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Q9Y297

- FBW1A_HUMAN

UniProt

Q9Y297 - FBW1A_HUMAN

Protein

F-box/WD repeat-containing protein 1A

Gene

BTRC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      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. Recognizes and binds to phosphorylated target proteins. SCF(BTRC) mediates the ubiquitination of CTNNB1 and participates in Wnt signaling. SCF(BTRC) mediates the ubiquitination of NFKBIA, NFKBIB and NFKBIE; the degradation frees the associated NFKB1 to translocate into the nucleus and to activate transcription. Ubiquitination of NFKBIA occurs at 'Lys-21' and 'Lys-22'. SCF(BTRC) mediates the ubiquitination of phosphorylated NFKB1/nuclear factor NF-kappa-B p105 subunit, ATF4, CDC25A, DLG1, FBXO5, PER1, SMAD3, SMAD4, SNAI1 and probably NFKB2. Has an essential role in the control of the clock-dependent transcription via degradation of phosphorylated PER1 and PER2. May be involved in ubiquitination and subsequent proteasomal degradation through a DBB1-CUL4 E3 ubiquitin-protein ligase. Required for activation of NFKB-mediated transcription by IL1B, MAP3K14, MAP3K1, IKBKB and TNF. Required for proteolytic processing of GLI3.16 Publications

    Pathwayi

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. ubiquitin-protein transferase activity Source: Ensembl

    GO - Biological processi

    1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
    2. branching involved in mammary gland duct morphogenesis Source: Ensembl
    3. cellular response to organic cyclic compound Source: Ensembl
    4. G2/M transition of mitotic cell cycle Source: Reactome
    5. mammary gland epithelial cell proliferation Source: Ensembl
    6. mitotic cell cycle Source: Reactome
    7. negative regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    8. negative regulation of smoothened signaling pathway Source: BHF-UCL
    9. negative regulation of transcription, DNA-templated Source: UniProtKB
    10. positive regulation of circadian rhythm Source: UniProtKB
    11. positive regulation of proteolysis Source: UniProtKB
    12. positive regulation of transcription, DNA-templated Source: UniProtKB
    13. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    14. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
    15. protein dephosphorylation Source: UniProtKB
    16. protein destabilization Source: UniProtKB
    17. protein polyubiquitination Source: Ensembl
    18. protein ubiquitination Source: UniProtKB
    19. regulation of cell cycle Source: Ensembl
    20. regulation of circadian rhythm Source: UniProtKB
    21. regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
    22. regulation of proteasomal protein catabolic process Source: Ensembl
    23. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    24. rhythmic process Source: UniProtKB-KW
    25. SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Source: RefGenome
    26. signal transduction Source: ProtInc
    27. ubiquitin-dependent protein catabolic process Source: UniProtKB
    28. viral process Source: Reactome
    29. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Biological rhythms, Host-virus interaction, Ubl conjugation pathway, Wnt signaling pathway

    Enzyme and pathway databases

    ReactomeiREACT_115697. Prolactin receptor signaling.
    REACT_118656. Activation of NF-kappaB in B cells.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_200731. deactivation of the beta-catenin transactivating complex.
    REACT_22442. Interleukin-1 signaling.
    REACT_24941. Circadian Clock.
    REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_9031. Vpu mediated degradation of CD4.
    SignaLinkiQ9Y297.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    F-box/WD repeat-containing protein 1A
    Alternative name(s):
    E3RSIkappaB
    Epididymis tissue protein Li 2a
    F-box and WD repeats protein beta-TrCP
    pIkappaBalpha-E3 receptor subunit
    Gene namesi
    Name:BTRC
    Synonyms:BTRCP, FBW1A, FBXW1A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:1144. BTRC.

    Subcellular locationi

    Cytoplasm. Nucleus By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleus Source: UniProtKB-SubCell
    3. SCF ubiquitin ligase complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti2440. Split hand-split foot malformation.
    PharmGKBiPA25465.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 605605F-box/WD repeat-containing protein 1APRO_0000050980Add
    BLAST

    Proteomic databases

    MaxQBiQ9Y297.
    PaxDbiQ9Y297.
    PRIDEiQ9Y297.

    PTM databases

    PhosphoSiteiQ9Y297.

    Expressioni

    Tissue specificityi

    Expressed in epididymis (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ9Y297.
    BgeeiQ9Y297.
    CleanExiHS_BTRC.
    GenevestigatoriQ9Y297.

