PXD008369-2

PXD008369 is an original dataset announced via ProteomeXchange.

Title	Widespread protein histidine phosphorylation in bacteria
Description	For decades, extreme difficulties in analyzing histidine phosphorylation have limited the study of phosphohistidine signaling. Here we report a method revealing widespread and abundant protein histidine phosphorylation in E. coli. Our new approach generated the largest E. coli phosphoproteome dataset to date, of which a remarkable high percentage (~10%) are phosphohistidine sites. This resource enables a major step forward towards a better understanding of the biological function of histidine phosphorylation.
HostingRepository	jPOST
AnnounceDate	2017-12-07
AnnouncementXML	Submission_2018-02-08_01:57:15.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Miao-Hsia Lin
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationList	iodoacetamide derivatized residue; (2S,3R)-3-hydroxyaspartic acid; L-aspartic 4-phosphoric anhydride
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2017-12-05 05:55:14	ID requested
1	2017-12-07 01:15:53	announced
⏵ 2	2018-02-08 01:57:16	announced	Updated PubMed.
3	2018-09-19 00:44:44	announced	Updated CV, FTP location and Modification list.
4	2021-02-04 17:33:00	announced	2021-02-04: Updated FTP location.
5	2022-09-18 02:24:59	announced	2022-09-18: Updated FTP location.

Potel CM, Lin MH, Heck AJR, Lemeer S, Widespread bacterial protein histidine phosphorylation revealed by mass spectrometry-based proteomics. Nat Methods, 15(3):187-190(2018) [pubmed]

submitter keyword: histidine phosphorylation, E. coli, phosphoproteome

Albert J.R. Heck
lab head
Miao-Hsia Lin
contact affiliation	Institute of Chemistry, Academia Sinica
dataset submitter

jPOST dataset URI