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Q16254

- E2F4_HUMAN

UniProt

Q16254 - E2F4_HUMAN

Protein

Transcription factor E2F4

Gene

E2F4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      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. E2F4 binds with high affinity to RBL1 and RBL2. In some instances can also bind RB1.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi16 – 8570Sequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. protein domain specific binding Source: UniProtKB
    4. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    5. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. blood circulation Source: Ensembl
    2. cell volume homeostasis Source: Ensembl
    3. cilium assembly Source: Ensembl
    4. epithelial cell development Source: Ensembl
    5. gene expression Source: Reactome
    6. mitotic cell cycle Source: Reactome
    7. organ morphogenesis Source: Ensembl
    8. positive regulation of transcription from RNA polymerase II promoter Source: Reactome
    9. regulation of cell proliferation Source: Ensembl
    10. regulation of cell size Source: Ensembl
    11. regulation of transcription involved in G1/S transition of mitotic cell cycle Source: Ensembl
    12. transcription, DNA-templated Source: Reactome
    13. transcription initiation from RNA polymerase II promoter Source: Reactome
    14. transforming growth factor beta receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Cell cycle, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_111214. G0 and Early G1.
    REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
    REACT_821. Cyclin D associated events in G1.
    SignaLinkiQ16254.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription factor E2F4
    Short name:
    E2F-4
    Gene namesi
    Name:E2F4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:3118. E2F4.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nucleoplasm Source: Reactome
    3. nucleus Source: HPA
    4. transcription factor complex Source: InterPro

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27576.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 413412Transcription factor E2F4PRO_0000219468Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Post-translational modificationi

    Differentially phosphorylated in vivo.

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ16254.
    PaxDbiQ16254.
    PRIDEiQ16254.

    PTM databases

    PhosphoSiteiQ16254.

    Expressioni

    Tissue specificityi

    Found in all tissue examined including heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.

    Developmental stagei

    Present in the growth-arrested state, its abundance does not change significantly as cells move into and through the cell cycle.

    Gene expression databases

    ArrayExpressiQ16254.
    BgeeiQ16254.
    CleanExiHS_E2F4.
    GenevestigatoriQ16254.

    Organism-specific databases

    HPAiCAB016523.
    HPA054128.

    Interactioni

    Subunit structurei

    Component of the DRTF1/E2F transcription factor complex. Binds cooperatively with TFDP1/Dp-1 to E2F sites. The E2F4/TFDP1 dimer interacts preferentially with pocket protein RBL1, which inhibits the E2F transactivation domain. Lower affinity interaction has been found with retinoblastoma protein RB1. Interacts with TRRAP, which probably mediates its interaction with histone acetyltransferase complexes, leading to transcription activation. Interacts with HCFC1. Component of the DREAM complex (also named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent cells where it represses cell cycle-dependent genes. It dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds to MYBL2. Interacts with PML (isoform PML-1, isoform PML-2, isoform PML-3, isoform PML-4 and isoform PML-5).9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LIN9Q5TKA13EBI-448943,EBI-1389424

    Protein-protein interaction databases

    BioGridi108206. 59 interactions.
    DIPiDIP-24185N.
    IntActiQ16254. 20 interactions.
    MINTiMINT-88123.
    STRINGi9606.ENSP00000368686.

    Structurei

    Secondary structure

    1
    413
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni17 – 204
    Helixi22 – 3514
    Beta strandi40 – 423
    Helixi43 – 497
    Turni50 – 523
    Helixi56 – 6813
    Beta strandi70 – 756
    Beta strandi78 – 814

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CF7X-ray2.60A11-86[»]
    ProteinModelPortaliQ16254.
    SMRiQ16254. Positions 16-82, 96-198.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16254.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni43 – 6523Leucine-zipperAdd
    BLAST
    Regioni86 – 18196DimerizationSequence AnalysisAdd
    BLAST
    Regioni337 – 41377TransactivationSequence AnalysisAdd
    BLAST
    Regioni390 – 40718Interaction with RBL1 and RBL2Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi48 – 8538DEF boxAdd
    BLAST
    Motifi389 – 3924HCFC1-binding-motif (HBM)

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi9 – 124Poly-Pro
    Compositional biasi307 – 32721Poly-SerAdd
    BLAST

    Sequence similaritiesi

    Belongs to the E2F/DP family.Curated

    Phylogenomic databases

    eggNOGiNOG289227.
    HOGENOMiHOG000232045.
    HOVERGENiHBG002227.
    InParanoidiQ16254.
    KOiK04682.
    OMAiPHTLAYV.
    OrthoDBiEOG7WHHB1.
    PhylomeDBiQ16254.
    TreeFamiTF105566.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    InterProiIPR015633. E2F.
    IPR028312. E2F4.
    IPR003316. E2F_TDP.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PANTHERiPTHR12081. PTHR12081. 1 hit.
    PTHR12081:SF42. PTHR12081:SF42. 1 hit.
    PfamiPF02319. E2F_TDP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q16254-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEAGPQAPP PPGTPSRHEK SLGLLTTKFV SLLQEAKDGV LDLKLAADTL    50
    AVRQKRRIYD ITNVLEGIGL IEKKSKNSIQ WKGVGPGCNT REIADKLIEL 100
    KAEIEELQQR EQELDQHKVW VQQSIRNVTE DVQNSCLAYV THEDICRCFA 150
    GDTLLAIRAP SGTSLEVPIP EGLNGQKKYQ IHLKSVSGPI EVLLVNKEAW 200
    SSPPVAVPVP PPEDLLQSPS AVSTPPPLPK PALAQSQEAS RPNSPQLTPT 250
    AVPGSAEVQG MAGPAAEITV SGGPGTDSKD SGELSSLPLG PTTLDTRPLQ 300
    SSALLDSSSS SSSSSSSSSN SNSSSSSGPN PSTSFEPIKA DPTGVLELPK 350
    ELSEIFDPTR ECMSSELLEE LMSSEVFAPL LRLSPPPGDH DYIYNLDESE 400
    GVCDLFDVPV LNL 413
    Length:413
    Mass (Da):43,960
    Last modified:November 1, 1997 - v2
    Checksum:iBAAC95DE1B7E0832
    GO

    Polymorphismi

    The poly-Ser region of E2F4 is polymorphic and the number of Ser varies in the population (from 8 to 17). The variation might be associated with tumorigenesis.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti293 – 2931T → P.
    Corresponds to variant rs1801013 [ dbSNP | Ensembl ].
    VAR_014936
    Natural varianti319 – 3191S → SSSS.
    VAR_014024

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S75174 mRNA. Translation: AAB32597.1.
    X86096 mRNA. Translation: CAA60050.2.
    U15641 mRNA. Translation: AAC50119.1.
    AF250378 Genomic DNA. Translation: AAF65226.1.
    AB451292 mRNA. Translation: BAG70106.1.
    AB451425 mRNA. Translation: BAG70239.1.
    AF527540 Genomic DNA. Translation: AAM77918.1.
    AC040160 Genomic DNA. No translation available.
    CH471092 Genomic DNA. Translation: EAW83094.1.
    BC033180 mRNA. Translation: AAH33180.1.
    CCDSiCCDS32464.1.
    PIRiA55237.
    RefSeqiNP_001941.2. NM_001950.3.
    UniGeneiHs.108371.

    Genome annotation databases

    EnsembliENST00000379378; ENSP00000368686; ENSG00000205250.
    GeneIDi1874.
    KEGGihsa:1874.
    UCSCiuc002erz.3. human.

    Polymorphism databases

    DMDMi2494229.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S75174 mRNA. Translation: AAB32597.1 .
    X86096 mRNA. Translation: CAA60050.2 .
    U15641 mRNA. Translation: AAC50119.1 .
    AF250378 Genomic DNA. Translation: AAF65226.1 .
    AB451292 mRNA. Translation: BAG70106.1 .
    AB451425 mRNA. Translation: BAG70239.1 .
    AF527540 Genomic DNA. Translation: AAM77918.1 .
    AC040160 Genomic DNA. No translation available.
    CH471092 Genomic DNA. Translation: EAW83094.1 .
    BC033180 mRNA. Translation: AAH33180.1 .
    CCDSi CCDS32464.1.
    PIRi A55237.
    RefSeqi NP_001941.2. NM_001950.3.
    UniGenei Hs.108371.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CF7 X-ray 2.60 A 11-86 [» ]
    ProteinModelPortali Q16254.
    SMRi Q16254. Positions 16-82, 96-198.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108206. 59 interactions.
    DIPi DIP-24185N.
    IntActi Q16254. 20 interactions.
    MINTi MINT-88123.
    STRINGi 9606.ENSP00000368686.

    PTM databases

    PhosphoSitei Q16254.

    Polymorphism databases

    DMDMi 2494229.

    Proteomic databases

    MaxQBi Q16254.
    PaxDbi Q16254.
    PRIDEi Q16254.

    Protocols and materials databases

    DNASUi 1874.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000379378 ; ENSP00000368686 ; ENSG00000205250 .
    GeneIDi 1874.
    KEGGi hsa:1874.
    UCSCi uc002erz.3. human.

    Organism-specific databases

    CTDi 1874.
    GeneCardsi GC16P067226.
    HGNCi HGNC:3118. E2F4.
    HPAi CAB016523.
    HPA054128.
    MIMi 600659. gene.
    neXtProti NX_Q16254.
    PharmGKBi PA27576.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG289227.
    HOGENOMi HOG000232045.
    HOVERGENi HBG002227.
    InParanoidi Q16254.
    KOi K04682.
    OMAi PHTLAYV.
    OrthoDBi EOG7WHHB1.
    PhylomeDBi Q16254.
    TreeFami TF105566.

