Recombinant Human Serine/threonine-protein kinase N1 (PKN1), partial

Function

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

Subcellular Location

Cytoplasm; Nucleus; Endosome; Cell membrane (Peripheral membrane protein); Cleavage furrow; Midbody

Tissue Specificity

Found ubiquitously. Expressed in heart, brain, placenta, lung, skeletal muscle, kidney and pancreas. Expressed in numerous tumor cell lines, especially in breast tumor cells

Subunit

(Microbial infection) Interacts (via the second REM repeat) with S.typhimurium E3 ubiquitin-protein ligase SspH1 (via the leucine-rich repeat region) (PubMed:16611232, PubMed:24248594)

• Mukai H. et al. A novel protein kinase with leucine zipper-like sequences: its catalytic domain is highly homologous to that of protein kinase C. — Biochem. Biophys. Res. Commun. (1994)
• Palmer R.H. et al. Cloning and expression patterns of two members of a novel protein-kinase-C-related kinase family. — Eur. J. Biochem. (1995)
• Ota T. et al. Complete sequencing and characterization of 21,243 full-length human cDNAs. — Nat. Genet. (2004)
• Grimwood J. et al. The DNA sequence and biology of human chromosome 19. — Nature (2004)
• The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). — Genome Res. (2004)
• Palmer R.H. et al. Identification of multiple, novel, protein kinase C-related gene products. — FEBS Lett. (1994)
• Palmer R.H. et al. PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163. — FEBS Lett. (1996)
• Mukai H. et al. PKN associates and phosphorylates the head-rod domain of neurofilament protein. — J. Biol. Chem. (1996)