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F-box/WD repeat-containing protein 7 (F-box and WD-40 domain-containing protein 7) (Protein archipelago)

 FBXW7_DROME             Reviewed;        1326 AA.
Q9VZF4; A4V1G6;
01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
16-JAN-2019, entry version 151.
RecName: Full=F-box/WD repeat-containing protein 7;
AltName: Full=F-box and WD-40 domain-containing protein 7;
AltName: Full=Protein archipelago;
Name=ago {ECO:0000312|EMBL:AAL28848.1}; ORFNames=CG15010;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1] {ECO:0000305, ECO:0000312|EMBL:AAF47869.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2] {ECO:0000305, ECO:0000312|EMBL:AAF47869.1}
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[3] {ECO:0000305, ECO:0000312|EMBL:AAL28848.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
TISSUE=Embryo {ECO:0000269|PubMed:12537569};
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
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.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[4] {ECO:0000305}
FUNCTION, INTERACTION WITH CYCE, TISSUE SPECIFICITY, AND MUTAGENESIS
OF ALA-1117 AND GLY-1131.
PubMed=11565033; DOI=10.1038/35095068;
Moberg K.H., Bell D.W., Wahrer D.C.R., Haber D.A., Hariharan I.K.;
"Archipelago regulates cyclin E levels in Drosophila and is mutated in
human cancer cell lines.";
Nature 413:311-316(2001).
[5] {ECO:0000305}
FUNCTION, INTERACTION WITH MYC, AND TISSUE SPECIFICITY.
PubMed=15182669; DOI=10.1016/j.cub.2004.04.040;
Moberg K.H., Mukherjee A., Veraksa A., Artavanis-Tsakonas S.,
Hariharan I.K.;
"The Drosophila F box protein archipelago regulates dMyc protein
levels in vivo.";
Curr. Biol. 14:965-974(2004).
[6] {ECO:0000305}
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=15175253; DOI=10.1242/dev.01172;
Shcherbata H.R., Althauser C., Findley S.D., Ruohola-Baker H.;
"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.";
Development 131:3169-3181(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-813 AND SER-825, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
[8]
INTERACTION WITH MYC AND PUF, AND DISRUPTION PHENOTYPE.
PubMed=24173801; DOI=10.1242/dev.096941;
Li L., Anderson S., Secombe J., Eisenman R.N.;
"The Drosophila ubiquitin-specific protease Puffyeye regulates dMyc-
mediated growth.";
Development 140:4776-4787(2013).
-!- FUNCTION: 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 (By similarity). Probably recognizes and binds to
phosphorylated target proteins (By similarity). In the wing and
eye, negatively regulates cell growth and proliferation by
mediating the degradation of Myc and cyclin E, respectively
(PubMed:11565033, PubMed:15182669). Required for endocycles, but
not mitosis in follicle cell epithelium (PubMed:15175253).
{ECO:0000250, ECO:0000269|PubMed:11565033,
ECO:0000269|PubMed:15175253, ECO:0000269|PubMed:15182669,
ECO:0000269|PubMed:24173801}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Part of a SCF E3 ubiquitin-protein ligase complex.
Interacts with Myc and puf (PubMed:15182669, PubMed:24173801).
Interacts with CycE (PubMed:11565033).
{ECO:0000269|PubMed:11565033, ECO:0000269|PubMed:15182669,
ECO:0000269|PubMed:24173801}.
-!- INTERACTION:
Q9W4S7:Myc; NbExp=2; IntAct=EBI-138334, EBI-120162;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in follicle cell epithelium and
imaginal disks, particularly in the morphogenetic furrow.
{ECO:0000269|PubMed:11565033, ECO:0000269|PubMed:15175253,
ECO:0000269|PubMed:15182669}.
-!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the posterior
compartment of the larval wing disk increases cell size in the
posterior compartment of the adult wing, resulting in an increase
in the size of the posterior compartment as well as an increase in
the ratio between the posterior and anterior areas.
