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Transcription factor E2F4 (E2F-4)

 E2F4_HUMAN              Reviewed;         413 AA.
Q16254; A6NGR8; B5BU56; Q12991; Q15328;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
22-NOV-2017, entry version 184.
RecName: Full=Transcription factor E2F4;
Short=E2F-4;
Name=E2F4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-319 INS, INTERACTION WITH
RBL1, AND FUNCTION.
TISSUE=Cervix carcinoma;
PubMed=7958924; DOI=10.1101/gad.8.22.2665;
Ginsberg D., Vairo G., Chittenden T., Xiao Z.-X., Xu G., Wydner K.L.,
Decaprio J.A., Lawrence J.B., Livingston D.M.;
"E2F-4, a new member of the E2F transcription factor family, interacts
with p107.";
Genes Dev. 8:2665-2679(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH RBL1, AND FUNCTION.
TISSUE=Colon carcinoma;
PubMed=7958925; DOI=10.1101/gad.8.22.2680;
Beijersbergen R.L., Kerkhoven R.M., Zhu L., Carlee L., Voorhoeve P.M.,
Bernards R.;
"E2F-4, a new member of the E2F gene family, has oncogenic activity
and associates with p107 in vivo.";
Genes Dev. 8:2680-2690(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7892279; DOI=10.1073/pnas.92.6.2403;
Sardet C., Vidal M., Cobrinik D., Geng Y., Onufryk C., Chen A.,
Weinberg R.A.;
"E2F-4 and E2F-5, two members of the E2F family, are expressed in the
early phases of the cell cycle.";
Proc. Natl. Acad. Sci. U.S.A. 92:2403-2407(1995).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10797289;
DOI=10.1002/(SICI)1097-0215(20000601)86:5<672::AID-IJC11>3.0.CO;2-X;
Schwemmle S., Pfeifer G.P.;
"Genomic structure and mutation screening of the E2F4 gene in human
tumors.";
Int. J. Cancer 86:672-677(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=19054851; DOI=10.1038/nmeth.1273;
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.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
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.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
INTERACTION WITH RBL2.
PubMed=9074408; DOI=10.1046/j.1365-2141.1997.d01-2086.x;
Williams C.D., Linch D.C., Soerensen T.S., La Thangue N.B.,
Thomas N.S.B.;
"The predominant E2F complex in human primary haemopoietic cells and
in AML blasts contains E2F-4, DP-1 and p130.";
Br. J. Haematol. 96:688-696(1997).
[11]
INTERACTION WITH TRRAP.
PubMed=11418595; DOI=10.1074/jbc.M102067200;
Lang S.E., McMahon S.B., Cole M.D., Hearing P.;
"E2F transcriptional activation requires TRRAP and GCN5 cofactors.";
J. Biol. Chem. 276:32627-32634(2001).
[12]
INTERACTION WITH HCFC1.
PubMed=14532282; DOI=10.1074/jbc.M303470200;
Luciano R.L., Wilson A.C.;
"HCF-1 functions as a coactivator for the zinc finger protein
Krox20.";
J. Biol. Chem. 278:51116-51124(2003).
[13]
INTERACTION WITH CEBPA.
PubMed=15107404; DOI=10.1101/gad.1183304;
Wang G.L., Iakova P., Wilde M., Awad S., Timchenko N.A.;
"Liver tumors escape negative control of proliferation via PI3K/Akt-
mediated block of C/EBP alpha growth inhibitory activity.";
Genes Dev. 18:912-925(2004).
[14]
INTERACTION WITH WITH RB1; RBL1; TFDP1 AND TFDP2.
PubMed=16360038; DOI=10.1016/j.cell.2005.09.044;
Rubin S.M., Gall A.-L., Zheng N., Pavletich N.P.;
"Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism
for phosphorylation-induced E2F release.";
Cell 123:1093-1106(2005).
[15]
IDENTIFICATION IN THE DREAM COMPLEX.
