Transcription factor E2F1 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot Q01094 (E2F1_HUMAN)

Last modified November 25, 2008. Version 104. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Transcription factor E2F1
      Short name=E2F-1
Alternative name(s):
    Retinoblastoma-binding protein 3
      Short name=RBBP-3
    PRB-binding protein E2F-1
    PBR3
    Retinoblastoma-associated protein 1
      Short name=RBAP-1

Gene names

Name:	E2F1
Synonyms:	RBBP3

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	437 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (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 structure	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.
Subcellular location	Nucleus.
Post-translational modification	Phosphorylated by CDK2 and cyclin A-CDK2 in the S-phase.
Sequence similarities	Belongs to the E2F/DP family.

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Ontologies

Keywords
Biological process	Apoptosis Cell cycle Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Ligand	DNA-binding
Molecular function	Activator
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	G1 phase of mitotic cell cycle Traceable author statement. Source: ProtInc apoptosis Traceable author statement. Source: ProtInc cell proliferation Traceable author statement. Source: ProtInc negative regulation of transcription from RNA polymerase II promoter Traceable author statement. Source: ProtInc
Cellular component	transcription factor complex Inferred from electronic annotation. Source: InterPro
Molecular function	transcription corepressor activity Traceable author statement. Source: ProtInc transcription factor activity Ref.17 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
DDB2	Q92466	2	EBI-448924,EBI-1176171
PA2G4	Q9UQ80	1	EBI-448924,EBI-924893
PARP1	P09874	2	EBI-448924,EBI-355676
PRMT2	P55345	1	EBI-448924,EBI-78458
RB1	P06400	1	EBI-448924,EBI-491274
SP1	P08047	2	EBI-448924,EBI-298336
Sp1	O89090	1	EBI-448924,EBI-645192	From a different organism.
TRRAP	Q9Y4A5	1	EBI-448924,EBI-399128

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 437

437

Transcription factor E2F1

PRO_0000219461

Regions

Domain

153 – 174

Leucine-zipper

DNA binding

110 – 194

Potential

Region

67 – 108

Cyclin A/CDK2 binding

Region

195 – 284

Dimerization Potential

Region

368 – 437

Transactivation

Region

409 – 426

Retinoblastoma protein RB1 binding Potential

Motif

158 – 194

DEF box

Amino acid modifications

Modified residue

375

Phosphoserine

Natural variations

Natural variant

252

R → H: dbSNP rs3213172.

VAR_013607

Natural variant

276

V → M: dbSNP rs3213173.

VAR_013608

Natural variant

311

T → N: dbSNP rs3213174.

VAR_013609

Natural variant

393

G → S: dbSNP rs3213176.

VAR_013610

Experimental info

Mutagenesis

411

Y → C: No retinoblastoma protein binding

Sequence conflict

89 – 111

KRRLD…PARGR → RTPGTPRRQRRLCPPRRPGR APC Ref.8

Sequence conflict

313

S → Y in AAC50719. Ref.4

Sequence conflict

322

N → T in AAC50719. Ref.4

Sequence conflict

329

T → N in AAC50719. Ref.4

Secondary structure

437

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q01094-1 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 003B3F654F0C60DF
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FASTA

