O00716 (E2F3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription factor E2F3
Short name=E2F-3

Gene names

Name:	E2F3
Synonyms:	KIAA0075

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	465 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F-3 binds specifically to RB1 protein, in a cell-cycle dependent manner.
Subunit structure	Component of the DRTF1/E2F transcription factor complex. Binds cooperatively with DP-1 to E2F sites. Interacts with retinoblastoma protein RB1 and related proteins (such as RBL1) that inhibit the E2F transactivation domain. Binds EAPP. Ref.5
Subcellular location	Nucleus.
Sequence similarities	Belongs to the E2F/DP family.

Ontologies

Keywords
Biological process	Cell cycle Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Ligand	DNA-binding
Molecular function	Activator
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	G1 phase of mitotic cell cycle Traceable author statement. Source: Reactome G2 phase of mitotic cell cycle Traceable author statement. Source: Reactome transcription initiation from RNA polymerase II promoter Traceable author statement. Source: ProtInc
Cellular component	transcription factor complex Inferred from electronic annotation. Source: InterPro
Molecular function	core promoter binding Inferred from direct assay. Source: UniProtKB cyclin-dependent protein kinase activity Traceable author statement. Source: Reactome protein binding Inferred from physical interaction. Source: UniProtKB sequence-specific DNA binding transcription factor activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 465	465	Transcription factor E2F3		PRO_0000219466
Regions
	Domain	204 – 225	22	Leucine-zipper
	DNA binding	155 – 245	91	Potential
	Region	101 – 153	53	Cyclin A/CDK2 binding Potential
	Region	246 – 337	92	Dimerization Potential
	Region	391 – 465	75	Transactivation Potential
	Region	432 – 449	18	Retinoblastoma protein binding Potential
	Motif	209 – 245	37	DEF box
	Compositional bias	26 – 31	6	Poly-Ala
	Compositional bias	45 – 53	9	Poly-Ala
	Compositional bias	120 – 129	10	Poly-Gly
Natural variations
	Natural variant	344	1	G → R. Ref.2 Corresponds to variant rs4134973 [ dbSNP | Ensembl ].		VAR_014341
	Natural variant	389	1	D → N. Ref.2 Corresponds to variant rs4134982 [ dbSNP | Ensembl ].		VAR_014342

Sequences

	Sequence		Length	Mass (Da)
	O00716 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 4641565842CA99EC	FASTA	465	49,162
	10 20 30 40 50 60 MRKGIQPALE QYLVTAGGGE GAAVVAAAAA ASMDKRALLA SPGFAAAAAA AAAPGAYIQI 70 80 90 100 110 120 LTTNTSTTSC SSSLQSGAVA AGPLLPSAPG AEQTAGSLLY TTPHGPSSRA GLLQQPPALG 130 140 150 160 170 180 RGGSGGGGGP PAKRRLELGE SGHQYLSDGL KTPKGKGRAA LRSPDSPKTP KSPSEKTRYD 190 200 210 220 230 240 TSLGLLTKKF IQLLSQSPDG VLDLNKAAEV LKVQKRRIYD ITNVLEGIHL IKKKSKNNVQ 250 260 270 280 290 300 WMGCSLSEDG GMLAQCQGLS KEVTELSQEE KKLDELIQSC TLDLKLLTED SENQRLAYVT 310 320 330 340 350 360 YQDIRKISGL KDQTVIVVKA PPETRLEVPD SIESLQIHLA STQGPIEVYL CPEETETHSP 370 380 390 400 410 420 MKTNNQDHNG NIPKPASKDL ASTNSGHSDC SVSMGNLSPL ASPANLLQQT EDQIPSNLEG 430 440 450 460 PFVNLLPPLL QEDYLLSLGE EEGISDLFDA YDLEKLPLVE DFMCS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The retinoblastoma protein binds to a family of E2F transcription factors." Lees J.A., Saito M., Vidal M., Valentine M., Look T., Harlow E., Dyson N., Helin K. Mol. Cell. Biol. 13:7813-7825(1993) [PubMed: 8246996] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Pre-B cell.
[2]	NIEHS SNPs program Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-344 AND ASN-389.
[3]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1." Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S. DNA Res. 1:223-229(1994) [PubMed: 7584044] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 292-465. Tissue: Bone marrow.
[5]	"EAPP, a novel E2F binding protein that modulates E2F-dependent transcription." Novy M., Pohn R., Andorfer P., Novy-Weiland T., Galos B., Schwarzmayr L., Rotheneder H. Mol. Biol. Cell 16:2181-2190(2005) [PubMed: 15716352] [Abstract] Cited for: INTERACTION WITH EAPP.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y10479 mRNA. Translation: CAA71504.1. AF547386 Genomic DNA. Translation: AAN17846.1. AL132775, AL136303 Genomic DNA. Translation: CAI21471.1. AL136303 Genomic DNA. Translation: CAC28598.2. D38550 mRNA. Translation: BAA07553.1.
IPI	IPI00743509.
RefSeq	NP_001940.1. NM_001949.4.
UniGene	Hs.269408. Hs.703174.
3D structure databases
ProteinModelPortal	O00716.
SMR	O00716. Positions 177-241, 255-354.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-24230N.
IntAct	O00716. 4 interactions.
MINT	MINT-249699.
STRING	O00716.
PTM databases
PhosphoSite	O00716.
Proteomic databases
PRIDE	O00716.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000346618; ENSP00000262904; ENSG00000112242.
GeneID	1871.
KEGG	hsa:1871.
UCSC	uc003nda.2. human.
Organism-specific databases
CTD	1871.
GeneCards	GC06P020402.
H-InvDB	HIX0005612.
HGNC	HGNC:3115. E2F3.
MIM	600427. gene.
neXtProt	NX_O00716.
PharmGKB	PA27573.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG15153.
HOGENOM	HBG715983.
HOVERGEN	HBG002227.
InParanoid	O00716.
OMA	QILTTNT.
OrthoDB	EOG4CZBG6.
PhylomeDB	O00716.
Enzyme and pathway databases
Reactome	REACT_152. Cell Cycle, Mitotic.
Gene expression databases
ArrayExpress	O00716.
Bgee	O00716.
CleanEx	HS_E2F3.
Genevestigator	O00716.
GermOnline	ENSG00000112242. Homo sapiens.
Family and domain databases
InterPro	IPR015633. E2F. IPR003316. E2F_TDP. IPR011991. WHTH_trsnscrt_rep_DNA-bd. [Graphical view]
Gene3D	G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
KO	K06620.
PANTHER	PTHR12081. E2F. 1 hit.
Pfam	PF02319. E2F_TDP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	7651.
SOURCE	Search...

Entry information

Entry name

E2F3_HUMAN

Accession

Primary (citable) accession number: O00716
Secondary accession number(s): Q15000, Q9BZ44

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 1, 1997
Last modified:	December 14, 2011
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.