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. 2020 Jul 2;477(13):2451–2475. doi: 10.1042/BCJ20200309

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© 2020 The Author(s)

This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY). Open access for this article was enabled by the participation of University of Liverpool in an all-inclusive Read & Publish pilot with Portland Press and the Biochemical Society under a transformative agreement with JISC.

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Figure 4. — (A) Centrinone-down-regulated phosphorylation site sequence conservation using IceLogo [66] reveals extensive Pro enrichment around the site of phosphorylation. (B) Frequency of novel Pro-directed motifs (blue), the known consensus sequence for Aurora A (RR[pS/pT]), or the acidic residue-rich motifs of PLK1 ([D/E]x[pS/pT]Φ, where Φ represents hydrophobic Y/F/I/L/V residues and x is any amino acid), PLK2 ([D/E]xx[pS/pT], PLK3 ([pS/pT]x[D/E]) or the classic hydrophobic PLK4 consensus ([pS/pT]ΦΦ) across all centrinone-down-regulated phosphorylation sites.