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Functional analysis of HAE <i>in vitro</i> auto-phosphorylation sites.

By Isaiah Taylor (846370), Ying Wang (11406), Kati Seitz (846371), John Baer (846372), Stefan Bennewitz (846373), Brian P. Mooney (418500) and John C. Walker (728449)

Abstract

<p>A) Identified HAE auto-phosphorylation sites annotated on the amino acid sequence of the HAE intracellular domain. Conserved features of protein kinases, as well as the HAE specific juxtamembrane region and C-terminal tail, are annotated for reference. B) Ratio of mutant:wildtype <i>in situ</i> auto-phosphorylation levels of recombinant MBP-HAE mutants. N = 4 biological replicates. Wildtype is normalized to 1. Error bars represent the standard deviation. Tests for statistical significance were carried out by a one sample t-test. C) Representative stains for phosphorylation and total protein by Pro-Q Diamond and coomassie blue, respectively.</p

Topics: Biological Sciences, HAE activation segment residues exhibits, substrate specificity, HAESA, protein kinase activity, activation segment residue, modulates HAE activity, rlk, HAE protein kinase domain, analysis, activation segment phosphorylation site
Year: 2016
DOI identifier: 10.1371/journal.pone.0147203.g002
OAI identifier: oai:figshare.com:article/1638751
Provided by: FigShare
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