Protein kinase N1

Serine/threonine-protein kinase N1 is an enzyme that in humans is encoded by the PKN1 gene.

PKN1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1CXZ, 1URF, 2RMK, 4NKG, 4OTD, 4OTG, 4OTH, 4OTI
Identifiers
Aliases	PKN1, DBK, PAK-1, PAK1, PKN, PKN-ALPHA, PRK1, PRKCL1, Protein kinase N1
External IDs	OMIM: 601032; MGI: 108022; HomoloGene: 48130; GeneCards: PKN1; OMA:PKN1 - orthologs
Gene location (Human) Chr. Chromosome 19 (human) Band 19p13.12 Start 14,433,053 bp End 14,471,867 bp
Gene location (Mouse) Chr. Chromosome 8 (mouse) Band 8 C2|8 40.22 cM Start 84,393,165 bp End 84,425,808 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in apex of heart granulocyte ventricular zone right lung stromal cell of endometrium muscle of thigh ganglionic eminence monocyte upper lobe of left lung gastric mucosa Top expressed in granulocyte thymus muscle of thigh superior frontal gyrus external carotid artery ventricular zone right ventricle primary visual cortex right kidney internal carotid artery More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity protein kinase activity nucleotide binding protein kinase C activity histone binding histone deacetylase binding chromatin binding histone kinase activity (H3-T11 specific) kinase activity protein serine/threonine kinase activity protein binding androgen receptor binding nuclear receptor coactivator activity ATP binding protein kinase C binding Cellular component cytoplasm cytosol endosome membrane plasma membrane nucleoplasm midbody cleavage furrow nucleus cytoplasmic vesicle protein-containing complex Biological process regulation of germinal center formation negative regulation of protein phosphorylation renal system process regulation of transcription, DNA-templated B cell apoptotic process negative regulation of protein kinase activity phosphorylation regulation of transcription by RNA polymerase II B cell homeostasis spleen development hyperosmotic response transcription, DNA-templated regulation of cell motility protein phosphorylation peptidyl-serine phosphorylation epithelial cell migration negative regulation of B cell proliferation regulation of immunoglobulin production signal transduction chromatin organization positive regulation of nucleic acid-templated transcription intracellular signal transduction Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5585 320795 Ensembl ENSG00000123143 ENSMUSG00000057672 UniProt Q16512 P70268 RefSeq (mRNA) NM_002741 NM_213560 NM_001199593 NM_177262 RefSeq (protein) NP_002732 NP_998725 NP_001186522 NP_796236 Location (UCSC) Chr 19: 14.43 – 14.47 Mb Chr 8: 84.39 – 84.43 Mb PubMed search
Wikidata
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Function

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.

Interactions

Protein kinase N1 has been shown to interact with:

• AKAP9,
• Actinin, alpha 1,
• CCDC85B,
• NEFL,
• NEUROD2
• Phosphoinositide-dependent kinase-1,
• Phospholipase D1,
• RHOA, and
• Vimentin.
• TRAF1.

Further reading

• Palmer RH, Ridden J, Parker PJ (1995). "Cloning and expression patterns of two members of a novel protein-kinase-C-related kinase family". Eur. J. Biochem. 227 (1–2): 344–51. doi:10.1111/j.1432-1033.1995.tb20395.x. PMID 7851406.
• Chu W, Presky DH, Danho W, Swerlick RA, Burns DK (1994). "Identification and characterization of DBK, a novel putative serine/threonine protein kinase from human endothelial cells". Eur. J. Biochem. 225 (2): 695–702. doi:10.1111/j.1432-1033.1994.00695.x. PMID 7957185.
• Palmer RH, Ridden J, Parker PJ (1994). "Identification of multiple, novel, protein kinase C-related gene products". FEBS Lett. 356 (1): 5–8. doi:10.1016/0014-5793(94)01202-4. PMID 7988719. S2CID 32020105.
• Mukai H, Ono Y (1994). "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. 199 (2): 897–904. doi:10.1006/bbrc.1994.1313. PMID 8135837.
• Palmer RH, Schönwasser DC, Rahman D, Pappin DJ, Herget T, Parker PJ (1996). "PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163". FEBS Lett. 378 (3): 281–5. doi:10.1016/0014-5793(95)01454-3. PMID 8557118. S2CID 46417714.
• Amano M, Mukai H, Ono Y, Chihara K, Matsui T, Hamajima Y, Okawa K, Iwamatsu A, Kaibuchi K (1996). "Identification of a putative target for Rho as the serine-threonine kinase protein kinase N". Science. 271 (5249): 648–50. Bibcode:1996Sci...271..648A. doi:10.1126/science.271.5249.648. PMID 8571127. S2CID 206575961.
• Mukai H, Toshimori M, Shibata H, Kitagawa M, Shimakawa M, Miyahara M, Sunakawa H, Ono Y (1996). "PKN associates and phosphorylates the head-rod domain of neurofilament protein". J. Biol. Chem. 271 (16): 9816–22. doi:10.1074/jbc.271.16.9816. PMID 8621664.
• Brown JL, Stowers L, Baer M, Trejo J, Coughlin S, Chant J (1996). "Human Ste20 homologue hPAK1 links GTPases to the JNK MAP kinase pathway". Curr. Biol. 6 (5): 598–605. Bibcode:1996CBio....6..598B. doi:10.1016/S0960-9822(02)00546-8. PMID 8805275. S2CID 9697114.
• Mukai H, Miyahara M, Sunakawa H, Shibata H, Toshimori M, Kitagawa M, Shimakawa M, Takanaga H, Ono Y (1996). "Translocation of PKN from the cytosol to the nucleus induced by stresses". Proc. Natl. Acad. Sci. U.S.A. 93 (19): 10195–9. Bibcode:1996PNAS...9310195M. doi:10.1073/pnas.93.19.10195. PMC 38360. PMID 8816775.
• Mukai H, Toshimori M, Shibata H, Takanaga H, Kitagawa M, Miyahara M, Shimakawa M, Ono Y (1997). "Interaction of PKN with alpha-actinin". J. Biol. Chem. 272 (8): 4740–6. doi:10.1074/jbc.272.8.4740. PMID 9030526.
• Matsuzawa K, Kosako H, Inagaki N, Shibata H, Mukai H, Ono Y, Amano M, Kaibuchi K, Matsuura Y, Azuma I, Inagaki M (1997). "Domain-specific phosphorylation of vimentin and glial fibrillary acidic protein by PKN". Biochem. Biophys. Res. Commun. 234 (3): 621–5. doi:10.1006/bbrc.1997.6669. PMID 9175763.
• Goedert M, Hasegawa M, Jakes R, Lawler S, Cuenda A, Cohen P (1997). "Phosphorylation of microtubule-associated protein tau by stress-activated protein kinases". FEBS Lett. 409 (1): 57–62. doi:10.1016/S0014-5793(97)00483-3. PMID 9199504. S2CID 36383041.
• Flynn P, Mellor H, Palmer R, Panayotou G, Parker PJ (1998). "Multiple interactions of PRK1 with RhoA. Functional assignment of the Hr1 repeat motif". J. Biol. Chem. 273 (5): 2698–705. doi:10.1074/jbc.273.5.2698. PMID 9446575.
• Bekri S, Adélaïde J, Merscher S, Grosgeorge J, Caroli-Bosc F, Perucca-Lostanlen D, Kelley PM, Pébusque MJ, Theillet C, Birnbaum D, Gaudray P (1997). "Detailed map of a region commonly amplified at 11q13-->q14 in human breast carcinoma". Cytogenet. Cell Genet. 79 (1–2): 125–31. doi:10.1159/000134699. PMID 9533029.
• Zheng-Fischhöfer Q, Biernat J, Mandelkow EM, Illenberger S, Godemann R, Mandelkow E (1998). "Sequential phosphorylation of Tau by glycogen synthase kinase-3beta and protein kinase A at Thr212 and Ser214 generates the Alzheimer-specific epitope of antibody AT100 and requires a paired-helical-filament-like conformation". Eur. J. Biochem. 252 (3): 542–52. doi:10.1046/j.1432-1327.1998.2520542.x. PMID 9546672.
• Takanaga H, Mukai H, Shibata H, Toshimori M, Ono Y (1998). "PKN interacts with a paraneoplastic cerebellar degeneration-associated antigen, which is a potential transcription factor". Exp. Cell Res. 241 (2): 363–72. doi:10.1006/excr.1998.4060. PMID 9637778.
• Takahashi M, Mukai H, Toshimori M, Miyamoto M, Ono Y (1998). "Proteolytic activation of PKN by caspase-3 or related protease during apoptosis". Proc. Natl. Acad. Sci. U.S.A. 95 (20): 11566–71. Bibcode:1998PNAS...9511566T. doi:10.1073/pnas.95.20.11566. PMC 21681. PMID 9751706.
• Hanger DP, Betts JC, Loviny TL, Blackstock WP, Anderton BH (1998). "New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometry". J. Neurochem. 71 (6): 2465–76. doi:10.1046/j.1471-4159.1998.71062465.x. PMID 9832145. S2CID 45602824.
• Takahashi M, Shibata H, Shimakawa M, Miyamoto M, Mukai H, Ono Y (1999). "Characterization of a novel giant scaffolding protein, CG-NAP, that anchors multiple signaling enzymes to centrosome and the golgi apparatus". J. Biol. Chem. 274 (24): 17267–74. doi:10.1074/jbc.274.24.17267. PMID 10358086.