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Q9UKB1

- FBW1B_HUMAN

UniProt

Q9UKB1 - FBW1B_HUMAN

Protein

F-box/WD repeat-containing protein 11

Gene

FBXW11

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably recognizes and binds to phosphorylated target proteins. SCF(FBXW11) mediates the ubiquitination of phosphorylated CTNNB1 and participates in Wnt signaling. SCF(FBXW11) mediates the ubiquitination of phosphorylated NFKBIA, which degradation frees the associated NFKB1 to translocate into the nucleus and to activate transcription. SCF(FBXW11) mediates the ubiquitination of IFNAR1. Involved in the oxidative stress-induced a ubiquitin-mediated decrease in RCAN1. Mediates the degradation of CDC25A induced by ionizing radiation in cells progressing through S phase and thus may function in the intra-S-phase checkpoint. Has an essential role in the control of the clock-dependent transcription via degradation of phosphorylated PER1 and phosphorylated PER2. Is target of human immunodeficiency virus type 1 (HIV-1) protein VPU to polyubiquitinate and deplete BST2 from cells and antagonize its antiviral action.11 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. ubiquitin-protein transferase activity Source: UniProtKB

    GO - Biological processi

    1. G2/M transition of mitotic cell cycle Source: Reactome
    2. mitotic cell cycle Source: Reactome
    3. negative regulation of NF-kappaB import into nucleus Source: Ensembl
    4. negative regulation of transcription, DNA-templated Source: UniProtKB
    5. positive regulation of circadian rhythm Source: UniProtKB
    6. positive regulation of proteolysis Source: UniProtKB
    7. positive regulation of transcription, DNA-templated Source: UniProtKB
    8. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
    9. protein dephosphorylation Source: UniProtKB
    10. protein destabilization Source: UniProtKB
    11. protein polyubiquitination Source: UniProtKB
    12. protein ubiquitination Source: UniProtKB
    13. rhythmic process Source: UniProtKB-KW
    14. SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
    15. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Biological processi

    Biological rhythms, Cell cycle, Ubl conjugation pathway, Wnt signaling pathway

    Enzyme and pathway databases

    ReactomeiREACT_118656. Activation of NF-kappaB in B cells.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinkiQ9UKB1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    F-box/WD repeat-containing protein 11
    Alternative name(s):
    F-box and WD repeats protein beta-TrCP2
    F-box/WD repeat-containing protein 1B
    Homologous to Slimb protein
    Short name:
    HOS
    Gene namesi
    Name:FBXW11
    Synonyms:BTRCP2, FBW1B, FBXW1B, KIAA0696
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:13607. FBXW11.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. nucleus Source: UniProtKB
    4. SCF ubiquitin ligase complex Source: UniProtKB
    5. ubiquitin ligase complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28050.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 542542F-box/WD repeat-containing protein 11PRO_0000050981Add
    BLAST

    Proteomic databases

    MaxQBiQ9UKB1.
    PaxDbiQ9UKB1.
    PRIDEiQ9UKB1.

    PTM databases

    PhosphoSiteiQ9UKB1.

    Expressioni

    Inductioni

    Expression is negatively regulated by Wnt/beta-catenin pathway.1 Publication

    Gene expression databases

    ArrayExpressiQ9UKB1.
    BgeeiQ9UKB1.
    CleanExiHS_FBXW11.
    GenevestigatoriQ9UKB1.

    Interactioni

    Subunit structurei

    Self-associates. Component of the SCF(FBXW11) complex formed of CUL1, SKP1, RBX1 and a FBXW11 dimer. Interacts with BTRC, BST2, PER1, RCAN1 and USP47. Interacts with phosphorylated ubiquitination substrates CTNNB1, NFKBIA, IFNAR1, PER1 and PER2; the interaction requires the phosphorylation of the two serine residues in the substrates' destruction motif D-S-G-X(2,3,4)-S. Interacts with TRIM21. Interacts with PER3.12 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AXIN1O151694EBI-355189,EBI-710484
    CTNNB1P352222EBI-355189,EBI-491549
    CUL1Q136162EBI-355189,EBI-359390
    IFNAR1P171818EBI-355189,EBI-1547250
    MDM2Q009874EBI-355189,EBI-389668
    NFKBIBQ156532EBI-355189,EBI-352889
    SKP1P632084EBI-355189,EBI-307486
    WEE1P302913EBI-355189,EBI-914695