    Organism-specific databases

    HPAiCAB032986.

    Interactioni

    Subunit structurei

    Homodimer. Self-associates. Component of the SCF(BTRC) complex formed of CUL1, SKP1, RBX1 and a BTRC dimer. Direct interaction with SKP1 occurs via the F-box domain. Interacts with phosphorylated ubiquitination substrates SMAD3 and SMAD4. Interacts with phosphorylated ubiquitination substrates CTNNB1, NFKBIA, NFKBIB, NFKBIE, NFKB1/nuclear factor NF-kappa-B p105 subunit, ATF4, CDC25A, DLG1, FBXO5 and SNAI1; the interaction requires the phosphorylation of the 2 serine residues in the substrate destruction motif D-S-G-X(2,3,4)-S. Binds UBQLN1. Interacts with CDC34 and UBE2R2. Interacts with FBXW11. Interacts with CUL4A and DDB1. Part of a SCF(BTRC)-like complex lacking CUL1, which is associated with phosphorylated NKBIA and RELA; RELA interacts directly with NFKBIA. Interacts with HIV-1 Vpu. Interacts with the phosphorylated form of GLI3. Interacts with CLU. Interacts with PER1 (phosphorylated), PER2 (phosphorylated) and PER3.23 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ATF4P188485EBI-8826333,EBI-492498
    CTNNB1P352225EBI-307461,EBI-491549
    CUL1Q136165EBI-307461,EBI-359390
    DLG1Q129592EBI-307461,EBI-357481
    Dlg1Q626963EBI-307461,EBI-389325From a different organism.
    MAP2K1Q027503EBI-307461,EBI-492564
    MDM2Q009879EBI-307461,EBI-389668
    NEDD8Q158432EBI-307461,EBI-716247
    SKP1P632084EBI-307461,EBI-307486
    SNAI1O958632EBI-307461,EBI-1045459
    WEE1P302912EBI-307461,EBI-914695
    ZC3H12AQ5D1E83EBI-307461,EBI-747793

    Protein-protein interaction databases

    BioGridi114457. 167 interactions.
    DIPiDIP-31607N.
    IntActiQ9Y297. 56 interactions.
    MINTiMINT-108636.
    STRINGi9606.ENSP00000359206.

    Structurei

    Secondary structure

    1
    605
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi129 – 14113
    Helixi146 – 15813
    Helixi162 – 17211
    Helixi173 – 1753
    Helixi180 – 1834
    Helixi185 – 1873
    Helixi190 – 1978
    Helixi202 – 21110
    Helixi213 – 2219
    Helixi224 – 23310
    Helixi237 – 2448
    Beta strandi245 – 2473
    Helixi248 – 2514
    Helixi266 – 28520
    Turni286 – 2883
    Beta strandi306 – 3105
    Beta strandi313 – 32311
    Beta strandi325 – 3328
    Beta strandi335 – 3395
    Beta strandi346 – 3505
    Beta strandi353 – 3608
    Beta strandi365 – 3728
    Beta strandi375 – 3795
    Beta strandi386 – 3905
    Beta strandi395 – 4006
    Beta strandi405 – 4095
    Beta strandi411 – 4144
    Beta strandi417 – 4226
    Beta strandi429 – 4357
    Beta strandi438 – 4436
    Beta strandi446 – 4527
    Turni453 – 4553
    Beta strandi458 – 4636
    Beta strandi469 – 4757
    Beta strandi478 – 4836
    Beta strandi488 – 4925
    Turni493 – 4953
    Beta strandi498 – 5025
    Beta strandi509 – 5135
    Beta strandi516 – 5238
    Beta strandi528 – 5325
    Helixi533 – 5364
    Turni543 – 5464
    Beta strandi547 – 5515
    Beta strandi561 – 5633
    Beta strandi568 – 5703
    Beta strandi573 – 5808

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P22X-ray2.95A175-605[»]
    2P64X-ray2.50A/B128-177[»]
    ProteinModelPortaliQ9Y297.
    SMRiQ9Y297. Positions 127-581.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y297.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini190 – 22839F-boxPROSITE-ProRule annotationAdd
    BLAST
    Repeati301 – 33838WD 1Add
    BLAST
    Repeati341 – 37838WD 2Add
    BLAST
    Repeati381 – 41838WD 3Add
    BLAST
    Repeati424 – 46138WD 4Add
    BLAST
    Repeati464 – 50340WD 5Add
    BLAST
    Repeati505 – 54137WD 6Add
    BLAST
    Repeati553 – 59038WD 7Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni128 – 17750Homodimerization domain DAdd
    BLAST
    Regioni190 – 22839Required for down-regulation of SNAI1Add
    BLAST

    Domaini

    The N-terminal D domain mediates homodimerization.1 Publication

    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.
    InParanoidiQ9Y297.
    KOiK03362.
    OMAiNAYLKPM.
    OrthoDBiEOG76DTS5.
    PhylomeDBiQ9Y297.
    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. 6 hits.
    PS50082. WD_REPEATS_2. 7 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y297-1) [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

    MDPAEAVLQE KALKFMCSMP RSLWLGCSSL ADSMPSLRCL YNPGTGALTA    50
    FQNSSEREDC NNGEPPRKII PEKNSLRQTY NSCARLCLNQ ETVCLASTAM 100
    KTENCVAKTK LANGTSSMIV PKQRKLSASY EKEKELCVKY FEQWSESDQV 150
    EFVEHLISQM CHYQHGHINS YLKPMLQRDF ITALPARGLD HIAENILSYL 200
    DAKSLCAAEL VCKEWYRVTS DGMLWKKLIE RMVRTDSLWR GLAERRGWGQ 250
    YLFKNKPPDG NAPPNSFYRA LYPKIIQDIE TIESNWRCGR HSLQRIHCRS 300
    ETSKGVYCLQ YDDQKIVSGL RDNTIKIWDK NTLECKRILT GHTGSVLCLQ 350
    YDERVIITGS SDSTVRVWDV NTGEMLNTLI HHCEAVLHLR FNNGMMVTCS 400
    KDRSIAVWDM ASPTDITLRR VLVGHRAAVN VVDFDDKYIV SASGDRTIKV 450
    WNTSTCEFVR TLNGHKRGIA CLQYRDRLVV SGSSDNTIRL WDIECGACLR 500
    VLEGHEELVR CIRFDNKRIV SGAYDGKIKV WDLVAALDPR APAGTLCLRT 550
    LVEHSGRVFR LQFDEFQIVS SSHDDTILIW DFLNDPAAQA EPPRSPSRTY 600
    TYISR 605
    Length:605
    Mass (Da):68,867
    Last modified:November 1, 1999 - v1
    Checksum:i4C67F3B7E400FD37
    GO
    Isoform 2 (identifier: Q9Y297-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         17-52: Missing.

    Show »
    Length:569
    Mass (Da):65,049
    Checksum:i6E7C4FBE7BB520BA
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti543 – 5431A → S.
    Corresponds to variant rs4151060 [ dbSNP | Ensembl ].
    VAR_022027
    Natural varianti592 – 5921P → H.
    Corresponds to variant rs2270439 [ dbSNP | Ensembl ].
    VAR_020119

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei17 – 5236Missing in isoform 2. 2 PublicationsVSP_006764Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF101784 mRNA. Translation: AAD08702.1.
    Y14153 mRNA. Translation: CAA74572.1.
    AF129530 mRNA. Translation: AAF04464.1.
    GU727631 mRNA. Translation: ADU87633.1.
    AK313353 mRNA. Translation: BAG36155.1.
    AL133387, AL445463, AL627424 Genomic DNA. Translation: CAH70019.1.
    AL133387, AL445463, AL627424 Genomic DNA. Translation: CAH70020.1.
    AL445463, AL133387, AL627424 Genomic DNA. Translation: CAI12963.1.
    AL445463, AL133387, AL627424 Genomic DNA. Translation: CAI12964.1.
    AL627424, AL133387, AL445463 Genomic DNA. Translation: CAI41042.1.
    AL627424, AL133387, AL445463 Genomic DNA. Translation: CAI41043.1.
    CH471066 Genomic DNA. Translation: EAW49772.1.
    CH471066 Genomic DNA. Translation: EAW49774.1.
    BC027994 mRNA. Translation: AAH27994.1.
    CCDSiCCDS7511.1. [Q9Y297-2]
    CCDS7512.1. [Q9Y297-1]
    RefSeqiNP_003930.1. NM_003939.4. [Q9Y297-2]
    NP_378663.1. NM_033637.3. [Q9Y297-1]
    UniGeneiHs.643802.

    Genome annotation databases

    EnsembliENST00000370187; ENSP00000359206; ENSG00000166167. [Q9Y297-1]
    ENST00000408038; ENSP00000385339; ENSG00000166167. [Q9Y297-2]
    GeneIDi8945.
    KEGGihsa:8945.
    UCSCiuc001kta.4. human. [Q9Y297-1]
    uc001ktb.4. human. [Q9Y297-2]

    Polymorphism databases

    DMDMi13124271.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF101784 mRNA. Translation: AAD08702.1 .
    Y14153 mRNA. Translation: CAA74572.1 .
    AF129530 mRNA. Translation: AAF04464.1 .
    GU727631 mRNA. Translation: ADU87633.1 .
    AK313353 mRNA. Translation: BAG36155.1 .
    AL133387 , AL445463 , AL627424 Genomic DNA. Translation: CAH70019.1 .
    AL133387 , AL445463 , AL627424 Genomic DNA. Translation: CAH70020.1 .
    AL445463 , AL133387 , AL627424 Genomic DNA. Translation: CAI12963.1 .
    AL445463 , AL133387 , AL627424 Genomic DNA. Translation: CAI12964.1 .
    AL627424 , AL133387 , AL445463 Genomic DNA. Translation: CAI41042.1 .
    AL627424 , AL133387 , AL445463 Genomic DNA. Translation: CAI41043.1 .
    CH471066 Genomic DNA. Translation: EAW49772.1 .
    CH471066 Genomic DNA. Translation: EAW49774.1 .
    BC027994 mRNA. Translation: AAH27994.1 .
    CCDSi CCDS7511.1. [Q9Y297-2 ]
    CCDS7512.1. [Q9Y297-1 ]
    RefSeqi NP_003930.1. NM_003939.4. [Q9Y297-2 ]
    NP_378663.1. NM_033637.3. [Q9Y297-1 ]
    UniGenei Hs.643802.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1P22 X-ray 2.95 A 175-605 [» ]
    2P64 X-ray 2.50 A/B 128-177 [» ]
    ProteinModelPortali Q9Y297.
    SMRi Q9Y297. Positions 127-581.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114457. 167 interactions.
    DIPi DIP-31607N.
    IntActi Q9Y297. 56 interactions.
    MINTi MINT-108636.
    STRINGi 9606.ENSP00000359206.

    PTM databases

    PhosphoSitei Q9Y297.

    Polymorphism databases

    DMDMi 13124271.

    Proteomic databases

    MaxQBi Q9Y297.
    PaxDbi Q9Y297.
    PRIDEi Q9Y297.

    Protocols and materials databases

    DNASUi 8945.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000370187 ; ENSP00000359206 ; ENSG00000166167 . [Q9Y297-1 ]
    ENST00000408038 ; ENSP00000385339 ; ENSG00000166167 . [Q9Y297-2 ]
    GeneIDi 8945.
    KEGGi hsa:8945.
    UCSCi uc001kta.4. human. [Q9Y297-1 ]
    uc001ktb.4. human. [Q9Y297-2 ]

    Organism-specific databases

    CTDi 8945.
    GeneCardsi GC10P103103.
    HGNCi HGNC:1144. BTRC.
    HPAi CAB032986.
    MIMi 603482. gene.
    neXtProti NX_Q9Y297.
    Orphaneti 2440. Split hand-split foot malformation.
    PharmGKBi PA25465.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2319.
    HOGENOMi HOG000006638.
    HOVERGENi HBG002521.
    InParanoidi Q9Y297.
    KOi K03362.
    OMAi NAYLKPM.
    OrthoDBi EOG76DTS5.
    PhylomeDBi Q9Y297.
    TreeFami TF105679.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_115697. Prolactin receptor signaling.
    REACT_118656. Activation of NF-kappaB in B cells.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_200731. deactivation of the beta-catenin transactivating complex.
    REACT_22442. Interleukin-1 signaling.
    REACT_24941. Circadian Clock.
    REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_9031. Vpu mediated degradation of CD4.
    SignaLinki Q9Y297.

    Miscellaneous databases

    ChiTaRSi BTRC. human.
    EvolutionaryTracei Q9Y297.
    GeneWikii BTRC_(gene).
    GenomeRNAii 8945.
    NextBioi 33645.
    PROi Q9Y297.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y297.
    Bgeei Q9Y297.
    CleanExi HS_BTRC.
    Genevestigatori Q9Y297.

