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Q14209

- E2F2_HUMAN

UniProt

Q14209 - E2F2_HUMAN

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Protein

Transcription factor E2F2

Gene

E2F2

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. core promoter binding Source: UniProtKB
  2. DNA binding Source: ProtInc
  3. sequence-specific DNA binding transcription factor activity Source: ProtInc
  4. transcription factor binding Source: UniProtKB

GO - Biological processi

  1. intrinsic apoptotic signaling pathway by p53 class mediator Source: Ensembl
  2. lens fiber cell apoptotic process Source: Ensembl
  3. mitotic cell cycle Source: Reactome
  4. regulation of cell cycle Source: Ensembl
  5. transcription initiation from RNA polymerase II promoter Source: ProtInc
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: Chromosome 1

Organism-specific databases

HGNCiHGNC:3114. E2F2.

Subcellular locationi

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
  2. transcription factor complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27572.

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.
GenevestigatoriQ14209.

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. 19 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 – 4243

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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_TDP.
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:
EMBL
GenBank
DDBJ
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.

Polymorphism databases

DMDMi2494228.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS236.1.
PIRi A54595.
RefSeqi NP_004082.1. NM_004091.3.
UniGenei Hs.194333.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1N4M X-ray 2.20 C/D/E 410-427 [» ]
ProteinModelPortali Q14209.
SMRi Q14209. Positions 128-192, 205-306.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108202. 19 interactions.
DIPi DIP-258N.
IntActi Q14209. 9 interactions.
MINTi MINT-249663.
STRINGi 9606.ENSP00000355249.

PTM databases

PhosphoSitei Q14209.

Polymorphism databases

DMDMi 2494228.

Proteomic databases

MaxQBi Q14209.
PaxDbi Q14209.
PRIDEi Q14209.

Protocols and materials databases

DNASUi 1870.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000361729 ; ENSP00000355249 ; ENSG00000007968 .
GeneIDi 1870.
KEGGi hsa:1870.
UCSCi uc001bhe.2. human.

Organism-specific databases

CTDi 1870.
GeneCardsi GC01M023832.
HGNCi HGNC:3114. E2F2.
HPAi CAB016313.
MIMi 600426. gene.
neXtProti NX_Q14209.
PharmGKBi PA27572.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG289227.
GeneTreei ENSGT00550000074403.
HOGENOMi HOG000232045.
HOVERGENi HBG002227.
InParanoidi Q14209.
KOi K09389.
OMAi KELMSME.
OrthoDBi EOG738058.
PhylomeDBi Q14209.
TreeFami TF105566.

Enzyme and pathway databases

Reactomei REACT_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.
SignaLinki Q14209.

Miscellaneous databases

EvolutionaryTracei Q14209.
GeneWikii E2F2.
GenomeRNAii 1870.
NextBioi 7647.
PROi Q14209.
SOURCEi Search...

Gene expression databases

Bgeei Q14209.
CleanExi HS_E2F2.
Genevestigatori Q14209.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
InterProi IPR015633. E2F.
IPR003316. E2F_TDP.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
PANTHERi PTHR12081. PTHR12081. 1 hit.
Pfami PF02319. E2F_TDP. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 137 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