    Protein-protein interaction databases

    BioGridi116887. 67 interactions.
    DIPiDIP-27593N.
    IntActiQ9UKB1. 38 interactions.
    MINTiMINT-120522.
    STRINGi9606.ENSP00000265094.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UKB1.
    SMRiQ9UKB1. Positions 67-518.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini129 – 16739F-boxPROSITE-ProRule annotationAdd
    BLAST
    Repeati238 – 27538WD 1Add
    BLAST
    Repeati278 – 31538WD 2Add
    BLAST
    Repeati318 – 35538WD 3Add
    BLAST
    Repeati361 – 39838WD 4Add
    BLAST
    Repeati401 – 44040WD 5Add
    BLAST
    Repeati442 – 47837WD 6Add
    BLAST
    Repeati490 – 52738WD 7Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni67 – 11650Homodimerization domain DBy similarityAdd
    BLAST

    Domaini

    The N-terminal D domain mediates homodimerization.By similarity

    Sequence similaritiesi

    Contains 1 F-box domain.PROSITE-ProRule annotation
    Contains 7 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG2319.
    HOGENOMiHOG000006638.
    HOVERGENiHBG002521.
    InParanoidiQ9UKB1.
    KOiK03362.
    OMAiFDQWSEA.
    OrthoDBiEOG76DTS5.
    PhylomeDBiQ9UKB1.
    TreeFamiTF105679.

    Family and domain databases

    Gene3Di2.130.10.10. 2 hits.
    InterProiIPR021977. Beta-TrCP_D.
    IPR001810. F-box_dom.
    IPR020472. G-protein_beta_WD-40_rep.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    PfamiPF12125. Beta-TrCP_D. 1 hit.
    PF12937. F-box-like. 1 hit.
    PF00400. WD40. 7 hits.
    [Graphical view]
    PRINTSiPR00320. GPROTEINBRPT.
    SMARTiSM01028. Beta-TrCP_D. 1 hit.
    SM00256. FBOX. 1 hit.
    SM00320. WD40. 7 hits.
    [Graphical view]
    SUPFAMiSSF50978. SSF50978. 1 hit.
    SSF81383. SSF81383. 1 hit.
    PROSITEiPS50181. FBOX. 1 hit.
    PS00678. WD_REPEATS_1. 5 hits.
    PS50082. WD_REPEATS_2. 7 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform C (identifier: Q9UKB1-1) [UniParc]FASTAAdd to Basket

    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

    MEPDSVIEDK TIELMCSVPR SLWLGCANLV ESMCALSCLQ SMPSVRCLQI    50
    SNGTSSVIVS RKRPSEGNYQ KEKDLCIKYF DQWSESDQVE FVEHLISRMC 100
    HYQHGHINSY LKPMLQRDFI TALPEQGLDH IAENILSYLD ARSLCAAELV 150
    CKEWQRVISE GMLWKKLIER MVRTDPLWKG LSERRGWDQY LFKNRPTDGP 200
    PNSFYRSLYP KIIQDIETIE SNWRCGRHNL QRIQCRSENS KGVYCLQYDD 250
    EKIISGLRDN SIKIWDKTSL ECLKVLTGHT GSVLCLQYDE RVIVTGSSDS 300
    TVRVWDVNTG EVLNTLIHHN EAVLHLRFSN GLMVTCSKDR SIAVWDMASA 350
    TDITLRRVLV GHRAAVNVVD FDDKYIVSAS GDRTIKVWST STCEFVRTLN 400
    GHKRGIACLQ YRDRLVVSGS SDNTIRLWDI ECGACLRVLE GHEELVRCIR 450
    FDNKRIVSGA YDGKIKVWDL QAALDPRAPA STLCLRTLVE HSGRVFRLQF 500
    DEFQIISSSH DDTILIWDFL NVPPSAQNET RSPSRTYTYI SR 542
    Length:542
    Mass (Da):62,091
    Last modified:May 1, 2000 - v1
    Checksum:i7CD40087EFAA5C8A
    GO
    Isoform A (identifier: Q9UKB1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         16-49: Missing.

    Show »
    Length:508
    Mass (Da):58,422
    Checksum:i05C691DB32A91B50
    GO
    Isoform B (identifier: Q9UKB1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         16-48: CSVPRSLWLGCANLVESMCALSCLQSMPSVRCL → NTSVMEDQNEDESPKKNTLW

    Show »
    Length:529
    Mass (Da):60,898
    Checksum:i53D181B789313D0E
    GO

    Sequence cautioni

    The sequence BAA31671.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei16 – 4934Missing in isoform A. 1 PublicationVSP_006765Add
    BLAST
    Alternative sequencei16 – 4833CSVPR…SVRCL → NTSVMEDQNEDESPKKNTLW in isoform B. 1 PublicationVSP_006766Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF176022 mRNA. Translation: AAF04528.1.
    AB033279 mRNA. Translation: BAA92329.1.
    AB033280 mRNA. Translation: BAA92330.1.
    AB033281 mRNA. Translation: BAA92331.1.
    AB014596 mRNA. Translation: BAA31671.1. Different initiation.
    AK314999 mRNA. Translation: BAG37495.1.
    BC026213 mRNA. Translation: AAH26213.1.
    CCDSiCCDS34289.1. [Q9UKB1-1]
    CCDS47340.1. [Q9UKB1-2]
    CCDS47341.1. [Q9UKB1-3]
    RefSeqiNP_036432.2. NM_012300.2. [Q9UKB1-1]
    NP_387448.2. NM_033644.2. [Q9UKB1-3]
    NP_387449.2. NM_033645.2. [Q9UKB1-2]
    UniGeneiHs.484138.

    Genome annotation databases

    EnsembliENST00000265094; ENSP00000265094; ENSG00000072803. [Q9UKB1-1]
    ENST00000296933; ENSP00000296933; ENSG00000072803. [Q9UKB1-3]
    ENST00000393802; ENSP00000377391; ENSG00000072803. [Q9UKB1-2]
    GeneIDi23291.
    KEGGihsa:23291.
    UCSCiuc003mbl.1. human. [Q9UKB1-3]
    uc003mbm.1. human. [Q9UKB1-1]
    uc003mbn.1. human. [Q9UKB1-2]

    Polymorphism databases

    DMDMi13124267.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF176022 mRNA. Translation: AAF04528.1 .
    AB033279 mRNA. Translation: BAA92329.1 .
    AB033280 mRNA. Translation: BAA92330.1 .
    AB033281 mRNA. Translation: BAA92331.1 .
    AB014596 mRNA. Translation: BAA31671.1 . Different initiation.
    AK314999 mRNA. Translation: BAG37495.1 .
    BC026213 mRNA. Translation: AAH26213.1 .
    CCDSi CCDS34289.1. [Q9UKB1-1 ]
    CCDS47340.1. [Q9UKB1-2 ]
    CCDS47341.1. [Q9UKB1-3 ]
    RefSeqi NP_036432.2. NM_012300.2. [Q9UKB1-1 ]
    NP_387448.2. NM_033644.2. [Q9UKB1-3 ]
    NP_387449.2. NM_033645.2. [Q9UKB1-2 ]
    UniGenei Hs.484138.

    3D structure databases

    ProteinModelPortali Q9UKB1.
    SMRi Q9UKB1. Positions 67-518.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116887. 67 interactions.
    DIPi DIP-27593N.
    IntActi Q9UKB1. 38 interactions.
    MINTi MINT-120522.
    STRINGi 9606.ENSP00000265094.

    PTM databases

    PhosphoSitei Q9UKB1.

    Polymorphism databases

    DMDMi 13124267.

    Proteomic databases

    MaxQBi Q9UKB1.
    PaxDbi Q9UKB1.
    PRIDEi Q9UKB1.

