Q9QZN4 (FBX6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
F-box only protein 6

Alternative name(s):
F-box only protein 6b
F-box protein that recognizes sugar chains 2
F-box/G-domain protein 2

Gene names

Name:	Fbxo6
Synonyms:	Fbs2, Fbxo6b

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	295 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Substrate-recognition component of some SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complexes. Involved in DNA damage response by specifically recognizing activated CHEK1 (phosphorylated on 'Ser-345'), promoting its ubiquitination and degradation. Ubiquitination of CHEK1 is required to insure that activated CHEK1 does not accumulate as cells progress through S phase, or when replication forks encounter transient impediments during normal DNA replication By similarity. Involved in endoplasmic reticulum-associated degradation pathway (ERAD) for misfolded lumenal proteins by recognizing and binding sugar chains on unfolded glycoproteins that are retrotranlocated into the cytosol and promoting their ubiquitination and subsequent degradation. Able to recognize and bind denatured glycoproteins, which are modified with not only high-mannose but also complex-type oligosaccharides. Also recognizes sulfated glycans. Ref.6 Ref.7
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Interacts with CHEK1 and CUL1 By similarity. Part of a SCF (SKP1-cullin-F-box) protein ligase complex. Interacts with VCP. Ref.7
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Present in liver and kidney (at protein level). Widely expressed. Ref.6 Ref.9
Developmental stage	Weakly expressed in embryos. Ref.9
Sequence similarities	Contains 1 F-box domain. Contains 1 FBA (F-box associated) domain.
Sequence caution	The sequence CAM14908.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAQ51914.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAQ52206.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	DNA damage DNA repair Ubl conjugation pathway Unfolded protein response
Cellular component	Cytoplasm
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW ER-associated protein catabolic process Inferred from mutant phenotype Ref.6. Source: UniProtKB SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay Ref.6. Source: UniProtKB glycoprotein catabolic process Inferred from direct assay Ref.7. Source: MGI response to unfolded protein Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	SCF ubiquitin ligase complex Inferred from direct assay Ref.6. Source: UniProtKB cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	carbohydrate binding Inferred from direct assay Ref.6. Source: MGI glycoprotein binding Inferred from direct assay Ref.6. Source: UniProtKB ubiquitin-protein ligase activity Inferred from direct assay Ref.6. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 295	295	F-box only protein 6		PRO_0000119883
Regions
	Domain	1 – 48	48	F-box
	Domain	69 – 250	182	FBA
Amino acid modifications
	Modified residue	276	1	Phosphoserine Ref.8
Experimental info
	Sequence conflict	77	1	R → K in CAQ52204. Ref.3
	Sequence conflict	77	1	R → K in CAQ52206. Ref.3
	Sequence conflict	77	1	R → K in CAQ51912. Ref.3
	Sequence conflict	77	1	R → K in CAQ51914. Ref.3
	Sequence conflict	77	1	R → K in EDL14807. Ref.4
	Sequence conflict	77	1	R → K in EDL14805. Ref.4
	Sequence conflict	77	1	R → K in EDL14804. Ref.4
	Sequence conflict	252	1	T → A in BAE29703. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9QZN4 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: D515D3C25CC73B22	FASTA	295	34,493
	10 20 30 40 50 60 MVHINELPEN ILLELFIHIP APQLLRNCRL VCRLWRDLID VVSLWKRKSL REGFFTKDRC 70 80 90 100 110 120 EPVEDWKVFY ILCSLQRNLL RNPCAEENLS SWRIDSNGGD RWKVETLPGS CGTSFPDNKV 130 140 150 160 170 180 KKYFVTSFEM CLKSQMVDLK AEGYCEELMD TFRPDIVVKD WVAPRADCGC TYQLRVQLAS 190 200 210 220 230 240 ADYIVLASFE PPPVTFQQWN DAKWQEISHT FSDYPPGVRH ILFQHGGQDT QFWKGWYGPR 250 260 270 280 290 VTNSSIIISH RTAKNPPPAR TLPEETVVIG RRRRASDSNT HEGFFWQGLW QRLRR

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: 10531037] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Bone marrow, Kidney and Lung.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6.
[4]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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].
[6]	"Fbs2 is a new member of the E3 ubiquitin ligase family that recognizes sugar chains." Yoshida Y., Tokunaga F., Chiba T., Iwai K., Tanaka K., Tai T. J. Biol. Chem. 278:43877-43884(2003) [PubMed: 12939278] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN A SCF PROTEIN LIGASE COMPLEX, SUGAR-BINDING, TISSUE SPECIFICITY.
[7]	"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, SUGAR-BINDING, INTERACTION WITH VCP.
[8]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276, MASS SPECTROMETRY. Tissue: Liver.
[9]	"Diversity in tissue expression, substrate binding, and SCF complex formation for a lectin family of ubiquitin ligases." Glenn K.A., Nelson R.F., Wen H.M., Mallinger A.J., Paulson H.L. J. Biol. Chem. 283:12717-12729(2008) [PubMed: 18203720] [Abstract] Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF176526 mRNA. Translation: AAF09135.1. AK002840 mRNA. Translation: BAB22397.1. AK150612 mRNA. Translation: BAE29703.1. AK152888 mRNA. Translation: BAE31571.1. AK165867 mRNA. Translation: BAE38426.1. AK170743 mRNA. Translation: BAE41996.1. AK171483 mRNA. Translation: BAE42484.1. AL606929 Genomic DNA. Translation: CAM14906.1. AL606929 Genomic DNA. Translation: CAM14908.1. Sequence problems. CU207376, CU207417 Genomic DNA. Translation: CAQ51912.1. CU207376, CU207417 Genomic DNA. Translation: CAQ51914.1. Sequence problems. CU207417, CU207376 Genomic DNA. Translation: CAQ52204.1. CU207417, CU207376 Genomic DNA. Translation: CAQ52206.1. Sequence problems. CH466594 Genomic DNA. Translation: EDL14804.1. CH466594 Genomic DNA. Translation: EDL14805.1. CH466594 Genomic DNA. Translation: EDL14807.1. BC017512 mRNA. Translation: AAH17512.1.
IPI	IPI00137697.
RefSeq	NP_001157176.1. NM_001163704.1. NP_001157177.1. NM_001163705.1. NP_001157178.1. NM_001163706.1. NP_001157179.1. NM_001163707.1. NP_056612.1. NM_015797.4.
UniGene	Mm.27445.
3D structure databases
ProteinModelPortal	Q9QZN4.
SMR	Q9QZN4. Positions 2-250.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9QZN4. 1 interaction.
STRING	Q9QZN4.
PTM databases
PhosphoSite	Q9QZN4.
Proteomic databases
PRIDE	Q9QZN4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000030858; ENSMUSP00000030858; ENSMUSG00000055401. ENSMUST00000056965; ENSMUSP00000062348; ENSMUSG00000055401. ENSMUST00000105706; ENSMUSP00000101331; ENSMUSG00000055401. ENSMUST00000152098; ENSMUSP00000121379; ENSMUSG00000055401. ENSMUST00000168503; ENSMUSP00000130188; ENSMUSG00000055401.
GeneID	50762.
KEGG	mmu:50762.
UCSC	uc008vud.2. mouse.
Organism-specific databases
CTD	26270.
MGI	MGI:1354743. Fbxo6.
Phylogenomic databases
GeneTree	ENSGT00390000003865.
HOGENOM	HBG716440.
HOVERGEN	HBG003593.
InParanoid	Q9QZN4.
OMA	KYFVTSF.
OrthoDB	EOG4VX267.
PhylomeDB	Q9QZN4.
Enzyme and pathway databases
Reactome	REACT_93132. Metabolism of proteins.
Gene expression databases
ArrayExpress	Q9QZN4.
Bgee	Q9QZN4.
CleanEx	MM_FBXO6.
Genevestigator	Q9QZN4.
GermOnline	ENSMUSG00000055401. 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]
KO	K10100.
Pfam	PF00646. F-box. 1 hit. PF04300. FBA. 1 hit. [Graphical view]
SMART	SM00256. FBOX. 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	307659.
SOURCE	Search...

Entry information

Entry name

FBX6_MOUSE

Accession

Primary (citable) accession number: Q9QZN4
Secondary accession number(s): A2A7H0 , A2A7H2, B2KFL0, B2KFL2, Q3TML5, Q3UCB0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	May 1, 2000
Last modified:	November 16, 2011
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program