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. 2019 Mar 20;11(3):393. doi: 10.3390/cancers11030393

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© 2019 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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The domain structure of FOXK2 protein. FOXK2 is composed of a forkhead-associated domain (FHA) localized towards the amino terminus and a highly conserved forkhead DNA-binding domain (FOX) localized towards the carboxy-terminal end of the protein. The FOX domain displays a nuclear localization signal (NLS) and mediates FOXK2 binding to consensus sequences with a GTAAACA core motif. The post-translational modifications (PTM) for FOXK2 are shown, where serines (S) are targets for phosphorylation by cyclin-dependent kinases (CDK) and lysines (K), for SUMOylation. Amino-acids sites which are targets for PTM are depicted above the scheme. FHRE, forkhead responsive elements.