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Q9Y297

- FBW1A_HUMAN

UniProt

Q9Y297 - FBW1A_HUMAN

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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

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. 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
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

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

Enzyme and pathway databases

ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
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_206597. Degradation of GLI2 by the proteasome.
REACT_22442. Interleukin-1 signaling.
REACT_231645. GLI3 is processed to GLI3R by the proteasome.
REACT_24941. Circadian Clock.
REACT_267605. Degradation of GLI1 by the proteasome.
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-KW
  3. SCF ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

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

BgeeiQ9Y297.
CleanExiHS_BTRC.
ExpressionAtlasiQ9Y297. baseline and differential.
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. 176 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 – 14113Combined sources
Helixi146 – 15813Combined sources
Helixi162 – 17211Combined sources
Helixi173 – 1753Combined sources
Helixi180 – 1834Combined sources
Helixi185 – 1873Combined sources
Helixi190 – 1978Combined sources
Helixi202 – 21110Combined sources
Helixi213 – 2219Combined sources
Helixi224 – 23310Combined sources
Helixi237 – 2448Combined sources
Beta strandi245 – 2473Combined sources
Helixi248 – 2514Combined sources
Helixi266 – 28520Combined sources
Turni286 – 2883Combined sources
Beta strandi306 – 3105Combined sources
Beta strandi313 – 32311Combined sources
Beta strandi325 – 3328Combined sources
Beta strandi335 – 3395Combined sources
Beta strandi346 – 3505Combined sources
Beta strandi353 – 3608Combined sources
Beta strandi365 – 3728Combined sources
Beta strandi375 – 3795Combined sources
Beta strandi386 – 3905Combined sources
Beta strandi395 – 4006Combined sources
Beta strandi405 – 4095Combined sources
Beta strandi411 – 4144Combined sources
Beta strandi417 – 4226Combined sources
Beta strandi429 – 4357Combined sources
Beta strandi438 – 4436Combined sources
Beta strandi446 – 4527Combined sources
Turni453 – 4553Combined sources
Beta strandi458 – 4636Combined sources
Beta strandi469 – 4757Combined sources
Beta strandi478 – 4836Combined sources
Beta strandi488 – 4925Combined sources
Turni493 – 4953Combined sources
Beta strandi498 – 5025Combined sources
Beta strandi509 – 5135Combined sources
Beta strandi516 – 5238Combined sources
Beta strandi528 – 5325Combined sources
Helixi533 – 5364Combined sources
Turni543 – 5464Combined sources
Beta strandi547 – 5515Combined sources
Beta strandi561 – 5633Combined sources
Beta strandi568 – 5703Combined sources
Beta strandi573 – 5808Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000119106.
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

        10         20         30         40         50
MDPAEAVLQE KALKFMCSMP RSLWLGCSSL ADSMPSLRCL YNPGTGALTA
60 70 80 90 100
FQNSSEREDC NNGEPPRKII PEKNSLRQTY NSCARLCLNQ ETVCLASTAM
110 120 130 140 150
KTENCVAKTK 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
YLFKNKPPDG NAPPNSFYRA LYPKIIQDIE TIESNWRCGR HSLQRIHCRS
310 320 330 340 350
ETSKGVYCLQ YDDQKIVSGL RDNTIKIWDK NTLECKRILT GHTGSVLCLQ
360 370 380 390 400
YDERVIITGS SDSTVRVWDV NTGEMLNTLI 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 WDLVAALDPR APAGTLCLRT
560 570 580 590 600
LVEHSGRVFR LQFDEFQIVS SSHDDTILIW DFLNDPAAQA EPPRSPSRTY

TYISR
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 176 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.
GeneTreei ENSGT00760000119106.
HOGENOMi HOG000006638.
HOVERGENi HBG002521.
InParanoidi Q9Y297.
KOi K03362.
OMAi NAYLKPM.
OrthoDBi EOG76DTS5.
PhylomeDBi Q9Y297.
TreeFami TF105679.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_11063. Degradation of beta-catenin by the destruction complex.
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_206597. Degradation of GLI2 by the proteasome.
REACT_22442. Interleukin-1 signaling.
REACT_231645. GLI3 is processed to GLI3R by the proteasome.
REACT_24941. Circadian Clock.
REACT_267605. Degradation of GLI1 by the proteasome.
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

Bgeei Q9Y297.
CleanExi HS_BTRC.
ExpressionAtlasi Q9Y297. baseline and differential.
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

« 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 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: November 26, 2014
This is version 153 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