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Transcription factor E2f1 (dE2F)

 E2F1_DROME              Reviewed;         805 AA.
Q27368; O77035; Q5U0Z6;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 2.
22-NOV-2017, entry version 157.
RecName: Full=Transcription factor E2f1;
AltName: Full=dE2F;
Name=E2f1 {ECO:0000312|FlyBase:FBgn0011766};
Synonyms=E2f {ECO:0000312|FlyBase:FBgn0011766};
ORFNames=CG6376 {ECO:0000312|FlyBase:FBgn0011766};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8114698; DOI=10.1128/MCB.14.3.1603;
Ohtani K., Nevins J.R.;
"Functional properties of a Drosophila homolog of the E2F1 gene.";
Mol. Cell. Biol. 14:1603-1612(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Eye imaginal disk;
PubMed=8022787; DOI=10.1073/pnas.91.14.6359;
Dynlacht B.D., Brook A., Dembski M., Yenush L., Dyson N.;
"DNA-binding and trans-activation properties of Drosophila E2F and DP
proteins.";
Proc. Natl. Acad. Sci. U.S.A. 91:6359-6363(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Oregon-R;
PubMed=9858578; DOI=10.1128/MCB.19.1.547;
Sasaki T., Sawado T., Yamaguchi M., Shinomiya T.;
"Specification of regions of DNA replication initiation during
embryogenesis in the 65-kilobase DNApolalpha-dE2F locus of Drosophila
melanogaster.";
Mol. Cell. Biol. 19:547-555(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
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).
[5]
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H.,
Yu C., Celniker S.E.;
Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
[7]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=8537434;
Hao X.F., Alphey L., Bandara L.R., Lam E.W., Glover D.,
La Thangue N.B.;
"Functional conservation of the cell cycle-regulating transcription
factor DRTF1/E2F and its pathway of control in Drosophila
melanogaster.";
J. Cell Sci. 108:2945-2954(1995).
[8]
FUNCTION.
PubMed=9271122; DOI=10.1101/gad.11.15.1999;
Royzman I., Whittaker A.J., Orr-Weaver T.L.;
"Mutations in Drosophila DP and E2F distinguish G1-S progression from
an associated transcriptional program.";
Genes Dev. 11:1999-2011(1997).
[9]
FUNCTION.
PubMed=9418862; DOI=10.1128/MCB.18.1.141;
Duronio R.J., Bonnette P.C., O'Farrell P.H.;
"Mutations of the Drosophila dDP, dE2F, and cyclin E genes reveal
distinct roles for the E2F-DP transcription factor and cyclin E during
the G1-S transition.";
Mol. Cell. Biol. 18:141-151(1998).
[10]
FUNCTION.
PubMed=14526388; DOI=10.1038/sj.cdd.4401321;
Delanoue R., Legent K., Godefroy N., Flagiello D., Dutriaux A.,
Vaudin P., Becker J.L., Silber J.;
"The Drosophila wing differentiation factor vestigial-scalloped is
required for cell proliferation and cell survival at the dorso-ventral
boundary of the wing imaginal disc.";
Cell Death Differ. 11:110-122(2004).
[11]
UBIQUITINATION, DOMAIN PIP-BOX K+4 MOTIF, INTERACTION WITH PCNA, AND
MUTAGENESIS OF 153-ILE--TYR-157.
PubMed=19081076; DOI=10.1016/j.devcel.2008.10.003;
Shibutani S.T., de la Cruz A.F., Tran V., Turbyfill W.J. III, Reis T.,
Edgar B.A., Duronio R.J.;
"Intrinsic negative cell cycle regulation provided by PIP box- and
Cul4Cdt2-mediated destruction of E2f1 during S phase.";
Dev. Cell 15:890-900(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434, 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).
-!- FUNCTION: Transcriptional activator that binds to E2f sites.
Required for wild-type growth in mitotic and polytene tissues,
Contributes to the expression of replication genes at the G1-S
transition and Cyclin E. Activates cell proliferation in wing
imaginal disk, which requires expression of vg.
