an AGC kinase of the PKN family. A PKC-related serine/threonine-protein kinase involved in various processes such as regulation of the intermediate filaments of the actin cytoskeleton, cell migration, tumor cell invasion and transcriptional regulation. Regulates the cytoskeletal network by phosphorylating intermediate filament proteins such as VIM and NFH, NFL and NFM, inhibiting their polymerization. Phosphorylates Tau, lowering its ability to bind to microtubules, resulting in disruption of tubulin assembly. Acts as a key coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of H3T11, a specific tag for epigenetic transcriptional activation that promotes demethylation of histone H3K9me by JMJD2C. Phosphorylates HDAC5, HDAC7 and HDAC9, impairing their import in the nucleus. Activated by lipids, particularly cardiolipin and to a lesser extent by other acidic phospholipids. Activated by CASP3 cleavage during apoptosis. Localization to endosomes is mediated via its interaction with RHOB. Accumulates during telophase at the cleavage furrow and finally concentrates around the midbody in cytokinesis. Three isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 126.96.36.199; Protein kinase, AGC; Protein kinase, Ser/Thr (non-receptor); Kinase, protein; AGC group; PKN family
Molecular Function: androgen receptor binding; ATP binding; chromatin binding; GTP-Rho binding; histone binding; histone deacetylase binding; ligand-dependent nuclear receptor transcription coactivator activity; protein binding; protein kinase activity; protein kinase C activity; protein kinase C binding; protein serine/threonine kinase activity; Rac GTPase binding
Biological Process: activation of JNK activity; B cell apoptosis; B cell homeostasis; hyperosmotic response; negative regulation of B cell proliferation; negative regulation of protein kinase activity; peptidyl-serine phosphorylation; protein amino acid phosphorylation; regulation of germinal center formation; regulation of immunoglobulin production; regulation of transcription from RNA polymerase II promoter; renal system process; signal transduction; spleen development; transcription, DNA-dependent
LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.