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Transcription factor E2F1 (E2F-1) (Fragment)

 E2F1_RAT                Reviewed;         432 AA.
O09139;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-APR-2015, sequence version 2.
22-NOV-2017, entry version 116.
RecName: Full=Transcription factor E2F1;
Short=E2F-1;
Flags: Fragment;
Name=E2f1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8673024;
Hosokawa Y., Yang M., Kaneko S., Tanaka M., Nakashima K.;
"Synergistic gene expressions of cyclin E, cdk2, cdk5 and E2F-1 during
the prolactin-induced G1/S transition in rat Nb2 pre-T lymphoma
cells.";
Biochem. Mol. Biol. Int. 37:393-399(1995).
[2]
INTERACTION WITH CEBPA.
PubMed=20176812; DOI=10.1128/MCB.01619-09;
Zaragoza K., Begay V., Schuetz A., Heinemann U., Leutz A.;
"Repression of transcriptional activity of C/EBPalpha by E2F-
dimerization partner complexes.";
Mol. Cell. Biol. 30:2293-2304(2010).
-!- FUNCTION: Transcription activator that binds DNA cooperatively
with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-
3' found in the promoter region of a number of genes whose
products are involved in cell cycle regulation or in DNA
replication. The DRTF1/E2F complex functions in the control of
cell-cycle progression from G1 to S phase. E2F1 binds
preferentially RB1 in a cell-cycle dependent manner. It can
mediate both cell proliferation and TP53/p53-dependent apoptosis.
Blocks adipocyte differentiation by binding to specific promoters
repressing CEBPA binding to its target gene promoters. Positively
regulates transcription of RRP1B. {ECO:0000250|UniProtKB:Q01094,
ECO:0000250|UniProtKB:Q61501}.
-!- ENZYME REGULATION: BIRC2/c-IAP1 stimulates its transcriptional
activity. {ECO:0000250}.
-!- SUBUNIT: Component of the DRTF1/E2F transcription factor complex.
Forms heterodimers with DP family members. The E2F1 complex binds
specifically hypophosphorylated retinoblastoma protein RB1. During
the cell cycle, RB1 becomes phosphorylated in mid-to-late G1
phase, detaches from the DRTF1/E2F complex, rendering E2F
transcriptionally active. Interacts with TRRAP, which probably
mediates its interaction with histone acetyltransferase complexes,
leading to transcription activation. Binds TOPBP1 and EAPP.
Interacts with ARID3A. Interacts with TRIM28; the interaction
inhibits E2F1 acetylation through recruiting HDAC1 and represses
its transcriptional activity. Interaction with KAT2B; the
interaction acetylates E2F1 enhancing its DNA-binding and
transcriptional activity. Interacts with BIRC2/c-IAP1 (via BIR
domains). The complex TFDP1:E2F1 interacts with CEBPA; the
interaction prevents CEBPA binding to target genes promoters and
represses its transcriptional activity. Interacts with RRP1B.
{ECO:0000250|UniProtKB:Q01094, ECO:0000250|UniProtKB:Q61501}.
-!- INTERACTION:
P33568:Rb1; NbExp=2; IntAct=EBI-1211101, EBI-1162932;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q01094}.
-!- PTM: Phosphorylated by CDK2 and cyclin A-CDK2 in the S-phase.
Phosphorylation by CHEK2 stabilizes E2F1 upon DNA damage and
regulates its effect on transcription and apoptosis (By
similarity). {ECO:0000250}.
-!- PTM: Acetylation stimulates DNA-binding. Enhanced under stress
conditions such as DNA damage and inhibited by retinoblastoma
protein RB1. Regulated by KAP1/TRIM28 which recruits HDAC1 to E2F1
resulting in deacetylation (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
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EMBL; D63165; BAA09641.1; -; mRNA.
RefSeq; NP_001094248.1; NM_001100778.1.
UniGene; Rn.72471; -.
SMR; O09139; -.
IntAct; O09139; 1.
STRING; 10116.ENSRNOP00000022428; -.
PaxDb; O09139; -.
Ensembl; ENSRNOT00000022428; ENSRNOP00000022428; ENSRNOG00000016708.
GeneID; 399489; -.
KEGG; rno:399489; -.
UCSC; RGD:728892; rat.
CTD; 1869; -.
RGD; 728892; E2f1.
eggNOG; KOG2577; Eukaryota.
eggNOG; ENOG410XNYI; LUCA.
GeneTree; ENSGT00550000074403; -.
HOGENOM; HOG000232045; -.
InParanoid; O09139; -.
KO; K17454; -.
OMA; ICTTQLR; -.
OrthoDB; EOG091G087U; -.
Reactome; R-RNO-68689; CDC6 association with the ORC:origin complex.
Reactome; R-RNO-68911; G2 Phase.
Reactome; R-RNO-69231; Cyclin D associated events in G1.
Reactome; R-RNO-69298; Association of licensing factors with the pre-replicative complex.
Proteomes; UP000002494; Chromosome 3.
Bgee; ENSRNOG00000016708; -.
ExpressionAtlas; O09139; baseline and differential.
Genevisible; O09139; RN.
GO; GO:0005813; C:centrosome; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0000790; C:nuclear chromatin; ISO:RGD.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0035189; C:Rb-E2F complex; ISO:RGD.
GO; GO:0005667; C:transcription factor complex; ISO:RGD.
GO; GO:0001047; F:core promoter binding; ISO:RGD.
GO; GO:0003677; F:DNA binding; ISO:RGD.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0019901; F:protein kinase binding; IPI:RGD.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISO:RGD.
GO; GO:0008134; F:transcription factor binding; ISO:RGD.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISO:RGD.
GO; GO:0043276; P:anoikis; ISO:RGD.
GO; GO:0071398; P:cellular response to fatty acid; IEP:RGD.
GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IDA:RGD.
GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISO:RGD.
GO; GO:0000077; P:DNA damage checkpoint; ISS:UniProtKB.
GO; GO:0030900; P:forebrain development; ISO:RGD.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:RGD.
GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; ISO:RGD.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISS:UniProtKB.
GO; GO:1990086; P:lens fiber cell apoptotic process; ISO:RGD.
GO; GO:0048255; P:mRNA stabilization; ISO:RGD.
GO; GO:0043392; P:negative regulation of DNA binding; ISS:UniProtKB.
GO; GO:0045599; P:negative regulation of fat cell differentiation; ISS:UniProtKB.
GO; GO:0070345; P:negative regulation of fat cell proliferation; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISO:RGD.
GO; GO:0071930; P:negative regulation of transcription involved in G1/S transition of mitotic cell cycle; ISO:RGD.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:RGD.
GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
GO; GO:0051726; P:regulation of cell cycle; ISO:RGD.
GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; ISO:RGD.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0007283; P:spermatogenesis; IEP:RGD.
GO; GO:0006351; P:transcription, DNA-templated; ISS:UniProtKB.
CDD; cd14660; E2F_DD; 1.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR015633; E2F.
InterPro; IPR037241; E2F-DP_heterodim.
InterPro; IPR032198; E2F_CC-MB.
InterPro; IPR003316; E2F_WHTH_DNA-bd_dom.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
PANTHER; PTHR12081; PTHR12081; 1.
Pfam; PF16421; E2F_CC-MB; 1.
Pfam; PF02319; E2F_TDP; 1.
SMART; SM01372; E2F_TDP; 1.
SUPFAM; SSF144074; SSF144074; 1.
SUPFAM; SSF46785; SSF46785; 1.
1: Evidence at protein level;
Acetylation; Activator; Complete proteome; DNA-binding; Nucleus;
Phosphoprotein; Reference proteome; Transcription;
Transcription regulation.
CHAIN 1 432 Transcription factor E2F1.
/FTId=PRO_0000219463.
DNA_BIND 108 192 {ECO:0000255}.
REGION 65 106 Cyclin A:CDK2 binding.
{ECO:0000250|UniProtKB:Q01094}.
REGION 87 189 Interaction with BIRC2/c-IAP1.
{ECO:0000250|UniProtKB:Q01094}.
REGION 151 172 Leucine-zipper.
{ECO:0000250|UniProtKB:Q01094}.
REGION 190 377 Required for interaction with TRIM28.
{ECO:0000250|UniProtKB:Q01094}.
REGION 193 282 Dimerization. {ECO:0000255}.
REGION 363 432 Transactivation.
{ECO:0000250|UniProtKB:Q01094}.
REGION 404 421 RB1 binding.
{ECO:0000250|UniProtKB:Q01094}.
MOTIF 156 192 DEF box. {ECO:0000250|UniProtKB:Q01094}.
MOD_RES 115 115 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q01094}.
MOD_RES 118 118 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q01094}.
MOD_RES 123 123 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q01094}.
MOD_RES 370 370 Phosphoserine.
{ECO:0000250|UniProtKB:Q01094}.
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


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