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Protein

F-box only protein 6

Gene

Fbxo6

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity2 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.

GO - Molecular functioni

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

GO - Biological processi

  • DNA repair Source: UniProtKB-KW
  • ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • glycoprotein catabolic process Source: MGI
  • glycoprotein ERAD pathway Source: ParkinsonsUK-UCL
  • response to unfolded protein Source: UniProtKB-KW
  • SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway, Unfolded protein response

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
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 namesi
Name:Fbxo6
Synonyms:Fbs2, Fbxo6b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1354743. Fbxo6.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • endoplasmic reticulum quality control compartment Source: ParkinsonsUK-UCL
  • SCF ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 295295F-box only protein 6PRO_0000119883Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei249 – 2491PhosphoserineBy similarity
Modified residuei276 – 2761PhosphoserineCombined sources
Modified residuei280 – 2801PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9QZN4.
MaxQBiQ9QZN4.
PaxDbiQ9QZN4.
PeptideAtlasiQ9QZN4.
PRIDEiQ9QZN4.

PTM databases

iPTMnetiQ9QZN4.
PhosphoSiteiQ9QZN4.

Expressioni

Tissue specificityi

Present in liver and kidney (at protein level). Widely expressed.2 Publications

Developmental stagei

Weakly expressed in embryos.1 Publication

Gene expression databases

BgeeiQ9QZN4.
CleanExiMM_FBXO6.
ExpressionAtlasiQ9QZN4. baseline and differential.
GenevisibleiQ9QZN4. MM.

Interactioni

Subunit structurei

Interacts with CHEK1 and CUL1 (By similarity). Part of a SCF (SKP1-cullin-F-box) protein ligase complex. Interacts with VCP.By similarity2 Publications

GO - Molecular functioni

  • glycoprotein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi206095. 4 interactions.
IntActiQ9QZN4. 2 interactions.
MINTiMINT-4095047.
STRINGi10090.ENSMUSP00000030858.

Structurei

3D structure databases

ProteinModelPortaliQ9QZN4.
SMRiQ9QZN4. Positions 3-248.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 4848F-boxPROSITE-ProRule annotationAdd
BLAST
Domaini69 – 250182FBAPROSITE-ProRule annotationAdd
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.
HOVERGENiHBG003593.
InParanoidiQ9QZN4.
KOiK10100.
OMAiEMCLKSQ.
OrthoDBiEOG7DRJ3R.
PhylomeDBiQ9QZN4.
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]
PfamiPF12937. F-box-like. 1 hit.
PF04300. FBA. 1 hit.
[Graphical view]
SMARTiSM01198. FBA. 1 hit.
SM00256. FBOX. 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.

Q9QZN4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVHINELPEN ILLELFIHIP APQLLRNCRL VCRLWRDLID VVSLWKRKSL
60 70 80 90 100
REGFFTKDRC EPVEDWKVFY ILCSLQRNLL RNPCAEENLS SWRIDSNGGD
110 120 130 140 150
RWKVETLPGS CGTSFPDNKV KKYFVTSFEM CLKSQMVDLK AEGYCEELMD
160 170 180 190 200
TFRPDIVVKD WVAPRADCGC TYQLRVQLAS ADYIVLASFE PPPVTFQQWN
210 220 230 240 250
DAKWQEISHT FSDYPPGVRH ILFQHGGQDT QFWKGWYGPR VTNSSIIISH
260 270 280 290
RTAKNPPPAR TLPEETVVIG RRRRASDSNT HEGFFWQGLW QRLRR
Length:295
Mass (Da):34,493
Last modified:May 1, 2000 - v1
Checksum:iD515D3C25CC73B22
GO

Sequence cautioni

The sequence CAM14908.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAQ51914.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAQ52206.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti77 – 771R → K in CAQ52204 (PubMed:19468303).Curated
Sequence conflicti77 – 771R → K in CAQ52206 (PubMed:19468303).Curated
Sequence conflicti77 – 771R → K in CAQ51912 (PubMed:19468303).Curated
Sequence conflicti77 – 771R → K in CAQ51914 (PubMed:19468303).Curated
Sequence conflicti77 – 771R → K in EDL14807 (Ref. 4) Curated
Sequence conflicti77 – 771R → K in EDL14805 (Ref. 4) Curated
Sequence conflicti77 – 771R → K in EDL14804 (Ref. 4) Curated
Sequence conflicti252 – 2521T → A in BAE29703 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS18933.1.
RefSeqiNP_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.
XP_006536020.1. XM_006535957.2.
UniGeneiMm.27445.

Genome annotation databases

EnsembliENSMUST00000030858; ENSMUSP00000030858; ENSMUSG00000055401.
ENSMUST00000056965; ENSMUSP00000062348; ENSMUSG00000055401.
ENSMUST00000105706; ENSMUSP00000101331; ENSMUSG00000055401.
ENSMUST00000168503; ENSMUSP00000130188; ENSMUSG00000055401.
GeneIDi50762.
KEGGimmu:50762.
UCSCiuc008vud.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS18933.1.
RefSeqiNP_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.
XP_006536020.1. XM_006535957.2.
UniGeneiMm.27445.

3D structure databases

ProteinModelPortaliQ9QZN4.
SMRiQ9QZN4. Positions 3-248.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi206095. 4 interactions.
IntActiQ9QZN4. 2 interactions.
MINTiMINT-4095047.
STRINGi10090.ENSMUSP00000030858.

PTM databases

iPTMnetiQ9QZN4.
PhosphoSiteiQ9QZN4.

Proteomic databases

EPDiQ9QZN4.
MaxQBiQ9QZN4.
PaxDbiQ9QZN4.
PeptideAtlasiQ9QZN4.
PRIDEiQ9QZN4.

Protocols and materials databases

DNASUi50762.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030858; ENSMUSP00000030858; ENSMUSG00000055401.
ENSMUST00000056965; ENSMUSP00000062348; ENSMUSG00000055401.
ENSMUST00000105706; ENSMUSP00000101331; ENSMUSG00000055401.
ENSMUST00000168503; ENSMUSP00000130188; ENSMUSG00000055401.
GeneIDi50762.
KEGGimmu:50762.
UCSCiuc008vud.2. mouse.

Organism-specific databases

CTDi26270.
MGIiMGI:1354743. Fbxo6.

Phylogenomic databases

eggNOGiENOG410IK6V. Eukaryota.
ENOG4111MF5. LUCA.
GeneTreeiENSGT00390000003865.
HOVERGENiHBG003593.
InParanoidiQ9QZN4.
KOiK10100.
OMAiEMCLKSQ.
OrthoDBiEOG7DRJ3R.
PhylomeDBiQ9QZN4.
TreeFamiTF320527.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ9QZN4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QZN4.
CleanExiMM_FBXO6.
ExpressionAtlasiQ9QZN4. baseline and differential.
GenevisibleiQ9QZN4. 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]
PfamiPF12937. F-box-like. 1 hit.
PF04300. FBA. 1 hit.
[Graphical view]
SMARTiSM01198. FBA. 1 hit.
SM00256. FBOX. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF81383. SSF81383. 1 hit.
PROSITEiPS51114. FBA. 1 hit.
PS50181. FBOX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Bone marrow, Kidney and Lung.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUGAR-BINDING, INTERACTION WITH VCP.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276 AND THR-280, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiFBX6_MOUSE
AccessioniPrimary (citable) accession number: Q9QZN4
Secondary accession number(s): A2A7H0
, A2A7H2, B2KFL0, B2KFL2, Q3TML5, Q3UCB0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: May 1, 2000
Last modified: July 6, 2016
This is version 118 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

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. 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.