Protein kinase which is a key regulator of actin cytoskeleton and cell polarity. Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of ADD1, BRCA2, CNN1, EZR, DPYSL2, EP300, MSN, MYL9/MLC2, NPM1, RDX, PPP1R12A and VIM. Phosphorylates SORL1 and IRF4. Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Positively regulates the activation of p42/MAPK1-p44/MAPK3 and of p90RSK/RPS6KA1 during myogenic differentiation. Plays an important role in the timely initiation of centrosome duplication. Inhibits keratinocyte terminal differentiation. May regulate closure of the eyelids and ventral body wall through organization of actomyosin bundles. Plays a critical role in the regulation of spine and synaptic properties in the hippocampus. Homodimer. Interacts with IRS1, RHOB and RHOC. Interacts with RHOA (activated by GTP), PPP1R12A, CHORDC1, SORL1, EP300 and BRCA2. Interacts with NPM1 and this interaction enhances its activity. Interacts with RAF1. Activated by RHOA binding. Inhibited by Y-27632. Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. Note: This description may include information from UniProtKB.
Protein type: AGC group; DMPK family; EC 18.104.22.168; Kinase, protein; Protein kinase, AGC; Protein kinase, Ser/Thr (non-receptor); ROCK subfamily
Chromosomal Location of Human Ortholog: 12|12 A1.1
Molecular Function: ATP binding; kinase activity; metal ion binding; nucleotide binding; protein binding; protein kinase activity; protein serine/threonine kinase activity; Rho GTPase binding; Rho-dependent protein serine/threonine kinase activity; transferase activity
Biological Process: actin cytoskeleton organization; cellular response to testosterone stimulus; centrosome duplication; cortical actin cytoskeleton organization and biogenesis; dendrite morphogenesis; I-kappaB kinase/NF-kappaB signaling; induction of apoptosis via death domain receptors; negative regulation of angiogenesis; neural tube closure; peptidyl-serine phosphorylation; peptidyl-threonine phosphorylation; phosphorylation; positive regulation of amyloid-beta formation; positive regulation of cardiac muscle hypertrophy; positive regulation of centrosome duplication; positive regulation of connective tissue replacement; positive regulation of endothelial cell migration; positive regulation of gene expression; positive regulation of MAPK cascade; positive regulation of protein phosphorylation; protein amino acid phosphorylation; protein localization to plasma membrane; regulation of actin cytoskeleton organization; regulation of angiotensin-activated signaling pathway; regulation of circadian rhythm; regulation of keratinocyte differentiation; regulation of protein metabolic process; response to transforming growth factor beta; Rho protein signal transduction; rhythmic process; smooth muscle contraction