E2f1
entrez
13555
canonical
uniprot
Q61501
canonical
ensembl
ENSMUSG00000027490
resolver
ensp
ENSMUSP00000000894
resolver
ensp
ENSMUSP00000099434
resolver
enst
ENSMUST00000000894
resolver
enst
ENSMUST00000103145
resolver
genesymbol
E2f1
resolver
uniprot
F6XDK8
resolver
uniprot
Q547J6
resolver
uniprot
Q80VZ3
resolver
uniprot
Q9CYB4
resolver
uniprot_entry
E2F1_MOUSE
resolver
uniprot_entry
F6XDK8_MOUSE
resolver
uniprot_entry
Q547J6_MOUSE
resolver
uniprot_entry
Q9CYB4_MOUSE
resolver
uniprot_sec
Q80VZ3
resolver
activity_regulation
ACTIVITY REGULATION: BIRC2/c-IAP1 stimulates its transcriptional activity. {ECO:0000250|UniProtKB:Q01094}.
uniprot
proteins
amino_acid_sequence
MAVAPAGGQHAPALEALLGAGALRLLDSSQIVIISTAPDVGAPQLPAAPPTGPRDSDVLLFATPQAPRPAPSAPRPALGRPPVKRRLDLETDHQYLAGSSGPFRGRGRHPGKGVKSPGEKSRYETSLNLTTKRFLELLSRSADGVVDLNWAAEVLKVQKRRIYDITNVLEGIQLIAKKSKNHIQWLGSHTMVGIGKRLEGLTQDLQQLQESEQQLDHLMHICTTQLQLLSEDSDTQRLAYVTCQDLRSIADPAEQMVIVIKAPPETQLQAVDSSETFQISLKSKQGPIDVFLCPEESADGISPGKTSCQETSSGEDRTADSGPAGPPPSPPSTSPALDPSQSLLGLEQEAVLPRMGHLRVPMEEDQLSPLVAADSLLEHVKEDFSGLLPGEFISLSPPHEALDYHFGLEEGEGIRDLFDCDFGDLTPLDF
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:11672531, PubMed:20176812, PubMed:9674698). The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase (By similarity). E2F1 binds preferentially RB1 in a cell-cycle dependent manner (By similarity). It can mediate both cell proliferation and TP53/p53-dependent apoptosis (PubMed:9674698). Blocks adipocyte differentiation by binding to specific promoters repressing CEBPA binding to its target gene promoters (PubMed:11672531, PubMed:20176812). Directly activates transcription of PEG10 (By similarity). Positively regulates transcription of RRP1B (By similarity). {ECO:0000250|UniProtKB:Q01094, ECO:0000269|PubMed:11672531, ECO:0000269|PubMed:20176812, ECO:0000269|PubMed:9674698}.
uniprot
proteins
mass_dalton
46323
uniprot
proteins
post_translational_modification
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. Phosphorylation at Ser-396 by GSK3B promotes interaction with USP11, leading to its deubiquitination and stabilization. {ECO:0000250|UniProtKB:Q01094}.; PTM: Ubiquitinated via 'Lys-63'-linked ubiquitin, leading to its degradation. Deubiquitinated by USP11 following phosphorylation by GSK3B, promoting its stability. {ECO:0000250|UniProtKB:Q01094}.; 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 (By similarity). {ECO:0000250|UniProtKB:Q01094}.; PTM: Methylation at Lys-180 by SETD7 promotes E2F1 ubiquitin-dependent proteasomal degradation. {ECO:0000250|UniProtKB:Q01094}.
uniprot
proteins
protein_family
E2F/DP family
uniprot
proteins
pubmed
11672531
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15716352
uniprot
proteins
pubmed
20176812
uniprot
proteins
pubmed
20940255
uniprot
proteins
pubmed
36689330
uniprot
proteins
pubmed
8114719
uniprot
proteins
pubmed
8336704
uniprot
proteins
pubmed
9376316
uniprot
proteins
pubmed
9674698
uniprot
proteins
sequence_length
430
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q01094}.
uniprot
proteins