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Q61501 (E2F1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription factor E2F1

Short name=E2F-1
Gene names
Name:E2f1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length430 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processApoptosis
Cell cycle
Transcription
Transcription regulation
   Cellular componentNucleus
   LigandDNA-binding
   Molecular functionActivator
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage checkpoint

Inferred from sequence or structural similarity. Source: UniProtKB

anoikis

Inferred from direct assay PubMed 14667810. Source: MGI

cellular response to fatty acid

Inferred from electronic annotation. Source: Ensembl

cellular response to hypoxia

Inferred from electronic annotation. Source: Ensembl

forebrain development

Inferred from mutant phenotype PubMed 15525772. Source: MGI

intrinsic apoptotic signaling pathway by p53 class mediator

Inferred from direct assay PubMed 11095619. Source: MGI

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from electronic annotation. Source: Ensembl

lens fiber cell apoptotic process

Inferred from direct assay PubMed 11095619. Source: MGI

mRNA stabilization

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription involved in G1/S transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

positive regulation of fibroblast proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 11004506. Source: MGI

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 11331592PubMed 12893818PubMed 15722552. Source: MGI

regulation of G1/S transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

regulation of cell cycle

Inferred from direct assay PubMed 11095619. Source: MGI

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 11071387PubMed 14593116PubMed 14667810. Source: MGI

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentRb-E2F complex

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 8918469. Source: MGI

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 10082561PubMed 8918469. Source: MGI

transcription factor complex

Inferred from direct assay PubMed 10082561. Source: MGI

   Molecular_functionDNA binding

Inferred from sequence orthology PubMed 15073182. Source: MGI

core promoter binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 10779331PubMed 11095619PubMed 14667810PubMed 15722552. Source: MGI

transcription factor binding

Inferred from physical interaction PubMed 10597240. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 430430Transcription factor E2F1
PRO_0000219462

Regions

DNA binding105 – 18985 Potential
Region62 – 10342Cyclin A/CDK2 binding Potential
Region84 – 186103Interaction with BIRC2/c-IAP1 By similarity
Region148 – 16922Leucine-zipper
Region190 – 27990Dimerization Potential
Region361 – 43070Transactivation Potential
Region402 – 41918Retinoblastoma protein RB1 binding Potential
Motif153 – 18937DEF box

Amino acid modifications

Modified residue1121N6-acetyllysine By similarity
Modified residue1151N6-acetyllysine By similarity
Modified residue1201N6-acetyllysine By similarity
Modified residue3681Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q61501 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: C5DF18AD3B4DFEFA

FASTA43046,323
        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 

« Hide

References

« Hide '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.
PIRA56209.
RefSeqNP_031917.1. NM_007891.4.
UniGeneMm.18036.
Mm.441323.

3D structure databases

ProteinModelPortalQ61501.
SMRQ61501. Positions 121-185, 197-296.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199350. 17 interactions.
IntActQ61501. 6 interactions.
MINTMINT-4302111.

PTM databases

PhosphoSiteQ61501.

Proteomic databases

PRIDEQ61501.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000103145; ENSMUSP00000099434; ENSMUSG00000027490.
GeneID13555.
KEGGmmu:13555.
UCSCuc008njk.1. mouse.

Organism-specific databases

CTD1869.
MGIMGI:101941. E2f1.

Phylogenomic databases

eggNOGNOG328718.
GeneTreeENSGT00550000074403.
HOGENOMHOG000232045.
HOVERGENHBG002227.
InParanoidQ61501.
KOK17454.
OMARHPGKGV.
OrthoDBEOG738058.
PhylomeDBQ61501.
TreeFamTF105566.

Enzyme and pathway databases

ReactomeREACT_188804. Cell Cycle.

Gene expression databases

ArrayExpressQ61501.
BgeeQ61501.
CleanExMM_E2F1.
GenevestigatorQ61501.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR015633. E2F.
IPR003316. E2F_TDP.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERPTHR12081. PTHR12081. 1 hit.
PfamPF02319. E2F_TDP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio284170.
PROQ61501.
SOURCESearch...

Entry information

Entry nameE2F1_MOUSE
AccessionPrimary (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: April 16, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot