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. Author manuscript; available in PMC: 2015 Jun 1.
Published in final edited form as: Chromosoma. 2013 Dec 6;123(3):169–181. doi: 10.1007/s00412-013-0446-5

Figure 1. Domain architecture of human KNL1.

Figure 1

Key regions involved in KNL1 function are indicated schematically (top), and the corresponding amino acid sequences for each region in human KNL1 are listed (bottom). Aurora B kinase phosphorylates the N-terminus of KNL1 to inhibit association with PP1 (Liu et al. 2010). Mps1 phosphorylates the KNL1 MELT repeats to promote association with Bub1 and Bub3 (London et al. 2012; Primorac et al. 2013; Shepperd et al. 2012; Yamagishi et al. 2012). Amino acid residues 1-68 indicate the MT binding domain (Welburn et al. 2010), and underlined is a basic patch of residues (RRRH), whose analogous residues in C. elegans have been implicated in direct MT interaction (Espeut et al. 2012).