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 18-SEP-2013, entry version 100. 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; 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 MASS RP SPECTROMETRY. 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 MASS RP SPECTROMETRY. 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 Q9NS23-2:RASSF1; NbExp=7; IntAct=EBI-1227043, EBI-438698; 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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 IPI; IPI00184135; -. DR RefSeq; NP_004415.2; NM_004424.3. DR UniGene; Hs.513268; -. DR UniGene; Hs.615283; -. DR ProteinModelPortal; Q66K89; -. DR SMR; Q66K89; 113-297, 404-596. DR IntAct; Q66K89; 1. DR MINT; MINT-137139; -. DR STRING; 9606.ENSP00000301727; -. DR PhosphoSite; Q66K89; -. DR DMDM; 296434488; -. 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 MIM; 603022; gene. DR neXtProt; NX_Q66K89; -. DR PharmGKB; PA27579; -. DR eggNOG; COG5048; -. DR HOGENOM; HOG000168447; -. DR HOVERGEN; HBG052707; -. DR InParanoid; Q66K89; -. DR OMA; RERRFRC; -. DR OrthoDB; EOG4PZJ8D; -. DR PhylomeDB; Q66K89; -. DR SignaLink; Q66K89; -. DR UniPathway; UPA00143; -. DR GeneWiki; E4F1; -. DR GenomeRNAi; 1877; -. DR NextBio; 7679; -. 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:0005819; C:spindle; IEA:Compara. DR GO; GO:0035497; F:cAMP response element binding; IDA:UniProtKB. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. 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:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc. DR GO; GO:0006260; P:DNA replication; IEA:Compara. DR GO; GO:0009790; P:embryo development; IEA:Compara. 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:Compara. DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. DR GO; GO:0019048; P:virus-host interaction; 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 //