TFDP2_HUMAN
ID TFDP2_HUMAN Reviewed; 446 AA.
AC Q14188; B7Z8C8; B7Z8L5; D3DNG1; E9PFC3; F8WAI2; Q13331; Q14187; Q6R754;
AC Q8WU88; Q9UG28;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Transcription factor Dp-2;
DE AltName: Full=E2F dimerization partner 2;
GN Name=TFDP2; Synonyms=DP2;
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 DELTA), AND CHARACTERIZATION.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM EPSILON).
RC TISSUE=Kidney;
RX PubMed=7784053;
RA Zhang Y., Chellappan S.P.;
RT "Cloning and characterization of human DP2, a novel dimerization partner of
RT E2F.";
RL Oncogene 10:2085-2093(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-81.
RG NIEHS SNPs program;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6 AND 7).
RC TISSUE=Thymus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RC TISSUE=Neuroblastoma;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [7]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM EPSILON).
RC TISSUE=Placenta;
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 [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-102 (ISOFORM ALPHA).
RA Zhang Y., Chellappan S.P.;
RT "Transcriptional activation and expression of DP transcription factors
RT during cell cycle and TPA-induced U937 differentiation.";
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-418 (ISOFORM 8).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 62-79 (ISOFORM DELTA), AND ALTERNATIVE
RP SPLICING.
RC TISSUE=Keratinocyte;
RX PubMed=8755520; DOI=10.1073/pnas.93.15.7594;
RA Rogers K.T., Higgins P.D.R., Milla M.M., Phillips R.S., Horowitz J.M.;
RT "DP-2, a heterodimeric partner of E2F: identification and characterization
RT of DP-2 proteins expressed in vivo.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:7594-7599(1996).
RN [12]
RP INTERACTION WITH RB1 AND E2F4.
RX PubMed=16360038; DOI=10.1016/j.cell.2005.09.044;
RA Rubin S.M., Gall A.-L., Zheng N., Pavletich N.P.;
RT "Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism for
RT phosphorylation-induced E2F release.";
RL Cell 123:1093-1106(2005).
RN [13]
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 [14]
RP IDENTIFICATION BY 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 [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 IDENTIFICATION BY 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 ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-122, AND
RP IDENTIFICATION BY 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).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 121-215.
RX PubMed=10090723; DOI=10.1101/gad.13.6.666;
RA Zheng N., Fraenkel E., Pabo C.O., Pavletich N.P.;
RT "Structural basis of DNA recognition by the heterodimeric cell cycle
RT transcription factor E2F-DP.";
RL Genes Dev. 13:666-674(1999).
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. The TFDP2:E2F complex functions in the control of cell-
CC cycle progression from G1 to S phase. The E2F1:DP complex appears to
CC mediate both cell proliferation and apoptosis. Blocks adipocyte
CC differentiation by repressing CEBPA binding to its target gene
CC promoters (PubMed:20176812). {ECO:0000305|PubMed:20176812}.
CC -!- SUBUNIT: Component of the DRTF1/E2F 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. During the
CC cell cycle, RB becomes phosphorylated in mid-to-late G1 phase, detaches
CC from the DRTF1/E2F complex rendering E2F transcriptionally active.
CC Viral oncoproteins, notably E1A, T-antigen and HPV E7, are capable of
CC sequestering RB protein, thus releasing the active complex. Interacts
CC with GMCL (By similarity). Component of the DREAM complex (also named
CC LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52,
CC LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex
CC exists in quiescent cells where it represses cell cycle-dependent
CC genes. It dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form
CC a subcomplex that binds to MYBL2. The complex TFDP2:E2F1 interacts with
CC CEBPA; the interaction prevents CEBPA binding to target genes promoters
CC and represses its transcriptional activity (PubMed:20176812).
CC {ECO:0000250|UniProtKB:Q64163, ECO:0000269|PubMed:16360038,
CC ECO:0000269|PubMed:17531812}.
CC -!- INTERACTION:
CC Q14188; O75461: E2F6; NbExp=9; IntAct=EBI-752268, EBI-749694;
CC Q14188; P03129: E7; Xeno; NbExp=2; IntAct=EBI-752268, EBI-866453;
CC Q14188-5; Q16254: E2F4; NbExp=3; IntAct=EBI-12181237, EBI-448943;
CC Q14188-5; O75461: E2F6; NbExp=11; IntAct=EBI-12181237, EBI-749694;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=Alpha; Synonyms=49 kDa;
CC IsoId=Q14188-1; Sequence=Displayed;
CC Name=Beta; Synonyms=43 kDa;
CC IsoId=Q14188-2; Sequence=VSP_001352, VSP_001353;
CC Name=Gamma;
CC IsoId=Q14188-3; Sequence=VSP_001352, VSP_001353, VSP_001354;
CC Name=Delta; Synonyms=48 kDa;
CC IsoId=Q14188-4; Sequence=VSP_001352;
CC Name=Epsilon;
CC IsoId=Q14188-5; Sequence=VSP_001352, VSP_001354;
CC Name=6;
CC IsoId=Q14188-6; Sequence=VSP_043140, VSP_043141;
CC Name=7;
CC IsoId=Q14188-7; Sequence=VSP_045455;
CC Name=8;
CC IsoId=Q14188-8; Sequence=VSP_047415;
CC -!- TISSUE SPECIFICITY: High levels in heart and skeletal muscle. Also
CC found in placenta, kidney, brain, lung and liver. The presence as well
CC as the abundance of the different transcripts appear to vary
CC significantly in different tissues and cell lines.
CC -!- PTM: Ser-24 is probably phosphorylated by CDK2.
CC -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAR89905.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB45775.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/tfdp2/";
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DR EMBL; L40386; AAA69016.1; -; mRNA.
DR EMBL; U18422; AAB60378.1; -; mRNA.
DR EMBL; AY509596; AAR89905.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK303181; BAH13914.1; -; mRNA.
DR EMBL; AK303634; BAH14001.1; -; mRNA.
DR EMBL; CR597951; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC108679; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC112504; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC128648; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC133435; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78977.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78981.1; -; Genomic_DNA.
DR EMBL; BC021113; AAH21113.1; -; mRNA.
DR EMBL; U75488; AAB37321.1; -; mRNA.
DR EMBL; AL080206; CAB45775.2; ALT_INIT; mRNA.
DR EMBL; U35117; AAC50642.1; -; mRNA.
DR CCDS; CCDS43159.1; -. [Q14188-5]
DR CCDS; CCDS54647.1; -. [Q14188-7]
DR CCDS; CCDS54648.1; -. [Q14188-8]
DR CCDS; CCDS54649.1; -. [Q14188-6]
DR CCDS; CCDS54650.1; -. [Q14188-1]
DR RefSeq; NP_001171609.1; NM_001178138.1. [Q14188-5]
DR RefSeq; NP_001171610.1; NM_001178139.1. [Q14188-1]
DR RefSeq; NP_001171611.1; NM_001178140.1. [Q14188-8]
DR RefSeq; NP_001171612.1; NM_001178141.1. [Q14188-6]
DR RefSeq; NP_001171613.1; NM_001178142.1. [Q14188-7]
DR RefSeq; NP_006277.1; NM_006286.4. [Q14188-5]
DR RefSeq; XP_016862580.1; XM_017007091.1. [Q14188-1]
DR RefSeq; XP_016862585.1; XM_017007096.1.
DR RefSeq; XP_016862586.1; XM_017007097.1.
DR RefSeq; XP_016862587.1; XM_017007098.1.
DR RefSeq; XP_016862588.1; XM_017007099.1.
DR PDB; 1CF7; X-ray; 2.60 A; B=121-215.
DR PDBsum; 1CF7; -.
DR AlphaFoldDB; Q14188; -.
DR SMR; Q14188; -.
DR BioGRID; 112887; 50.
DR DIP; DIP-294N; -.
DR IntAct; Q14188; 26.
DR MINT; Q14188; -.
DR STRING; 9606.ENSP00000420616; -.
DR BindingDB; Q14188; -.
DR ChEMBL; CHEMBL4105986; -.
DR iPTMnet; Q14188; -.
DR PhosphoSitePlus; Q14188; -.
DR BioMuta; TFDP2; -.
DR DMDM; 8039810; -.
DR EPD; Q14188; -.
DR jPOST; Q14188; -.
DR MassIVE; Q14188; -.
DR MaxQB; Q14188; -.
DR PaxDb; Q14188; -.
DR PeptideAtlas; Q14188; -.
DR PRIDE; Q14188; -.
DR ProteomicsDB; 20073; -.
DR ProteomicsDB; 30503; -.
DR ProteomicsDB; 59905; -. [Q14188-1]
DR ProteomicsDB; 59906; -. [Q14188-2]
DR ProteomicsDB; 59907; -. [Q14188-3]
DR ProteomicsDB; 59908; -. [Q14188-4]
DR ProteomicsDB; 59909; -. [Q14188-5]
DR ProteomicsDB; 59910; -. [Q14188-6]
DR Antibodypedia; 4341; 242 antibodies from 30 providers.
DR DNASU; 7029; -.
