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Database: UniProt
Entry: Q66K89
LinkDB: Q66K89
Original site: Q66K89 
ID   E4F1_HUMAN              Reviewed;         784 AA.
AC   Q66K89; A8K2R4; O00146;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   09-JUL-2014, entry version 109.
DE   RecName: Full=Transcription factor E4F1;
DE            EC=6.3.2.-;
DE   AltName: Full=E4F transcription factor 1;
DE   AltName: Full=Putative E3 ubiquitin-protein ligase E4F1;
DE   AltName: Full=Transcription factor E4F;
DE   AltName: Full=p120E4F;
DE   AltName: Full=p50E4F;
GN   Name=E4F1; Synonyms=E4F;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PROTEOLYTIC PROCESSING,
RP   PHOSPHORYLATION, DNA-BINDING, AND VARIANT HIS-167.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=9121437;
RA   Fernandes E.R., Rooney R.J.;
RT   "The adenovirus E1A-regulated transcription factor E4F is generated
RT   from the human homolog of nuclear factor phiAP3.";
RL   Mol. Cell. Biol. 17:1890-1903(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-167.
RC   TISSUE=Tongue;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
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.,
RA   Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA   Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA   Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA   Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA   Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA   Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA   Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA   Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA   Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA   Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA   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.,
RA   Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA   Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA   Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA   Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA   Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA   Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA   Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA   Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA   Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT HIS-167.
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-167.
RC   TISSUE=Uterus;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=9530632; DOI=10.1007/s003359900758;
RA   Rooney R.J., Daniels R.R., Jenkins N.A., Gilbert D.J., Rothammer K.,
RA   Morris S.W., Higgs D.R., Copeland N.G.;
RT   "Chromosomal location and tissue expression of the gene encoding the
RT   adenovirus E1A-regulated transcription factor E4F in humans and
RT   mice.";
RL   Mamm. Genome 9:320-323(1998).
RN   [7]
RP   FUNCTION.
RX   PubMed=9418893;
RA   Fernandes E.R., Zhang J.Y., Rooney R.J.;
RT   "Adenovirus E1A-regulated transcription factor p120E4F inhibits cell
RT   growth and induces the stabilization of the cdk inhibitor p21WAF1.";
RL   Mol. Cell. Biol. 18:459-467(1998).
RN   [8]
RP   OLIGOMERIZATION, PHOSPHORYLATION, DNA-BINDING, AND MUTAGENESIS OF
RP   CYS-194; CYS-197; HIS-210; ARG-237; HIS-238; LYS-249 AND CYS-250.
RX   PubMed=9512539; DOI=10.1093/nar/26.7.1681;
RA   Rooney R.J., Rothammer K., Fernandes E.R.;
RT   "Mutational analysis of p50E4F suggests that DNA binding activity is
RT   mediated through an alternative structure in a zinc finger domain that
RT   is regulated by phosphorylation.";
RL   Nucleic Acids Res. 26:1681-1688(1998).
RN   [9]
RP   FUNCTION.
RX   PubMed=10373523;
RA   Fernandes E.R., Rooney R.J.;
RT   "Suppression of E1A-mediated transformation by the p50E4F
RT   transcription factor.";
RL   Mol. Cell. Biol. 19:4739-4749(1999).
RN   [10]
RP   FUNCTION, AND INTERACTION WITH TP53.
RX   PubMed=10644996; DOI=10.1038/sj.onc.1203250;
RA   Sandy P., Gostissa M., Fogal V., Cecco L.D., Szalay K., Rooney R.J.,
RA   Schneider C., Del Sal G.;
RT   "p53 is involved in the p120E4F-mediated growth arrest.";
RL   Oncogene 19:188-199(2000).
RN   [11]
RP   FUNCTION, REGULATION BY RB1, AND INTERACTION WITH RB1.
RX   PubMed=10869426; DOI=10.1073/pnas.130198397;
RA   Fajas L., Paul C., Zugasti O., Le Cam L., Polanowska J., Fabbrizio E.,
RA   Medema R., Vignais M.-L., Sardet C.;
RT   "pRB binds to and modulates the transrepressing activity of the E1A-
RT   regulated transcription factor p120E4F.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:7738-7743(2000).
RN   [12]
RP   FUNCTION.
RX   PubMed=11283272; DOI=10.1128/MCB.21.8.2956-2966.2001;
RA   Fajas L., Paul C., Vie A., Estrach S., Medema R., Blanchard J.M.,
RA   Sardet C., Vignais M.-L.;
RT   "Cyclin A is a mediator of p120E4F-dependent cell cycle arrest in
RT   G1.";
RL   Mol. Cell. Biol. 21:2956-2966(2001).
RN   [13]
RP   FUNCTION, IDENTIFICATION IN A COMPLEX WITH CDKN2A AND TP53, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=12446718; DOI=10.1074/jbc.M210978200;
RA   Rizos H., Diefenbach E., Badhwar P., Woodruff S., Becker T.M.,
RA   Rooney R.J., Kefford R.F.;
RT   "Association of p14ARF with the p120E4F transcriptional repressor
RT   enhances cell cycle inhibition.";
RL   J. Biol. Chem. 278:4981-4989(2003).
RN   [14]
RP   INTERACTION WITH HMGA2.
RX   PubMed=14645522; DOI=10.1128/MCB.23.24.9104-9116.2003;
RA   Tessari M.A., Gostissa M., Altamura S., Sgarra R., Rustighi A.,
RA   Salvagno C., Caretti G., Imbriano C., Mantovani R., Del Sal G.,
RA   Giancotti V., Manfioletti G.;
RT   "Transcriptional activation of the cyclin A gene by the architectural
RT   transcription factor HMGA2.";
RL   Mol. Cell. Biol. 23:9104-9116(2003).
RN   [15]
RP   INTERACTION WITH HDAC1.
RX   PubMed=12730668; DOI=10.1038/sj.onc.1206379;
RA   Colombo R., Draetta G.F., Chiocca S.;
RT   "Modulation of p120E4F transcriptional activity by the Gam1 adenoviral
RT   early protein.";
RL   Oncogene 22:2541-2547(2003).
RN   [16]
RP   INDUCTION BY ESTROGEN.
RX   PubMed=15579445; DOI=10.1016/S0002-9440(10)63253-1;
RA   Nakamura Y., Igarashi K., Suzuki T., Kanno J., Inoue T., Tazawa C.,
RA   Saruta M., Ando T., Moriyama N., Furukawa T., Ono M., Moriya T.,
RA   Ito K., Saito H., Ishibashi T., Takahashi S., Yamada S., Sasano H.;
RT   "E4F1, a novel estrogen-responsive gene in possible atheroprotection,
RT   revealed by microarray analysis.";
RL   Am. J. Pathol. 165:2019-2031(2004).
RN   [17]
RP   INTERACTION WITH RASSF1.
RX   PubMed=14729613; DOI=10.1158/0008-5472.CAN-03-2622;
RA   Fenton S.L., Dallol A., Agathanggelou A., Hesson L.,
RA   Ahmed-Choudhury J., Baksh S., Sardet C., Dammann R., Minna J.D.,
RA   Downward J., Maher E.R., Latif F.;
RT   "Identification of the E1A-regulated transcription factor p120 E4F as
RT   an interacting partner of the RASSF1A candidate tumor suppressor
RT   gene.";
RL   Cancer Res. 64:102-107(2004).
RN   [18]
RP   FUNCTION.
RX   PubMed=15805267; DOI=10.1158/0008-5472.CAN-04-3593;
RA   Ahmed-Choudhury J., Agathanggelou A., Fenton S.L., Ricketts C.,
RA   Clark G.J., Maher E.R., Latif F.;
RT   "Transcriptional regulation of cyclin A2 by RASSF1A through the
RT   enhanced binding of p120E4F to the cyclin A2 promoter.";
RL   Cancer Res. 65:2690-2697(2005).
RN   [19]
RP   SUMOYLATION.
RX   PubMed=15876874;
RA   Rizos H., Woodruff S., Kefford R.F.;
RT   "p14ARF interacts with the SUMO-conjugating enzyme Ubc9 and promotes
RT   the sumoylation of its binding partners.";
RL   Cell Cycle 4:597-603(2005).
RN   [20]
RP   FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH TP53.
RX   PubMed=17110336; DOI=10.1016/j.cell.2006.09.031;
RA   Le Cam L., Linares L.K., Paul C., Julien E., Lacroix M., Hatchi E.,
RA   Triboulet R., Bossis G., Shmueli A., Rodriguez M.S., Coux O.,
RA   Sardet C.;
RT   "E4F1 is an atypical ubiquitin ligase that modulates p53 effector
RT   functions independently of degradation.";
RL   Cell 127:775-788(2006).
RN   [21]
RP   FUNCTION, INTERACTION WITH BMI1, AND SUBCELLULAR LOCATION.
RX   PubMed=16882984; DOI=10.1101/gad.1453406;
RA   Chagraoui J., Niessen S.L., Lessard J., Girard S., Coulombe P.,
RA   Sauvageau M., Meloche S., Sauvageau G.;
RT   "E4F1: a novel candidate factor for mediating BMI1 function in
RT   primitive hematopoietic cells.";
RL   Genes Dev. 20:2110-2120(2006).
RN   [22]
RP   FUNCTION, AND INTERACTION WITH FHL2.
RX   PubMed=16652157; DOI=10.1038/sj.onc.1209567;
RA   Paul C., Lacroix M., Iankova I., Julien E., Schaefer B.W.,
RA   Labalette C., Wei Y., Le Cam A., Le Cam L., Sardet C.;
RT   "The LIM-only protein FHL2 is a negative regulator of E4F1.";
RL   Oncogene 25:5475-5484(2006).
RN   [23]
RP   INTERACTION WITH HBV PROTEIN X.
RX   PubMed=16112766; DOI=10.1016/j.virusres.2005.07.003;
RA   Rui E., Moura P.R., Goncalves K.A., Rooney R.J., Kobarg J.;
RT   "Interaction of the hepatitis B virus protein HBx with the human
RT   transcription regulatory protein p120E4F in vitro.";
RL   Virus Res. 115:31-42(2006).
RN   [24]
RP   INTERACTION WITH ANP32A.
RX   PubMed=17557114; DOI=10.1038/sj.embor.7400983;
RA   Cvetanovic M., Rooney R.J., Garcia J.J., Toporovskaya N., Zoghbi H.Y.,
RA   Opal P.;
RT   "The role of LANP and ataxin 1 in E4F-mediated transcriptional
RT   repression.";
RL   EMBO Rep. 8:671-677(2007).
RN   [25]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [26]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [27]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
CC   -!- FUNCTION: May function as a transcriptional repressor. May also
CC       function as a ubiquitin ligase mediating ubiquitination of
CC       chromatin-associated TP53. Functions in cell survival and
CC       proliferation through control of the cell cycle. Functions in the
CC       p53 and pRB tumor suppressor pathways and regulates the cyclin
CC       CCNA2 transcription.
CC   -!- FUNCTION: Identified as a cellular target of the adenoviral
CC       oncoprotein E1A, it is required for both transcriptional
CC       activation and repression of viral genes.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Homodimer; binds DNA as a dimer. Forms a complex with
CC       CDKN2A and TP53. Interactions with TP53, RB1, ANP32A, BMI1 and
CC       FHL2 regulate E4F1 activity. Interacts with HDAC1, HMGA2 and
CC       RASSF1. Interacts with HBV protein X.
CC   -!- INTERACTION:
CC       Q64770:8 (xeno); NbExp=4; IntAct=EBI-1227043, EBI-8642971;
CC       P39687:ANP32A; NbExp=3; IntAct=EBI-1227043, EBI-359234;
CC       Q13547:HDAC1; NbExp=3; IntAct=EBI-1227043, EBI-301834;
CC       Q6IT96:HDAC1; NbExp=2; IntAct=EBI-1227043, EBI-6979193;
CC       A4VCF7:lnx2b (xeno); NbExp=3; IntAct=EBI-1227043, EBI-6979266;
CC       Q9NS23-2:RASSF1; NbExp=7; IntAct=EBI-1227043, EBI-438698;
CC       Q9YHE8:tcf7l1a (xeno); NbExp=2; IntAct=EBI-1227043, EBI-6979298;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Cytoplasm. Note=A
CC       small fraction is detected in the cytoplasm. Excluded from the
CC       nucleolus where it is targeted upon CDKN2A overexpression.
CC       Localizes to the mitotic spindle during embryogenesis (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC   -!- DEVELOPMENTAL STAGE: Expressed in a variety of fetal tissues.
CC   -!- INDUCTION: Up-regulated by estrogen.
CC   -!- PTM: Proteolytic cleavage produces a 50 kDa N-terminal peptide
CC       (p50E4F) which has a DNA-binding activity and activates
CC       transcription in presence of the adenoviral E1A protein. The major
CC       full length protein (p120E4F) functions as a repressor of
CC       transcription.
CC   -!- PTM: Phosphorylated; p120E4F and p50E4F are both phosphorylated.
CC       Phosphorylation is cell cycle-dependent and differentially
CC       regulates DNA-binding activity and function of both forms.
CC   -!- PTM: May be sumoylated by UBE2I upon interaction with CDKN2A.
CC   -!- SIMILARITY: Contains 9 C2H2-type zinc fingers.
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DR   EMBL; U87269; AAD09139.1; -; mRNA.
DR   EMBL; AK290329; BAF83018.1; -; mRNA.
DR   EMBL; AC009065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471112; EAW85532.1; -; Genomic_DNA.
DR   EMBL; BC080524; AAH80524.1; -; mRNA.
DR   CCDS; CCDS32370.1; -.
DR   RefSeq; NP_001275705.1; NM_001288776.1.
DR   RefSeq; NP_001275707.1; NM_001288778.1.
DR   RefSeq; NP_004415.3; NM_004424.4.
DR   UniGene; Hs.513268; -.
DR   ProteinModelPortal; Q66K89; -.
DR   SMR; Q66K89; 191-296, 405-599.
DR   BioGrid; 108209; 12.
DR   IntAct; Q66K89; 11.
DR   MINT; MINT-137139; -.
DR   STRING; 9606.ENSP00000301727; -.
DR   PhosphoSite; Q66K89; -.
DR   DMDM; 296434488; -.
DR   MaxQB; Q66K89; -.
DR   PaxDb; Q66K89; -.
DR   PRIDE; Q66K89; -.
DR   Ensembl; ENST00000301727; ENSP00000301727; ENSG00000167967.
DR   GeneID; 1877; -.
DR   KEGG; hsa:1877; -.
DR   UCSC; uc002cpm.3; human.
DR   CTD; 1877; -.
DR   GeneCards; GC16P002276; -.
DR   HGNC; HGNC:3121; E4F1.
DR   HPA; HPA052042; -.
DR   MIM; 603022; gene.
DR   neXtProt; NX_Q66K89; -.
DR   PharmGKB; PA27579; -.
DR   eggNOG; COG5048; -.
DR   HOGENOM; HOG000168447; -.
DR   HOVERGEN; HBG052707; -.
DR   InParanoid; Q66K89; -.
DR   OMA; CQFCSRG; -.
DR   OrthoDB; EOG761BT6; -.
DR   PhylomeDB; Q66K89; -.
DR   TreeFam; TF315387; -.
DR   SignaLink; Q66K89; -.
DR   UniPathway; UPA00143; -.
DR   GeneWiki; E4F1; -.
DR   GenomeRNAi; 1877; -.
DR   NextBio; 7679; -.
DR   PRO; PR:Q66K89; -.
DR   ArrayExpress; Q66K89; -.
DR   Bgee; Q66K89; -.
DR   CleanEx; HS_E4F1; -.
DR   Genevestigator; Q66K89; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:HPA.
DR   GO; GO:0005819; C:spindle; IEA:Ensembl.
DR   GO; GO:0035497; F:cAMP response element binding; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc.
DR   GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
DR   GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
DR   GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR   GO; GO:0006260; P:DNA replication; IEA:Ensembl.
DR   GO; GO:0009790; P:embryo development; IEA:Ensembl.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   GO; GO:0071850; P:mitotic cell cycle arrest; TAS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0010564; P:regulation of cell cycle process; IDA:UniProtKB.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR   GO; GO:0009794; P:regulation of mitotic cell cycle, embryonic; IEA:Ensembl.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.160.60; -; 9.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00355; ZnF_C2H2; 10.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Complete proteome; Cytoplasm; DNA-binding;
KW   Growth regulation; Host-virus interaction; Ligase; Metal-binding;
KW   Mitosis; Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
KW   Repeat; Repressor; Transcription; Transcription regulation;
KW   Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1    784       Transcription factor E4F1.
FT                                /FTId=PRO_0000324307.
FT   ZN_FING     192    214       C2H2-type 1.
FT   ZN_FING     220    242       C2H2-type 2.
FT   ZN_FING     248    272       C2H2-type 3; degenerate.
FT   ZN_FING     435    457       C2H2-type 4.
FT   ZN_FING     463    485       C2H2-type 5.
FT   ZN_FING     491    513       C2H2-type 6.
FT   ZN_FING     519    541       C2H2-type 7.
FT   ZN_FING     547    569       C2H2-type 8.
FT   ZN_FING     575    597       C2H2-type 9; degenerate.
FT   REGION       41     85       Required for ubiquitin ligase activity.
FT   REGION      184    263       Mediates dimerization, DNA-binding,
FT                                transcription repression of CCNA2 and
FT                                interaction with HMGA2.
FT   REGION      369    566       Mediates interaction with CDKN2A.
FT   REGION      435    599       Interaction with BMI1.
FT   REGION      521    580       Mediates interaction with TP53.
FT   REGION      575    597       Mediates interaction with RASSF1.
FT   MOD_RES      50     50       Phosphoserine.
FT   VARIANT     167    167       R -> H (in dbSNP:rs26839).
FT                                /FTId=VAR_060270.
FT   VARIANT     355    355       V -> I (in dbSNP:rs59784157).
FT                                /FTId=VAR_060271.
FT   MUTAGEN     194    194       C->S: Increases DNA-binding; when
FT                                associated with S-197.
FT   MUTAGEN     197    197       C->S: Increases DNA-binding; when
FT                                associated with S-194.
FT   MUTAGEN     210    210       H->A: Alters DNA-binding.
FT   MUTAGEN     237    237       R->L: Alters DNA-binding; when associated
FT                                with N-238.
FT   MUTAGEN     238    238       H->N: Alters DNA-binding; when associated
FT                                with L-237.
FT   MUTAGEN     249    249       K->M: Alters DNA-binding; when associated
FT                                with S-250.
FT   MUTAGEN     250    250       C->S: Alters DNA-binding; when associated
FT                                with M-249.
FT   CONFLICT      4      4       A -> E (in Ref. 1; AAD09139).
FT   CONFLICT    363    364       SE -> RK (in Ref. 1; AAD09139).
FT   CONFLICT    425    425       A -> V (in Ref. 2; BAF83018).
FT   CONFLICT    480    481       KH -> TD (in Ref. 1; AAD09139).
FT   CONFLICT    544    544       E -> D (in Ref. 2; BAF83018).
FT   CONFLICT    681    682       QA -> PR (in Ref. 1; AAD09139).
FT   CONFLICT    704    705       EA -> RG (in Ref. 1; AAD09139).
SQ   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
//
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