[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0092-8674(92)90107-N; PubMed=1638634 [NCBI, ExPASy, EBI, Israel, Japan] 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]. DOI=10.1016/0092-8674(92)90108-O; PubMed=1638635 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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]. DOI=10.1016/0378-1119(96)00184-9; PubMed=8964493 [NCBI, ExPASy, EBI, Israel, Japan] 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]. DOI=10.1038/414865a; PubMed=11780052 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1016/0092-8674(94)90582-7; PubMed=8033208 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1073/pnas.91.9.3602; PubMed=8170954 [NCBI, ExPASy, EBI, Israel, Japan] 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]	PHOSPHORYLATION. PubMed=7838523 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[15]	REGULATION BY CYCLIN-DEPENDENT KINASES. PubMed=9199321 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[16]	INTERACTION WITH ARID3A. DOI=10.1038/sj.onc.1202163; PubMed=9780002 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[17]	INTERACTION WITH TRRAP. DOI=10.1074/jbc.M102067200; PubMed=11418595 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[18]	INTERACTION WITH TOPBP1. DOI=10.1128/MCB.23.9.3287-3304.2003; PubMed=12697828 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[19]	INTERACTION WITH EAPP. DOI=10.1091/mbc.E04-11-0975; PubMed=15716352 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[20]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[21]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[22]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 87-95. DOI=10.1021/bi0268910; PubMed=12501191 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[23]	X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 409-426 IN COMPLEX WITH RB1. DOI=10.1073/pnas.0436813100; PubMed=12598654 [NCBI, ExPASy, EBI, Israel, Japan] 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).

Comments

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. E2F-1 binds preferentially RB1 protein, in a cell-cycle dependent manner. It can mediate both cell proliferation and p53-dependent apoptosis.
SUBUNIT: Component of the DRTF1/E2F transcription factor complex. Forms heterodimers with DP family members. The E2F-1 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 RB protein, 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.
INTERACTION:
Q92466:DDB2; NbExp=2; IntAct=EBI-448924, EBI-1176171;
Q9UQ80:PA2G4; NbExp=1; IntAct=EBI-448924, EBI-924893;
P09874:PARP1; NbExp=2; IntAct=EBI-448924, EBI-355676;
P55345:PRMT2; NbExp=1; IntAct=EBI-448924, EBI-78458;
P06400:RB1; NbExp=1; IntAct=EBI-448924, EBI-491274;
P08047:SP1; NbExp=2; IntAct=EBI-448924, EBI-298336;
O89090:Sp1 (xeno); NbExp=1; IntAct=EBI-448924, EBI-645192;
Q9Y4A5:TRRAP; NbExp=1; IntAct=EBI-448924, EBI-399128;
SUBCELLULAR LOCATION: Nucleus.
PTM: Phosphorylated by CDK2 and cyclin A-CDK2 in the S-phase.
SIMILARITY: Belongs to the E2F/DP family.
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/";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M96577; AAA35782.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U47677; AAC50719.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U47675; AAC50719.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U47676; AAC50719.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S49592; AAB24289.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF516106; AAM47604.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL121906; CAC08486.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC050369; AAH50369.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC058902; AAH58902.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S74230; AAD14150.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00005630; -.

JC4929; JC4929.

NP_005216.1; -.

3D structure databases

PDB

1H24; X-ray; 2.50 A; E=87-95.	[ExPASy / RCSB / EBI]
1O9K; X-ray; 2.60 A; P/Q/R/S=409-426.	[ExPASy / RCSB / EBI]
2AZE; X-ray; 2.55 A; B=200-301.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1H24; -.
1O9K; -.
2AZE; -.

SMR

Q01094; 126-190.

ModBase

Q01094.

Protein-protein interaction databases

DIP

DIP:200N; -.
DIP:24227N; -.
DIP:498N; -.

IntAct

Q01094; 9.

PTM databases

PhosphoSite

Q01094; -.

Enzyme and pathway databases

Pathway_Interaction_DB

nfat_tfpathway; Calcineurin-regulated NFAT-dependent transcription in lymphocytes.
il2_pi3kpathway; IL2 signaling events mediated by PI3K.
p75ntrpathway; p75(NTR)-mediated signaling.
telomerasepathway; Regulation of Telomerase.

Reactome

REACT_152; Cell Cycle, Mitotic.

Organism-specific databases

GC20M031727; -.

HIX0027663; -.

HGNC:3113; E2F1.

CAB000329; -.

189971; gene. [NCBI / EBI]

PharmGKB

PA152; -.

Gene expression databases

Q01094; -.

Q01094; -.

HS_E2F1; -.

ENSG00000101412; Homo sapiens.

Ontologies

GO:0003714;	Molecular function: transcription corepressor activity (traceable author statement from ProtInc).
GO:0003700;	Molecular function: transcription factor activity (inferred from direct assay from UniProtKB).
GO:0006915;	Biological process: apoptosis (traceable author statement from ProtInc).
GO:0008283;	Biological process: cell proliferation (traceable author statement from ProtInc).
GO:0000080;	Biological process: G1 phase of mitotic cell cycle (traceable author statement from ProtInc).
GO:0000122;	Biological process: negative regulation of transcription from RNA polymerase II promoter (traceable author statement from ProtInc).
GO:0006350;	Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR015633; E2F.
IPR015634; E2F1.
IPR003316; E2F_TDP.
IPR011991; Wing_hlx_DNA_bd.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.

PANTHER

PTHR12081; E2F; 1.
PTHR12081:SF13; E2F1; 1.

Pfam

PF02319; E2F_TDP; 1.
Pfam graphical view of domain structure.

Proteomic databases

PRIDE

Q01094; -.

Genome annotation databases

Ensembl

ENSG00000101412; Homo sapiens. [Contig view]

GeneID

1869; -.

KEGG

hsa:1869; -.

Phylogenomic databases

HOVERGEN

Q01094; -.

OMA

Q01094; QWLGSHT.

Other

7643; -.

E2F1; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Activator; Apoptosis; Cell cycle; DNA-binding; Nucleus; Phosphoprotein; Polymorphism; Transcription; Transcription regulation.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 437`	`437`	`Transcription factor E2F1.`	`PRO_0000219461`
`DOMAIN`	`153 174`	`22`	`Leucine-zipper.`
`DNA_BIND`	`110 194`	`85`	`Potential.`
`REGION`	`67 108`	`42`	`Cyclin A/CDK2 binding.`
`REGION`	`195 284`	`90`	`Dimerization (Potential).`
`REGION`	`368 437`	`70`	`Transactivation.`
`REGION`	`409 426`	`18`	`Retinoblastoma protein RB1 binding (Potential).`
`MOTIF`	`158 194`	`37`	`DEF box.`
`MOD_RES`	`375 375`		`Phosphoserine.`
`VARIANT`	`200 200`	`1`	`G -> S (in dbSNP:rs35385772 [NCBI]).`	`VAR_048907`
`VARIANT`	`252 252`	`1`	`R -> H (in dbSNP:rs3213172 [NCBI]).`	`VAR_013607`
`VARIANT`	`276 276`	`1`	`V -> M (in dbSNP:rs3213173 [NCBI]).`	`VAR_013608`
`VARIANT`	`311 311`	`1`	`T -> N (in dbSNP:rs3213174 [NCBI]).`	`VAR_013609`
`VARIANT`	`393 393`	`1`	`G -> S (in dbSNP:rs3213176 [NCBI]).`	`VAR_013610`
`MUTAGEN`	`411 411`		`Y->C: No retinoblastoma protein binding.`
`CONFLICT`	`89 111`		`KRRLDLETDHQYLAESSGPARGR -> RTPGTPRRQRRLCPPRRPGRAPC (in Ref. 8).`
`CONFLICT`	`313 313`		`S -> Y (in Ref. 4; AAC50719).`
`CONFLICT`	`322 322`		`N -> T (in Ref. 4; AAC50719).`
`CONFLICT`	`329 329`		`T -> N (in Ref. 4; AAC50719).`
`HELIX`	`202 236`	`35`
`HELIX`	`238 243`	`6`
`STRAND`	`245 247`	`3`
`HELIX`	`248 252`	`5`
`TURN`	`257 259`	`3`
`STRAND`	`260 266`	`7`
`STRAND`	`272 277`	`6`
`STRAND`	`282 287`	`6`
`STRAND`	`289 291`	`3`
`STRAND`	`294 296`	`3`
`HELIX`	`421 424`	`4`

Sequence information

Length: 437 AA [This is the length of the unprocessed precursor]

Molecular weight: 46920 Da [This is the MW of the unprocessed precursor]

CRC64: 003B3F654F0C60DF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALAGAPAGG PCAPALEALL GAGALRLLDS SQIVIISAAQ DASAPPAPTG PAAPAAGPCD 

        70         80         90        100        110        120 
PDLLLFATPQ APRPTPSAPR PALGRPPVKR RLDLETDHQY LAESSGPARG RGRHPGKGVK 

       130        140        150        160        170        180 
SPGEKSRYET SLNLTTKRFL ELLSHSADGV VDLNWAAEVL KVQKRRIYDI TNVLEGIQLI 

       190        200        210        220        230        240 
AKKSKNHIQW LGSHTTVGVG GRLEGLTQDL RQLQESEQQL DHLMNICTTQ LRLLSEDTDS 

       250        260        270        280        290        300 
QRLAYVTCQD LRSIADPAEQ MVMVIKAPPE TQLQAVDSSE NFQISLKSKQ GPIDVFLCPE 

       310        320        330        340        350        360 
ETVGGISPGK TPSQEVTSEE ENRATDSATI VSPPPSSPPS SLTTDPSQSL LSLEQEPLLS 

       370        380        390        400        410        420 
RMGSLRAPVD EDRLSPLVAA DSLLEHVRED FSGLLPEEFI SLSPPHEALD YHFGLEEGEG 

       430 
IRDLFDCDFG DLTPLDF

Q01094 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools