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Q01094

- E2F1_HUMAN

UniProt

Q01094 - E2F1_HUMAN

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Protein

Transcription factor E2F1

Gene

E2F1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.4 Publications

Enzyme regulationi

BIRC2/c-IAP1 stimulates its transcriptional activity.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi110 – 19485Sequence AnalysisAdd
BLAST

GO - Molecular functioni

  1. core promoter binding Source: UniProtKB
  2. DNA binding Source: UniProtKB
  3. sequence-specific DNA binding Source: Ensembl
  4. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  5. transcription factor binding Source: UniProtKB

GO - Biological processi

  1. anoikis Source: Ensembl
  2. apoptotic process Source: Reactome
  3. cellular response to fatty acid Source: Ensembl
  4. cellular response to hypoxia Source: Ensembl
  5. DNA damage checkpoint Source: UniProtKB
  6. forebrain development Source: Ensembl
  7. G1/S transition of mitotic cell cycle Source: Reactome
  8. intrinsic apoptotic signaling pathway Source: Reactome
  9. intrinsic apoptotic signaling pathway by p53 class mediator Source: Ensembl
  10. intrinsic apoptotic signaling pathway in response to DNA damage Source: UniProtKB
  11. lens fiber cell apoptotic process Source: Ensembl
  12. mitotic cell cycle Source: Reactome
  13. mRNA stabilization Source: BHF-UCL
  14. negative regulation of transcription, DNA-templated Source: BHF-UCL
  15. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  16. negative regulation of transcription involved in G1/S transition of mitotic cell cycle Source: BHF-UCL
  17. Notch signaling pathway Source: Reactome
  18. positive regulation of fibroblast proliferation Source: BHF-UCL
  19. positive regulation of gene expression Source: BHF-UCL
  20. positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
  21. positive regulation of transcription, DNA-templated Source: BHF-UCL
  22. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  23. regulation of G1/S transition of mitotic cell cycle Source: BHF-UCL
  24. regulation of transcription, DNA-templated Source: UniProtKB
  25. spermatogenesis Source: Ensembl
  26. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Apoptosis, Cell cycle, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_111214. G0 and Early G1.
REACT_1181. Association of licensing factors with the pre-replicative complex.
REACT_118568. Pre-NOTCH Transcription and Translation.
REACT_1194. Activation of NOXA and translocation to mitochondria.
REACT_121. Activation of PUMA and translocation to mitochondria.
REACT_169325. Oncogene Induced Senescence.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_1707. CDC6 association with the ORC:origin complex.
REACT_1915. G2 Phase.
REACT_329. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_471. E2F mediated regulation of DNA replication.
REACT_683. G1/S-Specific Transcription.
REACT_821. Cyclin D associated events in G1.
SignaLinkiQ01094.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:E2F1
Synonyms:RBBP3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:3113. E2F1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. nucleoplasm Source: Reactome
  3. nucleus Source: UniProtKB
  4. Rb-E2F complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi117 – 1171K → R: Abolishes acetylation; when associated with R-120 and R-125. 1 Publication
Mutagenesisi120 – 1201K → R: Abolishes acetylation; when associated with R-117 and R-125. 1 Publication
Mutagenesisi125 – 1251K → R: Abolishes acetylation; when associated with R-117 and R-120. 1 Publication
Mutagenesisi364 – 3641S → A: Abrogates in vitro phosphorylation by CHEK2 and CHEK2-dependent stabilization of E2F1 upon DNA damage. 1 Publication
Mutagenesisi411 – 4111Y → C: No retinoblastoma protein binding. 1 Publication

Organism-specific databases

PharmGKBiPA152.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 437437Transcription factor E2F1PRO_0000219461Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei117 – 1171N6-acetyllysine1 Publication
Modified residuei120 – 1201N6-acetyllysine1 Publication
Modified residuei125 – 1251N6-acetyllysine1 Publication
Modified residuei364 – 3641Phosphoserine; by CHEK21 Publication
Modified residuei375 – 3751Phosphoserine3 Publications

Post-translational modificationi

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.5 Publications
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.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ01094.
PaxDbiQ01094.
PRIDEiQ01094.

PTM databases

PhosphoSiteiQ01094.

Expressioni

Gene expression databases

BgeeiQ01094.
CleanExiHS_E2F1.
GenevestigatoriQ01094.

Organism-specific databases

HPAiCAB000329.
CAB019308.
HPA008003.

Interactioni

Subunit structurei

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 UL123.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BTG3Q142013EBI-448924,EBI-948192
CDK7P506132EBI-448924,EBI-1245958
DDB2Q924662EBI-448924,EBI-1176171
MCPH1Q8NEM06EBI-448924,EBI-1565483
NCOR2Q9Y6182EBI-448924,EBI-80830
PARP1P098742EBI-448924,EBI-355676
PRMT5O147448EBI-448924,EBI-351098
RB1P0640020EBI-448924,EBI-491274
SIRT1Q96EB63EBI-448924,EBI-1802965
Sirt1Q923E43EBI-448924,EBI-1802585From a different organism.
SP1P080472EBI-448924,EBI-298336
STAT1P422242EBI-448924,EBI-1057697
TFDP1Q141869EBI-448924,EBI-749713
TOPBP1Q925473EBI-448924,EBI-308302
TRIM16O953612EBI-448924,EBI-727384

Protein-protein interaction databases

BioGridi108201. 110 interactions.
DIPiDIP-24227N.
IntActiQ01094. 34 interactions.
MINTiMINT-112765.
STRINGi9606.ENSP00000345571.

Structurei

Secondary structure

1
437
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi202 – 23635
Helixi238 – 2436
Beta strandi245 – 2473
Helixi248 – 2525
Turni257 – 2593
Beta strandi260 – 2667
Beta strandi272 – 2776
Beta strandi282 – 2876
Beta strandi289 – 2913
Beta strandi294 – 2963
Helixi421 – 4244

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H24X-ray2.50E87-95[»]
1O9KX-ray2.60P/Q/R/S409-426[»]
2AZEX-ray2.55B200-301[»]
ProteinModelPortaliQ01094.
SMRiQ01094. Positions 126-190, 201-301.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01094.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni67 – 10842Cyclin A/CDK2 bindingAdd
BLAST
Regioni89 – 191103Interaction with BIRC2/c-IAP1Add
BLAST
Regioni153 – 17422Leucine-zipperAdd
BLAST
Regioni192 – 382191Required for interaction with TRIM28Add
BLAST
Regioni195 – 28490DimerizationSequence AnalysisAdd
BLAST
Regioni368 – 43770TransactivationAdd
BLAST
Regioni409 – 42618Retinoblastoma protein RB1 bindingSequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi158 – 19437DEF boxAdd
BLAST

Sequence similaritiesi

Belongs to the E2F/DP family.Curated

Phylogenomic databases

eggNOGiNOG328718.
GeneTreeiENSGT00550000074403.
HOGENOMiHOG000232045.
HOVERGENiHBG002227.
InParanoidiQ01094.
KOiK17454.
OMAiRHPGKGV.
OrthoDBiEOG738058.
PhylomeDBiQ01094.
TreeFamiTF105566.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR015633. E2F.
IPR003316. E2F_TDP.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR12081. PTHR12081. 1 hit.
PfamiPF02319. E2F_TDP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q01094 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MALAGAPAGG PCAPALEALL GAGALRLLDS SQIVIISAAQ DASAPPAPTG
60 70 80 90 100
PAAPAAGPCD PDLLLFATPQ APRPTPSAPR PALGRPPVKR RLDLETDHQY
110 120 130 140 150
LAESSGPARG RGRHPGKGVK SPGEKSRYET SLNLTTKRFL ELLSHSADGV
160 170 180 190 200
VDLNWAAEVL KVQKRRIYDI TNVLEGIQLI AKKSKNHIQW LGSHTTVGVG
210 220 230 240 250
GRLEGLTQDL RQLQESEQQL DHLMNICTTQ LRLLSEDTDS QRLAYVTCQD
260 270 280 290 300
LRSIADPAEQ MVMVIKAPPE TQLQAVDSSE NFQISLKSKQ GPIDVFLCPE
310 320 330 340 350
ETVGGISPGK TPSQEVTSEE ENRATDSATI VSPPPSSPPS SLTTDPSQSL
360 370 380 390 400
LSLEQEPLLS RMGSLRAPVD EDRLSPLVAA DSLLEHVRED FSGLLPEEFI
410 420 430
SLSPPHEALD YHFGLEEGEG IRDLFDCDFG DLTPLDF
Length:437
Mass (Da):46,920
Last modified:July 1, 1993 - v1
Checksum:i003B3F654F0C60DF
GO

Sequence cautioni

The sequence AAB24289.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti89 – 11123KRRLD…PARGR → RTPGTPRRQRRLCPPRRPGR APC in AAD14150. (PubMed:7958836)CuratedAdd
BLAST
Sequence conflicti313 – 3131S → Y in AAC50719. (PubMed:8964493)Curated
Sequence conflicti322 – 3221N → T in AAC50719. (PubMed:8964493)Curated
Sequence conflicti329 – 3291T → N in AAC50719. (PubMed:8964493)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti200 – 2001G → S.
Corresponds to variant rs35385772 [ dbSNP | Ensembl ].
VAR_048907
Natural varianti252 – 2521R → H.1 Publication
Corresponds to variant rs3213172 [ dbSNP | Ensembl ].
VAR_013607
Natural varianti276 – 2761V → M.1 Publication
Corresponds to variant rs3213173 [ dbSNP | Ensembl ].
VAR_013608
Natural varianti311 – 3111T → N.1 Publication
Corresponds to variant rs3213174 [ dbSNP | Ensembl ].
VAR_013609
Natural varianti393 – 3931G → S.1 Publication
Corresponds to variant rs3213176 [ dbSNP | Ensembl ].
VAR_013610

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS13224.1.
PIRiJC4929.
RefSeqiNP_005216.1. NM_005225.2.
UniGeneiHs.654393.

Genome annotation databases

EnsembliENST00000343380; ENSP00000345571; ENSG00000101412.
ENST00000622594; ENSP00000480001; ENSG00000101412.
GeneIDi1869.
KEGGihsa:1869.
UCSCiuc002wzu.4. human.

Polymorphism databases

DMDMi400928.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS13224.1.
PIRi JC4929.
RefSeqi NP_005216.1. NM_005225.2.
UniGenei Hs.654393.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q01094.
SMRi Q01094. Positions 126-190, 201-301.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108201. 110 interactions.
DIPi DIP-24227N.
IntActi Q01094. 34 interactions.
MINTi MINT-112765.
STRINGi 9606.ENSP00000345571.

Chemistry

BindingDBi Q01094.
ChEMBLi CHEMBL4382.

PTM databases

PhosphoSitei Q01094.

Polymorphism databases

DMDMi 400928.

Proteomic databases

MaxQBi Q01094.
PaxDbi Q01094.
PRIDEi Q01094.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000343380 ; ENSP00000345571 ; ENSG00000101412 .
ENST00000622594 ; ENSP00000480001 ; ENSG00000101412 .
GeneIDi 1869.
KEGGi hsa:1869.
UCSCi uc002wzu.4. human.

Organism-specific databases

CTDi 1869.
GeneCardsi GC20M032263.
HGNCi HGNC:3113. E2F1.
HPAi CAB000329.
CAB019308.
HPA008003.
MIMi 189971. gene.
neXtProti NX_Q01094.
PharmGKBi PA152.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG328718.
GeneTreei ENSGT00550000074403.
HOGENOMi HOG000232045.
HOVERGENi HBG002227.
InParanoidi Q01094.
KOi K17454.
OMAi RHPGKGV.
OrthoDBi EOG738058.
PhylomeDBi Q01094.
TreeFami TF105566.

Enzyme and pathway databases

Reactomei REACT_111214. G0 and Early G1.
REACT_1181. Association of licensing factors with the pre-replicative complex.
REACT_118568. Pre-NOTCH Transcription and Translation.
REACT_1194. Activation of NOXA and translocation to mitochondria.
REACT_121. Activation of PUMA and translocation to mitochondria.
REACT_169325. Oncogene Induced Senescence.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_1707. CDC6 association with the ORC:origin complex.
REACT_1915. G2 Phase.
REACT_329. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_471. E2F mediated regulation of DNA replication.
REACT_683. G1/S-Specific Transcription.
REACT_821. Cyclin D associated events in G1.
SignaLinki Q01094.

Miscellaneous databases

ChiTaRSi E2F1. human.
EvolutionaryTracei Q01094.
GeneWikii E2F1.
GenomeRNAii 1869.
NextBioi 7643.
PROi Q01094.
SOURCEi Search...

Gene expression databases

Bgeei Q01094.
CleanExi HS_E2F1.
Genevestigatori Q01094.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
InterProi IPR015633. E2F.
IPR003316. E2F_TDP.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
PANTHERi PTHR12081. PTHR12081. 1 hit.
Pfami PF02319. E2F_TDP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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.

Entry informationi

Entry nameiE2F1_HUMAN
AccessioniPrimary (citable) accession number: Q01094
Secondary accession number(s): Q13143, Q92768
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: October 29, 2014
This is version 172 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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