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P51116

- FXR2_HUMAN

UniProt

P51116 - FXR2_HUMAN

Protein

Fragile X mental retardation syndrome-related protein 2

Gene

FXR2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (07 Mar 2006)
      Previous versions | rss
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    Functioni

    RNA-binding protein.

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. RNA binding Source: ProtInc

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fragile X mental retardation syndrome-related protein 2
    Gene namesi
    Name:FXR2
    Synonyms:FMR1L2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:4024. FXR2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosolic large ribosomal subunit Source: ProtInc
    3. extracellular vesicular exosome Source: UniProt
    4. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28440.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 673673Fragile X mental retardation syndrome-related protein 2PRO_0000050110Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei411 – 4111Phosphothreonine1 Publication
    Modified residuei533 – 5331Phosphoserine1 Publication
    Modified residuei566 – 5661Phosphoserine2 Publications
    Modified residuei598 – 5981Phosphothreonine3 Publications
    Modified residuei601 – 6011Phosphoserine2 Publications
    Modified residuei603 – 6031Phosphoserine4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP51116.
    PaxDbiP51116.
    PRIDEiP51116.

    PTM databases

    PhosphoSiteiP51116.

    Expressioni

    Gene expression databases

    ArrayExpressiP51116.
    BgeeiP51116.
    CleanExiHS_FXR2.
    GenevestigatoriP51116.

    Organism-specific databases

    HPAiCAB011205.
    HPA022997.

    Interactioni

    Subunit structurei

    Interacts with FMR1 and FXR1. Interacts with CYFIP2 but not with CYFIP1. Interacts with TDRD3.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-740459,EBI-740459
    ARL6IP1Q150413EBI-740459,EBI-714543
    LCMT1Q9UIC82EBI-740459,EBI-747632
    LDOC1O957513EBI-740459,EBI-740738
    MBIPQ9NS733EBI-740459,EBI-741953
    MEAF6Q9HAF13EBI-740459,EBI-399266
    NT5C2P499023EBI-740459,EBI-742084
    PAICSP222343EBI-740459,EBI-712261
    RABAC1Q9UI143EBI-740459,EBI-712367

    Protein-protein interaction databases

    BioGridi114890. 81 interactions.
    IntActiP51116. 68 interactions.
    MINTiMINT-108243.
    STRINGi9606.ENSP00000250113.

    Structurei

    Secondary structure

    1
    673
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi15 – 195
    Beta strandi25 – 339
    Beta strandi35 – 428
    Beta strandi50 – 534
    Helixi54 – 563
    Beta strandi74 – 796
    Beta strandi88 – 9811
    Beta strandi101 – 1066
    Beta strandi115 – 1173
    Helixi119 – 1213
    Beta strandi122 – 1243

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3H8ZX-ray1.92A13-136[»]
    ProteinModelPortaliP51116.
    SMRiP51116. Positions 13-131, 222-369.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP51116.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini14 – 6047Agenet-like 1Add
    BLAST
    Domaini73 – 12553Agenet-like 2Add
    BLAST
    Domaini232 – 26130KH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini295 – 32430KH 2PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi414 – 4185Poly-Ser
    Compositional biasi544 – 5529Poly-Arg
    Compositional biasi584 – 59411Poly-ArgAdd
    BLAST

    Domaini

    The tandem Tudor domains preferentially recognize trimethylated histone peptides.1 Publication

    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.
    InParanoidiP51116.
    KOiK15516.
    OMAiFRSIRTK.
    OrthoDBiEOG7NKKJT.
    PhylomeDBiP51116.
    TreeFamiTF105427.

    Family and domain databases

    Gene3Di3.30.1370.10. 2 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]

    Sequencei

    Sequence statusi: Complete.

