E2F1_DROME
ID E2F1_DROME Reviewed; 805 AA.
AC Q27368; O77035; Q5U0Z6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Transcription factor E2f1;
DE AltName: Full=dE2F;
GN Name=E2f1 {ECO:0000312|FlyBase:FBgn0011766};
GN Synonyms=E2f {ECO:0000312|FlyBase:FBgn0011766};
GN ORFNames=CG6376 {ECO:0000312|FlyBase:FBgn0011766};
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].
RX PubMed=8114698; DOI=10.1128/mcb.14.3.1603-1612.1994;
RA Ohtani K., Nevins J.R.;
RT "Functional properties of a Drosophila homolog of the E2F1 gene.";
RL Mol. Cell. Biol. 14:1603-1612(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Eye imaginal disk;
RX PubMed=8022787; DOI=10.1073/pnas.91.14.6359;
RA Dynlacht B.D., Brook A., Dembski M., Yenush L., Dyson N.;
RT "DNA-binding and trans-activation properties of Drosophila E2F and DP
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:6359-6363(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=9858578; DOI=10.1128/mcb.19.1.547;
RA Sasaki T., Sawado T., Yamaguchi M., Shinomiya T.;
RT "Specification of regions of DNA replication initiation during
RT embryogenesis in the 65-kilobase DNApolalpha-dE2F locus of Drosophila
RT melanogaster.";
RL Mol. Cell. Biol. 19:547-555(1999).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA Celniker S.E.;
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=8537434; DOI=10.1242/jcs.108.9.2945;
RA Hao X.F., Alphey L., Bandara L.R., Lam E.W., Glover D., La Thangue N.B.;
RT "Functional conservation of the cell cycle-regulating transcription factor
RT DRTF1/E2F and its pathway of control in Drosophila melanogaster.";
RL J. Cell Sci. 108:2945-2954(1995).
RN [8]
RP FUNCTION.
RX PubMed=9271122; DOI=10.1101/gad.11.15.1999;
RA Royzman I., Whittaker A.J., Orr-Weaver T.L.;
RT "Mutations in Drosophila DP and E2F distinguish G1-S progression from an
RT associated transcriptional program.";
RL Genes Dev. 11:1999-2011(1997).
RN [9]
RP FUNCTION.
RX PubMed=9418862; DOI=10.1128/mcb.18.1.141;
RA Duronio R.J., Bonnette P.C., O'Farrell P.H.;
RT "Mutations of the Drosophila dDP, dE2F, and cyclin E genes reveal distinct
RT roles for the E2F-DP transcription factor and cyclin E during the G1-S
RT transition.";
RL Mol. Cell. Biol. 18:141-151(1998).
RN [10]
RP FUNCTION.
RX PubMed=14526388; DOI=10.1038/sj.cdd.4401321;
RA Delanoue R., Legent K., Godefroy N., Flagiello D., Dutriaux A., Vaudin P.,
RA Becker J.L., Silber J.;
RT "The Drosophila wing differentiation factor vestigial-scalloped is required
RT for cell proliferation and cell survival at the dorso-ventral boundary of
RT the wing imaginal disc.";
RL Cell Death Differ. 11:110-122(2004).
RN [11]
RP UBIQUITINATION, DOMAIN PIP-BOX K+4 MOTIF, INTERACTION WITH PCNA, AND
RP MUTAGENESIS OF 153-ILE--TYR-157.
RX PubMed=19081076; DOI=10.1016/j.devcel.2008.10.003;
RA Shibutani S.T., de la Cruz A.F., Tran V., Turbyfill W.J. III, Reis T.,
RA Edgar B.A., Duronio R.J.;
RT "Intrinsic negative cell cycle regulation provided by PIP box- and
RT Cul4Cdt2-mediated destruction of E2f1 during S phase.";
RL Dev. Cell 15:890-900(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434, AND IDENTIFICATION BY
RP MASS 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: Transcriptional activator that binds to E2f sites. Required
CC for wild-type growth in mitotic and polytene tissues, Contributes to
CC the expression of replication genes at the G1-S transition and Cyclin
CC E. Activates cell proliferation in wing imaginal disk, which requires
CC expression of vg. {ECO:0000269|PubMed:14526388,
CC ECO:0000269|PubMed:9271122, ECO:0000269|PubMed:9418862}.
CC -!- SUBUNIT: Heterodimer of E2f and Dp. Cooperates to give sequence-
CC specific DNA binding and optimal trans-activation. Interacts with PCNA.
CC {ECO:0000269|PubMed:19081076}.
CC -!- INTERACTION:
CC Q27368; Q9VT57: Cdk8; NbExp=2; IntAct=EBI-108384, EBI-163640;
CC Q27368; Q24472: Rbf; NbExp=3; IntAct=EBI-108384, EBI-145741;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Segmentally repeated expression throughout early
CC embryos is restricted to the ventral nerve cord in later embryos.
CC {ECO:0000269|PubMed:8537434}.
CC -!- DEVELOPMENTAL STAGE: Throughout embryonic development.
CC {ECO:0000269|PubMed:8537434}.
CC -!- DOMAIN: The PIP-box K+4 motif mediates both the interaction with PCNA
CC and the recruitment of the DCX(DTL) complex: while the PIP-box
CC interacts with PCNA, the presence of the K+4 submotif, recruits the
CC DCX(DTL) complex, leading to its ubiquitination.
CC {ECO:0000269|PubMed:19081076}.
CC -!- PTM: Ubiquitinated by the DCX(DTL) complex, also named CRL4(CDT2)
CC complex, leading to its degradation during S phase. Ubiquitination by
CC the DCX(DTL) complex is essential for cell cycle control and is PCNA-
CC dependent: interacts with PCNA via its PIP-box, while the presence of
CC the containing the 'K+4' motif in the PIP box, recruit the DCX(DTL)
CC complex, leading to its degradation. {ECO:0000269|PubMed:19081076}.
CC -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
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DR EMBL; U10184; AAA19003.1; -; mRNA.
DR EMBL; X78421; CAA55186.1; -; mRNA.
DR EMBL; AB011813; BAA32746.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF55904.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13878.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13879.1; -; Genomic_DNA.
DR EMBL; BT016096; AAV36981.1; -; mRNA.
DR PIR; A56199; A56199.
DR RefSeq; NP_001287455.1; NM_001300526.1.
DR RefSeq; NP_524437.2; NM_079713.3.
DR RefSeq; NP_732646.1; NM_169961.3.
DR RefSeq; NP_732647.1; NM_169962.3.
DR AlphaFoldDB; Q27368; -.
DR SMR; Q27368; -.
DR BioGRID; 67516; 73.
DR DIP; DIP-21076N; -.
DR ELM; Q27368; -.
DR IntAct; Q27368; 15.
DR STRING; 7227.FBpp0083516; -.
DR iPTMnet; Q27368; -.
DR PaxDb; Q27368; -.
DR EnsemblMetazoa; FBtr0084117; FBpp0083516; FBgn0011766.
DR EnsemblMetazoa; FBtr0084118; FBpp0083517; FBgn0011766.
DR EnsemblMetazoa; FBtr0084119; FBpp0083518; FBgn0011766.
DR EnsemblMetazoa; FBtr0346157; FBpp0311985; FBgn0011766.
DR GeneID; 42550; -.
DR KEGG; dme:Dmel_CG6376; -.
DR UCSC; CG6376-RB; d. melanogaster.
DR CTD; 1869; -.
DR FlyBase; FBgn0011766; E2f1.
DR VEuPathDB; VectorBase:FBgn0011766; -.
DR eggNOG; KOG2577; Eukaryota.
DR GeneTree; ENSGT00940000170364; -.
DR InParanoid; Q27368; -.
DR OMA; YNCAMED; -.
DR OrthoDB; 566379at2759; -.
DR PhylomeDB; Q27368; -.
DR Reactome; R-DME-68911; G2 Phase.
DR Reactome; R-DME-69231; Cyclin D associated events in G1.
DR Reactome; R-DME-8953750; Transcriptional Regulation by E2F6.
DR SignaLink; Q27368; -.
DR BioGRID-ORCS; 42550; 1 hit in 3 CRISPR screens.
DR ChiTaRS; E2f1; fly.
DR GenomeRNAi; 42550; -.
DR PRO; PR:Q27368; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0011766; Expressed in spermathecum and 74 other tissues.
DR ExpressionAtlas; Q27368; baseline and differential.
DR Genevisible; Q27368; DM.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA: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:0003677; F:DNA binding; IDA:FlyBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:FlyBase.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:FlyBase.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:FlyBase.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
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:0007307; P:eggshell chorion gene amplification; TAS:FlyBase.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:FlyBase.
DR GO; GO:0035167; P:larval lymph gland hemopoiesis; IMP:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:FlyBase.
DR GO; GO:0032877; P:positive regulation of DNA endoreduplication; IMP:FlyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:FlyBase.
DR GO; GO:0045850; P:positive regulation of nurse cell apoptotic process; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:FlyBase.
DR GO; GO:1900117; P:regulation of execution phase of apoptosis; IMP:FlyBase.
DR GO; GO:0010468; P:regulation of gene expression; IMP:FlyBase.
DR GO; GO:0035206; P:regulation of hemocyte proliferation; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007419; P:ventral cord development; HMP:FlyBase.
DR CDD; cd14660; E2F_DD; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR015633; E2F.
DR InterPro; IPR037241; E2F-DP_heterodim.
DR InterPro; IPR032198; E2F_CC-MB.
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; PF16421; E2F_CC-MB; 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 Activator; Developmental protein; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..805
FT /note="Transcription factor E2f1"
FT /id="PRO_0000219474"
FT DNA_BIND 253..318
FT /evidence="ECO:0000255"
FT REGION 9..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..411
FT /note="Dimerization"
FT /evidence="ECO:0000255"
FT REGION 578..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 147..161
FT /note="PIP-box K+4 motif"
FT COMPBIAS 9..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 153..156
FT /note="ITNY->ATAA: Abolishes interaction with PCNA and
FT subsequent degradation by the proteasome."
FT CONFLICT 127
FT /note="H -> Q (in Ref. 1; CAA55186 and 2; AAA19003)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 805 AA; 87460 MW; BD49C813DDB2A77D CRC64;
MSKFFVNVAP INNSNSSSSH TTTSSNTQRH QQHQQHYGGS GTTGHTMVAR RLNYDLHGGT
TSINNNNNIV IKNESVDLDY DHVLSSSDSN SNGGVAAHLR DHVYISLDKG HNTGAVATAA
AAATAGHTQQ QLQQQHHHQN QQQRKATGKS NDITNYYKVK RRPHAVSDEI HPKKQAKQSA
HHQTVYQKHT ASSAPQQLRH SHHQLRHDAD AELDEDVVER VAKPASHHPF SLSTPQQQLA
ASVASSSSSG DRNRADTSLG ILTKKFVDLL QESPDGVVDL NEASNRLHVQ KRRIYDITNV
LEGINILEKK SKNNIQWRCG QSMVSQERSR HIEADSLRLE QQENELNKAI DLMRENLAEI
SQEVENSGGM AYVTQNDLLN VDLFKDQIVI VIKAPPEAKL VLPNTKLPRE IYVKAENSGE
INVFLCHDTS PENSPIAPGA GYVGAPGAGC VRTATSTRLH PLTNQRLNDP LFNNIDAMST
KGLFQTPYRS ARNLSKSIEE AAKQSQPEYN NICDIAMGQH HNLNQQQQQQ QQQLLQQPEE
DDVDVELNQL VPTLTNPVVR THQFQQHQQP SIQELFSSLT ESSPPTPTKR RREAAAAAIA
AGSSTTATTT LNSHNNRNHS NHSNHSNHSS SNNSKSQPPT IGYGSSQRRS DVPMYNCAME
GATTTSATAD TTAATSRSAA ASSLQMQFAA VAESNNGSSS GGGGGGGGYG SIAGAGANAD
PHQPYSHDRN SLPPGVADCD ANSNSSSVTL QGLDALFNDI GSDYFSNDIA FVSINPPDDN
DYPYALNANE GIDRLFDFGS DAYGP
