E2F4_HUMAN
ID E2F4_HUMAN Reviewed; 413 AA.
AC Q16254; A6NGR8; B5BU56; Q12991; Q15328;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Transcription factor E2F4;
DE Short=E2F-4;
GN Name=E2F4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-319 INS, INTERACTION WITH RBL1, AND
RP FUNCTION.
RC TISSUE=Cervix carcinoma;
RX PubMed=7958924; DOI=10.1101/gad.8.22.2665;
RA Ginsberg D., Vairo G., Chittenden T., Xiao Z.-X., Xu G., Wydner K.L.,
RA Decaprio J.A., Lawrence J.B., Livingston D.M.;
RT "E2F-4, a new member of the E2F transcription factor family, interacts with
RT p107.";
RL Genes Dev. 8:2665-2679(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH RBL1, AND FUNCTION.
RC TISSUE=Colon carcinoma;
RX PubMed=7958925; DOI=10.1101/gad.8.22.2680;
RA Beijersbergen R.L., Kerkhoven R.M., Zhu L., Carlee L., Voorhoeve P.M.,
RA Bernards R.;
RT "E2F-4, a new member of the E2F gene family, has oncogenic activity and
RT associates with p107 in vivo.";
RL Genes Dev. 8:2680-2690(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7892279; DOI=10.1073/pnas.92.6.2403;
RA Sardet C., Vidal M., Cobrinik D., Geng Y., Onufryk C., Chen A.,
RA Weinberg R.A.;
RT "E2F-4 and E2F-5, two members of the E2F family, are expressed in the early
RT phases of the cell cycle.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:2403-2407(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10797289;
RX DOI=10.1002/(sici)1097-0215(20000601)86:5<672::aid-ijc11>3.0.co;2-x;
RA Schwemmle S., Pfeifer G.P.;
RT "Genomic structure and mutation screening of the E2F4 gene in human
RT tumors.";
RL Int. J. Cancer 86:672-677(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human protein factory for converting the transcriptome into an in vitro-
RT expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP INTERACTION WITH RBL2.
RX PubMed=9074408; DOI=10.1046/j.1365-2141.1997.d01-2086.x;
RA Williams C.D., Linch D.C., Soerensen T.S., La Thangue N.B., Thomas N.S.B.;
RT "The predominant E2F complex in human primary haemopoietic cells and in AML
RT blasts contains E2F-4, DP-1 and p130.";
RL Br. J. Haematol. 96:688-696(1997).
RN [11]
RP INTERACTION WITH TRRAP.
RX PubMed=11418595; DOI=10.1074/jbc.m102067200;
RA Lang S.E., McMahon S.B., Cole M.D., Hearing P.;
RT "E2F transcriptional activation requires TRRAP and GCN5 cofactors.";
RL J. Biol. Chem. 276:32627-32634(2001).
RN [12]
RP INTERACTION WITH HCFC1.
RX PubMed=14532282; DOI=10.1074/jbc.m303470200;
RA Luciano R.L., Wilson A.C.;
RT "HCF-1 functions as a coactivator for the zinc finger protein Krox20.";
RL J. Biol. Chem. 278:51116-51124(2003).
RN [13]
RP INTERACTION WITH CEBPA.
RX PubMed=15107404; DOI=10.1101/gad.1183304;
RA Wang G.L., Iakova P., Wilde M., Awad S., Timchenko N.A.;
RT "Liver tumors escape negative control of proliferation via PI3K/Akt-
RT mediated block of C/EBP alpha growth inhibitory activity.";
RL Genes Dev. 18:912-925(2004).
RN [14]
RP INTERACTION WITH RB1; RBL1; TFDP1 AND TFDP2.
RX PubMed=16360038; DOI=10.1016/j.cell.2005.09.044;
RA Rubin S.M., Gall A.-L., Zheng N., Pavletich N.P.;
RT "Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism for
RT phosphorylation-induced E2F release.";
RL Cell 123:1093-1106(2005).
RN [15]
RP IDENTIFICATION IN THE DREAM COMPLEX.
RX PubMed=17671431; DOI=10.4161/cc.6.15.4512;
RA Schmit F., Korenjak M., Mannefeld M., Schmitt K., Franke C., von Eyss B.,
RA Gagrica S., Haenel F., Brehm A., Gaubatz S.;
RT "LINC, a human complex that is related to pRB-containing complexes in
RT invertebrates regulates the expression of G2/M genes.";
RL Cell Cycle 6:1903-1913(2007).
RN [16]
RP IDENTIFICATION IN THE DREAM COMPLEX.
RX PubMed=17531812; DOI=10.1016/j.molcel.2007.04.015;
RA Litovchick L., Sadasivam S., Florens L., Zhu X., Swanson S.K.,
RA Velmurugan S., Chen R., Washburn M.P., Liu X.S., DeCaprio J.A.;
RT "Evolutionarily conserved multisubunit RBL2/p130 and E2F4 protein complex
RT represses human cell cycle-dependent genes in quiescence.";
RL Mol. Cell 26:539-551(2007).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [18]
RP INTERACTION WITH PML.
RX PubMed=22002537; DOI=10.1038/emboj.2011.370;
RA Martin N., Benhamed M., Nacerddine K., Demarque M.D., van Lohuizen M.,
RA Dejean A., Bischof O.;
RT "Physical and functional interaction between PML and TBX2 in the
RT establishment of cellular senescence.";
RL EMBO J. 31:95-109(2012).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 11-86.
RX PubMed=10090723; DOI=10.1101/gad.13.6.666;
RA Zheng N., Fraenkel E., Pabo C.O., Pavletich N.P.;
RT "Structural basis of DNA recognition by the heterodimeric cell cycle
RT transcription factor E2F-DP.";
RL Genes Dev. 13:666-674(1999).
RN [22]
RP POLYMORPHISM.
RX PubMed=10679953;
RX DOI=10.1002/(sici)1098-1004(200003)15:3<296::aid-humu18>3.0.co;2-x;
RA Zhong X., Hemmi H., Koike J., Tsujita K., Shimatake H.;
RT "Various AGC repeat numbers in the coding region of the human transcription
RT factor gene E2F-4.";
RL Hum. Mutat. 15:296-297(2000).
CC -!- FUNCTION: Transcription activator that binds DNA cooperatively with DP
CC proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in
CC the promoter region of a number of genes whose products are involved in
CC cell cycle regulation or in DNA replication. The DRTF1/E2F complex
CC functions in the control of cell-cycle progression from G1 to S phase.
CC E2F4 binds with high affinity to RBL1 and RBL2. In some instances can
CC also bind RB1. Specifically required for multiciliate cell
CC differentiation: together with MCIDAS and E2F5, binds and activate
CC genes required for centriole biogenesis. {ECO:0000250|UniProtKB:Q6DE14,
CC ECO:0000269|PubMed:7958924, ECO:0000269|PubMed:7958925}.
CC -!- SUBUNIT: Component of the DRTF1/E2F transcription factor complex. Binds
CC cooperatively with TFDP1/Dp-1 to E2F sites. The E2F4/TFDP1 dimer
CC interacts preferentially with pocket protein RBL1, which inhibits the
CC E2F transactivation domain. Lower affinity interaction has been found
CC with retinoblastoma protein RB1. Interacts with TRRAP, which probably
CC mediates its interaction with histone acetyltransferase complexes,
CC leading to transcription activation. Interacts with HCFC1. Component of
CC the DREAM complex (also named LINC complex) at least composed of E2F4,
CC E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1
CC and TFDP2. The complex exists in quiescent cells where it represses
CC cell cycle-dependent genes. It dissociates in S phase when LIN9, LIN37,
CC LIN52 and LIN54 form a subcomplex that binds to MYBL2. Interacts with
CC PML (isoform PML-1, isoform PML-2, isoform PML-3, isoform PML-4 and
CC isoform PML-5). Interacts with CEBPA (when phosphorylated)
CC (PubMed:15107404). {ECO:0000269|PubMed:11418595,
CC ECO:0000269|PubMed:14532282, ECO:0000269|PubMed:15107404,
CC ECO:0000269|PubMed:16360038, ECO:0000269|PubMed:17531812,
CC ECO:0000269|PubMed:17671431, ECO:0000269|PubMed:22002537,
CC ECO:0000269|PubMed:7958924, ECO:0000269|PubMed:7958925,
CC ECO:0000269|PubMed:9074408}.
CC -!- INTERACTION:
CC Q16254; Q92993: KAT5; NbExp=3; IntAct=EBI-448943, EBI-399080;
CC Q16254; Q5TKA1: LIN9; NbExp=3; IntAct=EBI-448943, EBI-1389424;
CC Q16254; Q13526: PIN1; NbExp=3; IntAct=EBI-448943, EBI-714158;
CC Q16254; Q08999: RBL2; NbExp=7; IntAct=EBI-448943, EBI-971439;
CC Q16254; Q14186: TFDP1; NbExp=7; IntAct=EBI-448943, EBI-749713;
CC Q16254; Q14188-5: TFDP2; NbExp=3; IntAct=EBI-448943, EBI-12181237;
CC Q16254; P03129: E7; Xeno; NbExp=2; IntAct=EBI-448943, EBI-866453;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Found in all tissue examined including heart,
CC brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.
