Identification of mouse ULK1, a novel protein kinase structurally related to C. elegans UNC-51.
Journal:
Biochem. Biophys. Res. Commun. 1998 MayAuthors:
Yan J, Kuroyanagi H, Kuroiwa A, Matsuda Y, Tokumitsu H, Tomoda T, Shirasawa T, Muramatsu M
Abstract
A novel protein kinase related to the C. elegans serine/threonine kinase UNC-51 was cloned from mouse. The UNC-51-Like Kinase (ULK)1 is encoded by a cDNA of 1051 amino acids with calculated MW of 113 kDa. Comparison of the ULK1 and UNC-51 shows the highest conservation in the amino-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 and rat chro
...[more]mosome 12q16.3, by fluorescent in situ hybridization. HA-tagged ULK1 is expressed as a protein of approximately 150 kDa in COS7 cells and is auto-phosphorylated in vitro in its PS domain. We propose that ULK1, UNC-51 and a yeast protein kinase Apg1p comprise a novel subfamily of protein kinase, which is structurally conserved among eukaryotes.[less]
Mesh Headings:
Amino Acid Sequence, Animals, Base Sequence, Caenorhabditis elegans, Caenorhabditis elegans Proteins, Chromosome Mapping, Cloning, Molecular, DNA, Complementary, Gene Expression, Helminth Proteins, In Situ Hybridization, Fluorescence, Mice, Molecular Sequence Data, Molecular Weight, Phosphorylation, Protein Kinases, Protein-Serine-Threonine Kinases, RNA, Messenger, Rats, Sequence Homology, Amino Acid