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Q9Y297 (FBW1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:BTRC
Synonyms:BTRCP, FBW1A, FBXW1A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length605 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.9 Ref.10 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.27 Ref.30

Pathway

Protein modification; protein ubiquitination.

Subunit structure

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. Ref.2 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.31 Ref.33

Subcellular location

Cytoplasm. Nucleus By similarity.

Tissue specificity

Expressed in epididymis (at protein level). Ref.4

Domain

The N-terminal D domain mediates homodimerization. Ref.33

Sequence similarities

Contains 1 F-box domain.

Contains 7 WD repeats.

Ontologies

Keywords
   Biological processBiological rhythms
Host-virus interaction
Ubl conjugation pathway
Wnt signaling pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
WD repeat
   Molecular functionLigase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

SCF-dependent proteasomal ubiquitin-dependent protein catabolic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

Wnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process

Traceable author statement. Source: Reactome

branching involved in mammary gland duct morphogenesis

Inferred from electronic annotation. Source: Ensembl

cellular response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

mammary gland epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of sequence-specific DNA binding transcription factor activity

Traceable author statement PubMed 11001584. Source: BHF-UCL

negative regulation of smoothened signaling pathway

Traceable author statement PubMed 11001584. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 19966869. Source: UniProtKB

positive regulation of circadian rhythm

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of proteolysis

Inferred from mutant phenotype PubMed 16885022. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.27. Source: UniProtKB

protein dephosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

protein destabilization

Inferred from mutant phenotype PubMed 16885022. Source: UniProtKB

protein polyubiquitination

Inferred from electronic annotation. Source: Ensembl

protein ubiquitination

Inferred from direct assay PubMed 16885022. Source: UniProtKB

regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from electronic annotation. Source: Ensembl

regulation of cell cycle

Inferred from electronic annotation. Source: Ensembl

regulation of circadian rhythm

Inferred from direct assay Ref.27. Source: UniProtKB

regulation of proteasomal protein catabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

signal transduction

Traceable author statement PubMed 9990853. Source: ProtInc

ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.25. Source: UniProtKB

viral process

Traceable author statement. Source: Reactome

   Cellular_componentSCF ubiquitin ligase complex

Inferred from direct assay PubMed 19966869. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein binding

Inferred from physical interaction Ref.16. Source: IntAct

ubiquitin-protein transferase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y297-1)

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.
Isoform 2 (identifier: Q9Y297-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 605605F-box/WD repeat-containing protein 1A
PRO_0000050980

Regions

Domain190 – 22839F-box
Repeat301 – 33838WD 1
Repeat341 – 37838WD 2
Repeat381 – 41838WD 3
Repeat424 – 46138WD 4
Repeat464 – 50340WD 5
Repeat505 – 54137WD 6
Repeat553 – 59038WD 7
Region128 – 17750Homodimerization domain D
Region190 – 22839Required for down-regulation of SNAI1

Natural variations

Alternative sequence17 – 5236Missing in isoform 2.
VSP_006764
Natural variant5431A → S.
Corresponds to variant rs4151060 [ dbSNP | Ensembl ].
VAR_022027
Natural variant5921P → H.
Corresponds to variant rs2270439 [ dbSNP | Ensembl ].
VAR_020119

Secondary structure

....................................................................................... 605
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 4C67F3B7E400FD37

FASTA60568,867
        10         20         30         40         50         60 
MDPAEAVLQE KALKFMCSMP RSLWLGCSSL ADSMPSLRCL YNPGTGALTA FQNSSEREDC 

        70         80         90        100        110        120 
NNGEPPRKII PEKNSLRQTY NSCARLCLNQ ETVCLASTAM KTENCVAKTK LANGTSSMIV 

       130        140        150        160        170        180 
PKQRKLSASY EKEKELCVKY FEQWSESDQV EFVEHLISQM CHYQHGHINS YLKPMLQRDF 

       190        200        210        220        230        240 
ITALPARGLD HIAENILSYL DAKSLCAAEL VCKEWYRVTS DGMLWKKLIE RMVRTDSLWR 

       250        260        270        280        290        300 
GLAERRGWGQ YLFKNKPPDG NAPPNSFYRA LYPKIIQDIE TIESNWRCGR HSLQRIHCRS 

       310        320        330        340        350        360 
ETSKGVYCLQ YDDQKIVSGL RDNTIKIWDK NTLECKRILT GHTGSVLCLQ YDERVIITGS 

       370        380        390        400        410        420 
SDSTVRVWDV NTGEMLNTLI HHCEAVLHLR FNNGMMVTCS KDRSIAVWDM ASPTDITLRR 

       430        440        450        460        470        480 
VLVGHRAAVN VVDFDDKYIV SASGDRTIKV WNTSTCEFVR TLNGHKRGIA CLQYRDRLVV 

       490        500        510        520        530        540 
SGSSDNTIRL WDIECGACLR VLEGHEELVR CIRFDNKRIV SGAYDGKIKV WDLVAALDPR 

       550        560        570        580        590        600 
APAGTLCLRT LVEHSGRVFR LQFDEFQIVS SSHDDTILIW DFLNDPAAQA EPPRSPSRTY 


TYISR 

« Hide

Isoform 2 [UniParc].

Checksum: 6E7C4FBE7BB520BA
Show »

FASTA56965,049

References

« Hide 'large scale' references
[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]"Identification of a family of human F-box proteins."
Cenciarelli C., Chiaur D.S., Guardavaccaro D., Parks W., Vidal M., Pagano M.
Curr. Biol. 9:1177-1179(1999) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS7511.1. [Q9Y297-2]
CCDS7512.1. [Q9Y297-1]
RefSeqNP_003930.1. NM_003939.4. [Q9Y297-2]
NP_378663.1. NM_033637.3. [Q9Y297-1]
UniGeneHs.643802.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1P22X-ray2.95A175-605[»]
2P64X-ray2.50A/B128-177[»]
ProteinModelPortalQ9Y297.
SMRQ9Y297. Positions 127-581.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114457. 162 interactions.
DIPDIP-31607N.
IntActQ9Y297. 56 interactions.
MINTMINT-108636.
STRING9606.ENSP00000359206.

PTM databases

PhosphoSiteQ9Y297.

Polymorphism databases

DMDM13124271.

Proteomic databases

MaxQBQ9Y297.
PaxDbQ9Y297.
PRIDEQ9Y297.

Protocols and materials databases

DNASU8945.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370187; ENSP00000359206; ENSG00000166167. [Q9Y297-1]
ENST00000408038; ENSP00000385339; ENSG00000166167. [Q9Y297-2]
GeneID8945.
KEGGhsa:8945.
UCSCuc001kta.4. human. [Q9Y297-1]
uc001ktb.4. human. [Q9Y297-2]

Organism-specific databases

CTD8945.
GeneCardsGC10P103103.
HGNCHGNC:1144. BTRC.
HPACAB032986.
MIM603482. gene.
neXtProtNX_Q9Y297.
Orphanet2440. Split hand-split foot malformation.
PharmGKBPA25465.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2319.
HOGENOMHOG000006638.
HOVERGENHBG002521.
InParanoidQ9Y297.
KOK03362.
OMANAYLKPM.
OrthoDBEOG76DTS5.
PhylomeDBQ9Y297.
TreeFamTF105679.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_24941. Circadian Clock.
REACT_6900. Immune System.
SignaLinkQ9Y297.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ9Y297.
BgeeQ9Y297.
CleanExHS_BTRC.
GenevestigatorQ9Y297.

Family and domain databases

Gene3D2.130.10.10. 2 hits.
InterProIPR021977. 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]
PfamPF12125. Beta-TrCP_D. 1 hit.
PF12937. F-box-like. 1 hit.
PF00400. WD40. 7 hits.
[Graphical view]
PRINTSPR00320. GPROTEINBRPT.
SMARTSM01028. Beta-TrCP_D. 1 hit.
SM00256. FBOX. 1 hit.
SM00320. WD40. 7 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
SSF81383. SSF81383. 1 hit.
PROSITEPS50181. FBOX. 1 hit.
PS00678. WD_REPEATS_1. 6 hits.
PS50082. WD_REPEATS_2. 7 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBTRC. human.
EvolutionaryTraceQ9Y297.
GeneWikiBTRC_(gene).
GenomeRNAi8945.
NextBio33645.
PROQ9Y297.
SOURCESearch...

Entry information

Entry nameFBW1A_HUMAN
AccessionPrimary (citable) accession number: Q9Y297
Secondary accession number(s): B5MD49 expand/collapse secondary AC list , Q5W141, Q5W142, Q9Y213
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM