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Protein

F-box/WD repeat-containing protein 7

Gene

ago

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably recognizes and binds to phosphorylated target proteins (By similarity). Involved in the degradation of cyclin E and dm/Myc. Required for endocycles, but not mitosis in follicle cell epithelium.By similarity3 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

  • cyclin binding Source: FlyBase

GO - Biological processi

  • axon guidance Source: FlyBase
  • branch fusion, open tracheal system Source: FlyBase
  • cellular response to hypoxia Source: FlyBase
  • DNA endoreduplication Source: FlyBase
  • negative regulation of cellular response to hypoxia Source: FlyBase
  • negative regulation of cyclin-dependent protein serine/threonine kinase by cyclin degradation Source: FlyBase
  • negative regulation of glial cell proliferation Source: FlyBase
  • negative regulation of growth Source: FlyBase
  • protein ubiquitination Source: UniProtKB-UniPathway
  • regulation of exit from mitosis Source: FlyBase
  • regulation of mitophagy Source: FlyBase
  • regulation of mitotic nuclear division Source: FlyBase
  • regulation of proteolysis Source: FlyBase
  • SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Source: FlyBase
  • trachea development Source: FlyBase
  • ventral cord development Source: FlyBase
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-DME-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ9VZF4.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
F-box/WD repeat-containing protein 7
Alternative name(s):
F-box and WD-40 domain-containing protein 7
Protein archipelago
Gene namesi
Name:agoImported
ORF Names:CG15010
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0041171. ago.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1117 – 11171A → V in ago-4; increased cell proliferation. 1 Publication
Mutagenesisi1131 – 11311G → E in ago-3; increased cell proliferation and decrease in ability to bind CycE. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13261326F-box/WD repeat-containing protein 7PRO_0000050996Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei813 – 8131Phosphothreonine1 Publication
Modified residuei825 – 8251Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9VZF4.
PRIDEiQ9VZF4.

PTM databases

iPTMnetiQ9VZF4.

Expressioni

Tissue specificityi

Expressed in follicle cell epithelium and imaginal disks, particularly in the morphogenetic furrow.3 Publications

Gene expression databases

BgeeiQ9VZF4.
GenevisibleiQ9VZF4. DM.

Interactioni

Subunit structurei

Part of a SCF E3 ubiquitin-protein ligase complex. Interacts with dm and CycE.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
dmQ9W4S72EBI-138334,EBI-120162

GO - Molecular functioni

  • cyclin binding Source: FlyBase

Protein-protein interaction databases

BioGridi63994. 44 interactions.
DIPiDIP-32477N.
IntActiQ9VZF4. 11 interactions.
MINTiMINT-901835.
STRINGi7227.FBpp0073101.

Structurei

3D structure databases

ProteinModelPortaliQ9VZF4.
SMRiQ9VZF4. Positions 874-1319.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini889 – 93547F-boxPROSITE-ProRule annotationAdd
BLAST
Repeati992 – 103039WD 1Sequence analysisAdd
BLAST
Repeati1033 – 107038WD 2Sequence analysisAdd
BLAST
Repeati1073 – 111038WD 3Sequence analysisAdd
BLAST
Repeati1113 – 115038WD 4Sequence analysisAdd
BLAST
Repeati1153 – 119038WD 5Sequence analysisAdd
BLAST
Repeati1193 – 123240WD 6Sequence analysisAdd
BLAST
Repeati1236 – 127338WD 7Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi337 – 580244Ser-richAdd
BLAST

Sequence similaritiesi

Contains 1 F-box domain.PROSITE-ProRule annotation
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG0274. Eukaryota.
ENOG410XRWX. LUCA.
GeneTreeiENSGT00760000119106.
InParanoidiQ9VZF4.
KOiK10260.
OMAiDLEEICT.
OrthoDBiEOG7VX8VF.

Family and domain databases

Gene3Di2.130.10.10. 4 hits.
InterProiIPR001810. F-box_dom.
IPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF12937. F-box-like. 1 hit.
PF00400. WD40. 7 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00256. FBOX. 1 hit.
SM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
SSF81383. SSF81383. 1 hit.
PROSITEiPS50181. FBOX. 1 hit.
PS00678. WD_REPEATS_1. 5 hits.
PS50082. WD_REPEATS_2. 7 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VZF4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERGCPAASS ESVTSAGERT QSAVTSSTST WVKSQASTSR KTEASEESGL
60 70 80 90 100
GAVDAEVGAG REAFVSMSTL REDVEDVCVS SNSQHGFAVV LDDESSTFEI
110 120 130 140 150
SSSNSLPTSA GAASTVGVVA VDDSSSTDTL NGGHPDLGHP ASSEHSRQGF
160 170 180 190 200
FNEDNEDPPV VCLINDDDDD EEPEPEEDDE EELIEDEDED AVDIVTGAIS
210 220 230 240 250
CPNTSQLALA DGTIMAADGS KIFLETPVVE EAQPHPGQVV TTGSQSELTG
260 270 280 290 300
KPKRLSDEFL LGEEDQAENL ALGRCIKSEP VNPVDDNPSE GDDGATCFSL
310 320 330 340 350
HDRLMSVRLK QMSLTANTVS NPSPAASANA AAPEEASTSN SSSTSSSALS
360 370 380 390 400
RADIESMDLI ERRDFETEQR LTGGIILRTS SMVSQNKLNL SLIKSMAGGS
410 420 430 440 450
KAANGSGTAN SDDWPSSSNG RTVSSDSKYT YKDLSTTPTS SRKYTNSRLS
460 470 480 490 500
KSTAKLNLGS SLGASSCSQH RSGSSSTSKS MESSTSCTGA ARTDVYTNTN
510 520 530 540 550
SNDYPSLAPT TSGSSTSGGS CQQDQEENVS ASVSYSSVGS QTSQESGCSR
560 570 580 590 600
TTAINPTAAC STGSACLGDS QASTSASTSS GAGASNRCQY ATTSTTKAAR
610 620 630 640 650
QVNASAQTQE RFLTRSNPPA ASGAGSVGAN PTASVRQRRN GSSDVVHLEV
660 670 680 690 700
VVEEGAGGGD GGVVEPGDFS AEEPWANCDE ENNCSDLEEI CTCQNGNGSS
710 720 730 740 750
YGGSNASLSE TFDMDAMDPD EPISLSLSSA SAGFTEYSLT NPSSLMSHQR
760 770 780 790 800
KRKFNEGRLL DGGDYSVTIS SSGEVGGPGS GVSDNCRKRI AYDFASTPRS
810 820 830 840 850
SQHLGPTAVL SVTPSSHLTS STPGSALGRR TPRSVPSRDN PPPELQHWLA
860 870 880 890 900
QFQRWSHVER LLALDRLIDH CDPSQVRHMM KVIEPQFQRD FISLLPRELA
910 920 930 940 950
LFVLSYLEPK DLLRAAQTCR SWRFLCDDNL LWKEKCRKAQ ILAEPRSDRP
960 970 980 990 1000
KRGRDGNMPP IASPWKAAYM RQHIIEMNWR SRPVRKPKVL KGHDDHVITC
1010 1020 1030 1040 1050
LQFSGNRIVS GSDDNTLKVW SAVNGKCLRT LVGHTGGVWS SQMSGNIIIS
1060 1070 1080 1090 1100
GSTDRTLKVW DMDSGACVHT LQGHTSTVRC MHLHGSKVVS GSRDATLRVW
1110 1120 1130 1140 1150
DIEQGSCLHV LVGHLAAVRC VQYDGKLIVS GAYDYMVKIW HPERQECLHT
1160 1170 1180 1190 1200
LQGHTNRVYS LQFDGLHVVS GSLDTSIRVW DVETGNCKHT LMGHQSLTSG
1210 1220 1230 1240 1250
MELRQNILVS GNADSTVKVW DITTGQCLQT LSGPNKHHSA VTCLQFNSRF
1260 1270 1280 1290 1300
VVTSSDDGTV KLWDVKTGDF IRNLVALDSG GSGGVVWRIR ANDTKLICAV
1310 1320
GSRNGTEETK LMVLDFDVEG ACVKCS
Length:1,326
Mass (Da):141,361
Last modified:May 1, 2000 - v1
Checksum:i3F42C873CFA3027F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014296 Genomic DNA. Translation: AAF47869.1.
AE014296 Genomic DNA. Translation: AAG22246.1.
AE014296 Genomic DNA. Translation: AAG22247.1.
AY061300 mRNA. Translation: AAL28848.1.
AY075401 mRNA. Translation: AAL68231.1.
RefSeqiNP_523922.1. NM_079198.3.
NP_728964.1. NM_168072.2.
NP_728965.1. NM_168073.2.
UniGeneiDm.2559.

Genome annotation databases

EnsemblMetazoaiFBtr0073245; FBpp0073101; FBgn0041171.
FBtr0073246; FBpp0073102; FBgn0041171.
FBtr0073247; FBpp0073103; FBgn0041171.
GeneIDi38516.
KEGGidme:Dmel_CG15010.
UCSCiCG15010-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014296 Genomic DNA. Translation: AAF47869.1.
AE014296 Genomic DNA. Translation: AAG22246.1.
AE014296 Genomic DNA. Translation: AAG22247.1.
AY061300 mRNA. Translation: AAL28848.1.
AY075401 mRNA. Translation: AAL68231.1.
RefSeqiNP_523922.1. NM_079198.3.
NP_728964.1. NM_168072.2.
NP_728965.1. NM_168073.2.
UniGeneiDm.2559.

3D structure databases

ProteinModelPortaliQ9VZF4.
SMRiQ9VZF4. Positions 874-1319.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi63994. 44 interactions.
DIPiDIP-32477N.
IntActiQ9VZF4. 11 interactions.
MINTiMINT-901835.
STRINGi7227.FBpp0073101.

PTM databases

iPTMnetiQ9VZF4.

Proteomic databases

PaxDbiQ9VZF4.
PRIDEiQ9VZF4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0073245; FBpp0073101; FBgn0041171.
FBtr0073246; FBpp0073102; FBgn0041171.
FBtr0073247; FBpp0073103; FBgn0041171.
GeneIDi38516.
KEGGidme:Dmel_CG15010.
UCSCiCG15010-RA. d. melanogaster.

Organism-specific databases

CTDi38516.
FlyBaseiFBgn0041171. ago.

Phylogenomic databases

eggNOGiKOG0274. Eukaryota.
ENOG410XRWX. LUCA.
GeneTreeiENSGT00760000119106.
InParanoidiQ9VZF4.
KOiK10260.
OMAiDLEEICT.
OrthoDBiEOG7VX8VF.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-DME-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ9VZF4.

Miscellaneous databases

GenomeRNAii38516.
PROiQ9VZF4.

Gene expression databases

BgeeiQ9VZF4.
GenevisibleiQ9VZF4. DM.

Family and domain databases

Gene3Di2.130.10.10. 4 hits.
InterProiIPR001810. F-box_dom.
IPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF12937. F-box-like. 1 hit.
PF00400. WD40. 7 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00256. FBOX. 1 hit.
SM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
SSF81383. SSF81383. 1 hit.
PROSITEiPS50181. FBOX. 1 hit.
PS00678. WD_REPEATS_1. 5 hits.
PS50082. WD_REPEATS_2. 7 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley1 Publication.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley1 Publication.
    Tissue: Embryo1 Publication.
  4. "Archipelago regulates cyclin E levels in Drosophila and is mutated in human cancer cell lines."
    Moberg K.H., Bell D.W., Wahrer D.C.R., Haber D.A., Hariharan I.K.
    Nature 413:311-316(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CYCE, TISSUE SPECIFICITY, MUTAGENESIS OF ALA-1117 AND GLY-1131.
  5. "The Drosophila F box protein archipelago regulates dMyc protein levels in vivo."
    Moberg K.H., Mukherjee A., Veraksa A., Artavanis-Tsakonas S., Hariharan I.K.
    Curr. Biol. 14:965-974(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DM, TISSUE SPECIFICITY.
  6. "The mitotic-to-endocycle switch in Drosophila follicle cells is executed by Notch-dependent regulation of G1/S, G2/M and M/G1 cell-cycle transitions."
    Shcherbata H.R., Althauser C., Findley S.D., Ruohola-Baker H.
    Development 131:3169-3181(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  7. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-813 AND SER-825, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiFBXW7_DROME
AccessioniPrimary (citable) accession number: Q9VZF4
Secondary accession number(s): A4V1G6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: May 1, 2000
Last modified: June 8, 2016
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  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.