Protein kinase N1

Protein kinase N1

Protein kinase N1, also known as PKN1, is a human gene.cite web | title = Entrez Gene: PKN1 protein kinase N1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5585| accessdate = ]

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summary_text = 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.cite web | title = Entrez Gene: PKN1 protein kinase N1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5585| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Palmer RH, Ridden J, Parker PJ |title=Cloning and expression patterns of two members of a novel protein-kinase-C-related kinase family. |journal=Eur. J. Biochem. |volume=227 |issue= 1-2 |pages= 344–51 |year= 1995 |pmid= 7851406 |doi=
*cite journal | author=Chu W, Presky DH, Danho W, "et al." |title=Identification and characterization of DBK, a novel putative serine/threonine protein kinase from human endothelial cells. |journal=Eur. J. Biochem. |volume=225 |issue= 2 |pages= 695–702 |year= 1994 |pmid= 7957185 |doi=
*cite journal | author=Palmer RH, Ridden J, Parker PJ |title=Identification of multiple, novel, protein kinase C-related gene products. |journal=FEBS Lett. |volume=356 |issue= 1 |pages= 5–8 |year= 1995 |pmid= 7988719 |doi=
*cite journal | author=Mukai H, Ono Y |title=A novel protein kinase with leucine zipper-like sequences: its catalytic domain is highly homologous to that of protein kinase C. |journal=Biochem. Biophys. Res. Commun. |volume=199 |issue= 2 |pages= 897–904 |year= 1994 |pmid= 8135837 |doi= 10.1006/bbrc.1994.1313
*cite journal | author=Palmer RH, Schönwasser DC, Rahman D, "et al." |title=PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163. |journal=FEBS Lett. |volume=378 |issue= 3 |pages= 281–5 |year= 1996 |pmid= 8557118 |doi=
*cite journal | author=Amano M, Mukai H, Ono Y, "et al." |title=Identification of a putative target for Rho as the serine-threonine kinase protein kinase N. |journal=Science |volume=271 |issue= 5249 |pages= 648–50 |year= 1996 |pmid= 8571127 |doi=
*cite journal | author=Mukai H, Toshimori M, Shibata H, "et al." |title=PKN associates and phosphorylates the head-rod domain of neurofilament protein. |journal=J. Biol. Chem. |volume=271 |issue= 16 |pages= 9816–22 |year= 1996 |pmid= 8621664 |doi=
*cite journal | author=Brown JL, Stowers L, Baer M, "et al." |title=Human Ste20 homologue hPAK1 links GTPases to the JNK MAP kinase pathway. |journal=Curr. Biol. |volume=6 |issue= 5 |pages= 598–605 |year= 1997 |pmid= 8805275 |doi=
*cite journal | author=Mukai H, Miyahara M, Sunakawa H, "et al." |title=Translocation of PKN from the cytosol to the nucleus induced by stresses. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 19 |pages= 10195–9 |year= 1996 |pmid= 8816775 |doi=
*cite journal | author=Mukai H, Toshimori M, Shibata H, "et al." |title=Interaction of PKN with alpha-actinin. |journal=J. Biol. Chem. |volume=272 |issue= 8 |pages= 4740–6 |year= 1997 |pmid= 9030526 |doi=
*cite journal | author=Matsuzawa K, Kosako H, Inagaki N, "et al." |title=Domain-specific phosphorylation of vimentin and glial fibrillary acidic protein by PKN. |journal=Biochem. Biophys. Res. Commun. |volume=234 |issue= 3 |pages= 621–5 |year= 1997 |pmid= 9175763 |doi= 10.1006/bbrc.1997.6669
*cite journal | author=Goedert M, Hasegawa M, Jakes R, "et al." |title=Phosphorylation of microtubule-associated protein tau by stress-activated protein kinases. |journal=FEBS Lett. |volume=409 |issue= 1 |pages= 57–62 |year= 1997 |pmid= 9199504 |doi=
*cite journal | author=Flynn P, Mellor H, Palmer R, "et al." |title=Multiple interactions of PRK1 with RhoA. Functional assignment of the Hr1 repeat motif. |journal=J. Biol. Chem. |volume=273 |issue= 5 |pages= 2698–705 |year= 1998 |pmid= 9446575 |doi=
*cite journal | author=Bekri S, Adélaïde J, Merscher S, "et al." |title=Detailed map of a region commonly amplified at 11q13-->q14 in human breast carcinoma. |journal=Cytogenet. Cell Genet. |volume=79 |issue= 1-2 |pages= 125–31 |year= 1998 |pmid= 9533029 |doi=
*cite journal | author=Zheng-Fischhöfer Q, Biernat J, Mandelkow EM, "et al." |title=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. |journal=Eur. J. Biochem. |volume=252 |issue= 3 |pages= 542–52 |year= 1998 |pmid= 9546672 |doi=
*cite journal | author=Bartsch JW, Mukai H, Takahashi N, "et al." |title=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. |journal=Genomics |volume=49 |issue= 1 |pages= 129–32 |year= 1998 |pmid= 9570957 |doi= 10.1006/geno.1997.5208
*cite journal | author=Takanaga H, Mukai H, Shibata H, "et al." |title=PKN interacts with a paraneoplastic cerebellar degeneration-associated antigen, which is a potential transcription factor. |journal=Exp. Cell Res. |volume=241 |issue= 2 |pages= 363–72 |year= 1998 |pmid= 9637778 |doi= 10.1006/excr.1998.4060
*cite journal | author=Takahashi M, Mukai H, Toshimori M, "et al." |title=Proteolytic activation of PKN by caspase-3 or related protease during apoptosis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 20 |pages= 11566–71 |year= 1998 |pmid= 9751706 |doi=
*cite journal | author=Hanger DP, Betts JC, Loviny TL, "et al." |title=New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometry. |journal=J. Neurochem. |volume=71 |issue= 6 |pages= 2465–76 |year= 1998 |pmid= 9832145 |doi=
*cite journal | author=Takahashi M, Shibata H, Shimakawa M, "et al." |title=Characterization of a novel giant scaffolding protein, CG-NAP, that anchors multiple signaling enzymes to centrosome and the golgi apparatus. |journal=J. Biol. Chem. |volume=274 |issue= 24 |pages= 17267–74 |year= 1999 |pmid= 10358086 |doi=

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