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Identification of mouse ULK1, a novel protein kinase structurally related to C. elegans UNC-51.

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 chromosome 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.

Pubmed ID: 9600096

Authors

  • Yan J
  • Kuroyanagi H
  • Kuroiwa A
  • Matsuda Y
  • Tokumitsu H
  • Tomoda T
  • Shirasawa T
  • Muramatsu M

Journal

Biochemical and biophysical research communications

Publication Data

May 8, 1998

Associated Grants

None

Mesh Terms

  • 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