Profiling of Histidine Phosphoproteome in Danio rerio by TiO2 Enrichment.

Abstract:

:Histidine phosphorylation is a reversible post-translational modification that is known to regulate signal transduction in prokaryotes. However, functional studies in eukaryotes have been largely neglected due to the labile nature of N-linked phosphorylated amino acids. In an effort to help elucidate the heretofore hidden vertebrate phosphoproteome, this report presents a global phosphorylation analysis of Danio rerio (zebrafish) larvae. Phosphopeptide enrichment is performed using a TiO2 affinity technique. A total of 68 unique phosphohistidine sites are detected on 63 proteins among 1076 unique phosphosites on 708 proteins. Data are available via ProteomeXchange with identifier PXD012735. This report provides the first phosphohistidine dataset obtained from zebrafish.

journal_name

Proteomics

journal_title

Proteomics

authors

Gao Y,Lee H,Kwon OK,Cheng Z,Tan M,Kim KT,Lee S

doi

10.1002/pmic.201800471

subject

Has Abstract

pub_date

2019-05-01 00:00:00

pages

e1800471

issue

9

eissn

1615-9853

issn

1615-9861

journal_volume

19

pub_type

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