{ECO:0000269|PubMed:24173801}.
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EMBL; AE014296; AAF47869.1; -; Genomic_DNA.
EMBL; AE014296; AAG22246.1; -; Genomic_DNA.
EMBL; AE014296; AAG22247.1; -; Genomic_DNA.
EMBL; AY061300; AAL28848.1; -; mRNA.
EMBL; AY075401; AAL68231.1; -; mRNA.
RefSeq; NP_523922.1; NM_079198.3.
RefSeq; NP_728964.1; NM_168072.2.
RefSeq; NP_728965.1; NM_168073.2.
UniGene; Dm.2559; -.
ProteinModelPortal; Q9VZF4; -.
SMR; Q9VZF4; -.
BioGrid; 63994; 59.
DIP; DIP-32477N; -.
IntAct; Q9VZF4; 12.
STRING; 7227.FBpp0073101; -.
iPTMnet; Q9VZF4; -.
PaxDb; Q9VZF4; -.
PRIDE; Q9VZF4; -.
EnsemblMetazoa; FBtr0073245; FBpp0073101; FBgn0041171.
EnsemblMetazoa; FBtr0073246; FBpp0073102; FBgn0041171.
EnsemblMetazoa; FBtr0073247; FBpp0073103; FBgn0041171.
GeneID; 38516; -.
KEGG; dme:Dmel_CG15010; -.
UCSC; CG15010-RA; d. melanogaster.
CTD; 38516; -.
FlyBase; FBgn0041171; ago.
eggNOG; KOG0274; Eukaryota.
eggNOG; ENOG410XRWX; LUCA.
GeneTree; ENSGT00940000154986; -.
InParanoid; Q9VZF4; -.
KO; K10260; -.
OMA; EEICTCQ; -.
OrthoDB; 666965at2759; -.
Reactome; R-DME-8951664; Neddylation.
Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SignaLink; Q9VZF4; -.
UniPathway; UPA00143; -.
GenomeRNAi; 38516; -.
PRO; PR:Q9VZF4; -.
Proteomes; UP000000803; Chromosome 3L.
Bgee; FBgn0041171; Expressed in 27 organ(s), highest expression level in embryo.
Genevisible; Q9VZF4; DM.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:FlyBase.
GO; GO:0030332; F:cyclin binding; TAS:FlyBase.
GO; GO:1990381; F:ubiquitin-specific protease binding; IPI:UniProtKB.
GO; GO:0007411; P:axon guidance; IMP:FlyBase.
GO; GO:0035147; P:branch fusion, open tracheal system; IMP:FlyBase.
GO; GO:0071456; P:cellular response to hypoxia; IMP:FlyBase.
GO; GO:0042023; P:DNA endoreduplication; IMP:FlyBase.
GO; GO:1900038; P:negative regulation of cellular response to hypoxia; IMP:FlyBase.
GO; GO:0060253; P:negative regulation of glial cell proliferation; IGI:FlyBase.
GO; GO:0045926; P:negative regulation of growth; IMP:FlyBase.
GO; GO:0045571; P:negative regulation of imaginal disc growth; IMP:FlyBase.
GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
GO; GO:1903146; P:regulation of autophagy of mitochondrion; IMP:FlyBase.
GO; GO:0007096; P:regulation of exit from mitosis; TAS:FlyBase.
GO; GO:0007088; P:regulation of mitotic nuclear division; IMP:FlyBase.
GO; GO:0030162; P:regulation of proteolysis; TAS:FlyBase.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; ISS:FlyBase.
GO; GO:0060438; P:trachea development; IMP:FlyBase.
GO; GO:0007419; P:ventral cord development; HMP:FlyBase.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR036047; F-box-like_dom_sf.
InterPro; IPR001810; F-box_dom.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF12937; F-box-like; 1.
Pfam; PF00400; WD40; 7.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00256; FBOX; 1.
SMART; SM00320; WD40; 7.
SUPFAM; SSF50978; SSF50978; 1.
