The MAP kinase-activated protein kinase 2 contains a proline-rich SH3-binding domain.
The protein sequence of MAP kinase-activated protein kinase 2 (MAPKAP kinase 2) deduced from mouse cDNA sequence reveals structural features of the enzyme, which could be of importance for its function: a proline-rich SH3-binding domain N-terminal to the catalytic region, a MAP kinase phosphorylation site and a bipartite nuclear targeting sequence located C-terminal to the catalytic region. The catalytic domain itself has the strongest homology to calcium/calmodulin-dependent protein kinase II. Northern blot analysis demonstrates a 3.5 kb MAPKAP kinase 2 transcript which is ubiquitously expressed and, hence, co-expressed with the mRNA of the recently identified substrate Hsp25 in all tissues analysed. However, the functional consequences of the nuclear targeting sequence present in MAPKAP kinase 2 suggest the existence of further substrates for the enzyme in the nucleus.
Engel
K
K
Max-Delbrück-Center of Molecular Medicine, Berlin, Germany.
Plath
K
K
Gaestel
M
M
D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites; D018076:DNA, Complementary; D004789:Enzyme Activation; D006360:Heat-Shock Proteins / Q000096:biosynthesis / Q000235:genetics; D047908:Intracellular Signaling Peptides and Proteins; D008969:Molecular Sequence Data; D011392:Proline / Q000032:analysis*; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D012333:RNA, Messenger / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D000099190:MAP-Kinase-Activated Kinase 2
D018076:DNA, Complementary; D006360:Heat-Shock Proteins; D047908:Intracellular Signaling Peptides and Proteins; D011392:Proline; D017346:Protein Serine-Threonine Kinases; D012333:RNA, Messenger; D000099190:MAP-Kinase-Activated Kinase 2