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Protein

F-box/WD repeat-containing protein 1A

Gene

Btrc

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 CEP68; this is required for centriole separation during mitosis (By similarity). 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.By similarity5 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.3 Publications
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

  • beta-catenin binding Source: BHF-UCL
  • protein phosphorylated amino acid binding Source: BHF-UCL
  • ubiquitin protein ligase activity Source: BHF-UCL
  • ubiquitin-protein transferase activity Source: Reactome

GO - Biological processi

  • branching involved in mammary gland duct morphogenesis Source: MGI
  • cellular response to organic cyclic compound Source: MGI
  • circadian rhythm Source: Reactome
  • mammary gland epithelial cell proliferation Source: MGI
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of circadian rhythm Source: UniProtKB
  • positive regulation of proteolysis Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • protein catabolic process Source: MGI
  • protein dephosphorylation Source: UniProtKB
  • protein destabilization Source: UniProtKB
  • protein polyubiquitination Source: BHF-UCL
  • protein ubiquitination Source: MGI
  • regulation of canonical Wnt signaling pathway Source: ParkinsonsUK-UCL
  • regulation of cell cycle Source: MGI
  • regulation of circadian rhythm Source: UniProtKB
  • regulation of I-kappaB kinase/NF-kappaB signaling Source: MGI
  • regulation of proteasomal protein catabolic process Source: MGI
  • ubiquitin-dependent protein catabolic process Source: UniProtKB
  • Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Biological rhythms, Ubl conjugation pathway, Wnt signaling pathway

Enzyme and pathway databases

ReactomeiR-MMU-1169091. Activation of NF-kappaB in B cells.
R-MMU-1170546. Prolactin receptor signaling.
R-MMU-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-MMU-195253. Degradation of beta-catenin by the destruction complex.
R-MMU-202424. Downstream TCR signaling.
R-MMU-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-MMU-2871837. FCERI mediated NF-kB activation.
R-MMU-3769402. Deactivation of the beta-catenin transactivating complex.
R-MMU-400253. Circadian Clock.
R-MMU-508751. Circadian Clock.
R-MMU-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-MMU-5607764. CLEC7A (Dectin-1) signaling.
R-MMU-5610780. Degradation of GLI1 by the proteasome.
R-MMU-5610785. GLI3 is processed to GLI3R by the proteasome.
R-MMU-5676590. NIK-->noncanonical NF-kB signaling.
R-MMU-5684264. MAP3K8 (TPL2)-dependent MAPK1/3 activation.
R-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
F-box/WD repeat-containing protein 1ABy similarityImported
Alternative name(s):
Beta-TrCP protein E3RS-IkappaBImported
Beta-transducin repeat-containing proteinImported
Short name:
Beta-TrCP1 Publication
E3RSIkappaBBy similarity
Short name:
mE3RS-IkappaB1 Publication
F-box and WD repeats protein beta-TrCPBy similarity
HOS1 Publication
Ubiquitin ligase FWD11 PublicationImported
pIkappaB-E3 receptor subunit1 Publication
Gene namesi
Name:BtrcImported
Synonyms:Fbw1, Fbxw1Imported, Fwd1, Kiaa4123
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1338871. Btrc.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: ParkinsonsUK-UCL
  • cytosol Source: Reactome
  • nucleus Source: ParkinsonsUK-UCL
  • SCF ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mutants have normal circadian behavior with normal PER2 expression in the suprachiasmatic nucleus.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 605605F-box/WD repeat-containing protein 1APRO_0000393571Add
BLAST

Proteomic databases

EPDiQ3ULA2.
MaxQBiQ3ULA2.
PaxDbiQ3ULA2.
PRIDEiQ3ULA2.

PTM databases

iPTMnetiQ3ULA2.
PhosphoSiteiQ3ULA2.

Expressioni

Tissue specificityi

Expressed in heart, brain, liver, skeletal muscle and, most strongly, in testis.1 Publication

Gene expression databases

BgeeiQ3ULA2.
GenevisibleiQ3ULA2. MM.

