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Q01094 (E2F1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 169. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription factor E2F1

Short name=E2F-1
Alternative name(s):
PBR3
Retinoblastoma-associated protein 1
Short name=RBAP-1
Retinoblastoma-binding protein 3
Short name=RBBP-3
pRB-binding protein E2F-1
Gene names
Name:E2F1
Synonyms:RBBP3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length437 AA.
Sequence statusComplete.
Protein existenceEvidence 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. E2F1 binds preferentially RB1 in a cell-cycle dependent manner. It can mediate both cell proliferation and TP53/p53-dependent apoptosis. Ref.13 Ref.18 Ref.21 Ref.25

Enzyme regulation

BIRC2/c-IAP1 stimulates its transcriptional activity. Ref.28

Subunit structure

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). Interacts with human cytomegalovirus/HHV-5 protein UL123. Ref.14 Ref.17 Ref.18 Ref.19 Ref.20 Ref.22 Ref.23 Ref.25 Ref.28

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.15 Ref.21

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. Ref.18 Ref.25

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 processApoptosis
Cell cycle
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   LigandDNA-binding
   Molecular functionActivator
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage checkpoint

Inferred from mutant phenotype Ref.21. Source: UniProtKB

G1/S transition of mitotic cell cycle

Traceable author statement. Source: Reactome

Notch signaling pathway

Traceable author statement. Source: Reactome

anoikis

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Traceable author statement. Source: Reactome

cell proliferation

Traceable author statement PubMed 10199402. Source: ProtInc

cellular response to fatty acid

Inferred from electronic annotation. Source: Ensembl

cellular response to hypoxia

Inferred from electronic annotation. Source: Ensembl

forebrain development

Inferred from electronic annotation. Source: Ensembl

intrinsic apoptotic signaling pathway

Traceable author statement. Source: Reactome

intrinsic apoptotic signaling pathway by p53 class mediator

Inferred from electronic annotation. Source: Ensembl

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from mutant phenotype Ref.21. Source: UniProtKB

lens fiber cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

mRNA stabilization

Inferred from direct assay PubMed 15766563. Source: BHF-UCL

mitotic G1 phase

Traceable author statement PubMed 10199402. Source: ProtInc

mitotic G2 phase

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 20224733. Source: BHF-UCL

negative regulation of transcription involved in G1/S transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 20224733. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 20224733. Source: BHF-UCL

positive regulation of fibroblast proliferation

Inferred from mutant phenotype PubMed 20224733. Source: BHF-UCL

positive regulation of gene expression

Inferred from direct assay PubMed 15766563. Source: BHF-UCL

positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway

Traceable author statement. Source: Reactome

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 20224733. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 20224733. Source: BHF-UCL

regulation of G1/S transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 20224733. Source: BHF-UCL

regulation of transcription, DNA-templated

Inferred from direct assay Ref.21. Source: UniProtKB

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentRb-E2F complex

Inferred from direct assay PubMed 20224733. Source: BHF-UCL

cytoplasm

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.21. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from direct assay PubMed 15731768. Source: UniProtKB

core promoter binding

Inferred from direct assay PubMed 15735762. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.19PubMed 11486038Ref.22Ref.25PubMed 20622854Ref.28. Source: UniProtKB

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 15731768. Source: UniProtKB

transcription corepressor activity

Traceable author statement PubMed 10199402. Source: ProtInc

transcription factor binding

Inferred from physical interaction Ref.22. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 437437Transcription factor E2F1
PRO_0000219461

Regions

DNA binding110 – 19485 Potential
Region67 – 10842Cyclin A/CDK2 binding
Region89 – 191103Interaction with BIRC2/c-IAP1
Region153 – 17422Leucine-zipper
Region192 – 382191Required for interaction with TRIM28
Region195 – 28490Dimerization Potential
Region368 – 43770Transactivation
Region409 – 42618Retinoblastoma protein RB1 binding Potential
Motif158 – 19437DEF box

Amino acid modifications

Modified residue1171N6-acetyllysine Ref.18
Modified residue1201N6-acetyllysine Ref.18
Modified residue1251N6-acetyllysine Ref.18
Modified residue3641Phosphoserine; by CHEK2 Probable
Modified residue3751Phosphoserine Ref.24 Ref.26 Ref.27

Natural variations

Natural variant2001G → S.
Corresponds to variant rs35385772 [ dbSNP | Ensembl ].
VAR_048907
Natural variant2521R → H. Ref.5
Corresponds to variant rs3213172 [ dbSNP | Ensembl ].
VAR_013607
Natural variant2761V → M. Ref.5
Corresponds to variant rs3213173 [ dbSNP | Ensembl ].
VAR_013608
Natural variant3111T → N. Ref.5
Corresponds to variant rs3213174 [ dbSNP | Ensembl ].
VAR_013609
Natural variant3931G → S. Ref.5
Corresponds to variant rs3213176 [ dbSNP | Ensembl ].
VAR_013610

