Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Transcription factor E2FA

Gene

E2FA

Organism
Arabidopsis thaliana (Mouse-ear cress)
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 binding of retinoblastoma-related proteins represses transactivation. Regulates gene expression both positively and negatively. Activates the expression of E2FB. Involved in the control of cell-cycle progression from G1 to S phase. Stimulates cell proliferation and delays differentiation.9 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi167 – 23266Add
BLAST

GO - Molecular functioni

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • positive regulation of meiotic cell cycle Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Cell cycle, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor E2FA
Alternative name(s):
E2F transcription factor-3
Short name:
AtE2F3
Gene namesi
Name:E2FA
Synonyms:E2F3, E2F4
Ordered Locus Names:At2g36010
ORF Names:F11F19.8
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G36010.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus 1 Publication

  • Note: Interaction with DPA induces an exclusive nuclear localization, but an interaction with DPB has no effect.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 485485Transcription factor E2FAPRO_0000406289Add
BLAST

Proteomic databases

PRIDEiQ9FNY0.

Expressioni

Tissue specificityi

Highly expressed in the shoot apical meristem, emerging leaf primordia, and vascular tissues of young leaf primordia. Expressed in flowers, in epidermis and cortex of hypocotyls, and at lower levels in leaves.2 Publications

Developmental stagei

Expressed in a cell cycle-dependent manner. Most abundant in early S phase. Decreased expression during the passage into G2.3 Publications

Gene expression databases

ExpressionAtlasiQ9FNY0. baseline and differential.
GenevisibleiQ9FNY0. AT.

Interactioni

Subunit structurei

Heterodimer with DP proteins. Interacts (via dimerization domain) preferentially with DPA, but also with DPB. Interacts with maize retinoblastoma-related protein RBR1. No interaction with E2FD.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DPAQ9FNY36EBI-1774747,EBI-1774763
DPBQ9FNY25EBI-1774747,EBI-1774876
RBR1Q9LKZ34EBI-1774747,EBI-398590

Protein-protein interaction databases

BioGridi3518. 17 interactions.
DIPiDIP-40175N.
IntActiQ9FNY0. 10 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9FNY0.
SMRiQ9FNY0. Positions 167-231, 249-350.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni249 – 27729Leucine-zipperAdd
BLAST
Regioni435 – 45016Retinoblastoma protein bindingSequence analysisAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili245 – 28642Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi9 – 5345Pro-richAdd
BLAST

Domaini

The C-terminal region (366-485) is required for transactivational activity. The N-terminal region (92-128) is important for nuclear localization.

Sequence similaritiesi

Belongs to the E2F/DP family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

HOGENOMiHOG000232044.
InParanoidiQ9FNY0.
KOiK06620.
PhylomeDBiQ9FNY0.

Family and domain databases

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.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9FNY0-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSGVVRSSPG SSQPPPPPPH HPPSSPVPVT STPVIPPIRR HLAFASTKPP
60 70 80 90 100
FHPSDDYHRF NPSSLSNNND RSFVHGCGVV DREEDAVVVR SPSRKRKATM
110 120 130 140 150
DMVVAPSNNG FTSSGFTNIP SSPCQTPRKG GRVNIKSKAK GNKSTPQTPI
160 170 180 190 200
STNAGSPITL TPSGSCRYDS SLGLLTKKFV NLIKQAKDGM LDLNKAAETL
210 220 230 240 250
EVQKRRIYDI TNVLEGIDLI EKPFKNRILW KGVDACPGDE DADVSVLQLQ
260 270 280 290 300
AEIENLALEE QALDNQIRQT EERLRDLSEN EKNQKWLFVT EEDIKSLPGF
310 320 330 340 350
QNQTLIAVKA PHGTTLEVPD PDEAADHPQR RYRIILRSTM GPIDVYLVSE
360 370 380 390 400
FEGKFEDTNG SGAAPPACLP IASSSGSTGH HDIEALTVDN PETAIVSHDH
410 420 430 440 450
PHPQPGDTSD LNYLQEQVGG MLKITPSDVE NDESDYWLLS NAEISMTDIW
460 470 480
KTDSGIDWDY GIADVSTPPP GMGEIAPTAV DSTPR
Length:485
Mass (Da):52,839
Last modified:March 1, 2001 - v1
Checksum:i838A5AD7A31B035C
GO
Isoform 2 (identifier: Q9FNY0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     247-248: Missing.

Show »
Length:483
Mass (Da):52,598
Checksum:i63B41EDCD742A4CB
GO
Isoform 3 (identifier: Q9FNY0-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     92-92: P → PIFPSEIGLEIRGCFGDFDCYLLLLSLIQKLRSVRLSSIRVNFCRLFSFAM
     155-173: GSPITLTPSGSCRYDSSLG → VRSFYEISFMSRVTS

Show »
Length:531
Mass (Da):58,521
Checksum:i34AE922E7B40BE69
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti264 – 2641D → G in CAC15486 (PubMed:11108847).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei92 – 921P → PIFPSEIGLEIRGCFGDFDC YLLLLSLIQKLRSVRLSSIR VNFCRLFSFAM in isoform 3. 1 PublicationVSP_040801
Alternative sequencei155 – 17319GSPIT…DSSLG → VRSFYEISFMSRVTS in isoform 3. 1 PublicationVSP_040802Add
BLAST
Alternative sequencei247 – 2482Missing in isoform 2. CuratedVSP_040803

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ294534 mRNA. Translation: CAC15486.1.
AF242582 mRNA. Translation: AAG17610.1.
AJ276619 mRNA. Translation: CAC34724.1.
AJ271597 mRNA. Translation: CAB70599.1.
AC007017 Genomic DNA. Translation: AAD21456.2.
CP002685 Genomic DNA. Translation: AEC09191.1.
CP002685 Genomic DNA. Translation: AEC09192.1.
BT026376 mRNA. Translation: ABH04483.1.
PIRiG84775.
RefSeqiNP_565831.3. NM_129160.4. [Q9FNY0-2]
NP_973610.1. NM_201881.2.
NP_973611.1. NM_201882.2. [Q9FNY0-1]
UniGeneiAt.10190.
At.64435.

Genome annotation databases

EnsemblPlantsiAT2G36010.3; AT2G36010.3; AT2G36010. [Q9FNY0-1]
GeneIDi818174.
KEGGiath:AT2G36010.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ294534 mRNA. Translation: CAC15486.1.
AF242582 mRNA. Translation: AAG17610.1.
AJ276619 mRNA. Translation: CAC34724.1.
AJ271597 mRNA. Translation: CAB70599.1.
AC007017 Genomic DNA. Translation: AAD21456.2.
CP002685 Genomic DNA. Translation: AEC09191.1.
CP002685 Genomic DNA. Translation: AEC09192.1.
BT026376 mRNA. Translation: ABH04483.1.
PIRiG84775.
RefSeqiNP_565831.3. NM_129160.4. [Q9FNY0-2]
NP_973610.1. NM_201881.2.
NP_973611.1. NM_201882.2. [Q9FNY0-1]
UniGeneiAt.10190.
At.64435.

3D structure databases

ProteinModelPortaliQ9FNY0.
SMRiQ9FNY0. Positions 167-231, 249-350.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi3518. 17 interactions.
DIPiDIP-40175N.
IntActiQ9FNY0. 10 interactions.

Proteomic databases

PRIDEiQ9FNY0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G36010.3; AT2G36010.3; AT2G36010. [Q9FNY0-1]
GeneIDi818174.
KEGGiath:AT2G36010.

Organism-specific databases

TAIRiAT2G36010.

Phylogenomic databases

HOGENOMiHOG000232044.
InParanoidiQ9FNY0.
KOiK06620.
PhylomeDBiQ9FNY0.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ9FNY0.

Gene expression databases

ExpressionAtlasiQ9FNY0. baseline and differential.
GenevisibleiQ9FNY0. AT.

Family and domain databases

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...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of two distinct DP-related genes from Arabidopsis thaliana."
    Magyar Z., Atanassova A., De Veylder L., Rombauts S., Inze D.
    FEBS Lett. 486:79-87(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH DPA AND DPB, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  2. "Arabidopsis E2F1 binds a sequence present in the promoter of S-phase-regulated gene AtCDC6 and is a member of a multigene family with differential activities."
    de Jager S.M., Menges M., Bauer U.M., Murra J.A.
    Plant Mol. Biol. 47:555-568(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH MAIZE RBR1, DEVELOPMENTAL STAGE.
    Strain: cv. Columbia.
  3. "The E2F family of transcription factors from Arabidopsis thaliana. Novel and conserved components of the retinoblastoma/E2F pathway in plants."
    Mariconti L., Pellegrini B., Cantoni R., Stevens R., Bergounioux C., Cella R., Albani D.
    J. Biol. Chem. 277:9911-9919(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH DPA AND DPB, DEVELOPMENTAL STAGE, GENE FAMILY, NOMENCLATURE.
    Strain: cv. Columbia.
  4. "Isolation and characterization of E2F-like protein in Arabidopsis thaliana."
    Labra M., Ghiani A., Citterio S., Sgorbati S.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  6. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  7. "Arabidopsis ORF Clones."
    Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  8. "Control of proliferation, endoreduplication and differentiation by the Arabidopsis E2Fa-DPa transcription factor."
    De Veylder L., Beeckman T., Beemster G.T., de Almeida Engler J., Ormenese S., Maes S., Naudts M., Van Der Schueren E., Jacqmard A., Engler G., Inze D.
    EMBO J. 21:1360-1368(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  9. "E2Ls, E2F-like repressors of Arabidopsis that bind to E2F sites in a monomeric form."
    Kosugi S., Ohashi Y.
    J. Biol. Chem. 277:16553-16558(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DPA; DPB AND E2FD.
  10. "AtE2F-a and AtDP-a, members of the E2F family of transcription factors, induce Arabidopsis leaf cells to re-enter S phase."
    Rossignol P., Stevens R., Perennes C., Jasinski S., Cella R., Tremousaygue D., Bergounioux C.
    Mol. Genet. Genomics 266:995-1003(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Genome-wide analysis of core cell cycle genes in Arabidopsis."
    Vandepoele K., Raes J., de Veylder L., Rouze P., Rombauts S., Inze D.
    Plant Cell 14:903-916(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.
  12. "Interaction of the Arabidopsis E2F and DP proteins confers their concomitant nuclear translocation and transactivation."
    Kosugi S., Ohashi Y.
    Plant Physiol. 128:833-843(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DPA AND DPB.
    Strain: cv. Columbia.
  13. "Constitutive E2F expression in tobacco plants exhibits altered cell cycle control and morphological change in a cell type-specific manner."
    Kosugi S., Ohashi Y.
    Plant Physiol. 132:2012-2022(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "The plant-specific cyclin-dependent kinase CDKB1;1 and transcription factor E2Fa-DPa control the balance of mitotically dividing and endoreduplicating cells in Arabidopsis."
    Boudolf V., Vlieghe K., Beemster G.T.S., Magyar Z., Torres Acosta J.A., Maes S., Van Der Schueren E., Inze D., De Veylder L.
    Plant Cell 16:2683-2692(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "Interplay between Arabidopsis activating factors E2Fb and E2Fa in cell cycle progression and development."
    Sozzani R., Maggio C., Varotto S., Canova S., Bergounioux C., Albani D., Cella R.
    Plant Physiol. 140:1355-1366(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "Dissecting regulatory pathways of G1/S control in Arabidopsis: common and distinct targets of CYCD3;1, E2Fa and E2Fc."
    de Jager S.M., Scofield S., Huntley R.P., Robinson A.S., den Boer B.G., Murray J.A.
    Plant Mol. Biol. 71:345-365(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiE2FA_ARATH
AccessioniPrimary (citable) accession number: Q9FNY0
Secondary accession number(s): Q9C5B5
, Q9FV69, Q9M454, Q9SJ49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: March 1, 2001
Last modified: May 11, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  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.