PXD002411-2

PXD002411 is an original dataset announced via ProteomeXchange.

Title	Phosphoproteomic Profiling Reveals Epstein-Barr Virus Protein Kinase Integration of DNA Damage Response and Mitotic Signaling
Description	Epstein-Barr virus (EBV) is etiologically linked to infectious mononucleosis and several human cancers. EBV encodes a conserved protein kinase BGLF4 that plays a key role in the viral life cycle. To provide new insight into the host proteins regulated by BGLF4, we utilized SILAC-based quantitative proteomics to compare site-specific phosphorylation in BGLF4-expressing cells and found up-regulated phosphorylation of 3,046 unique sites on 1,328 proteins. Motif analysis of the upregulated phospho-proteins found enrichment in CDK1/BGLF4, ATM, ATR and Aurora kinase substrates while functional analyses revealed significant enrichment of pathways related to the DNA damage response, mitosis and cell cycle plus phosphorylation of nuclear pore proteins. Phosphorylation of proteins associated with the mitotic spindle assembly checkpoint (SAC) indicated checkpoint activation, an event that inactivates the anaphase promoting complex/cyclosome, APC/C. Our data reveal that manipulation of mitotic kinase signaling and SAC activation are mechanisms associated with lytic EBV replication.
HostingRepository	PRIDE
AnnounceDate	2015-12-07
AnnouncementXML	Submission_2016-01-05_15:13:19.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Renfeng Li
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue; 6x(13)C labeled residue
Instrument	LTQ Orbitrap Velos; LTQ Orbitrap Elite

Revision	Datetime	Status	ChangeLog Entry
0	2015-06-23 01:12:13	ID requested
1	2015-12-07 03:18:51	announced
⏵ 2	2016-01-05 15:13:21	announced	Updated publication reference for PubMed record(s): 26714015.
3	2024-10-22 04:05:52	announced	2024-10-22: Updated project metadata.

Li R, Liao G, Nirujogi RS, Pinto SM, Shaw PG, Huang TC, Wan J, Qian J, Gowda H, Wu X, Lv DW, Zhang K, Manda SS, Pandey A, Hayward SD, Phosphoproteomic Profiling Reveals Epstein-Barr Virus Protein Kinase Integration of DNA Damage Response and Mitotic Signaling. PLoS Pathog, 11(12):e1005346(2015) [pubmed]

submitter keyword: Epstein-Barr Virus, Protein Kinase, Phosphoproteome, Signaling

Renfeng Li
contact affiliation	School of Dentistry, Virginia Commonwealth University, Richmond, Virginia 23298 USA
contact email	rli@vcu.edu
lab head
Renfeng Li
contact affiliation	School of Dentistry, Virginia Commonwealth University, Richmond, Virginia 23298 USA
contact email	rli@vcu.edu
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/2015/12/PXD002411

PRIDE project URI

• PRIDE
  1. PXD002411
     1. Label: PRIDE project
     2. Name: Phosphoproteomic Profiling Reveals Epstein-Barr Virus Protein Kinase Integration of DNA Damage Response and Mitotic Signaling