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Q06787 (FMR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fragile X mental retardation protein 1

Short name=FMRP
Short name=Protein FMR-1
Gene names
Name:FMR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length632 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 similarity. 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).

Subunit structure

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 By similarity. Homooligomer. Found in a RNP granule complex with IGF2BP1. Directly interacts with SMN and TDRD3. Interacts with the SMN core complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP. Interacts with FXR1, FXR2, IGF2BP1, NUFIP1, NUFIP2, MCRS1 and RANBP9. Ref.17 Ref.19 Ref.20 Ref.21 Ref.23 Ref.24 Ref.25 Ref.30 Ref.38

Subcellular location

Cytoplasm. Nucleusnucleolus Ref.12 Ref.13 Ref.15 Ref.19 Ref.23 Ref.30.

Tissue specificity

Highest levels found in neurons, brain, testis, placenta and lymphocytes. Also expressed in epithelial tissues and at very low levels in glial cells. Ref.2 Ref.13

Domain

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

Post-translational modification

Phosphorylated on several serine residues By similarity. Ref.18

Involvement in disease

Fragile X syndrome (FRAX) [MIM:300624]: Common genetic disease (has a prevalence of one in every 2000 children) which is characterized by moderate to severe mental retardation, macroorchidism (enlargement of the testicles), large ears, prominent jaw, and high-pitched, jocular speech. The defect in most fragile X syndrome patients results from an amplification of a CGG repeat region which is directly in front of the coding region.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.13 Ref.31 Ref.32 Ref.33 Ref.35 Ref.37 Ref.38

Fragile X tremor/ataxia syndrome (FXTAS) [MIM:300623]: In FXTAS, the expanded repeats range in size from 55 to 200 repeats and are referred to as 'premutations'. Full repeat expansions with greater than 200 repeats results in fragile X mental retardation syndrome [MIM:300624]. Carriers of the premutation typically do not show the full fragile X syndrome phenotype, but comprise a subgroup that may have some physical features of fragile X syndrome or mild cognitive and emotional problems.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.36

Premature ovarian failure 1 (POF1) [MIM:311360]: An ovarian disorder defined as the cessation of ovarian function under the age of 40 years. It is characterized by oligomenorrhea or amenorrhea, in the presence of elevated levels of serum gonadotropins and low estradiol.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16

Miscellaneous

RNA-binding activity is inhibited by RANBP9.

The mechanism of the severe phenotype in the Asn-304 patient lies in the sequestration of bound mRNAs in nontranslatable mRNP particles. In the absence of FMRP, these same mRNAs may be partially translated via alternate mRNPs, although perhaps abnormally localized or regulated, resulting in typical fragile X syndrome. Asn-304 mutation maps to a position within the second KH domain of FMRP that is critical for stabilizing sequence-specific RNA-protein interactions. Asn-304 mutation abrogates the association of the FMRP KH 2 domain with its target, kissing complex RNA.

Sequence similarities

Belongs to the FMR1 family.

Contains 2 Agenet-like domains.

Contains 2 KH domains.

Sequence caution

The sequence AAA52458.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAA62466.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAA62467.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processmRNA transport
Transport
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Mental retardation
Premature ovarian failure
   DomainRepeat
   LigandRNA-binding
   Molecular functionRepressor
   PTMAcetylation
Methylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcentral nervous system development

Inferred from electronic annotation. Source: Ensembl

mRNA transport

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of translational initiation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Traceable author statement Ref.30. Source: HGNC

cytoplasmic stress granule

Inferred from electronic annotation. Source: Ensembl

dendritic shaft

Inferred from electronic annotation. Source: Ensembl

dendritic spine

Inferred from electronic annotation. Source: Ensembl

mRNA cap binding complex

Inferred from sequence or structural similarity. Source: UniProtKB

neuronal ribonucleoprotein granule

Inferred from electronic annotation. Source: Ensembl

nucleolus

Traceable author statement Ref.30. Source: HGNC

nucleoplasm

Traceable author statement PubMed 10888599. Source: ProtInc

synapse

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionRNA binding

Traceable author statement PubMed 8156595. Source: ProtInc

mRNA binding

Traceable author statement Ref.14. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 11438699. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CYFIP1Q7L5764EBI-366305,EBI-1048143
CYFIP2Q96F072EBI-366305,EBI-2433893

