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andr21-sup-0001-FigS1-Part-1.tifimage/tif12593KFigure S1. Alignment of amino acid sequences of TSSK1, TSSK1B and TSSK2 in mammalian species. The multiple sequence alignment was performed using ClustalW1.83 program (Chenna et al., 2003). The amino acid sequence 1–272 represents the N-terminal domain, described in the present report, and the sequence from amino acid 273-end represents the C-terminus. The serine/threonine protein kinase catalytic domain, amino acid residues 1–269, was defined by a NCBI CDD search (Marchler-Bauer et al., 2005), and is shown as a black arrow bar. Completely conserved amino acid residues are indicated by asterisks. Amino acid residues consistently found in TSSK1B but not in TSSK1 or TSSK2 are indicated with a blue mark. The conserved lysine K27 is indicated with a green mark. Species represented are: human (Homo sapiens; Hs), chimpanzee (Pan troglodytes; Pt), gorilla (Gorilla gorilla; Gg), orangutan (Pongo pygmaeus; Pp), gibbon (Nomascus leucogenys; Nl), macaque (Macaca mulatta; Ma), marmoset (Callithrix jacchus; Cj), bushbaby (Otolemur garnetti; Og), mouse (Mus musculus; Mm), cattle (Bos taurus; Bt), dog (Canis familiaris; Cf), elephant (Loxodonta africana; La) and opossum (Monodelphis domestica; Md).
andr21-sup-0002-FigS1-Part-2.tifimage/tif7575K 
andr21-sup-0003-FigS2.tifimage/tif993KFigure S2. TSSK2 and TSSK2–27R in an in vitro phosphorylation assay. The enzymatic activity of human TSSK2–27R was examined in an in vitro phosphorylation assay, in which the wild-type human TSSK2 was used as a positive control and a 50 kDa human TSKS fragment was used as the substrate. Both wild-type TSSK2 and TSSK2–27R showed autophosphorylation (open arrow heads) and phosphorylation of the TSKS fragment (closed arrowheads).

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