TFDP1_MOUSE
ID TFDP1_MOUSE Reviewed; 410 AA.
AC Q08639;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Transcription factor Dp-1;
DE AltName: Full=DRTF1-polypeptide 1;
DE AltName: Full=E2F dimerization partner 1;
GN Name=Tfdp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8446173; DOI=10.1038/362083a0;
RA Girling R., Partridge J.F., Bandara L.R., Burden N., Totty N.F.,
RA Hsuan J.J., La Thangue N.B.;
RT "A new component of the transcription factor DRTF1/E2F.";
RL Nature 362:83-87(1993).
RN [2]
RP SEQUENCE REVISION TO 388-410.
RX PubMed=8413592; DOI=10.1038/365468d0;
RA Girling R., Partridge J.F., Bandara L.R., Burden N., Totty N.F.,
RA Hsuan J.J., La Thangue N.B.;
RT "A new component of the transcription factor DRTF1/E2F.";
RL Nature 365:468-468(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=9149906;
RA Dagnino L., Fry C.J., Bartley S.M., Farnham P., Gallie B.L., Phillips R.A.;
RT "Expression patterns of the E2F family of transcription factors during
RT murine epithelial development.";
RL Cell Growth Differ. 8:553-563(1997).
RN [5]
RP DEVELOPMENTAL STAGE.
RX PubMed=9376316; DOI=10.1016/s0925-4773(97)00083-x;
RA Dagnino L., Fry C.J., Bartley S.M., Farnham P., Gallie B.L., Phillips R.A.;
RT "Expression patterns of the E2F family of transcription factors during
RT mouse nervous system development.";
RL Mech. Dev. 66:13-25(1997).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION.
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 [8]
RP SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX PubMed=25940086; DOI=10.1074/jbc.m114.629956;
RA Gong W., Gohla R.M., Bowlin K.M., Koyano-Nakagawa N., Garry D.J., Shi X.;
RT "Kelch repeat and BTB domain containing protein 5 (Kbtbd5) regulates
RT skeletal muscle myogenesis through the E2F1-DP1 complex.";
RL J. Biol. Chem. 290:15350-15361(2015).
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 E2F1:DP complex appears to mediate both cell
CC proliferation and apoptosis. Blocks adipocyte differentiation by
CC repressing CEBPA binding to its target gene promoters
CC (PubMed:20176812). {ECO:0000250|UniProtKB:Q14186,
CC ECO:0000269|PubMed:20176812}.
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. Part of the E2F6.com-1 complex in G0 phase is
CC composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2,
CC MBLR, L3MBTL2 YAF2. Component of the DREAM complex (also named LINC
CC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54,
CC MYBL1, 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 (By similarity).
CC {ECO:0000250|UniProtKB:Q14186}.
CC -!- INTERACTION:
CC Q08639; P51141: Dvl1; NbExp=3; IntAct=EBI-1216575, EBI-1538407;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25940086}. Cytoplasm
CC {ECO:0000269|PubMed:25940086}. Note=Shuttles between the cytoplasm and
CC nucleus and translocates into the nuclear compartment upon
CC heterodimerization with E2F1. {ECO:0000305|PubMed:25940086}.
CC -!- DEVELOPMENTAL STAGE: In the intestinal epithelium, first expressed in
CC undifferentiated and mesenchymal tissues, levels increasing by 12.5 dpc
CC in the epithelial compartment. With epithelial differentiation at 15.5
CC dpc, Its expression increases substantially in the intervillus
CC epithelium with lower levels in the mesenchyme. At later stages,
CC expression continues in the intervillus epithelium. Also found at lower
CC levels in the developing villi. In the developing brain, highest levels
CC found between 11.5 and 13.5 dpc in the ventricular region. In the
CC developing retina, it is expressed both in retinoblast and ganglion
CC cell layers from 14.5 dpc to 6 days after birth. In other developing
CC tissues, its expression is highest in the thymus. Also present in
CC kidney, lung, liver, heart and chondrocytes. Weakly expressed in
CC skeletal muscle and absent from choroid plexus.
CC {ECO:0000269|PubMed:9149906, ECO:0000269|PubMed:9376316}.
CC -!- PTM: Ubiquitinated by the BCR(KBTBD5) complex, leading to its
CC subsequent degradation. {ECO:0000269|PubMed:25940086}.
CC -!- PTM: Phosphorylation by E2F1-bound cyclin A-CDK2, in the S phase,
CC inhibits E2F-mediated DNA binding and transactivation.
CC {ECO:0000250|UniProtKB:Q14186}.
CC -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
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DR EMBL; X72310; CAA51056.1; -; mRNA.
DR CCDS; CCDS22110.1; -.
DR PIR; B48585; B48585.
DR RefSeq; NP_001278694.1; NM_001291765.1.
DR RefSeq; NP_033387.1; NM_009361.3.
DR RefSeq; XP_006508814.1; XM_006508751.3.
DR AlphaFoldDB; Q08639; -.
DR SMR; Q08639; -.
DR BioGRID; 204138; 19.
DR ComplexPortal; CPX-159; E2F1-DP1 transcription factor complex.
DR ComplexPortal; CPX-160; RB1-E2F1-TFDP1 transcription repressor complex.
DR ComplexPortal; CPX-176; E2F2-DP1 transcription factor complex.
DR ComplexPortal; CPX-177; RB1-E2F2-TFDP1 transcription repressor complex.
DR CORUM; Q08639; -.
DR DIP; DIP-724N; -.
DR IntAct; Q08639; 7.
DR MINT; Q08639; -.
DR STRING; 10090.ENSMUSP00000127952; -.
DR iPTMnet; Q08639; -.
DR PhosphoSitePlus; Q08639; -.
DR EPD; Q08639; -.
DR jPOST; Q08639; -.
DR PaxDb; Q08639; -.
DR PeptideAtlas; Q08639; -.
DR PRIDE; Q08639; -.
DR ProteomicsDB; 262886; -.
DR Antibodypedia; 11828; 373 antibodies from 35 providers.
DR DNASU; 21781; -.
DR Ensembl; ENSMUST00000170909; ENSMUSP00000127952; ENSMUSG00000038482.
DR Ensembl; ENSMUST00000209885; ENSMUSP00000147881; ENSMUSG00000038482.
DR GeneID; 21781; -.
DR KEGG; mmu:21781; -.
DR UCSC; uc009kxp.2; mouse.
DR CTD; 7027; -.
DR MGI; MGI:101934; Tfdp1.
DR VEuPathDB; HostDB:ENSMUSG00000038482; -.
DR eggNOG; KOG2829; Eukaryota.
DR GeneTree; ENSGT00940000154652; -.
DR HOGENOM; CLU_039874_3_1_1; -.
DR InParanoid; Q08639; -.
DR OMA; FSTTDNH; -.
DR OrthoDB; 1046304at2759; -.
DR PhylomeDB; Q08639; -.
DR TreeFam; TF314396; -.
DR Reactome; R-MMU-1538133; G0 and Early G1.
DR Reactome; R-MMU-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-MMU-69231; Cyclin D associated events in G1.
DR Reactome; R-MMU-8953750; Transcriptional Regulation by E2F6.
DR BioGRID-ORCS; 21781; 24 hits in 75 CRISPR screens.
DR ChiTaRS; Tfdp1; mouse.
DR PRO; PR:Q08639; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q08639; protein.
DR Bgee; ENSMUSG00000038482; Expressed in granulocyte and 279 other tissues.
DR ExpressionAtlas; Q08639; baseline and differential.
DR Genevisible; Q08639; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0035189; C:Rb-E2F complex; ISO:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0140416; F:transcription regulator inhibitor activity; ISO:MGI.
DR GO; GO:0043276; P:anoikis; IDA:MGI.
DR GO; GO:0008544; P:epidermis development; IMP:MGI.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IC:ComplexPortal.
DR GO; GO:0070345; P:negative regulation of fat cell proliferation; IMP:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IEA:Ensembl.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:2000278; P:regulation of DNA biosynthetic process; IMP:MGI.
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; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR CDD; cd14458; DP_DD; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.20.140.80; -; 1.
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 Acetylation; Activator; Cell cycle; Cytoplasm; Direct protein sequencing;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..410
FT /note="Transcription factor Dp-1"
FT /id="PRO_0000219476"
FT DNA_BIND 113..195
FT /evidence="ECO:0000255"
FT REGION 79..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..127
FT /note="Interaction with CEBPA"
FT /evidence="ECO:0000250|UniProtKB:Q14186"
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 /evidence="ECO:0000250|UniProtKB:Q14186"
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 79..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:0000250|UniProtKB:Q14186"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 410 AA; 45231 MW; FEEA090C781071B9 CRC64;
MAKDASLIEA NGELKVFIDQ NLSPGKGVVS LVAVHPSTVN TLGKQLLPKT FGQSNVNITQ
QVVIGTPQRP AASNTIVVGS PHTPNTHFVS QNQTSDSSPW SAGKRNRKGE KNGKGLRHFS
MKVCEKVQRK GTTSYNEVAD ELVAEFSAAD NHILPNESAY DQKNIRRRVY DALNVLMAMN
IISKEKKEIK WIGLPTNSAQ ECQNLEVERQ RRLERIKQKQ SQLQELILQQ IAFKNLVQRN
RQAEQQARRP PPPNSVIHLP FIIVNTSRKT VIDCSISNDK FEYLFNFDNT FEIHDDIEVL
KRMGMACGLE SGNCSAEDLK VARSLVPKAL EPYVTEMAQG SIGGVFVTTT GSTSNGTRLS
ASDLSNGADG MLATSSNGSQ YSGSRVETPV SYVGEDDDDD DDFNENDEED
