Protein kinase N1

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Protein kinase N1
Protein PKN1 PDB 1cxz.png
PDB rendering based on 1cxz.
Available structures
PDB Ortholog search: PDBe, RCSB
External IDs OMIM601032 MGI108022 HomoloGene48130 ChEMBL: 3384 GeneCards: PKN1 Gene
EC number
RNA expression pattern
PBB GE PKN1 202161 at tn.png
More reference expression data
Species Human Mouse
Entrez 5585 320795
Ensembl ENSG00000123143 ENSMUSG00000057672
UniProt Q16512 P70268
RefSeq (mRNA) NM_002741 NM_001199593
RefSeq (protein) NP_002732 NP_001186522
Location (UCSC) Chr 19:
14.54 – 14.58 Mb
Chr 8:
83.67 – 83.7 Mb
PubMed search [1] [2]

Serine/threonine-protein kinase N1 is an enzyme that in humans is encoded by the PKN1 gene.[1][2]

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.[2]


Protein kinase N1 has been shown to interact with Phospholipase D1,[3] Phosphoinositide-dependent kinase-1,[4] Vimentin,[5] AKAP9,[6] CCDC85B,[7] Actinin, alpha 1,[8] NEFL,[9] NEUROD2[10] and RHOA.[11][12][13]


  1. ^ Bartsch JW, Mukai H, Takahashi N, Ronsiek M, Fuchs S, Jockusch H, Ono Y (June 1998). "The protein kinase N (PKN) gene PRKCL1/Prkcl1 maps to human chromosome 19p12-p13.1 and mouse chromosome 8 with close linkage to the myodystrophy (myd) mutation". Genomics 49 (1): 129–132. doi:10.1006/geno.1997.5208. PMID 9570957. 
  2. ^ a b "Entrez Gene: PKN1 protein kinase N1". 
  3. ^ Oishi, K; Takahashi M; Mukai H; Banno Y; Nakashima S; Kanaho Y; Nozawa Y; Ono Y (May 2001). "PKN regulates phospholipase D1 through direct interaction". J. Biol. Chem. (United States) 276 (21): 18096–18101. doi:10.1074/jbc.M010646200. ISSN 0021-9258. PMID 11259428. 
  4. ^ Balendran, A; Biondi R M; Cheung P C; Casamayor A; Deak M; Alessi D R (July 2000). "A 3-phosphoinositide-dependent protein kinase-1 (PDK1) docking site is required for the phosphorylation of protein kinase Czeta (PKCzeta ) and PKC-related kinase 2 by PDK1". J. Biol. Chem. (UNITED STATES) 275 (27): 20806–20813. doi:10.1074/jbc.M000421200. ISSN 0021-9258. PMID 10764742. 
  5. ^ Matsuzawa, K; Kosako H, Inagaki N, Shibata H, Mukai H, Ono Y, Amano M, Kaibuchi K, Matsuura Y, Azuma I, Inagaki M (May 1997). "Domain-specific phosphorylation of vimentin and glial fibrillary acidic protein by PKN". Biochem. Biophys. Res. Commun. (UNITED STATES) 234 (3): 621–625. doi:10.1006/bbrc.1997.6669. ISSN 0006-291X. PMID 9175763. 
  6. ^ Takahashi, M; Shibata H; Shimakawa M; Miyamoto M; Mukai H; Ono Y (June 1999). "Characterization of a novel giant scaffolding protein, CG-NAP, that anchors multiple signaling enzymes to centrosome and the golgi apparatus". J. Biol. Chem. (UNITED STATES) 274 (24): 17267–17274. doi:10.1074/jbc.274.24.17267. ISSN 0021-9258. PMID 10358086. 
  7. ^ Rual, Jean-François; Venkatesan Kavitha, Hao Tong, Hirozane-Kishikawa Tomoko, Dricot Amélie, Li Ning, Berriz Gabriel F, Gibbons Francis D, Dreze Matija, Ayivi-Guedehoussou Nono, Klitgord Niels, Simon Christophe, Boxem Mike, Milstein Stuart, Rosenberg Jennifer, Goldberg Debra S, Zhang Lan V, Wong Sharyl L, Franklin Giovanni, Li Siming, Albala Joanna S, Lim Janghoo, Fraughton Carlene, Llamosas Estelle, Cevik Sebiha, Bex Camille, Lamesch Philippe, Sikorski Robert S, Vandenhaute Jean, Zoghbi Huda Y, Smolyar Alex, Bosak Stephanie, Sequerra Reynaldo, Doucette-Stamm Lynn, Cusick Michael E, Hill David E, Roth Frederick P, Vidal Marc (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature (England) 437 (7062): 1173–1178. doi:10.1038/nature04209. PMID 16189514. 
  8. ^ Feng, Shuju; Reséndiz Julio C; Christodoulides Nicolaos; Lu Xin; Arboleda David; Berndt Michael C; Kroll Michael H (January 2002). "Pathological shear stress stimulates the tyrosine phosphorylation of alpha-actinin associated with the glycoprotein Ib-IX complex". Biochemistry (United States) 41 (4): 1100–1108. doi:10.1021/bi0156005. ISSN 0006-2960. PMID 11802708. 
  9. ^ Mukai, H; Toshimori M; Shibata H; Kitagawa M; Shimakawa M; Miyahara M; Sunakawa H; Ono Y (April 1996). "PKN associates and phosphorylates the head-rod domain of neurofilament protein". J. Biol. Chem. (UNITED STATES) 271 (16): 9816–9822. doi:10.1074/jbc.271.16.9816. ISSN 0021-9258. PMID 8621664. 
  10. ^ Shibata, H; Oda H; Mukai H; Oishi K; Misaki K; Ohkubo H; Ono Y (December 1999). "Interaction of PKN with a neuron-specific basic helix-loop-helix transcription factor, NDRF/NeuroD2". Brain Res. Mol. Brain Res. (NETHERLANDS) 74 (1–2): 126–134. doi:10.1016/S0169-328X(99)00273-9. ISSN 0169-328X. PMID 10640683. 
  11. ^ Riento, Kirsi; Guasch Rosa M; Garg Ritu; Jin Boquan; Ridley Anne J (June 2003). "RhoE binds to ROCK I and inhibits downstream signaling". Mol. Cell. Biol. (United States) 23 (12): 4219–4229. doi:10.1128/MCB.23.12.4219-4229.2003. ISSN 0270-7306. PMC 156133. PMID 12773565. 
  12. ^ Alberts, A S; Bouquin N; Johnston L H; Treisman R (April 1998). "Analysis of RhoA-binding proteins reveals an interaction domain conserved in heterotrimeric G protein beta subunits and the yeast response regulator protein Skn7". J. Biol. Chem. (UNITED STATES) 273 (15): 8616–8622. doi:10.1074/jbc.273.15.8616. ISSN 0021-9258. PMID 9535835. 
  13. ^ Flynn, P; Mellor H; Palmer R; Panayotou G; Parker P J (January 1998). "Multiple interactions of PRK1 with RhoA. Functional assignment of the Hr1 repeat motif". J. Biol. Chem. (UNITED STATES) 273 (5): 2698–2705. doi:10.1074/jbc.273.5.2698. ISSN 0021-9258. PMID 9446575. 

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