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]

Note: At least 12 different isoforms are produced.
Isoform 6 (identifier: Q06787-1)

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 1 (identifier: Q06787-2)

The sequence of this isoform differs from the canonical sequence as follows:
     376-396: Missing.
     580-596: Missing.
Isoform 2 (identifier: Q06787-3)

The sequence of this isoform differs from the canonical sequence as follows:
     491-502: Missing.
Isoform 3 (identifier: Q06787-4)

The sequence of this isoform differs from the canonical sequence as follows:
     491-502: Missing.
     580-596: Missing.
Isoform 4 (identifier: Q06787-5)

The sequence of this isoform differs from the canonical sequence as follows:
     491-515: Missing.
Isoform 5 (identifier: Q06787-6)

The sequence of this isoform differs from the canonical sequence as follows:
     491-515: Missing.
     580-596: Missing.
Isoform 7 (identifier: Q06787-7)

The sequence of this isoform differs from the canonical sequence as follows:
     580-596: Missing.
Isoform 8 (identifier: Q06787-8)

The sequence of this isoform differs from the canonical sequence as follows:
     376-396: Missing.
     491-515: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 632632Fragile X mental retardation protein 1
PRO_0000050102

Regions

Domain4 – 5047Agenet-like 1
Domain63 – 11553Agenet-like 2
Domain222 – 25130KH 1
Domain285 – 31430KH 2
Region419 – 632214Interaction with RANBP9
Region534 – 54815RNA-binding RGG-box

Amino acid modifications

Modified residue11N-acetylmethionine Ref.28
Modified residue3371Phosphoserine By similarity
Modified residue3701Phosphoserine Ref.26
Modified residue5001Phosphoserine Ref.18
Modified residue5441Omega-N-methylated arginine Ref.22

Natural variations

Alternative sequence376 – 39621Missing in isoform 1 and isoform 8.
VSP_002823
Alternative sequence491 – 51525Missing in isoform 4, isoform 5 and isoform 8.
VSP_002825
Alternative sequence491 – 50212Missing in isoform 2 and isoform 3.
VSP_002824
Alternative sequence580 – 59617Missing in isoform 1, isoform 3, isoform 5 and isoform 7.
VSP_002826
Natural variant1381R → Q Rare variant found in a developmentally delayed male; unknown pathological significance. Ref.39
VAR_064507
Natural variant1451A → S.
Corresponds to variant rs29281 [ dbSNP | Ensembl ].
VAR_029278
Natural variant3041I → N in FRAX; alters protein folding and stability; the protein is able to bind RNA, but has reduced affinity for RNA at high salt concentrations. Ref.31 Ref.32 Ref.33 Ref.35 Ref.37 Ref.38
VAR_005234
Natural variant5461R → H. Ref.34
VAR_005235

Experimental info

Mutagenesis125 – 1262TF → AA: Alters the structural integrity of the N-terminus and leads to aggregation. Ref.30
Mutagenesis5001S → A: Loss of phosphorylation. Ref.18 Ref.30
Mutagenesis5441R → K: Reduces arginine methylation by 80%. Ref.22 Ref.30
Mutagenesis5461R → K: Slightly reduced methylation. Ref.22 Ref.30
Sequence conflict294 – 2952Missing in AAA52458. Ref.1

Secondary structure

.................................................. 632
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 6 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: F853D6C82E3489B9

FASTA63271,174
        10         20         30         40         50         60 
MEELVVEVRG SNGAFYKAFV KDVHEDSITV AFENNWQPDR QIPFHDVRFP PPVGYNKDIN 

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

       130        140        150        160        170        180 
ATKDTFHKIK LDVPEDLRQM CAKEAAHKDF KKAVGAFSVT YDPENYQLVI LSINEVTSKR 

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

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

       310        320        330        340        350        360 
GKLIQEIVDK SGVVRVRIEA ENEKNVPQEE EIMPPNSLPS NNSRVGPNAP EEKKHLDIKE 

       370        380        390        400        410        420 
NSTHFSQPNS TKVQRVLVAS SVVAGESQKP ELKAWQGMVP FVFVGTKDSI ANATVLLDYH 

       430        440        450        460        470        480 
LNYLKEVDQL RLERLQIDEQ LRQIGASSRP PPNRTDKEKS YVTDDGQGMG RGSRPYRNRG 

       490        500        510        520        530        540 
HGRRGPGYTS GTNSEASNAS ETESDHRDEL SDWSLAPTEE ERESFLRRGD GRRRGGGGRG 

       550        560        570        580        590        600 
QGGRGRGGGF KGNDDHSRTD NRPRNPREAK GRTTDGSLQI RVDCNNERSV HTKTLQNTSS 

       610        620        630 
EGSRLRTGKD RNQKKEKPDS VDGQQPLVNG VP 

« Hide

Isoform 1 [UniParc].

Checksum: BC65C14768EB268C
Show »

FASTA59466,971
Isoform 2 [UniParc].

Checksum: 8C8BC3876E1D92CA
Show »

FASTA62070,025
Isoform 3 [UniParc].

Checksum: B8F3364E88A3489B
Show »

FASTA60368,030
Isoform 4 [UniParc].

Checksum: 561113CBB00CCAD0
Show »

FASTA60768,455
Isoform 5 [UniParc].

Checksum: 643FA1A3826879A3
Show »

FASTA59066,460
Isoform 7 [UniParc].

Checksum: FE061178DA0A7ABB
Show »

FASTA61569,179
Isoform 8 [UniParc].

Checksum: B413D4F8FA0D697F
Show »

FASTA58666,246

References

« Hide 'large scale' references
[1]"Identification of a gene (FMR-1) containing a CGG repeat coincident with a breakpoint cluster region exhibiting length variation in fragile X syndrome."
Verkerk A.J.M.H., Pieretti M., Sutcliffe J.S., Fu Y.H., Kuhl D.P., Pizzuti A., Reiner O., Richards S., Victoria M.F., Zhang F., Eussen B.E., van Ommen G.-J.B., Blonden L.A.J., Riggins G.J., Chastain J.L., Kunst C.B., Galjaard H., Caskey C.T. expand/collapse author list , Nelson D.L., Oostra B.A., Warren S.T.
Cell 65:905-914(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING.
Tissue: Fetal brain.
[2]"Alternative splicing in the fragile X gene FMR1."
Verkerk A.J.M.H., de Graaff E., de Boulle K., Eichler E.E., Konecki D.S., Reyniers E., Manca A., Poustka A., Willems P.J., Nelson D.L., Oostra B.A.
Hum. Mol. Genet. 2:399-404(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), TISSUE SPECIFICITY.
Tissue: Fetal brain and Liver.
[3]Erratum
Verkerk A.J.H.M., de Graaff E., de Boulle K., Eichler E.E., Konecki D.S., Reyniers E., Manca A., Poustka A., Willems P.J., Nelson D.L., Oostra B.A.
Hum. Mol. Genet. 2:1348-1348(1993) [PubMed] [Europe PMC] [Abstract]
[4]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
Tissue: Placenta.
[7]"Fine structure of the human FMR1 gene."
Eichler E.E., Richards S., Gibbs R.A., Nelson D.L.
Hum. Mol. Genet. 2:1147-1153(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34; 36-139; 141-293; 295-490 AND 492-632.
[8]Erratum
Eichler E.E., Richards S., Gibbs R.A., Nelson D.L.
Hum. Mol. Genet. 3:684-685(1994) [PubMed] [Europe PMC] [Abstract]
[9]Eichler E.E., Richards S., Gibbs R.A., Nelson D.L.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 18-34.
[10]"Two new cases of FMR1 deletion associated with mental impairment."
Hirst M., Grewal P., Flannery A., Slatter R., Maher E., Barton D., Fryns J.-P., Davies K.
Am. J. Hum. Genet. 56:67-74(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
[11]"The protein product of the fragile X gene, FMR1, has characteristics of an RNA-binding protein."
Siomi H., Siomi M.C., Nussbaum R.L., Dreyfuss G.
Cell 74:291-298(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA-BINDING, INVOLVEMENT IN FRAX.
[12]"Characterization and localization of the FMR-1 gene product associated with fragile X syndrome."
Verheij C., Bakker C.E., de Graaff E., Keulemans J., Willemsen R., Verkerk A.J.M.H., Galjaard H., Reuser A.J.J., Hoogeveen A.T., Oostra B.A.
Nature 363:722-724(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[13]"The FMR-1 protein is cytoplasmic, most abundant in neurons and appears normal in carriers of a fragile X premutation."
Devys D., Lutz Y., Rouyer N., Bellocq J.-P., Mandel J.-L.
Nat. Genet. 4:335-340(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INVOLVEMENT IN FRAX.
[14]"FMR1 protein: conserved RNP family domains and selective RNA binding."
Ashley C.T. Jr., Wilkinson K.D., Reines D., Warren S.T.
Science 262:563-566(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA-BINDING.
[15]"FXR1, an autosomal homolog of the fragile X mental retardation gene."
Siomi M.C., Siomi H., Sauer W.H., Srinivasan S., Nussbaum R.L., Dreyfuss G.
EMBO J. 14:2401-2408(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA-BINDING, SUBCELLULAR LOCATION.
[16]"Studies of FRAXA and FRAXE in women with premature ovarian failure."
Murray A., Webb J., Grimley S., Conway G., Jacobs P.
J. Med. Genet. 35:637-640(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN POF1.
[17]"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.
[18]"Casein kinase II phosphorylates the fragile X mental retardation protein and modulates its biological properties."
Siomi M.C., Higashijima K., Ishizuka A., Siomi H.
Mol. Cell. Biol. 22:8438-8447(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-500, MUTAGENESIS OF SER-500.
[19]"82-FIP, a novel FMRP (fragile X mental retardation protein) interacting protein, shows a cell cycle-dependent intracellular localization."
Bardoni B., Castets M., Huot M.-E., Schenck A., Adinolfi S., Corbin F., Pastore A., Khandjian E.W., Mandel J.-L.
Hum. Mol. Genet. 12:1689-1698(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NUFIP2, SUBCELLULAR LOCATION.
[20]"Visualization of RNA-protein interactions in living cells: FMRP and IMP1 interact on mRNAs."
Rackham O., Brown C.M.
EMBO J. 23:3346-3355(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A RNP GRANULE COMPLEX WITH IGF2BP1, INTERACTION WITH IGF2BP1.
[21]"The C-terminus of fragile X mental retardation protein interacts with the multi-domain Ran-binding protein in the microtubule-organising centre."
Menon R.P., Gibson T.J., Pastore A.
J. Mol. Biol. 343:43-53(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RANBP9.
[22]"Alternative splicing modulates protein arginine methyltransferase-dependent methylation of fragile X syndrome mental retardation protein."
Dolzhanskaya N., Merz G., Denman R.B.
Biochemistry 45:10385-10393(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT ARG-544, MUTAGENESIS OF ARG-544 AND ARG-546.
[23]"The nuclear microspherule protein 58 is a novel RNA-binding protein that interacts with fragile X mental retardation protein in polyribosomal mRNPs from neurons."
Davidovic L., Bechara E., Gravel M., Jaglin X.H., Tremblay S., Sik A., Bardoni B., Khandjian E.W.
Hum. Mol. Genet. 15:1525-1538(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MCRS1, SUBCELLULAR LOCATION.
[24]"TDRD3, a novel Tudor domain-containing protein, localizes to cytoplasmic stress granules."
Goulet I., Boisvenue S., Mokas S., Mazroui R., Cote J.
Hum. Mol. Genet. 17:3055-3074(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TDRD3.
[25]"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 SMN AND THE SMN CORE COMPLEX.
