Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Coordination of Mediator Complex and Histone Acetyltransferase CBP/p300 in Transcriptional Regulation [ChIP-seq]

ABSTRACT: Coordination of Mediator Complex and Histone Acetyltransferase CBP/p300 in Transcriptional Regulation [ChIP-seq]

PROVIDER: PRJNA681903 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR13177429_1.fastq.gz	Fastqsanger.gz
	SRR13177429_2.fastq.gz	Fastqsanger.gz
	SRR13177430_1.fastq.gz	Fastqsanger.gz
	SRR13177430_2.fastq.gz	Fastqsanger.gz
	SRR13177431_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 12

Similar Datasets

Coordination of Mediator Complex and Histone Acetyltransferase CBP/p300 in Transcriptional Regulation

Project description:Coordination of Mediator Complex and Histone Acetyltransferase CBP/p300 in Transcriptional Regulation

| PRJNA681894 | ENA

Coordination of Mediator Complex and Histone Acetyltransferase CBP/p300 in Transcriptional Regulation [RNA-seq]

Project description:Coordination of Mediator Complex and Histone Acetyltransferase CBP/p300 in Transcriptional Regulation [RNA-seq]

| PRJNA681899 | ENA

Coordination of Mediator Complex and Histone Acetyltransferase CBP/p300 in Transcriptional Regulation [ChIP-seq]

Project description:CBP/p300 is one group of histone acetyltransferases, which catalyze the acetylation of histone lysine in order to loosen the chromatin structure and promote transcription. The multiple-subunits complex MEDIATOR is important for the transcription initiation through participating in the assembly of transcriptional pre-initiation complex (PIC). Our study identified that MEDIATOR interacts with HAC1 and HAC5, and participate in the regulation of transcription coordinately, thereby regulating the development of Arabidopsis. Besides, MEDIATOR, HAC1, and HAC5 may be organized together by the LLPS to regulate transcription.

2021-01-01 | GSE162458 | GEO

Coordination of Mediator Complex and Histone Acetyltransferase CBP/p300 in Transcriptional Regulation [RNA-seq]

2021-01-01 | GSE162457 | GEO

CBP/p300 transcriptome

Project description:Comparison of CBP/p300 gene knock-out, bromodomain inhibitor, and acetyltransferase inhibitors Cmpd-R and A-485 in the same cell line (MEF).

2018-06-13 | GSE92613 | GEO

Regulation of p300 acetyltransferase activity by the TAZ2 domain [ATAC-seq]

Project description:The E1A binding protein P300 (EP300, also known as p300, lysine acetyltransferase 3B or KAT3B) and its close paralogue CREB-binding protein (CREBBP, aka CBP or KAT3A) possess intrinsic histone acetyltransferase (HAT) activity that can act on both histone and non-histone proteins. P300 and CBP are composed of multiple conserved protein domains, many of which are in proximity to the HAT domain modulating its catalytic activity. Here we show that the TAZ2 domain regulates the intrinsic catalytic activity of p300 in vitro and histone acetylation and chromatin accessibility in cells. Our study extends the knowledge of p300 self-regulation and provides new therapeutic stratagies for human cancers with corresponding p300/CBP mutations.

2023-08-07 | GSE193647 | GEO

Regulation of p300 acetyltransferase activity by the TAZ2 domain [RNA-seq]

2023-08-07 | GSE193645 | GEO

Regulation of p300 acetyltransferase activity by the TAZ2 domain [ChIP-seq]

2023-08-07 | GSE193646 | GEO

CBP/p300 transcriptome

Project description:CBP/p300 transcriptome

| PRJNA358160 | ENA

Combination Targeting of the Bromodomain and Acetyltransferase Active Site of p300/CBP [RNA-seq]

Project description:p300 and CBP are highly related histone acetyltransferase (HAT) enzymes that regulate gene expression, and their dysregulation has been linked to cancer and other diseases. p300/CBP is composed of a number of domains including a HAT domain which is inhibited by the small molecule A-485 and an acetyl-lysine binding bromodomain which was recently found to be selectively antagonized by the small molecule I-CBP112. Here we show that the combination of I-CBP112 and A-485 can synergize to inhibit prostate cancer cell proliferation. We find that the combination confers a dramatic reduction in p300 chromatin occupancy compared to the individual effects of blocking either domain alone. Accompanying this loss of p300 on chromatin, combination treatment predominantly leads to the reduction of specific mRNAs including androgen-dependent and pro-oncogenic prostate genes such as KLK3 (PSA) and c-Myc. Consistent with p300 chromatin binding directly affecting gene expression, mRNAs that are significantly reduced by combination treatment also exhibit a strong reduction in p300 chromatin occupancy at their gene promoters. The relatively few mRNAs that are up-regulated upon combination treatment show no correlation with p300 occupancy. These studies provide support for the pharmacologic advantage of concurrent targeting of two domains within one key epigenetic modification enzyme.

2019-12-31 | GSE124643 | GEO

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data