PXD009234 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Global phosphoproteomic analysis identifies SRMS-regulated signaling intermediates |
Description | The non-receptor tyrosine kinase, SRMS (Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristoylation sites) is a member of the BRK family kinases (BFKs) which represents an evolutionarily conserved relative of the Src family kinases (SFKs). Tyrosine kinases are known to regulate a number of cellular processes and pathways via phosphorylating substrate proteins directly and/or by partaking in signaling cross-talks leading to the indirect modulation of various signaling intermediates. In a previous study, we profiled the tyrosine-phosphoproteome of SRMS and identified multiple candidate substrates of the kinase. In order to uncover the broader SRMS-regulated phosphoproteome and identify the SRMS-regulated indirect signaling intermediates, we performed global phosphoproteomics analysis on cells expressing wild-type SRMS. Our analyses identified 60 hyperphosphorylated (phosphoserine/phosphothreonine) proteins mapped from 140 hyperphosphorylated peptides. Bioinfomatics analyses identified a number of significantly enriched biological and cellular processes among which DNA repair pathways were found to be upregulated while apoptotic pathways were found to be downregulated. Analyses of motifs derived from the upregulated phosphosites identified Casein kinase 2 alpha (CK2) as one of the major potential kinases contributing to the SRMS-dependent indirect regulation of signaling intermediates. Overall, our phosphoproteomics analyses identified serine/threonine phosphorylation dynamics as important secondary events of the SRMS-regulated phosphoproteome with implications in the regulation of cellular and biological processes. |
HostingRepository | PRIDE |
AnnounceDate | 2024-10-22 |
AnnouncementXML | Submission_2024-10-22_04:43:43.762.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Raghuveera Goel |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | phosphorylated residue |
Instrument | Q Exactive |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2018-03-16 07:29:02 | ID requested | |
1 | 2018-10-19 11:43:56 | announced | |
⏵ 2 | 2024-10-22 04:43:52 | announced | 2024-10-22: Updated project metadata. |
Publication List
10.1186/s12953-018-0143-7; |
Goel RK, Meyer M, Paczkowska M, Reimand J, Vizeacoumar F, Vizeacoumar F, Lam TT, Lukong KE, Global phosphoproteomic analysis identifies SRMS-regulated secondary signaling intermediates. Proteome Sci, 16():16(2018) [pubmed] |
Keyword List
curator keyword: Biological |
submitter keyword: FRK,SRMS, BRK, mass spectrometry, PTK5, PTK6, PTK70, Src, phosphoproteomics, non-receptor tyrosine kinase |
Contact List
Kiven Erique Lukong |
contact affiliation | Department of Biochemistry, College of Medicine, University of Saskatchewan |
contact email | kel232@mail.usask.ca |
lab head | |
Raghuveera Goel |
contact affiliation | University of Saskatchewan |
contact email | raghu.goel@usask.ca |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD009234
- Label: PRIDE project
- Name: Global phosphoproteomic analysis identifies SRMS-regulated signaling intermediates