TFDP1_HUMAN
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 03-AUG-2022, entry version 203.
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=14; 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 AlphaFoldDB; Q14186; -.
DR SASBDB; Q14186; -.
DR SMR; Q14186; -.
DR BioGRID; 112885; 111.
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; 81.
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; 373 antibodies from 35 providers.
DR DNASU; 7027; -.
DR Ensembl; ENST00000375370.10; ENSP00000364519.4; ENSG00000198176.13. [Q14186-1]
DR GeneID; 7027; -.
DR KEGG; hsa:7027; -.
DR MANE-Select; ENST00000375370.10; ENSP00000364519.4; NM_007111.5; NP_009042.1.
DR UCSC; uc001vtw.4; human. [Q14186-1]
DR CTD; 7027; -.
DR DisGeNET; 7027; -.
DR GeneCards; TFDP1; -.
DR HGNC; HGNC:11749; TFDP1.
DR HPA; ENSG00000198176; Tissue enhanced (bone).
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 SignaLink; Q14186; -.
DR SIGNOR; Q14186; -.
DR BioGRID-ORCS; 7027; 425 hits in 1107 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 secondary oocyte and 205 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:0035189; C:Rb-E2F complex; IPI:ComplexPortal.
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:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0043276; P:anoikis; IEA:Ensembl.
DR GO; GO:0008544; P:epidermis development; IEA:Ensembl.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:ComplexPortal.
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:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IDA:ComplexPortal.
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
