Q01094 (E2F1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription factor E2F1
Short name=E2F-1

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

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

Protein attributes

Sequence length	437 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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. Ref.13 Ref.17 Ref.20 Ref.24
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. 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. Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.22 Ref.24
Subcellular location	Nucleus.
Post-translational modification	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. Ref.14 Ref.20 Ref.23 Ref.25 Ref.26 Acetylation stimulates DNA-binding. Enhanced under stress conditions such as DNA damage and inhibited by retinoblastoma protein pRB. Regulated by KAP1/TRIM28 which recruits HDAC1 to E2F1 resulting in deacetylation. Acetylated by P/CAF/KAT2B.
Sequence similarities	Belongs to the E2F/DP family.
Sequence caution	The sequence AAB24289.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Apoptosis Cell cycle Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Ligand	DNA-binding
Molecular function	Activator
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA damage checkpoint Inferred from mutant phenotype Ref.20. Source: UniProtKB G1 phase of mitotic cell cycle Traceable author statement. Source: Reactome G2 phase of mitotic cell cycle Traceable author statement. Source: Reactome apoptotic process Inferred from mutant phenotype Ref.20. Source: UniProtKB cell proliferation Traceable author statement. Source: ProtInc mRNA stabilization Inferred from direct assay. Source: BHF-UCL negative regulation of transcription involved in G1/S phase of mitotic cell cycle Inferred from mutant phenotype. Source: BHF-UCL positive regulation of fibroblast proliferation Inferred from mutant phenotype. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: BHF-UCL regulation of G1/S transition of mitotic cell cycle Inferred from mutant phenotype. Source: BHF-UCL transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Rb-E2F complex Inferred from direct assay. Source: BHF-UCL mitochondrion Inferred from direct assay. Source: HPA
Molecular function	core promoter binding Inferred from direct assay. Source: UniProtKB cyclin-dependent protein kinase activity Traceable author statement. Source: Reactome sequence-specific DNA binding transcription factor activity Inferred from direct assay. Source: UniProtKB transcription corepressor activity Traceable author statement. Source: ProtInc transcription factor binding Inferred from physical interaction Ref.21. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DDB2	Q92466	2	EBI-448924,EBI-1176171
NCOR2	Q9Y618	2	EBI-448924,EBI-80830
PARP1	P09874	2	EBI-448924,EBI-355676
RB1	P06400	10	EBI-448924,EBI-491274
SIRT1	Q96EB6	3	EBI-448924,EBI-1802965
Sirt1	Q923E4	3	EBI-448924,EBI-1802585	From a different organism.
SP1	P08047	2	EBI-448924,EBI-298336
STAT1	P42224	2	EBI-448924,EBI-1057697
TRIM16	O95361	2	EBI-448924,EBI-727384

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

22

Leucine-zipper

DNA binding

110 – 194

85

Potential

Region

67 – 108

42

Cyclin A/CDK2 binding

Region

192 – 382

191

Required for interaction with TRIM28

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

Amino acid modifications

Modified residue

117

1

N6-acetyllysine Ref.17

Modified residue

120

1

N6-acetyllysine Ref.17

Modified residue

125

1

N6-acetyllysine Ref.17

Modified residue

364

1

Phosphoserine; by CHEK2 Probable

Modified residue

375

1

Phosphoserine Ref.23 Ref.25 Ref.26

Natural variations

Natural variant

200

1

G → S.
Corresponds to variant rs35385772 [ dbSNP | Ensembl ].

VAR_048907

Natural variant

252

1

R → H. Ref.5
Corresponds to variant rs3213172 [ dbSNP | Ensembl ].

VAR_013607

Natural variant

276

1

V → M. Ref.5
Corresponds to variant rs3213173 [ dbSNP | Ensembl ].

VAR_013608

Natural variant

311

1

T → N. Ref.5
Corresponds to variant rs3213174 [ dbSNP | Ensembl ].

VAR_013609

Natural variant

393

1

G → S. Ref.5
Corresponds to variant rs3213176 [ dbSNP | Ensembl ].

VAR_013610

Experimental info

Mutagenesis

117

1

K → R: Abolishes acetylation; when associated with R-120 and R-125. Ref.17

Mutagenesis

120

1

K → R: Abolishes acetylation; when associated with R-117 and R-125. Ref.17

Mutagenesis

125

1

K → R: Abolishes acetylation; when associated with R-117 and R-120. Ref.17

Mutagenesis

364

1

S → A: Abrogates in vitro phosphorylation by CHEK2 and CHEK2-dependent stabilization of E2F1 upon DNA damage. Ref.20

Mutagenesis

411

1

Y → C: No retinoblastoma protein binding. Ref.9

Sequence conflict

89 – 111

23

KRRLD…PARGR → RTPGTPRRQRRLCPPRRPGR APC in AAD14150. Ref.8

Sequence conflict

313

1

S → Y in AAC50719. Ref.4

Sequence conflict

322

1

N → T in AAC50719. Ref.4

Sequence conflict

329

1

T → N in AAC50719. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

437

Helix Strand Turn

Details...

Helix

202 – 236

35

Helix

238 – 243

6

Beta strand

245 – 247

3

Helix

248 – 252

5

Turn

257 – 259

3

Beta strand

260 – 266

7

Beta strand

272 – 277

6

Beta strand

282 – 287

6

Beta strand

289 – 291

3

Beta strand

294 – 296

3

Helix

421 – 424

4

Sequences

	Sequence		Length	Mass (Da)
	Q01094 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 003B3F654F0C60DF	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

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 program 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. , 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. 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]	"Regulation of E2F1 activity by acetylation." Martinez-Balbas M.A., Bauer U.M., Nielsen S.J., Brehm A., Kouzarides T. EMBO J. 19:662-671(2000) [PubMed: 10675335] [Abstract] Cited for: ACETYLATION AT LYS-117; LYS-120 AND LYS-125, DNA-BINDING, INTERACTION WITH KAT2B, FUNCTION, MUTAGENESIS OF LYS-117; LYS-120 AND LYS-125.
[18]	"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.
[19]	"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.
[20]	"Chk2 activates E2F-1 in response to DNA damage." Stevens C., Smith L., La Thangue N.B. Nat. Cell Biol. 5:401-409(2003) [PubMed: 12717439] [Abstract] Cited for: FUNCTION IN TRANSCRIPTION REGULATION, FUNCTION IN APOPTOSIS, PHOSPHORYLATION AT SER-364 BY CHEK2, MUTAGENESIS OF SER-364.
[21]	"Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism for phosphorylation-induced E2F release." Rubin S.M., Gall A.-L., Zheng N., Pavletich N.P. Cell 123:1093-1106(2005) [PubMed: 16360038] [Abstract] Cited for: INTERACTION WITH WITH RB1 AND TFDP1.
[22]	"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.
[23]	"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: Cervix carcinoma.
[24]	"Regulation of E2F1 function by the nuclear corepressor KAP1." Wang C., Rauscher F.J. III, Cress W.D., Chen J. J. Biol. Chem. 282:29902-29909(2007) [PubMed: 17704056] [Abstract] Cited for: INTERACTION WITH HDAC1 AND TRIM28, FUNCTION, ACETYLATION, DEACETYLATION.
[25]	"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. Tissue: Cervix carcinoma.
[26]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[27]	"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.
[28]	"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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00005630.

PIR

JC4929.

RefSeq

NP_005216.1. NM_005225.2.

UniGene

Hs.654393.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H24	X-ray	2.50	E	87-95	[»]
1O9K	X-ray	2.60	P/Q/R/S	409-426	[»]
2AZE	X-ray	2.55	B	200-301	[»]

ProteinModelPortal

Q01094.

SMR

Q01094. Positions 126-190, 201-301.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-24227N.

IntAct

Q01094. 23 interactions.

MINT

MINT-112765.

STRING

Q01094.

PTM databases

PhosphoSite

Q01094.

Polymorphism databases

DMDM

400928.

Proteomic databases

PRIDE

Q01094.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000343380; ENSP00000345571; ENSG00000101412.
ENST00000402461; ENSP00000385002; ENSG00000101412.

GeneID

1869.

KEGG

hsa:1869.

UCSC

uc002wzu.2. human.

Organism-specific databases

CTD

1869.

GeneCards

GC20M032263.

H-InvDB

HIX0027663.

HGNC

HGNC:3113. E2F1.

HPA

CAB000329.
CAB019308.
HPA008003.

MIM

189971. gene.

neXtProt

NX_Q01094.

PharmGKB

PA152.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG19885.

GeneTree

ENSGT00550000074403.

HOGENOM

HBG715983.

HOVERGEN

HBG002227.

InParanoid

Q01094.

OMA

ICTTQLR.

OrthoDB

EOG42821X.

PhylomeDB

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.

Gene expression databases

ArrayExpress

Q01094.

Bgee

Q01094.

CleanEx

HS_E2F1.

Genevestigator

Q01094.

GermOnline

ENSG00000101412. Homo sapiens.

Family and domain databases

InterPro

IPR015633. E2F.
IPR003316. E2F_TDP.
IPR015634. Transcription_factor_E2F1.
IPR011991. WHTH_trsnscrt_rep_DNA-bd.
[Graphical view]

Gene3D

G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.

KO

K06620.

PANTHER

PTHR12081. E2F. 1 hit.
PTHR12081:SF13. E2F1. 1 hit.

Pfam

PF02319. E2F_TDP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

7643.

SOURCE

Search...

Entry information

Entry name

E2F1_HUMAN

Accession

Primary (citable) accession number: Q01094
Secondary accession number(s): Q13143, Q92768

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	January 25, 2012
This is version 142 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.