| First Author | Engel K | Year | 1993 |
| Journal | FEBS Lett | Volume | 336 |
| Issue | 1 | Pages | 143-7 |
| PubMed ID | 8262198 | Mgi Jnum | J:20645 |
| Mgi Id | MGI:68845 | Doi | 10.1016/0014-5793(93)81628-d |
| Citation | Engel K, et al. (1993) The MAP kinase-activated protein kinase 2 contains a proline-rich SH3-binding domain. FEBS Lett 336(1):143-7 |
| abstractText | 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. |
