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Transcription factor E2F5 (E2F-5)

 E2F5_HUMAN              Reviewed;         346 AA.
Q15329; E9PBN9; Q16601; Q92756;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 165.
RecName: Full=Transcription factor E2F5;
Short=E2F-5;
Name=E2F5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Fetal lung, and Placenta;
PubMed=8589754;
Itoh A., Levinson S.F., Morita T., Kourembanas S., Brody J.S.,
Mitsialis S.A.;
"Structural characterization and specificity of expression of E2F-5: a
new member of the E2F family of transcription factors.";
Cell. Mol. Biol. Res. 41:147-154(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH RBL2.
TISSUE=Colon carcinoma;
PubMed=7760804; DOI=10.1128/MCB.15.6.3082;
Hijmans E.M., Voorhoeve P.M., Beijersbergen R.L., van 't Veer L.J.,
Bernards R.;
"E2F-5, a new E2F family member that interacts with p130 in vivo.";
Mol. Cell. Biol. 15:3082-3089(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=7892279; DOI=10.1073/pnas.92.6.2403;
Sardet C., Vidal M., Cobrinik D., Geng Y., Onufryk C., Chen A.,
Weinberg R.A.;
"E2F-4 and E2F-5, two members of the E2F family, are expressed in the
early phases of the cell cycle.";
Proc. Natl. Acad. Sci. U.S.A. 92:2403-2407(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9464260; DOI=10.1006/bbrc.1997.8010;
Vaishnav Y.N., Vaishnav M.Y., Pant V.;
"The molecular and functional characterization of E2F-5 transcription
factor.";
Biochem. Biophys. Res. Commun. 242:586-592(1998).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-18.
NIEHS SNPs program;
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=B-cell;
Li W.B., Gruber C., Jessee J., Polayes D.;
"Full-length cDNA libraries and normalization.";
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[8]
INTERACTION WITH WITH RB1 AND TFDP1.
PubMed=16360038; DOI=10.1016/j.cell.2005.09.044;
Rubin S.M., Gall A.-L., Zheng N., Pavletich N.P.;
"Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism
for phosphorylation-induced E2F release.";
Cell 123:1093-1106(2005).
[9]
IDENTIFICATION IN THE DREAM COMPLEX.
PubMed=17531812; DOI=10.1016/j.molcel.2007.04.015;
Litovchick L., Sadasivam S., Florens L., Zhu X., Swanson S.K.,
Velmurugan S., Chen R., Washburn M.P., Liu X.S., DeCaprio J.A.;
"Evolutionarily conserved multisubunit RBL2/p130 and E2F4 protein
complex represses human cell cycle-dependent genes in quiescence.";
Mol. Cell 26:539-551(2007).
-!- FUNCTION: Transcriptional activator that binds to E2F sites, these
sites are present in the promoter of many genes whose products are
involved in cell proliferation. May mediate growth factor-
initiated signal transduction. It is likely involved in the early
responses of resting cells to growth factor stimulation.
Specifically required for multiciliate cell differentiation:
together with MCIDAS and E2F5, binds and activate genes required
for centriole biogenesis. {ECO:0000250|UniProtKB:Q6DE14}.
-!- SUBUNIT: Component of the DRTF1/E2F transcription factor complex.
Binds cooperatively with DP-1 to E2F sites. Interaction with
retinoblastoma protein RB1 or proteins RBL1 and RBL2 inhibits the
E2F transactivation domain. Component of the DREAM complex (also
named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37,
LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2.
The complex exists in quiescent cells where it represses cell
cycle-dependent genes. It dissociates in S phase when LIN9, LIN37,
LIN52 and LIN54 form a subcomplex that binds to MYBL2.
{ECO:0000269|PubMed:16360038, ECO:0000269|PubMed:17531812,
ECO:0000269|PubMed:7760804}.
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q15329-1; Sequence=Displayed;
Name=2;
IsoId=Q15329-2; Sequence=VSP_040098;
Name=3;
IsoId=Q15329-3; Sequence=VSP_044660;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/e2f5/";
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EMBL; U31556; AAB00179.1; -; mRNA.
EMBL; X86097; CAA60051.1; -; mRNA.
EMBL; U15642; AAC50120.1; -; mRNA.
EMBL; Z78409; CAB01634.1; -; mRNA.
EMBL; AY162833; AAN46737.1; -; Genomic_DNA.
EMBL; AL583354; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC011773; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS47885.1; -. [Q15329-1]
CCDS; CCDS47886.1; -. [Q15329-2]
CCDS; CCDS55254.1; -. [Q15329-3]
PIR; JC5833; JC5833.
RefSeq; NP_001077057.1; NM_001083588.1. [Q15329-2]
RefSeq; NP_001077058.1; NM_001083589.1. [Q15329-3]
RefSeq; NP_001942.2; NM_001951.3. [Q15329-1]
UniGene; Hs.445758; -.
PDB; 5TUV; X-ray; 2.90 A; B/E=124-232.
PDBsum; 5TUV; -.
ProteinModelPortal; Q15329; -.
SMR; Q15329; -.
BioGrid; 108207; 10.
CORUM; Q15329; -.
DIP; DIP-24229N; -.
IntAct; Q15329; 8.
STRING; 9606.ENSP00000398124; -.
iPTMnet; Q15329; -.
PhosphoSitePlus; Q15329; -.
BioMuta; E2F5; -.
DMDM; 2494230; -.
MaxQB; Q15329; -.
PaxDb; Q15329; -.
PeptideAtlas; Q15329; -.
PRIDE; Q15329; -.
DNASU; 1875; -.
Ensembl; ENST00000416274; ENSP00000398124; ENSG00000133740. [Q15329-1]
Ensembl; ENST00000418930; ENSP00000414312; ENSG00000133740. [Q15329-2]
Ensembl; ENST00000517476; ENSP00000429120; ENSG00000133740. [Q15329-3]
GeneID; 1875; -.
KEGG; hsa:1875; -.
UCSC; uc003ycz.6; human. [Q15329-1]
CTD; 1875; -.
DisGeNET; 1875; -.
EuPathDB; HostDB:ENSG00000133740.10; -.
GeneCards; E2F5; -.
HGNC; HGNC:3119; E2F5.
HPA; HPA055723; -.
MIM; 600967; gene.
neXtProt; NX_Q15329; -.
OpenTargets; ENSG00000133740; -.
PharmGKB; PA27577; -.
eggNOG; KOG2577; Eukaryota.
eggNOG; ENOG410XNYI; LUCA.
GeneTree; ENSGT00550000074403; -.
HOGENOM; HOG000232045; -.
HOVERGEN; HBG002227; -.
InParanoid; Q15329; -.
KO; K04682; -.
OMA; INNRYPF; -.
OrthoDB; EOG091G0CJQ; -.
PhylomeDB; Q15329; -.
TreeFam; TF105566; -.
Reactome; R-HSA-1362277; Transcription of E2F targets under negative control by DREAM complex.
Reactome; R-HSA-1362300; Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1.
Reactome; R-HSA-1538133; G0 and Early G1.
Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
Reactome; R-HSA-539107; Activation of E2F1 target genes at G1/S.
Reactome; R-HSA-69202; Cyclin E associated events during G1/S transition.
Reactome; R-HSA-69231; Cyclin D associated events in G1.
Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry.
SignaLink; Q15329; -.
ChiTaRS; E2F5; human.
GeneWiki; E2F5; -.
GenomeRNAi; 1875; -.
PRO; PR:Q15329; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000133740; -.
CleanEx; HS_E2F5; -.
ExpressionAtlas; Q15329; baseline and differential.
Genevisible; Q15329; HS.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0001650; C:fibrillar center; IDA:HPA.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005667; C:transcription factor complex; IEA:InterPro.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; NAS:ProtInc.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0009887; P:animal organ morphogenesis; IEA:Ensembl.
GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd14660; E2F_DD; 1.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR015633; E2F.
InterPro; IPR037241; E2F-DP_heterodim.
InterPro; IPR028316; E2F5.
InterPro; IPR032198; E2F_CC-MB.
InterPro; IPR003316; E2F_WHTH_DNA-bd_dom.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
PANTHER; PTHR12081; PTHR12081; 2.
PANTHER; PTHR12081:SF35; PTHR12081:SF35; 2.
Pfam; PF16421; E2F_CC-MB; 1.
Pfam; PF02319; E2F_TDP; 1.
SMART; SM01372; E2F_TDP; 1.
SUPFAM; SSF144074; SSF144074; 1.
SUPFAM; SSF46785; SSF46785; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing;
Cilium biogenesis/degradation; Complete proteome; DNA-binding;
Nucleus; Polymorphism; Reference proteome; Transcription;
Transcription regulation.
CHAIN 1 346 Transcription factor E2F5.
/FTId=PRO_0000219469.
DNA_BIND 47 118 {ECO:0000255}.
REGION 76 98 Leucine-zipper.
REGION 119 215 Dimerization. {ECO:0000255}.
REGION 287 346 Transactivation. {ECO:0000255}.
REGION 323 340 RBL2 association. {ECO:0000255}.
MOTIF 81 118 DEF box.
COMPBIAS 33 39 Poly-Pro.
COMPBIAS 233 236 Poly-Ser.
VAR_SEQ 1 161 Missing (in isoform 3).
{ECO:0000303|Ref.6}.
/FTId=VSP_044660.
VAR_SEQ 295 295 Missing (in isoform 2).
{ECO:0000303|PubMed:7892279,
ECO:0000303|PubMed:8589754}.
/FTId=VSP_040098.
VARIANT 18 18 G -> A (in dbSNP:rs4150841).
{ECO:0000269|Ref.5}.
/FTId=VAR_014348.
CONFLICT 153 153 W -> L (in Ref. 4; CAB01634).
{ECO:0000305}.
HELIX 127 162 {ECO:0000244|PDB:5TUV}.
HELIX 165 169 {ECO:0000244|PDB:5TUV}.
HELIX 175 181 {ECO:0000244|PDB:5TUV}.
STRAND 184 191 {ECO:0000244|PDB:5TUV}.
STRAND 197 201 {ECO:0000244|PDB:5TUV}.
STRAND 213 218 {ECO:0000244|PDB:5TUV}.
STRAND 220 222 {ECO:0000244|PDB:5TUV}.
STRAND 224 229 {ECO:0000244|PDB:5TUV}.
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


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