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Protein

F-box only protein 4

Gene

Fbxo4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 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).By similarity

Pathwayi

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_275351. Association of TriC/CCT with target proteins during biosynthesis.
REACT_343568. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
F-box only protein 4
Gene namesi
Name:Fbxo4
Synonyms:Fbx4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:2146220. Fbxo4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 385385F-box only protein 4PRO_0000119880Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei11 – 111Phosphoserine1 Publication

Post-translational modificationi

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 CCND1.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8CHQ0.
PaxDbiQ8CHQ0.
PRIDEiQ8CHQ0.

PTM databases

PhosphoSiteiQ8CHQ0.

Expressioni

Gene expression databases

BgeeiQ8CHQ0.
CleanExiMM_FBXO4.
GenevestigatoriQ8CHQ0.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
YwhaeP622592EBI-3895153,EBI-356480

Protein-protein interaction databases

BioGridi222983. 3 interactions.
IntActiQ8CHQ0. 1 interaction.
STRINGi10090.ENSMUSP00000022791.

Structurei

3D structure databases

ProteinModelPortaliQ8CHQ0.
SMRiQ8CHQ0. Positions 55-382.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini54 – 10047F-boxPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 F-box domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG39270.
GeneTreeiENSGT00390000014416.
HOGENOMiHOG000112550.
HOVERGENiHBG051585.
InParanoidiQ8CHQ0.
KOiK10291.
OMAiHEWQDEF.
OrthoDBiEOG7GBG00.
TreeFamiTF331105.

Family and domain databases

InterProiIPR001810. F-box_dom.
[Graphical view]
PfamiPF12937. F-box-like. 1 hit.
[Graphical view]
SMARTiSM00256. FBOX. 1 hit.
[Graphical view]
SUPFAMiSSF81383. SSF81383. 1 hit.
PROSITEiPS50181. FBOX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8CHQ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGSEPRGAG SPPPASDWGR LEAAILSGWR TFWYSVAKER ATPTASRKEA
60 70 80 90 100
AEETSALTRL PVDVQLYILS FLSPHDLCQL GSTDHYWNKT IRDPILWRYF
110 120 130 140 150
LLRDLPSWSS VDWKSLPDLE ILKKPISEVT DSTCLDYMEV YKMCCPYTRR
160 170 180 190 200
ALKASRPMYG VVTSFLHSLI IQNEPRFAMF GPGLEELNTS LVLSLMSSED
210 220 230 240 250
LCPTAGLPHR QIDGIGSGVN FQLNNQQKFN ILILYSTTRK ERDRAREEHT
260 270 280 290 300
STVNKMFSLQ SEGDEQQGSR YSVIPQIQKV CEVVDGFIYV ANAEAHRRHE
310 320 330 340 350
WQDEFSRIMA MTDPAFGSSG RPMLVLSCIS QADVKRMPCF YLAHELHLSL
360 370 380
LNHPWMVQDT EAETLTGFLN GIEWILEEVE SKRAK
Length:385
Mass (Da):43,777
Last modified:July 27, 2011 - v2
Checksum:i36D78194EAF9EE95
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911I → V in AAH40086 (PubMed:15489334).Curated
Sequence conflicti347 – 3471H → R in AAH40086 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC137902 Genomic DNA. No translation available.
BC040086 mRNA. Translation: AAH40086.1.
AJ300659 mRNA. Translation: CAC36404.1.
CCDSiCCDS27359.1.
RefSeqiNP_598860.2. NM_134099.2.
UniGeneiMm.234191.

Genome annotation databases

EnsembliENSMUST00000022791; ENSMUSP00000022791; ENSMUSG00000022184.
GeneIDi106052.
KEGGimmu:106052.
UCSCiuc007vcf.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC137902 Genomic DNA. No translation available.
BC040086 mRNA. Translation: AAH40086.1.
AJ300659 mRNA. Translation: CAC36404.1.
CCDSiCCDS27359.1.
RefSeqiNP_598860.2. NM_134099.2.
UniGeneiMm.234191.

3D structure databases

ProteinModelPortaliQ8CHQ0.
SMRiQ8CHQ0. Positions 55-382.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi222983. 3 interactions.
IntActiQ8CHQ0. 1 interaction.
STRINGi10090.ENSMUSP00000022791.

PTM databases

PhosphoSiteiQ8CHQ0.

Proteomic databases

MaxQBiQ8CHQ0.
PaxDbiQ8CHQ0.
PRIDEiQ8CHQ0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022791; ENSMUSP00000022791; ENSMUSG00000022184.
GeneIDi106052.
KEGGimmu:106052.
UCSCiuc007vcf.2. mouse.

Organism-specific databases

CTDi26272.
MGIiMGI:2146220. Fbxo4.

Phylogenomic databases

eggNOGiNOG39270.
GeneTreeiENSGT00390000014416.
HOGENOMiHOG000112550.
HOVERGENiHBG051585.
InParanoidiQ8CHQ0.
KOiK10291.
OMAiHEWQDEF.
OrthoDBiEOG7GBG00.
TreeFamiTF331105.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_275351. Association of TriC/CCT with target proteins during biosynthesis.
REACT_343568. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

NextBioi358036.
PROiQ8CHQ0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CHQ0.
CleanExiMM_FBXO4.
GenevestigatoriQ8CHQ0.

Family and domain databases

InterProiIPR001810. F-box_dom.
[Graphical view]
PfamiPF12937. F-box-like. 1 hit.
[Graphical view]
SMARTiSM00256. FBOX. 1 hit.
[Graphical view]
SUPFAMiSSF81383. SSF81383. 1 hit.
PROSITEiPS50181. FBOX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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.

Entry informationi

Entry nameiFBX4_MOUSE
AccessioniPrimary (citable) accession number: Q8CHQ0
Secondary accession number(s): E9QPM9, Q99JG8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: July 27, 2011
Last modified: April 1, 2015
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.