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Transcription factor Dp-2 (E2F dimerization partner 2)

 TFDP2_HUMAN             Reviewed;         446 AA.
Q14188; B7Z8C8; B7Z8L5; D3DNG1; E9PFC3; F8WAI2; Q13331; Q14187;
Q6R754; Q8WU88; Q9UG28;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
30-MAY-2000, sequence version 2.
22-NOV-2017, entry version 172.
RecName: Full=Transcription factor Dp-2;
AltName: Full=E2F dimerization partner 2;
Name=TFDP2; Synonyms=DP2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DELTA), AND CHARACTERIZATION.
PubMed=7739537; DOI=10.1128/MCB.15.5.2536;
Wu C.-L., Zukerberg L.R., Ngwu C., Harlow E., Lees J.A.;
"In vivo association of E2F and DP family proteins.";
Mol. Cell. Biol. 15:2536-2546(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM EPSILON).
TISSUE=Kidney;
PubMed=7784053;
Zhang Y., Chellappan S.P.;
"Cloning and characterization of human DP2, a novel dimerization
partner of E2F.";
Oncogene 10:2085-2093(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-81.
NIEHS SNPs program;
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6 AND 7).
TISSUE=Thymus;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
TISSUE=Neuroblastoma;
Li W.B., Gruber C., Jessee J., Polayes D.;
"Full-length cDNA libraries and normalization.";
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM EPSILON).
TISSUE=Placenta;
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).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-102 (ISOFORM ALPHA).
Zhang Y., Chellappan S.P.;
"Transcriptional activation and expression of DP transcription factors
during cell cycle and TPA-induced U937 differentiation.";
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-418 (ISOFORM 8).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 62-79 (ISOFORM DELTA), AND ALTERNATIVE
SPLICING.
TISSUE=Keratinocyte;
PubMed=8755520; DOI=10.1073/pnas.93.15.7594;
Rogers K.T., Higgins P.D.R., Milla M.M., Phillips R.S., Horowitz J.M.;
"DP-2, a heterodimeric partner of E2F: identification and
characterization of DP-2 proteins expressed in vivo.";
Proc. Natl. Acad. Sci. U.S.A. 93:7594-7599(1996).
[12]
INTERACTION WITH WITH RB1 AND E2F4.
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).
[13]
IDENTIFICATION IN THE DREAM COMPLEX.
PubMed=17531812; DOI=10.1016/j.molcel.2007.04.015;
Litovchick L., Sadasivam S., Florens L., Zhu X., Swanson S.K.,
Velmurugan S., Chen R., Washburn M.P., Liu X.S., DeCaprio J.A.;
"Evolutionarily conserved multisubunit RBL2/p130 and E2F4 protein
complex represses human cell cycle-dependent genes in quiescence.";
Mol. Cell 26:539-551(2007).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
FUNCTION, AND INTERACTION WITH CEBPA.
PubMed=20176812; DOI=10.1128/MCB.01619-09;
Zaragoza K., Begay V., Schuetz A., Heinemann U., Leutz A.;
"Repression of transcriptional activity of C/EBPalpha by E2F-
dimerization partner complexes.";
Mol. Cell. Biol. 30:2293-2304(2010).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-122, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 121-215.
PubMed=10090723; DOI=10.1101/gad.13.6.666;
Zheng N., Fraenkel E., Pabo C.O., Pavletich N.P.;
"Structural basis of DNA recognition by the heterodimeric cell cycle
transcription factor E2F-DP.";
Genes Dev. 13:666-674(1999).
-!- FUNCTION: Can stimulate E2F-dependent transcription. Binds DNA
cooperatively with E2F family members 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 TFDP2:E2F complex functions in the control
of cell-cycle progression from G1 to S phase. The E2F1:DP complex
appears to mediate both cell proliferation and apoptosis. Blocks
adipocyte differentiation by repressing CEBPA binding to its
target gene promoters (PubMed:20176812).
{ECO:0000305|PubMed:20176812}.
-!- SUBUNIT: Component of the DRTF1/E2F transcription factor complex.
Forms heterodimers with E2F family members. The complex can
interact with hypophosphorylated retinoblastoma protein RB1 and
related proteins (RBL1 and RBL2) that inhibit the E2F
transactivation domain. During the cell cycle, RB 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.
Interacts with GMCL (By similarity). Component of the DREAM
complex (also named LINC complex) at least composed of E2F4, E2F5,
LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1
and TFDP2. The complex exists in quiescent cells where it
represses cell cycle-dependent genes. It dissociates in S phase
when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds to
MYBL2. The complex TFDP2:E2F1 interacts with CEBPA; the
interaction prevents CEBPA binding to target genes promoters and
represses its transcriptional activity (PubMed:20176812).
{ECO:0000250|UniProtKB:Q64163, ECO:0000269|PubMed:16360038,
ECO:0000269|PubMed:17531812}.
-!- INTERACTION:
O75461:E2F6; NbExp=8; IntAct=EBI-752268, EBI-749694;
P03129:E7 (xeno); NbExp=2; IntAct=EBI-752268, EBI-866453;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Name=Alpha; Synonyms=49 kDa;
IsoId=Q14188-1; Sequence=Displayed;
Name=Beta; Synonyms=43 kDa;
IsoId=Q14188-2; Sequence=VSP_001352, VSP_001353;
Note=Gene prediction based on similarity to mouse ortholog. No
experimental confirmation available.;
Name=Gamma;
IsoId=Q14188-3; Sequence=VSP_001352, VSP_001353, VSP_001354;
Note=Gene prediction based on similarity to mouse ortholog. No
experimental confirmation available.;
Name=Delta; Synonyms=48 kDa;
IsoId=Q14188-4; Sequence=VSP_001352;
Name=Epsilon;
IsoId=Q14188-5; Sequence=VSP_001352, VSP_001354;
Name=6;
IsoId=Q14188-6; Sequence=VSP_043140, VSP_043141;
Name=7;
IsoId=Q14188-7; Sequence=VSP_045455;
Note=No experimental confirmation available.;
Name=8;
IsoId=Q14188-8; Sequence=VSP_047415;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: High levels in heart and skeletal muscle. Also
found in placenta, kidney, brain, lung and liver. The presence as
well as the abundance of the different transcripts appear to vary
significantly in different tissues and cell lines.
-!- PTM: Ser-24 is probably phosphorylated by CDK2.
-!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAR89905.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAB45775.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/tfdp2/";
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EMBL; L40386; AAA69016.1; -; mRNA.
EMBL; U18422; AAB60378.1; -; mRNA.
EMBL; AY509596; AAR89905.1; ALT_SEQ; Genomic_DNA.
EMBL; AK303181; BAH13914.1; -; mRNA.
EMBL; AK303634; BAH14001.1; -; mRNA.
EMBL; CR597951; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AC108679; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC112504; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC128648; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC133435; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471052; EAW78977.1; -; Genomic_DNA.
EMBL; CH471052; EAW78981.1; -; Genomic_DNA.
EMBL; BC021113; AAH21113.1; -; mRNA.
EMBL; U75488; AAB37321.1; -; mRNA.
EMBL; AL080206; CAB45775.2; ALT_INIT; mRNA.
EMBL; U35117; AAC50642.1; -; mRNA.
CCDS; CCDS43159.1; -. [Q14188-5]
CCDS; CCDS54647.1; -. [Q14188-7]
CCDS; CCDS54648.1; -. [Q14188-8]
CCDS; CCDS54649.1; -. [Q14188-6]
CCDS; CCDS54650.1; -. [Q14188-1]
RefSeq; NP_001171609.1; NM_001178138.1. [Q14188-5]
RefSeq; NP_001171610.1; NM_001178139.1. [Q14188-1]
RefSeq; NP_001171611.1; NM_001178140.1. [Q14188-8]
RefSeq; NP_001171612.1; NM_001178141.1. [Q14188-6]
RefSeq; NP_001171613.1; NM_001178142.1. [Q14188-7]
RefSeq; NP_006277.1; NM_006286.4. [Q14188-5]
RefSeq; XP_016862580.1; XM_017007091.1. [Q14188-1]
RefSeq; XP_016862585.1; XM_017007096.1. [Q14188-5]
RefSeq; XP_016862586.1; XM_017007097.1. [Q14188-4]
RefSeq; XP_016862587.1; XM_017007098.1. [Q14188-5]
RefSeq; XP_016862588.1; XM_017007099.1. [Q14188-4]
UniGene; Hs.379018; -.
PDB; 1CF7; X-ray; 2.60 A; B=121-215.
PDBsum; 1CF7; -.
ProteinModelPortal; Q14188; -.
SMR; Q14188; -.
BioGrid; 112887; 16.
DIP; DIP-294N; -.
IntAct; Q14188; 10.
MINT; MINT-88143; -.
STRING; 9606.ENSP00000420616; -.
iPTMnet; Q14188; -.
PhosphoSitePlus; Q14188; -.
BioMuta; TFDP2; -.
DMDM; 8039810; -.
EPD; Q14188; -.
MaxQB; Q14188; -.
PaxDb; Q14188; -.
PeptideAtlas; Q14188; -.
PRIDE; Q14188; -.
DNASU; 7029; -.
Ensembl; ENST00000467072; ENSP00000418590; ENSG00000114126. [Q14188-5]
Ensembl; ENST00000477292; ENSP00000418971; ENSG00000114126. [Q14188-7]
Ensembl; ENST00000479040; ENSP00000417585; ENSG00000114126. [Q14188-4]
Ensembl; ENST00000486111; ENSP00000420599; ENSG00000114126. [Q14188-5]
Ensembl; ENST00000489671; ENSP00000420616; ENSG00000114126. [Q14188-1]
Ensembl; ENST00000495310; ENSP00000419036; ENSG00000114126. [Q14188-6]
Ensembl; ENST00000499676; ENSP00000439782; ENSG00000114126. [Q14188-8]
GeneID; 7029; -.
KEGG; hsa:7029; -.
UCSC; uc003euk.5; human. [Q14188-1]
CTD; 7029; -.
DisGeNET; 7029; -.
EuPathDB; HostDB:ENSG00000114126.17; -.
GeneCards; TFDP2; -.
HGNC; HGNC:11751; TFDP2.
HPA; CAB018396; -.
MIM; 602160; gene.
neXtProt; NX_Q14188; -.
OpenTargets; ENSG00000114126; -.
PharmGKB; PA36466; -.
eggNOG; KOG2829; Eukaryota.
eggNOG; ENOG410Y9QP; LUCA.
GeneTree; ENSGT00390000018222; -.
HOGENOM; HOG000030696; -.
HOVERGEN; HBG009894; -.
InParanoid; Q14188; -.
KO; K09392; -.
OMA; EGYITDM; -.
OrthoDB; EOG091G0AVY; -.
PhylomeDB; Q14188; -.
TreeFam; TF314396; -.
Reactome; R-HSA-111448; Activation of NOXA and translocation to mitochondria.
Reactome; R-HSA-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
Reactome; R-HSA-1362277; Transcription of E2F targets under negative control by DREAM complex.
Reactome; R-HSA-1362300; Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1.
Reactome; R-HSA-139915; Activation of PUMA and translocation to mitochondria.
Reactome; R-HSA-1538133; G0 and Early G1.
Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-2559585; Oncogene Induced Senescence.
Reactome; R-HSA-539107; Activation of E2F1 target genes at G1/S.
Reactome; R-HSA-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
Reactome; R-HSA-69202; Cyclin E associated events during G1/S transition.
Reactome; R-HSA-69231; Cyclin D associated events in G1.
Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry.
Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
ChiTaRS; TFDP2; human.
EvolutionaryTrace; Q14188; -.
GeneWiki; TFDP2; -.
GenomeRNAi; 7029; -.
PRO; PR:Q14188; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000114126; -.
CleanEx; HS_TFDP2; -.
ExpressionAtlas; Q14188; baseline and differential.
Genevisible; Q14188; HS.
GO; GO:0005739; C:mitochondrion; IEA:GOC.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; IDA:NTNU_SB.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0003712; F:transcription cofactor activity; TAS:ProtInc.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; NAS:ProtInc.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IBA:GO_Central.
GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; IEA:GOC.
CDD; cd14458; DP_DD; 1.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR028314; DP-2.
InterPro; IPR037241; E2F-DP_heterodim.
InterPro; IPR003316; E2F_WHTH_DNA-bd_dom.
InterPro; IPR014889; Transc_factor_DP_C.
InterPro; IPR015648; Transcrpt_fac_DP.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
PANTHER; PTHR12548; PTHR12548; 1.
PANTHER; PTHR12548:SF5; PTHR12548:SF5; 1.
Pfam; PF08781; DP; 1.
Pfam; PF02319; E2F_TDP; 1.
PIRSF; PIRSF009404; Transcription_factor_DP; 1.
SMART; SM01138; DP; 1.
SMART; SM01372; E2F_TDP; 1.
SUPFAM; SSF144074; SSF144074; 1.
SUPFAM; SSF46785; SSF46785; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
Cell cycle; Complete proteome; DNA-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Transcription;
Transcription regulation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 446 Transcription factor Dp-2.
/FTId=PRO_0000219477.
DNA_BIND 129 210 {ECO:0000255}.
REGION 60 82 Interaction with CEBPA.
{ECO:0000269|PubMed:20176812}.
REGION 219 292 Dimerization. {ECO:0000255}.
REGION 229 261 DCB1.
REGION 274 330 DCB2.
MOTIF 103 118 Nuclear localization signal.
{ECO:0000250}.
MOTIF 176 210 DEF box.
COMPBIAS 432 446 Asp/Glu-rich (acidic; NCB domain).
MOD_RES 2 2 N-acetylthreonine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 24 24 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 122 122 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 136 Missing (in isoform 7).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045455.
VAR_SEQ 1 62 MTAKNVGLTSTNAEVRGFIDQNLSPTKGNISFVAFPVSNTN
SPTKILPKTLGPINVNVGPQM -> MQPEGIIFEAENKPSP
GTESAGTFILDLSATSRT (in isoform 8).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_047415.
VAR_SEQ 1 61 Missing (in isoform Beta, isoform Gamma,
isoform Delta and isoform Epsilon).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7739537,
ECO:0000303|PubMed:7784053,
ECO:0000303|PubMed:8755520}.
/FTId=VSP_001352.
VAR_SEQ 1 6 MTAKNV -> MLDPKC (in isoform 6).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043140.
VAR_SEQ 7 103 Missing (in isoform 6).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043141.
VAR_SEQ 103 118 Missing (in isoform Beta and isoform
Gamma). {ECO:0000305}.
/FTId=VSP_001353.
VAR_SEQ 173 173 S -> SQ (in isoform Gamma and isoform
Epsilon). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7784053}.
/FTId=VSP_001354.
VARIANT 64 64 I -> T (in dbSNP:rs748095099).
/FTId=VAR_002272.
VARIANT 81 81 P -> S (in dbSNP:rs11569200).
{ECO:0000269|Ref.3}.
/FTId=VAR_020567.
CONFLICT 269 269 N -> S (in Ref. 4; BAH13914).
{ECO:0000305}.
HELIX 131 146 {ECO:0000244|PDB:1CF7}.
STRAND 147 149 {ECO:0000244|PDB:1CF7}.
HELIX 151 163 {ECO:0000244|PDB:1CF7}.
HELIX 170 172 {ECO:0000244|PDB:1CF7}.
HELIX 174 193 {ECO:0000244|PDB:1CF7}.
STRAND 204 206 {ECO:0000244|PDB:1CF7}.
SEQUENCE 446 AA; 49236 MW; 19A6C85BAD61DFF1 CRC64;
MTAKNVGLTS TNAEVRGFID QNLSPTKGNI SFVAFPVSNT NSPTKILPKT LGPINVNVGP
QMIISTPQRL TSSGSVLIGS PYTPAPAMVT QTHIAEATGW VPGDRKRARK FIDSDFSESK
RSKKGDKNGK GLRHFSMKVC EKVQRKGTTS YNEVADELVS EFTNSNNHLA ADSAYDQKNI
RRRVYDALNV LMAMNIISKE KKEIKWIGLP TNSAQECQNL EIEKQRRIER IKQKRAQLQE
LLLQQIAFKN LVQRNRQNEQ QNQGPPALNS TIQLPFIIIN TSRKTVIDCS ISSDKFEYLF
NFDNTFEIHD DIEVLKRMGM SFGLESGKCS LEDLKLAKSL VPKALEGYIT DISTGPSWLN
QGLLLNSTQS VSNLDLTTGA TLPQSSVNQG LCLDAEVALA TGQFLAPNSH QSSSAASHCS
ESRGETPCSF NDEDEEDDEE DSSSPE


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