Protein kinase N1

From Wikipedia, the free encyclopedia

Protein kinase N1

PDB rendering based on 1cxz.

Available structures: 1cxz, 1urf

Identifiers

Symbol(s)

PKN1; PAK1; DBK; MGC46204; PKN; PRK1; PRKCL1

External IDs

OMIM: 601032 MGI: 108022 HomoloGene: 48130

Gene ontology
Molecular Function:	• nucleotide binding • protein serine/threonine kinase activity • protein binding • ATP binding • transferase activity
Cellular Component:	• intracellular
Biological Process:	• protein amino acid phosphorylation • signal transduction • activation of JNK activity

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002741 (mRNA)
NP_002732 (protein)

NM_177262 (mRNA)
NP_796236 (protein)

Location

Chr 19: 14.41 - 14.44 Mb

Chr 8: 86.56 - 86.59 Mb

Pubmed search

[1]

[2]

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]

[edit] References

^ ^a ^b Entrez Gene: PKN1 protein kinase N1.

[edit] 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.