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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)DescriptionActionsGraphical viewLength
DNA bindingi105 – 189Sequence analysisAdd BLAST85

GO - Molecular functioni

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

ReactomeiR-MMU-113510. E2F mediated regulation of DNA replication.
R-MMU-1538133. G0 and Early G1.
R-MMU-68689. CDC6 association with the ORC:origin complex.
R-MMU-68911. G2 Phase.
R-MMU-69205. G1/S-Specific Transcription.
R-MMU-69231. Cyclin D associated events in G1.
R-MMU-69298. 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
Proteomesi
  • UP000000589 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)DescriptionActionsGraphical viewLength
ChainiPRO_00002194621 – 430Transcription factor E2F1Add BLAST430

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei112N6-acetyllysineBy similarity1
Modified residuei115N6-acetyllysineBy similarity1
Modified residuei120N6-acetyllysineBy similarity1
Modified residuei368PhosphoserineBy similarity1

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

PaxDbiQ61501.
PRIDEiQ61501.

PTM databases

iPTMnetiQ61501.
PhosphoSitePlusiQ61501.

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

BgeeiENSMUSG00000027490.
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
Nsmce3Q9CPR85EBI-1025536,EBI-5529102

GO - Molecular functioni

  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi199350. 18 interactors.
IntActiQ61501. 6 interactors.
MINTiMINT-4302111.
STRINGi10090.ENSMUSP00000099434.

Structurei

3D structure databases

ProteinModelPortaliQ61501.
SMRiQ61501.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni62 – 103Cyclin A:CDK2 bindingBy similarityAdd BLAST42
Regioni84 – 186Interaction with BIRC2/c-IAP1By similarityAdd BLAST103
Regioni148 – 169Leucine-zipperAdd BLAST22
Regioni187 – 375Required for interaction with TRIM28By similarityAdd BLAST189
Regioni190 – 279DimerizationSequence analysisAdd BLAST90
Regioni361 – 430TransactivationBy similarityAdd BLAST70
Regioni402 – 419RB1 bindingBy similarityAdd BLAST18

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi153 – 189DEF boxAdd BLAST37

Sequence similaritiesi

Belongs to the E2F/DP family.Curated

Phylogenomic databases

eggNOGiKOG2577. Eukaryota.
ENOG410XNYI. LUCA.
GeneTreeiENSGT00550000074403.
HOGENOMiHOG000232045.
HOVERGENiHBG002227.
InParanoidiQ61501.
KOiK17454.
OMAiHVREDFS.
OrthoDBiEOG091G087U.
PhylomeDBiQ61501.
TreeFamiTF105566.

Family and domain databases

CDDicd14660. E2F_DD. 1 hit.
Gene3Di1.10.10.10. 1 hit.
InterProiIPR015633. E2F.
IPR032198. E2F_CC-MB.
IPR003316. E2F_WHTH_DNA-bd_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR12081. PTHR12081. 1 hit.
PfamiPF16421. E2F_CC-MB. 1 hit.
PF02319. E2F_TDP. 1 hit.
[Graphical view]
SMARTiSM01372. E2F_TDP. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.

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.
KEGGimmu:13555.
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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199350. 18 interactors.
IntActiQ61501. 6 interactors.
MINTiMINT-4302111.
STRINGi10090.ENSMUSP00000099434.

PTM databases

iPTMnetiQ61501.
PhosphoSitePlusiQ61501.

Proteomic databases

PaxDbiQ61501.
PRIDEiQ61501.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000103145; ENSMUSP00000099434; ENSMUSG00000027490.
GeneIDi13555.
KEGGimmu:13555.
UCSCiuc008njk.2. mouse.

Organism-specific databases

CTDi1869.
MGIiMGI:101941. E2f1.

Phylogenomic databases

eggNOGiKOG2577. Eukaryota.
ENOG410XNYI. LUCA.
GeneTreeiENSGT00550000074403.
HOGENOMiHOG000232045.
HOVERGENiHBG002227.
InParanoidiQ61501.
KOiK17454.
OMAiHVREDFS.
OrthoDBiEOG091G087U.
PhylomeDBiQ61501.
TreeFamiTF105566.

Enzyme and pathway databases

ReactomeiR-MMU-113510. E2F mediated regulation of DNA replication.
R-MMU-1538133. G0 and Early G1.
R-MMU-68689. CDC6 association with the ORC:origin complex.
R-MMU-68911. G2 Phase.
R-MMU-69205. G1/S-Specific Transcription.
R-MMU-69231. Cyclin D associated events in G1.
R-MMU-69298. Association of licensing factors with the pre-replicative complex.

Miscellaneous databases

PROiQ61501.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000027490.
CleanExiMM_E2F1.
ExpressionAtlasiQ61501. baseline and differential.
GenevisibleiQ61501. MM.

Family and domain databases

CDDicd14660. E2F_DD. 1 hit.
Gene3Di1.10.10.10. 1 hit.
InterProiIPR015633. E2F.
IPR032198. E2F_CC-MB.
IPR003316. E2F_WHTH_DNA-bd_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR12081. PTHR12081. 1 hit.
PfamiPF16421. E2F_CC-MB. 1 hit.
PF02319. E2F_TDP. 1 hit.
[Graphical view]
SMARTiSM01372. E2F_TDP. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
ProtoNetiSearch...

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: November 2, 2016
This is version 147 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

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 one 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.