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Transcription factor Dp-1 (DRTF1-polypeptide 1) (DRTF1) (E2F dimerization partner 1)

 TFDP1_HUMAN             Reviewed;         410 AA.
Q14186; B4DLQ9; Q5JSB4; Q8IZL5;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 171.
RecName: Full=Transcription factor Dp-1;
AltName: Full=DRTF1-polypeptide 1;
Short=DRTF1;
AltName: Full=E2F dimerization partner 1;
Name=TFDP1; Synonyms=DP1;
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 1), FUNCTION, AND SUBUNIT.
PubMed=8405995; DOI=10.1101/gad.7.10.1850;
Helin K., Wu C.-L., Fattaey A.R., Lees J.A., Dynlacht B.D., Ngwu C.,
Harlow E.;
"Heterodimerization of the transcription factors E2F-1 and DP-1 leads
to cooperative trans-activation.";
Genes Dev. 7:1850-1861(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle;
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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-410.
NIEHS SNPs program;
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
[7]
PHOSPHORYLATION.
PubMed=8039504;
Bandara L.R., Lam E.W.-F., Soerensen T.S., Zamanian M., Girling R.,
la Thangue N.B.;
"DP-1: a cell cycle-regulated and phosphorylated component of
transcription factor DRTF1/E2F which is functionally important for
recognition by pRb and the adenovirus E4 orf 6/7 protein.";
EMBO J. 13:3104-3114(1994).
[8]
FUNCTION, AND SUBUNIT.
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).
[9]
IDENTIFICATION IN COMPLEX WITH E2F6; MAX; MGA; EUHMTASE1; BAT8; CBX3;
RING1; RNF2; MBLR; L3MBTL2 AND YAF2.
PubMed=12004135; DOI=10.1126/science.1069861;
Ogawa H., Ishiguro K., Gaubatz S., Livingston D.M., Nakatani Y.;
"A complex with chromatin modifiers that occupies E2F- and Myc-
responsive genes in G0 cells.";
Science 296:1132-1136(2002).
[10]
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).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND 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).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND 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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, 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).
-!- 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 (PubMed:8405995, PubMed:7739537). 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:0000269|PubMed:20176812, ECO:0000269|PubMed:7739537,
ECO:0000269|PubMed:8405995}.
-!- SUBUNIT: Component of the E2F:DP 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. This repression involves recruitment of
histone deacetylase (HDAC). During the cell cycle, from mid-to-
late G1 phase, RB family members become phosphorylated, detach
from the DRTF1/E2F complex to render E2F transcriptionally active.
Viral oncoproteins, notably E1A, T-antigen and HPV E7, are capable
of sequestering RB protein, thus releasing the active complex.
Part of the E2F6.com-1 complex in G0 phase is composed of E2F6,
MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR, L3MBTL2
YAF2. 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 TFDP1:E2F1 interacts
with CEBPA; the interaction prevents CEBPA binding to target gene
promoters and represses its transcriptional activity
(PubMed:20176812). {ECO:0000269|PubMed:12004135,
ECO:0000269|PubMed:17531812, ECO:0000269|PubMed:20176812,
ECO:0000269|PubMed:7739537, ECO:0000269|PubMed:8405995}.
-!- INTERACTION:
O14640:DVL1; NbExp=3; IntAct=EBI-749713, EBI-723489;
Q01094:E2F1; NbExp=10; IntAct=EBI-749713, EBI-448924;
Q16254:E2F4; NbExp=5; IntAct=EBI-749713, EBI-448943;
O75461:E2F6; NbExp=12; IntAct=EBI-749713, EBI-749694;
P61244:MAX; NbExp=4; IntAct=EBI-749713, EBI-751711;
Q9UBE8:NLK; NbExp=2; IntAct=EBI-749713, EBI-366978;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q08639}.
Cytoplasm {ECO:0000250|UniProtKB:Q08639}. Note=Shuttles between
the cytoplasm and nucleus and translocates into the nuclear
compartment upon heterodimerization with E2F1.
{ECO:0000250|UniProtKB:Q08639}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q14186-1; Sequence=Displayed;
Name=2;
IsoId=Q14186-2; Sequence=VSP_056499, VSP_056500;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highest levels in muscle. Also expressed in
brain, placenta, liver and kidney. Lower levels in lung and
pancreas. Not detected in heart.
-!- INDUCTION: Down-regulated during differentiation.
-!- PTM: Phosphorylation by E2F1-bound cyclin A-CDK2, in the S phase,
inhibits E2F-mediated DNA binding and transactivation.
{ECO:0000269|PubMed:8039504}.
-!- PTM: Ubiquitinated by the BCR(KBTBD5) complex, leading to its
subsequent degradation. {ECO:0000250|UniProtKB:Q08639}.
-!- MISCELLANEOUS: E2F/DP transactivation can be mediated by several
cofactors including TBP, TFIIH, MDM2 and CBP.
-!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/tfdp1/";
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EMBL; L23959; AAA58440.1; -; mRNA.
EMBL; AK297114; BAG59621.1; -; mRNA.
EMBL; AL442125; CAI39789.1; -; Genomic_DNA.
EMBL; CH471085; EAX09216.1; -; Genomic_DNA.
EMBL; BC011685; AAH11685.1; -; mRNA.
EMBL; AF550129; AAN46090.1; -; Genomic_DNA.
CCDS; CCDS9538.1; -. [Q14186-1]
PIR; A48585; A48585.
RefSeq; NP_009042.1; NM_007111.4. [Q14186-1]
RefSeq; XP_005268384.1; XM_005268327.1. [Q14186-1]
RefSeq; XP_005268388.1; XM_005268331.1. [Q14186-2]
UniGene; Hs.79353; -.
PDB; 2AZE; X-ray; 2.55 A; A=199-350.
PDB; 5GOW; NMR; -; A=392-410.
PDB; 5TUU; X-ray; 2.25 A; A=199-350.
PDB; 5TUV; X-ray; 2.90 A; A/D=199-350.
PDBsum; 2AZE; -.
PDBsum; 5GOW; -.
PDBsum; 5TUU; -.
PDBsum; 5TUV; -.
ProteinModelPortal; Q14186; -.
SMR; Q14186; -.
BioGrid; 112885; 46.
CORUM; Q14186; -.
DIP; DIP-238N; -.
IntAct; Q14186; 67.
MINT; MINT-3029193; -.
STRING; 9606.ENSP00000364519; -.
iPTMnet; Q14186; -.
PhosphoSitePlus; Q14186; -.
BioMuta; TFDP1; -.
DMDM; 3122926; -.
EPD; Q14186; -.
MaxQB; Q14186; -.
PaxDb; Q14186; -.
PeptideAtlas; Q14186; -.
PRIDE; Q14186; -.
DNASU; 7027; -.
Ensembl; ENST00000375370; ENSP00000364519; ENSG00000198176. [Q14186-1]
GeneID; 7027; -.
KEGG; hsa:7027; -.
UCSC; uc001vtw.4; human. [Q14186-1]
CTD; 7027; -.
DisGeNET; 7027; -.
EuPathDB; HostDB:ENSG00000198176.12; -.
GeneCards; TFDP1; -.
H-InvDB; HIX0002608; -.
H-InvDB; HIX0033825; -.
HGNC; HGNC:11749; TFDP1.
HPA; CAB033605; -.
HPA; HPA044754; -.
HPA; HPA068909; -.
MIM; 189902; gene.
neXtProt; NX_Q14186; -.
OpenTargets; ENSG00000198176; -.
PharmGKB; PA36464; -.
eggNOG; KOG2829; Eukaryota.
eggNOG; ENOG410Y9QP; LUCA.
GeneTree; ENSGT00390000018222; -.
HOGENOM; HOG000030696; -.
HOVERGEN; HBG009894; -.
InParanoid; Q14186; -.
KO; K04683; -.
OMA; HPSTVNT; -.
OrthoDB; EOG091G0AVY; -.
PhylomeDB; Q14186; -.
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.
SIGNOR; Q14186; -.
