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Protein

Transcription factor E2F8

Gene

E2f8

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

Functioni

Atypical E2F transcription factor that participates in various processes such as angiogenesis and polyploidization of specialized cells. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represses transcription of classical E2F transcription factors such as E2F1: component of a feedback loop in S phase by repressing the expression of E2F1, thereby preventing p53/TP53-dependent apoptosis. Plays a key role in polyploidization of cells in placenta and liver by regulating the endocycle, probably by repressing genes promoting cytokinesis and antagonizing action of classical E2F proteins (E2F1, E2F2 and/or E2F3). Required for placental development by promoting polyploidization of trophoblast giant cells. Acts as a promoter of sprouting angiogenesis, possibly by acting as a transcription activator: associates with HIF1A, recognizes and binds the VEGFA promoter, which is different from canonical E2 recognition site, and activates expression of the VEGFA gene.5 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi113 – 182Sequence analysisAdd BLAST70
DNA bindingi261 – 347Sequence analysisAdd BLAST87

GO - Molecular functioni

GO - Biological processi

  • cell cycle comprising mitosis without cytokinesis Source: UniProtKB
  • cell proliferation Source: MGI
  • chorionic trophoblast cell differentiation Source: UniProtKB
  • hepatocyte differentiation Source: UniProtKB
  • negative regulation of cytokinesis Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • placenta development Source: UniProtKB
  • positive regulation of DNA endoreduplication Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • sprouting angiogenesis Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
  • trophoblast giant cell differentiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Cell cycle, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor E2F8
Short name:
E2F-8
Gene namesi
Name:E2f8
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1922038. E2f8.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: MGI
  • transcription factor complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

No visible phenotype; mice develop normally and live to old age. E2f7 and E2f8 double knockout embryos die by 11.5 dpc of massive apoptosis and dilation of blood vessels and show increased expression of E2f1 and p53/Tp53, as well as many stress-related genes.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi118 – 119LG → EF: Loss of DNA-binding. 1 Publication2
Mutagenesisi266 – 267LR → EF: Loss of DNA-binding. 1 Publication2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002989101 – 860Transcription factor E2F8Add BLAST860

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei71PhosphoserineCombined sources1
Modified residuei102PhosphoserineBy similarity1
Modified residuei412PhosphoserineBy similarity1
Modified residuei416PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ58FA4.
PaxDbiQ58FA4.
PeptideAtlasiQ58FA4.
PRIDEiQ58FA4.

PTM databases

iPTMnetiQ58FA4.
PhosphoSitePlusiQ58FA4.

Expressioni

Tissue specificityi

Highly expressed in liver, skin, thymus and testis. Expressed in trophoblast giant cells throughout placenta development (at protein level).3 Publications

Inductioni

Induced at the onset of hepatocyte polyploidization.1 Publication

Gene expression databases

BgeeiENSMUSG00000046179.
CleanExiMM_E2F8.
GenevisibleiQ58FA4. MM.

Interactioni

Subunit structurei

Interacts with HIF1A (By similarity). Homodimer and heterodimer: mainly forms homodimers and, to a lesser extent, heterodimers with E2F8. Dimerization is important for DNA-binding.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-1390691,EBI-1390691

GO - Molecular functioni

  • protein homodimerization activity Source: MGI

Protein-protein interaction databases

BioGridi224496. 1 interactor.
IntActiQ58FA4. 2 interactors.
MINTiMINT-8410110.
STRINGi10090.ENSMUSP00000056778.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WZHmodel-A263-341[»]
F112-181[»]
ProteinModelPortaliQ58FA4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

In contrast to classical members of the E2F transcription factor, atypical members contain 2 DNA-binding domains and regulate transcription in a DP-independent manner. Both DNA-binding domains are required for DNA-binding and are proposed to form an intramolecular structure that is similar to the winged helix structure of the E2F-DP heterodimer (By similarity).By similarity

Sequence similaritiesi

Belongs to the E2F/DP family.Curated

Phylogenomic databases

eggNOGiKOG2578. Eukaryota.
ENOG4111IGY. LUCA.
GeneTreeiENSGT00530000063616.
HOGENOMiHOG000013193.
HOVERGENiHBG063270.
InParanoidiQ58FA4.
KOiK09391.
OMAiLIPLTQC.
OrthoDBiEOG091G0F9Z.
PhylomeDBiQ58FA4.
TreeFamiTF105567.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
InterProiIPR015633. E2F.
IPR003316. E2F_WHTH_DNA-bd_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR12081. PTHR12081. 5 hits.
PfamiPF02319. E2F_TDP. 2 hits.
[Graphical view]
SMARTiSM01372. E2F_TDP. 2 hits.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 2 hits.

Sequencei

Sequence statusi: Complete.

Q58FA4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENQKENLFS EPHKRGLMKS PLHPSSKANM VLAEIQPDLG PLTTPTKPKE
60 70 80 90 100
VSQGEPWTPT ANLKMLISAV SPEIRSRDQK RGLSDNRSAL PEARDCLHEH
110 120 130 140 150
LSGDEFEKSQ PSRKEKSLGL LCHKFLARYP KYPNPAVNND ICLDEVAEEL
160 170 180 190 200
NVERRRIYDI VNVLESLHMV SRLAKNRYTW HGRHNLTKTL GTLKSVGEEN
210 220 230 240 250
KYAEQIMMIK RKEYEQEFDF IKSCGIEDHV IKSHTGQNGH SDMCFVELPG
260 270 280 290 300
VEFRAASVNS RKDKSLRVMS QKFVMLFLVS TPQIVSLEIA AKILIGEDHV
310 320 330 340 350
EDLDKSKYKT KIRRLYDIAN VLSSLDLIKK VHVTEERGRK PAFKWTGPEI
360 370 380 390 400
SPNNSGSSPI MPLPASLEAE QSAKENCAKN LFSTRGKPSF TRHPSLIKLV
410 420 430 440 450
KSIENDRRKI SSAPSSPVKS NKAESSQNSP PVPNKMAQLA AICKMQLEEQ
460 470 480 490 500
SSEPRKKVKV NLARSGHYKP LAPLDPTVNT ELELLTPSLI QPLGVVPLIP
510 520 530 540 550
SPLSSAVPVI LPQAPSGPSY AIYLQPAQAQ MLTPPPGLSP TVCPTQPSNA
560 570 580 590 600
TGSKDPTDAP AEKTATDAAT TGSLQPAPER HGAKHRSKET TGDRGTKRMI
610 620 630 640 650
TAEDSGPSSV KKPKEDLKAL ENVPTPTPLF PSGYLIPLTQ CSSLGPDSVL
660 670 680 690 700
SNTENSGTPS PNHRIYGSPI AGVIPVASSE LTAVNFPPFH VTPLKLMVSP
710 720 730 740 750
TSMAAVPVGN SPALNSGHPA PAQNPSSAIV NFTLQHLGLI SPGVQMSASP
760 770 780 790 800
GPGAGTVPVS PRVEADNLSS RQRRATNHDS PVLGQSQLNG QPVAGTGAQQ
810 820 830 840 850
PVPVTPKGSQ LVAENFFRTP GGPTKPTSSP YTDFDGANKT SFGTLFVPQR
860
KLEVSTEDIH
Length:860
Mass (Da):93,276
Last modified:April 26, 2005 - v1
Checksum:i792E3DDCA299ACE7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti65M → T in BAC33794 (PubMed:16141072).Curated1
Sequence conflicti138N → Y in AAH86675 (PubMed:15489334).Curated1
Sequence conflicti155R → Q in BAC39205 (PubMed:16141072).Curated1
Sequence conflicti209I → T in BAC39205 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY957576 mRNA. Translation: AAX49603.1.
AK049525 mRNA. Translation: BAC33794.1.
AK084513 mRNA. Translation: BAC39205.1.
AK154018 mRNA. Translation: BAE32318.1.
AK157235 mRNA. Translation: BAE34010.1.
AK160240 mRNA. Translation: BAE35708.1.
BC086675 mRNA. Translation: AAH86675.1.
BC100357 mRNA. Translation: AAI00358.1.
CCDSiCCDS39967.1.
RefSeqiNP_001013386.2. NM_001013368.5.
XP_006540616.1. XM_006540553.3.
XP_006540617.1. XM_006540554.3.
UniGeneiMm.240566.

Genome annotation databases

EnsembliENSMUST00000058745; ENSMUSP00000056778; ENSMUSG00000046179.
ENSMUST00000119223; ENSMUSP00000112883; ENSMUSG00000046179.
GeneIDi108961.
KEGGimmu:108961.
UCSCiuc009haz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY957576 mRNA. Translation: AAX49603.1.
AK049525 mRNA. Translation: BAC33794.1.
AK084513 mRNA. Translation: BAC39205.1.
AK154018 mRNA. Translation: BAE32318.1.
AK157235 mRNA. Translation: BAE34010.1.
AK160240 mRNA. Translation: BAE35708.1.
BC086675 mRNA. Translation: AAH86675.1.
BC100357 mRNA. Translation: AAI00358.1.
CCDSiCCDS39967.1.
RefSeqiNP_001013386.2. NM_001013368.5.
XP_006540616.1. XM_006540553.3.
XP_006540617.1. XM_006540554.3.
UniGeneiMm.240566.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WZHmodel-A263-341[»]
F112-181[»]
ProteinModelPortaliQ58FA4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi224496. 1 interactor.
IntActiQ58FA4. 2 interactors.
MINTiMINT-8410110.
STRINGi10090.ENSMUSP00000056778.

PTM databases

iPTMnetiQ58FA4.
PhosphoSitePlusiQ58FA4.

Proteomic databases

EPDiQ58FA4.
PaxDbiQ58FA4.
PeptideAtlasiQ58FA4.
PRIDEiQ58FA4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000058745; ENSMUSP00000056778; ENSMUSG00000046179.
ENSMUST00000119223; ENSMUSP00000112883; ENSMUSG00000046179.
GeneIDi108961.
KEGGimmu:108961.
UCSCiuc009haz.2. mouse.

Organism-specific databases

CTDi79733.
MGIiMGI:1922038. E2f8.

Phylogenomic databases

eggNOGiKOG2578. Eukaryota.
ENOG4111IGY. LUCA.
GeneTreeiENSGT00530000063616.
HOGENOMiHOG000013193.
HOVERGENiHBG063270.
InParanoidiQ58FA4.
KOiK09391.
OMAiLIPLTQC.
OrthoDBiEOG091G0F9Z.
PhylomeDBiQ58FA4.
TreeFamiTF105567.

Miscellaneous databases

ChiTaRSiE2f8. mouse.
PROiQ58FA4.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000046179.
CleanExiMM_E2F8.
GenevisibleiQ58FA4. MM.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
InterProiIPR015633. E2F.
IPR003316. E2F_WHTH_DNA-bd_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR12081. PTHR12081. 5 hits.
PfamiPF02319. E2F_TDP. 2 hits.
[Graphical view]
SMARTiSM01372. E2F_TDP. 2 hits.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiE2F8_MOUSE
AccessioniPrimary (citable) accession number: Q58FA4
Secondary accession number(s): Q3U4W2
, Q497V7, Q5PRE4, Q8BQJ5, Q8C3Y5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: April 26, 2005
Last modified: November 2, 2016
This is version 120 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.