Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all synonyms
Select your origin of interest
E2f4 and E2f5 display overlapping roles in controlling the normal development of the male reproductive system.
Following stress exposure, E2F4-p130 complexes are lost rapidly along with the presence of E2F4 at E2F (show E2F1 Proteins)-containing B-Myb (show MYBL2 Proteins) promoter sites.
E2F4 is part of a transcriptional repressor complex comprising p130 and HDAC1 (show HDAC1 Proteins) in cardiac myocytes. Relief from E2F4-dependent gene silencing induces the expression of pro-apoptotic genes.
In terminally differentiated cells, common KDM5A (show KDM5A Proteins) and E2F4 gene targets were bound by the pRB (show PGR Proteins)-related protein p130, a DREAM complex component.
We report here a new cellular function of p27 (show CDKN1B Proteins) as a transcriptional regulator in association with p130/E2F4 complexes that could be relevant for tumorigenesis.
Induction of Wnt (show WNT2 Proteins)/beta-catenin (show CTNNB1 Proteins) signaling in mouse mesenchymal stem cells is associated with activation of the p130 and E2f4 and formation of the p130/Gsk3beta/beta-catenin (show CTNNB1 Proteins) complex.
E2F4 plays an important role in enabling osteoblast progenitors to exit the cell cycle and subsequently differentiate thereby contributing to the commitment of these cells to the bone lineage.
Our data indicate that E2F4 is required for cardiomyocyte proliferation and suggest a function for E2F4 in mitosis
E2F4 controls cell cycle exit through different mechanisms.
interactions are regulated by G1 cyclin/cyclin (show PCNA Proteins)-dependent kinase (show CDK1 Proteins)-coordinated phosphorylation of endogenous pocket proteins
The authors found that phosphorylation of residues S650 and S975 in p107 (show RBL1 Proteins) weakens the E2F4 transactivation domain binding.
E2F4 gene expression in glioblastoma.
Integrative genomic analyses confirm that E2F4 or E2F1 (show E2F1 Proteins) expression level is high in liposarcoma patients which associate with unfavorable prognosis.
This study found evidence that the number of triplet AGC (show ACAN Proteins) repeats in the E2F4 gene may play a role in the susceptibility to early-onset colorectal cancer.
PHF8 (show PHF8 Proteins) reduces the H3K9me2 level at the E2F4 transcriptional start site, demonstrating a direct function of PHF8 (show PHF8 Proteins) in endothelial E2F4 gene regulation
cell cycle-dependent transcription of the TRAIP (show TRAIP Proteins) gene by E2F1 (show E2F1 Proteins), E2F2 (show E2F2 Proteins), and E2F4 and rapid protein degradation leads to cell cycle-dependent expression with a maximum in G2/M
Authors show that BRCA1 and RAD17 (show RAD17 Proteins) genes, whose derived proteins play a pivotal role in DNA damage repair, are transcriptional targets of gain-of-function mutant p53 (show TP53 Proteins) proteins.
Data suggest that aberrant cell cycle activation in Ewing sarcoma is due to the de-repression of transcription factor E2F targets of transcriptional induction and physical recruitment of E2F3 by fusion protein EWS (show EWSR1 Proteins)-FLI1 (show FLI1 Proteins) replacing E2F4 on their promoters.
The inverse immunohistochemical relationship between E2F1 (show E2F1 Proteins) and E2F4 indicates a possible mechanistic interlink in colorectal cancer.
E2F4 promoter occupancy is globally associated with p53 (show TP53 Proteins)-repression targets, but not with p53 (show TP53 Proteins) activation targets.
The protein encoded by this gene is a member of the E2F family of transcription factors. The E2F family plays a crucial role in the control of cell cycle and action of tumor suppressor proteins and is also a target of the transforming proteins of small DNA tumor viruses. The E2F proteins contain several evolutionally conserved domains found in most members of the family. These domains include a DNA binding domain, a dimerization domain which determines interaction with the differentiation regulated transcription factor proteins (DP), a transactivation domain enriched in acidic amino acids, and a tumor suppressor protein association domain which is embedded within the transactivation domain. This protein binds to all three of the tumor suppressor proteins pRB, p107 and p130, but with higher affinity to the last two. It plays an important role in the suppression of proliferation-associated genes, and its gene mutation and increased expression may be associated with human cancer.
, transcription factor E2F4
, E2F transcription factor 4, p107/p130-binding
, E2F transcription factor 4