PXD056543 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | PSKH1 kinase activity is differentially modulated via allosteric binding of Ca2+ sensor proteins |
Description | Protein Serine Kinase H1 (PSKH1) was recently identified as a crucial factor in kidney development and is overexpressed in prostate, lung and kidney cancers. However, little is known about PSKH1’s regulation, leading to its classification as a “dark” kinase. Here, we used biochemistry and mass spectrometry to define PSKH1’s consensus substrate motif, protein interactors, and how interactors, including Ca2+ sensor proteins, promote or suppress activity. |
HostingRepository | PRIDE |
AnnounceDate | 2025-01-26 |
AnnouncementXML | Submission_2025-01-26_13:42:31.725.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Laura Dagley |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | timsTOF Pro |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2024-10-07 05:14:31 | ID requested | |
⏵ 1 | 2025-01-26 13:42:32 | announced | |
Publication List
Dataset with its publication pending |
Keyword List
submitter keyword: Protein kinase |
allosteric regulation |
Calumenin |
ERC-55 |
Cab-45 |
Contact List
James M. Murphy |
contact affiliation | Head, Inflammation Division Professor and NHMRC Leadership Fellow Walter and Eliza Hall Institute of Medical Research 1G Royal Parade Parkville, VIC 3052, Australia |
contact email | jamesm@wehi.edu.au |
lab head | |
Laura Dagley |
contact affiliation | WEHI |
contact email | dagley.l@wehi.edu.au |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD056543
- Label: PRIDE project
- Name: PSKH1 kinase activity is differentially modulated via allosteric binding of Ca2+ sensor proteins