E2F1_RAT
ID E2F1_RAT Reviewed; 432 AA.
AC O09139;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Transcription factor E2F1 {ECO:0000303|PubMed:20176812};
DE Short=E2F-1 {ECO:0000303|PubMed:20176812};
GN Name=E2f1 {ECO:0000303|PubMed:20176812, ECO:0000312|RGD:728892};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8673024;
RA Hosokawa Y., Yang M., Kaneko S., Tanaka M., Nakashima K.;
RT "Synergistic gene expressions of cyclin E, cdk2, cdk5 and E2F-1 during the
RT prolactin-induced G1/S transition in rat Nb2 pre-T lymphoma cells.";
RL Biochem. Mol. Biol. Int. 37:393-399(1995).
RN [2]
RP 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).
CC -!- FUNCTION: Transcription activator that binds DNA cooperatively with DP
CC proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in
CC the promoter region of a number of genes whose products are involved in
CC cell cycle regulation or in DNA replication. The DRTF1/E2F complex
CC functions in the control of cell-cycle progression from G1 to S phase.
CC E2F1 binds preferentially RB1 in a cell-cycle dependent manner. It can
CC mediate both cell proliferation and TP53/p53-dependent apoptosis.
CC Blocks adipocyte differentiation by binding to specific promoters
CC repressing CEBPA binding to its target gene promoters. Directly
CC activates transcription of PEG10. Positively regulates transcription of
CC RRP1B. {ECO:0000250|UniProtKB:Q01094}.
CC -!- ACTIVITY REGULATION: BIRC2/c-IAP1 stimulates its transcriptional
CC activity. {ECO:0000250|UniProtKB:Q01094}.
CC -!- SUBUNIT: Component of the DRTF1/E2F transcription factor complex. Forms
CC heterodimers with DP family members. The E2F1 complex binds
CC specifically hypophosphorylated retinoblastoma protein RB1. During the
CC cell cycle, RB1 becomes phosphorylated in mid-to-late G1 phase,
CC detaches from the DRTF1/E2F complex, rendering E2F transcriptionally
CC active. Interacts with TRRAP, which probably mediates its interaction
CC with histone acetyltransferase complexes, leading to transcription
CC activation. Binds TOPBP1 and EAPP. Interacts with ARID3A. Interacts
CC with TRIM28; the interaction inhibits E2F1 acetylation through
CC recruiting HDAC1 and represses its transcriptional activity.
CC Interaction with KAT2B; the interaction acetylates E2F1 enhancing its
CC DNA-binding and transcriptional activity. Interacts with BIRC2/c-IAP1
CC (via BIR domains). The complex TFDP1:E2F1 interacts with CEBPA; the
CC interaction prevents CEBPA binding to target genes promoters and
CC represses its transcriptional activity. Interacts with RRP1B. Interacts
CC with HCFC1. Interacts with KMT2E; the interaction is probably indirect
CC and is mediated via HCFC1. {ECO:0000250|UniProtKB:Q01094,
CC ECO:0000250|UniProtKB:Q61501}.
CC -!- INTERACTION:
CC O09139; P33568: Rb1; NbExp=2; IntAct=EBI-1211101, EBI-1162932;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q01094}.
CC -!- PTM: Phosphorylated by CDK2 and cyclin A-CDK2 in the S-phase.
CC Phosphorylation by CHEK2 stabilizes E2F1 upon DNA damage and regulates
CC its effect on transcription and apoptosis. Phosphorylation at Ser-398
CC by GSK3B promotes interaction with USP11, leading to its
CC deubiquitination and stabilization. {ECO:0000250|UniProtKB:Q01094}.
CC -!- PTM: Ubiquitinated via 'Lys-63'-linked ubiquitin, leading to its
CC degradation. Deubiquitinated by USP11 follwong phosphorylation by
CC GSK3B, promoting its stability. {ECO:0000250|UniProtKB:Q01094}.
CC -!- PTM: Acetylation stimulates DNA-binding. Enhanced under stress
CC conditions such as DNA damage and inhibited by retinoblastoma protein
CC RB1. Regulated by KAP1/TRIM28 which recruits HDAC1 to E2F1 resulting in
CC deacetylation (By similarity). {ECO:0000250|UniProtKB:Q01094}.
CC -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
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DR EMBL; D63165; BAA09641.1; -; mRNA.
DR RefSeq; NP_001094248.1; NM_001100778.1.
DR AlphaFoldDB; O09139; -.
DR SMR; O09139; -.
DR IntAct; O09139; 1.
DR STRING; 10116.ENSRNOP00000022428; -.
DR PaxDb; O09139; -.
DR GeneID; 399489; -.
DR KEGG; rno:399489; -.
DR UCSC; RGD:728892; rat.
DR CTD; 1869; -.
DR RGD; 728892; E2f1.
DR VEuPathDB; HostDB:ENSRNOG00000016708; -.
DR eggNOG; KOG2577; Eukaryota.
DR HOGENOM; CLU_032091_0_1_1; -.
DR InParanoid; O09139; -.
DR OMA; HVCTTQL; -.
DR OrthoDB; 1087250at2759; -.
DR Reactome; R-RNO-68911; G2 Phase.
DR Reactome; R-RNO-69231; Cyclin D associated events in G1.
DR PRO; PR:O09139; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000016708; Expressed in frontal cortex and 18 other tissues.
DR ExpressionAtlas; O09139; baseline and differential.
DR Genevisible; O09139; RN.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0000228; C:nuclear chromosome; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0035189; C:Rb-E2F complex; ISO:RGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:RGD.
DR GO; GO:0043276; P:anoikis; ISO:RGD.
DR GO; GO:0071398; P:cellular response to fatty acid; IEP:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IDA:RGD.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISO:RGD.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0030900; P:forebrain development; ISO:RGD.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:RGD.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; ISO:RGD.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISS:UniProtKB.
DR GO; GO:1990086; P:lens fiber cell apoptotic process; ISO:RGD.
DR GO; GO:0048255; P:mRNA stabilization; ISO:RGD.
DR GO; GO:0043392; P:negative regulation of DNA binding; ISS:UniProtKB.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0070345; P:negative regulation of fat cell proliferation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0071930; P:negative regulation of transcription involved in G1/S transition of mitotic cell cycle; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0060252; P:positive regulation of glial cell proliferation; IMP:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:RGD.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
DR GO; GO:0006351; P:transcription, DNA-templated; ISS:UniProtKB.
DR CDD; cd14660; E2F_DD; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR015633; E2F.
DR InterPro; IPR037241; E2F-DP_heterodim.
DR InterPro; IPR032198; E2F_CC-MB.
DR InterPro; IPR003316; E2F_WHTH_DNA-bd_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12081; PTHR12081; 1.
DR Pfam; PF16421; E2F_CC-MB; 1.
DR Pfam; PF02319; E2F_TDP; 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; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..432
FT /note="Transcription factor E2F1"
FT /id="PRO_0000219463"
FT DNA_BIND 108..192
FT /evidence="ECO:0000255"
FT REGION 39..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..106
FT /note="Cyclin A:CDK2 binding"
FT /evidence="ECO:0000250|UniProtKB:Q01094"
FT REGION 87..189
FT /note="Interaction with BIRC2/c-IAP1"
FT /evidence="ECO:0000250|UniProtKB:Q01094"
FT REGION 98..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..172
FT /note="Leucine-zipper"
FT /evidence="ECO:0000250|UniProtKB:Q01094"
FT REGION 190..377
FT /note="Required for interaction with TRIM28"
FT /evidence="ECO:0000250|UniProtKB:Q01094"
FT REGION 193..282
FT /note="Dimerization"
FT /evidence="ECO:0000255"
FT REGION 297..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..432
FT /note="Transactivation"
FT /evidence="ECO:0000250|UniProtKB:Q01094"
FT REGION 404..421
FT /note="RB1 binding"
FT /evidence="ECO:0000250|UniProtKB:Q01094"
FT MOTIF 156..192
FT /note="DEF box"
FT /evidence="ECO:0000250|UniProtKB:Q01094"
FT COMPBIAS 305..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 115
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q01094"
FT MOD_RES 118
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q01094"
FT MOD_RES 123
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q01094"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01094"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01094"
FT MOD_RES 428
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q01094"
SQ SEQUENCE 432 AA; 46548 MW; 4E401ADF6E20C13C CRC64;
MAVAPAGGQH APALEALLGA GALRLLDSSQ IVIISTAPDV GAPQVPTGPA APPAGPRDPD
VLLFATPQAP RPAPSAPRPA LGRPPVKRRL DLETDHQYLA GSSGPFRGRG RHPGKGVKSP
GEKSRYETSL NLTTKRFLEL LSHSADGVVD LNWAAEVLKV QKRRIYDITN VLEGIQLIAK
KSKNHIQWLG SRTMVGIGQR LEGLTQDLQQ LQESEQQLDH LMHICTTQLQ LLSEDSDIQR
LAYVTCQDLR SIADPAEQMV IVIKAPPETQ LQAVDSAETF QISLKSKQGP IDVFLCPEES
AEGISPGRTS YQETSGEDRN ADSGTAGPPP SPPSTSPTLD PSQSLLGLEQ EAVLPRIGNL
RAPMEEDRLS PLVAADSLLE HVKEDFSGLL PGEFISLSPP HEAVDYHFGL EEGEGIRDLF
DCDFGDLTPL DF
