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MT000196

UniProt Annotations

Entry Information

Gene Name	E2F transcription factor 1
Protein Entry	E2F1_HUMAN
UniProt ID	Q01094
Species	Human

Comments

Comment type	Description
Enzyme Regulation	BIRC2/c-IAP1 stimulates its transcriptional activity. {ECO:0000269\|PubMed:21653699}.
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. {ECO:0000269\|PubMed:10675335, ECO:0000269\|PubMed:12717439, ECO:0000269\|PubMed:17704056, ECO:0000269\|PubMed:8170954}.
Interaction	Q14201:BTG3; NbExp=3; IntAct=EBI-448924, EBI-948192; P50613:CDK7; NbExp=2; IntAct=EBI-448924, EBI-1245958; Q92466:DDB2; NbExp=2; IntAct=EBI-448924, EBI-1176171; Q8NEM0:MCPH1; NbExp=6; IntAct=EBI-448924, EBI-1565483; Q9Y618:NCOR2; NbExp=2; IntAct=EBI-448924, EBI-80830; P09874:PARP1; NbExp=2; IntAct=EBI-448924, EBI-355676; O14744:PRMT5; NbExp=8; IntAct=EBI-448924, EBI-351098; P06400:RB1; NbExp=20; IntAct=EBI-448924, EBI-491274; Q96EB6:SIRT1; NbExp=3; IntAct=EBI-448924, EBI-1802965; Q923E4:Sirt1 (xeno); NbExp=3; IntAct=EBI-448924, EBI-1802585; P08047:SP1; NbExp=2; IntAct=EBI-448924, EBI-298336; P42224:STAT1; NbExp=2; IntAct=EBI-448924, EBI-1057697; Q14186:TFDP1; NbExp=9; IntAct=EBI-448924, EBI-749713; Q92547:TOPBP1; NbExp=3; IntAct=EBI-448924, EBI-308302; O95361:TRIM16; NbExp=2; IntAct=EBI-448924, EBI-727384;
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. Acetylated by P/CAF/KAT2B. {ECO:0000269\|PubMed:10675335, ECO:0000269\|PubMed:17704056}.
Ptm	Phosphorylated by CDK2 and cyclin A-CDK2 in the S-phase. Phosphorylation at Ser-364 by CHEK2 stabilizes E2F1 upon DNA damage and regulates its effect on transcription and apoptosis. {ECO:0000269\|PubMed:12717439, ECO:0000269\|PubMed:17081983, ECO:0000269\|PubMed:18669648, ECO:0000269\|PubMed:19690332, ECO:0000269\|PubMed:7838523}.
Sequence Caution	Sequence=AAB24289.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Similarity	Belongs to the E2F/DP family. {ECO:0000305}.
Subcellular Location	Nucleus.
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. Viral oncoproteins, notably E1A, T- antigen and HPV E7, are capable of sequestering RB1, thus releasing the active complex. 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). Interacts with human cytomegalovirus/HHV-5 protein UL123. {ECO:0000269\|PubMed:10675335, ECO:0000269\|PubMed:11418595, ECO:0000269\|PubMed:12598654, ECO:0000269\|PubMed:12697828, ECO:0000269\|PubMed:15716352, ECO:0000269\|PubMed:16360038, ECO:0000269\|PubMed:17704056, ECO:0000269\|PubMed:21653699, ECO:0000269\|PubMed:7494286, ECO:0000269\|PubMed:9780002}.
Web Resource	Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/E2F1ID40382ch20q11.html";
Web Resource	Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/e2f1/";