PKC-related serine/threonine-protein kinase and Rho/Rac effector protein that participates in specific signal transduction responses in the cell. Plays a role in the regulation of cell cycle progression, actin cytoskeleton assembly, cell migration, cell adhesion, tumor cell invasion and transcription activation signaling processes. Phosphorylates CTTN in hyaluronan-induced astrocytes and hence decreases CTTN ability to associate with filamentous actin. Phosphorylates HDAC5, therefore lead to impair HDAC5 import. Direct RhoA target required for the regulation of the maturation of primordial junctions into apical junction formation in bronchial epithelial cells. Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner. Stimulates FYN kinase activity that is required for establishment of skin cell-cell adhesion during keratinocytes differentiation. Regulates epithelial bladder cells speed and direction of movement during cell migration and tumor cell invasion. Inhibits Akt pro-survival-induced kinase activity. Mediates Rho protein-induced transcriptional activation via the c-fos serum response factor (SRF). Involved in the negative regulation of ciliogenesis (By similarity). ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Kinase activity is activated upon binding to GTP-bound Rho1/Rac1 GTPases. Activated by caspase-3 (CASP3) cleavage during apoptosis. Activated by lipids, particularly cardiolipin and to a lesser extent by other acidic phospholipids and unsaturated fatty acids. Two specific sites, Thr-815 (activation loop of the kinase domain) and Thr-957 (turn motif), need to be phosphorylated for its full activation (By similarity). Interacts (via the REM repeats) with RHOA (GTP-bound form preferentially) and interacts (via the REM repeats) with RAC1 (GTP-bound form preferentially); the interactions induce its autophosphorylation (PubMed:17403031, PubMed:20974804). Interacts with NCK1 (via SH3 domains) (PubMed:8910519). Interacts with RHOC. Interacts with NCK1 and NCK2 (By similarity). Interacts with CD44 (PubMed:17403031). Interacts (via C-terminal kinase domain) with PDPK1; the interaction stimulates PDPK1 kinase activity (By similarity). Interacts with MAP3K2; the interaction activates PRK2 kinase activity in a MAP3K2-independent kinase activity (PubMed:10818102). Interacts (via C-terminal domain) with AKT1; the interaction occurs with the C-terminal cleavage product of PRK2 in apoptotic cells. Interacts (via C-terminus) with PTPN13 (via PDZ 3 domain). Interacts with CDK10 (By similarity). Colocalizes with PTPN13 in lamellipodia-like structures, regions of large actin turnover. Accumulates during telophase at the cleavage furrow and concentrates finally around the midbody in cytokinesis. Recruited to nascent cell-cell contacts at the apical surface of cells. Ubiquitous. Highly expressed in liver and lung Expressed in astrocytes (at protein level). Ubiquitous. The N-terminal regioninterferes with the interaction between AKT1 and the C-terminal regionof PKN2. The C1 domain does not bind the diacylglycerol (DAG). The apoptotic C-terminal cleavage product inhibits EGF-induced kinase activity of AKT1 phosphorylation at 'Thr-308' and 'Ser-473' sites, PDPK1 autophosphorylation and kinases PRKCD and PRKCZ phosphorylations. Phosphorylated during mitosis (By similarity). Autophosphorylated. Phosphorylated. Phosphorylated by CDK10 (By similarity). Activated by limited proteolysis with trypsin. Proteolytically cleaved by caspase-3 during the induction of apoptotic cell death. Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.