F-box only protein 2 - Mus musculus (Mouse)

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Q80UW2 (FBX2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 69. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
F-box only protein 2

Gene names

Name:	Fbxo2
Synonyms:	Fbs1, Fbx2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	297 AA.
Sequence status	Complete.
Protein existence	Evidence 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. 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. Ref.2 Ref.3 Ref.4 Ref.5 Ref.7
Pathway	Protein modification; protein ubiquitination.
Subunit structure	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. Ref.2 Ref.5
Subcellular location	Cytoplasm. Microsome membrane; Peripheral membrane protein; Cytoplasmic side Ref.2 Ref.3 Ref.5 Ref.6.
Tissue specificity	Detected in brain and cochlea, in epithelial support cells and hair cells of the organ of Corti (at protein level). Ref.5 Ref.6
Disruption phenotype	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. Ref.6
Sequence similarities	Contains 1 F-box domain. Contains 1 FBA (F-box associated) domain.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm Endoplasmic reticulum Membrane Microsome
Ligand	Lectin
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ER-associated protein catabolic process Inferred from direct assay Ref.3. Source: MGI SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay Ref.2. Source: UniProtKB glycoprotein catabolic process Inferred from direct assay Ref.2. Source: UniProtKB protein ubiquitination Inferred from direct assay Ref.2. Source: UniProtKB regulation of protein ubiquitination Inferred from direct assay. Source: MGI
Cellular component	SCF ubiquitin ligase complex Inferred from direct assay Ref.2. Source: UniProtKB cytosol Inferred from direct assay Ref.2. Source: UniProtKB dendritic spine Inferred from direct assay. Source: MGI endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW membrane Inferred from electronic annotation. Source: UniProtKB-KW microsome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	beta-amyloid binding Inferred from direct assay. Source: MGI glycoprotein binding Inferred from direct assay Ref.3. Source: MGI sugar binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 297

297

F-box only protein 2

PRO_0000119876

Regions

Domain

48 – 95

F-box

Domain

117 – 297

181

FBA

Region

214 – 216

Carbohydrate binding

Region

279 – 280

Carbohydrate binding

Compositional bias

14 – 56

Glu-rich

Sites

Site

159

Important for carbohydrate binding

Site

177

Important for carbohydrate binding

Experimental info

Mutagenesis

177

F → A: Abolishes binding of glycoprotein targets. Ref.7

Mutagenesis

279

Y → A: Abolishes binding of glycoprotein targets. Ref.7

Mutagenesis

280

W → A: Abolishes binding of glycoprotein targets. Strongly reduced ubiquitination of glycoprotein targets. Ref.7

Mutagenesis

281

K → A: No effect on carbohydrate binding. Ref.7

Secondary structure

297

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q80UW2 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: E0F8A5601CE5930C
Show »

FASTA

297

33,676

        10         20         30         40         50         60 
MDGDGDPESV SHPEEASPEE QPEEAGAEAS AEEEQLREAE EEEEAEAVEY LAELPEPLLL 

        70         80         90        100        110        120 
RVLAELPATE LVQACRLVCL RWKELVDGAP LWLLKCQQEG LVPEGSADEE RDHWQQFYFL 

       130        140        150        160        170        180 
SKRRRNLLRN PCGEEDLEGW SDVEHGGDGW RVEELPGDNG VEFTQDDSVK KYFASSFEWC 

       190        200        210        220        230        240 
RKAQVIDLQA EGYWEELLDT TQPAIVVKDW YSGRTDAGSL YELTVRLLSE NEDVLAEFAT 

