Q9UKB1 (FBW1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	FBXW11
Synonyms:	BTRCP2, FBW1B, FBXW1B, KIAA0696

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	542 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Probably recognizes and binds to phosphorylated target proteins. SCF(FBXW11) mediates the ubiquitination of 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. Targets phosphorylation-dependent degradation of beta-catenin. 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 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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19
Subunit structure	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 substrate PER2 By similarity. Interacts with phosphorylated ubiquitination substrates CTNNB1, NFKBIA, IFNAR1; 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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Induction	Expression is negatively regulated by Wnt/beta-catenin pathway. Ref.13
Domain	The N-terminal D domain mediates homodimerization By similarity.
Sequence similarities	Contains 1 F-box domain. Contains 7 WD repeats.
Sequence caution	The sequence BAA31671.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Biological rhythms Cell cycle Ubl conjugation pathway Wnt signaling pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat WD repeat
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay Ref.18. Source: UniProtKB Wnt receptor signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW cell cycle Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of NF-kappaB import into nucleus Inferred from electronic annotation. Source: Compara negative regulation of transcription, DNA-dependent Inferred from mutant phenotype Ref.19. 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-dependent Inferred from sequence or structural similarity. 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 direct assay Ref.18. Source: UniProtKB rhythmic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	SCF ubiquitin ligase complex Inferred from direct assay Ref.11Ref.18. Source: UniProtKB centrosome Inferred from direct assay PubMed 21399614. Source: UniProtKB cytosol Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ubiquitin-protein ligase activity Inferred from direct assay Ref.18. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AXIN1	O15169	4	EBI-355189,EBI-710484
CTNNB1	P35222	2	EBI-355189,EBI-491549
MDM2	Q00987	4	EBI-355189,EBI-389668
SKP1	P63208	4	EBI-355189,EBI-307486
WEE1	P30291	2	EBI-355189,EBI-914695

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform C (identifier: Q9UKB1-1)

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 A (identifier: Q9UKB1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     16-49: Missing.

Isoform B (identifier: Q9UKB1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     16-48: CSVPRSLWLGCANLVESMCALSCLQSMPSVRCL → NTSVMEDQNEDESPKKNTLW

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 542	542	F-box/WD repeat-containing protein 11		PRO_0000050981
Regions
	Domain	129 – 167	39	F-box
	Repeat	238 – 275	38	WD 1
	Repeat	278 – 315	38	WD 2
	Repeat	318 – 355	38	WD 3
	Repeat	361 – 398	38	WD 4
	Repeat	401 – 440	40	WD 5
	Repeat	442 – 478	37	WD 6
	Repeat	490 – 527	38	WD 7
	Region	67 – 116	50	Homodimerization domain D By similarity
Natural variations
	Alternative sequence	16 – 49	34	Missing in isoform A.		VSP_006765
	Alternative sequence	16 – 48	33	CSVPR…SVRCL → NTSVMEDQNEDESPKKNTLW in isoform B.		VSP_006766

