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P51116 (FXR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fragile X mental retardation syndrome-related protein 2
Gene names
Name:FXR2
Synonyms:FMR1L2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length673 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

RNA-binding protein.

Subunit structure

Interacts with FMR1 and FXR1. Interacts with CYFIP2 but not with CYFIP1. Interacts with TDRD3. Ref.9

Subcellular location

Cytoplasm.

Domain

The tandem Tudor domains preferentially recognize trimethylated histone peptides. Ref.18

Sequence similarities

Belongs to the FMR1 family.

Contains 2 Agenet-like domains.

Contains 2 KH domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 673673Fragile X mental retardation syndrome-related protein 2
PRO_0000050110

Regions

Domain14 – 6047Agenet-like 1
Domain73 – 12553Agenet-like 2
Domain232 – 26130KH 1
Domain295 – 32430KH 2
Compositional bias414 – 4185Poly-Ser
Compositional bias544 – 5529Poly-Arg
Compositional bias584 – 59411Poly-Arg

Amino acid modifications

Modified residue4111Phosphothreonine Ref.12
Modified residue5331Phosphoserine Ref.12
Modified residue5661Phosphoserine Ref.12 Ref.15
Modified residue5981Phosphothreonine Ref.10 Ref.12 Ref.14
Modified residue6011Phosphoserine Ref.12 Ref.14
Modified residue6031Phosphoserine Ref.12 Ref.14 Ref.15 Ref.17

Natural variations

Natural variant2521Q → H. Ref.5
Corresponds to variant rs17854734 [ dbSNP | Ensembl ].
VAR_067039
Natural variant5911R → P.
Corresponds to variant rs36013555 [ dbSNP | Ensembl ].
VAR_055979

Experimental info

Sequence conflict625 – 6262RP → SA in AAC50292. Ref.1

Secondary structure

..................... 673
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P51116 [UniParc].

Last modified March 7, 2006. Version 2.
Checksum: B8A498C3F634D41F

FASTA67374,223
        10         20         30         40         50         60 
MGGLASGGDV EPGLPVEVRG SNGAFYKGFV KDVHEDSVTI FFENNWQSER QIPFGDVRLP 

        70         80         90        100        110        120 
PPADYNKEIT EGDEVEVYSR ANEQEPCGWW LARVRMMKGD FYVIEYAACD ATYNEIVTLE 

       130        140        150        160        170        180 
RLRPVNPNPL ATKGSFFKVT MAVPEDLREA CSNENVHKEF KKALGANCIF LNITNSELFI 

       190        200        210        220        230        240 
LSTTEAPVKR ASLLGDMHFR SLRTKLLLMS RNEEATKHLE TSKQLAAAFQ EEFTVREDLM 

       250        260        270        280        290        300 
GLAIGTHGAN IQQARKVPGV TAIELGEETC TFRIYGETPE ACRQARSYLE FSEDSVQVPR 

       310        320        330        340        350        360 
NLVGKVIGKN GKVIQEIVDK SGVVRVRVEG DNDKKNPREE GMVPFIFVGT RENISNAQAL 

       370        380        390        400        410        420 
LEYHLSYLQE VEQLRLERLQ IDEQLRQIGL GFRPPGSGRG SGGSDKAGYS TDESSSSSLH 

       430        440        450        460        470        480 
ATRTYGGSYG GRGRGRRTGG PAYGPSSDVS TASETESEKR EEPNRAGPGD RDPPTRGEES 

       490        500        510        520        530        540 
RRRPTGGRGR GPPPAPRPTS RYNSSSISSV LKDPDSNPYS LLDTSEPEPP VDSEPGEPPP 

       550        560        570        580        590        600 
ASARRRRSRR RRTDEDRTVM DGGLESDGPN MTENGLEDES RPQRRNRSRR RRNRGNRTDG 

       610        620        630        640        650        660 
SISGDRQPVT VADYISRAES QSRQRPPLER TKPSEDSLSG QKGDSVSKLP KGPSENGELS 

       670 
APLELGSMVN GVS 

« Hide

References

« Hide 'large scale' references
[1]"The fragile X mental retardation syndrome protein interacts with novel homologs FXR1 and FXR2."
Zhang Y., O'Connor J.P., Siomi M.C., Srinivasan S., Dutra A., Nussbaum R.L., Dreyfuss G.
EMBO J. 14:5358-5366(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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].
Tissue: Kidney.
[4]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].
[5]"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], VARIANT HIS-252.
Tissue: Lymph, PNS and Skin.
[6]"The rat androgen-binding protein (ABP/SHBG) gene contains triplet repeats similar to unstable triplets: evidence that the ABP/SHBG and the fragile X-related 2 genes overlap."
Joseph D.R.
Steroids 63:2-4(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
[7]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[8]"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.
[9]"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.
[10]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-598, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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 THR-411; SER-533; SER-566; THR-598; SER-601 AND SER-603, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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].
[14]"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 THR-598; SER-601 AND SER-603, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"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-566 AND SER-603, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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].
[17]"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-603, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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 (1.92 ANGSTROMS) OF 13-136, DOMAINS TUDOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U31501 mRNA. Translation: AAC50292.1.
BT009817 mRNA. Translation: AAP88819.1.
AK313836 mRNA. Translation: BAG36569.1.
CH471108 Genomic DNA. Translation: EAW90154.1.
CH471108 Genomic DNA. Translation: EAW90155.1.
BC020090 mRNA. Translation: AAH20090.1.
BC051907 mRNA. Translation: AAH51907.1.
BC067272 mRNA. Translation: AAH67272.1.
AF044263 Genomic DNA. Translation: AAC03357.1.
CCDSCCDS45604.1.
PIRS60173.
RefSeqNP_004851.2. NM_004860.3.
UniGeneHs.52788.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3H8ZX-ray1.92A13-136[»]
ProteinModelPortalP51116.
SMRP51116. Positions 13-131, 222-369.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114890. 75 interactions.
IntActP51116. 68 interactions.
MINTMINT-108243.
STRING9606.ENSP00000250113.

PTM databases

PhosphoSiteP51116.

Polymorphism databases

DMDM90177782.

Proteomic databases

MaxQBP51116.
PaxDbP51116.
PRIDEP51116.

Protocols and materials databases

DNASU9513.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000250113; ENSP00000250113; ENSG00000129245.
GeneID9513.
KEGGhsa:9513.
UCSCuc002gia.2. human.

Organism-specific databases

CTD9513.
GeneCardsGC17M007494.
HGNCHGNC:4024. FXR2.
HPACAB011205.
HPA022997.
MIM605339. gene.
neXtProtNX_P51116.
PharmGKBPA28440.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG75351.
HOGENOMHOG000293377.
HOVERGENHBG005739.
InParanoidP51116.
KOK15516.
OMAFRSIRTK.
OrthoDBEOG7NKKJT.
PhylomeDBP51116.
TreeFamTF105427.

Gene expression databases

ArrayExpressP51116.
BgeeP51116.
CleanExHS_FXR2.
GenevestigatorP51116.

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. 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

EvolutionaryTraceP51116.
GeneWikiFXR2.
GenomeRNAi9513.
NextBio35646.
PROP51116.
SOURCESearch...

Entry information

Entry nameFXR2_HUMAN
AccessionPrimary (citable) accession number: P51116
Secondary accession number(s): B2R9M2 expand/collapse secondary AC list , D3DTQ1, Q86V09, Q8WUM2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: March 7, 2006
Last modified: July 9, 2014
This is version 130 of the entry and version 2 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 17

Human chromosome 17: entries, gene names and cross-references to MIM