Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

CFTR PTM analysis

ABSTRACT: CFTR IPs with different CFTR mutants or under different conditions to identify CFTR PTMs.

INSTRUMENT(S): LTQ Orbitrap Velos, LTQ Orbitrap XL, LTQ Orbitrap Elite

ORGANISM(S): Rattus Sp. (ncbitaxon:10118) Homo Sapiens (ncbitaxon:9606)

SUBMITTER: John R. Yates III

PROVIDER: MSV000082908 | MassIVE |

REPOSITORIES: MassIVE

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

Purinosome Protein PTM Analysis

Project description:This data supports a publication on the PTM status of purinosome proteins transiently expressed in HEK293 cells under +/-purine supplementation cell culture conditions.

2018-06-24 | MSV000082496 | MassIVE

SCASP-PTM multiple PTM enrichment method

Project description:Multiple post-translational modification (PTM) proteomics generally relies on combining the enrichment of various PTMs with multiplex isobaric labeling and extensive peptide fractionation. However, effective methods for sequentially enriching multiple PTMs from a single sample for data-independent acquisition mass spectrometry (DIA-MS) are still lacking. Here, we present SCASP-PTM, a novel approach enabling desalting-free enrichment of diverse PTMs—including phosphopeptides, ubiquitinated peptides, acetylated peptides, glycopeptides, and biotinylated peptides. SCASP-PTM utilizes SDS for protein denaturation, which is sequestered by cyclodextrins before trypsin digestion, allowing sequential PTM enrichment without additional purification steps. By combing SCASP-PTM with DIA-MS, we quantified the proteome, ubiquitinome, phosphoproteome, and glycoproteome from 18 poly(I:C)-treated HeLa-S3 cell samples, identifying serine 28 phosphorylation as the key driver of poly(I:C)-induced p62 degradation. Additionally, this method enabled the quantification of proteome, ubiquitinome, acetylomes, phosphoproteome, and glycoproteome from 32 clinical tissue samples, revealing that ubiquitination/acetylation of lysine 330 on ALDOA is critical for tumor progression. In summary, SCASP-PTM is a robust method by enabling desalting-free, sequential enrichment of multiple PTMs from a single sample, offering a streamlined workflow for comprehensive PTM analysis when combined with DIA-MS in both basic research and clinical application.

2024-10-12 | PXD056746 |

Project description:under different water temperature culture conditions.

| PRJNA1012676 | ENA

Project description:sewer sediments under different nitrogen conditions

| PRJNA1124238 | ENA

Project description:sewer sediment under different nitrogen conditions

| PRJNA1123178 | ENA

Transcriptomic analysis of HCT116 cells cultured under different oxygen conditions

Project description:Transcriptomic analysis of HCT116 cells cultured under different oxygen conditions

| PRJNA430679 | ENA

Transcriptome analysis of mouse heart under different intermittent fasting conditions

Project description:Transcriptome analysis of mouse heart under different intermittent fasting conditions

| PRJNA550998 | ENA

Flow-injection analysis of Saccharomyces cerevisiae mutant AYT1

Project description:The intracellular metabolome of S. cerevisiae mutants in the gene AYT1 were measured under glucose growth conditions, as well as growth on oleate.

2021-01-27 | MSV000086772 | MassIVE

Substrate selectivity of semisynthetic Akt with pSer473 or O-GlcNAcSer473

Project description:Akt is a Ser/Thr protein kinase that regulates cell growth, metabolism and is considered a therapeutic target for cancer. Regulation of Akt by membrane recruitment and post-translational modifications (PTMs) has been extensively studied. The most well-established mechanism for cellular Akt activation involves phosphorylation on its activation loop on Thr308 by PDK1 and on its C-terminal tail on Ser473 by mTORC2. Other C-terminal tail PTMs have been identified, but their functional impacts have not been well-characterized. We use expressed protein ligation (EPL) as a tool to produce semisynthetic Akt proteins to dissect the enzymatic functions of these PTMs. We performed kinase assays employing human protein microarrays to investigate global substrate specificity of Akt, comparing phosphorylated vs. O-GlcNAcylated Ser473 forms.

2021-08-13 | GSE181983 | GEO

Histone PTM profiling analysis of EZH2 mutants in isogenic cells

Project description:The Enhancer of Zeste 2 Polycomb Repressive Complex 2 Subunit (EZH2) is an essential epigenetic modifier able to methylate lysine 27 on histone H3 (H3K27) to induce chromatin compaction, protein complex recruitment and ultimately transcriptional repression. Hematologic malignancies, including Diffuse Large B cell lymphoma (DLBCL) and Acute myeloid leukemia (AML) have shown a high EZH2-mutation frequency (>20%) associated with poor clinical outcomes. Particularly, two distinct oncogenic mutations, so-called gain-of-function (Y641F and A677G) and loss-of-function (H689A and F667I) are found in the catalytic domain of EZH2. In this study, a comprehensive multi-omics approach was employed to characterize downstream effects of H3K27me3 deposition driven by EZH2 mutations. Human embryonic kidney cells (HEK293T) were transfected to generate three stable EZH2 mutants: EZH2(Y641F), EZH2(A677G), and EZH2(H689A/F667I), which were validated via immunoblotting and DIA-MS-based histone profiling assay. The histone profiling assay demonstrated a significant increase of approximately two-fold in H3.1/H3.3K27me3 for Y641F EZH2 mutant. There was a modest increase in the combinatorial PTMs H3.1/H3.3K27me3K36me1 and a significant depletion in H3.1 and H3.3 K27me2. The most depleted peptide was H3.3K27me2K36me2. For the A677G EZH2 mutant, the assay demonstrated an enrichment on H3.1/H3.3K27me3, combinatorial K27me3K36me1 and a slight increase in K27me1 and K18ac but only on H3.1. The most depleted peptide was H3.3K27me2K36me2. The H689A/F667I cell line has the most alterations in global histone PTMs. The most highly enriched were H3.1/H3.3K36me2, H3.1K9me3 and H3.3K36me1. The most depleted modifications were H3.1K23ac and H3.1K27me3.

2023-10-24 | PXD042953 | Pride

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