Q9UK22 (FBX2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
F-box only protein 2

Gene names

Name:	FBXO2
Synonyms:	FBX2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	296 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 By similarity.
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 By similarity.
Subcellular location	Cytoplasm By similarity. Microsome membrane; Peripheral membrane protein; Cytoplasmic side By similarity.
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
Coding sequence diversity	Polymorphism
Ligand	Lectin
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ER-associated protein catabolic process Inferred from electronic annotation. Source: Compara SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from sequence or structural similarity. Source: UniProtKB glycoprotein catabolic process Inferred from sequence or structural similarity. Source: UniProtKB regulation of protein ubiquitination Inferred from electronic annotation. Source: Compara
Cellular_component	SCF ubiquitin ligase complex Inferred from sequence or structural similarity. Source: UniProtKB cytosol Inferred from sequence or structural similarity. Source: UniProtKB dendritic spine Inferred from electronic annotation. Source: Compara endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW organelle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	beta-amyloid binding Inferred from electronic annotation. Source: Compara carbohydrate binding Inferred from electronic annotation. Source: Compara ubiquitin-protein ligase activity Traceable author statement Ref.7. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 296	296	F-box only protein 2		PRO_0000119875
Regions
	Domain	44 – 91	48	F-box
	Domain	113 – 296	184	FBA
	Region	210 – 212	3	Carbohydrate binding By similarity
	Region	278 – 279	2	Carbohydrate binding By similarity
Sites
	Site	173	1	Important for carbohydrate binding By similarity
Natural variations
	Natural variant	118	1	K → T. Ref.2 Corresponds to variant rs9614 [ dbSNP | Ensembl ].		VAR_049036
Experimental info
	Sequence conflict	45	1	Missing in AAF01822. Ref.1
	Sequence conflict	125	1	R → C in CAG46907. Ref.2
	Sequence conflict	163	1	E → D in CAG46907. Ref.2
	Sequence conflict	275	1	D → G in AAF04515. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Q9UK22 [UniParc]. Last modified August 16, 2004. Version 2. Checksum: 5226F19E27D884AF	FASTA	296	33,328
	10 20 30 40 50 60 MDGDGDPESV GQPEEASPEE QPEEASAEEE RPEDQQEEEA AAAAAYLDEL PEPLLLRVLA 70 80 90 100 110 120 ALPAAELVQA CRLVCLRWKE LVDGAPLWLL KCQQEGLVPE GGVEEERDHW QQFYFLSKRR 130 140 150 160 170 180 RNLLRNPCGE EDLEGWCDVE HGGDGWRVEE LPGDSGVEFT HDESVKKYFA SSFEWCRKAQ 190 200 210 220 230 240 VIDLQAEGYW EELLDTTQPA IVVKDWYSGR SDAGCLYELT VKLLSEHENV LAEFSSGQVA 250 260 270 280 290 VPQDSDGGGW MEISHTFTDY GPGVRFVRFE HGGQDSVYWK GWFGARVTNS SVWVEP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A family of mammalian F-box proteins." Winston J.T., Koepp D.M., Zhu C., Elledge S.J., Harper J.W. Curr. Biol. 9:1180-1182(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-118.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cerebellum.
[4]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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]. Tissue: Brain and Pancreas.
[7]	"Identification of a family of human F-box proteins." Cenciarelli C., Chiaur D.S., Guardavaccaro D., Parks W., Vidal M., Pagano M. Curr. Biol. 9:1177-1179(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 40-296.
[8]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF187318 mRNA. Translation: AAF01822.1. CR542110 mRNA. Translation: CAG46907.1. AK313019 mRNA. Translation: BAG35854.1. AL031731 Genomic DNA. Translation: CAI20209.1. CH471130 Genomic DNA. Translation: EAW71689.1. BC025233 mRNA. Translation: AAH25233.1. BC096747 mRNA. Translation: AAH96747.1. AF174594 mRNA. Translation: AAF04515.1.
IPI	IPI01018924.
RefSeq	NP_036300.2. NM_012168.5.
UniGene	Hs.132753. Hs.556006.
3D structure databases
ProteinModelPortal	Q9UK22.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UK22. 1 interaction.
STRING	9606.ENSP00000346240.
PTM databases
PhosphoSite	Q9UK22.
Polymorphism databases
DMDM	51338836.
Proteomic databases
PaxDb	Q9UK22.
PeptideAtlas	Q9UK22.
PRIDE	Q9UK22.
Protocols and materials databases
DNASU	26232.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000354287; ENSP00000346240; ENSG00000116661.
GeneID	26232.
KEGG	hsa:26232.
UCSC	uc001asj.3. human.
Organism-specific databases
CTD	26232.
GeneCards	GC01M011708.
HGNC	HGNC:13581. FBXO2.
MIM	607112. gene.
neXtProt	NX_Q9UK22.
PharmGKB	PA31895.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG85061.
HOGENOM	HOG000231084.
HOVERGEN	HBG003593.
InParanoid	Q9UK22.
KO	K10099.
OMA	WIEISHT.
OrthoDB	EOG4J1191.
Enzyme and pathway databases
Reactome	REACT_6900. Immune System.
UniPathway	UPA00143.
Gene expression databases
Bgee	Q9UK22.
CleanEx	HS_FBXO2.
Genevestigator	Q9UK22.
GermOnline	ENSG00000116661. Homo sapiens.
Family and domain databases
InterPro	IPR007397. F-box-assoc_dom. IPR001810. F-box_dom_cyclin-like. IPR008979. Galactose-bd-like. [Graphical view]
Pfam	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
ChiTaRS	FBXO2. human.
GenomeRNAi	26232.
NextBio	48407.
SOURCE	Search...

Entry information

Entry name

FBX2_HUMAN

Accession

Primary (citable) accession number: Q9UK22
Secondary accession number(s): B2R7K7 , Q5TGY0, Q6FGJ7, Q8TB29, Q9UKC6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	August 16, 2004
Last modified:	May 1, 2013
This is version 111 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.