E2F2_DROME
ID E2F2_DROME Reviewed; 370 AA.
AC O77051;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Transcription factor E2F2;
DE Short=dE2F2 {ECO:0000303|PubMed:9792788};
DE AltName: Full=E2F transcription factor 2 {ECO:0000312|EMBL:AAF53965.1};
DE AltName: Full=E2F-like transcription factor E2F2;
GN Name=E2f2; ORFNames=CG1071;
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] {ECO:0000305, ECO:0000312|EMBL:BAA33742.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=9792788; DOI=10.1006/bbrc.1998.9407;
RA Sawado T., Yamaguchi M., Nishimoto Y., Ohno K., Sakaguchi K., Matsukage A.;
RT "dE2F2, a novel E2F-family transcription factor in Drosophila
RT melanogaster.";
RL Biochem. Biophys. Res. Commun. 251:409-415(1998).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAL39263.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000269|Ref.2};
RA Harvey D., Hong L., Evans-Holm M., Pendleton J., Su C., Brokstein P.,
RA Lewis S., Rubin G.M.;
RT "BDGP/HHMI Drosophila EST Project.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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] {ECO:0000305, ECO:0000312|EMBL:AAL39263.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL39263.1}; TISSUE=Head;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Farfan D., Frise E., George R., Gonzalez M.,
RA Guarin H., Li P., Liao G., Miranda A., Mungall C.J., Nunoo J., Pacleb J.,
RA Paragas V., Park S., Phouanenavong S., Wan K., Yu C., Lewis S.E.,
RA Rubin G.M., Celniker S.;
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305}
RP FUNCTION, SUBUNIT, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=11748144; DOI=10.1242/dev.128.24.5085;
RA Cayirlioglu P., Bonnette P.C., Dickson M.R., Duronio R.J.;
RT "Drosophila E2f2 promotes the conversion from genomic DNA replication to
RT gene amplification in ovarian follicle cells.";
RL Development 128:5085-5098(2001).
RN [7] {ECO:0000305}
RP FUNCTION, HETERODIMER WITH DP, INTERACTION WITH RBF, TISSUE SPECIFICITY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=11511545; DOI=10.1101/gad.903901;
RA Frolov M.V., Huen D.S., Stevaux O., Dimova D., Balczarek-Strang K.,
RA Elsdon M., Dyson N.J.;
RT "Functional antagonism between E2F family members.";
RL Genes Dev. 15:2146-2160(2001).
RN [8] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH RBF AND RBF2.
RX PubMed=12234932; DOI=10.1093/emboj/cdf501;
RA Stevaux O., Dimova D., Frolov M.V., Taylor-Harding B., Morris E., Dyson N.;
RT "Distinct mechanisms of E2F regulation by Drosophila RBF1 and RBF2.";
RL EMBO J. 21:4927-4937(2002).
RN [9] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12612083; DOI=10.1128/mcb.23.6.2123-2134.2003;
RA Cayirlioglu P., Ward W.O., Silver Key S.C., Duronio R.J.;
RT "Transcriptional repressor functions of Drosophila E2F1 and E2F2 cooperate
RT to inhibit genomic DNA synthesis in ovarian follicle cells.";
RL Mol. Cell. Biol. 23:2123-2134(2003).
RN [10] {ECO:0000305}
RP FUNCTION, AND IDENTIFICATION IN THE DREAM COMPLEX.
RX PubMed=15479636; DOI=10.1016/j.cell.2004.09.034;
RA Korenjak M., Taylor-Harding B., Binne U.K., Satterlee J.S., Stevaux O.,
RA Aasland R., White-Cooper H., Dyson N., Brehm A.;
RT "Native E2F/RBF complexes contain Myb-interacting proteins and repress
RT transcription of developmentally controlled E2F target genes.";
RL Cell 119:181-193(2004).
RN [11] {ECO:0000305}
RP IDENTIFICATION IN THE DREAM COMPLEX.
RX PubMed=15545624; DOI=10.1101/gad.1255204;
RA Lewis P.W., Beall E.L., Fleischer T.C., Georlette D., Link A.J.,
RA Botchan M.R.;
RT "Identification of a Drosophila Myb-E2F2/RBF transcriptional repressor
RT complex.";
RL Genes Dev. 18:2929-2940(2004).
RN [12] {ECO:0000305}
RP FUNCTION.
RX PubMed=15456884; DOI=10.1128/mcb.24.20.9124-9136.2004;
RA Taylor-Harding B., Binne U.K., Korenjak M., Brehm A., Dyson N.J.;
RT "p55, the Drosophila ortholog of RbAp46/RbAp48, is required for the
RT repression of dE2F2/RBF-regulated genes.";
RL Mol. Cell. Biol. 24:9124-9136(2004).
RN [13] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20659447; DOI=10.1016/j.ydbio.2010.07.023;
RA Wichmann A., Uyetake L., Su T.T.;
RT "E2F1 and E2F2 have opposite effects on radiation-induced p53-independent
RT apoptosis in Drosophila.";
RL Dev. Biol. 346:80-89(2010).
RN [14] {ECO:0000305}
RP FUNCTION.
RX PubMed=20548101; DOI=10.1083/jcb.200910006;
RA Buttitta L.A., Katzaroff A.J., Edgar B.A.;
RT "A robust cell cycle control mechanism limits E2F-induced proliferation of
RT terminally differentiated cells in vivo.";
RL J. Cell Biol. 189:981-996(2010).
RN [15] {ECO:0000305}
RP FUNCTION.
RX PubMed=22451490; DOI=10.1128/mcb.06314-11;
RA Lee H., Ragusano L., Martinez A., Gill J., Dimova D.K.;
RT "A dual role for the dREAM/MMB complex in the regulation of
RT differentiation-specific E2F/RB target genes.";
RL Mol. Cell. Biol. 32:2110-2120(2012).
CC -!- FUNCTION: Transcriptional repressor that binds to E2f sites and
CC represses E2f-regulated target genes. Binding to E2f sites requires
CC transcription factor Dp. Acts synergistically with Rbf2 to antagonize
CC E2f1-mediated transcriptional activation. Component of the DREAM
CC complex, a multiprotein complex that can both act as a transcription
CC activator or repressor depending on the context. The DREAM complex is
CC required for recruiting E2f2 at differentiation-specific promoters and
CC for stabilizing E2f2-Rbf complexes during S phase. During development,
CC the complex represses transcription of developmentally controlled E2f
CC target genes. During oogenesis, plays a role in restricting DNA
CC synthesis to sites of chorion gene amplification in late stage ovarian
CC follicle cells. Plays an inhibitory role in ionizing radiation (IR)-
CC induced p53-independent apoptosis. May be involved in cell cycle exit
CC by temporarily limiting CycE-dependent activation of E2f-regulated
CC transcription. {ECO:0000269|PubMed:11511545,
CC ECO:0000269|PubMed:11748144, ECO:0000269|PubMed:12234932,
CC ECO:0000269|PubMed:12612083, ECO:0000269|PubMed:15456884,
CC ECO:0000269|PubMed:15479636, ECO:0000269|PubMed:20548101,
CC ECO:0000269|PubMed:20659447, ECO:0000269|PubMed:22451490,
CC ECO:0000269|PubMed:9792788}.
CC -!- SUBUNIT: Forms a heterodimer with Dp. Interacts with Rbf/Rbf1 and Rbf2.
CC Component of the DREAM complex, which is at least composed of Myb,
CC Caf1-55, mip40, mip120, mip130, E2f2, Dp, Rbf, Rbf2, lin-52, HDAC1/Rpd3
CC and l(3)mbt. {ECO:0000269|PubMed:11511545, ECO:0000269|PubMed:11748144,
CC ECO:0000269|PubMed:12234932, ECO:0000269|PubMed:15479636,
CC ECO:0000269|PubMed:15545624}.
CC -!- INTERACTION:
CC O77051; Q9W542: mip130; NbExp=4; IntAct=EBI-93258, EBI-75943;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:9792788}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in eye disk.
CC {ECO:0000269|PubMed:11511545}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout embryonic development, with
CC highest levels detected in cycling cells including in mitotically
CC active cells during germ-band extended stages, as well as proliferating
CC cells of the CNS and endoreduplicating cells of tissues such as the
CC midgut at later embryonic stages. Maternal mRNA detected in syncytial
CC stage embryos and disappears by the cellular blastoderm stage. A single
CC transcript of 1.4 kb is detected at the highest level in 4 to 8 hour
CC embryos, and at a relatively high level in 0 to 2 hour embryos. Lower
CC levels of the transcript are detected in unfertilized eggs, larvae,
CC pupae and adult. {ECO:0000269|PubMed:11748144,
CC ECO:0000269|PubMed:9792788}.
CC -!- DISRUPTION PHENOTYPE: Flies show reduced viability, with between 20 to
CC 35% surviving until adult stages and both male and female flies showing
CC significantly reduced fertility (PubMed:11511545). E2f1 and E2f2 double
CC mutants die at the pupal stage during development compared with E2f1
CC mutants that die earlier at the larval stage, indicating that E2f1 and
CC E2f2 functionally antagonize each other in vivo. According to
CC PubMed:11748144, flies are viable, with males that are fully fertile
CC and females that are partially sterile. p53 and E2f2 double mutants
CC exhibit substantially more apoptosis at 20 and 24 hours after exposure
CC to IR as compared to p53 single mutants, indicating that E2f2 limits
CC IR-induced p53-independent apoptosis. {ECO:0000269|PubMed:11511545,
CC ECO:0000269|PubMed:11748144, ECO:0000269|PubMed:12612083,
CC ECO:0000269|PubMed:20659447}.