    Protocols and materials databases

    DNASUi 23291.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265094 ; ENSP00000265094 ; ENSG00000072803 . [Q9UKB1-1 ]
    ENST00000296933 ; ENSP00000296933 ; ENSG00000072803 . [Q9UKB1-3 ]
    ENST00000393802 ; ENSP00000377391 ; ENSG00000072803 . [Q9UKB1-2 ]
    GeneIDi 23291.
    KEGGi hsa:23291.
    UCSCi uc003mbl.1. human. [Q9UKB1-3 ]
    uc003mbm.1. human. [Q9UKB1-1 ]
    uc003mbn.1. human. [Q9UKB1-2 ]

    Organism-specific databases

    CTDi 23291.
    GeneCardsi GC05M171288.
    HGNCi HGNC:13607. FBXW11.
    MIMi 605651. gene.
    neXtProti NX_Q9UKB1.
    PharmGKBi PA28050.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2319.
    HOGENOMi HOG000006638.
    HOVERGENi HBG002521.
    InParanoidi Q9UKB1.
    KOi K03362.
    OMAi FDQWSEA.
    OrthoDBi EOG76DTS5.
    PhylomeDBi Q9UKB1.
    TreeFami TF105679.

    Enzyme and pathway databases

    Reactomei REACT_118656. Activation of NF-kappaB in B cells.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinki Q9UKB1.

    Miscellaneous databases

    GeneWikii FBXW11.
    GenomeRNAii 23291.
    NextBioi 45108.
    PROi Q9UKB1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UKB1.
    Bgeei Q9UKB1.
    CleanExi HS_FBXW11.
    Genevestigatori Q9UKB1.

    Family and domain databases

    Gene3Di 2.130.10.10. 2 hits.
    InterProi IPR021977. Beta-TrCP_D.
    IPR001810. F-box_dom.
    IPR020472. G-protein_beta_WD-40_rep.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    Pfami PF12125. Beta-TrCP_D. 1 hit.
    PF12937. F-box-like. 1 hit.
    PF00400. WD40. 7 hits.
    [Graphical view ]
    PRINTSi PR00320. GPROTEINBRPT.
    SMARTi SM01028. Beta-TrCP_D. 1 hit.
    SM00256. FBOX. 1 hit.
    SM00320. WD40. 7 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 1 hit.
    SSF81383. SSF81383. 1 hit.
    PROSITEi PS50181. FBOX. 1 hit.
    PS00678. WD_REPEATS_1. 5 hits.
    PS50082. WD_REPEATS_2. 7 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Molecular cloning and genomic structure of the betaTRCP2 gene on chromosome 5q35.1."
      Koike J., Sagara N., Kirikoshi H., Takagi A., Miwa T., Hirai M., Katoh M.
      Biochem. Biophys. Res. Commun. 269:103-109(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
      Tissue: Fetal lung.
    3. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    4. "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 A).
      Tissue: Hippocampus.
    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] (ISOFORM B).
      Tissue: Lymph.
    6. "IkappaBalpha ubiquitination is catalyzed by an SCF-like complex containing Skp1, cullin-1, and two F-box/WD40-repeat proteins, betaTrCP1 and betaTrCP2."
      Suzuki H., Chiba T., Kobayashi M., Takeuchi M., Suzuki T., Ichiyama A., Ikenoue T., Omata M., Furuichi K., Tanaka K.
      Biochem. Biophys. Res. Commun. 256:127-132(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE SCF(FBXW11) COMPLEX.
    7. "HOS, a human homolog of Slimb, forms an SCF complex with Skp1 and Cullin1 and targets the phosphorylation-dependent degradation of IkappaB and beta-catenin."
      Fuchs S.Y., Chen A., Xiong Y., Pan Z.Q., Ronai Z.
      Oncogene 18:2039-2046(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NFKBIA AND CTNNB1, FUNCTION IN UBIQUITINATION OF NFKBIA AND CTNNB1.
    8. "Homodimer of two F-box proteins betaTrCP1 or betaTrCP2 binds to IkappaBalpha for signal-dependent ubiquitination."
      Suzuki H., Chiba T., Suzuki T., Fujita T., Ikenoue T., Omata M., Furuichi K., Shikama H., Tanaka K.
      J. Biol. Chem. 275:2877-2884(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SELF-ASSOCIATION, INTERACTION WITH BTRC AND NFKBIA, FUNCTION IN UBIQUITINATION OF NFKBIA.
    9. "SCF(HOS) ubiquitin ligase mediates the ligand-induced down-regulation of the interferon-alpha receptor."
      Kumar K.G., Tang W., Ravindranath A.K., Clark W.A., Croze E., Fuchs S.Y.
      EMBO J. 22:5480-5490(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PHOSPHORYLATED IFNAR1, FUNCTION IN IFNAR1 UBIQUITINATION.
    10. "A complex containing betaTrCP recruits Cdc34 to catalyse ubiquitination of IkappaBalpha."
      Vuillard L., Nicholson J., Hay R.T.
      FEBS Lett. 455:311-314(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE SCF(FBXW11) COMPLEX, INTERACTION WITH NFKBIA, FUNCTION IN UBIQUITINATION OF NFKBIA.
    11. "Regulation of p27 degradation and S-phase progression by Ro52 RING finger protein."
      Sabile A., Meyer A.M., Wirbelauer C., Hess D., Kogel U., Scheffner M., Krek W.
      Mol. Cell. Biol. 26:5994-6004(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRIM21.
    12. "The SCF(HOS/beta-TRCP)-ROC1 E3 ubiquitin ligase utilizes two distinct domains within CUL1 for substrate targeting and ubiquitin ligation."
      Wu K., Fuchs S.Y., Chen A., Tan P., Gomez C., Ronai Z., Pan Z.Q.
      Mol. Cell. Biol. 20:1382-1393(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE SCF(FBXW11) COMPLEX.
    13. "Inhibition of HOS expression and activities by Wnt pathway."
      Spiegelman V.S., Tang W., Katoh M., Slaga T.J., Fuchs S.Y.
      Oncogene 21:856-860(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    14. "Degradation of Cdc25A by beta-TrCP during S phase and in response to DNA damage."
      Busino L., Donzelli M., Chiesa M., Guardavaccaro D., Ganoth D., Dorrello N.V., Hershko A., Pagano M., Draetta G.F.
      Nature 426:87-91(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CDC25A.
    15. "SCFbeta-TRCP controls clock-dependent transcription via casein kinase 1-dependent degradation of the mammalian period-1 (Per1) protein."
      Shirogane T., Jin J., Ang X.L., Harper J.W.
      J. Biol. Chem. 280:26863-26872(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CIRCADIAN CLOCK, INTERACTION WITH PER1 AND PER3.
    16. "Oxidative stress-induced ubiquitination of RCAN1 mediated by SCFbeta-TrCP ubiquitin ligase."
      Asada S., Ikeda A., Nagao R., Hama H., Sudo T., Fukamizu A., Kasuya Y., Kishi T.
      Int. J. Mol. Med. 22:95-104(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RCAN1.
    17. "HIV-1 Vpu neutralizes the antiviral factor Tetherin/BST-2 by binding it and directing its beta-TrCP2-dependent degradation."
      Mangeat B., Gers-Huber G., Lehmann M., Zufferey M., Luban J., Piguet V.
      PLoS Pathog. 5:E1000574-E1000574(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BST2.
    18. "Priming and extending: a UbcH5/Cdc34 E2 handoff mechanism for polyubiquitination on a SCF substrate."
      Wu K., Kovacev J., Pan Z.Q.
      Mol. Cell 37:784-796(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE SCF(FBXW11) COMPLEX, INTERACTION WITH NFKBIA.
    19. "The ubiquitin-specific protease USP47 is a novel beta-TRCP interactor regulating cell survival."
      Peschiaroli A., Skaar J.R., Pagano M., Melino G.
      Oncogene 29:1384-1393(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH USP47.

    Entry informationi

    Entry nameiFBW1B_HUMAN
    AccessioniPrimary (citable) accession number: Q9UKB1
    Secondary accession number(s): B2RC98
    , Q9P2S8, Q9P2S9, Q9Y4C6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 147 of the entry and version 1 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3