PXD025873

PXD025873 is an original dataset announced via ProteomeXchange.

Title	Phosphorylation of Hsp90 on serine residues in the charged linker modulates binding to interacting proteins and has implications for overall Hsp90β conformation
Description	Serine residues in the charged linker region of human Hsp90beta are highly phoshporylated in vivo. Mutation of these residues to alanines resulted in altered binding of many Hsp90beta interactors. This project contains the data and searches related to co-immunoprecipitation experiments with wild-type and mutant Hsp90beta, as well as input.
HostingRepository	PRIDE
AnnounceDate	2021-07-07
AnnouncementXML	Submission_2021-07-07_00:17:37.954.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Manfredo Quadroni
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	isotope labeled residue; iodoacetamide derivatized residue
Instrument	Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2021-05-07 04:25:41	ID requested
⏵ 1	2021-07-07 00:17:38	announced

Dataset with its publication pending

submitter keyword: Hsp90, interactome, phosphorylation

Manfredo Quadroni
contact affiliation	Protein Analysis Facility, Université de Lausanne, Switzerland
contact email	manfredo.quadroni@unil.ch
lab head
Manfredo Quadroni
contact affiliation	University of Lausanne
contact email	manfredo.quadroni@unil.ch
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/2021/07/PXD025873

PRIDE project URI

• PRIDE
  1. PXD025873
     1. Label: PRIDE project
     2. Name: Phosphorylation of Hsp90 on serine residues in the charged linker modulates binding to interacting proteins and has implications for overall Hsp90β conformation