CC -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000255}.
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DR EMBL; AB016824; BAA33742.1; -; mRNA.
DR EMBL; AA202711; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AE014134; AAF53965.1; -; Genomic_DNA.
DR EMBL; AY069118; AAL39263.1; -; mRNA.
DR PIR; JE0342; JE0342.
DR RefSeq; NP_001286115.1; NM_001299186.1.
DR RefSeq; NP_477355.1; NM_058007.5.
DR AlphaFoldDB; O77051; -.
DR SMR; O77051; -.
DR BioGRID; 61336; 82.
DR DIP; DIP-18289N; -.
DR IntAct; O77051; 45.
DR STRING; 7227.FBpp0081029; -.
DR PaxDb; O77051; -.
DR EnsemblMetazoa; FBtr0081501; FBpp0081029; FBgn0024371.
DR EnsemblMetazoa; FBtr0346451; FBpp0312101; FBgn0024371.
DR GeneID; 35381; -.
DR KEGG; dme:Dmel_CG1071; -.
DR UCSC; CG1071-RA; d. melanogaster.
DR CTD; 1870; -.
DR FlyBase; FBgn0024371; E2f2.
DR VEuPathDB; VectorBase:FBgn0024371; -.
DR eggNOG; KOG2577; Eukaryota.
DR HOGENOM; CLU_750673_0_0_1; -.
DR InParanoid; O77051; -.
DR OMA; PQEDFNF; -.
DR OrthoDB; 1087250at2759; -.
DR PhylomeDB; O77051; -.
DR Reactome; R-DME-1538133; G0 and Early G1.
DR Reactome; R-DME-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-DME-69231; Cyclin D associated events in G1.
DR SignaLink; O77051; -.
DR BioGRID-ORCS; 35381; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 35381; -.
DR PRO; PR:O77051; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0024371; Expressed in secondary oocyte and 56 other tissues.
DR ExpressionAtlas; O77051; baseline and differential.
DR Genevisible; O77051; DM.
DR GO; GO:0000785; C:chromatin; IDA:FlyBase.
DR GO; GO:0031523; C:Myb complex; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; HDA:FlyBase.
DR GO; GO:0035189; C:Rb-E2F complex; IDA:FlyBase.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0008134; F:transcription factor binding; IPI:FlyBase.
DR GO; GO:0042023; P:DNA endoreduplication; IMP:FlyBase.
DR GO; GO:0007113; P:endomitotic cell cycle; TAS:FlyBase.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:FlyBase.
DR GO; GO:0007444; P:imaginal disc development; TAS:FlyBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0008156; P:negative regulation of DNA replication; IMP:FlyBase.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IDA:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0048477; P:oogenesis; TAS:FlyBase.
DR GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR015633; E2F.
DR InterPro; IPR037241; E2F-DP_heterodim.
DR InterPro; IPR003316; E2F_WHTH_DNA-bd_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12081; PTHR12081; 1.
DR Pfam; PF02319; E2F_TDP; 1.
DR SMART; SM01372; E2F_TDP; 1.
DR SUPFAM; SSF144074; SSF144074; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..370
FT /note="Transcription factor E2F2"
FT /id="PRO_0000420434"
FT DNA_BIND 72..137
FT /evidence="ECO:0000255, ECO:0000305"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..226
FT /note="Dimerization"
FT /evidence="ECO:0000255, ECO:0000305"
FT COMPBIAS 12..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 370 AA; 41395 MW; 20BE683AED914842 CRC64;
MYKRKTASIV KRDSSAAGTT SSAMMMKVDS AETSVRSQSY ESTPVSMDTS PDPPTPIKSP
SNSQSQSQPG QQRSVGSLVL LTQKFVDLVK ANEGSIDLKA ATKILDVQKR RIYDITNVLE
GIGLIDKGRH CSLVRWRGGG FNNAKDQENY DLARSRTNHL KMLEDDLDRQ LEYAQRNLRY
VMQDPSNRSY AYVTRDDLLD IFGDDSVFTI PNYDEEVDIK RNHYELAVSL DNGSAIDIRL
VTNQGKSTTN PHDVDGFFDY HRLDTPSPST SSHSSEDGNA PACAGNVITD EHGYSCNPGM
KDEMKLLENE LTAKIIFQNY LSGHSLRRFY PDDPNLENPP LLQLNPPQED FNFALKSDEG
ICELFDVQCS
