Article
Characterization of recombinant Xenopus MAP kinase kinases mutated at potential phosphorylation sites.
Oncogene - 1 Jul 1994
Gotoh Y, Matsuda S, Takenaka K, Hattori S, Iwamatsu A, Ishikawa M, Kosako H, Nishida E
Abstract excerpt
Xenopus mitogen-activated protein kinase kinase (MAPKK) previously inactivated with protein phosphatase 2A can be reactivated by serine phosphorylation catalyzed by a partially purified MAPKK kinase (MAPKK-K), and is phosphorylated by MAPK on a threonine residue. The sequence analysis of a threon...
Topics
- Amino Acid Sequence
- Animals
- Base Sequence
- DNA Primers
- Enzyme Activation
- Fungal Proteins
- Humans
- Mitogen-Activated Protein Kinase Kinases
- Molecular Sequence Data
- Mutation
- Phosphorylation
- Protein Kinases
- Protein Serine-Threonine Kinases
- Proto-Oncogene Proteins
- Proto-Oncogene Proteins c-raf
- Recombinant Proteins
- Schizosaccharomyces pombe Proteins
- Sequence Alignment