPI00230031.
IPI00270737.
IPI00469993.
IPI00474739.
IPI00475390.
PIRS36173.
UniGeneMm.3451.

3D structure databases

ProteinModelPortalP35922.
SMRP35922. Positions 1-134, 216-334, 395-424.
ModBaseSearch...

Protein-protein interaction databases

IntActP35922. 3 interactions.
MINTMINT-111096.

PTM databases

PhosphoSiteP35922.

Proteomic databases

PaxDbP35922.
PRIDEP35922.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCuc009tiu.1. mouse.
uc009tiv.1. mouse.

Organism-specific databases

MGIMGI:95564. Fmr1.

Phylogenomic databases

eggNOGNOG75351.
HOGENOMHOG000293377.
HOVERGENHBG005739.
OrthoDBEOG4PK27F.

Gene expression databases

CleanExMM_FMR1.
GenevestigatorP35922.
GermOnlineENSMUSG00000000838. Mus musculus.

Family and domain databases

InterProIPR008395. Agenet-like_dom.
IPR022034. Frag_X_MRP_fam.
IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
[Graphical view]
PfamPF05641. Agenet. 1 hit.
PF12235. FXR1P_C. 1 hit.
PF00013. KH_1. 2 hits.
[Graphical view]
SMARTSM00322. KH. 2 hits.
[Graphical view]
PROSITEPS51641. AGENET_LIKE. 2 hits.
PS50084. KH_TYPE_1. 2 hits.
PS50304. TUDOR. False negative.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFMR1. mouse.
SOURCESearch...

Entry information

Entry nameFMR1_MOUSE
AccessionPrimary (citable) accession number: P35922
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: May 1, 2013
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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