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P51114

- FXR1_HUMAN

UniProt

P51114 - FXR1_HUMAN

Protein

Fragile X mental retardation syndrome-related protein 1

Gene

FXR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 3 (20 May 2008)
      Previous versions | rss
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    Functioni

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

    GO - Molecular functioni

    1. G-quadruplex RNA binding Source: Ensembl
    2. mRNA 3'-UTR binding Source: Ensembl
    3. poly(A) RNA binding Source: UniProtKB
    4. RNA binding Source: ProtInc

    GO - Biological processi

    1. apoptotic process Source: ProtInc
    2. cell differentiation Source: UniProtKB-KW
    3. muscle organ development Source: UniProtKB-KW
    4. negative regulation of translation Source: Ensembl

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Differentiation, Myogenesis

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fragile X mental retardation syndrome-related protein 1
    Short name:
    hFXR1p
    Gene namesi
    Name:FXR1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:4023. FXR1.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. costamere Source: Ensembl
    2. cytoplasm Source: HPA
    3. membrane Source: UniProtKB
    4. nucleolus Source: ProtInc
    5. polysome Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28439.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 621620Fragile X mental retardation syndrome-related protein 1PRO_0000050106Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei68 – 681PhosphotyrosineBy similarity
    Modified residuei406 – 4061Phosphoserine3 Publications
    Modified residuei409 – 4091Phosphoserine3 Publications
    Modified residuei420 – 4201Phosphoserine2 Publications
    Modified residuei423 – 4231Phosphoserine2 Publications
    Modified residuei485 – 4851Phosphoserine1 Publication
    Modified residuei587 – 5871Phosphoserine2 Publications
    Modified residuei611 – 6111Phosphothreonine1 Publication

    Post-translational modificationi

    Arg-445 is dimethylated, probably to asymmetric dimethylarginine.

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP51114.
    PaxDbiP51114.
    PRIDEiP51114.

    PTM databases

    PhosphoSiteiP51114.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiP51114.
    BgeeiP51114.
    CleanExiHS_FXR1.
    GenevestigatoriP51114.

    Organism-specific databases

    HPAiHPA018246.
    HPA055475.

    Interactioni

    Subunit structurei

    Interacts with FMR1 and FXR2. Interacts with TDRD3, and with CYFIP2 but not with CYFIP1.1 Publication

    Protein-protein interaction databases

    BioGridi113760. 32 interactions.
    IntActiP51114. 14 interactions.
    MINTiMINT-1369113.
    STRINGi9606.ENSP00000350170.

    Structurei

    Secondary structure

    1
    621
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 95
    Beta strandi15 – 239
    Beta strandi28 – 347
    Beta strandi40 – 423
    Helixi44 – 463
    Beta strandi64 – 696
    Beta strandi78 – 8811
    Beta strandi91 – 955
    Beta strandi104 – 1085
    Helixi109 – 1113
    Beta strandi112 – 1143
    Beta strandi213 – 2164
    Beta strandi218 – 2247
    Helixi227 – 2348
    Helixi239 – 2457
    Beta strandi250 – 2567
    Turni257 – 2604
    Beta strandi261 – 2688
    Helixi269 – 27911

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CPQNMR-A212-289[»]
    3KUFX-ray2.70A2-132[»]
    3O8VX-ray2.50A2-132[»]
    ProteinModelPortaliP51114.
    SMRiP51114. Positions 3-121, 212-359.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP51114.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 5047Agenet-like 1Add
    BLAST
    Domaini63 – 11553Agenet-like 2Add
    BLAST
    Domaini222 – 25130KH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini285 – 31430KH 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni442 – 45716RNA-binding RGG-boxAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi50 – 534Poly-Pro
    Compositional biasi502 – 5109Poly-Arg

    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.
    InParanoidiP51114.
    KOiK15516.
    OMAiGMVPFTF.
    OrthoDBiEOG7NKKJT.
    PhylomeDBiP51114.
    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. 2 hits.
    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]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Alternative splicing appears to be tissue-specific.

    Isoform 1 (identifier: P51114-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MAELTVEVRG SNGAFYKGFI KDVHEDSLTV VFENNWQPER QVPFNEVRLP    50
    PPPDIKKEIS EGDEVEVYSR ANDQEPCGWW LAKVRMMKGE FYVIEYAACD 100
    ATYNEIVTFE RLRPVNQNKT VKKNTFFKCT VDVPEDLREA CANENAHKDF 150
    KKAVGACRIF YHPETTQLMI LSASEATVKR VNILSDMHLR SIRTKLMLMS 200
    RNEEATKHLE CTKQLAAAFH EEFVVREDLM GLAIGTHGSN IQQARKVPGV 250
    TAIELDEDTG TFRIYGESAD AVKKARGFLE FVEDFIQVPR NLVGKVIGKN 300
    GKVIQEIVDK SGVVRVRIEG DNENKLPRED GMVPFVFVGT KESIGNVQVL 350
    LEYHIAYLKE VEQLRMERLQ IDEQLRQIGS RSYSGRGRGR RGPNYTSGYG 400
    TNSELSNPSE TESERKDELS DWSLAGEDDR DSRHQRDSRR RPGGRGRSVS 450
    GGRGRGGPRG GKSSISSVLK DPDSNPYSLL DNTESDQTAD TDASESHHST 500
    NRRRRSRRRR TDEDAVLMDG MTESDTASVN ENGLVTVADY ISRAESQSRQ 550
    RNLPRETLAK NKKEMAKDVI EEHGPSEKAI NGPTSASGDD ISKLQRTPGE 600
    EKINTLKEEN TQEAAVLNGV S 621
    Length:621
    Mass (Da):69,721
    Last modified:May 20, 2008 - v3
    Checksum:i0474A9B593C7C228
    GO
    Isoform 2 (identifier: P51114-2) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:539
    Mass (Da):60,792
    Checksum:i7D9452D150FC9EE7
    GO
    Isoform 3 (identifier: P51114-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-85: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:536
    Mass (Da):59,920
    Checksum:i4E66F53C3A15BFF8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 42EL → DV in AAC50155. (PubMed:7781595)Curated
    Sequence conflicti27 – 271S → P in BAF85322. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti233 – 2331A → T in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036050
    Natural varianti429 – 4291D → N.1 Publication
    Corresponds to variant rs1051080 [ dbSNP | Ensembl ].
    VAR_016077
    Natural varianti614 – 6141A → V.
    Corresponds to variant rs11499 [ dbSNP | Ensembl ].
    VAR_014890

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8585Missing in isoform 3. 1 PublicationVSP_019709Add
    BLAST
    Alternative sequencei535 – 5395VTVAD → GKRCD in isoform 2. 2 PublicationsVSP_019710
    Alternative sequencei540 – 62182Missing in isoform 2. 2 PublicationsVSP_019711Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U25165 mRNA. Translation: AAC50155.1.
    AY341428 mRNA. Translation: AAQ20045.1.
    AK292633 mRNA. Translation: BAF85322.1.
    BC028983 mRNA. Translation: AAH28983.1.
    CCDSiCCDS3238.1. [P51114-1]
    CCDS33894.1. [P51114-3]
    CCDS46965.1. [P51114-2]
    PIRiS55330.
    RefSeqiNP_001013456.1. NM_001013438.2. [P51114-2]
    NP_001013457.1. NM_001013439.2. [P51114-3]
    NP_005078.2. NM_005087.3. [P51114-1]
    UniGeneiHs.478407.

    Genome annotation databases

    EnsembliENST00000305586; ENSP00000307633; ENSG00000114416. [P51114-3]
    ENST00000357559; ENSP00000350170; ENSG00000114416. [P51114-1]
    ENST00000445140; ENSP00000388828; ENSG00000114416. [P51114-2]
    GeneIDi8087.
    KEGGihsa:8087.
    UCSCiuc003fkp.3. human. [P51114-1]
    uc003fkr.3. human. [P51114-2]

    Polymorphism databases

    DMDMi189047132.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U25165 mRNA. Translation: AAC50155.1 .
    AY341428 mRNA. Translation: AAQ20045.1 .
    AK292633 mRNA. Translation: BAF85322.1 .
    BC028983 mRNA. Translation: AAH28983.1 .
    CCDSi CCDS3238.1. [P51114-1 ]
    CCDS33894.1. [P51114-3 ]
    CCDS46965.1. [P51114-2 ]
    PIRi S55330.
    RefSeqi NP_001013456.1. NM_001013438.2. [P51114-2 ]
    NP_001013457.1. NM_001013439.2. [P51114-3 ]
    NP_005078.2. NM_005087.3. [P51114-1 ]
    UniGenei Hs.478407.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CPQ NMR - A 212-289 [» ]
    3KUF X-ray 2.70 A 2-132 [» ]
    3O8V X-ray 2.50 A 2-132 [» ]
    ProteinModelPortali P51114.
    SMRi P51114. Positions 3-121, 212-359.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113760. 32 interactions.
    IntActi P51114. 14 interactions.
    MINTi MINT-1369113.
    STRINGi 9606.ENSP00000350170.

    PTM databases

    PhosphoSitei P51114.

    Polymorphism databases

    DMDMi 189047132.

    Proteomic databases

    MaxQBi P51114.
    PaxDbi P51114.
    PRIDEi P51114.

    Protocols and materials databases

    DNASUi 8087.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000305586 ; ENSP00000307633 ; ENSG00000114416 . [P51114-3 ]
    ENST00000357559 ; ENSP00000350170 ; ENSG00000114416 . [P51114-1 ]
    ENST00000445140 ; ENSP00000388828 ; ENSG00000114416 . [P51114-2 ]
    GeneIDi 8087.
    KEGGi hsa:8087.
    UCSCi uc003fkp.3. human. [P51114-1 ]
    uc003fkr.3. human. [P51114-2 ]

    Organism-specific databases

    CTDi 8087.
    GeneCardsi GC03P180585.
    HGNCi HGNC:4023. FXR1.
    HPAi HPA018246.
    HPA055475.
    MIMi 600819. gene.
    neXtProti NX_P51114.
    PharmGKBi PA28439.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG75351.
    HOGENOMi HOG000293377.
    HOVERGENi HBG005739.
    InParanoidi P51114.
    KOi K15516.
    OMAi GMVPFTF.
    OrthoDBi EOG7NKKJT.
    PhylomeDBi P51114.
    TreeFami TF105427.

    Miscellaneous databases

    ChiTaRSi FXR1. human.
    EvolutionaryTracei P51114.
    GeneWikii FXR1.
    GenomeRNAii 8087.
    NextBioi 30714.
    PROi P51114.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P51114.
    Bgeei P51114.
    CleanExi HS_FXR1.
    Genevestigatori P51114.

    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. 2 hits.
    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. "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.
      , 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. 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. 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. 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-233.

    Entry informationi

    Entry nameiFXR1_HUMAN
    AccessioniPrimary (citable) accession number: P51114
    Secondary accession number(s): A8K9B8, Q7Z450, Q8N6R8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: May 20, 2008
    Last modified: October 1, 2014
    This is version 146 of the entry and version 3 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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