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Transcription factor E2F1 (E2F-1) (PBR3) (Retinoblastoma-associated protein 1) (RBAP-1) (Retinoblastoma-binding protein 3) (RBBP-3) (pRB-binding protein E2F-1)

 E2F1_HUMAN              Reviewed;         437 AA.
Q01094; Q13143; Q92768;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
22-NOV-2017, entry version 205.
RecName: Full=Transcription factor E2F1;
Short=E2F-1;
AltName: Full=PBR3;
AltName: Full=Retinoblastoma-associated protein 1;
Short=RBAP-1;
AltName: Full=Retinoblastoma-binding protein 3;
Short=RBBP-3;
AltName: Full=pRB-binding protein E2F-1;
Name=E2F1; Synonyms=RBBP3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1638634; DOI=10.1016/0092-8674(92)90107-N;
Helin K., Lees J.A., Vidal M., Dyson N.J., Harlow E., Fattaey A.;
"A cDNA encoding a pRB-binding protein with properties of the
transcription factor E2F.";
Cell 70:337-350(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1638635; DOI=10.1016/0092-8674(92)90108-O;
Kaelin W.G. Jr., Krek W., Sellers W.R., Decaprio J.A., Ajchenbaum F.,
Fuchs C.S., Chittenden T., Li Y., Farnham P.J., Blanar M.A.,
Livingston D.M., Flemington E.K.;
"Expression cloning of a cDNA encoding a retinoblastoma-binding
protein with E2F-like properties.";
Cell 70:351-364(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1448092; DOI=10.1128/MCB.12.12.5620;
Shan B., Zhu X., Chen P.L., Durfee T., Yang Y., Sharp D., Lee W.H.;
"Molecular cloning of cellular genes encoding retinoblastoma-
associated proteins: identification of a gene with properties of the
transcription factor E2F.";
Mol. Cell. Biol. 12:5620-5631(1992).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8964493; DOI=10.1016/0378-1119(96)00184-9;
Neuman E., Sellers W.R.S., McNeil J.A., Lawrence J.B.,
Kaelin W.G. Jr.;
"Structure and partial genomic sequence of the human E2F1 gene.";
Gene 173:163-169(1996).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-252; MET-276;
ASN-311 AND SER-393.
NIEHS SNPs program;
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-111.
PubMed=7958836; DOI=10.1101/gad.8.13.1514;
Johnson D.G., Ohtani K., Nevins J.R.;
"Autoregulatory control of E2F1 expression in response to positive and
negative regulators of cell cycle progression.";
Genes Dev. 8:1514-1525(1994).
[9]
TRANSACTIVATION INHIBITION, AND MUTAGENESIS OF TYR-411.
PubMed=8413249; DOI=10.1128/MCB.13.10.6501;
Helin K., Harlow E., Fattaey A.;
"Inhibition of E2F-1 transactivation by direct binding of the
retinoblastoma protein.";
Mol. Cell. Biol. 13:6501-6508(1993).
[10]
DOMAIN CYCLIN A:CDK2 BINDING.
PubMed=8033208; DOI=10.1016/0092-8674(94)90582-7;
Krek W., Ewen M.E., Shirodkar S., Arany Z., Kaelin W.G. Jr.,
Livingston D.M.;
"Negative regulation of the growth-promoting transcription factor E2F-
1 by a stably bound cyclin A-dependent protein kinase.";
Cell 78:161-172(1994).
[11]
DIFFERENTIAL REGULATION BY CYCLIN/CDK2 KINASES.
PubMed=7958856; DOI=10.1101/gad.8.15.1772;
Dynlacht B.D., Flores O., Lees J.A., Harlow E.;
"Differential regulation of E2F transactivation by cyclin/cdk2
complexes.";
Genes Dev. 8:1772-1786(1994).
[12]
INHIBITION OF DNA-BINDING.
PubMed=7969176; DOI=10.1128/MCB.14.12.8420;
Xu M., Sheppard K.-A., Peng C.-Y., Yee A.S., Piwnica-Worms H.;
"Cyclin A/CDK2 binds directly to E2F-1 and inhibits the DNA-binding
activity of E2F-1/DP-1 by phosphorylation.";
Mol. Cell. Biol. 14:8420-8431(1994).
[13]
FUNCTION IN APOPTOSIS.
PubMed=8170954; DOI=10.1073/pnas.91.9.3602;
Wu X., Levine A.J.;
"P53 and E2F-1 cooperate to mediate apoptosis.";
Proc. Natl. Acad. Sci. U.S.A. 91:3602-3606(1994).
[14]
INTERACTION WITH HHV-5 PROTEIN UL123.
PubMed=7494286;
Margolis M.J., Pajovic S., Wong E.L., Wade M., Jupp R., Nelson J.A.,
Azizkhan J.C.;
"Interaction of the 72-kilodalton human cytomegalovirus IE1 gene
product with E2F1 coincides with E2F-dependent activation of
dihydrofolate reductase transcription.";
J. Virol. 69:7759-7767(1995).
[15]
PHOSPHORYLATION.
PubMed=7838523;
Kitagawa M., Higashi H., Suzuki-Takahashi I., Segawa K., Hanks S.K.,
Taya Y., Nishimura S., Okuyama A.;
"Phosphorylation of E2F-1 by cyclin A-cdk2.";
Oncogene 10:229-236(1995).
[16]
REGULATION BY CYCLIN-DEPENDENT KINASES.
PubMed=9199321; DOI=10.1128/MCB.17.7.3867;
Dynlacht B.D., Moberg K., Lees J.A., Harlow E., Zhu L.;
"Specific regulation of E2F family members by cyclin-dependent
kinases.";
Mol. Cell. Biol. 17:3867-3875(1997).
[17]
INTERACTION WITH ARID3A.
PubMed=9780002; DOI=10.1038/sj.onc.1202163;
Suzuki M., Okuyama S., Okamoto S., Shirasuna K., Nakajima T.,
Hachiya T., Nojima H., Sekiya S., Oda K.;
"A novel E2F binding protein with Myc-type HLH motif stimulates E2F-
dependent transcription by forming a heterodimer.";
Oncogene 17:853-865(1998).
[18]
ACETYLATION AT LYS-117; LYS-120 AND LYS-125, DNA-BINDING, INTERACTION
WITH KAT2B, FUNCTION, AND MUTAGENESIS OF LYS-117; LYS-120 AND LYS-125.
PubMed=10675335; DOI=10.1093/emboj/19.4.662;
Martinez-Balbas M.A., Bauer U.M., Nielsen S.J., Brehm A.,
Kouzarides T.;
"Regulation of E2F1 activity by acetylation.";
EMBO J. 19:662-671(2000).
[19]
INTERACTION WITH TRRAP.
PubMed=11418595; DOI=10.1074/jbc.M102067200;
Lang S.E., McMahon S.B., Cole M.D., Hearing P.;
"E2F transcriptional activation requires TRRAP and GCN5 cofactors.";
J. Biol. Chem. 276:32627-32634(2001).
[20]
INTERACTION WITH TOPBP1.
PubMed=12697828; DOI=10.1128/MCB.23.9.3287-3304.2003;
Liu K., Lin F.-T., Ruppert J.M., Lin W.-C.;
"Regulation of E2F1 by BRCT domain-containing protein TopBP1.";
Mol. Cell. Biol. 23:3287-3304(2003).
[21]
FUNCTION IN TRANSCRIPTION REGULATION, FUNCTION IN APOPTOSIS,
PHOSPHORYLATION AT SER-364 BY CHEK2, AND MUTAGENESIS OF SER-364.
PubMed=12717439; DOI=10.1038/ncb974;
Stevens C., Smith L., La Thangue N.B.;
"Chk2 activates E2F-1 in response to DNA damage.";
Nat. Cell Biol. 5:401-409(2003).
[22]
INTERACTION WITH WITH RB1 AND TFDP1.
PubMed=16360038; DOI=10.1016/j.cell.2005.09.044;
Rubin S.M., Gall A.-L., Zheng N., Pavletich N.P.;
"Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism
for phosphorylation-induced E2F release.";
Cell 123:1093-1106(2005).
[23]
INTERACTION WITH EAPP.
PubMed=15716352; DOI=10.1091/mbc.E04-11-0975;
Novy M., Pohn R., Andorfer P., Novy-Weiland T., Galos B.,
Schwarzmayr L., Rotheneder H.;
"EAPP, a novel E2F binding protein that modulates E2F-dependent
transcription.";
Mol. Biol. Cell 16:2181-2190(2005).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[25]
INTERACTION WITH HDAC1 AND TRIM28, FUNCTION, ACETYLATION, AND
DEACETYLATION.
PubMed=17704056; DOI=10.1074/jbc.M704757200;
Wang C., Rauscher F.J. III, Cress W.D., Chen J.;
"Regulation of E2F1 function by the nuclear corepressor KAP1.";
J. Biol. Chem. 282:29902-29909(2007).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[28]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RRP1B.
PubMed=20040599; DOI=10.1074/jbc.M109.072074;
Paik J.C., Wang B., Liu K., Lue J.K., Lin W.C.;
"Regulation of E2F1-induced apoptosis by the nucleolar protein
RRP1B.";
J. Biol. Chem. 285:6348-6363(2010).
[29]
FUNCTION, INTERACTION WITH CEBPA, AND MUTAGENESIS OF LEU-132 AND
TYR-411.
PubMed=20176812; DOI=10.1128/MCB.01619-09;
Zaragoza K., Begay V., Schuetz A., Heinemann U., Leutz A.;
"Repression of transcriptional activity of C/EBPalpha by E2F-
dimerization partner complexes.";
Mol. Cell. Biol. 30:2293-2304(2010).
[30]
INTERACTION WITH BIRC2, AND ENZYME REGULATION.
PubMed=21653699; DOI=10.1074/jbc.M110.191239;
Cartier J., Berthelet J., Marivin A., Gemble S., Edmond V.,
Plenchette S., Lagrange B., Hammann A., Dupoux A., Delva L., Eymin B.,
Solary E., Dubrez L.;
"Cellular inhibitor of apoptosis protein-1 (cIAP1) can regulate E2F1
transcription factor-mediated control of cyclin transcription.";
J. Biol. Chem. 286:26406-26417(2011).
[31]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 87-95.
PubMed=12501191; DOI=10.1021/bi0268910;
Lowe E.D., Tews I., Cheng K.Y., Brown N.R., Gul S., Noble M.E.M.,
Gamblin S.J., Johnson L.N.;
"Specificity determinants of recruitment peptides bound to phospho-
CDK2/cyclin A.";
Biochemistry 41:15625-15634(2002).
[32]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 409-426 IN COMPLEX WITH RB1.
PubMed=12598654; DOI=10.1073/pnas.0436813100;
Xiao B., Spencer J., Clements A., Ali-Khan N., Mittnacht S.,
Broceno C., Burghammer M., Perrakis A., Marmorstein R., Gamblin S.J.;
"Crystal structure of the retinoblastoma tumor suppressor protein
bound to E2F and the molecular basis of its regulation.";
Proc. Natl. Acad. Sci. U.S.A. 100:2363-2368(2003).
-!- FUNCTION: Transcription activator that binds DNA cooperatively
with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-
3' found in the promoter region of a number of genes whose
products are involved in cell cycle regulation or in DNA
replication. The DRTF1/E2F complex functions in the control of
cell-cycle progression from G1 to S phase. E2F1 binds
preferentially RB1 in a cell-cycle dependent manner. It can
mediate both cell proliferation and TP53/p53-dependent apoptosis.
Blocks adipocyte differentiation by binding to specific promoters
repressing CEBPA binding to its target gene promoters
(PubMed:20176812). Positively regulates transcription of RRP1B
(PubMed:20040599). {ECO:0000250|UniProtKB:Q61501,
ECO:0000269|PubMed:10675335, ECO:0000269|PubMed:12717439,
ECO:0000269|PubMed:17704056, ECO:0000269|PubMed:20040599,
ECO:0000269|PubMed:20176812, ECO:0000269|PubMed:8170954}.
-!- ENZYME REGULATION: BIRC2/c-IAP1 stimulates its transcriptional
activity. {ECO:0000269|PubMed:21653699}.
-!- SUBUNIT: Component of the DRTF1/E2F transcription factor complex.
Forms heterodimers with DP family members. The E2F1 complex binds
specifically hypophosphorylated retinoblastoma protein RB1. During
the cell cycle, RB1 becomes phosphorylated in mid-to-late G1
phase, detaches from the DRTF1/E2F complex, rendering E2F
transcriptionally active. Viral oncoproteins, notably E1A, T-
antigen and HPV E7, are capable of sequestering RB1, thus
releasing the active complex. Interacts with TRRAP, which probably
mediates its interaction with histone acetyltransferase complexes,
leading to transcription activation. Binds TOPBP1 and EAPP.
Interacts with ARID3A. Interacts with TRIM28; the interaction
inhibits E2F1 acetylation through recruiting HDAC1 and represses
its transcriptional activity. Interaction with KAT2B; the
interaction acetylates E2F1 enhancing its DNA-binding and
transcriptional activity. Interacts with BIRC2/c-IAP1 (via BIR
domains). The complex TFDP1:E2F1 interacts with CEBPA; the
interaction prevents CEBPA binding to target genes promoters and
represses its transcriptional activity (PubMed:20176812).
Interacts with RRP1B (PubMed:20040599).
{ECO:0000250|UniProtKB:Q61501, ECO:0000269|PubMed:10675335,
ECO:0000269|PubMed:11418595, ECO:0000269|PubMed:12598654,
ECO:0000269|PubMed:12697828, ECO:0000269|PubMed:15716352,
ECO:0000269|PubMed:16360038, ECO:0000269|PubMed:17704056,
ECO:0000269|PubMed:20040599, ECO:0000269|PubMed:20176812,
ECO:0000269|PubMed:21653699, ECO:0000269|PubMed:9780002}.
-!- SUBUNIT: (Microbial infection) Interacts with human
cytomegalovirus/HHV-5 protein UL123. {ECO:0000269|PubMed:7494286}.
-!- INTERACTION:
Q14201:BTG3; NbExp=3; IntAct=EBI-448924, EBI-948192;
P50613:CDK7; NbExp=2; IntAct=EBI-448924, EBI-1245958;
P49336:CDK8; NbExp=3; IntAct=EBI-448924, EBI-394377;
Q92466:DDB2; NbExp=2; IntAct=EBI-448924, EBI-1176171;
P03129:E7 (xeno); NbExp=2; IntAct=EBI-448924, EBI-866453;
Q13547:HDAC1; NbExp=2; IntAct=EBI-448924, EBI-301834;
Q8NEM0:MCPH1; NbExp=6; IntAct=EBI-448924, EBI-1565483;
Q9Y618:NCOR2; NbExp=2; IntAct=EBI-448924, EBI-80830;
P09874:PARP1; NbExp=3; IntAct=EBI-448924, EBI-355676;
O14744:PRMT5; NbExp=8; IntAct=EBI-448924, EBI-351098;
P06400:RB1; NbExp=21; IntAct=EBI-448924, EBI-491274;
Q96EB6:SIRT1; NbExp=3; IntAct=EBI-448924, EBI-1802965;
Q923E4:Sirt1 (xeno); NbExp=3; IntAct=EBI-448924, EBI-1802585;
P08047:SP1; NbExp=2; IntAct=EBI-448924, EBI-298336;
P42224:STAT1; NbExp=2; IntAct=EBI-448924, EBI-1057697;
Q14186:TFDP1; NbExp=10; IntAct=EBI-448924, EBI-749713;
Q92547:TOPBP1; NbExp=3; IntAct=EBI-448924, EBI-308302;
O95361:TRIM16; NbExp=2; IntAct=EBI-448924, EBI-727384;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20040599}.
-!- PTM: Phosphorylated by CDK2 and cyclin A-CDK2 in the S-phase.
Phosphorylation at Ser-364 by CHEK2 stabilizes E2F1 upon DNA
damage and regulates its effect on transcription and apoptosis.
{ECO:0000269|PubMed:12717439, ECO:0000269|PubMed:7838523}.
-!- PTM: Acetylation stimulates DNA-binding. Enhanced under stress
conditions such as DNA damage and inhibited by retinoblastoma
protein RB1. Regulated by KAP1/TRIM28 which recruits HDAC1 to E2F1
resulting in deacetylation. Acetylated by P/CAF/KAT2B.
{ECO:0000269|PubMed:10675335, ECO:0000269|PubMed:17704056}.
-!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB24289.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/E2F1ID40382ch20q11.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/e2f1/";
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EMBL; M96577; AAA35782.1; -; mRNA.
EMBL; U47677; AAC50719.1; -; Genomic_DNA.
EMBL; U47675; AAC50719.1; JOINED; Genomic_DNA.
EMBL; U47676; AAC50719.1; JOINED; Genomic_DNA.
EMBL; S49592; AAB24289.1; ALT_INIT; mRNA.
EMBL; AF516106; AAM47604.1; -; Genomic_DNA.
EMBL; AL121906; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC050369; AAH50369.1; -; mRNA.
EMBL; BC058902; AAH58902.1; -; mRNA.
EMBL; S74230; AAD14150.1; -; Genomic_DNA.
CCDS; CCDS13224.1; -.
PIR; JC4929; JC4929.
RefSeq; NP_005216.1; NM_005225.2.
UniGene; Hs.654393; -.
PDB; 1H24; X-ray; 2.50 A; E=87-95.
PDB; 1O9K; X-ray; 2.60 A; P/Q/R/S=409-426.
PDB; 2AZE; X-ray; 2.55 A; B=200-301.
PDB; 5M9N; X-ray; 1.95 A; C=104-120.
PDB; 5M9O; X-ray; 1.45 A; B=108-116.
PDBsum; 1H24; -.
PDBsum; 1O9K; -.
PDBsum; 2AZE; -.
PDBsum; 5M9N; -.
PDBsum; 5M9O; -.
ProteinModelPortal; Q01094; -.
SMR; Q01094; -.
BioGrid; 108201; 116.
CORUM; Q01094; -.
DIP; DIP-24227N; -.
ELM; Q01094; -.
IntAct; Q01094; 43.
MINT; MINT-112765; -.
STRING; 9606.ENSP00000345571; -.
ChEMBL; CHEMBL4382; -.
iPTMnet; Q01094; -.
PhosphoSitePlus; Q01094; -.
BioMuta; E2F1; -.
DMDM; 400928; -.
MaxQB; Q01094; -.
PaxDb; Q01094; -.
PeptideAtlas; Q01094; -.
PRIDE; Q01094; -.
Ensembl; ENST00000343380; ENSP00000345571; ENSG00000101412.
GeneID; 1869; -.
KEGG; hsa:1869; -.
UCSC; uc002wzu.5; human.
CTD; 1869; -.
DisGeNET; 1869; -.
EuPathDB; HostDB:ENSG00000101412.12; -.
GeneCards; E2F1; -.
HGNC; HGNC:3113; E2F1.
HPA; CAB000329; -.
HPA; CAB019308; -.
HPA; HPA008003; -.
HPA; HPA029735; -.
MIM; 189971; gene.
neXtProt; NX_Q01094; -.
OpenTargets; ENSG00000101412; -.
PharmGKB; PA152; -.
eggNOG; KOG2577; Eukaryota.
eggNOG; ENOG410XNYI; LUCA.
GeneTree; ENSGT00550000074403; -.
HOGENOM; HOG000232045; -.
HOVERGEN; HBG002227; -.
InParanoid; Q01094; -.
KO; K17454; -.
OMA; ICTTQLR; -.
OrthoDB; EOG091G087U; -.
PhylomeDB; Q01094; -.
TreeFam; TF105566; -.
Reactome; R-HSA-111448; Activation of NOXA and translocation to mitochondria.
Reactome; R-HSA-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
Reactome; R-HSA-1362277; Transcription of E2F targets under negative control by DREAM complex.
Reactome; R-HSA-1362300; Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1.
Reactome; R-HSA-139915; Activation of PUMA and translocation to mitochondria.
Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-2559585; Oncogene Induced Senescence.
Reactome; R-HSA-539107; Activation of E2F1 target genes at G1/S.
Reactome; R-HSA-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
Reactome; R-HSA-68689; CDC6 association with the ORC:origin complex.
Reactome; R-HSA-68911; G2 Phase.
Reactome; R-HSA-69202; Cyclin E associated events during G1/S transition.
Reactome; R-HSA-69231; Cyclin D associated events in G1.
Reactome; R-HSA-69298; Association of licensing factors with the pre-replicative complex.
Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry.
Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
SignaLink; Q01094; -.
SIGNOR; Q01094; -.
ChiTaRS; E2F1; human.
EvolutionaryTrace; Q01094; -.
GeneWiki; E2F1; -.
GenomeRNAi; 1869; -.
PRO; PR:Q01094; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000101412; -.
CleanEx; HS_E2F1; -.
Genevisible; Q01094; HS.
GO; GO:0005813; C:centrosome; IDA:HPA.
GO; GO:0005739; C:mitochondrion; IEA:GOC.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0035189; C:Rb-E2F complex; IDA:BHF-UCL.
GO; GO:0001047; F:core promoter binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IMP:UniProtKB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0001227; F:transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding; IC:NTNU_SB.
GO; GO:0043276; P:anoikis; IEA:Ensembl.
GO; GO:0071398; P:cellular response to fatty acid; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEA:Ensembl.
GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
GO; GO:0000077; P:DNA damage checkpoint; IMP:UniProtKB.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
GO; GO:0030900; P:forebrain development; IEA:Ensembl.
GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IEA:Ensembl.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:UniProtKB.
GO; GO:1990086; P:lens fiber cell apoptotic process; IEA:Ensembl.
GO; GO:0048255; P:mRNA stabilization; IDA:BHF-UCL.
GO; GO:0043392; P:negative regulation of DNA binding; IDA:UniProtKB.
GO; GO:0045599; P:negative regulation of fat cell differentiation; ISS:UniProtKB.
GO; GO:0070345; P:negative regulation of fat cell proliferation; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0071930; P:negative regulation of transcription involved in G1/S transition of mitotic cell cycle; IMP:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IDA:BHF-UCL.
GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IMP:BHF-UCL.
GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; ISS:UniProtKB.
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;
3D-structure; Acetylation; Activator; Apoptosis; Cell cycle;
Complete proteome; DNA-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Transcription; Transcription regulation.
CHAIN 1 437 Transcription factor E2F1.
/FTId=PRO_0000219461.
DNA_BIND 110 194 {ECO:0000255}.
REGION 67 108 Cyclin A:CDK2 binding.
{ECO:0000269|PubMed:8033208}.
REGION 89 191 Interaction with BIRC2/c-IAP1.
{ECO:0000269|PubMed:21653699}.
REGION 153 174 Leucine-zipper.
REGION 192 382 Required for interaction with TRIM28.
{ECO:0000269|PubMed:17704056}.
REGION 195 284 Dimerization. {ECO:0000255}.
REGION 368 437 Transactivation.
REGION 409 426 RB1 binding.
{ECO:0000269|PubMed:12598654}.
MOTIF 158 194 DEF box.
MOD_RES 117 117 N6-acetyllysine.
{ECO:0000269|PubMed:10675335}.
MOD_RES 120 120 N6-acetyllysine.
{ECO:0000269|PubMed:10675335}.
MOD_RES 125 125 N6-acetyllysine.
{ECO:0000269|PubMed:10675335}.
MOD_RES 364 364 Phosphoserine; by CHEK2.
{ECO:0000305|PubMed:12717439}.
MOD_RES 375 375 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
VARIANT 200 200 G -> S (in dbSNP:rs35385772).
/FTId=VAR_048907.
VARIANT 252 252 R -> H (in dbSNP:rs3213172).
{ECO:0000269|Ref.5}.
