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Q92837

- FRAT1_HUMAN

UniProt

Q92837 - FRAT1_HUMAN

Protein

Proto-oncogene FRAT1

Gene

FRAT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 3 (16 Aug 2004)
      Previous versions | rss
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    Functioni

    Positively regulates the Wnt signaling pathway by stabilizing beta-catenin through the association with GSK-3. May play a role in tumor progression and collaborate with PIM1 and MYC in lymphomagenesis.1 Publication

    GO - Biological processi

    1. embryonic axis specification Source: Ensembl
    2. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Biological processi

    Wnt signaling pathway

    Enzyme and pathway databases

    ReactomeiREACT_11065. Beta-catenin phosphorylation cascade.
    REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    SignaLinkiQ92837.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proto-oncogene FRAT1
    Alternative name(s):
    Frequently rearranged in advanced T-cell lymphomas 1
    Short name:
    FRAT-1
    Gene namesi
    Name:FRAT1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:3944. FRAT1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    PharmGKBiPA28361.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 279279Proto-oncogene FRAT1PRO_0000087332Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei88 – 881Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ92837.
    PRIDEiQ92837.

    PTM databases

    PhosphoSiteiQ92837.

    Expressioni

    Gene expression databases

    BgeeiQ92837.
    CleanExiHS_FRAT1.
    GenevestigatoriQ92837.

    Organism-specific databases

    HPAiCAB037271.
    CAB046472.

    Interactioni

    Subunit structurei

    Binds DVL1. Binds GSK-3 and prevent GSK-3-dependent phosphorylation.1 Publication

    Protein-protein interaction databases

    BioGridi115340. 14 interactions.
    IntActiQ92837. 13 interactions.
    MINTiMINT-100904.
    STRINGi9606.ENSP00000360060.

    Structurei

    Secondary structure

    1
    279
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi201 – 2099
    Helixi212 – 2198

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GNGX-ray2.60X/Y188-226[»]
    3ZRKX-ray2.37X/Y197-226[»]
    3ZRLX-ray2.48X/Y197-226[»]
    3ZRMX-ray2.49X/Y197-226[»]
    4AFJX-ray1.98X/Y197-226[»]
    ProteinModelPortaliQ92837.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ92837.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni198 – 22023Involved in GSK-3 bindingAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi6 – 2217Glu-rich (highly acidic)Add
    BLAST
    Compositional biasi6 – 105Poly-Glu
    Compositional biasi13 – 2210Poly-Glu

    Sequence similaritiesi

    Belongs to the GSK-3-binding protein family.Curated

    Phylogenomic databases

    eggNOGiNOG43447.
    HOGENOMiHOG000112642.
    HOVERGENiHBG051660.
    InParanoidiQ92837.
    KOiK03069.
    OMAiGKQGIPQ.
    OrthoDBiEOG72ZCH6.
    PhylomeDBiQ92837.
    TreeFamiTF330804.

    Family and domain databases

    InterProiIPR008014. GSK3-bd.
    [Graphical view]
    PfamiPF05350. GSK-3_bind. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q92837-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPCRREEEEE AGEEAEGEEE EEDSFLLLQQ SVALGSSGEV DRLVAQIGET    50
    LQLDAAQHSP ASPCGPPGAP LRAPGPLAAA VPADKARSPA VPLLLPPALA 100
    ETVGPAPPGV LRCALGDRGR VRGRAAPYCV AELATGPSAL SPLPPQADLD 150
    GPPGAGKQGI PQPLSGPCRR GWLRGAAASR RLQQRRGSQP ETRTGDDDPH 200
    RLLQQLVLSG NLIKEAVRRL HSRRLQLRAK LPQRPLLGPL SAPVHEPPSP 250
    RSPRAACSDP GASGRAQLRT GDGVLVPGS 279
    Length:279
    Mass (Da):29,093
    Last modified:August 16, 2004 - v3
    Checksum:i629AFD6CEA1DC0BD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti58 – 581H → D in AAB97096. (PubMed:9034327)Curated
    Sequence conflicti179 – 1791S → P in AAH34476. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U58975 mRNA. Translation: AAB97096.2.
    AB074890 mRNA. Translation: BAB86352.1.
    AL355490 Genomic DNA. Translation: CAI40773.1.
    BC034476 mRNA. Translation: AAH34476.1.
    CCDSiCCDS7455.1.
    RefSeqiNP_005470.2. NM_005479.3.
    UniGeneiHs.126057.

    Genome annotation databases

    EnsembliENST00000371021; ENSP00000360060; ENSG00000165879.
    GeneIDi10023.
    KEGGihsa:10023.
    UCSCiuc001knc.1. human.

    Polymorphism databases

    DMDMi51338813.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U58975 mRNA. Translation: AAB97096.2 .
    AB074890 mRNA. Translation: BAB86352.1 .
    AL355490 Genomic DNA. Translation: CAI40773.1 .
    BC034476 mRNA. Translation: AAH34476.1 .
    CCDSi CCDS7455.1.
    RefSeqi NP_005470.2. NM_005479.3.
    UniGenei Hs.126057.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GNG X-ray 2.60 X/Y 188-226 [» ]
    3ZRK X-ray 2.37 X/Y 197-226 [» ]
    3ZRL X-ray 2.48 X/Y 197-226 [» ]
    3ZRM X-ray 2.49 X/Y 197-226 [» ]
    4AFJ X-ray 1.98 X/Y 197-226 [» ]
    ProteinModelPortali Q92837.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115340. 14 interactions.
    IntActi Q92837. 13 interactions.
    MINTi MINT-100904.
    STRINGi 9606.ENSP00000360060.

    PTM databases

    PhosphoSitei Q92837.

    Polymorphism databases

    DMDMi 51338813.

    Proteomic databases

    PaxDbi Q92837.
    PRIDEi Q92837.

    Protocols and materials databases

    DNASUi 10023.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371021 ; ENSP00000360060 ; ENSG00000165879 .
    GeneIDi 10023.
    KEGGi hsa:10023.
    UCSCi uc001knc.1. human.

    Organism-specific databases

    CTDi 10023.
    GeneCardsi GC10P099069.
    HGNCi HGNC:3944. FRAT1.
    HPAi CAB037271.
    CAB046472.
    MIMi 602503. gene.
    neXtProti NX_Q92837.
    PharmGKBi PA28361.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG43447.
    HOGENOMi HOG000112642.
    HOVERGENi HBG051660.
    InParanoidi Q92837.
    KOi K03069.
    OMAi GKQGIPQ.
    OrthoDBi EOG72ZCH6.
    PhylomeDBi Q92837.
    TreeFami TF330804.

    Enzyme and pathway databases

    Reactomei REACT_11065. Beta-catenin phosphorylation cascade.
    REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    SignaLinki Q92837.

    Miscellaneous databases

    EvolutionaryTracei Q92837.
    GeneWikii FRAT1.
    GenomeRNAii 10023.
    NextBioi 37873.
    PROi Q92837.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q92837.
    CleanExi HS_FRAT1.
    Genevestigatori Q92837.

    Family and domain databases

    InterProi IPR008014. GSK3-bd.
    [Graphical view ]
    Pfami PF05350. GSK-3_bind. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Activation of a novel proto-oncogene, Frat1, contributes to progression of mouse T-cell lymphomas."
      Jonkers J., Korswagen H.C., Acton D., Breuer M., Berns A.
      EMBO J. 16:441-450(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Jonkers J., Korswagen H.C., Acton D., Breuer M., Berns A.
      Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 170.
    3. "Molecular cloning and expression of proto-oncogene FRAT1 in human cancer."
      Saitoh T., Mine T., Katoh M.
      Int. J. Oncol. 20:785-789(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lung.
    4. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Tissue: Testis.
    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].
      Tissue: Testis.
    6. "Casein kinase I epsilon enhances the binding of Dvl-1 to Frat-1 and is essential for Wnt-3a-induced accumulation of beta-catenin."
      Hino S., Michiue T., Asashima M., Kikuchi A.
      J. Biol. Chem. 278:14066-14073(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DVL1, ROLE IN WNT SIGNALING.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "The structure of phosphorylated GSK-3beta complexed with a peptide, FRATtide, that inhibits beta-catenin phosphorylation."
      Bax B., Carter P.S., Lewis C., Guy A.R., Bridges A., Tanner R., Pettman G., Mannix C., Culbert A.A., Brown M.J.B., Smith D.G., Reith A.D.
      Structure 9:1143-1152(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 198-223 IN COMPLEX WITH GSK-3.

    Entry informationi

    Entry nameiFRAT1_HUMAN
    AccessioniPrimary (citable) accession number: Q92837
    Secondary accession number(s): Q5JTI1, Q8NE74, Q8TDW9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: August 16, 2004
    Last modified: October 1, 2014
    This is version 116 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, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3