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
Proteomicsjournal_title
Proteomicsauthors
Gao Y,Lee H,Kwon OK,Cheng Z,Tan M,Kim KT,Lee Sdoi
10.1002/pmic.201800471subject
Has Abstractpub_date
2019-05-01 00:00:00pages
e1800471issue
9eissn
1615-9853issn
1615-9861journal_volume
19pub_type
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