Q14209 (E2F2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription factor E2F2
Short name=E2F-2

Gene names

Name:

E2F2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	437 AA.
Sequence status	Complete.
Protein existence	Evidence 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. E2F-2 binds specifically to RB1 protein, in a cell-cycle dependent manner.
Subunit structure	Component of the DRTF1/E2F transcription factor complex. Forms heterodimers with DP family members. The E2F-2 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 RB protein, 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.

Ontologies

Keywords
Biological process	Cell cycle Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Ligand	DNA-binding
Molecular function	Activator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	G1 phase of mitotic cell cycle Traceable author statement. Source: Reactome transcription initiation from RNA polymerase II promoter Traceable author statement. Source: ProtInc
Cellular component	transcription factor complex Inferred from electronic annotation. Source: InterPro
Molecular function	core promoter binding Inferred from direct assay. Source: UniProtKB sequence-specific DNA binding transcription factor activity Non-traceable author statement. Source: ProtInc transcription factor binding Inferred from physical interaction Ref.6. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 437

437

Transcription factor E2F2

PRO_0000219464

Regions

Domain

155 – 176

22

Leucine-zipper

DNA binding

107 – 196

90

Potential

Region

65 – 105

41

Cyclin A/CDK2 binding Potential

Region

197 – 289

93

Dimerization Potential

Region

359 – 437

79

Transactivation Potential

Region

410 – 427

18

Retinoblastoma protein binding Potential

Motif

160 – 196

37

DEF box

Compositional bias

360 – 363

4

Poly-Pro

Natural variations

Natural variant

205

1

G → R. Ref.3
Corresponds to variant rs2229297 [ dbSNP | Ensembl ].

VAR_018990

Natural variant

226

1

Q → H. Ref.3 Ref.5
Corresponds to variant rs2075995 [ dbSNP | Ensembl ].

VAR_018991

Secondary structure

1

.

.

.

437

Helix Strand Turn

Details...

Helix

422 – 424

3

Sequences

	Sequence		Length	Mass (Da)
	Q14209 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 60541F4235507005	FASTA	437	47,506
	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

References

	« Hide 'large scale' referencesShow '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: 8246995] [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: 14702039] [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: 16710414] [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: 15489334] [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: 16360038] [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: 15716352] [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: 12502741] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 410-427 IN COMPLEX WITH RB.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

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.

IPI

IPI00290548.

PIR

A54595.

RefSeq

NP_004082.1. NM_004091.3.

UniGene

Hs.194333.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1N4M	X-ray	2.20	C/D/E	410-427	[»]

ProteinModelPortal

Q14209.

SMR

Q14209. Positions 128-192, 206-306.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-258N.

IntAct

Q14209. 5 interactions.

MINT

MINT-249663.

STRING

Q14209.

PTM databases

PhosphoSite

Q14209.

Polymorphism databases

DMDM

2494228.

Proteomic databases

PRIDE

Q14209.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000361729; ENSP00000355249; ENSG00000007968.

GeneID

1870.

KEGG

hsa:1870.

UCSC

uc001bhe.1. human.

Organism-specific databases

CTD

1870.

GeneCards

GC01M023832.

H-InvDB

HIX0017689.

HGNC

HGNC:3114. E2F2.

HPA

CAB016313.

MIM

600426. gene.

neXtProt

NX_Q14209.

PharmGKB

PA27572.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG12779.

HOGENOM

HBG715983.

HOVERGEN

HBG002227.

InParanoid

Q14209.

OMA

DYLWGLE.

OrthoDB

EOG4THVTC.

PhylomeDB

Q14209.

Enzyme and pathway databases

Reactome

REACT_152. Cell Cycle, Mitotic.

Gene expression databases

ArrayExpress

Q14209.

Bgee

Q14209.

CleanEx

HS_E2F2.

Genevestigator

Q14209.

GermOnline

ENSG00000007968. Homo sapiens.

Family and domain databases

InterPro

IPR015633. E2F.
IPR003316. E2F_TDP.
IPR011991. WHTH_trsnscrt_rep_DNA-bd.
[Graphical view]

Gene3D

G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.

KO

K09389.

PANTHER

PTHR12081. E2F. 1 hit.

Pfam

PF02319. E2F_TDP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

7647.

SOURCE

Search...

Entry information

Entry name

E2F2_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.