PXD033644-2

PXD033644 is an original dataset announced via ProteomeXchange.

Title	Transforming chemical proteomics into high-throughput method using SP2E workflow.
Description	Protein post-translational modifications (PTMs) play a critical role in regulation of protein catalytic activity, localization and protein-protein interactions. An attachment of PTMs onto proteins significantly diversify their structure and function resulting in so called proteoforms. However, the sole identification of post-translationally modified proteins, which are often cell type and disease specific, is still a highly challenging task. Sub-stoichiometric amounts and modification of low abundant proteins necessitate purification or enrichment of the modified proteins. Introduction of the mass spectrometry-based chemical proteomic strategy has enabled to screen protein PTMs with increased throughput, but the sample preparation has remained highly time consuming and tedious. Here, we report an optimized workflow for enrichment of PTM proteins in 96-well plate format which could be extended to robotic automation. This platform allows to significantly lower the input of total protein, which opens up the possibility to screen specialized and difficult to culture cell lines in high-throughput manner. The presented SP2E protocol is robust, time- and cost-effective as well as suitable for large-scale screening of proteoforms. Application of the SP2E protocol will thus enable the characterization of proteoforms in various processes such as neurodevelopment, neurodegeneration and cancer. This may contribute to an overall acceleration of the recently launched Human Proteoform Project.
HostingRepository	PRIDE
AnnounceDate	2023-11-14
AnnouncementXML	Submission_2023-11-14_08:56:51.123.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Tobias Becker
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	acetylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Fusion Lumos

Revision	Datetime	Status	ChangeLog Entry
0	2022-05-04 14:41:36	ID requested
1	2022-07-04 06:43:17	announced
⏵ 2	2023-11-14 08:56:51	announced	2023-11-14: Updated project metadata.

Dataset with its publication pending

submitter keyword: Method development, AMPylation

Dr. Pavel Kielkowski
contact affiliation	LMU Munich, Department of Chemistry
contact email	pavel.kielkwoski@cup.uni-muenchen.de
lab head
Tobias Becker
contact affiliation	Ludwig-Maximilians-University Junior Group Dr. Kielkowski
contact email	tobias.becker@cup.lmu.de
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2022/07/PXD033644

PRIDE project URI

• PRIDE
  1. PXD033644
     1. Label: PRIDE project
     2. Name: Transforming chemical proteomics into high-throughput method using SP2E workflow.