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Protein

F-box only protein 2

Gene

Fbxo2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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 that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Involved in the endoplasmic reticulum-associated degradation pathway (ERAD) for misfolded lumenal proteins by recognizing and binding sugar chains on unfolded glycoproteins that are retrotranslocated into the cytosol and promoting their ubiquitination and subsequent degradation. Prevents formation of cytosolic aggregates of unfolded glycoproteins that have been retrotranslocated into the cytosol. Able to recognize and bind denatured glycoproteins, preferentially those of the high-mannose type.5 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei159Important for carbohydrate binding1
Sitei177Important for carbohydrate binding1

GO - Molecular functioni

  • beta-amyloid binding Source: MGI
  • carbohydrate binding Source: MGI
  • glycoprotein binding Source: MGI
  • ubiquitin-protein transferase activity Source: MGI

GO - Biological processi

  • ER-associated ubiquitin-dependent protein catabolic process Source: MGI
  • glycoprotein catabolic process Source: UniProtKB
  • negative regulation of cell proliferation Source: Ensembl
  • protein ubiquitination Source: UniProtKB
  • regulation of protein ubiquitination Source: MGI
  • SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  • ubiquitin-dependent protein catabolic process Source: MGI
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Lectin

Enzyme and pathway databases

ReactomeiR-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
F-box only protein 2
Gene namesi
Name:Fbxo2
Synonyms:Fbs1, Fbx2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:2446216. Fbxo2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: UniProtKB
  • dendritic spine Source: MGI
  • endoplasmic reticulum Source: UniProtKB-KW
  • extracellular exosome Source: MGI
  • organelle membrane Source: UniProtKB-SubCell
  • SCF ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Disruption phenotypei

No visible phenotype at birth. Mice are viable and fertile, but after two to four months, gradual hearing loss sets in, due to degeneration of epithelial support cells and hair cells of the organ of Corti and spiral ganglion neurodegeneration.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi177F → A: Abolishes binding of glycoprotein targets. 1 Publication1
Mutagenesisi279Y → A: Abolishes binding of glycoprotein targets. 1 Publication1
Mutagenesisi280W → A: Abolishes binding of glycoprotein targets. Strongly reduced ubiquitination of glycoprotein targets. 1 Publication1
Mutagenesisi281K → A: No effect on carbohydrate binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001198761 – 297F-box only protein 2Add BLAST297

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei106PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ80UW2.
MaxQBiQ80UW2.
PaxDbiQ80UW2.
PRIDEiQ80UW2.

PTM databases

iPTMnetiQ80UW2.
PhosphoSitePlusiQ80UW2.

Expressioni

Tissue specificityi

Detected in brain and cochlea, in epithelial support cells and hair cells of the organ of Corti (at protein level).2 Publications

Gene expression databases

BgeeiENSMUSG00000041556.
CleanExiMM_FBXO2.
ExpressionAtlasiQ80UW2. baseline and differential.
GenevisibleiQ80UW2. MM.

Interactioni

Subunit structurei

Component of the SCF(FBXO2) complex consisting of CUL1, RBX1, SKP1 and FBXO2. Predominantly detected as heterodimer with SKP1; the heterodimer with SKP1 is not part of the SCF(FBXO2) complex.3 Publications

Protein-protein interaction databases

BioGridi231053. 5 interactors.
DIPiDIP-54758N.
IntActiQ80UW2. 1 interactor.
STRINGi10090.ENSMUSP00000037377.

Structurei

Secondary structure

1297
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi56 – 64Combined sources9
Helixi68 – 73Combined sources6
Helixi75 – 77Combined sources3
Helixi80 – 86Combined sources7
Helixi89 – 98Combined sources10
Helixi117 – 123Combined sources7
Beta strandi128 – 130Combined sources3
Beta strandi131 – 133Combined sources3
Turni134 – 139Combined sources6
Beta strandi141 – 145Combined sources5
Helixi146 – 149Combined sources4
Beta strandi151 – 154Combined sources4
Turni164 – 166Combined sources3
Beta strandi171 – 174Combined sources4
Beta strandi180 – 187Combined sources8
Turni188 – 192Combined sources5
Helixi195 – 200Combined sources6
Beta strandi204 – 212Combined sources9
Beta strandi215 – 217Combined sources3
Beta strandi219 – 229Combined sources11
Beta strandi234 – 239Combined sources6
Beta strandi242 – 244Combined sources3
Beta strandi252 – 258Combined sources7
Beta strandi265 – 278Combined sources14
Beta strandi281 – 283Combined sources3
Beta strandi287 – 296Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UMHX-ray2.00A117-297[»]
1UMIX-ray2.40A117-297[»]
2E31X-ray2.40A1-297[»]
2E32X-ray3.52A/C1-297[»]
2E33X-ray2.70A105-297[»]
2RJ2X-ray1.70A117-297[»]
5B4NX-ray2.30A/B117-297[»]
ProteinModelPortaliQ80UW2.
SMRiQ80UW2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ80UW2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini48 – 95F-boxPROSITE-ProRule annotationAdd BLAST48
Domaini117 – 297FBAPROSITE-ProRule annotationAdd BLAST181

