PKN1

The protein encoded by this gene belongs to the protein kinase C superfamily. This kinase is activated by Rho family of small G proteins and may mediate the Rho-dependent signaling pathway. This kinase can be activated by phospholipids and by limited proteolysis. The 3-phosphoinositide dependent protein kinase-1 (PDPK1/PDK1) is reported to phosphorylate this kinase, which may mediate insulin signals to the actin cytoskeleton. The proteolytic activation of this kinase by caspase-3 or related proteases during apoptosis suggests its role in signal transduction related to apoptosis. Alternatively spliced transcript variants encoding distinct isoforms have been observed. [provided by RefSeq]

PKN1

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 transcription regulation. Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation of MAPK14. Regulates the cytoskeletal network by phosphorylating proteins such as VIM and neurofilament proteins NEFH, NEFL and NEFM, leading to inhibit their polymerization. Phosphorylates 'Ser-575', 'Ser-637' and 'Ser-669' of MAPT/Tau, lowering its ability to bind to microtubules, resulting in disruption of tubulin assembly. Acts as a key coactivator of androgen receptor (AR)-dependent transcription, by being recruited to AR target genes and specifically mediating phosphorylation of 'Thr-11' of histone H3 (H3T11ph), a specific tag for epigenetic transcriptional activation that promotes demethylation of histone H3 'Lys-9' (H3K9me) by KDM4C/JMJD2C. Phosphorylates HDAC5, HDAC7 and HDAC9, leading to impair their import in the nucleus. Phosphorylates 'Thr-38' of PPP1R14A, 'Ser-159', 'Ser-163' and 'Ser-170' of MARCKS, and GFAP. Able to phosphorylate RPS6 in vitro.

B cell apoptotic processIEA:Ensembl
B cell homeostasisIEA:Ensembl
Chromatin organizationIEA:UniProtKB-KW
Epithelial cell migrationManual Assertion Based On ExperimentIMP:UniProtKB
Histone H3-T11 phosphorylationManual Assertion Based On ExperimentIDA:UniProtKB
Hyperosmotic responseIEA:Ensembl
Intracellular signal transductionManual Assertion Based On ExperimentIBA:GO_Central
Negative regulation of B cell proliferationIEA:Ensembl
Negative regulation of protein kinase activityIEA:Ensembl
Peptidyl-serine phosphorylationManual Assertion Based On ExperimentIBA:GO_Central
Protein phosphorylationManual Assertion Based On ExperimentIDA:UniProtKB
Regulation of androgen receptor signaling pathwayTAS:Reactome
Regulation of cell motilityManual Assertion Based On ExperimentIMP:UniProtKB
Regulation of germinal center formationIEA:Ensembl
Regulation of immunoglobulin productionIEA:Ensembl
Regulation of transcription by RNA polymerase IIManual Assertion Based On ExperimentIDA:UniProtKB
Renal system processIEA:Ensembl
Signal transductionManual Assertion Based On ExperimentTAS:ProtInc
Spleen developmentIEA:Ensembl

Cytoplasm
Nucleus
Endosome
Cell membrane
Cleavage furrow
Midbody
Associates with chromatin in a ligand-dependent manner. Localization to endosomes is mediated via its interaction with RHOB. Association to the cell membrane is dependent on Ser-377 phosphorylation. Accumulates during telophase at the cleavage furrow and finally concentrates around the midbody in cytokinesis.

Autophosphorylated; preferably on serine. Phosphorylated during mitosis.
Activated by limited proteolysis with trypsin.
(Microbial infection) In case of infection, polyubiquitinated by the bacterial E3 ubiquitin-protein ligase SspH1, leading to its proteasomal degradation.