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Protein

Transcription factor E2F1

Gene

E2f1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Blocks adipocyte differentiation by binding to specific promoters repressing CEBPA binding to its target gene promoters (PubMed:11672531, PubMed:20176812).By similarity3 Publications

Enzyme regulationi

BIRC2/c-IAP1 stimulates its transcriptional activity.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi105 – 18985Sequence AnalysisAdd
BLAST

GO - Molecular functioni

  • core promoter binding Source: MGI
  • DNA binding Source: MGI
  • sequence-specific DNA binding Source: UniProtKB
  • sequence-specific DNA binding transcription factor activity Source: MGI
  • transcription factor binding Source: UniProtKB
  • transcription regulatory region DNA binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Apoptosis, Cell cycle, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_274086. G0 and Early G1.
REACT_283368. G2 Phase.
REACT_289448. Cyclin D associated events in G1.
REACT_297337. CDC6 association with the ORC:origin complex.
REACT_314754. E2F mediated regulation of DNA replication.
REACT_324544. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_339329. G1/S-Specific Transcription.
REACT_349855. Association of licensing factors with the pre-replicative complex.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor E2F1
Short name:
E2F-1
Gene namesi
Name:E2f1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:101941. E2f1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • nuclear chromatin Source: BHF-UCL
  • nucleoplasm Source: Reactome
  • nucleus Source: MGI
  • Rb-E2F complex Source: MGI
  • transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 430430Transcription factor E2F1PRO_0000219462Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei112 – 1121N6-acetyllysineBy similarity
Modified residuei115 – 1151N6-acetyllysineBy similarity
Modified residuei120 – 1201N6-acetyllysineBy similarity
Modified residuei368 – 3681PhosphoserineBy similarity

Post-translational modificationi

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).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).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiQ61501.

PTM databases

PhosphoSiteiQ61501.

Expressioni

Developmental stagei

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.1 Publication

Gene expression databases

BgeeiQ61501.
CleanExiMM_E2F1.
ExpressionAtlasiQ61501. baseline and differential.
GenevisibleiQ61501. MM.

Interactioni

Subunit structurei

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 and EAPP. Interacts with ARID3A. Interacts with TRIM28; the interaction inhibits E2F1 acetylation through recruiting HDAC1 and represses its transcriptional activity. Interaction with KAT2B; the interaction acetylates E2F1 enhancing its DNA-binding and transcriptional activity. Interacts with BIRC2/c-IAP1 (via BIR domains). The complex TFDP1:E2F1 interacts with CEBPA; the interaction prevents CEBPA binding to target genes promoters and represses its transcriptional activity.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
NdnP252335EBI-1025536,EBI-1801080
Ndnl2Q9CPR85EBI-1025536,EBI-5529102

Protein-protein interaction databases

BioGridi199350. 17 interactions.
IntActiQ61501. 6 interactions.
MINTiMINT-4302111.
STRINGi10090.ENSMUSP00000099434.

Structurei

3D structure databases

ProteinModelPortaliQ61501.
SMRiQ61501. Positions 121-185, 197-296.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni62 – 10342Cyclin A:CDK2 bindingBy similarityAdd
BLAST
Regioni84 – 186103Interaction with BIRC2/c-IAP1By similarityAdd
BLAST
Regioni148 – 16922Leucine-zipperAdd
BLAST
Regioni187 – 375189Required for interaction with TRIM28By similarityAdd
BLAST
Regioni190 – 27990DimerizationSequence AnalysisAdd
BLAST
Regioni361 – 43070TransactivationBy similarityAdd
BLAST
Regioni402 – 41918RB1 bindingBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi153 – 18937DEF boxAdd
BLAST

Sequence similaritiesi

Belongs to the E2F/DP family.Curated

Phylogenomic databases

eggNOGiNOG328718.
GeneTreeiENSGT00550000074403.
HOGENOMiHOG000232045.
HOVERGENiHBG002227.
InParanoidiQ61501.
OMAiHVREDFS.
OrthoDBiEOG738058.
PhylomeDBiQ61501.
TreeFamiTF105566.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR015633. E2F.
IPR003316. E2F_WHTH_DNA-bd_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR12081. PTHR12081. 1 hit.
PfamiPF02319. E2F_TDP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q61501-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVAPAGGQH APALEALLGA GALRLLDSSQ IVIISTAPDV GAPQLPAAPP
60 70 80 90 100
TGPRDSDVLL FATPQAPRPA PSAPRPALGR PPVKRRLDLE TDHQYLAGSS
110 120 130 140 150
GPFRGRGRHP GKGVKSPGEK SRYETSLNLT TKRFLELLSR SADGVVDLNW
160 170 180 190 200
AAEVLKVQKR RIYDITNVLE GIQLIAKKSK NHIQWLGSHT MVGIGKRLEG
210 220 230 240 250
LTQDLQQLQE SEQQLDHLMH ICTTQLQLLS EDSDTQRLAY VTCQDLRSIA
260 270 280 290 300
DPAEQMVIVI KAPPETQLQA VDSSETFQIS LKSKQGPIDV FLCPEESADG
310 320 330 340 350
ISPGKTSCQE TSSGEDRTAD SGPAGPPPSP PSTSPALDPS QSLLGLEQEA
360 370 380 390 400
VLPRMGHLRV PMEEDQLSPL VAADSLLEHV KEDFSGLLPG EFISLSPPHE
410 420 430
ALDYHFGLEE GEGIRDLFDC DFGDLTPLDF
Length:430
Mass (Da):46,323
Last modified:November 1, 1996 - v1
Checksum:iC5DF18AD3B4DFEFA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L21973 mRNA. Translation: AAA83217.1.
BC052160 mRNA. Translation: AAH52160.2.
CCDSiCCDS16935.1.
PIRiA56209.
RefSeqiNP_031917.1. NM_007891.5.
UniGeneiMm.18036.
Mm.441323.

Genome annotation databases

EnsembliENSMUST00000103145; ENSMUSP00000099434; ENSMUSG00000027490.
GeneIDi13555.
UCSCiuc008njk.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L21973 mRNA. Translation: AAA83217.1.
BC052160 mRNA. Translation: AAH52160.2.
CCDSiCCDS16935.1.
PIRiA56209.
RefSeqiNP_031917.1. NM_007891.5.
UniGeneiMm.18036.
Mm.441323.

3D structure databases

ProteinModelPortaliQ61501.
SMRiQ61501. Positions 121-185, 197-296.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199350. 17 interactions.
IntActiQ61501. 6 interactions.
MINTiMINT-4302111.
STRINGi10090.ENSMUSP00000099434.

PTM databases

PhosphoSiteiQ61501.

Proteomic databases

PRIDEiQ61501.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000103145; ENSMUSP00000099434; ENSMUSG00000027490.
GeneIDi13555.
UCSCiuc008njk.2. mouse.

Organism-specific databases

CTDi1869.
MGIiMGI:101941. E2f1.

Phylogenomic databases

eggNOGiNOG328718.
GeneTreeiENSGT00550000074403.
HOGENOMiHOG000232045.
HOVERGENiHBG002227.
InParanoidiQ61501.
OMAiHVREDFS.
OrthoDBiEOG738058.
PhylomeDBiQ61501.
TreeFamiTF105566.

Enzyme and pathway databases

ReactomeiREACT_274086. G0 and Early G1.
REACT_283368. G2 Phase.
REACT_289448. Cyclin D associated events in G1.
REACT_297337. CDC6 association with the ORC:origin complex.
REACT_314754. E2F mediated regulation of DNA replication.
REACT_324544. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_339329. G1/S-Specific Transcription.
REACT_349855. Association of licensing factors with the pre-replicative complex.

Miscellaneous databases

NextBioi284170.
PROiQ61501.
SOURCEiSearch...

Gene expression databases

BgeeiQ61501.
CleanExiMM_E2F1.
ExpressionAtlasiQ61501. baseline and differential.
GenevisibleiQ61501. MM.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR015633. E2F.
IPR003316. E2F_WHTH_DNA-bd_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR12081. PTHR12081. 1 hit.
PfamiPF02319. E2F_TDP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "E2F repression by C/EBPalpha is required for adipogenesis and granulopoiesis in vivo."
    Porse B.T., Pedersen T.A., Xu X., Lindberg B., Wewer U.M., Friis-Hansen L., Nerlov C.
    Cell 107:247-258(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "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.
  7. "Repression of transcriptional activity of C/EBPalpha by E2F-dimerization partner complexes."
    Zaragoza K., Begay V., Schuetz A., Heinemann U., Leutz A.
    Mol. Cell. Biol. 30:2293-2304(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiE2F1_MOUSE
AccessioniPrimary (citable) accession number: Q61501
Secondary accession number(s): Q80VZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 22, 2015
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.