PubMed=17671431; DOI=10.4161/cc.6.15.4512;
Schmit F., Korenjak M., Mannefeld M., Schmitt K., Franke C.,
von Eyss B., Gagrica S., Haenel F., Brehm A., Gaubatz S.;
"LINC, a human complex that is related to pRB-containing complexes in
invertebrates regulates the expression of G2/M genes.";
Cell Cycle 6:1903-1913(2007).
[16]
IDENTIFICATION IN THE DREAM COMPLEX.
PubMed=17531812; DOI=10.1016/j.molcel.2007.04.015;
Litovchick L., Sadasivam S., Florens L., Zhu X., Swanson S.K.,
Velmurugan S., Chen R., Washburn M.P., Liu X.S., DeCaprio J.A.;
"Evolutionarily conserved multisubunit RBL2/p130 and E2F4 protein
complex represses human cell cycle-dependent genes in quiescence.";
Mol. Cell 26:539-551(2007).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[18]
INTERACTION WITH PML.
PubMed=22002537; DOI=10.1038/emboj.2011.370;
Martin N., Benhamed M., Nacerddine K., Demarque M.D., van Lohuizen M.,
Dejean A., Bischof O.;
"Physical and functional interaction between PML and TBX2 in the
establishment of cellular senescence.";
EMBO J. 31:95-109(2012).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 11-86.
PubMed=10090723; DOI=10.1101/gad.13.6.666;
Zheng N., Fraenkel E., Pabo C.O., Pavletich N.P.;
"Structural basis of DNA recognition by the heterodimeric cell cycle
transcription factor E2F-DP.";
Genes Dev. 13:666-674(1999).
[22]
POLYMORPHISM.
PubMed=10679953;
DOI=10.1002/(SICI)1098-1004(200003)15:3<296::AID-HUMU18>3.3.CO;2-O;
Zhong X., Hemmi H., Koike J., Tsujita K., Shimatake H.;
"Various AGC repeat numbers in the coding region of the human
transcription factor gene E2F-4.";
Hum. Mutat. 15:296-297(2000).
-!- FUNCTION: Transcription activator that binds DNA cooperatively
with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-
3' found in the promoter region of a number of genes whose
products are involved in cell cycle regulation or in DNA
replication. The DRTF1/E2F complex functions in the control of
cell-cycle progression from G1 to S phase. E2F4 binds with high
affinity to RBL1 and RBL2. In some instances can also bind RB1.
Specifically required for multiciliate cell differentiation:
together with MCIDAS and E2F5, binds and activate genes required
for centriole biogenesis. {ECO:0000250|UniProtKB:Q6DE14,
ECO:0000269|PubMed:7958924, ECO:0000269|PubMed:7958925}.
-!- SUBUNIT: 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). Interacts with CEBPA (when
phosphorylated) (PubMed:15107404). {ECO:0000269|PubMed:11418595,
ECO:0000269|PubMed:14532282, ECO:0000269|PubMed:15107404,
ECO:0000269|PubMed:16360038, ECO:0000269|PubMed:17531812,
ECO:0000269|PubMed:17671431, ECO:0000269|PubMed:22002537,
ECO:0000269|PubMed:7958924, ECO:0000269|PubMed:7958925,
ECO:0000269|PubMed:9074408}.
-!- INTERACTION:
P03129:E7 (xeno); NbExp=2; IntAct=EBI-448943, EBI-866453;
Q5TKA1:LIN9; NbExp=3; IntAct=EBI-448943, EBI-1389424;
Q08999:RBL2; NbExp=7; IntAct=EBI-448943, EBI-971439;
Q14186:TFDP1; NbExp=5; IntAct=EBI-448943, EBI-749713;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- TISSUE SPECIFICITY: Found in all tissue examined including heart,
brain, placenta, lung, liver, skeletal muscle, kidney and
pancreas.
-!- DEVELOPMENTAL STAGE: Present in the growth-arrested state, its
abundance does not change significantly as cells move into and
through the cell cycle.
-!- PTM: Differentially phosphorylated in vivo.
-!- POLYMORPHISM: 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.
-!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/e2f4/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/E2F4ID40385ch16q22.html";
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EMBL; S75174; AAB32597.1; -; mRNA.
EMBL; X86096; CAA60050.2; -; mRNA.
EMBL; U15641; AAC50119.1; -; mRNA.
EMBL; AF250378; AAF65226.1; -; Genomic_DNA.
EMBL; AB451292; BAG70106.1; -; mRNA.
EMBL; AB451425; BAG70239.1; -; mRNA.
EMBL; AF527540; AAM77918.1; -; Genomic_DNA.
EMBL; AC040160; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471092; EAW83094.1; -; Genomic_DNA.
EMBL; BC033180; AAH33180.1; -; mRNA.
CCDS; CCDS32464.1; -.
PIR; A55237; A55237.
RefSeq; NP_001941.2; NM_001950.3.
UniGene; Hs.108371; -.
PDB; 1CF7; X-ray; 2.60 A; A=11-86.
PDB; 5TUU; X-ray; 2.25 A; B=91-198.
PDBsum; 1CF7; -.
PDBsum; 5TUU; -.
ProteinModelPortal; Q16254; -.
SMR; Q16254; -.
BioGrid; 108206; 50.
CORUM; Q16254; -.
DIP; DIP-24185N; -.
ELM; Q16254; -.
IntAct; Q16254; 28.
MINT; MINT-88123; -.
STRING; 9606.ENSP00000368686; -.
iPTMnet; Q16254; -.
PhosphoSitePlus; Q16254; -.
BioMuta; E2F4; -.
DMDM; 2494229; -.
EPD; Q16254; -.
MaxQB; Q16254; -.
PaxDb; Q16254; -.
PeptideAtlas; Q16254; -.
PRIDE; Q16254; -.
DNASU; 1874; -.
Ensembl; ENST00000379378; ENSP00000368686; ENSG00000205250.
GeneID; 1874; -.
KEGG; hsa:1874; -.
UCSC; uc002erz.4; human.
CTD; 1874; -.
DisGeNET; 1874; -.
EuPathDB; HostDB:ENSG00000205250.8; -.
GeneCards; E2F4; -.
HGNC; HGNC:3118; E2F4.
HPA; HPA054128; -.
MIM; 600659; gene.
neXtProt; NX_Q16254; -.
OpenTargets; ENSG00000205250; -.
PharmGKB; PA27576; -.
eggNOG; KOG2577; Eukaryota.
eggNOG; ENOG410XNYI; LUCA.
GeneTree; ENSGT00550000074403; -.
HOGENOM; HOG000232045; -.
HOVERGEN; HBG002227; -.
InParanoid; Q16254; -.
KO; K04682; -.
OMA; PHTLAYV; -.
OrthoDB; EOG091G0CJQ; -.
PhylomeDB; Q16254; -.
TreeFam; TF105566; -.
Reactome; R-HSA-1362277; Transcription of E2F targets under negative control by DREAM complex.
Reactome; R-HSA-1362300; Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1.
Reactome; R-HSA-1538133; G0 and Early G1.
Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
Reactome; R-HSA-539107; Activation of E2F1 target genes at G1/S.
Reactome; R-HSA-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
Reactome; R-HSA-69202; Cyclin E associated events during G1/S transition.
Reactome; R-HSA-69231; Cyclin D associated events in G1.
Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry.
SignaLink; Q16254; -.
SIGNOR; Q16254; -.
ChiTaRS; E2F4; human.
EvolutionaryTrace; Q16254; -.
GeneWiki; E2F4; -.
GenomeRNAi; 1874; -.
PRO; PR:Q16254; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000205250; -.
CleanEx; HS_E2F4; -.