Sequences

	Sequence		Length	Mass (Da)
	Isoform C [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 7CD40087EFAA5C8A	FASTA	542	62,091
	10 20 30 40 50 60 MEPDSVIEDK TIELMCSVPR SLWLGCANLV ESMCALSCLQ SMPSVRCLQI SNGTSSVIVS 70 80 90 100 110 120 RKRPSEGNYQ KEKDLCIKYF DQWSESDQVE FVEHLISRMC HYQHGHINSY LKPMLQRDFI 130 140 150 160 170 180 TALPEQGLDH IAENILSYLD ARSLCAAELV CKEWQRVISE GMLWKKLIER MVRTDPLWKG 190 200 210 220 230 240 LSERRGWDQY LFKNRPTDGP PNSFYRSLYP KIIQDIETIE SNWRCGRHNL QRIQCRSENS 250 260 270 280 290 300 KGVYCLQYDD EKIISGLRDN SIKIWDKTSL ECLKVLTGHT GSVLCLQYDE RVIVTGSSDS 310 320 330 340 350 360 TVRVWDVNTG EVLNTLIHHN EAVLHLRFSN GLMVTCSKDR SIAVWDMASA TDITLRRVLV 370 380 390 400 410 420 GHRAAVNVVD FDDKYIVSAS GDRTIKVWST STCEFVRTLN GHKRGIACLQ YRDRLVVSGS 430 440 450 460 470 480 SDNTIRLWDI ECGACLRVLE GHEELVRCIR FDNKRIVSGA YDGKIKVWDL QAALDPRAPA 490 500 510 520 530 540 STLCLRTLVE HSGRVFRLQF DEFQIISSSH DDTILIWDFL NVPPSAQNET RSPSRTYTYI SR
	Isoform A [UniParc]. Checksum: 05C691DB32A91B50	FASTA	508	58,422
	10 20 30 40 50 60 MEPDSVIEDK TIELMISNGT SSVIVSRKRP SEGNYQKEKD LCIKYFDQWS ESDQVEFVEH 70 80 90 100 110 120 LISRMCHYQH GHINSYLKPM LQRDFITALP EQGLDHIAEN ILSYLDARSL CAAELVCKEW 130 140 150 160 170 180 QRVISEGMLW KKLIERMVRT DPLWKGLSER RGWDQYLFKN RPTDGPPNSF YRSLYPKIIQ 190 200 210 220 230 240 DIETIESNWR CGRHNLQRIQ CRSENSKGVY CLQYDDEKII SGLRDNSIKI WDKTSLECLK 250 260 270 280 290 300 VLTGHTGSVL CLQYDERVIV TGSSDSTVRV WDVNTGEVLN TLIHHNEAVL HLRFSNGLMV 310 320 330 340 350 360 TCSKDRSIAV WDMASATDIT LRRVLVGHRA AVNVVDFDDK YIVSASGDRT IKVWSTSTCE 370 380 390 400 410 420 FVRTLNGHKR GIACLQYRDR LVVSGSSDNT IRLWDIECGA CLRVLEGHEE LVRCIRFDNK 430 440 450 460 470 480 RIVSGAYDGK IKVWDLQAAL DPRAPASTLC LRTLVEHSGR VFRLQFDEFQ IISSSHDDTI 490 500 LIWDFLNVPP SAQNETRSPS RTYTYISR
	Isoform B [UniParc]. Checksum: 53D181B789313D0E	FASTA	529	60,898
	10 20 30 40 50 60 MEPDSVIEDK TIELMNTSVM EDQNEDESPK KNTLWQISNG TSSVIVSRKR PSEGNYQKEK 70 80 90 100 110 120 DLCIKYFDQW SESDQVEFVE HLISRMCHYQ HGHINSYLKP MLQRDFITAL PEQGLDHIAE 130 140 150 160 170 180 NILSYLDARS LCAAELVCKE WQRVISEGML WKKLIERMVR TDPLWKGLSE RRGWDQYLFK 190 200 210 220 230 240 NRPTDGPPNS FYRSLYPKII QDIETIESNW RCGRHNLQRI QCRSENSKGV YCLQYDDEKI 250 260 270 280 290 300 ISGLRDNSIK IWDKTSLECL KVLTGHTGSV LCLQYDERVI VTGSSDSTVR VWDVNTGEVL 310 320 330 340 350 360 NTLIHHNEAV LHLRFSNGLM VTCSKDRSIA VWDMASATDI TLRRVLVGHR AAVNVVDFDD 370 380 390 400 410 420 KYIVSASGDR TIKVWSTSTC EFVRTLNGHK RGIACLQYRD RLVVSGSSDN TIRLWDIECG 430 440 450 460 470 480 ACLRVLEGHE ELVRCIRFDN KRIVSGAYDG KIKVWDLQAA LDPRAPASTL CLRTLVEHSG 490 500 510 520 RVFRLQFDEF QIISSSHDDT ILIWDFLNVP PSAQNETRSP SRTYTYISR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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].
[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(2000) [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(1998) [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(2004) [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(2004) [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(1999) [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(1999) [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(2000) [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(2003) [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(1999) [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(2006) [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(2000) [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(2002) [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(2003) [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(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PER1.
