Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Transcription factor E2F2 (E2F-2)

 E2F2_HUMAN              Reviewed;         437 AA.
Q14209; B2R9W1; Q7Z6H1;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 166.
RecName: Full=Transcription factor E2F2;
Short=E2F-2;
Name=E2F2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Cervix carcinoma;
PubMed=8246995; DOI=10.1128/MCB.13.12.7802;
Ivey-Hoyle M., Conroy R., Huber H.E., Goodhart P.J., Oliff A.,
Heimbrook D.C.;
"Cloning and characterization of E2F-2, a novel protein with the
biochemical properties of transcription factor E2F.";
Mol. Cell. Biol. 13:7802-7812(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-205 AND HIS-226.
NIEHS SNPs program;
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-226.
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
INTERACTION WITH WITH RB1 AND TFDP1.
PubMed=16360038; DOI=10.1016/j.cell.2005.09.044;
Rubin S.M., Gall A.-L., Zheng N., Pavletich N.P.;
"Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism
for phosphorylation-induced E2F release.";
Cell 123:1093-1106(2005).
[7]
INTERACTION WITH EAPP.
PubMed=15716352; DOI=10.1091/mbc.E04-11-0975;
Novy M., Pohn R., Andorfer P., Novy-Weiland T., Galos B.,
Schwarzmayr L., Rotheneder H.;
"EAPP, a novel E2F binding protein that modulates E2F-dependent
transcription.";
Mol. Biol. Cell 16:2181-2190(2005).
[8]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 410-427 IN COMPLEX WITH RB.
PubMed=12502741; DOI=10.1101/gad.1046102;
Lee C., Chang J.H., Lee H.S., Cho Y.;
"Structural basis for the recognition of the E2F transactivation
domain by the retinoblastoma tumor suppressor.";
Genes Dev. 16:3199-3212(2002).
-!- 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: 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.
{ECO:0000269|PubMed:12502741}.
-!- INTERACTION:
P06400:RB1; NbExp=3; IntAct=EBI-718476, EBI-491274;
-!- 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.
-!- PTM: Phosphorylated by CDK2 and cyclin A-CDK2 in the S-phase.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/e2f2/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L22846; AAA16890.1; -; mRNA.
EMBL; AK313939; BAG36658.1; -; mRNA.
EMBL; AF518877; AAM54044.1; -; Genomic_DNA.
EMBL; AL021154; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC053676; AAH53676.1; -; mRNA.
CCDS; CCDS236.1; -.
PIR; A54595; A54595.
RefSeq; NP_004082.1; NM_004091.3.
UniGene; Hs.194333; -.
PDB; 1N4M; X-ray; 2.20 A; C/D/E=410-427.
PDBsum; 1N4M; -.
ProteinModelPortal; Q14209; -.
SMR; Q14209; -.
BioGrid; 108202; 25.
DIP; DIP-258N; -.
ELM; Q14209; -.
IntAct; Q14209; 12.
MINT; MINT-249663; -.
STRING; 9606.ENSP00000355249; -.
iPTMnet; Q14209; -.
PhosphoSitePlus; Q14209; -.
BioMuta; E2F2; -.
DMDM; 2494228; -.
MaxQB; Q14209; -.
PaxDb; Q14209; -.
PeptideAtlas; Q14209; -.
PRIDE; Q14209; -.
DNASU; 1870; -.
Ensembl; ENST00000361729; ENSP00000355249; ENSG00000007968.
Ensembl; ENST00000634683; ENSP00000489612; ENSG00000282899.
GeneID; 1870; -.
KEGG; hsa:1870; -.
UCSC; uc001bhe.3; human.
CTD; 1870; -.
DisGeNET; 1870; -.
EuPathDB; HostDB:ENSG00000007968.6; -.
GeneCards; E2F2; -.
HGNC; HGNC:3114; E2F2.
HPA; CAB016313; -.
MIM; 600426; gene.
neXtProt; NX_Q14209; -.
OpenTargets; ENSG00000007968; -.
PharmGKB; PA27572; -.
eggNOG; KOG2577; Eukaryota.
eggNOG; ENOG410XNYI; LUCA.
GeneTree; ENSGT00550000074403; -.
HOGENOM; HOG000232045; -.
HOVERGEN; HBG002227; -.
InParanoid; Q14209; -.
KO; K09389; -.
OMA; NWATEVL; -.
OrthoDB; EOG091G087U; -.
PhylomeDB; Q14209; -.
TreeFam; TF105566; -.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-2559585; Oncogene Induced Senescence.
Reactome; R-HSA-68689; CDC6 association with the ORC:origin complex.
Reactome; R-HSA-69231; Cyclin D associated events in G1.
Reactome; R-HSA-69298; Association of licensing factors with the pre-replicative complex.
SignaLink; Q14209; -.
SIGNOR; Q14209; -.
EvolutionaryTrace; Q14209; -.
GeneWiki; E2F2; -.
GenomeRNAi; 1870; -.
PRO; PR:Q14209; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000007968; -.
CleanEx; HS_E2F2; -.
Genevisible; Q14209; HS.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; IDA:NTNU_SB.
GO; GO:0001047; F:core promoter binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; NAS:ProtInc.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IC:NTNU_SB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IEA:Ensembl.
GO; GO:1990086; P:lens fiber cell apoptotic process; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:ProtInc.
CDD; cd14660; E2F_DD; 1.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR015633; E2F.
InterPro; IPR037241; E2F-DP_heterodim.
InterPro; IPR032198; E2F_CC-MB.
InterPro; IPR003316; E2F_WHTH_DNA-bd_dom.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
PANTHER; PTHR12081; PTHR12081; 1.
Pfam; PF16421; E2F_CC-MB; 1.
Pfam; PF02319; E2F_TDP; 1.
SMART; SM01372; E2F_TDP; 1.
SUPFAM; SSF144074; SSF144074; 1.
SUPFAM; SSF46785; SSF46785; 1.
1: Evidence at protein level;
3D-structure; Activator; Cell cycle; Complete proteome; DNA-binding;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Transcription; Transcription regulation.
CHAIN 1 437 Transcription factor E2F2.
/FTId=PRO_0000219464.
DNA_BIND 107 196 {ECO:0000255}.
REGION 65 105 Cyclin A/CDK2 binding. {ECO:0000255}.
REGION 155 176 Leucine-zipper.
REGION 197 289 Dimerization. {ECO:0000255}.
REGION 359 437 Transactivation. {ECO:0000255}.
REGION 410 427 Retinoblastoma protein binding.
{ECO:0000255}.
MOTIF 160 196 DEF box.
COMPBIAS 360 363 Poly-Pro.
VARIANT 205 205 G -> R (in dbSNP:rs2229297).
{ECO:0000269|Ref.3}.
/FTId=VAR_018990.
VARIANT 226 226 Q -> H (in dbSNP:rs2075995).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.3}.
/FTId=VAR_018991.
HELIX 422 424 {ECO:0000244|PDB:1N4M}.
SEQUENCE 437 AA; 47506 MW; 60541F4235507005 CRC64;
MLQGPRALAS AAGQTPKVVP AMSPTELWPS GLSSPQLCPA TATYYTPLYP QTAPPAAAPG
TCLDATPHGP EGQVVRCLPA GRLPAKRKLD LEGIGRPVVP EFPTPKGKCI RVDGLPSPKT
PKSPGEKTRY DTSLGLLTKK FIYLLSESED GVLDLNWAAE VLDVQKRRIY DITNVLEGIQ
LIRKKAKNNI QWVGRGMFED PTRPGKQQQL GQELKELMNT EQALDQLIQS CSLSFKHLTE
DKANKRLAYV TYQDIRAVGN FKEQTVIAVK APPQTRLEVP DRTEDNLQIY LKSTQGPIEV
YLCPEEVQEP DSPSEEPLPS TSTLCPSPDS AQPSSSTDPS IMEPTASSVP APAPTPQQAP
PPPSLVPLEA TDSLLELPHP LLQQTEDQFL SPTLACSSPL ISFSPSLDQD DYLWGLEAGE
GISDLFDSYD LGDLLIN


Related products :

Catalog number Product name Quantity
E2F2_MOUSE ELISA Kit FOR Transcription factor E2F2; organism: Mouse; gene name: E2f2 96T
CSB-EL007341HU Human Transcription factor E2F2(E2F2) ELISA kit SpeciesHuman 96T
EIAAB12256 E2F2,E2F-2,Homo sapiens,Human,Transcription factor E2F2
CSB-EL007341MO Mouse Transcription factor E2F2(E2F2) ELISA kit SpeciesMouse 96T
E2F2-201AP E2F transcription factor 2 WB control: PC-E2F2 Host: Rabbit Affinity purifed 100-150ul
E2F2-201AP PC-E2F2 (WB control) E2F transcription factor 2 Immunogen: peptide (16mer) Host: Rabbit 100-150ul
E2F2-201AP E2F transcription factor 2 Antigenic peptide: P-E2F2 Host: Rabbit Affinity purifed 100ul
CSB-EL007341HU Human Transcription factor E2F2(E2F2) ELISA kit 96T
H7222 Transcription factor E2F2 (E2F2), Human, ELISA Kit 96T
EIAAB12255 E2f2,E2F-2,Mouse,Mus musculus,Transcription factor E2F2
CSB-EL007341MO Mouse Transcription factor E2F2(E2F2) ELISA kit 96T
H7223 Transcription factor E2F2 (E2F2), Mouse, ELISA Kit 96T
DL-E2F2-Hu Human E2F Transcription Factor 2 (E2F2) ELISA Kit 96T
E2F2-201AP E2F2-FITC (FITC-conjugates) E2F transcription factor 2 Immunogen: peptide (16mer) Host: Rabbit 200ul
E2F2-201AP E2F2-Biotin (Biotin Conjugates) E2F transcription factor 2 Immunogen: peptide (16mer) Host: Rabbit 200ul
E2F2-201AP E2F transcription factor 2 Biotin Conjugates: E2F2-Biotin Host: Rabbit Affinity purifed 200ul
E2F2-201AP E2F transcription factor 2 FITC-conjugates: E2F2-FITC Host: Rabbit Affinity purifed 200ul
E2F2-201AP P-E2F2 (Antigenic peptide) E2F transcription factor 2 Immunogen: peptide (16mer) Host: Rabbit 100ul
PC-E2F2 E2F transcription factor 2, WB control 100-150ul
E2F4 E2F2 Gene E2F transcription factor 2
15-288-21187 Transcription factor E2F2 - E2F-2 Polyclonal 0.1 mg
18-003-43067 Transcription factor E2F2 - E2F-2 Polyclonal 0.05 mg Aff Pur
15-288-21187 Transcription factor E2F2 - E2F-2 Polyclonal 0.05 mg
E2F2_HUMAN Human ELISA Kit FOR Transcription factor E2F2 96T
GWB-BBA2CF Anti- E2F2 (E2F transcription factor 2) Antibody


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur