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Q5SRY7 (FBW1B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length542 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably recognizes and binds to phosphorylated target proteins. SCF(FBXW11) mediates the ubiquitination of CTNNB1 and participates in Wnt signaling. Mediates also the ubiquitination of IFNAR1 and targets phosphorylation-dependent degradation of beta-catenin. Involved in the oxidative stress-induced ubiquitin-mediated decrease of RCAN1. Promotes the degradation of CDC25A induced by ionizing radiation in cells progressing through S phase and thus may function in the intra-S-phase checkpoint By similarity. Involved in the ubiquitination of phosphorylated NFKBIA, which degradation frees the associated NFKB1 to translocate into the nucleus and to activate transcription. Has an essential role in the control of the clock-dependent transcription via degradation of PER1 and phosphorylated PER2. Ref.1 Ref.6

Subunit structure

Self-associates. Interacts with TRIM21 By similarity. Component of the SCF(FBXW11) complex formed of CUL1, SKP1, RBX1 and a FBXW11 dimer By similarity. Interacts with BTRC, BST2, PER1 and RCAN1 By similarity. Interacts with phosphorylated ubiquitination substrates CTNNB1, IFNAR1; the interaction requires the phosphorylation of the two serine residues in the substrates' destruction motif D-S-G-X(2,3,4)-S By similarity. Interacts with SKP1 and phosphorylated ubiquitination substrates NFKBIA and PER2. Ref.1 Ref.6

Subcellular location

Cytoplasm. Nucleus Ref.6.

Induction

Expression is negatively regulated by Wnt/beta-catenin pathway. Ref.5

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 AAK72095.1 differs from that shown. Reason: Frameshift at position 349.

Ontologies

Keywords
   Biological processBiological rhythms
Cell cycle
Ubl conjugation pathway
Wnt signaling pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
WD repeat
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype Ref.1. Source: UniProtKB

Wnt 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 mutant phenotype Ref.1. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

positive regulation of circadian rhythm

Inferred from mutant phenotype Ref.6. Source: UniProtKB

positive regulation of proteolysis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.6. Source: UniProtKB

protein dephosphorylation

Inferred from direct assay Ref.6. Source: UniProtKB

protein destabilization

Inferred from sequence or structural similarity. Source: UniProtKB

protein polyubiquitination

Inferred from direct assay Ref.1. Source: UniProtKB

rhythmic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentSCF ubiquitin ligase complex

Inferred from direct assay Ref.1. Source: UniProtKB

centrosome

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay Ref.1. Source: UniProtKB

cytosol

Inferred from direct assay Ref.6. Source: UniProtKB

nucleus

Inferred from direct assay Ref.6. Source: UniProtKB

   Molecular_functionubiquitin-protein ligase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5SRY7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q5SRY7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     49-49: Q → QNTSVMEDQNEDESPKKSALWQ
Isoform 3 (identifier: Q5SRY7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     16-48: CSVPRSLWLGCANLVESMCALSCLQSMPSVRCL → NTSVMEDQNEDESPKKSALW
Isoform 4 (identifier: Q5SRY7-4)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 542542F-box/WD repeat-containing protein 11
PRO_0000396126

Regions

Domain121 – 16747F-box
Repeat238 – 27538WD 1
Repeat278 – 31538WD 2
Repeat318 – 35538WD 3
Repeat361 – 39838WD 4
Repeat401 – 44040WD 5
Repeat442 – 47837WD 6
Repeat490 – 52738WD 7
Region67 – 11650Homodimerization domain D By similarity

Natural variations

Alternative sequence16 – 4934Missing in isoform 4.
VSP_039579
Alternative sequence16 – 4833CSVPR…SVRCL → NTSVMEDQNEDESPKKSALW in isoform 3.
VSP_039580
Alternative sequence491Q → QNTSVMEDQNEDESPKKSAL WQ in isoform 2.
VSP_039581

Experimental info

Sequence conflict2191I → V in BAE38644. Ref.2
Sequence conflict5341S → F in AAK72095. Ref.1

Sequences

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

Last modified December 21, 2004. Version 1.
Checksum: D95A78A6977B828A

FASTA54262,063
        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 DKIISGLRDN SIKIWDKSSL 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 

« Hide

Isoform 2 [UniParc].

Checksum: 74D07E6BB850ABED
Show »

FASTA56364,481
Isoform 3 [UniParc].

Checksum: D2F382457FD80080
Show »

FASTA52960,813
Isoform 4 [UniParc].

Checksum: A048E9FA4A78C550
Show »

FASTA50858,394

References

« Hide 'large scale' references
[1]"Mouse homologue of HOS (mHOS) is overexpressed in skin tumors and implicated in constitutive activation of NF-kappaB."
Bhatia N., Herter J.R., Slaga T.J., Fuchs S.Y., Spiegelman V.S.
Oncogene 21:1501-1509(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH SKP1 AND NFKBIA.
Strain: FVB/N.
[2]"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. expand/collapse author list , 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] (ISOFORMS 1; 3 AND 4).
Strain: C57BL/6J.
Tissue: Kidney, Mammary gland, Osteoclast, Sympathetic ganglion and Thymus.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"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: FVB/N.
Tissue: Kidney.
[5]"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.
[6]"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, INTERACTION WITH PER2, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY038079 mRNA. Translation: AAK72095.1. Frameshift.
AK041532 mRNA. Translation: BAC30975.1.
AK149139 mRNA. Translation: BAE28749.1.
AK152181 mRNA. Translation: BAE31012.1.
AK160086 mRNA. Translation: BAE35617.1.
AK166226 mRNA. Translation: BAE38644.1.
AK168667 mRNA. Translation: BAE40519.1.
AL669844, AL669951 Genomic DNA. Translation: CAI25519.1.
AL669844, AL669951 Genomic DNA. Translation: CAI25520.1.
AL669951, AL669844 Genomic DNA. Translation: CAI26097.1.
AL669951, AL669844 Genomic DNA. Translation: CAI26098.1.
BC034261 mRNA. Translation: AAH34261.1.
RefSeqNP_001258276.1. NM_001271347.1.
NP_001258277.1. NM_001271348.1.
NP_001258278.1. NM_001271349.1.
NP_598776.1. NM_134015.3.
UniGeneMm.28017.
Mm.491286.

3D structure databases

ProteinModelPortalQ5SRY7.
SMRQ5SRY7. Positions 67-518.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid222123. 4 interactions.
DIPDIP-59921N.
STRING10090.ENSMUSP00000075721.

PTM databases

PhosphoSiteQ5SRY7.

Proteomic databases

PaxDbQ5SRY7.
PRIDEQ5SRY7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000076383; ENSMUSP00000075721; ENSMUSG00000020271. [Q5SRY7-2]
ENSMUST00000093205; ENSMUSP00000090893; ENSMUSG00000020271. [Q5SRY7-1]
ENSMUST00000109366; ENSMUSP00000104991; ENSMUSG00000020271. [Q5SRY7-3]
GeneID103583.
KEGGmmu:103583.
UCSCuc007ijx.1. mouse. [Q5SRY7-2]
uc007ijy.1. mouse. [Q5SRY7-3]
uc007ijz.1. mouse. [Q5SRY7-1]
uc007ika.1. mouse. [Q5SRY7-4]

Organism-specific databases

CTD23291.
MGIMGI:2144023. Fbxw11.

Phylogenomic databases

eggNOGCOG2319.
GeneTreeENSGT00710000106459.
HOGENOMHOG000006638.
HOVERGENHBG002521.
InParanoidQ923H0.
KOK03362.
OMAFDQWSEA.
OrthoDBEOG76DTS5.
TreeFamTF105679.

Gene expression databases

ArrayExpressQ5SRY7.
BgeeQ5SRY7.
GenevestigatorQ5SRY7.

Family and domain databases

Gene3D2.130.10.10. 2 hits.
InterProIPR021977. Beta-TrCP_D.
IPR001810. F-box_dom.
IPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF12125. Beta-TrCP_D. 1 hit.
PF00400. WD40. 7 hits.
[Graphical view]
PRINTSPR00320. GPROTEINBRPT.
SMARTSM01028. Beta-TrCP_D. 1 hit.
SM00256. FBOX. 1 hit.
SM00320. WD40. 7 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
SSF81383. SSF81383. 1 hit.
PROSITEPS50181. FBOX. 1 hit.
PS00678. WD_REPEATS_1. 5 hits.
PS50082. WD_REPEATS_2. 7 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFBXW11. mouse.
NextBio356027.
PROQ5SRY7.
SOURCESearch...

Entry information

Entry nameFBW1B_MOUSE
AccessionPrimary (citable) accession number: Q5SRY7
Secondary accession number(s): Q3TGM9 expand/collapse secondary AC list , Q3TLZ8, Q8BY90, Q8K022, Q923H0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: December 21, 2004
Last modified: April 16, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot