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Q01094

- E2F1_HUMAN

UniProt

Q01094 - E2F1_HUMAN

Protein

Transcription factor E2F1

Gene

E2F1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 171 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    4. sequence-specific DNA binding Source: Ensembl
    5. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    6. transcription corepressor activity Source: ProtInc
    7. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. anoikis Source: Ensembl
    2. apoptotic process Source: Reactome
    3. cell proliferation Source: ProtInc
    4. cellular response to fatty acid Source: Ensembl
    5. cellular response to hypoxia Source: Ensembl
    6. DNA damage checkpoint Source: UniProtKB
    7. forebrain development Source: Ensembl
    8. G1/S transition of mitotic cell cycle Source: Reactome
    9. intrinsic apoptotic signaling pathway Source: Reactome
    10. intrinsic apoptotic signaling pathway by p53 class mediator Source: Ensembl
    11. intrinsic apoptotic signaling pathway in response to DNA damage Source: UniProtKB
    12. lens fiber cell apoptotic process Source: Ensembl
    13. mitotic cell cycle Source: Reactome
    14. mitotic G1 phase Source: ProtInc
    15. mitotic G2 phase Source: Reactome
    16. mRNA stabilization Source: BHF-UCL
    17. negative regulation of transcription, DNA-templated Source: BHF-UCL
    18. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    19. negative regulation of transcription involved in G1/S transition of mitotic cell cycle Source: BHF-UCL
    20. Notch signaling pathway Source: Reactome
    21. positive regulation of fibroblast proliferation Source: BHF-UCL
    22. positive regulation of gene expression Source: BHF-UCL
    23. positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
    24. positive regulation of transcription, DNA-templated Source: BHF-UCL
    25. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    26. regulation of G1/S transition of mitotic cell cycle Source: BHF-UCL
    27. regulation of transcription, DNA-templated Source: UniProtKB
    28. spermatogenesis Source: Ensembl
    29. transcription, DNA-templated Source: UniProtKB-KW

    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

    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-acetyllysine2 Publications
    Modified residuei120 – 1201N6-acetyllysine2 Publications
    Modified residuei125 – 1251N6-acetyllysine2 Publications
    Modified residuei364 – 3641Phosphoserine; by CHEK22 Publications
    Modified residuei375 – 3751Phosphoserine4 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. 106 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.
    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.

    Q01094-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALAGAPAGG PCAPALEALL GAGALRLLDS SQIVIISAAQ DASAPPAPTG    50
    PAAPAAGPCD PDLLLFATPQ APRPTPSAPR PALGRPPVKR RLDLETDHQY 100
    LAESSGPARG RGRHPGKGVK SPGEKSRYET SLNLTTKRFL ELLSHSADGV 150
    VDLNWAAEVL KVQKRRIYDI TNVLEGIQLI AKKSKNHIQW LGSHTTVGVG 200
    GRLEGLTQDL RQLQESEQQL DHLMNICTTQ LRLLSEDTDS QRLAYVTCQD 250
    LRSIADPAEQ MVMVIKAPPE TQLQAVDSSE NFQISLKSKQ GPIDVFLCPE 300
    ETVGGISPGK TPSQEVTSEE ENRATDSATI VSPPPSSPPS SLTTDPSQSL 350
    LSLEQEPLLS RMGSLRAPVD EDRLSPLVAA DSLLEHVRED FSGLLPEEFI 400
    SLSPPHEALD YHFGLEEGEG IRDLFDCDFG DLTPLDF 437
    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.
    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. 106 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 .
    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.
    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

    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 1, 2014
    This is version 171 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

    Dasty 3