Proteomics

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Zebrafish, LC-MS/MS - 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. 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 was performed using a TiO2 affinity technique. A total of 68 unique phosphohistidine sites were detected on 63 proteins among 1076 unique phosphosites on 708 proteins. This report provides the first phosphohistidine dataset obtained from zebrafish.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Danio Rerio (zebrafish) (brachydanio Rerio)

TISSUE(S): Embryo

SUBMITTER: Yan Gao  

LAB HEAD: Sangkyu Lee

PROVIDER: PXD012735 | Pride | 2019-03-21

REPOSITORIES: Pride

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Profiling of Histidine Phosphoproteome in Danio rerio by TiO<sub>2</sub> Enrichment.

Gao Yan Y   Lee Hyojin H   Kwon Oh Kwang OK   Cheng Zhongyi Z   Tan Minjia M   Kim Ki-Tae KT   Lee Sangkyu S  

Proteomics 20190418 9


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 TiO<sub>2</  ...[more]

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