/FTId=VAR_013607.
VARIANT 276 276 V -> M (in dbSNP:rs3213173).
{ECO:0000269|Ref.5}.
/FTId=VAR_013608.
VARIANT 311 311 T -> N (in dbSNP:rs3213174).
{ECO:0000269|Ref.5}.
/FTId=VAR_013609.
VARIANT 393 393 G -> S (in dbSNP:rs3213176).
{ECO:0000269|Ref.5}.
/FTId=VAR_013610.
MUTAGEN 117 117 K->R: Abolishes acetylation; when
associated with R-120 and R-125.
{ECO:0000269|PubMed:10675335}.
MUTAGEN 120 120 K->R: Abolishes acetylation; when
associated with R-117 and R-125.
{ECO:0000269|PubMed:10675335}.
MUTAGEN 125 125 K->R: Abolishes acetylation; when
associated with R-117 and R-120.
{ECO:0000269|PubMed:10675335}.
MUTAGEN 132 132 L->E: Abolishes interaction with and
repression of CEBPA and inhibition of
adipogenesis.
{ECO:0000269|PubMed:20176812}.
MUTAGEN 364 364 S->A: Abrogates in vitro phosphorylation
by CHEK2 and CHEK2-dependent
stabilization of E2F1 upon DNA damage.
{ECO:0000269|PubMed:12717439}.
MUTAGEN 411 411 Y->C: No retinoblastoma protein binding.
No effect on interaction with and
repression of CEBPA.
{ECO:0000269|PubMed:20176812,
ECO:0000269|PubMed:8413249}.
CONFLICT 89 111 KRRLDLETDHQYLAESSGPARGR -> RTPGTPRRQRRLCP
PRRPGRAPC (in Ref. 8; AAD14150).
{ECO:0000305}.
CONFLICT 313 313 S -> Y (in Ref. 4; AAC50719).
{ECO:0000305}.
CONFLICT 322 322 N -> T (in Ref. 4; AAC50719).
{ECO:0000305}.
CONFLICT 329 329 T -> N (in Ref. 4; AAC50719).
{ECO:0000305}.
HELIX 202 236 {ECO:0000244|PDB:2AZE}.
HELIX 238 243 {ECO:0000244|PDB:2AZE}.
STRAND 245 247 {ECO:0000244|PDB:2AZE}.
HELIX 248 252 {ECO:0000244|PDB:2AZE}.
TURN 257 259 {ECO:0000244|PDB:2AZE}.
STRAND 260 266 {ECO:0000244|PDB:2AZE}.
STRAND 272 277 {ECO:0000244|PDB:2AZE}.
STRAND 282 287 {ECO:0000244|PDB:2AZE}.
STRAND 289 291 {ECO:0000244|PDB:2AZE}.
STRAND 294 296 {ECO:0000244|PDB:2AZE}.
HELIX 421 424 {ECO:0000244|PDB:1O9K}.
SEQUENCE 437 AA; 46920 MW; 003B3F654F0C60DF CRC64;
MALAGAPAGG PCAPALEALL GAGALRLLDS SQIVIISAAQ DASAPPAPTG PAAPAAGPCD
PDLLLFATPQ APRPTPSAPR PALGRPPVKR RLDLETDHQY LAESSGPARG RGRHPGKGVK
SPGEKSRYET SLNLTTKRFL ELLSHSADGV VDLNWAAEVL KVQKRRIYDI TNVLEGIQLI
AKKSKNHIQW LGSHTTVGVG GRLEGLTQDL RQLQESEQQL DHLMNICTTQ LRLLSEDTDS
QRLAYVTCQD LRSIADPAEQ MVMVIKAPPE TQLQAVDSSE NFQISLKSKQ GPIDVFLCPE
ETVGGISPGK TPSQEVTSEE ENRATDSATI VSPPPSSPPS SLTTDPSQSL LSLEQEPLLS
RMGSLRAPVD EDRLSPLVAA DSLLEHVRED FSGLLPEEFI SLSPPHEALD YHFGLEEGEG
IRDLFDCDFG DLTPLDF


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