PKN2: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Serine/threonine-protein kinase N2''' is an [[enzyme]] that in humans is encoded by the ''PKN2'' [[gene]].<ref name="pmid7988719">{{cite journal | vauthors = 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 | date = January 1995 | pmid = 7988719 | pmc =  | doi = 10.1016/0014-5793(94)01202-4 }}</ref><ref name="pmid7851406">{{cite journal | vauthors = 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 = 344–351 | date = March 1995 | pmid = 7851406 | pmc = | doi = 10.1111/j.1432-1033.1995.tb20395.x }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PKN2 protein kinase N2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5586| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Interactions ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =  
| Name = Protein kinase N2
| HGNCid = 9406
| Symbol = PKN2
| AltSymbols =; PAK2; MGC150606; MGC71074; PRK2; PRKCL2; PRO2042; Pak-2
| OMIM = 602549
| ECnumber = 
| Homologene = 2054
| MGIid = 109211
| GeneAtlas_image1 = PBB_GE_PKN2_210969_at_tn.png
| GeneAtlas_image2 = PBB_GE_PKN2_212628_at_tn.png
| GeneAtlas_image3 = PBB_GE_PKN2_212629_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007165 |text = signal transduction}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5586
    | Hs_Ensembl = ENSG00000065243
    | Hs_RefseqProtein = NP_006247
    | Hs_RefseqmRNA = NM_006256
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 88922493
    | Hs_GenLoc_end = 89074526
    | Hs_Uniprot = Q16513
    | Mm_EntrezGene = 109333
    | Mm_Ensembl = ENSMUSG00000004591
    | Mm_RefseqmRNA = NM_178654
    | Mm_RefseqProtein = NP_848769
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 3
    | Mm_GenLoc_start = 142730845
    | Mm_GenLoc_end = 142819376
    | Mm_Uniprot = Q3TBR3
  }}
}}
'''Protein kinase N2''', also known as '''PKN2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PKN2 protein kinase N2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5586| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
PKN2 has been shown to [[Protein-protein interaction|interact]] with:
{{PBB_Summary
{{div col|colwidth=20em}}
| section_title =  
* [[AKT1]],<ref name = pmid10926925>{{cite journal | vauthors = Koh H, Lee KH, Kim D, Kim S, Kim JW, Chung J | title = Inhibition of Akt and its anti-apoptotic activities by tumor necrosis factor-induced protein kinase C-related kinase 2 (PRK2) cleavage | journal = J. Biol. Chem. | volume = 275 | issue = 44 | pages = 34451–8 | date = November 2000 | pmid = 10926925 | doi = 10.1074/jbc.M001753200 }}</ref>
| summary_text =  
* [[NCK1]],<ref name = pmid8910519>{{cite journal | vauthors = Quilliam LA, Lambert QT, Mickelson-Young LA, Westwick JK, Sparks AB, Kay BK, Jenkins NA, Gilbert DJ, Copeland NG, Der CJ | title = Isolation of a NCK-associated kinase, PRK2, an SH3-binding protein and potential effector of Rho protein signaling | journal = J. Biol. Chem. | volume = 271 | issue = 46 | pages = 28772–6 | date = November 1996 | pmid = 8910519 | doi =  10.1074/jbc.271.46.28772}}</ref><ref name = pmid10026169>{{cite journal | vauthors = Braverman LE, Quilliam LA | title = Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing adapter protein having similar binding and biological properties to Nck | journal = J. Biol. Chem. | volume = 274 | issue = 9 | pages = 5542–9 | date = February 1999 | pmid = 10026169 | doi =  10.1074/jbc.274.9.5542}}</ref>
}}
* [[PTPN13]],<ref name = pmid11356191>{{cite journal | vauthors = Gross C, Heumann R, Erdmann KS | title = The protein kinase C-related kinase PRK2 interacts with the protein tyrosine phosphatase PTP-BL via a novel PDZ domain binding motif | journal = FEBS Lett. | volume = 496 | issue = 2–3 | pages = 101–4 | date = May 2001 | pmid = 11356191 | doi = 10.1016/s0014-5793(01)02401-2}}</ref>  
* [[Phosphoinositide-dependent kinase-1]],<ref name = pmid11781095>{{cite journal | vauthors = Hodgkinson CP, Sale GJ | title = Regulation of both PDK1 and the phosphorylation of PKC-zeta and -delta by a C-terminal PRK2 fragment | journal = Biochemistry | volume = 41 | issue = 2 | pages = 561–9 | date = January 2002 | pmid = 11781095 | doi =  10.1021/bi010719z}}</ref><ref name = pmid10764742>{{cite journal | vauthors = Balendran A, Biondi RM, Cheung PC, Casamayor A, Deak M, Alessi DR | title = 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 | journal = J. Biol. Chem. | volume = 275 | issue = 27 | pages = 20806–13 | date = July 2000 | pmid = 10764742 | doi = 10.1074/jbc.M000421200 }}</ref>  and
* [[RHOA]].<ref name = pmid8910519/><ref name = pmid9446575>{{cite journal | vauthors = Flynn P, Mellor H, Palmer R, Panayotou G, Parker PJ | 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 | date = January 1998 | pmid = 9446575 | doi = 10.1074/jbc.273.5.2698}}</ref>
{{Div col end}}


==References==
== Further reading ==
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Quilliam LA, Lambert QT, Mickelson-Young LA, Westwick JK, Sparks AB, Kay BK, Jenkins NA, Gilbert DJ, Copeland NG, Der CJ | title = Isolation of a NCK-associated kinase, PRK2, an SH3-binding protein and potential effector of Rho protein signaling | journal = J. Biol. Chem. | volume = 271 | issue = 46 | pages = 28772–28776 | year = 1997 | pmid = 8910519 | doi = 10.1074/jbc.271.46.28772 }}
| citations =
* {{cite journal | vauthors = Yu W, Liu J, Morrice NA, Wettenhall RE | title = Isolation and characterization of a structural homologue of human PRK2 from rat liver. Distinguishing substrate and lipid activator specificities | journal = J. Biol. Chem. | volume = 272 | issue = 15 | pages = 10030–10034 | year = 1997 | pmid = 9092545 | doi = 10.1074/jbc.272.15.10030 }}
*{{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 | vauthors = Vincent S, Settleman J | title = The PRK2 kinase is a potential effector target of both Rho and Rac GTPases and regulates actin cytoskeletal organization | journal = Mol. Cell. Biol. | volume = 17 | issue = 4 | pages = 2247–56 | year = 1997 | pmid = 9121475 | pmc = 232074 | 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 | vauthors = Cryns VL, Byun Y, Rana A, Mellor H, Lustig KD, Ghanem L, Parker PJ, Kirschner MW, Yuan J | title = Specific proteolysis of the kinase protein kinase C-related kinase 2 by caspase-3 during apoptosis. Identification by a novel, small pool expression cloning strategy | journal = J. Biol. Chem. | volume = 272 | issue = 47 | pages = 29449–29453 | year = 1997 | pmid = 9368003 | doi = 10.1074/jbc.272.47.29449 }}
*{{cite journal | author=Quilliam LA, Lambert QT, Mickelson-Young LA, ''et al.'' |title=Isolation of a NCK-associated kinase, PRK2, an SH3-binding protein and potential effector of Rho protein signaling. |journal=J. Biol. Chem. |volume=271 |issue= 46 |pages= 28772-6 |year= 1997 |pmid= 8910519 |doi=  }}
* {{cite journal | vauthors = Braverman LE, Quilliam LA | title = Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing adapter protein having similar binding and biological properties to Nck | journal = J. Biol. Chem. | volume = 274 | issue = 9 | pages = 5542–5549 | year = 1999 | pmid = 10026169 | doi = 10.1074/jbc.274.9.5542 }}
*{{cite journal | author=Yu W, Liu J, Morrice NA, Wettenhall RE |title=Isolation and characterization of a structural homologue of human PRK2 from rat liver. Distinguishing substrate and lipid activator specificities. |journal=J. Biol. Chem. |volume=272 |issue= 15 |pages= 10030-4 |year= 1997 |pmid= 9092545 |doi= }}
* {{cite journal | vauthors = Flynn P, Mellor H, Casamassima A, Parker PJ | title = Rho GTPase control of protein kinase C-related protein kinase activation by 3-phosphoinositide-dependent protein kinase | journal = J. Biol. Chem. | volume = 275 | issue = 15 | pages = 11064–11070 | year = 2000 | pmid = 10753910 | doi = 10.1074/jbc.275.15.11064 }}
