GenomeNet

Database: UniProt
Entry: Q14186
LinkDB: Q14186
Original site: Q14186 
ID   TFDP1_HUMAN             Reviewed;         410 AA.
AC   Q14186; B4DLQ9; Q5JSB4; Q8IZL5;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   29-SEP-2021, entry version 200.
DE   RecName: Full=Transcription factor Dp-1;
DE   AltName: Full=DRTF1-polypeptide 1;
DE            Short=DRTF1;
DE   AltName: Full=E2F dimerization partner 1;
GN   Name=TFDP1; Synonyms=DP1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBUNIT.
RX   PubMed=8405995; DOI=10.1101/gad.7.10.1850;
RA   Helin K., Wu C.-L., Fattaey A.R., Lees J.A., Dynlacht B.D., Ngwu C.,
RA   Harlow E.;
RT   "Heterodimerization of the transcription factors E2F-1 and DP-1 leads to
RT   cooperative trans-activation.";
RL   Genes Dev. 7:1850-1861(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057823; DOI=10.1038/nature02379;
RA   Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA   Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA   Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA   Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA   Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA   Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA   Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA   Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA   Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA   Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA   Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA   Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA   Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA   Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA   Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA   Rogers J., Ross M.T.;
RT   "The DNA sequence and analysis of human chromosome 13.";
RL   Nature 428:522-528(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Muscle;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-410.
RG   NIEHS SNPs program;
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   PHOSPHORYLATION.
RX   PubMed=8039504; DOI=10.1002/j.1460-2075.1994.tb06609.x;
RA   Bandara L.R., Lam E.W.-F., Soerensen T.S., Zamanian M., Girling R.,
RA   la Thangue N.B.;
RT   "DP-1: a cell cycle-regulated and phosphorylated component of transcription
RT   factor DRTF1/E2F which is functionally important for recognition by pRb and
RT   the adenovirus E4 orf 6/7 protein.";
RL   EMBO J. 13:3104-3114(1994).
RN   [8]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=7739537; DOI=10.1128/mcb.15.5.2536;
RA   Wu C.-L., Zukerberg L.R., Ngwu C., Harlow E., Lees J.A.;
RT   "In vivo association of E2F and DP family proteins.";
RL   Mol. Cell. Biol. 15:2536-2546(1995).
RN   [9]
RP   IDENTIFICATION IN COMPLEX WITH E2F6; MAX; MGA; EUHMTASE1; BAT8; CBX3;
RP   RING1; RNF2; MBLR; L3MBTL2 AND YAF2.
RX   PubMed=12004135; DOI=10.1126/science.1069861;
RA   Ogawa H., Ishiguro K., Gaubatz S., Livingston D.M., Nakatani Y.;
RT   "A complex with chromatin modifiers that occupies E2F- and Myc-responsive
RT   genes in G0 cells.";
RL   Science 296:1132-1136(2002).
RN   [10]
RP   IDENTIFICATION IN THE DREAM COMPLEX.
RX   PubMed=17531812; DOI=10.1016/j.molcel.2007.04.015;
RA   Litovchick L., Sadasivam S., Florens L., Zhu X., Swanson S.K.,
RA   Velmurugan S., Chen R., Washburn M.P., Liu X.S., DeCaprio J.A.;
RT   "Evolutionarily conserved multisubunit RBL2/p130 and E2F4 protein complex
RT   represses human cell cycle-dependent genes in quiescence.";
RL   Mol. Cell 26:539-551(2007).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [14]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [15]
RP   FUNCTION, AND INTERACTION WITH CEBPA.
RX   PubMed=20176812; DOI=10.1128/mcb.01619-09;
RA   Zaragoza K., Begay V., Schuetz A., Heinemann U., Leutz A.;
RT   "Repression of transcriptional activity of C/EBPalpha by E2F-dimerization
RT   partner complexes.";
RL   Mol. Cell. Biol. 30:2293-2304(2010).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
CC   -!- FUNCTION: Can stimulate E2F-dependent transcription. Binds DNA
CC       cooperatively with E2F family members through the E2 recognition site,
CC       5'-TTTC[CG]CGC-3', found in the promoter region of a number of genes
CC       whose products are involved in cell cycle regulation or in DNA
CC       replication (PubMed:8405995, PubMed:7739537). The E2F1:DP complex
CC       appears to mediate both cell proliferation and apoptosis. Blocks
CC       adipocyte differentiation by repressing CEBPA binding to its target
CC       gene promoters (PubMed:20176812). {ECO:0000269|PubMed:20176812,
CC       ECO:0000269|PubMed:7739537, ECO:0000269|PubMed:8405995}.
CC   -!- SUBUNIT: Component of the E2F:DP transcription factor complex. Forms
CC       heterodimers with E2F family members. The complex can interact with
CC       hypophosphorylated retinoblastoma protein RB1 and related proteins
CC       (RBL1 and RBL2) that inhibit the E2F transactivation domain. This
CC       repression involves recruitment of histone deacetylase (HDAC). During
CC       the cell cycle, from mid-to-late G1 phase, RB family members become
CC       phosphorylated, detach from the DRTF1/E2F complex to render E2F
CC       transcriptionally active. Viral oncoproteins, notably E1A, T-antigen
CC       and HPV E7, are capable of sequestering RB protein, thus releasing the
CC       active complex. Part of the E2F6.com-1 complex in G0 phase is composed
CC       of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR,
CC       L3MBTL2 YAF2. Component of the DREAM complex (also named LINC complex)
CC       at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1,
CC       MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in
CC       quiescent cells where it represses cell cycle-dependent genes. It
CC       dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a
CC       subcomplex that binds to MYBL2. The complex TFDP1:E2F1 interacts with
CC       CEBPA; the interaction prevents CEBPA binding to target gene promoters
CC       and represses its transcriptional activity (PubMed:20176812).
CC       {ECO:0000269|PubMed:12004135, ECO:0000269|PubMed:17531812,
CC       ECO:0000269|PubMed:20176812, ECO:0000269|PubMed:7739537,
CC       ECO:0000269|PubMed:8405995}.
CC   -!- INTERACTION:
CC       Q14186; O14640: DVL1; NbExp=3; IntAct=EBI-749713, EBI-723489;
CC       Q14186; Q01094: E2F1; NbExp=12; IntAct=EBI-749713, EBI-448924;
CC       Q14186; Q14209: E2F2; NbExp=3; IntAct=EBI-749713, EBI-718476;
CC       Q14186; Q16254: E2F4; NbExp=7; IntAct=EBI-749713, EBI-448943;
CC       Q14186; O75461: E2F6; NbExp=22; IntAct=EBI-749713, EBI-749694;
CC       Q14186; P61244: MAX; NbExp=5; IntAct=EBI-749713, EBI-751711;
CC       Q14186; Q9UBE8: NLK; NbExp=2; IntAct=EBI-749713, EBI-366978;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q08639}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q08639}. Note=Shuttles between the cytoplasm and
CC       nucleus and translocates into the nuclear compartment upon
CC       heterodimerization with E2F1. {ECO:0000250|UniProtKB:Q08639}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q14186-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q14186-2; Sequence=VSP_056499, VSP_056500;
CC   -!- TISSUE SPECIFICITY: Highest levels in muscle. Also expressed in brain,
CC       placenta, liver and kidney. Lower levels in lung and pancreas. Not
CC       detected in heart.
CC   -!- INDUCTION: Down-regulated during differentiation.
CC   -!- PTM: Phosphorylation by E2F1-bound cyclin A-CDK2, in the S phase,
CC       inhibits E2F-mediated DNA binding and transactivation.
CC       {ECO:0000269|PubMed:8039504}.
CC   -!- PTM: Ubiquitinated by the BCR(KBTBD5) complex, leading to its
CC       subsequent degradation. {ECO:0000250|UniProtKB:Q08639}.
CC   -!- MISCELLANEOUS: E2F/DP transactivation can be mediated by several
CC       cofactors including TBP, TFIIH, MDM2 and CBP.
CC   -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/tfdp1/";
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DR   EMBL; L23959; AAA58440.1; -; mRNA.
DR   EMBL; AK297114; BAG59621.1; -; mRNA.
DR   EMBL; AL442125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471085; EAX09216.1; -; Genomic_DNA.
DR   EMBL; BC011685; AAH11685.1; -; mRNA.
DR   EMBL; AF550129; AAN46090.1; -; Genomic_DNA.
DR   CCDS; CCDS9538.1; -. [Q14186-1]
DR   PIR; A48585; A48585.
DR   RefSeq; NP_009042.1; NM_007111.4. [Q14186-1]
DR   RefSeq; XP_005268384.1; XM_005268327.1. [Q14186-1]
DR   RefSeq; XP_005268388.1; XM_005268331.1.
DR   PDB; 2AZE; X-ray; 2.55 A; A=199-350.
DR   PDB; 5GOW; NMR; -; A=392-410.
DR   PDB; 5TUU; X-ray; 2.25 A; A=199-350.
DR   PDB; 5TUV; X-ray; 2.90 A; A/D=199-350.
DR   PDBsum; 2AZE; -.
DR   PDBsum; 5GOW; -.
DR   PDBsum; 5TUU; -.
DR   PDBsum; 5TUV; -.
DR   SMR; Q14186; -.
DR   BioGRID; 112885; 89.
DR   ComplexPortal; CPX-155; RB1-E2F1-TFDP1 transcription repressor complex.
DR   ComplexPortal; CPX-175; RB1-E2F2-TFDP1 transcription repressor complex.
DR   ComplexPortal; CPX-1971; E2F1-DP1 transcription factor complex.
DR   ComplexPortal; CPX-1972; E2F2-DP1 transcription factor complex.
DR   CORUM; Q14186; -.
DR   DIP; DIP-238N; -.
DR   IntAct; Q14186; 71.
DR   MINT; Q14186; -.
DR   STRING; 9606.ENSP00000364519; -.
DR   ChEMBL; CHEMBL4523289; -.
DR   iPTMnet; Q14186; -.
DR   PhosphoSitePlus; Q14186; -.
DR   BioMuta; TFDP1; -.
DR   DMDM; 3122926; -.
DR   EPD; Q14186; -.
DR   jPOST; Q14186; -.
DR   MassIVE; Q14186; -.
DR   MaxQB; Q14186; -.
DR   PaxDb; Q14186; -.
DR   PeptideAtlas; Q14186; -.
DR   PRIDE; Q14186; -.
DR   ProteomicsDB; 4551; -.
DR   ProteomicsDB; 59904; -. [Q14186-1]
DR   Antibodypedia; 11828; 370 antibodies.
DR   DNASU; 7027; -.
DR   Ensembl; ENST00000375370; ENSP00000364519; ENSG00000198176. [Q14186-1]
DR   GeneID; 7027; -.
DR   KEGG; hsa:7027; -.
DR   UCSC; uc001vtw.4; human. [Q14186-1]
DR   CTD; 7027; -.
DR   DisGeNET; 7027; -.
DR   GeneCards; TFDP1; -.
DR   HGNC; HGNC:11749; TFDP1.
DR   HPA; ENSG00000198176; Low tissue specificity.
DR   MIM; 189902; gene.
DR   neXtProt; NX_Q14186; -.
DR   OpenTargets; ENSG00000198176; -.
DR   PharmGKB; PA36464; -.
DR   VEuPathDB; HostDB:ENSG00000198176; -.
DR   eggNOG; KOG2829; Eukaryota.
DR   GeneTree; ENSGT00940000154652; -.
DR   HOGENOM; CLU_039874_3_1_1; -.
DR   InParanoid; Q14186; -.
DR   OMA; FSTTDNH; -.
DR   OrthoDB; 1046304at2759; -.
DR   PhylomeDB; Q14186; -.
DR   TreeFam; TF314396; -.
DR   PathwayCommons; Q14186; -.
DR   Reactome; R-HSA-111448; Activation of NOXA and translocation to mitochondria.
DR   Reactome; R-HSA-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR   Reactome; R-HSA-1362277; Transcription of E2F targets under negative control by DREAM complex.
DR   Reactome; R-HSA-1362300; Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1.
DR   Reactome; R-HSA-139915; Activation of PUMA and translocation to mitochondria.
DR   Reactome; R-HSA-1538133; G0 and Early G1.
DR   Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
DR   Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR   Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
DR   Reactome; R-HSA-2559585; Oncogene Induced Senescence.
DR   Reactome; R-HSA-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
DR   Reactome; R-HSA-69202; Cyclin E associated events during G1/S transition.
DR   Reactome; R-HSA-69205; G1/S-Specific Transcription.
DR   Reactome; R-HSA-69231; Cyclin D associated events in G1.
DR   Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR   Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
DR   Reactome; R-HSA-9616222; Transcriptional regulation of granulopoiesis.
DR   Reactome; R-HSA-9661069; Defective binding of RB1 mutants to E2F1,(E2F2, E2F3).
DR   SIGNOR; Q14186; -.
DR   BioGRID-ORCS; 7027; 418 hits in 1041 CRISPR screens.
DR   ChiTaRS; TFDP1; human.
DR   EvolutionaryTrace; Q14186; -.
DR   GeneWiki; TFDP1; -.
DR   GenomeRNAi; 7027; -.
DR   Pharos; Q14186; Tbio.
DR   PRO; PR:Q14186; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   RNAct; Q14186; protein.
DR   Bgee; ENSG00000198176; Expressed in trabecular bone tissue and 247 other tissues.
DR   ExpressionAtlas; Q14186; baseline and differential.
DR   Genevisible; Q14186; HS.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:NTNU_SB.
DR   GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR   GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
DR   GO; GO:0043276; P:anoikis; IEA:Ensembl.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0008544; P:epidermis development; IEA:Ensembl.
DR   GO; GO:0070345; P:negative regulation of fat cell proliferation; ISS:UniProtKB.
DR   GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR   GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IDA:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:2000278; P:regulation of DNA biosynthetic process; IEA:Ensembl.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IMP:CACAO.
DR   CDD; cd14458; DP_DD; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 1.20.140.80; -; 1.
DR   IDEAL; IID00076; -.
DR   InterPro; IPR028313; DP-1.
DR   InterPro; IPR037241; E2F-DP_heterodim.
DR   InterPro; IPR003316; E2F_WHTH_DNA-bd_dom.
DR   InterPro; IPR038168; TF_DP_C_sf.
DR   InterPro; IPR014889; Transc_factor_DP_C.
DR   InterPro; IPR015648; Transcrpt_fac_DP.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR12548; PTHR12548; 1.
DR   PANTHER; PTHR12548:SF4; PTHR12548:SF4; 1.
DR   Pfam; PF08781; DP; 1.
DR   Pfam; PF02319; E2F_TDP; 1.
DR   PIRSF; PIRSF009404; Transcription_factor_DP; 1.
DR   SMART; SM01138; DP; 1.
DR   SMART; SM01372; E2F_TDP; 1.
DR   SUPFAM; SSF144074; SSF144074; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Activator; Alternative splicing; Cell cycle;
KW   Cytoplasm; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN           1..410
FT                   /note="Transcription factor Dp-1"
FT                   /id="PRO_0000219475"
FT   DNA_BIND        113..195
FT                   /evidence="ECO:0000255"
FT   REGION          73..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          105..127
FT                   /note="Interaction with CEBPA"
FT                   /evidence="ECO:0000269|PubMed:20176812"
FT   REGION          204..277
FT                   /note="Dimerization"
FT                   /evidence="ECO:0000255"
FT   REGION          211..327
FT                   /note="Enhances binding of RB protein to E2F"
FT   REGION          214..246
FT                   /note="DCB1"
FT   REGION          259..315
FT                   /note="DCB2"
FT   REGION          370..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           161..195
FT                   /note="DEF box"
FT   COMPBIAS        73..102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..387
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..410
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         3
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         23
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..103
FT                   /note="MAKDAGLIEANGELKVFIDQNLSPGKGVVSLVAVHPSTVNPLGKQLLPKTFG
FT                   QSNVNIAQQVVIGTPQRPAASNTLVVGSPHTPSTHFASQNQPSDSSPWSAG -> MSTL
FT                   PSKW (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056499"
FT   VAR_SEQ         358..361
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056500"
FT   VARIANT         401
FT                   /note="D -> N (in dbSNP:rs4150823)"
FT                   /id="VAR_029293"
FT   HELIX           199..247
FT                   /evidence="ECO:0007829|PDB:5TUU"
FT   STRAND          253..260
FT                   /evidence="ECO:0007829|PDB:5TUU"
FT   STRAND          262..267
FT                   /evidence="ECO:0007829|PDB:5TUU"
FT   STRAND          272..276
FT                   /evidence="ECO:0007829|PDB:5TUU"
FT   STRAND          280..289
FT                   /evidence="ECO:0007829|PDB:5TUU"
FT   STRAND          291..295
FT                   /evidence="ECO:0007829|PDB:5TUU"
FT   HELIX           296..303
FT                   /evidence="ECO:0007829|PDB:5TUU"
FT   TURN            304..308
FT                   /evidence="ECO:0007829|PDB:5TUU"
FT   HELIX           309..311
FT                   /evidence="ECO:0007829|PDB:5TUU"
FT   HELIX           316..324
FT                   /evidence="ECO:0007829|PDB:5TUU"
FT   HELIX           328..330
FT                   /evidence="ECO:0007829|PDB:5TUU"
FT   HELIX           331..337
FT                   /evidence="ECO:0007829|PDB:5TUU"
SQ   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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