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Q14209 (E2F2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription factor E2F2

Short name=E2F-2
Gene names
Name:E2F2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length437 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

Nucleus.

Tissue specificity

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.

Post-translational modification

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

Sequence similarities

Belongs to the E2F/DP family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RB1P064003EBI-718476,EBI-491274

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 437437Transcription factor E2F2
PRO_0000219464

Regions

DNA binding107 – 19690 Potential
Region65 – 10541Cyclin A/CDK2 binding Potential
Region155 – 17622Leucine-zipper
Region197 – 28993Dimerization Potential
Region359 – 43779Transactivation Potential
Region410 – 42718Retinoblastoma protein binding Potential
Motif160 – 19637DEF box
Compositional bias360 – 3634Poly-Pro

Natural variations

Natural variant2051G → R. Ref.3
Corresponds to variant rs2229297 [ dbSNP | Ensembl ].
VAR_018990
Natural variant2261Q → H. Ref.3 Ref.5
Corresponds to variant rs2075995 [ dbSNP | Ensembl ].
VAR_018991

Secondary structure

... 437
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q14209 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 60541F4235507005

FASTA43747,506
        10         20         30         40         50         60 
MLQGPRALAS AAGQTPKVVP AMSPTELWPS GLSSPQLCPA TATYYTPLYP QTAPPAAAPG 

        70         80         90        100        110        120 
TCLDATPHGP EGQVVRCLPA GRLPAKRKLD LEGIGRPVVP EFPTPKGKCI RVDGLPSPKT 

       130        140        150        160        170        180 
PKSPGEKTRY DTSLGLLTKK FIYLLSESED GVLDLNWAAE VLDVQKRRIY DITNVLEGIQ 

       190        200        210        220        230        240 
LIRKKAKNNI QWVGRGMFED PTRPGKQQQL GQELKELMNT EQALDQLIQS CSLSFKHLTE 

       250        260        270        280        290        300 
DKANKRLAYV TYQDIRAVGN FKEQTVIAVK APPQTRLEVP DRTEDNLQIY LKSTQGPIEV 

       310        320        330        340        350        360 
YLCPEEVQEP DSPSEEPLPS TSTLCPSPDS AQPSSSTDPS IMEPTASSVP APAPTPQQAP 

       370        380        390        400        410        420 
PPPSLVPLEA TDSLLELPHP LLQQTEDQFL SPTLACSSPL ISFSPSLDQD DYLWGLEAGE 

       430 
GISDLFDSYD LGDLLIN 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS236.1.
PIRA54595.
RefSeqNP_004082.1. NM_004091.3.
UniGeneHs.194333.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1N4MX-ray2.20C/D/E410-427[»]
ProteinModelPortalQ14209.
SMRQ14209. Positions 128-192, 205-306.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108202. 18 interactions.
DIPDIP-258N.
IntActQ14209. 8 interactions.
MINTMINT-249663.
STRING9606.ENSP00000355249.

PTM databases

PhosphoSiteQ14209.

Polymorphism databases

DMDM2494228.

Proteomic databases

PaxDbQ14209.
PRIDEQ14209.

Protocols and materials databases

DNASU1870.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361729; ENSP00000355249; ENSG00000007968.
GeneID1870.
KEGGhsa:1870.
UCSCuc001bhe.2. human.

Organism-specific databases

CTD1870.
GeneCardsGC01M023832.
HGNCHGNC:3114. E2F2.
HPACAB016313.
MIM600426. gene.
neXtProtNX_Q14209.
PharmGKBPA27572.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG289227.
HOGENOMHOG000232045.
HOVERGENHBG002227.
InParanoidQ14209.
KOK09389.
OMAKELMSME.
OrthoDBEOG738058.
PhylomeDBQ14209.
TreeFamTF105566.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_120956. Cellular responses to stress.
SignaLinkQ14209.

Gene expression databases

BgeeQ14209.
CleanExHS_E2F2.
GenevestigatorQ14209.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR015633. E2F.
IPR003316. E2F_TDP.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERPTHR12081. PTHR12081. 1 hit.
PfamPF02319. E2F_TDP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ14209.
GeneWikiE2F2.
GenomeRNAi1870.
NextBio7647.
PROQ14209.
SOURCESearch...

Entry information

Entry nameE2F2_HUMAN
AccessionPrimary (citable) accession number: Q14209
Secondary accession number(s): B2R9W1, Q7Z6H1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM