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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)LengthDescriptionGraphical viewFeature identifierActions
Sitei159 – 1591Important for carbohydrate binding
Sitei177 – 1771Important for carbohydrate binding

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

  • 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi177 – 1771F → A: Abolishes binding of glycoprotein targets. 1 Publication
Mutagenesisi279 – 2791Y → A: Abolishes binding of glycoprotein targets. 1 Publication
Mutagenesisi280 – 2801W → A: Abolishes binding of glycoprotein targets. Strongly reduced ubiquitination of glycoprotein targets. 1 Publication
Mutagenesisi281 – 2811K → A: No effect on carbohydrate binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 297297F-box only protein 2PRO_0000119876Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei106 – 1061PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ80UW2.
MaxQBiQ80UW2.
PaxDbiQ80UW2.
PRIDEiQ80UW2.

PTM databases

iPTMnetiQ80UW2.
PhosphoSiteiQ80UW2.

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

GO - Molecular functioni

  • glycoprotein binding Source: MGI

Protein-protein interaction databases

BioGridi231053. 5 interactions.
DIPiDIP-54758N.
IntActiQ80UW2. 1 interaction.
STRINGi10090.ENSMUSP00000037377.

Structurei

Secondary structure

1
297
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi56 – 649Combined sources
Helixi68 – 736Combined sources
Helixi75 – 773Combined sources
Helixi80 – 867Combined sources
Helixi89 – 9810Combined sources
Helixi117 – 1237Combined sources
Beta strandi131 – 1333Combined sources
Turni134 – 1396Combined sources
Beta strandi141 – 1455Combined sources
Beta strandi151 – 1544Combined sources
Turni164 – 1663Combined sources
Beta strandi171 – 1744Combined sources
Beta strandi180 – 1878Combined sources
Turni188 – 1925Combined sources
Helixi195 – 2006Combined sources
Beta strandi204 – 2129Combined sources
Beta strandi215 – 2173Combined sources
Beta strandi219 – 22911Combined sources
Beta strandi234 – 2396Combined sources
Beta strandi242 – 2443Combined sources
Beta strandi252 – 2587Combined sources
Beta strandi265 – 27814Combined sources
Beta strandi281 – 2833Combined sources
Beta strandi287 – 29610Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ80UW2.
SMRiQ80UW2. Positions 47-297.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ80UW2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini48 – 9548F-boxPROSITE-ProRule annotationAdd
BLAST
Domaini117 – 297181FBAPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni214 – 2163Carbohydrate binding
Regioni279 – 2802Carbohydrate binding

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi14 – 5643Glu-richAdd
BLAST

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_006538814.2.
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_006538814.2.
UniGeneiMm.262287.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ80UW2.
SMRiQ80UW2. Positions 47-297.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi231053. 5 interactions.
DIPiDIP-54758N.
IntActiQ80UW2. 1 interaction.
STRINGi10090.ENSMUSP00000037377.

PTM databases

iPTMnetiQ80UW2.
PhosphoSiteiQ80UW2.

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: September 7, 2016
This is version 112 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.