J. Yan et al., IDENTIFICATION OF MOUSE ULK1, A NOVEL PROTEIN-KINASE STRUCTURALLY RELATED TO C-ELEGANS UNC-51, Biochemical and biophysical research communications, 246(1), 1998, pp. 222-227
A novel protein kinase related to the C. elegans serine/threonine kina
se UNC-51 was cloned from mouse. The UNC-51-Like Kinase (ULK)1 is enco
ded by a cDNA of 1051 amino acids with calculated MW of 113 kDa. Compa
rison of the ULK1 and UNC-51 shows the highest conservation in the ami
no-terminal kinase domain, which is followed by a proline/serine-rich
(PS) domain and a conserved carboxyl-terminal (C) domain. ULK1 mRNA is
expressed in various tissues, and is mapped to mouse chromosome 5F an
d rat chromosome 12q16.3, by fluorescent in situ hybridization. PIA-ta
gged ULK1 is expressed as a protein of similar to 150 kDa in COS7 cell
s and is auto-phosphorylated in vitro in its PS domain. We propose tha
t ULK1, UNC-51 and a yeast protein kinase Apg1p comprise a novel subfa
mily of protein kinase, which is structurally conserved among eukaryot
es. (C) 1998 Academic Press.