PXD054515

PXD054515 is an original dataset announced via ProteomeXchange.

Title	Human cell LC-MS/MS detect interacting proteins and asymmetric dimethylation modifications of Protein arginine
Description	Prmt1, an epigenetic regulatory gene, is the subject of our research aimed at identifying its interacting protein partners and elucidating the arginine sites within these proteins that undergo asymmetric dimethylation modification by Prmt1, utilizing the advanced technique of Liquid Chromatography-Tandem Mass Spectrometry (Lc-ms/ms).
HostingRepository	PRIDE
AnnounceDate	2024-08-27
AnnouncementXML	Submission_2024-08-26_18:10:51.839.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Xin Zhang
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	asymmetric dimethyl-L-arginine
Instrument	TripleTOF 5600

Revision	Datetime	Status	ChangeLog Entry
0	2024-08-01 20:38:27	ID requested
⏵ 1	2024-08-26 18:10:52	announced

10.1016/J.CELREP.2024.114662;

submitter keyword: Human, Cell, LC-MS/MS

Zhongyuan Wang
contact affiliation	State Key Laboratory of Natural Medicines, School of Life Science and Technology, China Pharmaceutical University
contact email	wangzhongyuan@cpu.edu.cn
lab head
Xin Zhang
contact affiliation	China Pharmaceutical University
contact email	752469048@qq.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/2024/08/PXD054515

PRIDE project URI

• PRIDE
  1. PXD054515
     1. Label: PRIDE project
     2. Name: Human cell LC-MS/MS detect interacting proteins and asymmetric dimethylation modifications of Protein arginine