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Protein

F-box/WD repeat-containing protein 11

Gene

FBXW11

Organism
Homo sapiens (Human)
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. 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. 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
Complete GO annotation...

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 Componenti: 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
Complete GO annotation...

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

BgeeiQ9UKB1.
CleanExiHS_FBXW11.
ExpressionAtlasiQ9UKB1. baseline and differential.
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. 150 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.
GeneTreeiENSGT00760000119106.
HOGENOMiHOG000006638.
HOVERGENiHBG002521.
InParanoidiQ9UKB1.
KOiK03362.
OMAiSTRAHNQ.
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. AlignAdd to basket

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

        10         20         30         40         50
MEPDSVIEDK TIELMCSVPR SLWLGCANLV ESMCALSCLQ SMPSVRCLQI
60 70 80 90 100
SNGTSSVIVS RKRPSEGNYQ KEKDLCIKYF DQWSESDQVE FVEHLISRMC
110 120 130 140 150
HYQHGHINSY LKPMLQRDFI TALPEQGLDH IAENILSYLD ARSLCAAELV
160 170 180 190 200
CKEWQRVISE GMLWKKLIER MVRTDPLWKG LSERRGWDQY LFKNRPTDGP
210 220 230 240 250
PNSFYRSLYP KIIQDIETIE SNWRCGRHNL QRIQCRSENS KGVYCLQYDD
260 270 280 290 300
EKIISGLRDN SIKIWDKTSL ECLKVLTGHT GSVLCLQYDE RVIVTGSSDS
310 320 330 340 350
TVRVWDVNTG EVLNTLIHHN EAVLHLRFSN GLMVTCSKDR SIAVWDMASA
360 370 380 390 400
TDITLRRVLV GHRAAVNVVD FDDKYIVSAS GDRTIKVWST STCEFVRTLN
410 420 430 440 450
GHKRGIACLQ YRDRLVVSGS SDNTIRLWDI ECGACLRVLE GHEELVRCIR
460 470 480 490 500
FDNKRIVSGA YDGKIKVWDL QAALDPRAPA STLCLRTLVE HSGRVFRLQF
510 520 530 540
DEFQIISSSH DDTILIWDFL NVPPSAQNET RSPSRTYTYI SR
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.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi116887. 150 interactions.
DIPiDIP-27593N.
IntActiQ9UKB1. 38 interactions.
MINTiMINT-120522.
STRINGi9606.ENSP00000265094.

PTM databases

PhosphoSiteiQ9UKB1.

Polymorphism databases

DMDMi13124267.

Proteomic databases

MaxQBiQ9UKB1.
PaxDbiQ9UKB1.
PRIDEiQ9UKB1.

Protocols and materials databases

DNASUi23291.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi23291.
GeneCardsiGC05M171288.
HGNCiHGNC:13607. FBXW11.
MIMi605651. gene.
neXtProtiNX_Q9UKB1.
PharmGKBiPA28050.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00760000119106.
HOGENOMiHOG000006638.
HOVERGENiHBG002521.
InParanoidiQ9UKB1.
KOiK03362.
OMAiSTRAHNQ.
OrthoDBiEOG76DTS5.
PhylomeDBiQ9UKB1.
TreeFamiTF105679.

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.

Miscellaneous databases

ChiTaRSiFBXW11. human.
GeneWikiiFBXW11.
GenomeRNAii23291.
NextBioi45108.
PROiQ9UKB1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UKB1.
CleanExiHS_FBXW11.
ExpressionAtlasiQ9UKB1. baseline and differential.
GenevestigatoriQ9UKB1.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1999) [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(1997) [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(2003) [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(2003) [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(1998) [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(1998) [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(1999) [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(2002) [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(1998) [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(2005) [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(1999) [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(2001) [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(2002) [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(2004) [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(2007) [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(2008) [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(2009) [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(2009) [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: February 4, 2015
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

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

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 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.