E2F5_HUMAN
ID E2F5_HUMAN Reviewed; 346 AA.
AC Q15329; E9PBN9; Q16601; Q92756;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Transcription factor E2F5;
DE Short=E2F-5;
GN Name=E2F5;
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 [MRNA] (ISOFORM 2).
RC TISSUE=Fetal lung, and Placenta;
RX PubMed=8589754;
RA Itoh A., Levinson S.F., Morita T., Kourembanas S., Brody J.S.,
RA Mitsialis S.A.;
RT "Structural characterization and specificity of expression of E2F-5: a new
RT member of the E2F family of transcription factors.";
RL Cell. Mol. Biol. Res. 41:147-154(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH RBL2.
RC TISSUE=Colon carcinoma;
RX PubMed=7760804; DOI=10.1128/mcb.15.6.3082;
RA Hijmans E.M., Voorhoeve P.M., Beijersbergen R.L., van 't Veer L.J.,
RA Bernards R.;
RT "E2F-5, a new E2F family member that interacts with p130 in vivo.";
RL Mol. Cell. Biol. 15:3082-3089(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=7892279; DOI=10.1073/pnas.92.6.2403;
RA Sardet C., Vidal M., Cobrinik D., Geng Y., Onufryk C., Chen A.,
RA Weinberg R.A.;
RT "E2F-4 and E2F-5, two members of the E2F family, are expressed in the early
RT phases of the cell cycle.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:2403-2407(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9464260; DOI=10.1006/bbrc.1997.8010;
RA Vaishnav Y.N., Vaishnav M.Y., Pant V.;
RT "The molecular and functional characterization of E2F-5 transcription
RT factor.";
RL Biochem. Biophys. Res. Commun. 242:586-592(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-18.
RG NIEHS SNPs program;
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=B-cell;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [8]
RP INTERACTION WITH RB1 AND TFDP1.
RX PubMed=16360038; DOI=10.1016/j.cell.2005.09.044;
RA Rubin S.M., Gall A.-L., Zheng N., Pavletich N.P.;
RT "Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism for
RT phosphorylation-induced E2F release.";
RL Cell 123:1093-1106(2005).
RN [9]
RP IDENTIFICATION IN THE DREAM COMPLEX.
RX PubMed=17531812; DOI=10.1016/j.molcel.2007.04.015;
RA Litovchick L., Sadasivam S., Florens L., Zhu X., Swanson S.K.,
RA Velmurugan S., Chen R., Washburn M.P., Liu X.S., DeCaprio J.A.;
RT "Evolutionarily conserved multisubunit RBL2/p130 and E2F4 protein complex
RT represses human cell cycle-dependent genes in quiescence.";
RL Mol. Cell 26:539-551(2007).
CC -!- FUNCTION: Transcriptional activator that binds to E2F sites, these
CC sites are present in the promoter of many genes whose products are
CC involved in cell proliferation. May mediate growth factor-initiated
CC signal transduction. It is likely involved in the early responses of
CC resting cells to growth factor stimulation. Specifically required for
CC multiciliate cell differentiation: together with MCIDAS and E2F5, binds
CC and activate genes required for centriole biogenesis.
CC {ECO:0000250|UniProtKB:Q6DE14}.
CC -!- SUBUNIT: Component of the DRTF1/E2F transcription factor complex. Binds
CC cooperatively with DP-1 to E2F sites. Interaction with retinoblastoma
CC protein RB1 or proteins RBL1 and RBL2 inhibits the E2F transactivation
CC domain. Component of the DREAM complex (also named LINC complex) at
CC least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2,
CC RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent
CC cells where it represses cell cycle-dependent genes. It dissociates in
CC S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds
CC to MYBL2. {ECO:0000269|PubMed:16360038, ECO:0000269|PubMed:17531812,
CC ECO:0000269|PubMed:7760804}.
CC -!- INTERACTION:
CC Q15329; P06400: RB1; NbExp=2; IntAct=EBI-1389773, EBI-491274;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q15329-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15329-2; Sequence=VSP_040098;
CC Name=3;
CC IsoId=Q15329-3; Sequence=VSP_044660;
CC -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/e2f5/";
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DR EMBL; U31556; AAB00179.1; -; mRNA.
DR EMBL; X86097; CAA60051.1; -; mRNA.
DR EMBL; U15642; AAC50120.1; -; mRNA.
DR EMBL; Z78409; CAB01634.1; -; mRNA.
DR EMBL; AY162833; AAN46737.1; -; Genomic_DNA.
DR EMBL; AL583354; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC011773; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS47885.1; -. [Q15329-1]
DR CCDS; CCDS47886.1; -. [Q15329-2]
DR CCDS; CCDS55254.1; -. [Q15329-3]
DR PIR; JC5833; JC5833.
DR RefSeq; NP_001077057.1; NM_001083588.1. [Q15329-2]
DR RefSeq; NP_001077058.1; NM_001083589.1. [Q15329-3]
DR RefSeq; NP_001942.2; NM_001951.3. [Q15329-1]
DR PDB; 5TUV; X-ray; 2.90 A; B/E=124-232.
DR PDBsum; 5TUV; -.
DR AlphaFoldDB; Q15329; -.
DR SMR; Q15329; -.
DR BioGRID; 108207; 24.
DR CORUM; Q15329; -.
DR DIP; DIP-24229N; -.
DR IntAct; Q15329; 11.
DR MINT; Q15329; -.
DR STRING; 9606.ENSP00000398124; -.
DR ChEMBL; CHEMBL4630726; -.
DR iPTMnet; Q15329; -.
DR PhosphoSitePlus; Q15329; -.
DR BioMuta; E2F5; -.
DR DMDM; 2494230; -.
DR EPD; Q15329; -.
DR jPOST; Q15329; -.
DR MassIVE; Q15329; -.
DR MaxQB; Q15329; -.
DR PaxDb; Q15329; -.
DR PeptideAtlas; Q15329; -.
DR PRIDE; Q15329; -.
DR ProteomicsDB; 19262; -.
DR ProteomicsDB; 60531; -. [Q15329-1]
DR ProteomicsDB; 60532; -. [Q15329-2]
DR Antibodypedia; 6582; 212 antibodies from 29 providers.
DR DNASU; 1875; -.
DR Ensembl; ENST00000416274.7; ENSP00000398124.2; ENSG00000133740.11. [Q15329-1]
DR Ensembl; ENST00000418930.6; ENSP00000414312.2; ENSG00000133740.11. [Q15329-2]
DR Ensembl; ENST00000517476.5; ENSP00000429120.1; ENSG00000133740.11. [Q15329-3]
DR GeneID; 1875; -.
DR KEGG; hsa:1875; -.
DR MANE-Select; ENST00000416274.7; ENSP00000398124.2; NM_001951.4; NP_001942.2.
DR UCSC; uc003ycz.6; human. [Q15329-1]
DR CTD; 1875; -.
DR DisGeNET; 1875; -.
DR GeneCards; E2F5; -.
DR HGNC; HGNC:3119; E2F5.
DR HPA; ENSG00000133740; Tissue enhanced (lymphoid).
DR MIM; 600967; gene.
DR neXtProt; NX_Q15329; -.
DR OpenTargets; ENSG00000133740; -.
DR PharmGKB; PA27577; -.
DR VEuPathDB; HostDB:ENSG00000133740; -.
DR eggNOG; KOG2577; Eukaryota.
DR GeneTree; ENSGT00940000157353; -.
DR HOGENOM; CLU_032091_2_0_1; -.
DR InParanoid; Q15329; -.
DR OMA; PQEDFNF; -.
DR OrthoDB; 1087250at2759; -.
DR PhylomeDB; Q15329; -.
DR TreeFam; TF105566; -.
DR PathwayCommons; Q15329; -.
DR Reactome; R-HSA-1362277; Transcription of E2F targets under negative control by DREAM complex.
DR Reactome; R-HSA-1362300; Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1.
DR Reactome; R-HSA-1538133; G0 and Early G1.
DR Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-HSA-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-HSA-69205; G1/S-Specific Transcription.
DR Reactome; R-HSA-69231; Cyclin D associated events in G1.
DR Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR SignaLink; Q15329; -.
DR SIGNOR; Q15329; -.
DR BioGRID-ORCS; 1875; 8 hits in 1101 CRISPR screens.
DR ChiTaRS; E2F5; human.
DR GeneWiki; E2F5; -.
DR GenomeRNAi; 1875; -.
DR Pharos; Q15329; Tbio.
DR PRO; PR:Q15329; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q15329; protein.
DR Bgee; ENSG00000133740; Expressed in ventricular zone and 117 other tissues.
DR ExpressionAtlas; Q15329; baseline and differential.
DR Genevisible; Q15329; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
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:0001216; F:DNA-binding transcription activator activity; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd14660; E2F_DD; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR015633; E2F.
DR InterPro; IPR037241; E2F-DP_heterodim.
DR InterPro; IPR028316; E2F5.
DR InterPro; IPR032198; E2F_CC-MB.
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; 2.
DR PANTHER; PTHR12081:SF35; PTHR12081:SF35; 2.
DR Pfam; PF16421; E2F_CC-MB; 1.
DR Pfam; PF02319; E2F_TDP; 1.
DR SMART; SM01372; E2F_TDP; 1.
DR SUPFAM; SSF144074; SSF144074; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing;
KW Cilium biogenesis/degradation; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..346
FT /note="Transcription factor E2F5"
FT /id="PRO_0000219469"
FT DNA_BIND 47..118
FT /evidence="ECO:0000255"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..98
FT /note="Leucine-zipper"
FT REGION 119..215
FT /note="Dimerization"
FT /evidence="ECO:0000255"
FT REGION 236..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..346
FT /note="Transactivation"
FT /evidence="ECO:0000255"
FT REGION 323..340
FT /note="RBL2 association"
FT /evidence="ECO:0000255"
FT MOTIF 81..118
FT /note="DEF box"
FT COMPBIAS 20..42
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..161
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_044660"
FT VAR_SEQ 295
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7892279,
FT ECO:0000303|PubMed:8589754"
FT /id="VSP_040098"
FT VARIANT 18
FT /note="G -> A (in dbSNP:rs4150841)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_014348"
FT CONFLICT 153
FT /note="W -> L (in Ref. 4; CAB01634)"
FT /evidence="ECO:0000305"
FT HELIX 127..162
FT /evidence="ECO:0007829|PDB:5TUV"
FT HELIX 165..169
FT /evidence="ECO:0007829|PDB:5TUV"
FT HELIX 175..181
FT /evidence="ECO:0007829|PDB:5TUV"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:5TUV"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:5TUV"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:5TUV"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:5TUV"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:5TUV"
SQ SEQUENCE 346 AA; 37610 MW; F1408A755E67D879 CRC64;
MAAAEPASSG QQAPAGQGQG QRPPPQPPQA QAPQPPPPPQ LGGAGGGSSR HEKSLGLLTT
KFVSLLQEAK DGVLDLKAAA DTLAVRQKRR IYDITNVLEG IDLIEKKSKN SIQWKGVGAG
CNTKEVIDRL RYLKAEIEDL ELKERELDQQ KLWLQQSIKN VMDDSINNRF SYVTHEDICN
CFNGDTLLAI QAPSGTQLEV PIPEMGQNGQ KKYQINLKSH SGPIHVLLIN KESSSSKPVV
FPVPPPDDLT QPSSQSLTPV TPQKSSMATQ NLPEQHVSER SQALQQTSAT DISSAGSISG
DIIDELMSSD VFPLLRLSPT PADDYNFNLD DNEGVCDLFD VQILNY
