Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Menin is a ‘reader’ of histone H3 lysine 79 methylation

ABSTRACT: Menin is a ‘reader’ of histone H3 lysine 79 methylation

PROVIDER: PRJNA836614 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR19149547_1.fastq.gz	Fastqsanger.gz
	SRR19149547_2.fastq.gz	Fastqsanger.gz
	SRR19149548_1.fastq.gz	Fastqsanger.gz
	SRR19149548_2.fastq.gz	Fastqsanger.gz
	SRR19149549_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 44

Similar Datasets

Menin is a ‘reader’ of histone H3 lysine 79 methylation (RNA-Seq)

Project description:Methylation of histone H3 lysine-79 is an epigenetic mark for gene regulation in development, cellular differentiation and disease progression. However, it remains poorly understood how this histone mark is translated into downstream effects due to the lack of knowledge of H3K79 methylation ‘readers’. Here, we develop a nucleosome-based photoaffinity probe to capture proteins that recognize H3K79 dimethylation (H3K79me2) in nucleosomal context. In combination with a quantitative proteomics approach, this probe identifies menin as a bona fide “reader” for H3K79me2. Menin directly and selectively binds to the nucleosome with H3K79me2 mark in vitro. In cells, menin is tightly associated with this histone mark on chromatin, particularly in gene bodies. Reading H3K79me2 at intragenic enhancers, menin promotes gene transcription, likely by mediating enhancer–promoter interactions.

2023-02-17 | GSE202592 | GEO

Menin is a ‘reader’ of histone H3 lysine 79 methylation (ChIP-Seq)

2023-02-17 | GSE202591 | GEO

Menin is a ‘reader’ of histone H3 lysine 79 methylation (RNA-Seq)

Project description:Menin is a ‘reader’ of histone H3 lysine 79 methylation (RNA-Seq)

| PRJNA836620 | ENA

Menin is a ‘reader’ of histone H3 lysine 79 methylation (ChIP-Seq)

Project description:Menin is a ‘reader’ of histone H3 lysine 79 methylation (ChIP-Seq)

| PRJNA836619 | ENA

Menin is a ‘reader’ of histone H3 lysine 79 methylation

Project description:This SuperSeries is composed of the SubSeries listed below.

2023-02-17 | GSE202593 | GEO

Genome-wide characterization of menin-dependent H3K4me3 reveals a specific role for menin in the regulation of genes implicated in MEN1-like tumors (mRNA)

Project description:Inactivating mutations in the MEN1 gene predisposing to the multiple endocrine neoplasia type 1 (MEN1) syndrome can also cause sporadic pancreatic endocrine tumors. MEN1 encodes menin, a subunit of MLL1/MLL2-containing histone methyltransferase complexes that trimethylate histone H3 at lysine 4 (H3K4me3). The importance of menin-dependent H3K4me3 in normal and transformed pancreatic endocrine cells is unclear. To study the role of menin-dependent H3K4me3, we performed in vitro differentiation of wild-type as well as menin-null mouse embryonic stem cells (mESCs) into pancreatic islet-like endocrine cells (PILECs). Gene expression analysis and genome-wide H3K4me3 ChIP-Seq profiling in wild-type and menin-null mESCs and PILECs revealed menin-dependent H3K4me3 at the imprinted Dlk1-Meg3 locus in mESCs, and all four Hox loci in differentiated PILECs. Specific and significant loss of H3K4me3 and gene expression was observed for genes within the imprinted Dlk1-Meg3 locus in menin-null mESCs and the Hox loci in menin-null PILECs. Given that the reduced expression of genes within the DLK1-MEG3 locus and the HOX loci is associated with MEN1-like sporadic tumors, our data suggests a possible role for menin-dependent H3K4me3 at these genes in the initiation and progression of sporadic pancreatic endocrine tumors. Furthermore, our investigation also demonstrates that menin-null mESCs can be differentiated in vitro into islet-like endocrine cells, underscoring the utility of menin-null mESC-derived specialized cell types for genome-wide high-throughput studies. Genome-wide mapping of H3K4me3 and microarray gene expression profiling in TC-1 wild-type (WT) mESCs, menin-null (Men1-ko) mESCs (3.2N), pancreatic islet-like endocrine cells (PILECs) derived from WT mESCs, and PILECs derived from Men1-ko mESCs.

2012-05-31 | E-GEOD-37775 | biostudies-arrayexpress

Genome-wide characterization of menin-dependent H3K4me3 reveals a specific role for menin in the regulation of genes implicated in MEN1-like tumors (ChIP-Seq)

2012-06-01 | E-GEOD-37774 | biostudies-arrayexpress

CpG islands recruit a histone H3 lysine 36 demethylase

Project description:This SuperSeries is composed of the following subset Series: GSE18588: CpG islands recruit a histone H3 lysine 36 demethylase [Illumina sequencing data] GSE21201: CpG islands recruit a histone H3 lysine 36 demethylase [Agilent data] Refer to individual Series

2010-04-26 | E-GEOD-21202 | biostudies-arrayexpress

NSD2 links dimethylation of histone H3 at lysine 36 to oncogenic programming

Project description:This SuperSeries is composed of the following subset Series: GSE29146: NSD2 links dimethylation of histone H3 at lysine 36 to oncogenic programming [ChIP] GSE29147: NSD2 links dimethylation of histone H3 at lysine 36 to oncogenic programming [RNAi] GSE29148: NSD2 links dimethylation of histone H3 at lysine 36 to oncogenic programming [TKO] GSE29150: NSD2 links dimethylation of histone H3 at lysine 36 to oncogenic programming [Transduction] Refer to individual Series

2011-11-29 | E-GEOD-29305 | biostudies-arrayexpress

Histone H3 lysine 27 trimethylation of miRNA genes in HMEC and HMF

Project description:Normal cell type specific histone H3 lysine 27 trimethylation of miRNA genes. HMEC and HMF represent two distinct differentiated cell type present in mammary gland each with a distinct phenotype, a distinct epigenotype as well as distinct miRNA expression pattern. The aim of the study was to determine how epigenetic modifications including histone H3 lysine 27 trimethylation affect miRNA expression. Two cell types HMEC vs. HMF. Biological replicates: 3 pairs of HMEC-HMF of 3 distinct genotypes. Immunoprecipitation using anti-histone H3 trimethylated at lysine 27 (07-449, Millipore).

2011-04-05 | E-GEOD-28376 | biostudies-arrayexpress

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