PXD031829-1

PXD031829 is an original dataset announced via ProteomeXchange.

Title	Mass spectrometry-based analysis of kindlin phosphorylation, ubiquitination and interactome
Description	Kindlin is an essential activator of integrins and thus indispensable in cell to extracellular matrix (ECM) adhesion. Kindlin abundance and functions are tightly regulated by multiple mechanisms including post-translational modifications (PTMs). Despite the critical roles of kindlin during embryonic development and pathogenesis, the knowledge of kindlin’s PTMs and interactome is far from complete. Here we analyze the phosphorylation, ubiquitination and interacting partners of kindlin in flat, firmly adherent interphase cells and round, weakly attached mitotic cells by immunoprecipitation-based mass spectrometry (IP-MS). The analysis generated potential phosphorylation and ubiquitination sites as well as interactors of kindlin and paved the way to investigate PTMs and binding partners of kindlin.
HostingRepository	PRIDE
AnnounceDate	2022-02-22
AnnouncementXML	Submission_2022-02-22_12:23:31.713.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Nanpeng Chen
SpeciesList	scientific name: Mus musculus (Mouse); NCBI TaxID: 10090; scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	phosphorylated residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2022-02-22 08:49:30	ID requested
⏵ 1	2022-02-22 12:23:32	announced

Dataset with its publication pending

submitter keyword: Mass spectrometry, kindlin, phosphorylation, ubiquitination

Reinhard Fässler
contact affiliation	Max Planck Institute for Biochemistry
contact email	faessler@biochem.mpg.de
lab head
Nanpeng Chen
contact affiliation	Max Planck Institute for Biochemistry
contact email	nchen@biochem.mpg.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD031829
     1. Label: PRIDE project
     2. Name: Mass spectrometry-based analysis of kindlin phosphorylation, ubiquitination and interactome