SUPFAM; SSF81383; SSF81383; 1.
PROSITE; PS50181; FBOX; 1.
PROSITE; PS00678; WD_REPEATS_1; 5.
PROSITE; PS50082; WD_REPEATS_2; 7.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
Cell cycle; Complete proteome; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Ubl conjugation pathway; WD repeat.
CHAIN 1 1326 F-box/WD repeat-containing protein 7.
/FTId=PRO_0000050996.
DOMAIN 889 935 F-box. {ECO:0000255|PROSITE-
ProRule:PRU00080}.
REPEAT 992 1030 WD 1. {ECO:0000255}.
REPEAT 1033 1070 WD 2. {ECO:0000255}.
REPEAT 1073 1110 WD 3. {ECO:0000255}.
REPEAT 1113 1150 WD 4. {ECO:0000255}.
REPEAT 1153 1190 WD 5. {ECO:0000255}.
REPEAT 1193 1232 WD 6. {ECO:0000255}.
REPEAT 1236 1273 WD 7. {ECO:0000255}.
COMPBIAS 337 580 Ser-rich.
MOD_RES 813 813 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 825 825 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MUTAGEN 1117 1117 A->V: In ago-4; increased cell
proliferation.
{ECO:0000269|PubMed:11565033}.
MUTAGEN 1131 1131 G->E: In ago-3; increased cell
proliferation and decrease in ability to
bind CycE. {ECO:0000269|PubMed:11565033}.
SEQUENCE 1326 AA; 141361 MW; 3F42C873CFA3027F CRC64;
MERGCPAASS ESVTSAGERT QSAVTSSTST WVKSQASTSR KTEASEESGL GAVDAEVGAG
REAFVSMSTL REDVEDVCVS SNSQHGFAVV LDDESSTFEI SSSNSLPTSA GAASTVGVVA
VDDSSSTDTL NGGHPDLGHP ASSEHSRQGF FNEDNEDPPV VCLINDDDDD EEPEPEEDDE
EELIEDEDED AVDIVTGAIS CPNTSQLALA DGTIMAADGS KIFLETPVVE EAQPHPGQVV
TTGSQSELTG KPKRLSDEFL LGEEDQAENL ALGRCIKSEP VNPVDDNPSE GDDGATCFSL
HDRLMSVRLK QMSLTANTVS NPSPAASANA AAPEEASTSN SSSTSSSALS RADIESMDLI
ERRDFETEQR LTGGIILRTS SMVSQNKLNL SLIKSMAGGS KAANGSGTAN SDDWPSSSNG
RTVSSDSKYT YKDLSTTPTS SRKYTNSRLS KSTAKLNLGS SLGASSCSQH RSGSSSTSKS
MESSTSCTGA ARTDVYTNTN SNDYPSLAPT TSGSSTSGGS CQQDQEENVS ASVSYSSVGS
QTSQESGCSR TTAINPTAAC STGSACLGDS QASTSASTSS GAGASNRCQY ATTSTTKAAR
QVNASAQTQE RFLTRSNPPA ASGAGSVGAN PTASVRQRRN GSSDVVHLEV VVEEGAGGGD
GGVVEPGDFS AEEPWANCDE ENNCSDLEEI CTCQNGNGSS YGGSNASLSE TFDMDAMDPD
EPISLSLSSA SAGFTEYSLT NPSSLMSHQR KRKFNEGRLL DGGDYSVTIS SSGEVGGPGS
GVSDNCRKRI AYDFASTPRS SQHLGPTAVL SVTPSSHLTS STPGSALGRR TPRSVPSRDN
PPPELQHWLA QFQRWSHVER LLALDRLIDH CDPSQVRHMM KVIEPQFQRD FISLLPRELA
LFVLSYLEPK DLLRAAQTCR SWRFLCDDNL LWKEKCRKAQ ILAEPRSDRP KRGRDGNMPP
IASPWKAAYM RQHIIEMNWR SRPVRKPKVL KGHDDHVITC LQFSGNRIVS GSDDNTLKVW
SAVNGKCLRT LVGHTGGVWS SQMSGNIIIS GSTDRTLKVW DMDSGACVHT LQGHTSTVRC
MHLHGSKVVS GSRDATLRVW DIEQGSCLHV LVGHLAAVRC VQYDGKLIVS GAYDYMVKIW
HPERQECLHT LQGHTNRVYS LQFDGLHVVS GSLDTSIRVW DVETGNCKHT LMGHQSLTSG
MELRQNILVS GNADSTVKVW DITTGQCLQT LSGPNKHHSA VTCLQFNSRF VVTSSDDGTV
KLWDVKTGDF IRNLVALDSG GSGGVVWRIR ANDTKLICAV GSRNGTEETK LMVLDFDVEG
ACVKCS


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Pathways :