       250        260        270        280        290 
GQVAVPEDGS WMEISHTFID YGPGVRFVRF EHGGQDSVYW KGWFGARVTN SSVWVEP

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N-3. Tissue: Eye and Mammary tumor.
[2]	"E3 ubiquitin ligase that recognizes sugar chains." Yoshida Y., Chiba T., Tokunaga F., Kawasaki H., Iwai K., Suzuki T., Ito Y., Matsuoka K., Yoshida M., Tanaka K., Tai T. Nature 418:438-442(2002) [PubMed: 12140560] [Abstract] Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
[3]	"Glycoprotein-specific ubiquitin ligases recognize N-glycans in unfolded substrates." Yoshida Y., Adachi E., Fukiya K., Iwai K., Tanaka K. EMBO Rep. 6:239-244(2005) [PubMed: 15723043] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VCP.
[4]	"Fbs1 protects the malfolded glycoproteins from the attack of peptide:N-glycanase." Yamaguchi Y., Hirao T., Sakata E., Kamiya Y., Kurimoto E., Yoshida Y., Suzuki T., Tanaka K., Kato K. Biochem. Biophys. Res. Commun. 362:712-716(2007) [PubMed: 17720138] [Abstract] Cited for: FUNCTION, NMR SPECTROSCOPY.
[5]	"A neural-specific F-box protein Fbs1 functions as a chaperone suppressing glycoprotein aggregation." Yoshida Y., Murakami A., Iwai K., Tanaka K. J. Biol. Chem. 282:7137-7144(2007) [PubMed: 17215248] [Abstract] Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[6]	"Selective cochlear degeneration in mice lacking the F-box protein, Fbx2, a glycoprotein-specific ubiquitin ligase subunit." Nelson R.F., Glenn K.A., Zhang Y., Wen H., Knutson T., Gouvion C.M., Robinson B.K., Zhou Z., Yang B., Smith R.J., Paulson H.L. J. Neurosci. 27:5163-5171(2007) [PubMed: 17494702] [Abstract] Cited for: DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH SKP1, TISSUE SPECIFICITY.
[7]	"Structural basis of sugar-recognizing ubiquitin ligase." Mizushima T., Hirao T., Yoshida Y., Lee S.J., Chiba T., Iwai K., Yamaguchi Y., Kato K., Tsukihara T., Tanaka K. Nat. Struct. Mol. Biol. 11:365-370(2004) [PubMed: 14990996] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 117-297 IN COMPLEX WITH CHITOBIOSE, FUNCTION, MUTAGENESIS OF PHE-177; TYR-279; TRP-280 AND LYS-281.
[8]	"Structural basis for the selection of glycosylated substrates by SCF(Fbs1) ubiquitin ligase." Mizushima T., Yoshida Y., Kumanomidou T., Hasegawa Y., Suzuki A., Yamane T., Tanaka K. Proc. Natl. Acad. Sci. U.S.A. 104:5777-5781(2007) [PubMed: 17389369] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEXES WITH SKP1 AND GLYCOPROTEIN SUBSTRATE RNASE1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BC027053 mRNA. Translation: AAH27053.1.
BC046586 mRNA. Translation: AAH46586.1.

IPI

IPI00153176.

RefSeq

NP_789818.1. NM_176848.1.

UniGene

Mm.262287.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UMH	X-ray	2.00	A	117-297	[»]
1UMI	X-ray	2.40	A	117-297	[»]
2E31	X-ray	2.40	A	1-297	[»]
2E32	X-ray	3.52	A/C	1-297	[»]
2E33	X-ray	2.70	A	105-297	[»]
2RJ2	X-ray	1.70	A	117-297	[»]

ProteinModelPortal

Q80UW2.

SMR

Q80UW2. Positions 47-297.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q80UW2. 1 interaction.

STRING

Q80UW2.

PTM databases

PhosphoSite

Q80UW2.

Proteomic databases

PRIDE

Q80UW2.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000047951; ENSMUSP00000037377; ENSMUSG00000041556.

GeneID

230904.

KEGG

mmu:230904.

Organism-specific databases

CTD

26232.

MGI

MGI:2446216. Fbxo2.

Phylogenomic databases

GeneTree

ENSGT00390000003865.

HOGENOM

HBG716440.

HOVERGEN

HBG003593.

InParanoid

Q80UW2.

OMA

WIEISHT.

OrthoDB

EOG4J1191.

PhylomeDB

Q80UW2.

Gene expression databases

ArrayExpress

Q80UW2.

Bgee

Q80UW2.

CleanEx

MM_FBXO2.

Genevestigator

Q80UW2.

GermOnline

ENSMUSG00000041556. Mus musculus.

Family and domain databases

InterPro

IPR007397. F-box-assoc_dom.
IPR001810. F-box_dom_cyclin-like.
IPR022364. F-box_dom_Skp2-like.
IPR008979. Galactose-bd-like.
[Graphical view]

K10099.

Pfam

PF00646. F-box. 1 hit.
PF04300. FBA. 1 hit.
[Graphical view]

SUPFAM

SSF81383. F-box_dom_Skp2-like. 1 hit.
SSF49785. Gal_bind_like. 1 hit.

PROSITE

PS51114. FBA. 1 hit.
PS50181. FBOX. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

380276.

SOURCE

Search...

Entry information

Entry name

FBX2_MOUSE

Accession

Primary (citable) accession number: Q80UW2
Secondary accession number(s): Q8R0D2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	June 1, 2003
Last modified:	November 16, 2011
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents