Protein kinase N1

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Protein kinase N1
File:PBB Protein PKN1 image.jpg
PDB rendering based on 1cxz.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols PKN1 ; PAK1; DBK; MGC46204; PKN; PRK1; PRKCL1
External IDs Template:OMIM5 Template:MGI HomoloGene48130
RNA expression pattern
File:PBB GE PKN1 202161 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Protein kinase N1, also known as PKN1, is a human gene.[1]

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.[1]

References

  1. 1.0 1.1 "Entrez Gene: PKN1 protein kinase N1".

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. PMID 7851406.
  • Chu W, Presky DH, Danho W; et al. (1994). "Identification and characterization of DBK, a novel putative serine/threonine protein kinase from human endothelial cells". Eur. J. Biochem. 225 (2): 695–702. PMID 7957185.
  • Palmer RH, Ridden J, Parker PJ (1995). "Identification of multiple, novel, protein kinase C-related gene products". FEBS Lett. 356 (1): 5–8. PMID 7988719.
  • 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; et al. (1996). "PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163". FEBS Lett. 378 (3): 281–5. PMID 8557118.
  • Amano M, Mukai H, Ono Y; et al. (1996). "Identification of a putative target for Rho as the serine-threonine kinase protein kinase N.". Science. 271 (5249): 648–50. PMID 8571127.
  • Mukai H, Toshimori M, Shibata H; et al. (1996). "PKN associates and phosphorylates the head-rod domain of neurofilament protein". J. Biol. Chem. 271 (16): 9816–22. PMID 8621664.
  • Brown JL, Stowers L, Baer M; et al. (1997). "Human Ste20 homologue hPAK1 links GTPases to the JNK MAP kinase pathway". Curr. Biol. 6 (5): 598–605. PMID 8805275.
  • Mukai H, Miyahara M, Sunakawa H; et al. (1996). "Translocation of PKN from the cytosol to the nucleus induced by stresses". Proc. Natl. Acad. Sci. U.S.A. 93 (19): 10195–9. PMID 8816775.
  • Mukai H, Toshimori M, Shibata H; et al. (1997). "Interaction of PKN with alpha-actinin". J. Biol. Chem. 272 (8): 4740–6. PMID 9030526.
  • Matsuzawa K, Kosako H, Inagaki N; et al. (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; et al. (1997). "Phosphorylation of microtubule-associated protein tau by stress-activated protein kinases". FEBS Lett. 409 (1): 57–62. PMID 9199504.
  • Flynn P, Mellor H, Palmer R; et al. (1998). "Multiple interactions of PRK1 with RhoA. Functional assignment of the Hr1 repeat motif". J. Biol. Chem. 273 (5): 2698–705. PMID 9446575.
  • Bekri S, Adélaïde J, Merscher S; et al. (1998). "Detailed map of a region commonly amplified at 11q13-->q14 in human breast carcinoma". Cytogenet. Cell Genet. 79 (1–2): 125–31. PMID 9533029.
  • Zheng-Fischhöfer Q, Biernat J, Mandelkow EM; et al. (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. PMID 9546672.
  • Bartsch JW, Mukai H, Takahashi N; et al. (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): 129–32. doi:10.1006/geno.1997.5208. PMID 9570957.
  • Takanaga H, Mukai H, Shibata H; et al. (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; et al. (1998). "Proteolytic activation of PKN by caspase-3 or related protease during apoptosis". Proc. Natl. Acad. Sci. U.S.A. 95 (20): 11566–71. PMID 9751706.
  • Hanger DP, Betts JC, Loviny TL; et al. (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. PMID 9832145.
  • Takahashi M, Shibata H, Shimakawa M; et al. (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. PMID 10358086.