ExpressionAtlas; Q16254; baseline and differential.
Genevisible; Q16254; HS.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005667; C:transcription factor complex; IEA:InterPro.
GO; GO:0003677; F:DNA binding; IMP:UniProtKB.
GO; GO:1990841; F:promoter-specific chromatin binding; IDA:MGI.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IC:NTNU_SB.
GO; GO:0009887; P:animal organ morphogenesis; IEA:Ensembl.
GO; GO:0008015; P:blood circulation; IEA:Ensembl.
GO; GO:0006884; P:cell volume homeostasis; IEA:Ensembl.
GO; GO:0098534; P:centriole assembly; ISS:UniProtKB.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
GO; GO:0002064; P:epithelial cell development; IEA:Ensembl.
GO; GO:0044458; P:motile cilium assembly; ISS:UniProtKB.
GO; GO:1903251; P:multi-ciliated epithelial cell differentiation; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl.
GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IEA:Ensembl.
CDD; cd14660; E2F_DD; 1.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR015633; E2F.
InterPro; IPR037241; E2F-DP_heterodim.
InterPro; IPR028312; E2F4.
InterPro; IPR032198; E2F_CC-MB.
InterPro; IPR003316; E2F_WHTH_DNA-bd_dom.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
PANTHER; PTHR12081; PTHR12081; 1.
PANTHER; PTHR12081:SF42; PTHR12081:SF42; 1.
Pfam; PF16421; E2F_CC-MB; 1.
Pfam; PF02319; E2F_TDP; 1.
SMART; SM01372; E2F_TDP; 1.
SUPFAM; SSF144074; SSF144074; 1.
SUPFAM; SSF46785; SSF46785; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Cell cycle;
Cilium biogenesis/degradation; Complete proteome; DNA-binding;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Transcription; Transcription regulation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 413 Transcription factor E2F4.
/FTId=PRO_0000219468.
DNA_BIND 16 85 {ECO:0000255}.
REGION 43 65 Leucine-zipper.
REGION 86 181 Dimerization. {ECO:0000255}.
REGION 337 413 Transactivation. {ECO:0000255}.
REGION 390 407 Interaction with RBL1 and RBL2.
{ECO:0000255}.
MOTIF 48 85 DEF box.
MOTIF 389 392 HCFC1-binding-motif (HBM).
COMPBIAS 9 12 Poly-Pro.
COMPBIAS 307 327 Poly-Ser.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 384 384 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VARIANT 293 293 T -> P (in dbSNP:rs1801013).
/FTId=VAR_014936.
VARIANT 319 319 S -> SSSS.
/FTId=VAR_014024.
TURN 17 20 {ECO:0000244|PDB:1CF7}.
HELIX 22 35 {ECO:0000244|PDB:1CF7}.
STRAND 40 42 {ECO:0000244|PDB:1CF7}.
HELIX 43 49 {ECO:0000244|PDB:1CF7}.
TURN 50 52 {ECO:0000244|PDB:1CF7}.
HELIX 56 68 {ECO:0000244|PDB:1CF7}.
STRAND 70 75 {ECO:0000244|PDB:1CF7}.
STRAND 78 81 {ECO:0000244|PDB:1CF7}.
HELIX 96 129 {ECO:0000244|PDB:5TUU}.
HELIX 132 134 {ECO:0000244|PDB:5TUU}.
STRAND 139 141 {ECO:0000244|PDB:5TUU}.
HELIX 142 148 {ECO:0000244|PDB:5TUU}.
TURN 149 151 {ECO:0000244|PDB:5TUU}.
STRAND 152 158 {ECO:0000244|PDB:5TUU}.
STRAND 164 166 {ECO:0000244|PDB:5TUU}.
STRAND 179 184 {ECO:0000244|PDB:5TUU}.
STRAND 186 188 {ECO:0000244|PDB:5TUU}.
STRAND 191 194 {ECO:0000244|PDB:5TUU}.
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


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