Mitogen-activated protein kinase 9 Adenovirus

A distant member of the MAP kinase family, designated c-Jun N-terminal kinase (JNK1), is activated by dual phosphorylation at a Thr-Pro-Tyr motif (as compared to the Thr-Glu-Tyr phosphorylation motif characteristic of MAP kinases) during response to ultraviolet (UV) light. JNK1 functions to phosphorylate c-Jun at N-terminal serine regulatory sites, Ser-63 and Ser-73, mapping within the transactivation domain. Phosphorylation of these sites in response to UV results in transcriptional activation of c-Jun. Two additional members of the JNK family, JNK2 (also designated p54(alpha), MAPK9) and JNK3 (also designated p54(beta)), were described in a study in which an independent isolate of JNK1 was designated p54(gamma). These proteins are designated stress-activated protein kinases, or SAPKs.