[26]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[27]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"The solution structure of the first KH domain of FMR1, the protein responsible for the fragile X syndrome."
Musco G., Kharrat A., Stier G., Fraternali F., Gibson T.J., Nilges M., Pastore A.
Nat. Struct. Biol. 4:712-716(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 216-280.
[30]"The structure of the N-terminal domain of the fragile X mental retardation protein: a platform for protein-protein interaction."
Ramos A., Hollingworth D., Adinolfi S., Castets M., Kelly G., Frenkiel T.A., Bardoni B., Pastore A.
Structure 14:21-31(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-134, MUTAGENESIS OF 125-THR-PHE-126, SUBCELLULAR LOCATION, INTERACTION WITH NUFIP2.
[31]"Fragile X mental retardation syndrome: structure of the KH1-KH2 domains of fragile X mental retardation protein."
Valverde R., Pozdnyakova I., Kajander T., Venkatraman J., Regan L.
Structure 15:1090-1098(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 397-425, CHARACTERIZATION OF VARIANT FRAX ASN-304.
[32]"A point mutation in the FMR-1 gene associated with fragile X mental retardation."
de Boulle K., Verkerk A.J.M.H., Reyniers E., Vits L., Hendrickx J., van Roy B., van den Bos F., de Graaff E., Oostra B.A., Willems P.J.
Nat. Genet. 3:31-35(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FRAX ASN-304.
[33]"Characterization of FMR1 proteins isolated from different tissues."
Verheij C., de Graaff E., Bakker C.E., Willemsen R., Willems P.J., Meijer N., Galjaard H., Reuser A.J.J., Oostra B.A., Hoogeveen A.T.
Hum. Mol. Genet. 4:895-901(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF FRAX ASN-304.
[34]"Novel point mutation within intron 10 of FMR-1 gene causing fragile X syndrome."
Wang Y.-C., Lin M.-L., Lin S.J., Li Y.-C., Li S.-Y.
Hum. Mutat. 10:393-399(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HIS-546.
[35]"FMRP associates with polyribosomes as an mRNP, and the I304N mutation of severe fragile X syndrome abolishes this association."
Feng Y., Absher D., Eberhart D.E., Brown V., Malter H.E., Warren S.T.
Mol. Cell 1:109-118(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT FRAX ASN-304.
[36]"Intention tremor, parkinsonism, and generalized brain atrophy in male carriers of fragile X."
Hagerman R.J., Leehey M., Heinrichs W., Tassone F., Wilson R., Hills J., Grigsby J., Gage B., Hagerman P.J.
Neurology 57:127-130(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN FXTAS.
[37]"Kissing complex RNAs mediate interaction between the Fragile-X mental retardation protein KH2 domain and brain polyribosomes."
Darnell J.C., Fraser C.E., Mostovetsky O., Stefani G., Jones T.A., Eddy S.R., Darnell R.B.
Genes Dev. 19:903-918(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT FRAX ASN-304.
[38]"Tdrd3 is a novel stress granule-associated protein interacting with the Fragile-X syndrome protein FMRP."
Linder B., Ploettner O., Kroiss M., Hartmann E., Laggerbauer B., Meister G., Keidel E., Fischer U.
Hum. Mol. Genet. 17:3236-3246(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT FRAX ASN-304, SUBUNIT, INTERACTION WITH TDRD3.
[39]"Identification of novel FMR1 variants by massively parallel sequencing in developmentally delayed males."
Collins S.C., Bray S.M., Suhl J.A., Cutler D.J., Coffee B., Zwick M.E., Warren S.T.
Am. J. Med. Genet. A 152:2512-2520(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLN-138.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L29074 Genomic DNA. Translation: AAB18828.1.
L29074 Genomic DNA. Translation: AAB18829.1.
L29074 Genomic DNA. Translation: AAB18830.1.
CH471171 Genomic DNA. Translation: EAW61294.1.
CH471171 Genomic DNA. Translation: EAW61296.1.
CH471171 Genomic DNA. Translation: EAW61298.1.
CH471171 Genomic DNA. Translation: EAW61301.1.
CH471171 Genomic DNA. Translation: EAW61302.1.
CH471171 Genomic DNA. Translation: EAW61303.1.
BC086957 mRNA. Translation: AAH86957.1.
L29074 Genomic DNA. Translation: AAB18831.1.
L29074 Genomic DNA. Translation: AAB18832.1.
L29074 Genomic DNA. Translation: AAB18833.1.
M67468 mRNA. Translation: AAA52458.1. Different initiation.
X69962 mRNA. Translation: CAA49586.1.
S65791 mRNA. Translation: AAB28395.2.
L19476 Genomic DNA. Translation: AAA62452.2.
L19477 Genomic DNA. Translation: AAA62453.1.
L19478 Genomic DNA. Translation: AAA62454.1.
L19479 Genomic DNA. Translation: AAA62455.1.
L19480 Genomic DNA. Translation: AAA62456.1.
L19481 Genomic DNA. Translation: AAA62457.1.
L19482 Genomic DNA. Translation: AAA62458.1.
L19483 Genomic DNA. Translation: AAA62459.1.
L19484 Genomic DNA. Translation: AAA62460.1.
L19485 Genomic DNA. Translation: AAA62461.1.
L19486 Genomic DNA. Translation: AAA62462.1.
L19487 Genomic DNA. Translation: AAA62463.1.
L19488 Genomic DNA. Translation: AAA62464.1.
L19489 Genomic DNA. Translation: AAA62465.1.
L19490 Genomic DNA. Translation: AAA62466.1. Sequence problems.
L19491 Genomic DNA. Translation: AAA62467.1. Sequence problems.
L19492 Genomic DNA. Translation: AAA62468.1.
L19493 Genomic DNA. Translation: AAA62469.1.
S76590 Genomic DNA. Translation: AAD14228.1.
CCDSCCDS14682.1. [Q06787-1]
PIRI68614.
A40724. S45243.
RefSeqNP_001172004.1. NM_001185075.1.
NP_001172005.1. NM_001185076.1.
NP_001172010.1. NM_001185081.1.
NP_001172011.1. NM_001185082.1. [Q06787-8]
NP_002015.1. NM_002024.5. [Q06787-1]
UniGeneHs.103183.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BKDNMR-N1-134[»]
2FMRNMR-A216-280[»]
2LA5NMR-B527-541[»]
2QNDX-ray1.90A/B216-425[»]
DisProtDP00134.
ProteinModelPortalQ06787.
SMRQ06787. Positions 1-134, 216-334, 369-425.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108619. 26 interactions.
DIPDIP-29022N.
DIP-29509N.
IntActQ06787. 20 interactions.
MINTMINT-108156.
STRING9606.ENSP00000359506.

PTM databases

PhosphoSiteQ06787.

Polymorphism databases

DMDM544328.

Proteomic databases

MaxQBQ06787.
PaxDbQ06787.
PRIDEQ06787.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370470; ENSP00000359501; ENSG00000102081. [Q06787-6]
ENST00000370475; ENSP00000359506; ENSG00000102081. [Q06787-1]
ENST00000599497; ENSP00000472650; ENSG00000268103. [Q06787-6]
ENST00000602057; ENSP00000472931; ENSG00000268103. [Q06787-1]
GeneID2332.
KEGGhsa:2332.
UCSCuc004fck.4. human. [Q06787-8]
uc010nst.3. human. [Q06787-1]

Organism-specific databases

CTD2332.
GeneCardsGC0XP146993.
GeneReviewsFMR1.
HGNCHGNC:3775. FMR1.
HPACAB012444.
HPA050118.
MIM300623. phenotype.
300624. phenotype.
309550. gene.
311360. phenotype.
neXtProtNX_Q06787.
Orphanet908. Fragile X syndrome.
93256. Fragile X-associated tremor/ataxia syndrome.
619. Primary ovarian failure.
261483. Xq27.3q28 duplication syndrome.
PharmGKBPA28191.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG75351.
HOVERGENHBG005739.
InParanoidQ06787.
KOK15516.
OMAKAWQGMV.
PhylomeDBQ06787.
TreeFamTF105427.

Gene expression databases

ArrayExpressQ06787.
BgeeQ06787.
CleanExHS_FMR1.
GenevestigatorQ06787.

Family and domain databases

Gene3D3.30.1370.10. 3 hits.
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]
SUPFAMSSF54791. SSF54791. 2 hits.
PROSITEPS51641. AGENET_LIKE. 2 hits.
PS50084. KH_TYPE_1. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFMR1. human.
EvolutionaryTraceQ06787.
GeneWikiFMR1.
GenomeRNAi2332.
NextBio9465.
PROQ06787.
SOURCESearch...

Entry information

Entry nameFMR1_HUMAN
AccessionPrimary (citable) accession number: Q06787
Secondary accession number(s): A6NNH4 expand/collapse secondary AC list , D3DWT0, D3DWT1, D3DWT2, Q16578, Q5PQZ6, Q99054
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 157 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM