ID E2F7_HUMAN Reviewed; 911 AA. AC Q96AV8; A6NC74; B2RMR7; B3KTZ5; B3KUP8; B5MED9; DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2010, sequence version 3. DT 04-NOV-2026, entry version 169. DE RecName: Full=Transcription factor E2F7; DE Short=E2F-7; GN Name=E2F7; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 595-911 (ISOFORM 2), AND VARIANT LEU-72. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 58-911 (ISOFORM 1), NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 504-911 (ISOFORM 3), AND VARIANT LEU-72. RC TISSUE=Testis; 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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 [4] RP IDENTIFICATION, FUNCTION, SELF-ASSOCIATION, AND MUTAGENESIS OF RP 147-LEU-GLY-148. RX PubMed=14633988; DOI=10.1093/emboj/cdg613; RA Di Stefano L., Jensen M.R., Helin K.; RT "E2F7, a novel E2F featuring DP-independent repression of a subset of E2F- RT regulated genes."; RL EMBO J. 22:6289-6298(2003). RN [5] RP FUNCTION, SELF-ASSOCIATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP ARG-185 AND ARG-334. RX PubMed=15133492; DOI=10.1038/sj.onc.1207649; RA Logan N., Delavaine L., Graham A., Reilly C., Wilson J., Brummelkamp T.R., RA Hijmans E.M., Bernards R., La Thangue N.B.; RT "E2F-7: a distinctive E2F family member with an unusual organization of RT DNA-binding domains."; RL Oncogene 23:5138-5150(2004). RN [6] RP SUBUNIT. RX PubMed=18194653; DOI=10.1016/j.devcel.2007.10.017; RA Li J., Ran C., Li E., Gordon F., Comstock G., Siddiqui H., Cleghorn W., RA Chen H.-Z., Kornacker K., Liu C.-G., Pandit S.K., Khanizadeh M., RA Weinstein M., Leone G., de Bruin A.; RT "Synergistic function of E2F7 and E2F8 is essential for cell survival and RT embryonic development."; RL Dev. Cell 14:62-75(2008). RN [7] RP FUNCTION, INDUCTION, SUBUNIT, AND MUTAGENESIS OF ARG-185 AND ARG-334. RX PubMed=18202719; DOI=10.1038/sj.embor.7401158; RA Zalmas L.P., Zhao X., Graham A.L., Fisher R., Reilly C., Coutts A.S., RA La Thangue N.B.; RT "DNA-damage response control of E2F7 and E2F8."; RL EMBO Rep. 9:252-259(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410, AND IDENTIFICATION BY RP 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410, AND IDENTIFICATION BY RP 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., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [10] RP FUNCTION, AND INTERACTION WITH HIF1A. RX PubMed=22903062; DOI=10.1038/emboj.2012.231; RA Weijts B.G., Bakker W.J., Cornelissen P.W., Liang K.H., Schaftenaar F.H., RA Westendorp B., de Wolf C.A., Paciejewska M., Scheele C.L., Kent L., RA Leone G., Schulte-Merker S., de Bruin A.; RT "E2F7 and E2F8 promote angiogenesis through transcriptional activation of RT VEGFA in cooperation with HIF1."; RL EMBO J. 31:3871-3884(2012). RN [11] RP FUNCTION. RX PubMed=19223542; DOI=10.1158/0008-5472.can-08-2725; RA Endo-Munoz L., Dahler A., Teakle N., Rickwood D., Hazar-Rethinam M., RA Abdul-Jabbar I., Sommerville S., Dickinson I., Kaur P., Paquet-Fifield S., RA Saunders N.; RT "E2F7 can regulate proliferation, differentiation, and apoptotic responses RT in human keratinocytes: implications for cutaneous squamous cell carcinoma RT formation."; RL Cancer Res. 69:1800-1808(2009). RN [12] RP FUNCTION. RX PubMed=21248772; DOI=10.1038/jid.2010.430; RA Hazar-Rethinam M., Cameron S.R., Dahler A.L., Endo-Munoz L.B., Smith L., RA Rickwood D., Saunders N.A.; RT "Loss of E2F7 expression is an early event in squamous differentiation and RT causes derepression of the key differentiation activator Sp1."; RL J. Invest. Dermatol. 131:1077-1084(2011). RN [13] RP FUNCTION, AND INDUCTION. RX PubMed=22802528; DOI=10.1101/gad.184911.111; RA Carvajal L.A., Hamard P.J., Tonnessen C., Manfredi J.J.; RT "E2F7, a novel target, is up-regulated by p53 and mediates DNA damage- RT dependent transcriptional repression."; RL Genes Dev. 26:1533-1545(2012). RN [14] RP FUNCTION, AND INDUCTION. RX PubMed=22802529; DOI=10.1101/gad.196238.112; RA Aksoy O., Chicas A., Zeng T., Zhao Z., McCurrach M., Wang X., Lowe S.W.; RT "The atypical E2F family member E2F7 couples the p53 and RB pathways during RT cellular senescence."; RL Genes Dev. 26:1546-1557(2012). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95; SER-410 AND SER-840, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [16] RP INTERACTION WITH MN1. RX PubMed=31839203; DOI=10.1016/j.ajhg.2019.11.011; RA Miyake N., Takahashi H., Nakamura K., Isidor B., Hiraki Y., Koshimizu E., RA Shiina M., Sasaki K., Suzuki H., Abe R., Kimura Y., Akiyama T., RA Tomizawa S.I., Hirose T., Hamanaka K., Miyatake S., Mitsuhashi S., RA Mizuguchi T., Takata A., Obo K., Kato M., Ogata K., Matsumoto N.; RT "Gain-of-function MN1 truncation variants cause a recognizable syndrome RT with craniofacial and brain abnormalities."; RL Am. J. Hum. Genet. 106:13-25(2020). CC -!- FUNCTION: Atypical E2F transcription factor that participates in CC various processes such as angiogenesis, polyploidization of specialized CC cells and DNA damage response. Mainly acts as a transcription repressor CC that binds DNA independently of DP proteins and specifically recognizes CC the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represses CC transcription of classical E2F transcription factors such as E2F1. Acts CC as a regulator of S-phase by recognizing and binding the E2-related CC site 5'-TTCCCGCC-3' and mediating repression of G1/S-regulated genes. CC Plays a key role in polyploidization of cells in placenta and liver by CC regulating the endocycle, probably by repressing genes promoting CC cytokinesis and antagonizing action of classical E2F proteins (E2F1, CC E2F2 and/or E2F3). Required for placental development by promoting CC polyploidization of trophoblast giant cells. Also involved in DNA CC damage response: up-regulated by p53/TP53 following genotoxic stress CC and acts as a downstream effector of p53/TP53-dependent repression by CC mediating repression of indirect p53/TP53 target genes involved in DNA CC replication. Acts as a promoter of sprouting angiogenesis, possibly by CC acting as a transcription activator: associates with HIF1A, recognizes CC and binds the VEGFA promoter, which is different from canonical E2 CC recognition site, and activates expression of the VEGFA gene. Acts as a CC negative regulator of keratinocyte differentiation. CC {ECO:0000269|PubMed:14633988, ECO:0000269|PubMed:15133492, CC ECO:0000269|PubMed:18202719, ECO:0000269|PubMed:19223542, CC ECO:0000269|PubMed:21248772, ECO:0000269|PubMed:22802528, CC ECO:0000269|PubMed:22802529, ECO:0000269|PubMed:22903062}. CC -!- SUBUNIT: Homodimer and heterodimer: mainly forms homodimers and, to a CC lesser extent, heterodimers with E2F8. Dimerization is important for CC DNA-binding. Interacts with HIF1A. Interacts with MN1 CC (PubMed:31839203). {ECO:0000269|PubMed:18194653, CC ECO:0000269|PubMed:18202719, ECO:0000269|PubMed:22903062, CC ECO:0000269|PubMed:31839203}. CC -!- INTERACTION: CC Q96AV8; Q96AV8: E2F7; NbExp=3; IntAct=EBI-1386765, EBI-1386765; CC Q96AV8; A0AVK6: E2F8; NbExp=4; IntAct=EBI-1386765, EBI-7779316; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15133492}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=E2F7b; CC IsoId=Q96AV8-1; Sequence=Displayed; CC Name=2; Synonyms=E2F7a; CC IsoId=Q96AV8-2; Sequence=VSP_027473, VSP_027474; CC Name=3; CC IsoId=Q96AV8-3; Sequence=VSP_044617; CC -!- INDUCTION: By p53/TP53 following DNA damage: expression is directly CC activated by p53/TP53 (at protein level). {ECO:0000269|PubMed:18202719, CC ECO:0000269|PubMed:22802528, ECO:0000269|PubMed:22802529}. CC -!- DOMAIN: In contrast to classical members of the E2F transcription CC factor, atypical members contain 2 DNA-binding domains and regulate CC transcription in a DP-independent manner. Both DNA-binding domains are CC required for DNA-binding and are proposed to form an intramolecular CC structure that is similar to the winged helix structure of the E2F-DP CC heterodimer (PubMed:14633988). {ECO:0000269|PubMed:14633988}. CC -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAG53257.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAG53510.1; Type=Frameshift; Evidence={ECO:0000305}; 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; AC025161; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC079030; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC016658; AAH16658.1; -; mRNA. DR EMBL; BC136366; AAI36367.1; -; mRNA. DR EMBL; BC136367; AAI36368.1; -; mRNA. DR EMBL; BC017481; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK097677; BAG53510.1; ALT_FRAME; mRNA. DR EMBL; AK096316; BAG53257.1; ALT_INIT; mRNA. DR CCDS; CCDS9016.1; -. [Q96AV8-1] DR RefSeq; NP_976328.2; NM_203394.3. [Q96AV8-1] DR AlphaFoldDB; Q96AV8; -. DR SMR; Q96AV8; -. DR BioGRID; 126855; 47. DR FunCoup; Q96AV8; 1752. DR IntAct; Q96AV8; 22. DR NDEx; IQUERY-CP-E2F7; 3 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000323246; -. DR ChEMBL; CHEMBL4630726; -. DR GlyCosmos; Q96AV8; 3 sites, 1 glycan. DR GlyGen; Q96AV8; 3 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q96AV8; -. DR PhosphoSitePlus; Q96AV8; -. DR BioMuta; E2F7; -. DR DMDM; 311033456; -. DR jPOST; Q96AV8; -. DR MassIVE; Q96AV8; -. DR PaxDb; 9606-ENSP00000323246; -. DR PeptideAtlas; Q96AV8; -. DR ProteomicsDB; 3696; -. DR ProteomicsDB; 75999; -. [Q96AV8-1] DR ProteomicsDB; 76000; -. [Q96AV8-2] DR Pumba; Q96AV8; -. DR Antibodypedia; 29706; 182 antibodies from 33 providers. DR DNASU; 144455; -. DR Ensembl; ENST00000322886.12; ENSP00000323246.7; ENSG00000165891.17. [Q96AV8-1] DR Ensembl; ENST00000416496.6; ENSP00000393639.2; ENSG00000165891.17. [Q96AV8-2] DR GeneID; 144455; -. DR KEGG; hsa:144455; -. DR MANE-Select; ENST00000322886.12; ENSP00000323246.7; NM_203394.3; NP_976328.2. DR UCSC; uc001sym.5; human. [Q96AV8-1] DR AGR; HGNC:23820; -. DR CTD; 144455; -. DR DisGeNET; 144455; -. DR GeneCards; E2F7; -. DR HGNC; HGNC:23820; E2F7. DR HPA; ENSG00000165891; Tissue enhanced (bone marrow, lymphoid tissue). DR MIM; 612046; gene. DR OpenTargets; ENSG00000165891; -. DR VEuPathDB; HostDB:ENSG00000165891; -. DR eggNOG; KOG2578; Eukaryota. DR GeneTree; ENSGT00940000157713; -. DR InParanoid; Q96AV8; -. DR OMA; AANKECT; -. DR OrthoDB; 5318at2759; -. DR PAN-GO; Q96AV8; 4 GO annotations based on evolutionary models. DR PhylomeDB; Q96AV8; -. DR PathwayCommons; Q96AV8; -. DR Reactome; R-HSA-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest. DR Reactome; R-HSA-9938024; Somatic hypermutation of immunoglobulin genes. DR SignaLink; Q96AV8; -. DR SIGNOR; Q96AV8; -. DR Agora; ENSG00000165891; -. DR BioGRID-ORCS; 144455; 16 hits in 1187 CRISPR screens. DR ChiTaRS; E2F7; human. DR GeneWiki; E2F7; -. DR GenomeRNAi; 144455; -. DR Pharos; Q96AV8; Tbio. DR PRO; PR:Q96AV8; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q96AV8; protein. DR Bgee; ENSG00000165891; Expressed in ventricular zone and 117 other cell types or tissues. DR ExpressionAtlas; Q96AV8; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central. DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:UniProtKB. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB. DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IDA:UniProtKB. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0060718; P:chorionic trophoblast cell differentiation; ISS:UniProtKB. DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; IDA:UniProtKB. DR GO; GO:0070365; P:hepatocyte differentiation; ISS:UniProtKB. DR GO; GO:0032466; P:negative regulation of cytokinesis; ISS:UniProtKB. DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0001890; P:placenta development; ISS:UniProtKB. DR GO; GO:0032877; P:positive regulation of DNA endoreduplication; ISS:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0002040; P:sprouting angiogenesis; IMP:UniProtKB. DR GO; GO:0060707; P:trophoblast giant cell differentiation; ISS:UniProtKB. DR FunFam; 1.10.10.10:FF:000073; E2F transcription factor 8; 1. DR FunFam; 1.10.10.10:FF:000100; E2F transcription factor 8; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2. DR InterPro; IPR015633; E2F. DR InterPro; IPR003316; E2F_WHTH_DNA-bd_dom. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR12081; TRANSCRIPTION FACTOR E2F; 1. DR PANTHER; PTHR12081:SF25; TRANSCRIPTION FACTOR E2F7; 1. DR Pfam; PF02319; WHD_E2F_TDP; 2. DR SMART; SM01372; E2F_TDP; 2. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 2. PE 1: Evidence at protein level; KW Activator; Alternative splicing; Cell cycle; DNA damage; DNA-binding; KW Nucleus; Phosphoprotein; Proteomics identification; Reference proteome; KW Repressor; Transcription; Transcription regulation. FT CHAIN 1..911 FT /note="Transcription factor E2F7" FT /id="PRO_0000298907" FT DNA_BIND 142..211 FT /evidence="ECO:0000255" FT DNA_BIND 282..367 FT /evidence="ECO:0000255" FT REGION 254..283 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 418..438 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 563..645 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 672..701 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 860..911 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 595..618 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 672..685 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 686..699 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 95 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 410 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 840 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 714..845 FT /note="GLNGFNVLLSGSQTPPTVGPSSGQLPSFSVPCMVLPSPPLGPFPVLYSPAMP FT GPVSSTLGALPNTGPVNFSLPGLGSIAQLLVGPTAVVNPKSSTLPSADPQLQSQPSLNL FT SPVMSRSHSVVQQPESPVYVG -> VTSSSDPQEHPTHTS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_027473" FT VAR_SEQ 772..787 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044617" FT VAR_SEQ 846..911 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_027474" FT VARIANT 72 FT /note="F -> L (in dbSNP:rs310791)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334" FT /id="VAR_034732" FT VARIANT 626 FT /note="M -> V (in dbSNP:rs3829295)" FT /id="VAR_034733" FT VARIANT 854 FT /note="H -> Q (in dbSNP:rs310831)" FT /id="VAR_034734" FT MUTAGEN 147..148 FT /note="LG->EE: Loss of DNA-binding and E2F-dependent FT repression." FT /evidence="ECO:0000269|PubMed:14633988" FT MUTAGEN 185 FT /note="R->A: Loss of DNA-binding and inhibition of FT E2F1-dependent activation. Impairs DNA-binding and FT dimerization; when associated with A-334." FT /evidence="ECO:0000269|PubMed:15133492, FT ECO:0000269|PubMed:18202719" FT MUTAGEN 334 FT /note="R->A: Loss of DNA-binding and inhibition of FT E2F1-dependent activation. Impairs DNA-binding and FT dimerization; when associated with A-185." FT /evidence="ECO:0000269|PubMed:15133492, FT ECO:0000269|PubMed:18202719" SQ SEQUENCE 911 AA; 99888 MW; 748FEC8F24EAC5D8 CRC64; MEVNCLTLKD LISPRQPRLD FAVEDGENAQ KENIFVDRSR MAPKTPIKNE PIDLSKQKKF TPERNPITPV KFVDRQQAEP WTPTANLKML ISAASPDIRD REKKKGLFRP IENKDDAFTD SLQLDVVGDS AVDEFEKQRP SRKQKSLGLL CQKFLARYPS YPLSTEKTTI SLDEVAVSLG VERRRIYDIV NVLESLHLVS RVAKNQYGWH GRHSLPKTLR NLQRLGEEQK YEEQMAYLQQ KELDLIDYKF GERKKDGDPD SQEQQLLDFS EPDCPSSSAN SRKDKSLRIM SQKFVMLFLV SKTKIVTLDV AAKILIEESQ DAPDHSKFKT KVRRLYDIAN VLTSLALIKK VHVTEERGRK PAFKWIGPVD FSSSDEELVD VSASVLPELK RETYGQIQVC AKQKLARHGS FNTVQASERI QRKVNSEPSS PYREEQGSGG YSLEIGSLAA VYRQKIEDNS QGKAFASKRV VPPSSSLDPV APFPVLSVDP EYCVNPLAHP VFSVAQTDLQ AFSMQNGLNG QVDVSLASAA SAVESLKPAL LAGQPLVYVP SASLFMLYGS LQEGPASGSG SERDDRSSEA PATVELSSAP SAQKRLCEER KPQEEDEPAT KRQSREYEDG PLSLVMPKKP SDSTDLASPK TMGNRASIPL KDIHVNGQLP AAEEISGKAT ANSLVSSEWG NPSRNTDVEK PSKENESTKE PSLLQYLCVQ SPAGLNGFNV LLSGSQTPPT VGPSSGQLPS FSVPCMVLPS PPLGPFPVLY SPAMPGPVSS TLGALPNTGP VNFSLPGLGS IAQLLVGPTA VVNPKSSTLP SADPQLQSQP SLNLSPVMSR SHSVVQQPES PVYVGHPVSV VKLHQSPVPV TPKSIQRTHR ETFFKTPGSL GDPVLKRRER NQSRNTSSAQ RRLEIPSGGA D //