Experimental info

Mutagenesis1171K → R: Abolishes acetylation; when associated with R-120 and R-125. Ref.18
Mutagenesis1201K → R: Abolishes acetylation; when associated with R-117 and R-125. Ref.18
Mutagenesis1251K → R: Abolishes acetylation; when associated with R-117 and R-120. Ref.18
Mutagenesis3641S → A: Abrogates in vitro phosphorylation by CHEK2 and CHEK2-dependent stabilization of E2F1 upon DNA damage. Ref.21
Mutagenesis4111Y → C: No retinoblastoma protein binding. Ref.9
Sequence conflict89 – 11123KRRLD…PARGR → RTPGTPRRQRRLCPPRRPGR APC in AAD14150. Ref.8
Sequence conflict3131S → Y in AAC50719. Ref.4
Sequence conflict3221N → T in AAC50719. Ref.4
Sequence conflict3291T → N in AAC50719. Ref.4

Secondary structure

..................... 437
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q01094 [UniParc].

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

FASTA43746,920
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION IN APOPTOSIS.
[14]"Interaction of the 72-kilodalton human cytomegalovirus IE1 gene product with E2F1 coincides with E2F-dependent activation of dihydrofolate reductase transcription."
Margolis M.J., Pajovic S., Wong E.L., Wade M., Jupp R., Nelson J.A., Azizkhan J.C.
J. Virol. 69:7759-7767(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HHV-5 PROTEIN UL123.
[15]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[16]"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] [Europe PMC] [Abstract]
Cited for: REGULATION BY CYCLIN-DEPENDENT KINASES.
[17]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARID3A.
[18]"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] [Europe PMC] [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.
[19]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRRAP.
[20]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TOPBP1.
[21]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TRANSCRIPTION REGULATION, FUNCTION IN APOPTOSIS, PHOSPHORYLATION AT SER-364 BY CHEK2, MUTAGENESIS OF SER-364.
[22]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH WITH RB1 AND TFDP1.
[23]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EAPP.
[24]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HDAC1 AND TRIM28, FUNCTION, ACETYLATION, DEACETYLATION.
[26]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[27]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[28]"Cellular inhibitor of apoptosis protein-1 (cIAP1) can regulate E2F1 transcription factor-mediated control of cyclin transcription."
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.
J. Biol. Chem. 286:26406-26417(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BIRC2/C-IAP1, ENZYME REGULATION.
[29]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 87-95.
[30]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 409-426 IN COMPLEX WITH RB1.
+Additional computationally mapped references.

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.
CCDSCCDS13224.1.
PIRJC4929.
RefSeqNP_005216.1. NM_005225.2.
UniGeneHs.654393.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H24X-ray2.50E87-95[»]
1O9KX-ray2.60P/Q/R/S409-426[»]
2AZEX-ray2.55B200-301[»]
ProteinModelPortalQ01094.
SMRQ01094. Positions 126-190, 201-301.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108201. 106 interactions.
DIPDIP-24227N.
IntActQ01094. 33 interactions.
MINTMINT-112765.
STRING9606.ENSP00000345571.

Chemistry

BindingDBQ01094.
ChEMBLCHEMBL4382.

PTM databases

PhosphoSiteQ01094.

Polymorphism databases

DMDM400928.

Proteomic databases

MaxQBQ01094.
PaxDbQ01094.
PRIDEQ01094.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000343380; ENSP00000345571; ENSG00000101412.
GeneID1869.
KEGGhsa:1869.
UCSCuc002wzu.4. human.

Organism-specific databases

CTD1869.
GeneCardsGC20M032263.
HGNCHGNC:3113. E2F1.
HPACAB000329.
CAB019308.
HPA008003.
MIM189971. gene.
neXtProtNX_Q01094.
PharmGKBPA152.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG328718.
HOGENOMHOG000232045.
HOVERGENHBG002227.
InParanoidQ01094.
KOK17454.
OMARHPGKGV.
OrthoDBEOG738058.
PhylomeDBQ01094.
TreeFamTF105566.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_115566. Cell Cycle.
REACT_120956. Cellular responses to stress.
REACT_578. Apoptosis.
SignaLinkQ01094.

Gene expression databases

BgeeQ01094.
CleanExHS_E2F1.
GenevestigatorQ01094.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR015633. E2F.
IPR003316. E2F_TDP.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERPTHR12081. PTHR12081. 1 hit.
PfamPF02319. E2F_TDP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSE2F1. human.
EvolutionaryTraceQ01094.
GeneWikiE2F1.
GenomeRNAi1869.
NextBio7643.
PROQ01094.
SOURCESearch...

Entry information

Entry nameE2F1_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 169 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM