E2F1
entrez
1869
canonical
uniprot
Q01094
canonical
ensembl
ENSG00000101412
resolver
ensp
ENSP00000345571
resolver
enst
ENST00000343380
resolver
genesymbol
E2F1
resolver
genesymbol_syn
RBBP3
resolver
hgnc
HGNC:3113
resolver
uniprot
Q13143
resolver
uniprot
Q92768
resolver
uniprot
Q9BSD8
resolver
uniprot_entry
E2F1_HUMAN
resolver
uniprot_entry
Q9BSD8_HUMAN
resolver
uniprot_sec
Q13143
resolver
uniprot_sec
Q92768
resolver
activity_regulation
ACTIVITY REGULATION: BIRC2/c-IAP1 stimulates its transcriptional activity. {ECO:0000269|PubMed:21653699}.
uniprot
proteins
amino_acid_sequence
MALAGAPAGGPCAPALEALLGAGALRLLDSSQIVIISAAQDASAPPAPTGPAAPAAGPCDPDLLLFATPQAPRPTPSAPRPALGRPPVKRRLDLETDHQYLAESSGPARGRGRHPGKGVKSPGEKSRYETSLNLTTKRFLELLSHSADGVVDLNWAAEVLKVQKRRIYDITNVLEGIQLIAKKSKNHIQWLGSHTTVGVGGRLEGLTQDLRQLQESEQQLDHLMNICTTQLRLLSEDTDSQRLAYVTCQDLRSIADPAEQMVMVIKAPPETQLQAVDSSENFQISLKSKQGPIDVFLCPEETVGGISPGKTPSQEVTSEEENRATDSATIVSPPPSSPPSSLTTDPSQSLLSLEQEPLLSRMGSLRAPVDEDRLSPLVAADSLLEHVREDFSGLLPEEFISLSPPHEALDYHFGLEEGEGIRDLFDCDFGDLTPLDF
uniprot
proteins
function
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 (PubMed:10675335, PubMed:12717439, PubMed:17050006, PubMed:17704056, PubMed:18625225, PubMed:28992046). The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase (PubMed:10675335, PubMed:12717439, PubMed:17704056). E2F1 binds preferentially RB1 in a cell-cycle dependent manner (PubMed:10675335, PubMed:12717439, PubMed:17704056). It can mediate both cell proliferation and TP53/p53-dependent apoptosis (PubMed:8170954). Blocks adipocyte differentiation by binding to specific promoters repressing CEBPA binding to its target gene promoters (PubMed:20176812). Directly activates transcription of PEG10 (PubMed:17050006, PubMed:18625225, PubMed:28992046). Positively regulates transcription of RRP1B (PubMed:20040599). {ECO:0000269|PubMed:10675335, ECO:0000269|PubMed:12717439, ECO:0000269|PubMed:17050006, ECO:0000269|PubMed:17704056, ECO:0000269|PubMed:18625225, ECO:0000269|PubMed:20040599, ECO:0000269|PubMed:20176812, ECO:0000269|PubMed:28992046, ECO:0000269|PubMed:8170954}.
uniprot
proteins
mass_dalton
46920
uniprot
proteins
mutagenesis
MUTAGEN 117; /note="K->R: Abolishes acetylation; when associated with R-120 and R-125."; /evidence="ECO:0000269|PubMed:10675335"; MUTAGEN 120; /note="K->R: Abolishes acetylation; when associated with R-117 and R-125."; /evidence="ECO:0000269|PubMed:10675335"; MUTAGEN 125; /note="K->R: Abolishes acetylation; when associated with R-117 and R-120."; /evidence="ECO:0000269|PubMed:10675335"; MUTAGEN 132; /note="L->E: Abolishes interaction with and repression of CEBPA and inhibition of adipogenesis."; /evidence="ECO:0000269|PubMed:20176812"; MUTAGEN 185; /note="K->R: Abrogates methylation by SETD7. Loss of interaction with L3MBTL3. Loss of ubiquitination by the CRL4-DCAF5 E3 ubiquitin ligase complex."; /evidence="ECO:0000269|PubMed:20603083, ECO:0000269|PubMed:29691401"; MUTAGEN 364; /note="S->A: Abrogates in vitro phosphorylation by CHEK2 and CHEK2-dependent stabilization of E2F1 upon DNA damage."; /evidence="ECO:0000269|PubMed:12717439"; MUTAGEN 403; /note="S->A: Decreased phosphorylation by GSK3B, leading to abolished interaction with USP11 and subsequent deubiquitination."; /evidence="ECO:0000269|PubMed:17050006, ECO:0000269|PubMed:28992046"; MUTAGEN 411; /note="Y->C: No retinoblastoma protein binding. No effect on interaction with and repression of CEBPA."; /evidence="ECO:0000269|PubMed:20176812, ECO:0000269|PubMed:8413249"; MUTAGEN 433; /note="T->A: Decreased phosphorylation by GSK3B."; /evidence="ECO:0000269|PubMed:17050006
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by CDK2 and cyclin A-CDK2 in the S-phase (PubMed:12717439, PubMed:7838523). Phosphorylation at Ser-364 by CHEK2 stabilizes E2F1 upon DNA damage and regulates its effect on transcription and apoptosis (PubMed:12717439). Phosphorylation at Ser-403 by GSK3B promotes interaction with USP11, leading to its deubiquitination and stabilization (PubMed:28992046). {ECO:0000269|PubMed:12717439, ECO:0000269|PubMed:28992046, ECO:0000269|PubMed:7838523}.; PTM: Ubiquitinated via 'Lys-63'-linked ubiquitin, leading to its degradation (PubMed:28992046). Deubiquitinated by USP11 following phosphorylation by GSK3B, promoting its stability (PubMed:28992046). {ECO:0000269|PubMed:28992046}.; 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: Methylation at Lys-185 by SETD7 promotes E2F1 ubiquitin-dependent proteasomal degradation. {ECO:0000269|PubMed:20603083, ECO:0000269|PubMed:29691401}.
uniprot
proteins
protein_family
E2F/DP family
uniprot
proteins
pubmed
10675335
uniprot
proteins
pubmed
11418595
uniprot
proteins
pubmed
11780052
uniprot
proteins
pubmed
12501191
uniprot
proteins
pubmed
12598654
uniprot
proteins
pubmed
12697828
uniprot
proteins
pubmed
12717439
uniprot
proteins
pubmed
1448092
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15716352
uniprot
proteins
pubmed
16360038
uniprot
proteins
pubmed
1638634
uniprot
proteins
pubmed
1638635
uniprot
proteins
pubmed
17050006
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17704056
uniprot
proteins
pubmed
18625225
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20040599
uniprot
proteins
pubmed
20176812
uniprot
proteins
pubmed
20603083
uniprot
proteins
pubmed
21653699
uniprot
proteins
pubmed
23629655
uniprot
proteins
pubmed
28992046
uniprot
proteins
pubmed
29691401
uniprot
proteins
pubmed
7494286
uniprot
proteins
pubmed
7838523
uniprot
proteins
pubmed
7958836
uniprot
proteins
pubmed
7958856
uniprot
proteins
pubmed
7969176
uniprot
proteins
pubmed
8033208
uniprot
proteins
pubmed
8170954
uniprot
proteins
pubmed
8336704
uniprot
proteins
pubmed
8413249
uniprot
proteins
pubmed
8964493
uniprot
proteins
pubmed
9199321
uniprot
proteins
pubmed
9780002
uniprot
proteins
sequence_length
437
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20040599, ECO:0000269|PubMed:28992046}.
uniprot
proteins