PXD012026

PXD012026 is an original dataset announced via ProteomeXchange.

Title	Chemical phosphoproteomic approaches reveal substrate specificity of protein phosphatases-1 and -2
Description	The phosphatases PP1 and PP2A are responsible for the majority of dephosphorylation reactions on phosphoserine (pS) and –threonine (pT), and are involved in basically all cellular processes and many related diseases. They are thought to have no appreciable intrinsic substrate specificity, but to gain specificity only in their holoenzyme forms. Through the development of a peptide library approach and application of a complementary phosphoproteomics assay, we uncover that PP1 and PP2A show intrinsic specificity towards pT over pS, as well as toward the sequence context surrounding the phospho-site. Our substrate specificity data reveal that PP1 is a key regulator of the 14-3-3 protein binding motif, which enabled us to establish an unknown role for PP1 as a regulator of the GRB-associated-binding-protein 2 downstream (Gab2)/14-3-3 complex, exemplifying predictive potential of the data. Thus, this data should serve as a rich resource for (de)phosphorylation studies covering multiple cellular processes and phosphoproteins.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_05:08:59.407.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Stephanie Wilhelm
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	TMT6plex-126 reporter+balance reagent acylated residue; phosphorylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2018-12-12 00:20:48	ID requested
1	2020-07-14 03:49:31	announced
2	2020-08-11 04:33:34	announced	2020-08-11: Updated publication reference for PubMed record(s): 32681005.
⏵ 3	2024-10-22 05:09:00	announced	2024-10-22: Updated project metadata.

Hoermann B, Kokot T, Helm D, Heinzlmeir S, Chojnacki JE, Schubert T, Ludwig C, Berteotti A, Kurzawa N, Kuster B, Savitski MM, K, ö, hn M, Dissecting the sequence determinants for dephosphorylation by the catalytic subunits of phosphatases PP1 and PP2A. Nat Commun, 11(1):3583(2020) [pubmed]

10.1038/s41467-020-17334-x;

curator keyword: Biological

submitter keyword: co-immunoprecipitation,phosphatase substrates, quantitative phosphoproteomics

BayBioMS Bavarian Center for Biomolecular Mass Spectrometry
contact affiliation	Technical University of Munich TUM School of Life Scienes Weihenstephan Freising, Germany
contact email	stephanie.heinzlmeir@tum.de
lab head
Stephanie Wilhelm
contact affiliation	Chair of Proteomics and Bioanalytics, Technische Universität München, Germany
contact email	stephanie.heinzlmeir@tum.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/2020/07/PXD012026

PRIDE project URI

• PRIDE
  1. PXD012026
     1. Label: PRIDE project
     2. Name: Chemical phosphoproteomic approaches reveal substrate specificity of protein phosphatases-1 and -2