PXD014028-1

PXD014028 is an original dataset announced via ProteomeXchange.

Title	A gatekeeper residue controls transcriptional activity of the extracellular signal-regulated protein kinase 5 (ERK5) through molecular interactions with the C terminal tail.
Description	We analyzed the interactome of the kinase ERK5 and its mutant Y733E in HeLa cells.
HostingRepository	PRIDE
AnnounceDate	2020-01-31
AnnouncementXML	Submission_2020-01-31_02:10:36.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Chiara Francavilla
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	phosphorylated residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2019-05-28 00:24:57	ID requested
⏵ 1	2020-01-31 02:10:37	announced
2	2024-10-22 04:55:59	announced	2024-10-22: Updated project metadata.

Dataset with its publication pending

curator keyword: Biological

submitter keyword: human, ERK5

Chiara Francavilla
contact affiliation	Division of Molecular&Cellular Functions | School of Biological Sciences | FBMH C.4252 | Michael Smith Building | Oxford Road | Manchester | M13 9PT Tel: +44 161 275 5208 | Email: chiara.francavilla@manchester.ac.uk
contact email	chiara.francavilla@manchester.ac.uk
lab head
Chiara Francavilla
contact affiliation	University of Manchester
contact email	chiara.francavilla@manchester.ac.uk
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/2020/01/PXD014028

PRIDE project URI

• PRIDE
  1. PXD014028
     1. Label: PRIDE project
     2. Name: A gatekeeper residue controls transcriptional activity of the extracellular signal-regulated protein kinase 5 (ERK5) through molecular interactions with the C terminal tail.