[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(2008) [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(2009) [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(2010) [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(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH USP47.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00301283. IPI00306671. IPI00328796.
RefSeq	NP_036432.2. NM_012300.2. NP_387448.2. NM_033644.2. NP_387449.2. NM_033645.2.
UniGene	Hs.484138.
3D structure databases
ProteinModelPortal	Q9UKB1.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-27593N.
IntAct	Q9UKB1. 30 interactions.
MINT	MINT-120522.
STRING	9606.ENSP00000265094.
PTM databases
PhosphoSite	Q9UKB1.
Polymorphism databases
DMDM	13124267.
Proteomic databases
PaxDb	Q9UKB1.
PRIDE	Q9UKB1.
Protocols and materials databases
DNASU	23291.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000265094; ENSP00000265094; ENSG00000072803. ENST00000296933; ENSP00000296933; ENSG00000072803. ENST00000393802; ENSP00000377391; ENSG00000072803.
GeneID	23291.
KEGG	hsa:23291.
UCSC	uc003mbl.1. human. uc003mbm.1. human. uc003mbn.1. human.
Organism-specific databases
CTD	23291.
GeneCards	GC05M171288.
HGNC	HGNC:13607. FBXW11.
MIM	605651. gene.
neXtProt	NX_Q9UKB1.
PharmGKB	PA28050.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2319.
HOGENOM	HOG000006638.
HOVERGEN	HBG002521.
InParanoid	Q9UKB1.
KO	K03362.
OMA	FDQWSEA.
OrthoDB	EOG4F1X2M.
PhylomeDB	Q9UKB1.
Enzyme and pathway databases
Pathway_Interaction_DB	nfkappabalternativepathway. Alternative NF-kappaB pathway. nfkappabatypicalpathway. Atypical NF-kappaB pathway. nfkappabcanonicalpathway. Canonical NF-kappaB pathway. wnt_canonical_pathway. Canonical Wnt signaling pathway. hedgehog_glipathway. Hedgehog signaling events mediated by Gli proteins. ps1pathway. Presenilin action in Notch and Wnt signaling. hdac_classi_pathway. Signaling events mediated by HDAC Class I.
Reactome	REACT_6900. Immune System.
Gene expression databases
ArrayExpress	Q9UKB1.
Bgee	Q9UKB1.
CleanEx	HS_FBXW11.
Genevestigator	Q9UKB1.
GermOnline	ENSG00000072803. Homo sapiens.
Family and domain databases
Gene3D	2.130.10.10. 2 hits.
InterPro	IPR021977. Beta-TrCP_D. IPR001810. F-box_dom_cyclin-like. 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]
Pfam	PF12125. Beta-TrCP_D. 1 hit. PF00400. WD40. 7 hits. [Graphical view]
PRINTS	PR00320. GPROTEINBRPT.
SMART	SM01028. Beta-TrCP_D. 1 hit. SM00256. FBOX. 1 hit. SM00320. WD40. 7 hits. [Graphical view]
SUPFAM	SSF81383. F-box_dom_Skp2-like. 1 hit. SSF50978. WD40_like. 1 hit.
PROSITE	PS50181. FBOX. 1 hit. PS00678. WD_REPEATS_1. 5 hits. PS50082. WD_REPEATS_2. 7 hits. PS50294. WD_REPEATS_REGION. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	23291.
NextBio	45108.
SOURCE	Search...

Entry information

Entry name

FBW1B_HUMAN

Accession

Primary (citable) accession number: Q9UKB1
Secondary accession number(s): B2RC98 , Q9P2S8, Q9P2S9, Q9Y4C6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 133 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.