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Q8CHQ0 (FBX4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
F-box only protein 4
Gene names
Name:Fbxo4
Synonyms:Fbx4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length385 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 that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes ubiquitination of CCND1 and its subsequent proteasomal degradation. Recognizes TERF1 and promotes its ubiquitination together with UBE2D1 By similarity. Ref.4 Ref.5 Ref.7

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Homodimer. Directly interacts with SKP1 and CUL1. Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complex SCF(FBXO4) formed of CUL1, SKP1, RBX1 and FBXO4. Interacts with TERF1; this interaction is prevented in the presence of GNL3L. Identified in a complex with CRYAB and CCND1 By similarity. Ref.4 Ref.6

Subcellular location

Cytoplasm Ref.4.

Post-translational modification

Phosphorylation at Ser-11 varies during the cell cycle. It is low in resting cells and high in the S phase and the G2/M phase of the cell cycle. Phosphorylation is decreased during late G1 phase. Phosphorylation at Ser-11 is important for homodimerization and for optimal ubiquitin ligase activity towards CCND1.

Sequence similarities

Contains 1 F-box domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

YwhaeP622592EBI-3895153,EBI-356480

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 385385F-box only protein 4
PRO_0000119880

Regions

Domain54 – 10047F-box

Amino acid modifications

Modified residue111Phosphoserine Ref.5

Experimental info

Sequence conflict911I → V in AAH40086. Ref.2
Sequence conflict3471H → R in AAH40086. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8CHQ0 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 36D78194EAF9EE95

FASTA38543,777
        10         20         30         40         50         60 
MAGSEPRGAG SPPPASDWGR LEAAILSGWR TFWYSVAKER ATPTASRKEA AEETSALTRL 

        70         80         90        100        110        120 
PVDVQLYILS FLSPHDLCQL GSTDHYWNKT IRDPILWRYF LLRDLPSWSS VDWKSLPDLE 

       130        140        150        160        170        180 
ILKKPISEVT DSTCLDYMEV YKMCCPYTRR ALKASRPMYG VVTSFLHSLI IQNEPRFAMF 

       190        200        210        220        230        240 
GPGLEELNTS LVLSLMSSED LCPTAGLPHR QIDGIGSGVN FQLNNQQKFN ILILYSTTRK 

       250        260        270        280        290        300 
ERDRAREEHT STVNKMFSLQ SEGDEQQGSR YSVIPQIQKV CEVVDGFIYV ANAEAHRRHE 

       310        320        330        340        350        360 
WQDEFSRIMA MTDPAFGSSG RPMLVLSCIS QADVKRMPCF YLAHELHLSL LNHPWMVQDT 

       370        380 
EAETLTGFLN GIEWILEEVE SKRAK 

« Hide

References

« Hide 'large scale' references
[1]"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.
[2]"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].
Strain: Czech II.
Tissue: Mammary tumor.
[3]"Osteoblasts express the mouse F-box protein mFbx4."
Kopecky B.S., Varga F., Klaushofer K.
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 245-385.
Tissue: Osteoblast.
[4]"Phosphorylation-dependent ubiquitination of cyclin D1 by the SCF(FBX4-alphaB crystallin) complex."
Lin D.I., Barbash O., Kumar K.G., Weber J.D., Harper J.W., Klein-Szanto A.J., Rustgi A., Fuchs S.Y., Diehl J.A.
Mol. Cell 24:355-366(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A SCF UBIQUITIN-PROTEIN LIGASE COMPLEX, SUBUNIT, SUBCELLULAR LOCATION.
[5]"Mutations in Fbx4 inhibit dimerization of the SCF(Fbx4) ligase and contribute to cyclin D1 overexpression in human cancer."
Barbash O., Zamfirova P., Lin D.I., Chen X., Yang K., Nakagawa H., Lu F., Rustgi A.K., Diehl J.A.
Cancer Cell 14:68-78(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT SER-11.
[6]"GNL3L stabilizes the TRF1 complex and promotes mitotic transition."
Zhu Q., Meng L., Hsu J.K., Lin T., Teishima J., Tsai R.Y.
J. Cell Biol. 185:827-839(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TERF1.
[7]"Lysine 269 is essential for cyclin D1 ubiquitylation by the SCF(Fbx4/alphaB-crystallin) ligase and subsequent proteasome-dependent degradation."
Barbash O., Egan E., Pontano L.L., Kosak J., Diehl J.A.
Oncogene 28:4317-4325(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC137902 Genomic DNA. No translation available.
BC040086 mRNA. Translation: AAH40086.1.
AJ300659 mRNA. Translation: CAC36404.1.
RefSeqNP_598860.2. NM_134099.2.
UniGeneMm.234191.

3D structure databases

ProteinModelPortalQ8CHQ0.
SMRQ8CHQ0. Positions 55-382.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid222983. 3 interactions.
IntActQ8CHQ0. 1 interaction.
STRING10090.ENSMUSP00000022791.

PTM databases

PhosphoSiteQ8CHQ0.

Proteomic databases

PaxDbQ8CHQ0.
PRIDEQ8CHQ0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022791; ENSMUSP00000022791; ENSMUSG00000022184.
GeneID106052.
KEGGmmu:106052.
UCSCuc007vcf.2. mouse.

Organism-specific databases

CTD26272.
MGIMGI:2146220. Fbxo4.

Phylogenomic databases

eggNOGNOG39270.
GeneTreeENSGT00390000014416.
HOGENOMHOG000112550.
HOVERGENHBG051585.
InParanoidQ8CHQ0.
KOK10291.
OMAHEWQDEF.
OrthoDBEOG7GBG00.
TreeFamTF331105.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

BgeeQ8CHQ0.
CleanExMM_FBXO4.
GenevestigatorQ8CHQ0.

Family and domain databases

InterProIPR001810. F-box_dom.
[Graphical view]
SMARTSM00256. FBOX. 1 hit.
[Graphical view]
SUPFAMSSF81383. SSF81383. 1 hit.
PROSITEPS50181. FBOX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio358036.
PROQ8CHQ0.
SOURCESearch...

Entry information

Entry nameFBX4_MOUSE
AccessionPrimary (citable) accession number: Q8CHQ0
Secondary accession number(s): E9QPM9, Q99JG8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 82 of the entry and version 2 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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