437

46,920

        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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A cDNA encoding a pRB-binding protein with properties of the transcription factor E2F." Helin K., Lees J.A., Vidal M., Dyson N.J., Harlow E., Fattaey A. Cell 70:337-350(1992) [PubMed: 1638634] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Expression cloning of a cDNA encoding a retinoblastoma-binding protein with E2F-like properties." 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. Cell 70:351-364(1992) [PubMed: 1638635] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Molecular cloning of cellular genes encoding retinoblastoma-associated proteins: identification of a gene with properties of the transcription factor E2F." Shan B., Zhu X., Chen P.L., Durfee T., Yang Y., Sharp D., Lee W.H. Mol. Cell. Biol. 12:5620-5631(1992) [PubMed: 1448092] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Structure and partial genomic sequence of the human E2F1 gene." Neuman E., Sellers W.R.S., McNeil J.A., Lawrence J.B., Kaelin W.G. Jr. Gene 173:163-169(1996) [PubMed: 8964493] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)." Rieder M.J., Livingston R.J., Braun A.C., Montoya M.A., Chung M.-W., Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-252; MET-276; ASN-311 AND SER-393.
[6]	"The DNA sequence and comparative analysis of human chromosome 20." 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. Rogers J. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pancreas and Skin.
[8]	"Autoregulatory control of E2F1 expression in response to positive and negative regulators of cell cycle progression." Johnson D.G., Ohtani K., Nevins J.R. Genes Dev. 8:1514-1525(1994) [PubMed: 7958836] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-111.
[9]	"Inhibition of E2F-1 transactivation by direct binding of the retinoblastoma protein." Helin K., Harlow E., Fattaey A. Mol. Cell. Biol. 13:6501-6508(1993) [PubMed: 8413249] [Abstract] Cited for: TRANSACTIVATION INHIBITION, MUTAGENESIS OF TYR-411.
[10]	"Negative regulation of the growth-promoting transcription factor E2F-1 by a stably bound cyclin A-dependent protein kinase." Krek W., Ewen M.E., Shirodkar S., Arany Z., Kaelin W.G. Jr., Livingston D.M. Cell 78:161-172(1994) [PubMed: 8033208] [Abstract] Cited for: DOMAIN CYCLIN A/CDK2 BINDING.
[11]	"Differential regulation of E2F transactivation by cyclin/cdk2 complexes." Dynlacht B.D., Flores O., Lees J.A., Harlow E. Genes Dev. 8:1772-1786(1994) [PubMed: 7958856] [Abstract] Cited for: DIFFERENTIAL REGULATION BY CYCLIN/CDK2 KINASES.
[12]	"Cyclin A/CDK2 binds directly to E2F-1 and inhibits the DNA-binding activity of E2F-1/DP-1 by phosphorylation." Xu M., Sheppard K.-A., Peng C.-Y., Yee A.S., Piwnica-Worms H. Mol. Cell. Biol. 14:8420-8431(1994) [PubMed: 7969176] [Abstract] Cited for: INHIBITION OF DNA-BINDING.
[13]	"P53 and E2F-1 cooperate to mediate apoptosis." Wu X., Levine A.J. Proc. Natl. Acad. Sci. U.S.A. 91:3602-3606(1994) [PubMed: 8170954] [Abstract] Cited for: FUNCTION IN APOPTOSIS.
[14]	"Phosphorylation of E2F-1 by cyclin A-cdk2." Kitagawa M., Higashi H., Suzuki-Takahashi I., Segawa K., Hanks S.K., Taya Y., Nishimura S., Okuyama A. Oncogene 10:229-236(1995) [PubMed: 7838523] [Abstract] Cited for: PHOSPHORYLATION.
[15]	"Specific regulation of E2F family members by cyclin-dependent kinases." Dynlacht B.D., Moberg K., Lees J.A., Harlow E., Zhu L. Mol. Cell. Biol. 17:3867-3875(1997) [PubMed: 9199321] [Abstract] Cited for: REGULATION BY CYCLIN-DEPENDENT KINASES.
[16]	"A novel E2F binding protein with Myc-type HLH motif stimulates E2F-dependent transcription by forming a heterodimer." Suzuki M., Okuyama S., Okamoto S., Shirasuna K., Nakajima T., Hachiya T., Nojima H., Sekiya S., Oda K. Oncogene 17:853-865(1998) [PubMed: 9780002] [Abstract] Cited for: INTERACTION WITH ARID3A.
[17]	"E2F transcriptional activation requires TRRAP and GCN5 cofactors." Lang S.E., McMahon S.B., Cole M.D., Hearing P. J. Biol. Chem. 276:32627-32634(2001) [PubMed: 11418595] [Abstract] Cited for: INTERACTION WITH TRRAP.
[18]	"Regulation of E2F1 by BRCT domain-containing protein TopBP1." Liu K., Lin F.-T., Ruppert J.M., Lin W.-C. Mol. Cell. Biol. 23:3287-3304(2003) [PubMed: 12697828] [Abstract] Cited for: INTERACTION WITH TOPBP1.
[19]	"EAPP, a novel E2F binding protein that modulates E2F-dependent transcription." Novy M., Pohn R., Andorfer P., Novy-Weiland T., Galos B., Schwarzmayr L., Rotheneder H. Mol. Biol. Cell 16:2181-2190(2005) [PubMed: 15716352] [Abstract] Cited for: INTERACTION WITH EAPP.
[20]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, MASS SPECTROMETRY. Tissue: Epithelium.
[21]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, MASS SPECTROMETRY.
[22]	"Specificity determinants of recruitment peptides bound to phospho-CDK2/cyclin A." Lowe E.D., Tews I., Cheng K.Y., Brown N.R., Gul S., Noble M.E.M., Gamblin S.J., Johnson L.N. Biochemistry 41:15625-15634(2002) [PubMed: 12501191] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 87-95.
[23]	"Crystal structure of the retinoblastoma tumor suppressor protein bound to E2F and the molecular basis of its regulation." Xiao B., Spencer J., Clements A., Ali-Khan N., Mittnacht S., Broceno C., Burghammer M., Perrakis A., Marmorstein R., Gamblin S.J. Proc. Natl. Acad. Sci. U.S.A. 100:2363-2368(2003) [PubMed: 12598654] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 409-426 IN COMPLEX WITH RB1.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

M96577 mRNA. Translation: AAA35782.1.
U47677, U47675, U47676 Genomic DNA. Translation: AAC50719.1.
S49592 mRNA. Translation: AAB24289.1. Different initiation.
AF516106 Genomic DNA. Translation: AAM47604.1.
AL121906 Genomic DNA. Translation: CAC08486.1.
BC050369 mRNA. Translation: AAH50369.1.
BC058902 mRNA. Translation: AAH58902.1.
S74230 Genomic DNA. Translation: AAD14150.1.

PIR

JC4929.

RefSeq

NP_005216.1.

UniGene

Hs.654393