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P51114 (FXR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fragile X mental retardation syndrome-related protein 1

Short name=hFXR1p
Gene names
Name:FXR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length621 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

RNA-binding protein required for embryonic and postnatal development of muscle tissue. May regulate intracellular transport and local translation of certain mRNAs By similarity.

Subunit structure

Interacts with FMR1 and FXR2. Interacts with TDRD3, and with CYFIP2 but not with CYFIP1. Ref.7

Subcellular location

Cytoplasm Ref.1.

Tissue specificity

Expressed in all tissues examined including heart, brain, kidney and testis. Ref.1

Domain

The tandem Tudor domains preferentially recognize trimethylated histone peptides. Ref.16

Post-translational modification

Arg-445 is dimethylated, probably to asymmetric dimethylarginine.

Sequence similarities

Belongs to the FMR1 family.

Contains 2 Agenet-like domains.

Contains 2 KH domains.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Alternative splicing appears to be tissue-specific.
Isoform 1 (identifier: P51114-1)

Also known as: Long;

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 2 (identifier: P51114-2)

Also known as: b; Short;

The sequence of this isoform differs from the canonical sequence as follows:
     535-539: VTVAD → GKRCD
     540-621: Missing.
Note: Contains a phosphoserine at position 524. Contains a phosphoserine at position 528.
Isoform 3 (identifier: P51114-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-85: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 621620Fragile X mental retardation syndrome-related protein 1
PRO_0000050106

Regions

Domain4 – 5047Agenet-like 1
Domain63 – 11553Agenet-like 2
Domain222 – 25130KH 1
Domain285 – 31430KH 2
Region442 – 45716RNA-binding RGG-box
Compositional bias50 – 534Poly-Pro
Compositional bias502 – 5109Poly-Arg

Amino acid modifications

Modified residue21N-acetylalanine Ref.5 Ref.14
Modified residue681Phosphotyrosine By similarity
Modified residue4061Phosphoserine Ref.8 Ref.10 Ref.13
Modified residue4091Phosphoserine Ref.8 Ref.10 Ref.13
Modified residue4201Phosphoserine Ref.11 Ref.13
Modified residue4231Phosphoserine Ref.11 Ref.13
Modified residue4851Phosphoserine Ref.13
Modified residue5871Phosphoserine Ref.10 Ref.13
Modified residue6111Phosphothreonine Ref.13

Natural variations

Alternative sequence1 – 8585Missing in isoform 3.
VSP_019709
Alternative sequence535 – 5395VTVAD → GKRCD in isoform 2.
VSP_019710
Alternative sequence540 – 62182Missing in isoform 2.
VSP_019711
Natural variant2331A → T in a breast cancer sample; somatic mutation. Ref.17
VAR_036050
Natural variant4291D → N. Ref.1
Corresponds to variant rs1051080 [ dbSNP | Ensembl ].
VAR_016077
Natural variant6141A → V.
Corresponds to variant rs11499 [ dbSNP | Ensembl ].
VAR_014890

Experimental info

Sequence conflict3 – 42EL → DV in AAC50155. Ref.1
Sequence conflict271S → P in BAF85322. Ref.3

Secondary structure

.................................. 621
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Long) [UniParc].

Last modified May 20, 2008. Version 3.
Checksum: 0474A9B593C7C228

FASTA62169,721
        10         20         30         40         50         60 
MAELTVEVRG SNGAFYKGFI KDVHEDSLTV VFENNWQPER QVPFNEVRLP PPPDIKKEIS 

        70         80         90        100        110        120 
EGDEVEVYSR ANDQEPCGWW LAKVRMMKGE FYVIEYAACD ATYNEIVTFE RLRPVNQNKT 

       130        140        150        160        170        180 
VKKNTFFKCT VDVPEDLREA CANENAHKDF KKAVGACRIF YHPETTQLMI LSASEATVKR 

       190        200        210        220        230        240 
VNILSDMHLR SIRTKLMLMS RNEEATKHLE CTKQLAAAFH EEFVVREDLM GLAIGTHGSN 

       250        260        270        280        290        300 
IQQARKVPGV TAIELDEDTG TFRIYGESAD AVKKARGFLE FVEDFIQVPR NLVGKVIGKN 

       310        320        330        340        350        360 
GKVIQEIVDK SGVVRVRIEG DNENKLPRED GMVPFVFVGT KESIGNVQVL LEYHIAYLKE 

       370        380        390        400        410        420 
VEQLRMERLQ IDEQLRQIGS RSYSGRGRGR RGPNYTSGYG TNSELSNPSE TESERKDELS 

       430        440        450        460        470        480 
DWSLAGEDDR DSRHQRDSRR RPGGRGRSVS GGRGRGGPRG GKSSISSVLK DPDSNPYSLL 

       490        500        510        520        530        540 
DNTESDQTAD TDASESHHST NRRRRSRRRR TDEDAVLMDG MTESDTASVN ENGLVTVADY 

       550        560        570        580        590        600 
ISRAESQSRQ RNLPRETLAK NKKEMAKDVI EEHGPSEKAI NGPTSASGDD ISKLQRTPGE 

       610        620 
EKINTLKEEN TQEAAVLNGV S 

« Hide

Isoform 2 (b) (Short) [UniParc].

Checksum: 7D9452D150FC9EE7
Show »

FASTA53960,792
Isoform 3 [UniParc].

Checksum: 4E66F53C3A15BFF8
Show »

FASTA53659,920

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, VARIANT ASN-429, TISSUE SPECIFICITY.
Tissue: Cervix carcinoma.
[2]"Identification of alternatively spliced genes related to spermatogenesis using cDNA microarrays."
Xu Z.Y., Huang X.Y., Wang H., Xu M., Li J.M., Zhou Z.M., Sha J.H.
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Testis.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Thymus.
[4]"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 2).
Tissue: Cervix.
[5]Bienvenut W.V., Calvo F., Kolch W.
Submitted (MAR-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-9; 58-70; 246-263 AND 369-376, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[6]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"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: INTERACTION WITH TDRD3.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406 AND SER-409, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406; SER-409 AND SER-587, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524 AND SER-528 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"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-420 AND SER-423, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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].
[13]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406; SER-409; SER-420; SER-423; SER-485; SER-587 AND THR-611, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Solution structure of the N-terminal KH domain of human FXR1."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 212-289.
[16]"Structural studies of the tandem Tudor domains of fragile X mental retardation related proteins FXR1 and FXR2."
Adams-Cioaba M.A., Guo Y., Bian C., Amaya M.F., Lam R., Wasney G.A., Vedadi M., Xu C., Min J.
PLoS ONE 5:E13559-E13559(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-132, DOMAINS TUDOR.
[17]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-233.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U25165 mRNA. Translation: AAC50155.1.
AY341428 mRNA. Translation: AAQ20045.1.
AK292633 mRNA. Translation: BAF85322.1.
BC028983 mRNA. Translation: AAH28983.1.
CCDSCCDS3238.1. [P51114-1]
CCDS33894.1. [P51114-3]
CCDS46965.1. [P51114-2]
PIRS55330.
RefSeqNP_001013456.1. NM_001013438.2. [P51114-2]
NP_001013457.1. NM_001013439.2. [P51114-3]
NP_005078.2. NM_005087.3. [P51114-1]
UniGeneHs.478407.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CPQNMR-A212-289[»]
3KUFX-ray2.70A2-132[»]
3O8VX-ray2.50A2-132[»]
ProteinModelPortalP51114.
SMRP51114. Positions 3-121, 212-359.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113760. 26 interactions.
IntActP51114. 14 interactions.
MINTMINT-1369113.
STRING9606.ENSP00000350170.

PTM databases

PhosphoSiteP51114.

Polymorphism databases

DMDM189047132.

Proteomic databases

MaxQBP51114.
PaxDbP51114.
PRIDEP51114.

Protocols and materials databases

DNASU8087.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000305586; ENSP00000307633; ENSG00000114416. [P51114-3]
ENST00000357559; ENSP00000350170; ENSG00000114416. [P51114-1]
ENST00000445140; ENSP00000388828; ENSG00000114416. [P51114-2]
GeneID8087.
KEGGhsa:8087.
UCSCuc003fkp.3. human. [P51114-1]
uc003fkr.3. human. [P51114-2]

Organism-specific databases

CTD8087.
GeneCardsGC03P180585.
HGNCHGNC:4023. FXR1.
HPAHPA018246.
HPA055475.
MIM600819. gene.
neXtProtNX_P51114.
PharmGKBPA28439.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG75351.
HOGENOMHOG000293377.
HOVERGENHBG005739.
InParanoidP51114.
KOK15516.
OMAGMVPFTF.
OrthoDBEOG7NKKJT.
PhylomeDBP51114.
TreeFamTF105427.

Gene expression databases

ArrayExpressP51114.
BgeeP51114.
CleanExHS_FXR1.
GenevestigatorP51114.

Family and domain databases

Gene3D3.30.1370.10. 2 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. 2 hits.
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

ChiTaRSFXR1. human.
EvolutionaryTraceP51114.
GeneWikiFXR1.
GenomeRNAi8087.
NextBio30714.
PROP51114.
SOURCESearch...

Entry information

Entry nameFXR1_HUMAN
AccessionPrimary (citable) accession number: P51114
Secondary accession number(s): A8K9B8, Q7Z450, Q8N6R8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 20, 2008
Last modified: July 9, 2014
This is version 144 of the entry and version 3 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 3

Human chromosome 3: entries, gene names and cross-references to MIM