A novel protein kinase with leucine zipper-like sequences: its catalytic domain is highly homologous to that of protein kinase C.
A novel protein kinase, designated PKN, was identified by molecular cloning from a human hippocampus cDNA library. PKN consists of 942 amino acids with a calculated molecular mass of 103,925 daltons. PKN has leucine zipper-like sequences in its amino terminal region and contains a catalytic domain that shows strong similarity to that of protein kinase C family. Northern blot analysis indicates PKN is expressed ubiquitously in human tissues. Antisera against PKN identified a 120K dalton protein on SDS polyacrylamide gel electrophoresis when PKN was expressed in the insect cells or COS7 cells. Recombinant PKN revealed an intrinsic protein kinase activity associated with a 120K protein. This activity was abolished by mutation of the lysine residue in the potential ATP binding site.
Mukai
H
H
Department of Biology, Faculty of Science, Kobe University, Japan.
Ono
Y
Y
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D015152:Blotting, Northern; D002460:Cell Line; D003001:Cloning, Molecular; D015870:Gene Expression; D015723:Gene Library; D006624:Hippocampus / Q000201:enzymology*; D006801:Humans; D016350:Leucine Zippers; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009036:Moths; D016297:Mutagenesis, Site-Directed; D011493:Protein Kinase C / Q000737:chemistry*; D017346:Protein Serine-Threonine Kinases; D011505:Protein-Tyrosine Kinases / Q000096:biosynthesis / Q000737:chemistry* / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D014162:Transfection
C061570:protein kinase N; D011505:Protein-Tyrosine Kinases; D017346:Protein Serine-Threonine Kinases; D011493:Protein Kinase C