TFDP2_MOUSE
ID TFDP2_MOUSE Reviewed; 446 AA.
AC Q64163;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Transcription factor Dp-2;
DE AltName: Full=Dp-3;
DE AltName: Full=E2F dimerization partner 2;
GN Name=Tfdp2; Synonyms=Dp2;
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] (ISOFORMS ALPHA; BETA; DELTA AND GAMMA).
RC TISSUE=Brain, and Kidney;
RX PubMed=7478568;
RA Ormondroyd E., De La Luna S., La Thangue N.B.;
RT "A new member of the DP family, DP-3, with distinct protein products
RT suggests a regulatory role for alternative splicing in the cell cycle
RT transcription factor DRTF1/E2F.";
RL Oncogene 11:1437-1446(1995).
RN [2]
RP NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=8923205; DOI=10.1242/jcs.109.10.2443;
RA de la Luna S., Burden M.J., Lee C.W., La Thangue N.B.;
RT "Nuclear accumulation of the E2F heterodimer regulated by subunit
RT composition and alternative splicing of a nuclear localization signal.";
RL J. Cell Sci. 109:2443-2452(1996).
RN [3]
RP INTERACTION WITH GMCL.
RX PubMed=9878064; DOI=10.1093/emboj/18.1.212;
RA de la Luna S., Allen K.E., Mason S.L., La Thangue N.B.;
RT "Integration of a growth-suppressing BTB/POZ domain protein with the DP
RT component of the E2F transcription factor.";
RL EMBO J. 18:212-228(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. {ECO:0000250|UniProtKB:Q14188}.
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 Interacts with GMCL (By similarity). Component of the DREAM complex
CC (also named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37,
CC LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The
CC complex exists in quiescent cells where it represses cell cycle-
CC dependent genes. It dissociates in S phase when LIN9, LIN37, LIN52 and
CC LIN54 form a subcomplex that binds to MYBL2. The complex TFDP2:E2F1
CC interacts with CEBPA; the interaction prevents CEBPA binding to target
CC gene promoters and represses its transcriptional activity (By
CC similarity). {ECO:0000250|UniProtKB:Q14188,
CC ECO:0000269|PubMed:9878064}.
CC -!- INTERACTION:
CC Q64163-4; Q61502: E2f5; NbExp=2; IntAct=EBI-8077763, EBI-7225685;
CC Q64163-4; P62259: Ywhae; NbExp=6; IntAct=EBI-8077763, EBI-356480;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=Alpha;
CC IsoId=Q64163-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=Q64163-2; Sequence=VSP_001355, VSP_001356;
CC Name=Gamma;
CC IsoId=Q64163-3; Sequence=VSP_001355, VSP_001356, VSP_001357;
CC Name=Delta;
CC IsoId=Q64163-4; Sequence=VSP_001355;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined. Highest levels
CC in spleen and heart.
CC -!- PTM: Phosphorylation by E2F1-bound cyclin A-CDK2, in the S phase,
CC inhibits E2F-mediated DNA binding and transactivation.
CC -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; S79780; AAB35506.2; -; mRNA.
DR CCDS; CCDS23413.1; -. [Q64163-4]
DR AlphaFoldDB; Q64163; -.
DR SMR; Q64163; -.
DR DIP; DIP-24228N; -.
DR IntAct; Q64163; 3.
DR MINT; Q64163; -.
DR STRING; 10090.ENSMUSP00000128260; -.
DR PhosphoSitePlus; Q64163; -.
DR MaxQB; Q64163; -.
DR PaxDb; Q64163; -.
DR PeptideAtlas; Q64163; -.
DR PRIDE; Q64163; -.
DR ProteomicsDB; 262887; -. [Q64163-1]
DR ProteomicsDB; 262888; -. [Q64163-2]
DR ProteomicsDB; 262889; -. [Q64163-3]
DR ProteomicsDB; 262890; -. [Q64163-4]
DR MGI; MGI:107167; Tfdp2.
DR eggNOG; KOG2829; Eukaryota.
DR InParanoid; Q64163; -.
DR PhylomeDB; Q64163; -.
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 ChiTaRS; Tfdp2; mouse.
DR PRO; PR:Q64163; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q64163; protein.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; TAS:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IC: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:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
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 GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
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 Acetylation; Activator; Alternative splicing; Cell cycle; DNA-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q14188"
FT CHAIN 2..446
FT /note="Transcription factor Dp-2"
FT /id="PRO_0000219478"
FT DNA_BIND 129..210
FT /evidence="ECO:0000255"
FT REGION 60..82
FT /note="Interaction with CEBPA"
FT /evidence="ECO:0000250|UniProtKB:Q14188"
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 404..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 103..118
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:8923205"
FT MOTIF 176..210
FT /note="DEF box"
FT COMPBIAS 404..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:0000250|UniProtKB:Q14188"
FT MOD_RES 24
FT /note="Phosphoserine; by CDK2"
FT /evidence="ECO:0000250|UniProtKB:Q14188, ECO:0000255"
FT MOD_RES 42
FT /note="Phosphoserine; by CDK2"
FT /evidence="ECO:0000255"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14188"
FT VAR_SEQ 1..61
FT /note="Missing (in isoform Beta, isoform Gamma and isoform
FT Delta)"
FT /evidence="ECO:0000303|PubMed:7478568"
FT /id="VSP_001355"
FT VAR_SEQ 103..118
FT /note="Missing (in isoform Beta and isoform Gamma)"
FT /evidence="ECO:0000303|PubMed:7478568"
FT /id="VSP_001356"
FT VAR_SEQ 173
FT /note="S -> SQ (in isoform Gamma)"
FT /evidence="ECO:0000303|PubMed:7478568"
FT /id="VSP_001357"
SQ SEQUENCE 446 AA; 49098 MW; 0E6E87AE8B82EE8A CRC64;
MTAKNVGLPS TNAKLRGFID QNFSPSKGNI SLVAFPVSST NSPTKILPKT LGPINVNVGP
QMIISTPQRI ANSGSVLIGN PYTPAPAMVT QTHIAEAAGW VPSDRKRARE FIDSDFSESK
RSKKGDKNGK GLRHFSMKVC EKVQRKGTTS YNEVADELVS EFTNSNNHLA ADSAYDQENI
RRRVYDALNV LMAMNIISSL PTGKKRNQVD CNSAQECQNL EIEKQRRIER IKQKRAQLQE
LLLQQIAFKN LVQRNRQNEQ QNQGPPAVNS TIQLPFIIIN TSRKTVIDCS ISSDKFEYLF
NFDNTFEIHD DIEVLKRMGM SFGLESGKCS LEDLKIARSL VPKALEGYIT DISTGPSWLN
QGLLLNSTQS VSNLDPTTGA TVPQSSVNQG LCLDAEVALA TGQLPASNSH QSSSAASHFS
ESRGETPCSF NDEDEEDEEE DPSSPE
