PXD038551

PXD038551 is an original dataset announced via ProteomeXchange.

Title	De novo BCR-ABL linear kinase motifs revealed by phosphoproteomics in yeast
Description	Protein tyrosine phosphorylation (pY) is central to many cellular signaling pathways. Deregulation of pY can lead to malignancies such as leukemia. Thus, assigning kinase-substrate relations is imperative to understand disease alterations. However, such efforts are complicated by kinase redundancy, overlapping specificity and magnitude differences in enzymatic activity. BCR/ABL, the predominant oncogene in leukemia, drives malignant transformation by deregulated tyrosine kinase activity. In this study, phosphorylation activity and specificity of human ABL1 and BCR/ABL have been examined in yeast by state-of-the-art phosphoproteomics. Linear sequence motif scores were generated and used for cross-kingdom (fungi to metazoa) phosphorylation analysis. Phosphoproteomic analysis of ABL1 and BCR/ABL yielded a high-confidence pY-dataset of 1186 peptides covering 1127 sites on 821 proteins. Motif scores generated from this dataset allow for examination of ABL1 and BCR/ABL kinase activity in human cell lines, and clearly identified BCR/ABL p210 in the chronic myeloid leukemia cell line K562. This cross-kingdom approach offers valuable insights into the human phosphoproteome.
HostingRepository	PRIDE
AnnounceDate	2023-11-14
AnnouncementXML	Submission_2023-11-14_09:03:15.986.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Ulrich Stelzl
SpeciesList	scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932;
ModificationList	phosphorylated residue
Instrument	timsTOF Pro

Revision	Datetime	Status	ChangeLog Entry
0	2022-12-05 05:10:51	ID requested
1	2023-07-20 11:19:16	announced
⏵ 2	2023-11-14 09:03:20	announced	2023-11-14: Updated project metadata.

Smolnig M, Fasching S, Stelzl U, Linear Phosphorylation Site Motifs for BCR-ABL Kinase Revealed by Phospho-Proteomics in Yeast. J Proteome Res, 22(6):1790-1799(2023) [pubmed]

submitter keyword: BCR-ABL, KSEA,Phosphoproteomics, ABL, linear sequence motif, Protein tyrosine phosphorylation

Ulrich Stelzl
contact affiliation	Network pharmacology, Institute of Pharmaceutical Sciences, University of Graz, Austria
contact email	ulrich.stelzl@uni-graz.at
lab head
Ulrich Stelzl
contact affiliation	University of Graz
contact email	ulrich.stelzl@uni-graz.at
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/2023/07/PXD038551

PRIDE project URI

• PRIDE
  1. PXD038551
     1. Label: PRIDE project
     2. Name: De novo BCR-ABL linear kinase motifs revealed by phosphoproteomics in yeast