{ECO:0000269|PubMed:14526388, ECO:0000269|PubMed:9271122,
ECO:0000269|PubMed:9418862}.
-!- SUBUNIT: Heterodimer of E2f and Dp. Cooperates to give sequence-
specific DNA binding and optimal trans-activation. Interacts with
PCNA. {ECO:0000269|PubMed:19081076}.
-!- INTERACTION:
Q9VT57:Cdk8; NbExp=2; IntAct=EBI-108384, EBI-163640;
Q24472:Rbf; NbExp=3; IntAct=EBI-108384, EBI-145741;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- TISSUE SPECIFICITY: Segmentally repeated expression throughout
early embryos is restricted to the ventral nerve cord in later
embryos. {ECO:0000269|PubMed:8537434}.
-!- DEVELOPMENTAL STAGE: Throughout embryonic development.
{ECO:0000269|PubMed:8537434}.
-!- DOMAIN: The PIP-box K+4 motif mediates both the interaction with
PCNA and the recruitment of the DCX(DTL) complex: while the PIP-
box interacts with PCNA, the presence of the K+4 submotif,
recruits the DCX(DTL) complex, leading to its ubiquitination.
{ECO:0000269|PubMed:19081076}.
-!- PTM: Ubiquitinated by the DCX(DTL) complex, also named CRL4(CDT2)
complex, leading to its degradation during S phase. Ubiquitination
by the DCX(DTL) complex is essential for cell cycle control and is
PCNA-dependent: interacts with PCNA via its PIP-box, while the
presence of the containing the 'K+4' motif in the PIP box, recruit
the DCX(DTL) complex, leading to its degradation.
{ECO:0000269|PubMed:19081076}.
-!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U10184; AAA19003.1; -; mRNA.
EMBL; X78421; CAA55186.1; -; mRNA.
EMBL; AB011813; BAA32746.1; -; Genomic_DNA.
EMBL; AE014297; AAF55904.1; -; Genomic_DNA.
EMBL; AE014297; AAN13878.1; -; Genomic_DNA.
EMBL; AE014297; AAN13879.1; -; Genomic_DNA.
EMBL; BT016096; AAV36981.1; -; mRNA.
PIR; A56199; A56199.
RefSeq; NP_001287455.1; NM_001300526.1.
RefSeq; NP_524437.2; NM_079713.3.
RefSeq; NP_732646.1; NM_169961.3.
RefSeq; NP_732647.1; NM_169962.3.
UniGene; Dm.7299; -.
ProteinModelPortal; Q27368; -.
SMR; Q27368; -.
BioGrid; 67516; 65.
DIP; DIP-21076N; -.
ELM; Q27368; -.
IntAct; Q27368; 7.
MINT; MINT-1019344; -.
STRING; 7227.FBpp0083516; -.
iPTMnet; Q27368; -.
PaxDb; Q27368; -.
PRIDE; Q27368; -.
EnsemblMetazoa; FBtr0084117; FBpp0083516; FBgn0011766.
EnsemblMetazoa; FBtr0084118; FBpp0083517; FBgn0011766.
EnsemblMetazoa; FBtr0084119; FBpp0083518; FBgn0011766.
EnsemblMetazoa; FBtr0346157; FBpp0311985; FBgn0011766.
GeneID; 42550; -.
KEGG; dme:Dmel_CG6376; -.
UCSC; CG6376-RB; d. melanogaster.
CTD; 1869; -.
FlyBase; FBgn0011766; E2f1.
eggNOG; KOG2577; Eukaryota.
eggNOG; ENOG410XNYI; LUCA.
GeneTree; ENSGT00550000074403; -.
InParanoid; Q27368; -.
KO; K06620; -.
OrthoDB; EOG091G0BHD; -.
PhylomeDB; Q27368; -.
Reactome; R-DME-68689; CDC6 association with the ORC:origin complex.
Reactome; R-DME-68911; G2 Phase.
Reactome; R-DME-69298; Association of licensing factors with the pre-replicative complex.
Reactome; R-DME-8953750; Transcriptional Regulation by E2F6.
ChiTaRS; E2f2; fly.
GenomeRNAi; 42550; -.
PRO; PR:Q27368; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0011766; -.
ExpressionAtlas; Q27368; differential.
Genevisible; Q27368; DM.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0035189; C:Rb-E2F complex; IDA:FlyBase.
GO; GO:0003677; F:DNA binding; IDA:FlyBase.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0001012; F:RNA polymerase II regulatory region DNA binding; IDA:FlyBase.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:FlyBase.
GO; GO:0008134; F:transcription factor binding; IPI:FlyBase.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:FlyBase.
GO; GO:0019730; P:antimicrobial humoral response; IMP:FlyBase.
GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
GO; GO:0042023; P:DNA endoreduplication; IMP:FlyBase.
GO; GO:0007307; P:eggshell chorion gene amplification; TAS:FlyBase.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:FlyBase.
GO; GO:0007444; P:imaginal disc development; TAS:FlyBase.
GO; GO:0035167; P:larval lymph gland hemopoiesis; IMP:FlyBase.
GO; GO:0060537; P:muscle tissue development; IMP:FlyBase.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:FlyBase.
GO; GO:0048666; P:neuron development; IMP:FlyBase.
GO; GO:0045476; P:nurse cell apoptotic process; TAS:FlyBase.
GO; GO:0008284; P:positive regulation of cell proliferation; NAS:FlyBase.
GO; GO:0010628; P:positive regulation of gene expression; IMP:FlyBase.
GO; GO:0045850; P:positive regulation of nurse cell apoptotic process; IMP:FlyBase.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:FlyBase.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; TAS:FlyBase.
GO; GO:0051726; P:regulation of cell cycle; IMP:FlyBase.
GO; GO:1900117; P:regulation of execution phase of apoptosis; IMP:FlyBase.
GO; GO:0010906; P:regulation of glucose metabolic process; IMP:FlyBase.
GO; GO:0035206; P:regulation of hemocyte proliferation; IMP:FlyBase.
GO; GO:0007419; P:ventral cord development; IMP:FlyBase.
CDD; cd14660; E2F_DD; 1.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR015633; E2F.
InterPro; IPR037241; E2F-DP_heterodim.
InterPro; IPR032198; E2F_CC-MB.
InterPro; IPR003316; E2F_WHTH_DNA-bd_dom.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
PANTHER; PTHR12081; PTHR12081; 1.
Pfam; PF16421; E2F_CC-MB; 1.
Pfam; PF02319; E2F_TDP; 1.
SMART; SM01372; E2F_TDP; 1.
SUPFAM; SSF144074; SSF144074; 1.
SUPFAM; SSF46785; SSF46785; 1.
1: Evidence at protein level;
Activator; Complete proteome; Developmental protein; DNA-binding;
Nucleus; Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 805 Transcription factor E2f1.
/FTId=PRO_0000219474.
DNA_BIND 253 318 {ECO:0000255}.
REGION 318 411 Dimerization. {ECO:0000255}.
MOTIF 147 161 PIP-box K+4 motif.
COMPBIAS 14 19 Poly-Ser.
COMPBIAS 64 68 Poly-Asn.
COMPBIAS 115 125 Poly-Ala.
COMPBIAS 129 143 Gly-rich.
COMPBIAS 245 249 Poly-Ser.
COMPBIAS 519 573 Gly-rich.
COMPBIAS 525 533 Poly-Gln.
COMPBIAS 594 601 Poly-Ala.
COMPBIAS 701 710 Poly-Gly.
MOD_RES 434 434 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MUTAGEN 153 156 ITNY->ATAA: Abolishes interaction with
PCNA and subsequent degradation by the
proteasome.
CONFLICT 127 127 H -> Q (in Ref. 1; CAA55186 and 2;
AAA19003). {ECO:0000305}.
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


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