*{{cite journal | author=Vincent S, Settleman J |title=The PRK2 kinase is a potential effector target of both Rho and Rac GTPases and regulates actin cytoskeletal organization. |journal=Mol. Cell. Biol. |volume=17 |issue= 4 |pages= 2247-56 |year= 1997 |pmid= 9121475 |doi= }}
* {{cite journal | vauthors = Sun W, Vincent S, Settleman J, Johnson GL | title = MEK kinase 2 binds and activates protein kinase C-related kinase 2. Bifurcation of kinase regulatory pathways at the level of an MAPK kinase kinase | journal = J. Biol. Chem. | volume = 275 | issue = 32 | pages = 24421–24428 | year = 2000 | pmid = 10818102 | doi = 10.1074/jbc.M003148200 }}
*{{cite journal | author=Cryns VL, Byun Y, Rana A, ''et al.'' |title=Specific proteolysis of the kinase protein kinase C-related kinase 2 by caspase-3 during apoptosis. Identification by a novel, small pool expression cloning strategy. |journal=J. Biol. Chem. |volume=272 |issue= 47 |pages= 29449-53 |year= 1997 |pmid= 9368003 |doi= }}
* {{cite journal | vauthors = Koh H, Lee KH, Kim D, Kim S, Kim JW, Chung J | title = Inhibition of Akt and its anti-apoptotic activities by tumor necrosis factor-induced protein kinase C-related kinase 2 (PRK2) cleavage | journal = J. Biol. Chem. | volume = 275 | issue = 44 | pages = 34451–34458 | year = 2000 | pmid = 10926925 | doi = 10.1074/jbc.M001753200 }}
*{{cite journal | author=Braverman LE, Quilliam LA |title=Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing adapter protein having similar binding and biological properties to Nck. |journal=J. Biol. Chem. |volume=274 |issue= 9 |pages= 5542-9 |year= 1999 |pmid= 10026169 |doi= }}
* {{cite journal | vauthors = Gross C, Heumann R, Erdmann KS | title = The protein kinase C-related kinase PRK2 interacts with the protein tyrosine phosphatase PTP-BL via a novel PDZ domain binding motif | journal = FEBS Lett. | volume = 496 | issue = 2–3 | pages = 101–104 | year = 2001 | pmid = 11356191 | doi = 10.1016/S0014-5793(01)02401-2 }}
*{{cite journal | author=Flynn P, Mellor H, Casamassima A, Parker PJ |title=Rho GTPase control of protein kinase C-related protein kinase activation by 3-phosphoinositide-dependent protein kinase. |journal=J. Biol. Chem. |volume=275 |issue= 15 |pages= 11064-70 |year= 2000 |pmid= 10753910 |doi= }}
* {{cite journal | vauthors = Hodgkinson CP, Sale GJ | title = Regulation of both PDK1 and the phosphorylation of PKC-zeta and -delta by a C-terminal PRK2 fragment | journal = Biochemistry | volume = 41 | issue = 2 | pages = 561–569 | year = 2002 | pmid = 11781095 | doi = 10.1021/bi010719z }}
*{{cite journal | author=Sun W, Vincent S, Settleman J, Johnson GL |title=MEK kinase 2 binds and activates protein kinase C-related kinase 2. Bifurcation of kinase regulatory pathways at the level of an MAPK kinase kinase. |journal=J. Biol. Chem. |volume=275 |issue= 32 |pages= 24421-8 |year= 2000 |pmid= 10818102 |doi= 10.1074/jbc.M003148200 }}
* {{cite journal | vauthors = McDonald C, Vacratsis PO, Bliska JB, Dixon JE | title = The yersinia virulence factor YopM forms a novel protein complex with two cellular kinases | journal = J. Biol. Chem. | volume = 278 | issue = 20 | pages = 18514–18523 | year = 2003 | pmid = 12626518 | doi = 10.1074/jbc.M301226200 }}
*{{cite journal | author=Koh H, Lee KH, Kim D, ''et al.'' |title=Inhibition of Akt and its anti-apoptotic activities by tumor necrosis factor-induced protein kinase C-related kinase 2 (PRK2) cleavage. |journal=J. Biol. Chem. |volume=275 |issue= 44 |pages= 34451-8 |year= 2000 |pmid= 10926925 |doi= 10.1074/jbc.M001753200 }}
* {{cite journal | vauthors = Anderson NL, Polanski M, Pieper R, Gatlin T, Tirumalai RS, Conrads TP, Veenstra TD, Adkins JN, Pounds JG, Fagan R, Lobley A | title = The human plasma proteome: a nonredundant list developed by combination of four separate sources | journal = Mol. Cell. Proteomics | volume = 3 | issue = 4 | pages = 311–326 | year = 2004 | pmid = 14718574 | doi = 10.1074/mcp.M300127-MCP200 }}
*{{cite journal | author=Gross C, Heumann R, