ID CCNE_DROME Reviewed; 709 AA.
AC P54733; Q24479; Q95RP5; Q9V3B3; Q9V456;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 27-MAR-2024, entry version 193.
DE RecName: Full=G1/S-specific cyclin-E;
DE Short=DmCycE;
GN Name=CycE; ORFNames=CG3938;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS I AND II), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=8187637; DOI=10.1242/dev.119.3.673;
RA Richardson H.E., O'Keefe L.V., Reed S.I., Saint R.;
RT "A Drosophila G1-specific cyclin E homolog exhibits different modes of
RT expression during embryogenesis.";
RL Development 119:673-690(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10471707; DOI=10.1093/genetics/153.1.179;
RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T.,
RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A.,
RA Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R.,
RA Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K.,
RA Celniker S.E., Rubin G.M.;
RT "An exploration of the sequence of a 2.9-Mb region of the genome of
RT Drosophila melanogaster: the Adh region.";
RL Genetics 153:179-219(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM II).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP FUNCTION, AND INTERACTION WITH AGO.
RX PubMed=11565033; DOI=10.1038/35095068;
RA Moberg K.H., Bell D.W., Wahrer D.C.R., Haber D.A., Hariharan I.K.;
RT "Archipelago regulates cyclin E levels in Drosophila and is mutated in
RT human cancer cell lines.";
RL Nature 413:311-316(2001).
RN [7]
RP INTERACTION WITH Z600.
RX PubMed=17431409; DOI=10.1038/sj.embor.7400948;
RA Gawlinski P., Nikolay R., Goursot C., Lawo S., Chaurasia B., Herz H.M.,
RA Kussler-Schneider Y., Ruppert T., Mayer M., Grosshans J.;
RT "The Drosophila mitotic inhibitor Fruehstart specifically binds to the
RT hydrophobic patch of cyclins.";
RL EMBO Rep. 8:490-496(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-115; SER-117;
RP SER-129; SER-187; SER-192; SER-195 AND SER-198, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Essential for the control of the cell cycle at the G1/S
CC (start) transition. Targeted by archipelago for degradation by the SFC
CC ubiquitin ligase complex. {ECO:0000269|PubMed:11565033,
CC ECO:0000269|PubMed:8187637}.
CC -!- SUBUNIT: Interacts with a member of the CDK2/CDK protein kinases to
CC form a serine/threonine kinase holoenzyme complex (PubMed:11565033).
CC The cyclin subunit imparts substrate specificity to the complex
CC (PubMed:11565033). Interacts (via C-terminus) with Z600 (via C-
CC terminus) (PubMed:17431409). {ECO:0000269|PubMed:11565033,
CC ECO:0000269|PubMed:17431409}.
CC -!- INTERACTION:
CC P54733; P23572: Cdk1; NbExp=6; IntAct=EBI-203549, EBI-108689;
CC P54733; P22469: Z600; NbExp=3; IntAct=EBI-203549, EBI-7376821;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8187637}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=II; Synonyms=A, C;
CC IsoId=P54733-1; Sequence=Displayed;
CC Name=I; Synonyms=B;
CC IsoId=P54733-2; Sequence=VSP_001254, VSP_001255;
CC -!- TISSUE SPECIFICITY: Isoform II is ubiquitous in early embryos and,
CC prior to mitosis 14, is rapidly degraded in all cells except the pole
CC (germ) cells. Expressed during G1 phase in proliferating peripheral
CC nervous system cells. Constitutive expression in embryonic cycles
CC lacking a G1 phase. {ECO:0000269|PubMed:8187637}.
CC -!- DEVELOPMENTAL STAGE: Isoform II is expressed maternally and isoform I
CC zygotically in larvae. {ECO:0000269|PubMed:8187637}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin E subfamily.
CC {ECO:0000305}.
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DR EMBL; X75026; CAA52934.1; -; mRNA.
DR EMBL; X75027; CAA52935.1; -; mRNA.
DR EMBL; AE014134; AAF53477.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF53479.1; -; Genomic_DNA.
DR EMBL; AY069507; AAL39652.1; -; mRNA.
DR EMBL; AY061233; AAL28781.1; -; mRNA.
DR PIR; S41755; S41755.
DR PIR; S41756; S41756.
DR RefSeq; NP_476959.1; NM_057611.5. [P54733-1]
DR RefSeq; NP_476960.1; NM_057612.5. [P54733-2]
DR RefSeq; NP_723924.1; NM_165123.3. [P54733-1]
DR RefSeq; NP_723925.1; NM_165124.3. [P54733-1]
DR RefSeq; NP_723926.1; NM_165125.3. [P54733-1]
DR AlphaFoldDB; P54733; -.
DR SMR; P54733; -.
DR BioGRID; 60939; 171.
DR DIP; DIP-18331N; -.
DR ELM; P54733; -.
DR IntAct; P54733; 24.
DR MINT; P54733; -.
DR STRING; 7227.FBpp0294012; -.
DR iPTMnet; P54733; -.
DR PaxDb; 7227-FBpp0294012; -.
DR EnsemblMetazoa; FBtr0080773; FBpp0080331; FBgn0010382. [P54733-1]
DR EnsemblMetazoa; FBtr0080774; FBpp0080332; FBgn0010382. [P54733-1]
DR EnsemblMetazoa; FBtr0080775; FBpp0080333; FBgn0010382. [P54733-1]
DR EnsemblMetazoa; FBtr0080776; FBpp0080334; FBgn0010382. [P54733-1]
DR EnsemblMetazoa; FBtr0080777; FBpp0080335; FBgn0010382. [P54733-2]
DR GeneID; 34924; -.
DR KEGG; dme:Dmel_CG3938; -.
DR AGR; FB:FBgn0010382; -.
DR CTD; 34924; -.
DR FlyBase; FBgn0010382; CycE.
DR VEuPathDB; VectorBase:FBgn0010382; -.
DR eggNOG; KOG0655; Eukaryota.
DR GeneTree; ENSGT00940000169122; -.
DR InParanoid; P54733; -.
DR PhylomeDB; P54733; -.
DR Reactome; R-DME-1538133; G0 and Early G1.
DR Reactome; R-DME-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-DME-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-DME-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
DR Reactome; R-DME-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-DME-69200; Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
DR Reactome; R-DME-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-DME-69231; Cyclin D associated events in G1.
DR Reactome; R-DME-69563; p53-Dependent G1 DNA Damage Response.
DR SignaLink; P54733; -.
DR BioGRID-ORCS; 34924; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 34924; -.
DR PRO; PR:P54733; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0010382; Expressed in cleaving embryo and 83 other cell types or tissues.
DR ExpressionAtlas; P54733; baseline and differential.
DR Genevisible; P54733; DM.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0097134; C:cyclin E1-CDK2 complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IDA:FlyBase.
DR GO; GO:0035736; P:cell proliferation involved in compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0007307; P:eggshell chorion gene amplification; IMP:FlyBase.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0007400; P:neuroblast fate determination; IMP:FlyBase.
DR GO; GO:0048665; P:neuron fate specification; IDA:FlyBase.
DR GO; GO:0007422; P:peripheral nervous system development; IEP:UniProtKB.
DR GO; GO:0007277; P:pole cell development; IEP:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:FlyBase.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IGI:FlyBase.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:FlyBase.
DR GO; GO:0006275; P:regulation of DNA replication; IMP:FlyBase.
DR GO; GO:0090210; P:regulation of establishment of blood-brain barrier; IMP:FlyBase.
DR GO; GO:0007096; P:regulation of exit from mitosis; IGI:FlyBase.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IDA:FlyBase.
DR GO; GO:0045035; P:sensory organ precursor cell division; IMP:FlyBase.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IDA:FlyBase.
DR GO; GO:0007419; P:ventral cord development; HMP:FlyBase.
DR GO; GO:0035220; P:wing disc development; IGI:FlyBase.
DR CDD; cd20519; CYCLIN_CCNE_rpt1; 1.
DR CDD; cd20520; CYCLIN_CCNE_rpt2; 1.
DR Gene3D; 1.10.472.10; Cyclin-like; 2.
DR InterPro; IPR039361; Cyclin.
DR InterPro; IPR013763; Cyclin-like_dom.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR InterPro; IPR048258; Cyclins_cyclin-box.
DR PANTHER; PTHR10177; CYCLINS; 1.
DR PANTHER; PTHR10177:SF344; G1_S-SPECIFIC CYCLIN-E; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SMART; SM01332; Cyclin_C; 1.
DR SUPFAM; SSF47954; Cyclin-like; 2.
DR PROSITE; PS00292; CYCLINS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Cyclin; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..709
FT /note="G1/S-specific cyclin-E"
FT /id="PRO_0000080459"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..259
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 651
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..107
FT /note="Missing (in isoform I)"
FT /evidence="ECO:0000303|PubMed:8187637"
FT /id="VSP_001254"
FT VAR_SEQ 108..119
FT /note="KRKRRLSSDSNE -> MKLEQKRKFIEM (in isoform I)"
FT /evidence="ECO:0000303|PubMed:8187637"
FT /id="VSP_001255"
FT CONFLICT 633
FT /note="A -> S (in Ref. 1; CAA52934)"
FT /evidence="ECO:0000305"
FT CONFLICT 644..645
FT /note="RA -> P (in Ref. 1; CAA52934)"
FT /evidence="ECO:0000305"
FT CONFLICT 691
FT /note="G -> V (in Ref. 1; CAA52934)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 709 AA; 77221 MW; F4E6CE53C6E30170 CRC64;
MGLNAKSVCS TSSTEPNGSI VTTAPSNGEV SSSIVVVVSS SSISSSSDSP IAILPHPDPI
PSTSFSSASQ RSEEELPGTS AASRTDEMCS CDSQNLAAST AATSNGNKRK RRLSSDSNED
PELGFEPPSA KRQQRLPALY GSEQGNLSSV ASSVYTSPVV SVDGQSTQEL LSIRSSPAED
LSEAPHSPLP DSPDSPPSPD RGSKQTPVVV RYAAEQVVTS TVVTQKTEDD DLLDDSCEDY
SYDEDDEDDV EEEDDDVEIY SSTISPASSG CSQQQAVNGE RTPGLPKHQE QIHHPVSDLM
INMRTPMSPA VENGLRQCPL PALAWANAAD VWRLMCHRDE QDSRLRSISM LEQHPGLQPR
MRAILLDWLI EVCEVYKLHR ETFYLAVDYL DRYLHVAHKV QKTHLQLIGI TCLFVAAKVE
EIYPPKIGEF AYVTDGACTE RDILNHEKIL LQALDWDISP ITITGWLGVY MQLNVNNRTP
ASFSQIGRQK SAEADDAFIY PQFSGFEFVQ TSQLLDLCTL DVGMANYSYS VLAAAAISHT
FSREMALRCS GLDWQVIQPC ARWMEPFFRV ISQKAPYLQL NEQNEQVSNK FGLGLICPNI
VTDDSHIIQT HTTTMDMYDE VLMAQDAAHA MRARIQASPA TALRAPESLL TPPASSHKPD
EYLGDEGDET GARSGISSTT TCCNTAASNK GGKSSSNNSV TSCSSRSNP
//
