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 = ]

PBB_Summary
section_title =
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=

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes


Wikimedia Foundation. 2010.

Look at other dictionaries:

  • Protein kinase D1 — Protein kinase D1, also known as PRKD1, is a human gene.cite web | title = Entrez Gene: PRKD1 protein kinase D1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene Cmd=ShowDetailView TermToSearch=5587| accessdate = ] PBB Summary section title …   Wikipedia

  • Protein kinase R — (Eukaryotic translation initiation factor 2 alpha kinase 2) is a protein protecting against viral infections. EIF2AK2 is its human gene.cite web | title = Entrez Gene: EIF2AK2 eukaryotic translation initiation factor 2 alpha kinase 2| url =… …   Wikipedia

  • Protein kinase C — ( PKC , EC number|2.7.11.13) is a family of protein kinases consisting of 10 isozymes.cite journal | author = Mellor H, Parker PJ | title = The extended protein kinase C superfamily | journal = Biochem. J. | volume = 332 ( Pt 2) | issue = | pages …   Wikipedia

  • Protein kinase Mζ — (also called PKMζ or PKMzeta) is the independent catalytic domain of protein kinase Cζ and, lacking an autoinhibitory regulatory domain of the full length PKCζ, is constitutively active. This constitutive or autonomous activity allows the kinase… …   Wikipedia

  • protein kinase C — sē n any of a group of isoenzymes of protein kinase that modify the conformation and activity of various intracellular proteins by catalyzing the phosphorylation of specific serine or threonine amino acid residues in the polypeptide chains of the …   Medical dictionary

  • protein kinase — n any of a class of allosteric enzymes that possess a catalytic subunit which transfers a phosphate from ATP to one or more amino acid residues (as serine, threonine, or tyrosine) in a protein s side chain resulting in a conformational change… …   Medical dictionary

  • Protein kinase A — In cell biology, Protein kinase A (PKA) refers to a family of enzymes whose activity is dependent on cellular levels of cyclic AMP (cAMP). PKA is also known as cAMP dependent protein kinase (EC 2.7.11.11). Protein kinase A has several functions… …   Wikipedia

  • Protein kinase — A protein kinase is a kinase enzyme that modifies other proteins by chemically adding phosphate groups to them (phosphorylation). This class of protein may further be separated into subsets as in the case of protein kinase C PKC alpha, PKC beta,… …   Wikipedia

  • protein kinase C — noun Date: 1981 a protein kinase that catalyzes the phosphorylation of specific serine or threonine amino acid residues …   New Collegiate Dictionary

  • protein kinase A — Cyclic AMP dependent protein kinase …   Dictionary of molecular biology


Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”

We are using cookies for the best presentation of our site. Continuing to use this site, you agree with this.