    Enzyme and pathway databases

    Reactomei REACT_111214. G0 and Early G1.
    REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
    REACT_821. Cyclin D associated events in G1.
    SignaLinki Q16254.

    Miscellaneous databases

    EvolutionaryTracei Q16254.
    GeneWikii E2F4.
    GenomeRNAii 1874.
    NextBioi 7659.
    PROi Q16254.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16254.
    Bgeei Q16254.
    CleanExi HS_E2F4.
    Genevestigatori Q16254.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    InterProi IPR015633. E2F.
    IPR028312. E2F4.
    IPR003316. E2F_TDP.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    PANTHERi PTHR12081. PTHR12081. 1 hit.
    PTHR12081:SF42. PTHR12081:SF42. 1 hit.
    Pfami PF02319. E2F_TDP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "E2F-4, a new member of the E2F transcription factor family, interacts with p107."
      Ginsberg D., Vairo G., Chittenden T., Xiao Z.-X., Xu G., Wydner K.L., Decaprio J.A., Lawrence J.B., Livingston D.M.
      Genes Dev. 8:2665-2679(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-319 INS, INTERACTION WITH RBL1.
      Tissue: Cervix carcinoma.
    2. "E2F-4, a new member of the E2F gene family, has oncogenic activity and associates with p107 in vivo."
      Beijersbergen R.L., Kerkhoven R.M., Zhu L., Carlee L., Voorhoeve P.M., Bernards R.
      Genes Dev. 8:2680-2690(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH RBL1.
      Tissue: Colon carcinoma.
    3. "E2F-4 and E2F-5, two members of the E2F family, are expressed in the early phases of the cell cycle."
      Sardet C., Vidal M., Cobrinik D., Geng Y., Onufryk C., Chen A., Weinberg R.A.
      Proc. Natl. Acad. Sci. U.S.A. 92:2403-2407(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Genomic structure and mutation screening of the E2F4 gene in human tumors."
      Schwemmle S., Pfeifer G.P.
      Int. J. Cancer 86:672-677(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
      Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
      , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
      Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. NIEHS SNPs program
      Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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: Kidney.
    10. "The predominant E2F complex in human primary haemopoietic cells and in AML blasts contains E2F-4, DP-1 and p130."
      Williams C.D., Linch D.C., Soerensen T.S., La Thangue N.B., Thomas N.S.B.
      Br. J. Haematol. 96:688-696(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RBL2.
    11. "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.
    12. "HCF-1 functions as a coactivator for the zinc finger protein Krox20."
      Luciano R.L., Wilson A.C.
      J. Biol. Chem. 278:51116-51124(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HCFC1.
    13. "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; RBL1; TFDP1 AND TFDP2.
    14. "LINC, a human complex that is related to pRB-containing complexes in invertebrates regulates the expression of G2/M genes."
      Schmit F., Korenjak M., Mannefeld M., Schmitt K., Franke C., von Eyss B., Gagrica S., Haenel F., Brehm A., Gaubatz S.
      Cell Cycle 6:1903-1913(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE DREAM COMPLEX.
    15. "Evolutionarily conserved multisubunit RBL2/p130 and E2F4 protein complex represses human cell cycle-dependent genes in quiescence."
      Litovchick L., Sadasivam S., Florens L., Zhu X., Swanson S.K., Velmurugan S., Chen R., Washburn M.P., Liu X.S., DeCaprio J.A.
      Mol. Cell 26:539-551(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE DREAM COMPLEX.
    16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    17. "Physical and functional interaction between PML and TBX2 in the establishment of cellular senescence."
      Martin N., Benhamed M., Nacerddine K., Demarque M.D., van Lohuizen M., Dejean A., Bischof O.
      EMBO J. 31:95-109(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PML.
    18. "Structural basis of DNA recognition by the heterodimeric cell cycle transcription factor E2F-DP."
      Zheng N., Fraenkel E., Pabo C.O., Pavletich N.P.
      Genes Dev. 13:666-674(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 11-86.
    19. "Various AGC repeat numbers in the coding region of the human transcription factor gene E2F-4."
      Zhong X., Hemmi H., Koike J., Tsujita K., Shimatake H.
      Hum. Mutat. 15:296-297(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: POLYMORPHISM.

    Entry informationi

    Entry nameiE2F4_HUMAN
    AccessioniPrimary (citable) accession number: Q16254
    Secondary accession number(s): A6NGR8
    , B5BU56, Q12991, Q15328
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 149 of the entry and version 2 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 16
      Human chromosome 16: 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