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Protein

Transcription factor E2F2

Gene

E2F2

Organism
Homo sapiens (Human)
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. E2F2 binds specifically to RB1 in a cell-cycle dependent manner.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi107 – 19690Sequence AnalysisAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Cell cycle, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_1181. Association of licensing factors with the pre-replicative complex.
REACT_169325. Oncogene Induced Senescence.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_1707. CDC6 association with the ORC:origin complex.
REACT_821. Cyclin D associated events in G1.
SignaLinkiQ14209.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor E2F2
Short name:
E2F-2
Gene namesi
Name:E2F2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:3114. E2F2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27572.

Polymorphism and mutation databases

BioMutaiE2F2.
DMDMi2494228.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 437437Transcription factor E2F2PRO_0000219464Add
BLAST

Post-translational modificationi

Phosphorylated by CDK2 and cyclin A-CDK2 in the S-phase.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ14209.
PaxDbiQ14209.
PRIDEiQ14209.

PTM databases

PhosphoSiteiQ14209.

Expressioni

Tissue specificityi

Highest level of expression is found in placenta, low levels are found in lung. Found as well in many immortalized cell lines derived from tumor samples.

Gene expression databases

BgeeiQ14209.
CleanExiHS_E2F2.
GenevisibleiQ14209. HS.

Organism-specific databases

HPAiCAB016313.

Interactioni

Subunit structurei

Component of the DRTF1/E2F transcription factor complex. Forms heterodimers with DP family members. The E2F2 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. Viral oncoproteins, notably E1A, T-antigen and HPV E7, are capable of sequestering RB1, thus releasing the active complex. Binds EAPP.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
RB1P064003EBI-718476,EBI-491274

Protein-protein interaction databases

BioGridi108202. 22 interactions.
DIPiDIP-258N.
IntActiQ14209. 9 interactions.
MINTiMINT-249663.
STRINGi9606.ENSP00000355249.

Structurei

Secondary structure

1
437
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi422 – 4243Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N4MX-ray2.20C/D/E410-427[»]
ProteinModelPortaliQ14209.
SMRiQ14209. Positions 128-192, 205-306.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14209.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni65 – 10541Cyclin A/CDK2 bindingSequence AnalysisAdd
BLAST
Regioni155 – 17622Leucine-zipperAdd
BLAST
Regioni197 – 28993DimerizationSequence AnalysisAdd
BLAST
Regioni359 – 43779TransactivationSequence AnalysisAdd
BLAST
Regioni410 – 42718Retinoblastoma protein bindingSequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi160 – 19637DEF boxAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi360 – 3634Poly-Pro

Sequence similaritiesi

Belongs to the E2F/DP family.Curated

Phylogenomic databases

eggNOGiNOG289227.
GeneTreeiENSGT00550000074403.
HOGENOMiHOG000232045.
HOVERGENiHBG002227.
InParanoidiQ14209.
KOiK09389.
OMAiKELMSME.
OrthoDBiEOG738058.
PhylomeDBiQ14209.
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.

Q14209-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLQGPRALAS AAGQTPKVVP AMSPTELWPS GLSSPQLCPA TATYYTPLYP
60 70 80 90 100
QTAPPAAAPG TCLDATPHGP EGQVVRCLPA GRLPAKRKLD LEGIGRPVVP
110 120 130 140 150
EFPTPKGKCI RVDGLPSPKT PKSPGEKTRY DTSLGLLTKK FIYLLSESED
160 170 180 190 200
GVLDLNWAAE VLDVQKRRIY DITNVLEGIQ LIRKKAKNNI QWVGRGMFED
210 220 230 240 250
PTRPGKQQQL GQELKELMNT EQALDQLIQS CSLSFKHLTE DKANKRLAYV
260 270 280 290 300
TYQDIRAVGN FKEQTVIAVK APPQTRLEVP DRTEDNLQIY LKSTQGPIEV
310 320 330 340 350
YLCPEEVQEP DSPSEEPLPS TSTLCPSPDS AQPSSSTDPS IMEPTASSVP
360 370 380 390 400
APAPTPQQAP PPPSLVPLEA TDSLLELPHP LLQQTEDQFL SPTLACSSPL
410 420 430
ISFSPSLDQD DYLWGLEAGE GISDLFDSYD LGDLLIN
Length:437
Mass (Da):47,506
Last modified:November 1, 1996 - v1
Checksum:i60541F4235507005
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti205 – 2051G → R.1 Publication
Corresponds to variant rs2229297 [ dbSNP | Ensembl ].
VAR_018990
Natural varianti226 – 2261Q → H.2 Publications
Corresponds to variant rs2075995 [ dbSNP | Ensembl ].
VAR_018991

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L22846 mRNA. Translation: AAA16890.1.
AK313939 mRNA. Translation: BAG36658.1.
AF518877 Genomic DNA. Translation: AAM54044.1.
AL021154 Genomic DNA. Translation: CAA15949.1.
BC053676 mRNA. Translation: AAH53676.1.
CCDSiCCDS236.1.
PIRiA54595.
RefSeqiNP_004082.1. NM_004091.3.
UniGeneiHs.194333.

Genome annotation databases

EnsembliENST00000361729; ENSP00000355249; ENSG00000007968.
GeneIDi1870.
KEGGihsa:1870.
UCSCiuc001bhe.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L22846 mRNA. Translation: AAA16890.1.
AK313939 mRNA. Translation: BAG36658.1.
AF518877 Genomic DNA. Translation: AAM54044.1.
AL021154 Genomic DNA. Translation: CAA15949.1.
BC053676 mRNA. Translation: AAH53676.1.
CCDSiCCDS236.1.
PIRiA54595.
RefSeqiNP_004082.1. NM_004091.3.
UniGeneiHs.194333.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N4MX-ray2.20C/D/E410-427[»]
ProteinModelPortaliQ14209.
SMRiQ14209. Positions 128-192, 205-306.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108202. 22 interactions.
DIPiDIP-258N.
IntActiQ14209. 9 interactions.
MINTiMINT-249663.
STRINGi9606.ENSP00000355249.

PTM databases

PhosphoSiteiQ14209.

Polymorphism and mutation databases

BioMutaiE2F2.
DMDMi2494228.

Proteomic databases

MaxQBiQ14209.
PaxDbiQ14209.
PRIDEiQ14209.

Protocols and materials databases

DNASUi1870.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361729; ENSP00000355249; ENSG00000007968.
GeneIDi1870.
KEGGihsa:1870.
UCSCiuc001bhe.2. human.

Organism-specific databases

CTDi1870.
GeneCardsiGC01M023832.
HGNCiHGNC:3114. E2F2.
HPAiCAB016313.
MIMi600426. gene.
neXtProtiNX_Q14209.
PharmGKBiPA27572.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG289227.
GeneTreeiENSGT00550000074403.
HOGENOMiHOG000232045.
HOVERGENiHBG002227.
InParanoidiQ14209.
KOiK09389.
OMAiKELMSME.
OrthoDBiEOG738058.
PhylomeDBiQ14209.
TreeFamiTF105566.

Enzyme and pathway databases

ReactomeiREACT_1181. Association of licensing factors with the pre-replicative complex.
REACT_169325. Oncogene Induced Senescence.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_1707. CDC6 association with the ORC:origin complex.
REACT_821. Cyclin D associated events in G1.
SignaLinkiQ14209.

Miscellaneous databases

EvolutionaryTraceiQ14209.
GeneWikiiE2F2.
GenomeRNAii1870.
NextBioi7647.
PROiQ14209.
SOURCEiSearch...

Gene expression databases

BgeeiQ14209.
CleanExiHS_E2F2.
GenevisibleiQ14209. HS.

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 and characterization of E2F-2, a novel protein with the biochemical properties of transcription factor E2F."
    Ivey-Hoyle M., Conroy R., Huber H.E., Goodhart P.J., Oliff A., Heimbrook D.C.
    Mol. Cell. Biol. 13:7802-7812(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Cervix carcinoma.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. NIEHS SNPs program
    Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-205 AND HIS-226.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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], VARIANT HIS-226.
    Tissue: Eye.
  6. "Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism for phosphorylation-induced E2F release."
    Rubin S.M., Gall A.-L., Zheng N., Pavletich N.P.
    Cell 123:1093-1106(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WITH RB1 AND TFDP1.
  7. "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.
  8. "Structural basis for the recognition of the E2F transactivation domain by the retinoblastoma tumor suppressor."
    Lee C., Chang J.H., Lee H.S., Cho Y.
    Genes Dev. 16:3199-3212(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 410-427 IN COMPLEX WITH RB.

Entry informationi

Entry nameiE2F2_HUMAN
AccessioniPrimary (citable) accession number: Q14209
Secondary accession number(s): B2R9W1, Q7Z6H1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 24, 2015
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.