PXD008931

PXD008931 is an original dataset announced via ProteomeXchange.

Title	Comprehensive Proteome Analyses of Lysine Acetylation in Tea leaves by sensing Nitrogen nutrition
Description	Acetylation of lysine is a highly dynamic and reversibly regulated post-translational modification (PTM), which changes protein function in multiple ways [1]. As one of the most common PTMs to proteins in both eukaryotes and prokaryotes [1, 2], lysine acetylation occurred on either the α-amino group at the N-terminus of the protein or the ε-amino group on the side chain of lysine residues[3]. Since the first reveal of lysine acetylome in mammalian cells [4], acetylome in eukaryotes has been reported and the mechanistic studies indicated that lysine acetylation impacted various cellular processes including transcriptional regulation and metabolic stability [5-8]. In addition, a growing number of studies indicated that lysine acetylation widely existed in prokaryotes, and functional annotation showed lysine acetylation plays a crucial role in metabolic pathways, stress responses and enzymatic activity regulations in bacteria [9-11].
HostingRepository	PRIDE
AnnounceDate	2018-11-30
AnnouncementXML	Submission_2019-02-15_09:07:17.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Rachel Green
SpeciesList	scientific name: Camellia sinensis; NCBI TaxID: 4442;
ModificationList	acetylated residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2018-02-12 07:45:04	ID requested
1	2018-11-30 05:08:06	announced
⏵ 2	2019-02-15 09:07:18	announced	Updated publication reference for PubMed record(s): 30477445.

Jiang J, Gai Z, Wang Y, Fan K, Sun L, Wang H, Ding Z, Comprehensive proteome analyses of lysine acetylation in tea leaves by sensing nitrogen nutrition. BMC Genomics, 19(1):840(2018) [pubmed]

curator keyword: Biological

submitter keyword: acetylation, acetylome, metabolism, PTM, tea, nitrogen, starvation, resupply

Zhaotang Ding
contact affiliation	Tea Research Institute, Qingdao Agricultural University, Qingdao, Shandong, China
contact email	dzttea@163.com
lab head
Rachel Green
contact affiliation	PTM Biolabs Inc.
contact email	xuan_mao@ptm-biolab.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/2018/11/PXD008931

PRIDE project URI

• PRIDE
  1. PXD008931
     1. Label: PRIDE project
     2. Name: Comprehensive Proteome Analyses of Lysine Acetylation in Tea leaves by sensing Nitrogen nutrition