CC -!- DEVELOPMENTAL STAGE: Present in the growth-arrested state, its
CC abundance does not change significantly as cells move into and through
CC the cell cycle.
CC -!- PTM: Differentially phosphorylated in vivo.
CC -!- POLYMORPHISM: The poly-Ser region of E2F4 is polymorphic and the number
CC of Ser varies in the population (from 8 to 17). The variation might be
CC associated with tumorigenesis.
CC -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/e2f4/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/E2F4ID40385ch16q22.html";
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DR EMBL; S75174; AAB32597.1; -; mRNA.
DR EMBL; X86096; CAA60050.2; -; mRNA.
DR EMBL; U15641; AAC50119.1; -; mRNA.
DR EMBL; AF250378; AAF65226.1; -; Genomic_DNA.
DR EMBL; AB451292; BAG70106.1; -; mRNA.
DR EMBL; AB451425; BAG70239.1; -; mRNA.
DR EMBL; AF527540; AAM77918.1; -; Genomic_DNA.
DR EMBL; AC040160; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471092; EAW83094.1; -; Genomic_DNA.
DR EMBL; BC033180; AAH33180.1; -; mRNA.
DR CCDS; CCDS32464.1; -.
DR PIR; A55237; A55237.
DR RefSeq; NP_001941.2; NM_001950.3.
DR PDB; 1CF7; X-ray; 2.60 A; A=11-86.
DR PDB; 5TUU; X-ray; 2.25 A; B=91-198.
DR PDBsum; 1CF7; -.
DR PDBsum; 5TUU; -.
DR AlphaFoldDB; Q16254; -.
DR SMR; Q16254; -.
DR BioGRID; 108206; 95.
DR CORUM; Q16254; -.
DR DIP; DIP-24185N; -.
DR ELM; Q16254; -.
DR IntAct; Q16254; 33.
DR MINT; Q16254; -.
DR STRING; 9606.ENSP00000368686; -.
DR ChEMBL; CHEMBL4630726; -.
DR GlyGen; Q16254; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q16254; -.
DR PhosphoSitePlus; Q16254; -.
DR BioMuta; E2F4; -.
DR DMDM; 2494229; -.
DR EPD; Q16254; -.
DR jPOST; Q16254; -.
DR MassIVE; Q16254; -.
DR MaxQB; Q16254; -.
DR PaxDb; Q16254; -.
DR PeptideAtlas; Q16254; -.
DR PRIDE; Q16254; -.
DR ProteomicsDB; 60845; -.
DR Antibodypedia; 4294; 464 antibodies from 41 providers.
DR DNASU; 1874; -.
DR Ensembl; ENST00000379378.8; ENSP00000368686.3; ENSG00000205250.9.
DR GeneID; 1874; -.
DR KEGG; hsa:1874; -.
DR MANE-Select; ENST00000379378.8; ENSP00000368686.3; NM_001950.4; NP_001941.2.
DR UCSC; uc002erz.4; human.
DR CTD; 1874; -.
DR DisGeNET; 1874; -.
DR GeneCards; E2F4; -.
DR HGNC; HGNC:3118; E2F4.
DR HPA; ENSG00000205250; Low tissue specificity.
DR MIM; 600659; gene.
DR neXtProt; NX_Q16254; -.
DR OpenTargets; ENSG00000205250; -.
DR PharmGKB; PA27576; -.
DR VEuPathDB; HostDB:ENSG00000205250; -.
DR eggNOG; KOG2577; Eukaryota.
DR GeneTree; ENSGT00940000156252; -.
DR HOGENOM; CLU_032091_2_2_1; -.
DR InParanoid; Q16254; -.
DR OMA; VQNSPHT; -.
DR OrthoDB; 1087250at2759; -.
DR PhylomeDB; Q16254; -.
DR TreeFam; TF105566; -.
DR PathwayCommons; Q16254; -.
DR Reactome; R-HSA-1362277; Transcription of E2F targets under negative control by DREAM complex.
DR Reactome; R-HSA-1362300; Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1.
DR Reactome; R-HSA-1538133; G0 and Early G1.
DR Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-HSA-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
DR Reactome; R-HSA-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-HSA-69205; G1/S-Specific Transcription.
DR Reactome; R-HSA-69231; Cyclin D associated events in G1.
DR Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR SignaLink; Q16254; -.
DR SIGNOR; Q16254; -.
DR BioGRID-ORCS; 1874; 27 hits in 1107 CRISPR screens.
DR ChiTaRS; E2F4; human.
DR EvolutionaryTrace; Q16254; -.
DR GeneWiki; E2F4; -.
DR GenomeRNAi; 1874; -.
DR Pharos; Q16254; Tbio.
DR PRO; PR:Q16254; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q16254; protein.
DR Bgee; ENSG00000205250; Expressed in pancreatic ductal cell and 106 other tissues.
DR ExpressionAtlas; Q16254; baseline and differential.
DR Genevisible; Q16254; HS.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IMP:UniProtKB.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:MGI.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:Ensembl.
DR GO; GO:0008015; P:blood circulation; IEA:Ensembl.
DR GO; GO:0006884; P:cell volume homeostasis; IEA:Ensembl.
DR GO; GO:0098534; P:centriole assembly; ISS:UniProtKB.
DR GO; GO:0002064; P:epithelial cell development; IEA:Ensembl.
DR GO; GO:0044458; P:motile cilium assembly; ISS:UniProtKB.
DR GO; GO:1903251; P:multi-ciliated epithelial cell differentiation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR CDD; cd14660; E2F_DD; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR015633; E2F.
DR InterPro; IPR037241; E2F-DP_heterodim.
DR InterPro; IPR028312; E2F4.
DR InterPro; IPR032198; E2F_CC-MB.
DR InterPro; IPR003316; E2F_WHTH_DNA-bd_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12081; PTHR12081; 1.
DR PANTHER; PTHR12081:SF42; PTHR12081:SF42; 1.
DR Pfam; PF16421; E2F_CC-MB; 1.
DR Pfam; PF02319; E2F_TDP; 1.
DR SMART; SM01372; E2F_TDP; 1.
DR SUPFAM; SSF144074; SSF144074; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Cell cycle;
KW Cilium biogenesis/degradation; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..413
FT /note="Transcription factor E2F4"
FT /id="PRO_0000219468"
FT DNA_BIND 16..85
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..65
FT /note="Leucine-zipper"
FT REGION 86..181
FT /note="Dimerization"
FT /evidence="ECO:0000255"
FT REGION 211..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..413
FT /note="Transactivation"
FT /evidence="ECO:0000255"
FT REGION 390..407
FT /note="Interaction with RBL1 and RBL2"
FT /evidence="ECO:0000255"
FT MOTIF 48..85
FT /note="DEF box"
FT MOTIF 389..392
FT /note="HCFC1-binding-motif (HBM)"
FT COMPBIAS 1..16
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VARIANT 293
FT /note="T -> P (in dbSNP:rs1801013)"
FT /id="VAR_014936"
FT VARIANT 319
FT /note="S -> SSSS"
FT /id="VAR_014024"
FT TURN 17..20
FT /evidence="ECO:0007829|PDB:1CF7"
FT HELIX 22..35
FT /evidence="ECO:0007829|PDB:1CF7"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:1CF7"
FT HELIX 43..49
FT /evidence="ECO:0007829|PDB:1CF7"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:1CF7"
FT HELIX 56..68
FT /evidence="ECO:0007829|PDB:1CF7"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:1CF7"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:1CF7"
FT HELIX 96..129
FT /evidence="ECO:0007829|PDB:5TUU"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:5TUU"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:5TUU"
FT HELIX 142..148
FT /evidence="ECO:0007829|PDB:5TUU"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:5TUU"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:5TUU"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:5TUU"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:5TUU"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:5TUU"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:5TUU"
SQ SEQUENCE 413 AA; 43960 MW; BAAC95DE1B7E0832 CRC64;
MAEAGPQAPP PPGTPSRHEK SLGLLTTKFV SLLQEAKDGV LDLKLAADTL AVRQKRRIYD
ITNVLEGIGL IEKKSKNSIQ WKGVGPGCNT REIADKLIEL KAEIEELQQR EQELDQHKVW
VQQSIRNVTE DVQNSCLAYV THEDICRCFA GDTLLAIRAP SGTSLEVPIP EGLNGQKKYQ
IHLKSVSGPI EVLLVNKEAW SSPPVAVPVP PPEDLLQSPS AVSTPPPLPK PALAQSQEAS
RPNSPQLTPT AVPGSAEVQG MAGPAAEITV SGGPGTDSKD SGELSSLPLG PTTLDTRPLQ
SSALLDSSSS SSSSSSSSSN SNSSSSSGPN PSTSFEPIKA DPTGVLELPK ELSEIFDPTR
ECMSSELLEE LMSSEVFAPL LRLSPPPGDH DYIYNLDESE GVCDLFDVPV LNL
