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Q8N3Y1 (FBXW8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
F-box/WD repeat-containing protein 8
Alternative name(s):
F-box and WD-40 domain-containing protein 8
F-box only protein 29
Gene names
Name:FBXW8
Synonyms:FBW6, FBW8, FBX29, FBXO29, FBXW6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length598 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Substrate-recognition component of a SCF-like E3 ubiquitin-protein ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. In complex with CUL7, mediates ubiquitination and consequent degradation of GORASP1, acting as a component of the ubiquitin ligase pathway that regulates Golgi morphogenesis and dendrite patterning in brain. Ref.7

Subunit structure

Part of a SCF-like complex consisting of CUL7, RBX1, SKP1, FBXW8 and GLMN isoform 1. Interacts with CUL7. Interacts with OBSL1, CUL1, CUL2, SKP1, CCT6B, PFDN5, CCT2, CCT3, CCT6A, CCT7, VBP1, CCDC8, ARF1, TRIP13, PDCD5 and GORASP1. Ref.4 Ref.5 Ref.6 Ref.7

Subcellular location

Cytoplasmperinuclear region. Golgi apparatus. Note: Colocalizes with CUL7 at the Golgi apparatus in neurons By similarity. Ref.7

Sequence similarities

Contains 1 F-box domain.

Contains 5 WD repeats.

Sequence caution

The sequence AAF03129.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAF03129.1 differs from that shown. Reason: Frameshift at positions 282 and 295.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MYCP011063EBI-914770,EBI-447544

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8N3Y1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8N3Y1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     41-106: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 598598F-box/WD repeat-containing protein 8
PRO_0000050997

Regions

Domain113 – 15947F-box
Repeat197 – 24549WD 1
Repeat254 – 29441WD 2
Repeat297 – 33640WD 3
Repeat430 – 47041WD 4
Repeat473 – 51038WD 5

Amino acid modifications

Modified residue11N-acetylmethionine Ref.8

Natural variations

Alternative sequence41 – 10666Missing in isoform 2.
VSP_008501
Natural variant1921R → Q. Ref.1 Ref.3
Corresponds to variant rs4076700 [ dbSNP | Ensembl ].
VAR_060326
Natural variant2111T → A.
Corresponds to variant rs36021180 [ dbSNP | Ensembl ].
VAR_057597
Natural variant5361T → M.
Corresponds to variant rs3741466 [ dbSNP | Ensembl ].
VAR_057598
Natural variant5631V → M.
Corresponds to variant rs56350562 [ dbSNP | Ensembl ].
VAR_062096

Experimental info

Sequence conflict461G → S in AAH37296. Ref.3
Sequence conflict581R → G in AAH37296. Ref.3
Sequence conflict3801L → I in AAH37296. Ref.3
Sequence conflict5101E → K in AAF03129. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: 03B3C283BA46DB6B

FASTA59867,394
        10         20         30         40         50         60 
MDDYSLDEFR RRWQEELAQA QAPKKRRRPE AAERRARRPE VGSGRGEQAS GDPALAQRLL 

        70         80         90        100        110        120 
EGAGRPPAAR ATRAEGQDVA SRSRSPLARE GAGGGEQLVD QLIRDLNEMN DVPFFDIQLP 

       130        140        150        160        170        180 
YELAINIFQY LDRKELGRCA QVSKTWKVIA EDEVLWYRLC QQEGHLPDSS ISDYSCWKLI 

       190        200        210        220        230        240 
FQECRAKEHM LRTNWKNRKG AVSELEHVPD TVLCDVHSHD GVVIAGYTSG DVRVWDTRTW 

       250        260        270        280        290        300 
DYVAPFLESE DEEDEPGMQP NVSFVRINSS LAVAAYEDGF LNIWDLRTGK YPVHRFEHDA 

       310        320        330        340        350        360 
RIQALALSQD DATVATASAF DVVMLSPNEE GYWQIAAEFE VPKLVQYLEI VPETRRYPVA 

       370        380        390        400        410        420 
VAAAGDLMYL LKAEDSARTL LYAHGPPVTC LDVSANQVAF GVQGLGWVYE GSKILVYSLE 

       430        440        450        460        470        480 
AGRRLLKLGN VLRDFTCVNL SDSPPNLMVS GNMDGRVRIH DLRSGNIALS LSAHQLRVSA 

       490        500        510        520        530        540 
VQMDDWKIVS GGEEGLVSVW DYRMNQKLWE VYSGHPVQHI SFSSHSLITA NVPYQTVMRN 

       550        560        570        580        590 
ADLDSFTTHR RHRGLIRAYE FAVDQLAFQS PLPVCRSSCD AMATHYYDLA LAFPYNHV 

« Hide

Isoform 2 [UniParc].

Checksum: 921550273E26D2F2
Show »

FASTA53260,705

References

« Hide '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] (ISOFORM 2), VARIANT GLN-192.
[2]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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] (ISOFORM 1), VARIANT GLN-192.
Tissue: Brain.
[4]"CUL7: a DOC domain-containing cullin selectively binds Skp1.Fbx29 to form an SCF-like complex."
Dias D.C., Dolios G., Wang R., Pan Z.Q.
Proc. Natl. Acad. Sci. U.S.A. 99:16601-16606(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN SCF-LIKE COMPLEX.
[5]"Targeted disruption of p185/Cul7 gene results in abnormal vascular morphogenesis."
Arai T., Kasper J.S., Skaar J.R., Ali S.H., Takahashi C., DeCaprio J.A.
Proc. Natl. Acad. Sci. U.S.A. 100:9855-9860(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH CUL7; SKP1; RBX1 AND GLMN.
[6]"PARC and CUL7 form atypical cullin RING ligase complexes."
Skaar J.R., Florens L., Tsutsumi T., Arai T., Tron A., Swanson S.K., Washburn M.P., DeCaprio J.A.
Cancer Res. 67:2006-2014(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CUL7.
[7]"An OBSL1-Cul7Fbxw8 ubiquitin ligase signaling mechanism regulates Golgi morphology and dendrite patterning."
Litterman N., Ikeuchi Y., Gallardo G., O'Connell B.C., Sowa M.E., Gygi S.P., Harper J.W., Bonni A.
PLoS Biol. 9:E1001060-E1001060(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH OBSL1; CUL1; CUL2; CUL7; SKP1; CCT6B; PFDN5; CCT2; CCT3; CCT6A; CCT7; VBP1; CCDC8; ARF1; TRIP13; PDCD5 AND GORASP1, SUBCELLULAR LOCATION.
[8]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF176707 mRNA. Translation: AAF03129.1. Sequence problems.
AC026368 Genomic DNA. No translation available.
AC083806 Genomic DNA. No translation available.
AC127164 Genomic DNA. No translation available.
BC037296 mRNA. Translation: AAH37296.1.
RefSeqNP_036306.1. NM_012174.1.
NP_699179.2. NM_153348.2.
UniGeneHs.624537.
Hs.696428.

3D structure databases

ProteinModelPortalQ8N3Y1.
SMRQ8N3Y1. Positions 119-558.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117645. 38 interactions.
DIPDIP-37970N.
IntActQ8N3Y1. 3 interactions.
MINTMINT-8415331.
STRING9606.ENSP00000310686.

PTM databases

PhosphoSiteQ8N3Y1.

Polymorphism databases

DMDM296434513.

Proteomic databases

PaxDbQ8N3Y1.
PRIDEQ8N3Y1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309909; ENSP00000310686; ENSG00000174989. [Q8N3Y1-1]
ENST00000455858; ENSP00000389144; ENSG00000174989. [Q8N3Y1-2]
GeneID26259.
KEGGhsa:26259.
UCSCuc001twf.1. human. [Q8N3Y1-2]
uc001twg.1. human. [Q8N3Y1-1]

Organism-specific databases

CTD26259.
GeneCardsGC12P117348.
H-InvDBHIX0026457.
HIX0037115.
HGNCHGNC:13597. FBXW8.
HPAHPA038851.
MIM609073. gene.
neXtProtNX_Q8N3Y1.
PharmGKBPA28039.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG115403.
HOGENOMHOG000112555.
HOVERGENHBG051597.
InParanoidQ8N3Y1.
KOK10264.
OMANIFQYLD.
OrthoDBEOG7N8ZV2.
PhylomeDBQ8N3Y1.
TreeFamTF332593.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkQ8N3Y1.

Gene expression databases

BgeeQ8N3Y1.
CleanExHS_FBXW8.
GenevestigatorQ8N3Y1.

Family and domain databases

Gene3D2.130.10.10. 2 hits.
InterProIPR001810. F-box_dom.
IPR011047. Quinonprotein_ADH-like_supfam.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF00646. F-box. 1 hit.
PF00400. WD40. 1 hit.
[Graphical view]
SMARTSM00256. FBOX. 1 hit.
SM00320. WD40. 5 hits.
[Graphical view]
SUPFAMSSF50998. SSF50998. 2 hits.
SSF81383. SSF81383. 1 hit.
PROSITEPS50181. FBOX. 1 hit.
PS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFBXW8. human.
GeneWikiFBXW8.
GenomeRNAi26259.
NextBio48503.
PROQ8N3Y1.
SOURCESearch...

Entry information

Entry nameFBXW8_HUMAN
AccessionPrimary (citable) accession number: Q8N3Y1
Secondary accession number(s): Q9UK95
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: May 18, 2010
Last modified: March 19, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM