Q61501 (E2F1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription factor E2F1
Short name=E2F-1

Gene names

Name:

E2f1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	430 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. E2F1 binds preferentially RB1 in a cell-cycle dependent manner. It can mediate both cell proliferation and TP53/p53-dependent apoptosis. Ref.4
Enzyme regulation	BIRC2/c-IAP1 stimulates its transcriptional activity By similarity.
Subunit structure	Component of the DRTF1/E2F transcription factor complex. Forms heterodimers with DP family members. The E2F1 complex binds specifically hypophosphorylated retinoblastoma protein RB1. During the cell cycle, RB1 becomes phosphorylated in mid-to-late G1 phase, detaches from the DRTF1/E2F complex, rendering E2F transcriptionally active. Interacts with TRRAP, which probably mediates its interaction with histone acetyltransferase complexes, leading to transcription activation. Binds TOPBP1. Interacts with ARID3A. Interacts with TRIM28; the interaction represses the transcriptional activity through recruiting HDAC1 which deacetylates E2F1. Interaction with KAT2B; the interaction acetylates E2F1 enhancing its DNA-binding and transcriptional activity By similarity. Binds EAPP. Interacts with BIRC2/c-IAP1 (via BIR domains) By similarity. Ref.5
Subcellular location	Nucleus.
Developmental stage	In the developing nervous system, first detected in the neural tube at day 9.5 dpc. By day 10.5, levels increase throughout the brain, with highest levels in the hindbrain and in the spinal cord, expressed only in the rostral half. By day 11.5, expression found throughout the brain and spinal cord. From day 12.5, expression restricted to the ventricular regions of the brain, peaks at day 13.5 and declines thereafter. Only weak expression in the developing spinal cord from day 11.5-16.5. In the developing retina, expression is confined to the undifferentiated retinoblastic cell layer. In other developing tissues, E2F1 is expressed in kidney, lung, liver hepatocytes, heart and thymus. Highest levels in liver. Absent in choroid plexus. Ref.3
Post-translational modification	Phosphorylated by CDK2 and cyclin A-CDK2 in the S-phase. Phosphorylation by CHEK2 stabilizes E2F1 upon DNA damage and regulates its effect on transcription and apoptosis By similarity. Acetylation stimulates DNA-binding. Enhanced under stress conditions such as DNA damage and inhibited by retinoblastoma protein RB1. Regulated by KAP1/TRIM28 which recruits HDAC1 to E2F1 resulting in deacetylation. Acetylated by P/CAF/KAT2B By similarity.
Sequence similarities	Belongs to the E2F/DP family.

Ontologies

Keywords
Biological process	Apoptosis Cell cycle Transcription Transcription regulation
Cellular component	Nucleus
Ligand	DNA-binding
Molecular function	Activator
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage checkpoint Inferred from sequence or structural similarity. Source: UniProtKB apoptotic process Inferred from direct assay PubMed 11095619PubMed 14667810. Source: MGI cellular response to fatty acid Inferred from electronic annotation. Source: Compara cellular response to hypoxia Inferred from electronic annotation. Source: Compara forebrain development Inferred from mutant phenotype PubMed 15525772. Source: MGI mRNA stabilization Inferred from electronic annotation. Source: Compara negative regulation of transcription involved in G1/S phase of mitotic cell cycle Inferred from electronic annotation. Source: Compara positive regulation of fibroblast proliferation Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 11004506. Source: MGI regulation of G1/S transition of mitotic cell cycle Inferred from electronic annotation. Source: Compara regulation of cell cycle Inferred from direct assay PubMed 11095619. Source: MGI spermatogenesis Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Rb-E2F complex Inferred from electronic annotation. Source: Compara cytoplasm Inferred from direct assay PubMed 8918469. Source: MGI transcription factor complex Inferred from direct assay PubMed 10082561. Source: MGI
Molecular_function	DNA binding Inferred from sequence orthology PubMed 15073182. Source: MGI core promoter binding Inferred from electronic annotation. Source: Compara sequence-specific DNA binding Inferred from electronic annotation. Source: Compara sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 10779331PubMed 11095619PubMed 14667810PubMed 15722552. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Ndn	P25233	5	EBI-1025536,EBI-1801080
Ndnl2	Q9CPR8	5	EBI-1025536,EBI-5529102

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 430	430	Transcription factor E2F1		PRO_0000219462
Regions
	DNA binding	105 – 189	85	Potential
	Region	62 – 103	42	Cyclin A/CDK2 binding Potential
	Region	84 – 186	103	Interaction with BIRC2/c-IAP1 By similarity
	Region	148 – 169	22	Leucine-zipper
	Region	190 – 279	90	Dimerization Potential
	Region	361 – 430	70	Transactivation Potential
	Region	402 – 419	18	Retinoblastoma protein RB1 binding Potential
	Motif	153 – 189	37	DEF box
Amino acid modifications
	Modified residue	112	1	N6-acetyllysine By similarity
	Modified residue	115	1	N6-acetyllysine By similarity
	Modified residue	120	1	N6-acetyllysine By similarity
	Modified residue	368	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q61501 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: C5DF18AD3B4DFEFA	FASTA	430	46,323
	10 20 30 40 50 60 MAVAPAGGQH APALEALLGA GALRLLDSSQ IVIISTAPDV GAPQLPAAPP TGPRDSDVLL 70 80 90 100 110 120 FATPQAPRPA PSAPRPALGR PPVKRRLDLE TDHQYLAGSS GPFRGRGRHP GKGVKSPGEK 130 140 150 160 170 180 SRYETSLNLT TKRFLELLSR SADGVVDLNW AAEVLKVQKR RIYDITNVLE GIQLIAKKSK 190 200 210 220 230 240 NHIQWLGSHT MVGIGKRLEG LTQDLQQLQE SEQQLDHLMH ICTTQLQLLS EDSDTQRLAY 250 260 270 280 290 300 VTCQDLRSIA DPAEQMVIVI KAPPETQLQA VDSSETFQIS LKSKQGPIDV FLCPEESADG 310 320 330 340 350 360 ISPGKTSCQE TSSGEDRTAD SGPAGPPPSP PSTSPALDPS QSLLGLEQEA VLPRMGHLRV 370 380 390 400 410 420 PMEEDQLSPL VAADSLLEHV KEDFSGLLPG EFISLSPPHE ALDYHFGLEE GEGIRDLFDC 430 DFGDLTPLDF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, chromosomal location, and characterization of mouse E2F1." Li Y., Slansky J.E., Myers D.J., Drinkwater N.R., Kaelin W.G. Jr., Farnham P.J. Mol. Cell. Biol. 14:1861-1869(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Swiss albino.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Embryo.
[3]	"Expression patterns of the E2F family of transcription factors during mouse nervous system development." Dagnino L., Fry C.J., Bartley S.M., Farnham P., Gallie B.L., Phillips R.A. Mech. Dev. 66:13-25(1997) [PubMed] [Europe PMC] [Abstract] Cited for: DEVELOPMENTAL STAGE.
[4]	"E2F-1-induced p53-independent apoptosis in transgenic mice." Holmberg C., Helin K., Sehested M., Karlstroem O. Oncogene 17:143-155(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN APOPTOSIS.
[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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EAPP.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L21973 mRNA. Translation: AAA83217.1. BC052160 mRNA. Translation: AAH52160.2.
IPI	IPI00338528.
PIR	A56209.
RefSeq	NP_031917.1. NM_007891.4.
UniGene	Mm.18036. Mm.441323.
3D structure databases
ProteinModelPortal	Q61501.
SMR	Q61501. Positions 121-185, 197-296.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q61501. 5 interactions.
MINT	MINT-4302111.
PTM databases
PhosphoSite	Q61501.
Proteomic databases
PRIDE	Q61501.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000103145; ENSMUSP00000099434; ENSMUSG00000027490.
GeneID	13555.
KEGG	mmu:13555.
UCSC	uc008njk.1. mouse.
Organism-specific databases
CTD	1869.
MGI	MGI:101941. E2f1.
Phylogenomic databases
eggNOG	NOG328718.
GeneTree	ENSGT00550000074403.
HOGENOM	HOG000232045.
HOVERGEN	HBG002227.
InParanoid	Q61501.
KO	K06620.
OMA	ICTTQLR.
OrthoDB	EOG42821X.
Enzyme and pathway databases
Reactome	REACT_118161. Cell Cycle.
Gene expression databases
ArrayExpress	Q61501.
Bgee	Q61501.
CleanEx	MM_E2F1.
Genevestigator	Q61501.
GermOnline	ENSMUSG00000027490. Mus musculus.
Family and domain databases
Gene3D	1.10.10.10. 1 hit.
InterPro	IPR015633. E2F. IPR003316. E2F_TDP. IPR011991. WHTH_DNA-bd_dom. [Graphical view]
PANTHER	PTHR12081. PTHR12081. 1 hit.
Pfam	PF02319. E2F_TDP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	284170.
SOURCE	Search...

Entry information

Entry name

E2F1_MOUSE

Accession

Primary (citable) accession number: Q61501
Secondary accession number(s): Q80VZ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	May 29, 2013
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program