E2F7_HUMAN
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 03-AUG-2022, entry version 149.
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};
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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_203394.2. [Q96AV8-1]
DR AlphaFoldDB; Q96AV8; -.
DR SMR; Q96AV8; -.
DR BioGRID; 126855; 30.
DR IntAct; Q96AV8; 8.
DR MINT; Q96AV8; -.
DR STRING; 9606.ENSP00000323246; -.
DR ChEMBL; CHEMBL4630726; -.
DR iPTMnet; Q96AV8; -.
DR PhosphoSitePlus; Q96AV8; -.
DR BioMuta; E2F7; -.
DR DMDM; 311033456; -.
DR EPD; Q96AV8; -.
DR jPOST; Q96AV8; -.
DR MassIVE; Q96AV8; -.
DR MaxQB; Q96AV8; -.
DR PaxDb; Q96AV8; -.
DR PeptideAtlas; Q96AV8; -.
DR PRIDE; Q96AV8; -.
DR ProteomicsDB; 3696; -.
DR ProteomicsDB; 75999; -. [Q96AV8-1]
DR ProteomicsDB; 76000; -. [Q96AV8-2]
DR Antibodypedia; 29706; 181 antibodies from 32 providers.
DR DNASU; 144455; -.
DR Ensembl; ENST00000322886.12; ENSP00000323246.7; ENSG00000165891.16. [Q96AV8-1]
DR Ensembl; ENST00000416496.6; ENSP00000393639.2; ENSG00000165891.16. [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 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 neXtProt; NX_Q96AV8; -.
DR OpenTargets; ENSG00000165891; -.
DR VEuPathDB; HostDB:ENSG00000165891; -.
DR eggNOG; KOG2578; Eukaryota.
DR GeneTree; ENSGT00940000157713; -.
DR InParanoid; Q96AV8; -.
DR OMA; EPDCTSA; -.
DR OrthoDB; 145070at2759; -.
DR PhylomeDB; Q96AV8; -.
DR TreeFam; TF105567; -.
DR PathwayCommons; Q96AV8; -.
DR Reactome; R-HSA-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
DR SignaLink; Q96AV8; -.
DR BioGRID-ORCS; 144455; 14 hits in 1109 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 116 other tissues.
DR ExpressionAtlas; Q96AV8; baseline and differential.
DR Genevisible; Q96AV8; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
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; IDA: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; ISS: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:0008285; P:negative regulation of cell population proliferation; IMP: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:0071930; P:negative regulation of transcription involved in G1/S transition of mitotic cell cycle; 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 Gene3D; 1.10.10.10; -; 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; PTHR12081; 1.
DR Pfam; PF02319; E2F_TDP; 2.
DR SMART; SM01372; E2F_TDP; 2.
DR SUPFAM; SSF46785; SSF46785; 2.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Cell cycle; DNA damage; DNA-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW 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 263..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..686
FT /note="Polar 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 E2F1-
FT dependent activation. Impairs DNA-binding and dimerization;
FT 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 E2F1-
FT dependent activation. Impairs DNA-binding and dimerization;
FT 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