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni214 – 216Carbohydrate binding3
Regioni279 – 280Carbohydrate binding2

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi14 – 56Glu-richAdd BLAST43

Sequence similaritiesi

Contains 1 F-box domain.PROSITE-ProRule annotation
Contains 1 FBA (F-box associated) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IK6V. Eukaryota.
ENOG4111MF5. LUCA.
GeneTreeiENSGT00390000003865.
HOGENOMiHOG000231084.
HOVERGENiHBG003593.
InParanoidiQ80UW2.
KOiK10099.
OMAiEFNSGQV.
OrthoDBiEOG091G0G3L.
PhylomeDBiQ80UW2.
TreeFamiTF320527.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR007397. F-box-assoc_dom.
IPR001810. F-box_dom.
IPR008979. Galactose-bd-like.
[Graphical view]
PfamiPF00646. F-box. 1 hit.
PF04300. FBA. 1 hit.
[Graphical view]
SMARTiSM01198. FBA. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF81383. SSF81383. 1 hit.
PROSITEiPS51114. FBA. 1 hit.
PS50181. FBOX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q80UW2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDGDGDPESV SHPEEASPEE QPEEAGAEAS AEEEQLREAE EEEEAEAVEY
60 70 80 90 100
LAELPEPLLL RVLAELPATE LVQACRLVCL RWKELVDGAP LWLLKCQQEG
110 120 130 140 150
LVPEGSADEE RDHWQQFYFL SKRRRNLLRN PCGEEDLEGW SDVEHGGDGW
160 170 180 190 200
RVEELPGDNG VEFTQDDSVK KYFASSFEWC RKAQVIDLQA EGYWEELLDT
210 220 230 240 250
TQPAIVVKDW YSGRTDAGSL YELTVRLLSE NEDVLAEFAT GQVAVPEDGS
260 270 280 290
WMEISHTFID YGPGVRFVRF EHGGQDSVYW KGWFGARVTN SSVWVEP
Length:297
Mass (Da):33,676
Last modified:June 1, 2003 - v1
Checksum:iE0F8A5601CE5930C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC027053 mRNA. Translation: AAH27053.1.
BC046586 mRNA. Translation: AAH46586.1.
CCDSiCCDS18935.1.
RefSeqiNP_789818.1. NM_176848.1.
XP_006538877.1. XM_006538814.3.
UniGeneiMm.262287.

Genome annotation databases

EnsembliENSMUST00000047951; ENSMUSP00000037377; ENSMUSG00000041556.
GeneIDi230904.
KEGGimmu:230904.
UCSCiuc008vuk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC027053 mRNA. Translation: AAH27053.1.
BC046586 mRNA. Translation: AAH46586.1.
CCDSiCCDS18935.1.
RefSeqiNP_789818.1. NM_176848.1.
XP_006538877.1. XM_006538814.3.
UniGeneiMm.262287.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UMHX-ray2.00A117-297[»]
1UMIX-ray2.40A117-297[»]
2E31X-ray2.40A1-297[»]
2E32X-ray3.52A/C1-297[»]
2E33X-ray2.70A105-297[»]
2RJ2X-ray1.70A117-297[»]
5B4NX-ray2.30A/B117-297[»]
ProteinModelPortaliQ80UW2.
SMRiQ80UW2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi231053. 5 interactors.
DIPiDIP-54758N.
IntActiQ80UW2. 1 interactor.
STRINGi10090.ENSMUSP00000037377.

PTM databases

iPTMnetiQ80UW2.
PhosphoSitePlusiQ80UW2.

Proteomic databases

EPDiQ80UW2.
MaxQBiQ80UW2.
PaxDbiQ80UW2.
PRIDEiQ80UW2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000047951; ENSMUSP00000037377; ENSMUSG00000041556.
GeneIDi230904.
KEGGimmu:230904.
UCSCiuc008vuk.1. mouse.

Organism-specific databases

CTDi26232.
MGIiMGI:2446216. Fbxo2.

Phylogenomic databases

eggNOGiENOG410IK6V. Eukaryota.
ENOG4111MF5. LUCA.
GeneTreeiENSGT00390000003865.
HOGENOMiHOG000231084.
HOVERGENiHBG003593.
InParanoidiQ80UW2.
KOiK10099.
OMAiEFNSGQV.
OrthoDBiEOG091G0G3L.
PhylomeDBiQ80UW2.
TreeFamiTF320527.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiFbxo2. mouse.
EvolutionaryTraceiQ80UW2.
PROiQ80UW2.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000041556.
CleanExiMM_FBXO2.
ExpressionAtlasiQ80UW2. baseline and differential.
GenevisibleiQ80UW2. MM.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR007397. F-box-assoc_dom.
IPR001810. F-box_dom.
IPR008979. Galactose-bd-like.
[Graphical view]
PfamiPF00646. F-box. 1 hit.
PF04300. FBA. 1 hit.
[Graphical view]
SMARTiSM01198. FBA. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF81383. SSF81383. 1 hit.
PROSITEiPS51114. FBA. 1 hit.
PS50181. FBOX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFBX2_MOUSE
AccessioniPrimary (citable) accession number: Q80UW2
Secondary accession number(s): Q8R0D2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: June 1, 2003
Last modified: November 30, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.