Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Transcription factor E4F1 (EC 2.3.2.27) (E4F transcription factor 1) (Putative E3 ubiquitin-protein ligase E4F1) (RING-type E3 ubiquitin transferase E4F1) (Transcription factor E4F) (p120E4F) (p50E4F)

 E4F1_HUMAN              Reviewed;         784 AA.
Q66K89; A8K2R4; O00146;
18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 2.
30-AUG-2017, entry version 139.
RecName: Full=Transcription factor E4F1;
EC=2.3.2.27 {ECO:0000269|PubMed:17110336};
AltName: Full=E4F transcription factor 1;
AltName: Full=Putative E3 ubiquitin-protein ligase E4F1;
AltName: Full=RING-type E3 ubiquitin transferase E4F1 {ECO:0000305};
AltName: Full=Transcription factor E4F;
AltName: Full=p120E4F;
AltName: Full=p50E4F;
Name=E4F1; Synonyms=E4F;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PROTEOLYTIC PROCESSING,
PHOSPHORYLATION, DNA-BINDING, AND VARIANT HIS-167.
TISSUE=Cervix carcinoma;
PubMed=9121437; DOI=10.1128/MCB.17.4.1890;
Fernandes E.R., Rooney R.J.;
"The adenovirus E1A-regulated transcription factor E4F is generated
from the human homolog of nuclear factor phiAP3.";
Mol. Cell. Biol. 17:1890-1903(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-167.
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT HIS-167.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-167.
TISSUE=Uterus;
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).
[6]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=9530632; DOI=10.1007/s003359900758;
Rooney R.J., Daniels R.R., Jenkins N.A., Gilbert D.J., Rothammer K.,
Morris S.W., Higgs D.R., Copeland N.G.;
"Chromosomal location and tissue expression of the gene encoding the
adenovirus E1A-regulated transcription factor E4F in humans and
mice.";
Mamm. Genome 9:320-323(1998).
[7]
FUNCTION.
PubMed=9418893; DOI=10.1128/MCB.18.1.459;
Fernandes E.R., Zhang J.Y., Rooney R.J.;
"Adenovirus E1A-regulated transcription factor p120E4F inhibits cell
growth and induces the stabilization of the cdk inhibitor p21WAF1.";
Mol. Cell. Biol. 18:459-467(1998).
[8]
OLIGOMERIZATION, PHOSPHORYLATION, DNA-BINDING, AND MUTAGENESIS OF
CYS-194; CYS-197; HIS-210; ARG-237; HIS-238; LYS-249 AND CYS-250.
PubMed=9512539; DOI=10.1093/nar/26.7.1681;
Rooney R.J., Rothammer K., Fernandes E.R.;
"Mutational analysis of p50E4F suggests that DNA binding activity is
mediated through an alternative structure in a zinc finger domain that
is regulated by phosphorylation.";
Nucleic Acids Res. 26:1681-1688(1998).
[9]
FUNCTION.
PubMed=10373523; DOI=10.1128/MCB.19.7.4739;
Fernandes E.R., Rooney R.J.;
"Suppression of E1A-mediated transformation by the p50E4F
transcription factor.";
Mol. Cell. Biol. 19:4739-4749(1999).
[10]
FUNCTION, AND INTERACTION WITH TP53.
PubMed=10644996; DOI=10.1038/sj.onc.1203250;
Sandy P., Gostissa M., Fogal V., Cecco L.D., Szalay K., Rooney R.J.,
Schneider C., Del Sal G.;
"p53 is involved in the p120E4F-mediated growth arrest.";
Oncogene 19:188-199(2000).
[11]
FUNCTION, REGULATION BY RB1, AND INTERACTION WITH RB1.
PubMed=10869426; DOI=10.1073/pnas.130198397;
Fajas L., Paul C., Zugasti O., Le Cam L., Polanowska J., Fabbrizio E.,
Medema R., Vignais M.-L., Sardet C.;
"pRB binds to and modulates the transrepressing activity of the E1A-
regulated transcription factor p120E4F.";
Proc. Natl. Acad. Sci. U.S.A. 97:7738-7743(2000).
[12]
FUNCTION.
PubMed=11283272; DOI=10.1128/MCB.21.8.2956-2966.2001;
Fajas L., Paul C., Vie A., Estrach S., Medema R., Blanchard J.M.,
Sardet C., Vignais M.-L.;
"Cyclin A is a mediator of p120E4F-dependent cell cycle arrest in
G1.";
Mol. Cell. Biol. 21:2956-2966(2001).
[13]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH CDKN2A AND TP53, AND
SUBCELLULAR LOCATION.
PubMed=12446718; DOI=10.1074/jbc.M210978200;
Rizos H., Diefenbach E., Badhwar P., Woodruff S., Becker T.M.,
Rooney R.J., Kefford R.F.;
"Association of p14ARF with the p120E4F transcriptional repressor
enhances cell cycle inhibition.";
J. Biol. Chem. 278:4981-4989(2003).
[14]
INTERACTION WITH HMGA2.
PubMed=14645522; DOI=10.1128/MCB.23.24.9104-9116.2003;
Tessari M.A., Gostissa M., Altamura S., Sgarra R., Rustighi A.,
Salvagno C., Caretti G., Imbriano C., Mantovani R., Del Sal G.,
Giancotti V., Manfioletti G.;
"Transcriptional activation of the cyclin A gene by the architectural
transcription factor HMGA2.";
Mol. Cell. Biol. 23:9104-9116(2003).
[15]
INTERACTION WITH HDAC1.
PubMed=12730668; DOI=10.1038/sj.onc.1206379;
Colombo R., Draetta G.F., Chiocca S.;
"Modulation of p120E4F transcriptional activity by the Gam1 adenoviral
early protein.";
Oncogene 22:2541-2547(2003).
[16]
INDUCTION BY ESTROGEN.
PubMed=15579445; DOI=10.1016/S0002-9440(10)63253-1;
Nakamura Y., Igarashi K., Suzuki T., Kanno J., Inoue T., Tazawa C.,
Saruta M., Ando T., Moriyama N., Furukawa T., Ono M., Moriya T.,
Ito K., Saito H., Ishibashi T., Takahashi S., Yamada S., Sasano H.;
"E4F1, a novel estrogen-responsive gene in possible atheroprotection,
revealed by microarray analysis.";
Am. J. Pathol. 165:2019-2031(2004).
[17]
INTERACTION WITH RASSF1.
PubMed=14729613; DOI=10.1158/0008-5472.CAN-03-2622;
Fenton S.L., Dallol A., Agathanggelou A., Hesson L.,
Ahmed-Choudhury J., Baksh S., Sardet C., Dammann R., Minna J.D.,
Downward J., Maher E.R., Latif F.;
"Identification of the E1A-regulated transcription factor p120 E4F as
an interacting partner of the RASSF1A candidate tumor suppressor
gene.";
Cancer Res. 64:102-107(2004).
[18]
FUNCTION.
PubMed=15805267; DOI=10.1158/0008-5472.CAN-04-3593;
Ahmed-Choudhury J., Agathanggelou A., Fenton S.L., Ricketts C.,
Clark G.J., Maher E.R., Latif F.;
"Transcriptional regulation of cyclin A2 by RASSF1A through the
enhanced binding of p120E4F to the cyclin A2 promoter.";
Cancer Res. 65:2690-2697(2005).
[19]
SUMOYLATION.
PubMed=15876874;
Rizos H., Woodruff S., Kefford R.F.;
"p14ARF interacts with the SUMO-conjugating enzyme Ubc9 and promotes
the sumoylation of its binding partners.";
Cell Cycle 4:597-603(2005).
[20]
FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH TP53.
PubMed=17110336; DOI=10.1016/j.cell.2006.09.031;
Le Cam L., Linares L.K., Paul C., Julien E., Lacroix M., Hatchi E.,
Triboulet R., Bossis G., Shmueli A., Rodriguez M.S., Coux O.,
Sardet C.;
"E4F1 is an atypical ubiquitin ligase that modulates p53 effector
functions independently of degradation.";
Cell 127:775-788(2006).
[21]
FUNCTION, INTERACTION WITH BMI1, AND SUBCELLULAR LOCATION.
PubMed=16882984; DOI=10.1101/gad.1453406;
Chagraoui J., Niessen S.L., Lessard J., Girard S., Coulombe P.,
Sauvageau M., Meloche S., Sauvageau G.;
"E4F1: a novel candidate factor for mediating BMI1 function in
primitive hematopoietic cells.";
Genes Dev. 20:2110-2120(2006).
