PXD009931

PXD009931 is an original dataset announced via ProteomeXchange.

Title	Systems-wide analysis of serine-ADP-ribosylation reveals widespread occurrence and site-specific overlap with phosphorylation (part 2, phosphorylation data)
Description	Here we report systems-wide identification of serine ADP-ribosylation sites and quantification of their cellular changes in human cells upon oxidative stress. High-resolution mass spectrometry and unrestricted data processing confirmed that serine residues are the major target of ADP-ribosylation in HeLa cells. Proteome-wide analyses identified 3,090 serine ADP-ribosylation sites, with 97 percent of acceptor sites modulated more than 2-fold upon oxidative stress, while treatment with PARP inhibitor Olaparib abrogates induction (part 1, ADP-ribosylation data, PXD009208). Consistent with the nuclear expression of ARTD1/PARP1 and ARTD2/PARP2, serine ADP-ribosylation prominently occurred on nuclear proteins. Structural-predictive analyses revealed that serine ADP-ribosylation preferentially resides in disordered regions, and identified serine ADP-ribosylation sites to significantly overlap with known phosphorylation sites. Large-scale phosphoproteomics analysis supported these observations (part 2, phosphorylation data), hereby providing first evidence for site-specific crosstalk between serine ADP-ribosylation and phosphorylation. Collectively, we demonstrate that serine ADP-ribosylation is a widespread modification and a major nuclear responder to oxidative stress, and that its regulatory scope is comparable to other posttranslational modifications.
HostingRepository	PRIDE
AnnounceDate	2018-08-29
AnnouncementXML	Submission_2018-08-31_05:53:06.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Ivo Hendriks
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	phosphorylated residue
Instrument	Q Exactive HF-X

Revision	Datetime	Status	ChangeLog Entry
0	2018-05-28 04:00:18	ID requested
1	2018-08-29 08:08:07	announced
⏵ 2	2018-08-31 05:53:07	announced	Updated publication reference for PubMed record(s): 30157440.

Larsen SC, Hendriks IA, Lyon D, Jensen LJ, Nielsen ML, Systems-wide Analysis of Serine ADP-Ribosylation Reveals Widespread Occurrence and Site-Specific Overlap with Phosphorylation. Cell Rep, 24(9):2493-2505.e4(2018) [pubmed]

curator keyword: Biological

submitter keyword: Phosphorylation, ADP-ribosylation, ADP

Michael Lund Nielsen
contact affiliation	Proteomics program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark
contact email	michael.lund.nielsen@cpr.ku.dk
lab head
Ivo Hendriks
contact affiliation	Novo Nordisk Foundation Center for Protein Research, University of Copenhagen
contact email	ivo.a.hendriks@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/2018/08/PXD009931

PRIDE project URI

• PRIDE
  1. PXD009931
     1. Label: PRIDE project
     2. Name: Systems-wide analysis of serine-ADP-ribosylation reveals widespread occurrence and site-specific overlap with phosphorylation (part 2, phosphorylation data)