ChiTaRS; TFDP1; human.
EvolutionaryTrace; Q14186; -.
GeneWiki; TFDP1; -.
GenomeRNAi; 7027; -.
PRO; PR:Q14186; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000198176; -.
CleanEx; HS_TFDP1; -.
ExpressionAtlas; Q14186; baseline and differential.
Genevisible; Q14186; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005739; C:mitochondrion; IEA:GOC.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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; IEA:UniProtKB-KW.
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:0003713; F:transcription coactivator activity; TAS:ProtInc.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; TAS:ProtInc.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0043276; P:anoikis; IEA:Ensembl.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
GO; GO:0008544; P:epidermis development; IEA:Ensembl.
GO; GO:0070345; P:negative regulation of fat cell proliferation; ISS: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:2000278; P:regulation of DNA biosynthetic process; IEA:Ensembl.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
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; IPR028313; DP-1.
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:SF4; PTHR12548:SF4; 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; Cytoplasm; DNA-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 410 Transcription factor Dp-1.
/FTId=PRO_0000219475.
DNA_BIND 113 195 {ECO:0000255}.
REGION 105 127 Interaction with CEBPA.
{ECO:0000269|PubMed:20176812}.
REGION 204 277 Dimerization. {ECO:0000255}.
REGION 211 327 Enhances binding of RB protein to E2F.
REGION 214 246 DCB1.
REGION 259 315 DCB2.
MOTIF 161 195 DEF box.
COMPBIAS 250 253 Poly-Pro.
COMPBIAS 394 410 Asp/Glu-rich (acidic; NCB domain).
MOD_RES 3 3 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 23 23 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 103 MAKDAGLIEANGELKVFIDQNLSPGKGVVSLVAVHPSTVNP
LGKQLLPKTFGQSNVNIAQQVVIGTPQRPAASNTLVVGSPH
TPSTHFASQNQPSDSSPWSAG -> MSTLPSKW (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056499.
VAR_SEQ 358 361 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056500.
VARIANT 401 401 D -> N (in dbSNP:rs4150823).
/FTId=VAR_029293.
HELIX 199 247 {ECO:0000244|PDB:5TUU}.
STRAND 253 260 {ECO:0000244|PDB:5TUU}.
STRAND 262 267 {ECO:0000244|PDB:5TUU}.
STRAND 272 276 {ECO:0000244|PDB:5TUU}.
STRAND 280 289 {ECO:0000244|PDB:5TUU}.
STRAND 291 295 {ECO:0000244|PDB:5TUU}.
HELIX 296 303 {ECO:0000244|PDB:5TUU}.
TURN 304 308 {ECO:0000244|PDB:5TUU}.
HELIX 309 311 {ECO:0000244|PDB:5TUU}.
HELIX 316 324 {ECO:0000244|PDB:5TUU}.
HELIX 328 330 {ECO:0000244|PDB:5TUU}.
HELIX 331 337 {ECO:0000244|PDB:5TUU}.
SEQUENCE 410 AA; 45070 MW; 3FEEFE1E49FD9ED0 CRC64;
MAKDAGLIEA NGELKVFIDQ NLSPGKGVVS LVAVHPSTVN PLGKQLLPKT FGQSNVNIAQ
QVVIGTPQRP AASNTLVVGS PHTPSTHFAS QNQPSDSSPW SAGKRNRKGE KNGKGLRHFS
MKVCEKVQRK GTTSYNEVAD ELVAEFSAAD NHILPNESAY DQKNIRRRVY DALNVLMAMN
IISKEKKEIK WIGLPTNSAQ ECQNLEVERQ RRLERIKQKQ SQLQELILQQ IAFKNLVQRN
RHAEQQASRP PPPNSVIHLP FIIVNTSKKT VIDCSISNDK FEYLFNFDNT FEIHDDIEVL
KRMGMACGLE SGSCSAEDLK MARSLVPKAL EPYVTEMAQG TVGGVFITTA GSTSNGTRFS
ASDLTNGADG MLATSSNGSQ YSGSRVETPV SYVGEDDEED DDFNENDEDD


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