Interactioni

Subunit structurei

Homodimer. Self-associates. Component of the SCF(BTRC) complex, composed of SKP1, CUL1 and BTRC. Direct interaction with SKP1 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 the phosphorylated form of GLI3. Interacts with CLU. Interacts with PER1 (phosphorylated), PER2 (phosphorylated) and PER3. Interacts with phosphorylated ubiquitination substrate CEP68 (By similarity). Interacts with ZC3H12A; the interaction occurs when ZC3H12A is phosphorylated in a IKBKB/IKKB-dependent manner (PubMed:22037600).By similarity8 Publications

GO - Molecular functioni

  • beta-catenin binding Source: BHF-UCL
  • protein phosphorylated amino acid binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi198403. 20 interactions.
IntActiQ3ULA2. 16 interactions.
STRINGi10090.ENSMUSP00000070728.

Structurei

3D structure databases

ProteinModelPortaliQ3ULA2.
SMRiQ3ULA2. Positions 127-581.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini182 – 22847F-boxPROSITE-ProRule annotationAdd
BLAST
Repeati301 – 33838WD 1Sequence analysisAdd
BLAST
Repeati341 – 37838WD 2Sequence analysisAdd
BLAST
Repeati381 – 41838WD 3Sequence analysisAdd
BLAST
Repeati424 – 46138WD 4Sequence analysisAdd
BLAST
Repeati464 – 50340WD 5Sequence analysisAdd
BLAST
Repeati505 – 54137WD 6Sequence analysisAdd
BLAST
Repeati553 – 59038WD 7Sequence analysisAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni128 – 17750Homodimerization domain DBy similarityAdd
BLAST
Regioni190 – 22839Required for down-regulation of SNAI1By 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

eggNOGiKOG0281. Eukaryota.
ENOG410XTA8. LUCA.
GeneTreeiENSGT00760000119106.
HOGENOMiHOG000006638.
HOVERGENiHBG002521.
InParanoidiQ3ULA2.
KOiK03362.
OMAiWIQYLFK.
OrthoDBiEOG76DTS5.
PhylomeDBiQ3ULA2.
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. 6 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. AlignAdd to basket

Isoform 12 Publications (identifier: Q3ULA2-1) [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

        10         20         30         40         50
MDPAEAVLQE KALKFMCSMP RSLWLGCSSL ADSMPSLRCL YNPGTGALTA
60 70 80 90 100
FQNSSEREDC NNGEPPRKII PEKNSLRQTY NSCARLCINQ ETVCLTSTAM
110 120 130 140 150
KTENCVAKAK LANGTSSMIV PKQRKLSASY EKEKELCVKY FEQWSESDQV
160 170 180 190 200
EFVEHLISQM CHYQHGHINS YLKPMLQRDF ITALPARGLD HIAENILSYL
210 220 230 240 250
DAKSLCAAEL VCKEWYRVTS DGMLWKKLIE RMVRTDSLWR GLAERRGWGQ
260 270 280 290 300
YLFKNKPPDE NAPPNSFYRA LYPKIIQDIE TIESNWRCGR HSLQRIHCRS
310 320 330 340 350
ETSKGVYCLQ YDDQKIVSGL RDNTIKIWDK STLECKRILT GHTGSVLCLQ
360 370 380 390 400
YDERVIITGS SDSTVRVWDV NAGEMLNTLI HHCEAVLHLR FNNGMMVTCS
410 420 430 440 450
KDRSIAVWDM ASPTDITLRR VLVGHRAAVN VVDFDDKYIV SASGDRTIKV
460 470 480 490 500
WNTSTCEFVR TLNGHKRGIA CLQYRDRLVV SGSSDNTIRL WDIECGACLR
510 520 530 540 550
VLEGHEELVR CIRFDNKRIV SGAYDGKIKV WDLMAALDPR APAGTLCLRT
560 570 580 590 600
LVEHSGRVFR LQFDEFQIVS SSHDDTILIW DFLNDPAAHA EPPRSPSRTY

TYISR
Length:605
Mass (Da):68,923
Last modified:April 20, 2010 - v2
Checksum:i9E66D94D1EEEFF1B
GO
Isoform 25 Publications (identifier: Q3ULA2-2) [UniParc]FASTAAdd to basket

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

Show »
Length:569
Mass (Da):65,105
Checksum:iBC7D6544815B2296
GO

Sequence cautioni

The sequence BAD90368.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti193 – 1931A → T in AAD41025 (PubMed:10531037).Curated
Sequence conflicti226 – 2261K → E in BAE33798 (PubMed:16141072).Curated
Sequence conflicti297 – 2971H → R in BAE26547 (PubMed:16141072).Curated
Sequence conflicti352 – 3521D → G in AAD04181 (PubMed:9990853).Curated
Sequence conflicti377 – 3771N → D in AAD41025 (PubMed:10531037).Curated
Sequence conflicti380 – 3801I → T in AAD41025 (PubMed:10531037).Curated
Sequence conflicti523 – 5231A → R in AAD41025 (PubMed:10531037).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei17 – 5236Missing in isoform 2. 5 PublicationsVSP_053208Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF099932 mRNA. Translation: AAD08701.1.
AF110396 mRNA. Translation: AAD41025.1.
AF112979 mRNA. Translation: AAD04181.1.
AF081887 mRNA. Translation: AAD17755.1.
AF391190
, AF391178, AF391179, AF391180, AF391181, AF391182, AF391183, AF391184, AF391185, AF391186, AF391187, AF391188, AF391189 Genomic DNA. Translation: AAL40929.1.
AK145624 mRNA. Translation: BAE26547.1.
AK156660 mRNA. Translation: BAE33798.1.
AK220183 mRNA. Translation: BAD90368.1. Different initiation.
CH466534 Genomic DNA. Translation: EDL41951.1.
BC003989 mRNA. Translation: AAH03989.1.
CCDSiCCDS29860.1. [Q3ULA2-1]
CCDS38002.1. [Q3ULA2-2]
RefSeqiNP_001032847.2. NM_001037758.2. [Q3ULA2-1]
NP_001273394.1. NM_001286465.1. [Q3ULA2-1]
NP_001273395.1. NM_001286466.1.
NP_033901.1. NM_009771.3. [Q3ULA2-2]
UniGeneiMm.119717.
Mm.446448.

Genome annotation databases

EnsembliENSMUST00000065601; ENSMUSP00000070728; ENSMUSG00000025217. [Q3ULA2-1]
ENSMUST00000111936; ENSMUSP00000107567; ENSMUSG00000025217. [Q3ULA2-2]
GeneIDi12234.
KEGGimmu:12234.
UCSCiuc008hqx.2. mouse. [Q3ULA2-1]
uc008hqz.2. mouse. [Q3ULA2-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF099932 mRNA. Translation: AAD08701.1.
AF110396 mRNA. Translation: AAD41025.1.
AF112979 mRNA. Translation: AAD04181.1.
AF081887 mRNA. Translation: AAD17755.1.
AF391190
, AF391178, AF391179, AF391180, AF391181, AF391182, AF391183, AF391184, AF391185, AF391186, AF391187, AF391188, AF391189 Genomic DNA. Translation: AAL40929.1.
AK145624 mRNA. Translation: BAE26547.1.
AK156660 mRNA. Translation: BAE33798.1.
AK220183 mRNA. Translation: BAD90368.1. Different initiation.
CH466534 Genomic DNA. Translation: EDL41951.1.
BC003989 mRNA. Translation: AAH03989.1.
CCDSiCCDS29860.1. [Q3ULA2-1]
CCDS38002.1. [Q3ULA2-2]
RefSeqiNP_001032847.2. NM_001037758.2. [Q3ULA2-1]
NP_001273394.1. NM_001286465.1. [Q3ULA2-1]
NP_001273395.1. NM_001286466.1.
NP_033901.1. NM_009771.3. [Q3ULA2-2]
UniGeneiMm.119717.
Mm.446448.

3D structure databases

ProteinModelPortaliQ3ULA2.
SMRiQ3ULA2. Positions 127-581.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198403. 20 interactions.
IntActiQ3ULA2. 16 interactions.
STRINGi10090.ENSMUSP00000070728.

PTM databases

iPTMnetiQ3ULA2.
PhosphoSiteiQ3ULA2.

Proteomic databases

EPDiQ3ULA2.
MaxQBiQ3ULA2.
PaxDbiQ3ULA2.
PRIDEiQ3ULA2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000065601; ENSMUSP00000070728; ENSMUSG00000025217. [Q3ULA2-1]
ENSMUST00000111936; ENSMUSP00000107567; ENSMUSG00000025217. [Q3ULA2-2]
GeneIDi12234.
KEGGimmu:12234.
UCSCiuc008hqx.2. mouse. [Q3ULA2-1]
uc008hqz.2. mouse. [Q3ULA2-2]

Organism-specific databases

CTDi8945.
MGIiMGI:1338871. Btrc.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG0281. Eukaryota.
ENOG410XTA8. LUCA.
GeneTreeiENSGT00760000119106.
HOGENOMiHOG000006638.
HOVERGENiHBG002521.
InParanoidiQ3ULA2.
KOiK03362.
OMAiWIQYLFK.
OrthoDBiEOG76DTS5.
PhylomeDBiQ3ULA2.
TreeFamiTF105679.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-MMU-1169091. Activation of NF-kappaB in B cells.
R-MMU-1170546. Prolactin receptor signaling.
R-MMU-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-MMU-195253. Degradation of beta-catenin by the destruction complex.
R-MMU-202424. Downstream TCR signaling.
R-MMU-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-MMU-2871837. FCERI mediated NF-kB activation.
R-MMU-3769402. Deactivation of the beta-catenin transactivating complex.
R-MMU-400253. Circadian Clock.
R-MMU-508751. Circadian Clock.
R-MMU-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-MMU-5607764. CLEC7A (Dectin-1) signaling.
R-MMU-5610780. Degradation of GLI1 by the proteasome.
R-MMU-5610785. GLI3 is processed to GLI3R by the proteasome.
R-MMU-5676590. NIK-->noncanonical NF-kB signaling.
R-MMU-5684264. MAP3K8 (TPL2)-dependent MAPK1/3 activation.
R-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

PROiQ3ULA2.
SOURCEiSearch...

Gene expression databases

BgeeiQ3ULA2.
GenevisibleiQ3ULA2. MM.

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. 6 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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 2), FUNCTION, PATHWAY, INTERACTION WITH PHOSPHORYLATED NFKBIA.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  3. "Signal-induced ubiquitination of IkappaBalpha by the F-box protein Slimb/beta-TrCP."
    Spencer E., Jiang J., Chen Z.J.
    Genes Dev. 13:284-294(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, PATHWAY, IDENTIFICATION IN A COMPLEX WITH PHOSPHORYLATED NFKBIA; SKP1 AND RELA.
    Tissue: Embryo1 Publication.
  4. "Ubiquitin-dependent degradation of IkappaBalpha is mediated by a ubiquitin ligase Skp1/Cul 1/F-box protein FWD1."
    Hatakeyama S., Kitagawa M., Nakayama K., Shirane M., Matsumoto M., Hattori K., Higashi H., Nakano H., Okumura K., Onoe K., Good R.A., Nakayama K.
    Proc. Natl. Acad. Sci. U.S.A. 96:3859-3863(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, PATHWAY, IDENTIFICATION IN A COMPLEX WITH PHOSPHORYLATED NFKBIA; SKP1 AND CUL1.
  5. "Characterization of a mouse gene (Fbxw6) that encodes a homologue of Caenorhabditis elegans SEL-10."
    Maruyama S., Hatakeyama S., Nakayama K., Ishida N., Kawakami K., Nakayama K.
    Genomics 78:214-222(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION IN A COMPLEX WITH SKP1 AND CUL1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: 129/SvJ1 Publication.
  6. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 53-605 (ISOFORMS 1/2).
    Strain: C57BL/6JImported and NODImported.
    Tissue: BlastocystImported and SpleenImported.
  7. "Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: BrainImported.
  8. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: Czech IIImported.
    Tissue: Mammary tumorImported.
  10. "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: INTERACTION WITH PER3.
  11. "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, INTERACTION WITH GLI3.
  12. "The role of {beta}-TrCP1 and {beta}-TrCP2 in circadian rhythm generation by mediating degradation of clock protein PER2."
    Ohsaki K., Oishi K., Kozono Y., Nakayama K., Nakayama K.I., Ishida N.
    J. Biochem. 144:609-618(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CIRCADIAN RHYTHMS, INTERACTION WITH PER2, DISRUPTION PHENOTYPE.
  13. "The IkappaB kinase complex regulates the stability of cytokine-encoding mRNA induced by TLR-IL-1R by controlling degradation of regnase-1."
    Iwasaki H., Takeuchi O., Teraguchi S., Matsushita K., Uehata T., Kuniyoshi K., Satoh T., Saitoh T., Matsushita M., Standley D.M., Akira S.
    Nat. Immunol. 12:1167-1175(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZC3H12A.

Entry informationi

Entry nameiFBW1A_MOUSE
AccessioniPrimary (citable) accession number: Q3ULA2
Secondary accession number(s): Q3U0Q4
, Q571K6, Q9QUI5, Q9R1G7, Q9Z159
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: April 20, 2010
Last modified: June 8, 2016
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

PubMed:10531037 wrongly lists the species as human.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.