Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Echinobase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
Echinobase
ECB-ART-38080
J Biochem 2003 Jan 01;1331:17-27. doi: 10.1093/jb/mvg019.
Show Gene links Show Anatomy links

The structure and function of PKN, a protein kinase having a catalytic domain homologous to that of PKC.

Mukai H .


???displayArticle.abstract???
PKN is a serine/threonine protein kinase that has a catalytic domain homologous to protein kinase C (PKC) family members and a unique regulatory region containing antiparallel coiled-coil (ACC) domains. PKN is the first identified serine/threonine protein kinase that can bind to and be activated by a small GTPase Rho, and it can also be activated by fatty acids such as arachidonic acid in vitro. PKN is widely distributed in various organisms such as mammal, frog, fly, and starfish. There are at least three different isoforms of PKN (PKNalpha/PAK-1/PRK-1, PKNbeta, and PRK2/PAK-2/PKNgamma) in mammals, each of which shows different enzymological properties, tissue distribution, and varied functions.

???displayArticle.pubmedLink??? 12761194
???displayArticle.link??? J Biochem


Genes referenced: LOC100893746 LOC586799 LOC590371 LOC592256 pkcl2 pkn2