WP1689: Porphyrin and chlorophyll metabolism
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation
WP1675: Nitrogen metabolism
WP1676: Non-homologous end-joining

Related Genes :
[FBXW7 FBW7 FBX30 SEL10] F-box/WD repeat-containing protein 7 (Archipelago homolog) (hAgo) (F-box and WD-40 domain-containing protein 7) (F-box protein FBX30) (SEL-10) (hCdc4)
[Fbxw7 Fbw7 Fbwd6 Fbxw6] F-box/WD repeat-containing protein 7 (F-box and WD-40 domain-containing protein 7) (F-box protein FBW7) (F-box protein Fbxw6) (F-box-WD40 repeat protein 6) (SEL-10)
[FBXW8 FBW6 FBW8 FBX29 FBXO29 FBXW6] F-box/WD repeat-containing protein 8 (F-box and WD-40 domain-containing protein 8) (F-box only protein 29)
[FBXW11 BTRCP2 FBW1B FBXW1B KIAA0696] F-box/WD repeat-containing protein 11 (F-box and WD repeats protein beta-TrCP2) (F-box/WD repeat-containing protein 1B) (Homologous to Slimb protein) (HOS)
[FBXW5 FBW5 PP3971] F-box/WD repeat-containing protein 5 (F-box and WD-40 domain-containing protein 5)
[Fbxw5 Fbw5] F-box/WD repeat-containing protein 5 (F-box and WD-40 domain-containing protein 5)
[BTRC BTRCP FBW1A FBXW1A] F-box/WD repeat-containing protein 1A (E3RSIkappaB) (Epididymis tissue protein Li 2a) (F-box and WD repeats protein beta-TrCP) (pIkappaBalpha-E3 receptor subunit)
[Fbxw7] F-box/WD repeat-containing protein 7
[FBXW4 FBW4 SHFM3] F-box/WD repeat-containing protein 4 (Dactylin) (F-box and WD-40 domain-containing protein 4)
[sel-10 egl-41 F55B12.3] F-box/WD repeat-containing protein sel-10 (Egg laying defective protein 41) (Suppressor/enhancer of lin-12 protein 10)
[KDM2A CXXC8 FBL7 FBXL11 JHDM1A KIAA1004] Lysine-specific demethylase 2A (EC 1.14.11.27) (CXXC-type zinc finger protein 8) (F-box and leucine-rich repeat protein 11) (F-box protein FBL7) (F-box protein Lilina) (F-box/LRR-repeat protein 11) (JmjC domain-containing histone demethylation protein 1A) ([Histone-H3]-lysine-36 demethylase 1A)
[mec-15 T01E8.4] F-box/WD repeat-containing protein mec-15 (Mechanosensory abnormality protein 15)
[WRAP53 TCAB1 WDR79] Telomerase Cajal body protein 1 (WD repeat-containing protein 79) (WD40 repeat-containing protein antisense to TP53 gene) (WRAP53beta)
[KDM2B CXXC2 FBL10 FBXL10 JHDM1B PCCX2] Lysine-specific demethylase 2B (EC 1.14.11.27) (CXXC-type zinc finger protein 2) (F-box and leucine-rich repeat protein 10) (F-box protein FBL10) (F-box/LRR-repeat protein 10) (JmjC domain-containing histone demethylation protein 1B) (Jumonji domain-containing EMSY-interactor methyltransferase motif protein) (Protein JEMMA) (Protein-containing CXXC domain 2) ([Histone-H3]-lysine-36 demethylase 1B)
[FBXW7 FBW7] F-box/WD repeat-containing protein 7 (F-box and WD-40 domain-containing protein 7)
[DCAF7 HAN11 WDR68] DDB1- and CUL4-associated factor 7 (WD repeat-containing protein 68) (WD repeat-containing protein An11 homolog)
[Fbxw5] F-box/WD repeat-containing protein 5 (F-box and WD-40 domain-containing protein 5)
[RACK1A ARCA At1g18080 T10F20.9 T10O22.6] Receptor for activated C kinase 1A (Guanine nucleotide-binding protein subunit beta-like protein A) (WD-40 repeat auxin-dependent protein ARCA)
[Kdm2b Fbl10 Fbxl10 Jhdm1b Kiaa3014] Lysine-specific demethylase 2B (EC 1.14.11.27) (F-box and leucine-rich repeat protein 10) (F-box protein FBL10) (F-box/LRR-repeat protein 10) (JmjC domain-containing histone demethylation protein 1B) ([Histone-H3]-lysine-36 demethylase 1B)
[GRR1 CAT80 COT2 YJR090C J1885] SCF E3 ubiquitin ligase complex F-box protein GRR1 (F-box and leucine-rich repeat protein GRR1) (F-box/LRR-repeat protein GRR1)
[WDFY1 FENS1 KIAA1435 WDF1 ZFYVE17] WD repeat and FYVE domain-containing protein 1 (FYVE domain-containing protein localized to endosomes 1) (FENS-1) (Phosphoinositide-binding protein 1) (WD40- and FYVE domain-containing protein 1) (Zinc finger FYVE domain-containing protein 17)
[Kdm2a Fbxl11 Jhdm1a Kiaa1004] Lysine-specific demethylase 2A (EC 1.14.11.27) (F-box and leucine-rich repeat protein 11) (F-box/LRR-repeat protein 11) (JmjC domain-containing histone demethylation protein 1A) ([Histone-H3]-lysine-36 demethylase 1A)
[VIP3 SKI8 At4g29830 F27B13.70] WD repeat-containing protein VIP3 (Protein BOUQUET-1) (boq-1) (Protein SKI8 homolog) (Protein VERNALIZATION INDEPENDENCE 3) (Protein ZWERGERL) (zwg)
[WDR45B WDR45L WIPI3] WD repeat domain phosphoinositide-interacting protein 3 (WIPI-3) (WD repeat-containing protein 45-like) (WDR45-like protein) (WD repeat-containing protein 45B) (WIPI49-like protein)
[WDR11 BRWD2 KIAA1351 WDR15] WD repeat-containing protein 11 (Bromodomain and WD repeat-containing protein 2) (WD repeat-containing protein 15)
[WDR45 WDRX1 WDRXI4 WIPI4 JM5] WD repeat domain phosphoinositide-interacting protein 4 (WIPI-4) (WD repeat-containing protein 45)
[FBXL17 FBL17 FBX13 FBXO13] F-box/LRR-repeat protein 17 (F-box and leucine-rich repeat protein 17) (F-box only protein 13)
[Fbxo6 Fbs2 Fbxo6b] F-box only protein 6 (F-box only protein 6b) (F-box protein that recognizes sugar chains 2) (F-box/G-domain protein 2)
[SKP2 FBXL1] S-phase kinase-associated protein 2 (Cyclin-A/CDK2-associated protein p45) (F-box protein Skp2) (F-box/LRR-repeat protein 1) (p45skp2)
[pop2 sud1 SPAC4D7.03] WD repeat-containing protein pop2 (Proteolysis factor sud1)

Bibliography :
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