E2F3_HUMAN
ID E2F3_HUMAN Reviewed; 465 AA.
AC O00716; Q15000; Q68DT0; Q9BZ44;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Transcription factor E2F3;
DE Short=E2F-3;
GN Name=E2F3; Synonyms=KIAA0075;
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 1).
RC TISSUE=Pre-B cell;
RX PubMed=8246996; DOI=10.1128/mcb.13.12.7813-7825.1993;
RA Lees J.A., Saito M., Vidal M., Valentine M., Look T., Harlow E., Dyson N.,
RA Helin K.;
RT "The retinoblastoma protein binds to a family of E2F transcription
RT factors.";
RL Mol. Cell. Biol. 13:7813-7825(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-344 AND ASN-389.
RG NIEHS SNPs program;
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Rectum tumor;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 292-465 (ISOFORM 1/2).
RC TISSUE=Bone marrow;
RX PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N.,
RA Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II. The
RT coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [6]
RP INTERACTION WITH EAPP.
RX PubMed=15716352; DOI=10.1091/mbc.e04-11-0975;
RA Novy M., Pohn R., Andorfer P., Novy-Weiland T., Galos B., Schwarzmayr L.,
RA Rotheneder H.;
RT "EAPP, a novel E2F binding protein that modulates E2F-dependent
RT transcription.";
RL Mol. Biol. Cell 16:2181-2190(2005).
CC -!- FUNCTION: Transcription activator that binds DNA cooperatively with DP
CC proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in
CC the promoter region of a number of genes whose products are involved in
CC cell cycle regulation or in DNA replication. The DRTF1/E2F complex
CC functions in the control of cell-cycle progression from G1 to S phase.
CC E2F3 binds specifically to RB1 in a cell-cycle dependent manner.
CC Inhibits adipogenesis, probably through the repression of CEBPA binding
CC to its target gene promoters (By similarity).
CC {ECO:0000250|UniProtKB:O35261}.
CC -!- SUBUNIT: Component of the DRTF1/E2F transcription factor complex. Binds
CC cooperatively with TFDP1/Dp-1 to E2F sites. Interacts with
CC retinoblastoma protein RB1 and related proteins (such as RBL1) that
CC inhibit the E2F transactivation domain. Binds EAPP.
CC {ECO:0000269|PubMed:15716352}.
CC -!- INTERACTION:
CC O00716; Q9NRZ9: HELLS; NbExp=2; IntAct=EBI-765551, EBI-1056215;
CC O00716; Q96JM7: L3MBTL3; NbExp=3; IntAct=EBI-765551, EBI-2686809;
CC O00716; P06400: RB1; NbExp=4; IntAct=EBI-765551, EBI-491274;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O00716-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00716-2; Sequence=VSP_045066, VSP_045067, VSP_045068;
CC -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/E2F3ID40384ch6p22.html";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/e2f3/";
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DR EMBL; Y10479; CAA71504.1; -; mRNA.
DR EMBL; AF547386; AAN17846.1; -; Genomic_DNA.
DR EMBL; CR749285; CAH18140.1; -; mRNA.
DR EMBL; AL132775; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136303; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; D38550; BAA07553.1; -; mRNA.
DR CCDS; CCDS4545.1; -. [O00716-1]
DR CCDS; CCDS58999.1; -. [O00716-2]
DR RefSeq; NP_001230005.1; NM_001243076.2. [O00716-2]
DR RefSeq; NP_001940.1; NM_001949.4. [O00716-1]
DR AlphaFoldDB; O00716; -.
DR SMR; O00716; -.
DR BioGRID; 108203; 53.
DR DIP; DIP-24230N; -.
DR ELM; O00716; -.
DR IntAct; O00716; 136.
DR MINT; O00716; -.
DR STRING; 9606.ENSP00000262904; -.
DR ChEMBL; CHEMBL4630726; -.
DR iPTMnet; O00716; -.
DR PhosphoSitePlus; O00716; -.
DR BioMuta; E2F3; -.
DR EPD; O00716; -.
DR jPOST; O00716; -.
DR MassIVE; O00716; -.
DR MaxQB; O00716; -.
DR PaxDb; O00716; -.
DR PeptideAtlas; O00716; -.
DR PRIDE; O00716; -.
DR ProteomicsDB; 48008; -. [O00716-1]
DR ProteomicsDB; 66100; -.
DR Antibodypedia; 10438; 349 antibodies from 36 providers.
DR DNASU; 1871; -.
DR Ensembl; ENST00000346618.8; ENSP00000262904.4; ENSG00000112242.16. [O00716-1]
DR Ensembl; ENST00000535432.2; ENSP00000443418.1; ENSG00000112242.16. [O00716-2]
DR GeneID; 1871; -.
DR KEGG; hsa:1871; -.
DR MANE-Select; ENST00000346618.8; ENSP00000262904.4; NM_001949.5; NP_001940.1.
DR UCSC; uc003nda.3; human. [O00716-1]
DR CTD; 1871; -.
DR DisGeNET; 1871; -.
DR GeneCards; E2F3; -.
DR HGNC; HGNC:3115; E2F3.
DR HPA; ENSG00000112242; Low tissue specificity.
DR MIM; 600427; gene.
DR neXtProt; NX_O00716; -.
DR OpenTargets; ENSG00000112242; -.
DR PharmGKB; PA27573; -.
DR VEuPathDB; HostDB:ENSG00000112242; -.
DR eggNOG; KOG2577; Eukaryota.
DR GeneTree; ENSGT00940000155115; -.
DR HOGENOM; CLU_032091_0_0_1; -.
DR InParanoid; O00716; -.
DR OMA; WMGCNLS; -.
DR OrthoDB; 1087250at2759; -.
DR PhylomeDB; O00716; -.
DR TreeFam; TF105566; -.
DR PathwayCommons; O00716; -.
DR Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
DR Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-HSA-2559585; Oncogene Induced Senescence.
DR Reactome; R-HSA-68911; G2 Phase.
DR Reactome; R-HSA-69231; Cyclin D associated events in G1.
DR Reactome; R-HSA-9661069; Defective binding of RB1 mutants to E2F1,(E2F2, E2F3).
DR SignaLink; O00716; -.
DR SIGNOR; O00716; -.
DR BioGRID-ORCS; 1871; 169 hits in 1106 CRISPR screens.
DR ChiTaRS; E2F3; human.
DR GeneWiki; E2F3; -.
DR GenomeRNAi; 1871; -.
DR Pharos; O00716; Tbio.
DR PRO; PR:O00716; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O00716; protein.
DR Bgee; ENSG00000112242; Expressed in buccal mucosa cell and 188 other tissues.
DR ExpressionAtlas; O00716; baseline and differential.
DR Genevisible; O00716; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:NTNU_SB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS: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:0043565; F:sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0070345; P:negative regulation of fat cell proliferation; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:1905461; P:positive regulation of vascular associated smooth muscle cell apoptotic process; IMP:BHF-UCL.
DR GO; GO:0006606; P:protein import into nucleus; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:ProtInc.
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; 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; 1.
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 Activator; Alternative splicing; Cell cycle; DNA-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..465
FT /note="Transcription factor E2F3"
FT /id="PRO_0000219466"
FT DNA_BIND 155..245
FT /evidence="ECO:0000255"
FT REGION 96..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..153
FT /note="Cyclin A/CDK2 binding"
FT /evidence="ECO:0000255"
FT REGION 204..225
FT /note="Leucine-zipper"
FT REGION 246..337
FT /note="Dimerization"
FT /evidence="ECO:0000255"
FT REGION 357..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..465
FT /note="Transactivation"
FT /evidence="ECO:0000255"
FT REGION 432..449
FT /note="Retinoblastoma protein binding"
FT /evidence="ECO:0000255"
FT MOTIF 209..245
FT /note="DEF box"
FT VAR_SEQ 1..6
FT /note="MRKGIQ -> MPLQQQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_045066"
FT VAR_SEQ 7..131
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_045067"
FT VAR_SEQ 169..175
FT /note="TPKSPSE -> K (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_045068"
FT VARIANT 344
FT /note="G -> R (in dbSNP:rs4134973)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_014341"
FT VARIANT 389
FT /note="D -> N (in dbSNP:rs4134982)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_014342"
SQ SEQUENCE 465 AA; 49162 MW; 4641565842CA99EC CRC64;
MRKGIQPALE QYLVTAGGGE GAAVVAAAAA ASMDKRALLA SPGFAAAAAA AAAPGAYIQI
LTTNTSTTSC SSSLQSGAVA AGPLLPSAPG AEQTAGSLLY TTPHGPSSRA GLLQQPPALG
RGGSGGGGGP PAKRRLELGE SGHQYLSDGL KTPKGKGRAA LRSPDSPKTP KSPSEKTRYD
TSLGLLTKKF IQLLSQSPDG VLDLNKAAEV LKVQKRRIYD ITNVLEGIHL IKKKSKNNVQ
WMGCSLSEDG GMLAQCQGLS KEVTELSQEE KKLDELIQSC TLDLKLLTED SENQRLAYVT
YQDIRKISGL KDQTVIVVKA PPETRLEVPD SIESLQIHLA STQGPIEVYL CPEETETHSP
MKTNNQDHNG NIPKPASKDL ASTNSGHSDC SVSMGNLSPL ASPANLLQQT EDQIPSNLEG
PFVNLLPPLL QEDYLLSLGE EEGISDLFDA YDLEKLPLVE DFMCS
