PXD048719-1

PXD048719 is an original dataset announced via ProteomeXchange.

Title	A Long-Range Recruitment Mechanism for mTORC2 Phosphorylation of Akt
Description	Study of the phosphorylation of human Akt1 (Akt) by mTOR complex 2 (mTORC2) in vitro. Akt was prepared by semi-synthesis, resulting in a non-phosphorylated C-tail, allowing unbiased study of the sites phosphorylated by mTORC2. Because enzymologic data showed that the canonical hydrophobic motif residue, Akt Ser473, accounts for only a portion of the phosphorylation, and because the C-tail has at least 4 known phospho sites (Ser473, Ser475, Ser477, Thr479) and numerous other candidates, we sought to determine the catalog of sites on Akt that mTORC2 phosphorylates.
HostingRepository	PRIDE
AnnounceDate	2026-02-02
AnnouncementXML	Submission_2026-02-02_06:06:25.801.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Brad Palanski
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: NEWT:9606;
ModificationList	phosphorylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	timsTOF

Revision	Datetime	Status	ChangeLog Entry
0	2024-01-19 11:42:23	ID requested
⏵ 1	2026-02-02 06:06:27	announced

Taylor MS, Chen M, Hancock M, Wranik M, Miller BD, O'Meara TR, Palanski BA, Ficarro SB, Groendyke BJ, Xiang Y, Kondo KT, Linde-Garelli KY, Lee MJ, Mondal D, Freund D, Congreve S, Matas K, Hennink M, Xibinaku K, Valenstein ML, van Eeuwen T, Marto JA, Sali A, Shi Y, Gray NS, Sabatini DM, Chu N, Rogala KB, Cole PA, Structural basis for the recruitment and selective phosphorylation of Akt by mTORC2. Science, ():eadv7111(2025) [pubmed]

10.1126/science.adv7111;

submitter keyword: Akt, AGC Kinase, mTORC2,mTOR, phosphorylation, hydrophobic motif

Philip Cole
contact affiliation	Division of Genetics, Department of Medicine, Brigham and Women's Hospital, Boston, Massachusetts 02115, United States. Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, United States.
contact email	pacole@bwh.harvard.edu
lab head
Brad Palanski
contact affiliation	Stanford University, Brigham and Women's Hospital, Harvard Medical School
contact email	bpalanski@gmail.com
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/2026/02/PXD048719

PRIDE project URI

• PRIDE
  1. PXD048719
     1. Label: PRIDE project
     2. Name: A Long-Range Recruitment Mechanism for mTORC2 Phosphorylation of Akt