    P51116-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGGLASGGDV EPGLPVEVRG SNGAFYKGFV KDVHEDSVTI FFENNWQSER    50
    QIPFGDVRLP PPADYNKEIT EGDEVEVYSR ANEQEPCGWW LARVRMMKGD 100
    FYVIEYAACD ATYNEIVTLE RLRPVNPNPL ATKGSFFKVT MAVPEDLREA 150
    CSNENVHKEF KKALGANCIF LNITNSELFI LSTTEAPVKR ASLLGDMHFR 200
    SLRTKLLLMS RNEEATKHLE TSKQLAAAFQ EEFTVREDLM GLAIGTHGAN 250
    IQQARKVPGV TAIELGEETC TFRIYGETPE ACRQARSYLE FSEDSVQVPR 300
    NLVGKVIGKN GKVIQEIVDK SGVVRVRVEG DNDKKNPREE GMVPFIFVGT 350
    RENISNAQAL LEYHLSYLQE VEQLRLERLQ IDEQLRQIGL GFRPPGSGRG 400
    SGGSDKAGYS TDESSSSSLH ATRTYGGSYG GRGRGRRTGG PAYGPSSDVS 450
    TASETESEKR EEPNRAGPGD RDPPTRGEES RRRPTGGRGR GPPPAPRPTS 500
    RYNSSSISSV LKDPDSNPYS LLDTSEPEPP VDSEPGEPPP ASARRRRSRR 550
    RRTDEDRTVM DGGLESDGPN MTENGLEDES RPQRRNRSRR RRNRGNRTDG 600
    SISGDRQPVT VADYISRAES QSRQRPPLER TKPSEDSLSG QKGDSVSKLP 650
    KGPSENGELS APLELGSMVN GVS 673
    Length:673
    Mass (Da):74,223
    Last modified:March 7, 2006 - v2
    Checksum:iB8A498C3F634D41F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti625 – 6262RP → SA in AAC50292. (PubMed:7489725)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti252 – 2521Q → H.1 Publication
    Corresponds to variant rs17854734 [ dbSNP | Ensembl ].
    VAR_067039
    Natural varianti591 – 5911R → P.
    Corresponds to variant rs36013555 [ dbSNP | Ensembl ].
    VAR_055979

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS45604.1.
    PIRiS60173.
    RefSeqiNP_004851.2. NM_004860.3.
    UniGeneiHs.52788.

    Genome annotation databases

    EnsembliENST00000250113; ENSP00000250113; ENSG00000129245.
    GeneIDi9513.
    KEGGihsa:9513.
    UCSCiuc002gia.2. human.

    Polymorphism databases

    DMDMi90177782.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS45604.1.
    PIRi S60173.
    RefSeqi NP_004851.2. NM_004860.3.
    UniGenei Hs.52788.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3H8Z X-ray 1.92 A 13-136 [» ]
    ProteinModelPortali P51116.
    SMRi P51116. Positions 13-131, 222-369.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114890. 81 interactions.
    IntActi P51116. 68 interactions.
    MINTi MINT-108243.
    STRINGi 9606.ENSP00000250113.

    PTM databases

    PhosphoSitei P51116.

    Polymorphism databases

    DMDMi 90177782.

    Proteomic databases

    MaxQBi P51116.
    PaxDbi P51116.
    PRIDEi P51116.

    Protocols and materials databases

    DNASUi 9513.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000250113 ; ENSP00000250113 ; ENSG00000129245 .
    GeneIDi 9513.
    KEGGi hsa:9513.
    UCSCi uc002gia.2. human.

    Organism-specific databases

    CTDi 9513.
    GeneCardsi GC17M007494.
    HGNCi HGNC:4024. FXR2.
    HPAi CAB011205.
    HPA022997.
    MIMi 605339. gene.
    neXtProti NX_P51116.
    PharmGKBi PA28440.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG75351.
    HOGENOMi HOG000293377.
    HOVERGENi HBG005739.
    InParanoidi P51116.
    KOi K15516.
    OMAi FRSIRTK.
    OrthoDBi EOG7NKKJT.
    PhylomeDBi P51116.
    TreeFami TF105427.

    Miscellaneous databases

    EvolutionaryTracei P51116.
    GeneWikii FXR2.
    GenomeRNAii 9513.
    NextBioi 35646.
    PROi P51116.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P51116.
    Bgeei P51116.
    CleanExi HS_FXR2.
    Genevestigatori P51116.

    Family and domain databases

    Gene3Di 3.30.1370.10. 2 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. "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.
      , 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. 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. 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. 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.

    Entry informationi

    Entry nameiFXR2_HUMAN
    AccessioniPrimary (citable) accession number: P51116
    Secondary accession number(s): B2R9M2
    , D3DTQ1, Q86V09, Q8WUM2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: March 7, 2006
    Last modified: October 1, 2014
    This is version 132 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3