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PXD058704

PXD058704 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleAnalysis of mng-SHIP1-dCT with pY Peptide by HDX-MS
DescriptionHydrogen deuterium exchange mass spectrometry (HDX-MS) was used to analyze how the mng-SHIP1-dCT construct interacts receptor-derived phosphotryrosine peptides (pY) to probe how these peptides regulate SHIP1 autoinhibition. This HDX-MS helped to identify intramolecular contacts involved in the regulation of SHIP1 autoinibition. Results from this HDX analyzing the dimeric mng-SHIP1 construct are used in tandem with previous results analyzing the monomeric mini-SHIP construct to confirm the same mechanism of autoinhibtion exists. These results help confirm autoinhibition of monomeric SHIP1 is indeed likely regulated by the same mechanism to that of dimeric SHIP1.
HostingRepositoryPRIDE
AnnounceDate2025-10-15
AnnouncementXMLSubmission_2025-10-15_14:29:17.556.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterJohn Burke
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: NEWT:9606;
ModificationListphosphorylated residue
Instrumentimpact HD
Dataset History
RevisionDatetimeStatusChangeLog Entry
02024-12-09 12:37:23ID requested
12025-10-15 14:29:18announced
Publication List
10.1016/j.jbc.2025.110788;
Drew EE, Nyvall HG, Parson MAH, Talus RK, Burke JE, Hansen SD, SH2-mediated steric occlusion of the C2 domain regulates autoinhibition of SHIP1 inositol 5-phosphatase. J Biol Chem, ():110788(2025) [pubmed]
Keyword List
submitter keyword: SHIP1, HDX-MS
Contact List
Dr. John E. Burke
contact affiliationUniversity of Victoria
contact emailjeburke@uvic.ca
lab head
John Burke
contact affiliationUniversity of Victoria
contact emailjeburke@uvic.ca
dataset submitter
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Dataset FTP location
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PRIDE project URI
Repository Record List
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