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A homology probing approach was utilized to isolate a new human protein kinase. Deoxyoligonucleotide probes recognizing a conserved subdomain in the COOH-terminal portion of protein kinases identified a cDNA clone encoding a putative kinase with predicted serine/threonine phosphorylation specificity. The full-length, 1.7-kilobase pair cDNA hybridizes to 1.7- and 3.4-kilobase mRNA transcripts in a number of tissues. The size of the encoded protein is 454 amino acids and consists of an NH2-terminal 130-residue segment, which may represent a regulatory region, followed by a 324-residue catalytic domain. Comparisons and alignments of the primary sequence and predicted secondary structure of the catalytic region to other known kinases reveal that the new kinase, denoted "CLK" (for CDC-like kinase), represents a prototype for a new family of human protein kinases bearing significant homology to the yeast cdc2/CDC28 kinases that regulate the cell cycle.
K W Johnson, and
K A Smith
February 1991,
FEBS letters,
K W Johnson, and
K A Smith
October 1991,
Proceedings of the National Academy of Sciences of the United States of America,
K W Johnson, and
K A Smith
April 2003,
Biochemical and biophysical research communications,
K W Johnson, and
K A Smith
November 1992,
Oncogene,
K W Johnson, and
K A Smith
February 2000,
Biochimica et biophysica acta,
K W Johnson, and
K A Smith
November 1992,
Proceedings of the National Academy of Sciences of the United States of America,
K W Johnson, and
K A Smith
September 1989,
Molecular and cellular biology,
K W Johnson, and
K A Smith
March 1996,
Molecular marine biology and biotechnology,
K W Johnson, and
K A Smith
May 2014,
Current drug targets,
