A conserved motif at the amino termini of MEKs might mediate high-affinity interaction with the cognate MAPKs.
Bardwell
L
L
Department of Molecular and Cell Biology, University of California, Berkeley 94720-3202, USA. jthorner@mendel.berkeley.edu
Thorner
J
J
D000595:Amino Acid Sequence; D017871:Calcium-Calmodulin-Dependent Protein Kinases / Q000378:metabolism*; D017124:Conserved Sequence / Q000235:genetics; D005656:Fungal Proteins / Q000737:chemistry / Q000378:metabolism; D020929:Mitogen-Activated Protein Kinase Kinases; D008969:Molecular Sequence Data; D010675:Pheromones / Q000378:metabolism; D010766:Phosphorylation; D011494:Protein Kinases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment; D015398:Signal Transduction / Q000502:physiology*
D005656:Fungal Proteins; D010675:Pheromones; D011494:Protein Kinases; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D020929:Mitogen-Activated Protein Kinase Kinases