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Protein

F-box only protein 6

Gene

FBXO6

Organism
Homo sapiens (Human)
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 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. Also 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.2 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

GO - Biological processi

  • DNA damage checkpoint Source: UniProtKB
  • DNA repair Source: UniProtKB
  • ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • glycoprotein catabolic process Source: Ensembl
  • proteolysis Source: ProtInc
  • 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-HSA-390471. Association of TriC/CCT with target proteins during biosynthesis.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
F-box only protein 6
Alternative name(s):
F-box protein that recognizes sugar chains 2
F-box/G-domain protein 2
Gene namesi
Name:FBXO6
Synonyms:FBG2, FBS2, FBX6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:13585. FBXO6.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi241 – 2422YW → AA: Abolishes interaction with glycosylated concanavalin-A in vitro. 1 Publication

Organism-specific databases

PharmGKBiPA28046.

Polymorphism and mutation databases

BioMutaiFBXO6.
DMDMi24636846.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 293293F-box only protein 6PRO_0000119882Add
BLAST

Proteomic databases

EPDiQ9NRD1.
MaxQBiQ9NRD1.
PaxDbiQ9NRD1.
PRIDEiQ9NRD1.

PTM databases

iPTMnetiQ9NRD1.
PhosphoSiteiQ9NRD1.

Expressioni

Gene expression databases

BgeeiQ9NRD1.
CleanExiHS_FBXO6.
ExpressionAtlasiQ9NRD1. baseline and differential.
GenevisibleiQ9NRD1. HS.

Organism-specific databases

HPAiHPA051175.

Interactioni

Subunit structurei

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi117654. 622 interactions.
IntActiQ9NRD1. 4 interactions.
STRINGi9606.ENSP00000365944.

Structurei

3D structure databases

ProteinModelPortaliQ9NRD1.
SMRiQ9NRD1. Positions 9-259.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 5748F-boxPROSITE-ProRule annotationAdd
BLAST
Domaini78 – 259182FBAPROSITE-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.
HOGENOMiHOG000231084.
HOVERGENiHBG003593.
InParanoidiQ9NRD1.
KOiK10100.
OMAiEMCLKSQ.
OrthoDBiEOG7DRJ3R.
PhylomeDBiQ9NRD1.
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.

Q9NRD1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDAPHSKAAL DSINELPENI LLELFTHVPA RQLLLNCRLV CSLWRDLIDL
60 70 80 90 100
MTLWKRKCLR EGFITKDWDQ PVADWKIFYF LRSLHRNLLR NPCAEEDMFA
110 120 130 140 150
WQIDFNGGDR WKVESLPGAH GTDFPDPKVK KYFVTSYEMC LKSQLVDLVA
160 170 180 190 200
EGYWEELLDT FRPDIVVKDW FAARADCGCT YQLKVQLASA DYFVLASFEP
210 220 230 240 250
PPVTIQQWNN ATWTEVSYTF SDYPRGVRYI LFQHGGRDTQ YWAGWYGPRV
260 270 280 290
TNSSIVVSPK MTRNQASSEA QPGQKHGQEE AAQSPYRAVV QIF
Length:293
Mass (Da):33,933
Last modified:October 1, 2000 - v1
Checksum:iEA4235CD9CCD80FF
GO

Sequence cautioni

The sequence AAF04470.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAI20215.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181E → D in AAF04470 (PubMed:10531035).Curated
Sequence conflicti51 – 511M → L in AAF04470 (PubMed:10531035).Curated
Sequence conflicti61 – 611E → K in AAF04470 (PubMed:10531035).Curated
Sequence conflicti96 – 961E → N in AAF04470 (PubMed:10531035).Curated
Sequence conflicti114 – 1141E → D in AAF04470 (PubMed:10531035).Curated
Sequence conflicti123 – 1231D → E in AAF04470 (PubMed:10531035).Curated
Sequence conflicti132 – 1321Y → S in AAF04470 (PubMed:10531035).Curated
Sequence conflicti139 – 1391M → L in AAF04470 (PubMed:10531035).Curated
Sequence conflicti143 – 1442SQ → WE in AAF04470 (PubMed:10531035).Curated
Sequence conflicti149 – 1524VAEG → LADR in AAF04470 (PubMed:10531035).Curated
Sequence conflicti287 – 2871R → G in AAF04470 (PubMed:10531035).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti60 – 601R → Q.
Corresponds to variant rs3125818 [ dbSNP | Ensembl ].
VAR_049039
Natural varianti201 – 2011P → T.
Corresponds to variant rs2294639 [ dbSNP | Ensembl ].
VAR_022158

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF129536 mRNA. Translation: AAF04470.1. Different initiation.
AF233223 mRNA. Translation: AAF67153.1.
AK314989 mRNA. Translation: BAG37485.1.
AL031731 Genomic DNA. Translation: CAI20214.1.
AL031731 Genomic DNA. Translation: CAI20215.1. Sequence problems.
CH471130 Genomic DNA. Translation: EAW71696.1.
BC020880 mRNA. Translation: AAH20880.1.
CCDSiCCDS133.1.
RefSeqiNP_060908.1. NM_018438.5.
XP_005263505.1. XM_005263448.3.
XP_005263506.1. XM_005263449.3.
XP_005263508.1. XM_005263451.3.
XP_006710634.1. XM_006710571.2.
XP_011539534.1. XM_011541232.1.
UniGeneiHs.464419.

Genome annotation databases

EnsembliENST00000376753; ENSP00000365944; ENSG00000116663.
GeneIDi26270.
KEGGihsa:26270.
UCSCiuc001aso.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

hFBG2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF129536 mRNA. Translation: AAF04470.1. Different initiation.
AF233223 mRNA. Translation: AAF67153.1.
AK314989 mRNA. Translation: BAG37485.1.
AL031731 Genomic DNA. Translation: CAI20214.1.
AL031731 Genomic DNA. Translation: CAI20215.1. Sequence problems.
CH471130 Genomic DNA. Translation: EAW71696.1.
BC020880 mRNA. Translation: AAH20880.1.
CCDSiCCDS133.1.
RefSeqiNP_060908.1. NM_018438.5.
XP_005263505.1. XM_005263448.3.
XP_005263506.1. XM_005263449.3.
XP_005263508.1. XM_005263451.3.
XP_006710634.1. XM_006710571.2.
XP_011539534.1. XM_011541232.1.
UniGeneiHs.464419.

3D structure databases

ProteinModelPortaliQ9NRD1.
SMRiQ9NRD1. Positions 9-259.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117654. 622 interactions.
IntActiQ9NRD1. 4 interactions.
STRINGi9606.ENSP00000365944.

PTM databases

iPTMnetiQ9NRD1.
PhosphoSiteiQ9NRD1.

Polymorphism and mutation databases

BioMutaiFBXO6.
DMDMi24636846.

Proteomic databases

EPDiQ9NRD1.
MaxQBiQ9NRD1.
PaxDbiQ9NRD1.
PRIDEiQ9NRD1.

Protocols and materials databases

DNASUi26270.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000376753; ENSP00000365944; ENSG00000116663.
GeneIDi26270.
KEGGihsa:26270.
UCSCiuc001aso.4. human.

Organism-specific databases

CTDi26270.
GeneCardsiFBXO6.
HGNCiHGNC:13585. FBXO6.
HPAiHPA051175.
MIMi605647. gene.
neXtProtiNX_Q9NRD1.
PharmGKBiPA28046.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IK6V. Eukaryota.
ENOG4111MF5. LUCA.
GeneTreeiENSGT00390000003865.
HOGENOMiHOG000231084.
HOVERGENiHBG003593.
InParanoidiQ9NRD1.
KOiK10100.
OMAiEMCLKSQ.
OrthoDBiEOG7DRJ3R.
PhylomeDBiQ9NRD1.
TreeFamiTF320527.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-HSA-390471. Association of TriC/CCT with target proteins during biosynthesis.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiFBXO6. human.
GeneWikiiFBXO6.
GenomeRNAii26270.
NextBioi48557.
PROiQ9NRD1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NRD1.
CleanExiHS_FBXO6.
ExpressionAtlasiQ9NRD1. baseline and differential.
GenevisibleiQ9NRD1. HS.

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. "cDNA cloning and expression analysis of new members of the mammalian F-box protein family."
    Ilyin G.P., Rialland M., Pigeon C., Guguen-Guillouzo C.
    Genomics 67:40-47(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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: Lung.
  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. 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: Kidney.
  7. "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: FUNCTION, SUGAR-BINDING, INTERACTION WITH CUL1, MUTAGENESIS OF 241-TYR-TRP-242.
  8. "The F box protein Fbx6 regulates Chk1 stability and cellular sensitivity to replication stress."
    Zhang Y.-W., Brognard J., Coughlin C., You Z., Dolled-Filhart M., Aslanian A., Manning G., Abraham R.T., Hunter T.
    Mol. Cell 35:442-453(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A SCF PROTEIN LIGASE COMPLEX, INTERACTION WITH CHEK1.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFBX6_HUMAN
AccessioniPrimary (citable) accession number: Q9NRD1
Secondary accession number(s): B1AK42, B2RC88, Q9UKT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: October 1, 2000
Last modified: May 11, 2016
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. 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.