DR Ensembl; ENST00000467072.5; ENSP00000418590.1; ENSG00000114126.18. [Q14188-5]
DR Ensembl; ENST00000477292.5; ENSP00000418971.1; ENSG00000114126.18. [Q14188-7]
DR Ensembl; ENST00000479040.5; ENSP00000417585.1; ENSG00000114126.18. [Q14188-4]
DR Ensembl; ENST00000486111.5; ENSP00000420599.1; ENSG00000114126.18. [Q14188-5]
DR Ensembl; ENST00000489671.6; ENSP00000420616.1; ENSG00000114126.18. [Q14188-1]
DR Ensembl; ENST00000495310.5; ENSP00000419036.1; ENSG00000114126.18. [Q14188-6]
DR Ensembl; ENST00000499676.5; ENSP00000439782.2; ENSG00000114126.18. [Q14188-8]
DR GeneID; 7029; -.
DR KEGG; hsa:7029; -.
DR MANE-Select; ENST00000489671.6; ENSP00000420616.1; NM_001178139.2; NP_001171610.1.
DR UCSC; uc003euk.5; human. [Q14188-1]
DR CTD; 7029; -.
DR DisGeNET; 7029; -.
DR GeneCards; TFDP2; -.
DR HGNC; HGNC:11751; TFDP2.
DR HPA; ENSG00000114126; Tissue enhanced (lymphoid).
DR MIM; 602160; gene.
DR neXtProt; NX_Q14188; -.
DR OpenTargets; ENSG00000114126; -.
DR PharmGKB; PA36466; -.
DR VEuPathDB; HostDB:ENSG00000114126; -.
DR eggNOG; KOG2829; Eukaryota.
DR GeneTree; ENSGT00940000157909; -.
DR HOGENOM; CLU_039874_3_1_1; -.
DR InParanoid; Q14188; -.
DR OMA; TLEPINV; -.
DR OrthoDB; 1046304at2759; -.
DR PhylomeDB; Q14188; -.
DR TreeFam; TF314396; -.
DR PathwayCommons; Q14188; -.
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; Q14188; -.
DR BioGRID-ORCS; 7029; 14 hits in 1109 CRISPR screens.
DR ChiTaRS; TFDP2; human.
DR EvolutionaryTrace; Q14188; -.
DR GeneWiki; TFDP2; -.
DR GenomeRNAi; 7029; -.
DR Pharos; Q14188; Tbio.
DR PRO; PR:Q14188; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q14188; protein.
DR Bgee; ENSG00000114126; Expressed in calcaneal tendon and 195 other tissues.
DR ExpressionAtlas; Q14188; baseline and differential.
DR Genevisible; Q14188; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0072686; C:mitotic spindle; 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:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd14458; DP_DD; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.20.140.80; -; 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 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 DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..446
FT /note="Transcription factor Dp-2"
FT /id="PRO_0000219477"
FT DNA_BIND 129..210
FT /evidence="ECO:0000255"
FT REGION 60..82
FT /note="Interaction with CEBPA"
FT /evidence="ECO:0000269|PubMed:20176812"
FT REGION 219..292
FT /note="Dimerization"
FT /evidence="ECO:0000255"
FT REGION 229..261
FT /note="DCB1"
FT REGION 274..330
FT /note="DCB2"
FT REGION 409..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 103..118
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 176..210
FT /note="DEF box"
FT COMPBIAS 409..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..446
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..136
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045455"
FT VAR_SEQ 1..62
FT /note="MTAKNVGLTSTNAEVRGFIDQNLSPTKGNISFVAFPVSNTNSPTKILPKTLG
FT PINVNVGPQM -> MQPEGIIFEAENKPSPGTESAGTFILDLSATSRT (in
FT isoform 8)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_047415"
FT VAR_SEQ 1..61
FT /note="Missing (in isoform Beta, isoform Gamma, isoform
FT Delta and isoform Epsilon)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:7739537, ECO:0000303|PubMed:7784053,
FT ECO:0000303|PubMed:8755520"
FT /id="VSP_001352"
FT VAR_SEQ 1..6
FT /note="MTAKNV -> MLDPKC (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043140"
FT VAR_SEQ 7..103
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043141"
FT VAR_SEQ 103..118
FT /note="Missing (in isoform Beta and isoform Gamma)"
FT /evidence="ECO:0000305"
FT /id="VSP_001353"
FT VAR_SEQ 173
FT /note="S -> SQ (in isoform Gamma and isoform Epsilon)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:7784053"
FT /id="VSP_001354"
FT VARIANT 64
FT /note="I -> T (in dbSNP:rs748095099)"
FT /id="VAR_002272"
FT VARIANT 81
FT /note="P -> S (in dbSNP:rs11569200)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_020567"
FT CONFLICT 269
FT /note="N -> S (in Ref. 4; BAH13914)"
FT /evidence="ECO:0000305"
FT HELIX 131..146
FT /evidence="ECO:0007829|PDB:1CF7"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:1CF7"
FT HELIX 151..163
FT /evidence="ECO:0007829|PDB:1CF7"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:1CF7"
FT HELIX 174..193
FT /evidence="ECO:0007829|PDB:1CF7"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:1CF7"
SQ 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