    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. 6 hits.
    PS50082. WD_REPEATS_2. 7 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of the receptor component of the IkappaBalpha-ubiquitin ligase."
      Yaron A., Hatzubai A., Davis M., Lavon I., Amit S., Manning A.M., Andersen J.S., Mann M., Mercurio F., Ben-Neriah Y.
      Nature 396:590-594(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
    2. "A novel human WD protein, h-beta TrCp, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif."
      Margottin F., Bour S.P., Durand H., Selig L., Benichou S., Richard V., Thomas D., Strebel K., Benarous R.
      Mol. Cell 1:565-574(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH HIV-1 VPU.
      Tissue: Lymphoid tissue.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    4. "Systematic mapping and functional analysis of a family of human epididymal secretory sperm-located proteins."
      Li J., Liu F., Wang H., Liu X., Liu J., Li N., Wan F., Wang W., Zhang C., Jin S., Liu J., Zhu P., Liu Y.
      Mol. Cell. Proteomics 9:2517-2528(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Epididymis.
    5. "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: Testis.
    6. "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].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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 1).
      Tissue: Brain.
    9. "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(BTRC) COMPLEX, FUNCTION IN UBIQUITINATION OF NFKBIA.
    10. "Common pathway for the ubiquitination of IkappaBalpha, IkappaBbeta, and IkappaBepsilon mediated by the F-box protein FWD1."
      Shirane M., Hatakeyama S., Hattori K., Nakayama K., Nakayama K.
      J. Biol. Chem. 274:28169-28174(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NFKBIB AND NFKBIE, FUNCTION IN UBIQUITINATION OF NFKBIB AND NFKBIE.
    11. "The SCF(beta-TRCP)-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in I-kappa-B-alpha and beta-catenin and stimulates I-kappa-B-alpha ubiquitination in vitro."
      Winston J.T., Strack P., Beer-Romero P., Chu C.Y., Elledge S.J., Harper J.W.
      Genes Dev. 13:270-283(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    12. "SCF(beta)(-TrCP) ubiquitin ligase-mediated processing of NF-kappaB p105 requires phosphorylation of its C-terminus by IkappaB kinase."
      Orian A., Gonen H., Bercovich B., Fajerman I., Eytan E., Israel A., Mercurio F., Iwai K., Schwartz A.L., Ciechanover A.
      EMBO J. 19:2580-2591(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NFKB1, FUNCTION IN UBIQUITINATION OF NFKB1.
    13. "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 FBXW11 AND NFKBIA, FUNCTION IN UBIQUITINATION OF NFKBIA.
    14. "The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome."
      Kleijnen M.F., Shih A.H., Zhou P., Kumar S., Soccio R.E., Kedersha N.L., Gill G., Howley P.M.
      Mol. Cell 6:409-419(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UBQLN1.
      Tissue: B-cell.
    15. "Ligand-dependent degradation of Smad3 by a ubiquitin ligase complex of ROC1 and associated proteins."
      Fukuchi M., Imamura T., Chiba T., Ebisawa T., Kawabata M., Tanaka K., Miyazono K.
      Mol. Biol. Cell 12:1431-1443(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PHOSPHORYLATED SMAD3, FUNCTION IN SMAD3 UBIQUITINATION.
    16. "ATF4 degradation relies on a phosphorylation-dependent interaction with the SCF(betaTrCP) ubiquitin ligase."
      Lassot I., Segeral E., Berlioz-Torrent C., Durand H., Groussin L., Hai T., Benarous R., Margottin-Goguet F.
      Mol. Cell. Biol. 21:2192-2202(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PHOSPHORYLATED ATF4, FUNCTION IN ATF4 UBIQUITINATION.
    17. "Genetic evidence for the essential role of beta-transducin repeat-containing protein in the inducible processing of NF-kappa B2/p100."
      Fong A., Sun S.C.
      J. Biol. Chem. 277:22111-22114(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NFKB2 UBIQUITINATION.
    18. "Regulation of S33/S37 phosphorylated beta-catenin in normal and transformed cells."
      Sadot E., Conacci-Sorrell M., Zhurinsky J., Shnizer D., Lando Z., Zharhary D., Kam Z., Ben-Ze'ev A., Geiger B.
      J. Cell Sci. 115:2771-2780(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PHOSPHORYLATED CTNNB1.
    19. "CK2-dependent phosphorylation of the E2 ubiquitin conjugating enzyme UBC3B induces its interaction with beta-TrCP and enhances beta-catenin degradation."
      Semplici F., Meggio F., Pinna L.A., Oliviero S.
      Oncogene 21:3978-3987(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDC34 AND UBE2R2.
    20. "Prophase destruction of Emi1 by the SCF(betaTrCP/Slimb) ubiquitin ligase activates the anaphase promoting complex to allow progression beyond prometaphase."
      Margottin-Goguet F., Hsu J.Y., Loktev A., Hsieh H.-M., Reimann J.D.R., Jackson P.K.
      Dev. Cell 4:813-826(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PHOSPHORYLATED FBXO5, FUNCTION IN FBXO5 UBIQUITINATION.
    21. "SCFbeta-TRCP links Chk1 signaling to degradation of the Cdc25A protein phosphatase."
      Jin J., Shirogane T., Xu L., Nalepa G., Qin J., Elledge S.J., Harper J.W.
      Genes Dev. 17:3062-3074(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PHOSPHORYLATED CDC25A, FUNCTION IN CDC25A UBIQUITINATION.
    22. "Regulation of the discs large tumor suppressor by a phosphorylation-dependent interaction with the beta-TrCP ubiquitin ligase receptor."
      Mantovani F., Banks L.
      J. Biol. Chem. 278:42477-42486(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PHOSPHORYLATED DLG1, FUNCTION IN DLG1 UBIQUITINATION.
    23. "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: INTERACTION WITH PHOSPHORYLATED CDC25A, FUNCTION IN CDC25A UBIQUITINATION.
    24. "Smad4 protein stability is regulated by ubiquitin ligase SCF beta-TrCP1."
      Wan M., Tang Y., Tytler E.M., Lu C., Jin B., Vickers S.M., Yang L., Shi X., Cao X.
      J. Biol. Chem. 279:14484-14487(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PHOSPHORYLATED SMAD4, FUNCTION IN SMAD4 UBIQUITINATION.
    25. "Dual regulation of Snail by GSK-3beta-mediated phosphorylation in control of epithelial-mesenchymal transition."
      Zhou B.P., Deng J., Xia W., Xu J., Li Y.M., Gunduz M., Hung M.C.
      Nat. Cell Biol. 6:931-940(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SNAI1.
    26. "Wnt-dependent regulation of the E-cadherin repressor snail."
      Yook J.I., Li X.Y., Ota I., Fearon E.R., Weiss S.J.
      J. Biol. Chem. 280:11740-11748(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SNAI1.
    27. "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.
    28. "DDB1 functions as a linker to recruit receptor WD40 proteins to CUL4-ROC1 ubiquitin ligases."
      He Y.J., McCall C.M., Hu J., Zeng Y., Xiong Y.
      Genes Dev. 20:2949-2954(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CUL4A AND DDB1.
    29. "Multisite protein kinase A and glycogen synthase kinase 3beta phosphorylation leads to Gli3 ubiquitination by SCFbetaTrCP."
      Tempe D., Casas M., Karaz S., Blanchet-Tournier M.F., Concordet J.P.
      Mol. Cell. Biol. 26:4316-4326(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GLI3.
    30. "Evidence for the direct involvement of {beta}TrCP in Gli3 protein processing."
      Wang B., Li Y.
      Proc. Natl. Acad. Sci. U.S.A. 103:33-38(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    31. "Clusterin facilitates COMMD1 and I-kappaB degradation to enhance NF-kappaB activity in prostate cancer cells."
      Zoubeidi A., Ettinger S., Beraldi E., Hadaschik B., Zardan A., Klomp L.W., Nelson C.C., Rennie P.S., Gleave M.E.
      Mol. Cancer Res. 8:119-130(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CLU.
    32. "Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase."
      Wu G., Xu G., Schulman B.A., Jeffrey P.D., Harper J.W., Pavletich N.P.
      Mol. Cell 11:1445-1456(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 175-605 IN COMPLEX WITH SKP1 AND CTNNB1.
    33. "Suprafacial orientation of the SCFCdc4 dimer accommodates multiple geometries for substrate ubiquitination."
      Tang X., Orlicky S., Lin Z., Willems A., Neculai D., Ceccarelli D., Mercurio F., Shilton B.H., Sicheri F., Tyers M.
      Cell 129:1165-1176(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 128-177, DOMAIN, SUBUNIT.

    Entry informationi

    Entry nameiFBW1A_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y297
    Secondary accession number(s): B5MD49
    , Q5W141, Q5W142, Q9Y213
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 151 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3