[22]
FUNCTION, AND INTERACTION WITH FHL2.
PubMed=16652157; DOI=10.1038/sj.onc.1209567;
Paul C., Lacroix M., Iankova I., Julien E., Schaefer B.W.,
Labalette C., Wei Y., Le Cam A., Le Cam L., Sardet C.;
"The LIM-only protein FHL2 is a negative regulator of E4F1.";
Oncogene 25:5475-5484(2006).
[23]
INTERACTION WITH HBV PROTEIN X.
PubMed=16112766; DOI=10.1016/j.virusres.2005.07.003;
Rui E., Moura P.R., Goncalves K.A., Rooney R.J., Kobarg J.;
"Interaction of the hepatitis B virus protein HBx with the human
transcription regulatory protein p120E4F in vitro.";
Virus Res. 115:31-42(2006).
[24]
INTERACTION WITH ANP32A.
PubMed=17557114; DOI=10.1038/sj.embor.7400983;
Cvetanovic M., Rooney R.J., Garcia J.J., Toporovskaya N., Zoghbi H.Y.,
Opal P.;
"The role of LANP and ataxin 1 in E4F-mediated transcriptional
repression.";
EMBO Rep. 8:671-677(2007).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
-!- FUNCTION: May function as a transcriptional repressor. May also
function as a ubiquitin ligase mediating ubiquitination of
chromatin-associated TP53. Functions in cell survival and
proliferation through control of the cell cycle. Functions in the
p53 and pRB tumor suppressor pathways and regulates the cyclin
CCNA2 transcription.
-!- FUNCTION: Identified as a cellular target of the adenoviral
oncoprotein E1A, it is required for both transcriptional
activation and repression of viral genes.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000269|PubMed:17110336}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Homodimer; binds DNA as a dimer. Forms a complex with
CDKN2A and TP53. Interactions with TP53, RB1, ANP32A, BMI1 and
FHL2 regulate E4F1 activity. Interacts with HDAC1, HMGA2 and
RASSF1. Interacts with HBV protein X.
{ECO:0000269|PubMed:10644996, ECO:0000269|PubMed:10869426,
ECO:0000269|PubMed:12446718, ECO:0000269|PubMed:12730668,
ECO:0000269|PubMed:14645522, ECO:0000269|PubMed:14729613,
ECO:0000269|PubMed:16112766, ECO:0000269|PubMed:16652157,
ECO:0000269|PubMed:16882984, ECO:0000269|PubMed:17110336,
ECO:0000269|PubMed:17557114}.
-!- INTERACTION:
Q64770:8 (xeno); NbExp=4; IntAct=EBI-1227043, EBI-8642971;
P39687:ANP32A; NbExp=3; IntAct=EBI-1227043, EBI-359234;
Q13547:HDAC1; NbExp=3; IntAct=EBI-1227043, EBI-301834;
Q6IT96:HDAC1; NbExp=2; IntAct=EBI-1227043, EBI-6979193;
A4VCF7:lnx2b (xeno); NbExp=3; IntAct=EBI-1227043, EBI-6979266;
Q9NS23-2:RASSF1; NbExp=7; IntAct=EBI-1227043, EBI-438698;
Q9YHE8:tcf7l1a (xeno); NbExp=2; IntAct=EBI-1227043, EBI-6979298;
-!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Cytoplasm. Note=A
small fraction is detected in the cytoplasm. Excluded from the
nucleolus where it is targeted upon CDKN2A overexpression.
Localizes to the mitotic spindle during embryogenesis.
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:9530632}.
-!- DEVELOPMENTAL STAGE: Expressed in a variety of fetal tissues.
{ECO:0000269|PubMed:9530632}.
-!- INDUCTION: Up-regulated by estrogen.
{ECO:0000269|PubMed:15579445}.
-!- PTM: Proteolytic cleavage produces a 50 kDa N-terminal peptide
(p50E4F) which has a DNA-binding activity and activates
transcription in presence of the adenoviral E1A protein. The major
full length protein (p120E4F) functions as a repressor of
transcription. {ECO:0000269|PubMed:9121437}.
-!- PTM: Phosphorylated; p120E4F and p50E4F are both phosphorylated.
Phosphorylation is cell cycle-dependent and differentially
regulates DNA-binding activity and function of both forms.
{ECO:0000269|PubMed:9121437, ECO:0000269|PubMed:9512539}.
-!- PTM: May be sumoylated by UBE2I upon interaction with CDKN2A.
{ECO:0000269|PubMed:15876874}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U87269; AAD09139.1; -; mRNA.
EMBL; AK290329; BAF83018.1; -; mRNA.
EMBL; AC009065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471112; EAW85532.1; -; Genomic_DNA.
EMBL; BC080524; AAH80524.1; -; mRNA.
CCDS; CCDS32370.1; -.
RefSeq; NP_001275705.1; NM_001288776.1.
RefSeq; NP_001275707.1; NM_001288778.1.
RefSeq; NP_004415.3; NM_004424.4.
UniGene; Hs.513268; -.
ProteinModelPortal; Q66K89; -.
SMR; Q66K89; -.
BioGrid; 108209; 89.
IntAct; Q66K89; 13.
MINT; MINT-137139; -.
STRING; 9606.ENSP00000301727; -.
iPTMnet; Q66K89; -.
PhosphoSitePlus; Q66K89; -.
DMDM; 296434488; -.
EPD; Q66K89; -.
MaxQB; Q66K89; -.
PaxDb; Q66K89; -.
PeptideAtlas; Q66K89; -.
PRIDE; Q66K89; -.
Ensembl; ENST00000301727; ENSP00000301727; ENSG00000167967.
GeneID; 1877; -.
KEGG; hsa:1877; -.
UCSC; uc002cpm.5; human.
CTD; 1877; -.
DisGeNET; 1877; -.
GeneCards; E4F1; -.
HGNC; HGNC:3121; E4F1.
HPA; HPA052042; -.
HPA; HPA071325; -.
MIM; 603022; gene.
neXtProt; NX_Q66K89; -.
OpenTargets; ENSG00000167967; -.
PharmGKB; PA27579; -.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00840000129970; -.
HOGENOM; HOG000168447; -.
HOVERGEN; HBG052707; -.
InParanoid; Q66K89; -.
OMA; SGHQIIV; -.
OrthoDB; EOG091G03X5; -.
PhylomeDB; Q66K89; -.
TreeFam; TF315387; -.
SignaLink; Q66K89; -.
SIGNOR; Q66K89; -.
UniPathway; UPA00143; -.
GeneWiki; E4F1; -.
GenomeRNAi; 1877; -.
PRO; PR:Q66K89; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000167967; -.
CleanEx; HS_E4F1; -.
ExpressionAtlas; Q66K89; baseline and differential.
Genevisible; Q66K89; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005819; C:spindle; IEA:Ensembl.
GO; GO:0035497; F:cAMP response element binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; TAS:ProtInc.
GO; GO:0001227; F:transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding; IC:NTNU_SB.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0006260; P:DNA replication; IEA:Ensembl.
GO; GO:0071850; P:mitotic cell cycle arrest; TAS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
GO; GO:0010564; P:regulation of cell cycle process; IDA:UniProtKB.
GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
GO; GO:0009794; P:regulation of mitotic cell cycle, embryonic; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR013087; Znf_C2H2_type.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
SMART; SM00355; ZnF_C2H2; 10.
SUPFAM; SSF57667; SSF57667; 5.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
1: Evidence at protein level;
Cell cycle; Cell division; Complete proteome; Cytoplasm; DNA-binding;
Growth regulation; Host-virus interaction; Metal-binding; Mitosis;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Repressor; Transcription; Transcription regulation; Transferase;
Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 784 Transcription factor E4F1.
/FTId=PRO_0000324307.
ZN_FING 192 214 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 220 242 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 248 272 C2H2-type 3; degenerate.
{ECO:0000255|PROSITE-ProRule:PRU00042}.
ZN_FING 435 457 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 463 485 C2H2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 491 513 C2H2-type 6. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 519 541 C2H2-type 7. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 547 569 C2H2-type 8. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 575 597 C2H2-type 9; degenerate.
{ECO:0000255|PROSITE-ProRule:PRU00042}.
REGION 41 85 Required for ubiquitin ligase activity.
REGION 184 263 Mediates dimerization, DNA-binding,
transcription repression of CCNA2 and
interaction with HMGA2.
{ECO:0000269|PubMed:14645522}.
REGION 369 566 Mediates interaction with CDKN2A.
REGION 435 599 Interaction with BMI1.
{ECO:0000269|PubMed:16882984}.
REGION 521 580 Mediates interaction with TP53.
REGION 575 597 Mediates interaction with RASSF1.
{ECO:0000269|PubMed:14729613}.
MOD_RES 50 50 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
VARIANT 167 167 R -> H (in dbSNP:rs26839).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9121437,
ECO:0000269|Ref.4}.
/FTId=VAR_060270.
VARIANT 355 355 V -> I (in dbSNP:rs59784157).
/FTId=VAR_060271.
MUTAGEN 194 194 C->S: Increases DNA-binding; when
associated with S-197.
{ECO:0000269|PubMed:9512539}.
MUTAGEN 197 197 C->S: Increases DNA-binding; when
associated with S-194.
{ECO:0000269|PubMed:9512539}.
MUTAGEN 210 210 H->A: Alters DNA-binding.
{ECO:0000269|PubMed:9512539}.
MUTAGEN 237 237 R->L: Alters DNA-binding; when associated
with N-238. {ECO:0000269|PubMed:9512539}.
MUTAGEN 238 238 H->N: Alters DNA-binding; when associated
with L-237. {ECO:0000269|PubMed:9512539}.
MUTAGEN 249 249 K->M: Alters DNA-binding; when associated
with S-250. {ECO:0000269|PubMed:9512539}.
MUTAGEN 250 250 C->S: Alters DNA-binding; when associated
with M-249. {ECO:0000269|PubMed:9512539}.
CONFLICT 4 4 A -> E (in Ref. 1; AAD09139).
{ECO:0000305}.
CONFLICT 363 364 SE -> RK (in Ref. 1; AAD09139).
{ECO:0000305}.
CONFLICT 425 425 A -> V (in Ref. 2; BAF83018).
{ECO:0000305}.
CONFLICT 480 481 KH -> TD (in Ref. 1; AAD09139).
{ECO:0000305}.
CONFLICT 544 544 E -> D (in Ref. 2; BAF83018).
{ECO:0000305}.
CONFLICT 681 682 QA -> PR (in Ref. 1; AAD09139).
{ECO:0000305}.
CONFLICT 704 705 EA -> RG (in Ref. 1; AAD09139).
{ECO:0000305}.
SEQUENCE 784 AA; 83496 MW; 60F6E711F2748FD8 CRC64;
MEGAMAVRVT AAHTAEAQAE AGREAGEGAV AAVAAALAPS GFLGLPAPFS EEDEDDVHRC
GRCQAEFTAL EDFVQHKIQK ACQRAPPEAL PATPATTALL GQEVVPAAPG PEEPITVAHI
VVEAASLAAD ISHASDLVGG GHIKEVIVAA EAELGDGEMA EAPGSPRQQG LGLAGEGEQA
QVKLLVNKDG RYVCALCHKT FKTGSILKAH MVTHSSRKDH ECKLCGASFR TKGSLIRHHR
RHTDERPYKC SKCGKSFRES GALTRHLKSL TPCTEKIRFS VSKDVVVSKE DARAGSGAGA
AGLGTATSSV TGEPIETSPV IHLVTDAKGT VIHEVHVQMQ ELSLGMKALA PEPPVSQELP
CSSEGSRENL LHQAMQNSGI VLERAAGEEG ALEPAPAAGS SPQPLAVAAP QLPVLEVQPL
ETQVASEASA VPRTHPCPQC SETFPTAATL EAHKRGHTGP RPFACAQCGK AFPKAYLLKK
HQEVHVRERR FRCGDCGKLY KTIAHVRGHR RVHSDERPYP CPKCGKRYKT KNAQQVHFRT
HLEEKPHVCQ FCSRGFREKG SLVRHVRHHT GEKPFKCYKC GRGFAEHGTL NRHLRTKGGC
LLEVEELLVS EDSPAAATTV LTEDPHTVLV EFSSVVADTQ EYIIEATADD AETSEATEII
EGTQTEVDSH IMKVVQQIVH QASAGHQIIV QNVTMDEETA LGPEAAAADT ITIATPESLT
EQVAMTLASA ISEGTVLAAR AGTSGTEQAT VTMVSSEDIE ILEHAGELVI ASPEGQLEVQ
TVIV


Related products :

Catalog number Product name Quantity
EIAAB12289 E4F,E4F transcription factor 1,E4F1,Homo sapiens,Human,p120E4F,p50E4F,Putative E3 ubiquitin-protein ligase E4F1,Transcription factor E4F,Transcription factor E4F1
EIAAB12290 E4F transcription factor 1,E4f1,Mouse,Mus musculus,p120E4F,Putative E3 ubiquitin-protein ligase E4F1,Transcription factor E4F,Transcription factor E4F1,Transcription factor phi AP3
E4F1_MOUSE ELISA Kit FOR Transcription factor E4F1; organism: Mouse; gene name: E4f1 96T
CSB-EL007350HU Human Transcription factor E4F1(E4F1) ELISA kit SpeciesHuman 96T
CSB-EL007350MO Mouse Transcription factor E4F1(E4F1) ELISA kit SpeciesMouse 96T
H7241 Transcription factor E4F1 (E4F1), Human, ELISA Kit 96T
H7242 Transcription factor E4F1 (E4F1), Mouse, ELISA Kit 96T
CSB-EL007350MO Mouse Transcription factor E4F1(E4F1) ELISA kit 96T
CSB-EL007350HU Human Transcription factor E4F1(E4F1) ELISA kit 96T
EA7 E4F1 Gene E4F transcription factor 1
E4F1 E2F7 Gene E2F transcription factor 7
CSB-EL007350HU Human E4F transcription factor 1 (E4F1) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL007350MO Mouse E4F transcription factor 1 (E4F1) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
18-003-42098 Ets domain transcription factor - ESE3 transcription factor; EHF protein; DJ875K15.1.2 (Ets homologous factor (Ets-domain transcription factor. ESE-3B (Isoform 2))); ETS-family transcription factor EH 0.1 mg Protein A
EIAAB42084 Homo sapiens,Human,Mitochondrial transcription factor 1,MtTF1,mtTFA,TCF6,TCF-6,TCF6L2,TFAM,Transcription factor 6,Transcription factor 6-like 2,Transcription factor A, mitochondrial
EIAAB42103 Immunoglobulin enhancer-binding factor E12_E47,Pan,Pancreas specific transcription factor 1c,Ptf1c,Rat,Rattus norvegicus,Tcf3,TCF-3,Tcfe2a,Transcription factor 3,Transcription factor E2-alpha,Transcri
EIAAB42104 Alf2,Immunoglobulin enhancer-binding factor E12_E47,Me2,Mouse,Mus musculus,Tcf3,TCF-3,Tcfe2a,Transcription factor 3,Transcription factor A1,Transcription factor E2-alpha
31-248 Transcription initiation factor IIA . and . chains (GTranscription Factor Antibodies2A1, Transcription Factor AntibodiesIIA p35 and p19 subunits, Transcription Factor AntibodiesIIAL) binding ability o 0.05 mg
18-003-42235 POU domain. class 2. transcription factor 3 - Octamer-binding transcription factor 11; Oct-11; Transcription factor Skn-1; PLA-1 protein Polyclonal 0.05 mg Aff Pur
18-003-43070 T-box transcription factor TBX21 - T-box protein 21; Transcription factor TBLYM; T-cell-specific T-box transcription factor T-bet Polyclonal 0.1 mg Protein A
18-003-42235 POU domain. class 2. transcription factor 3 - Octamer-binding transcription factor 11; Oct-11; Transcription factor Skn-1; PLA-1 protein Polyclonal 0.1 mg Protein A
18-003-42234 POU domain. class 2. transcription factor 3 - Octamer-binding transcription factor 11; Oct-11; Transcription factor Skn-1; PLA-1 protein Polyclonal 0.05 mg Aff Pur
18-003-42234 POU domain. class 2. transcription factor 3 - Octamer-binding transcription factor 11; Oct-11; Transcription factor Skn-1; PLA-1 protein Polyclonal 0.1 mg Protein A
E1346h ELISA kit Activating transcription factor 1,ATF1,cAMP-dependent transcription factor ATF-1,Cyclic AMP-dependent transcription factor ATF-1,Homo sapiens,Human,Protein TREB36 96T
U1346h CLIA Activating transcription factor 1,ATF1,cAMP-dependent transcription factor ATF-1,Cyclic AMP-dependent transcription factor ATF-1,Homo sapiens,Human,Protein TREB36 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur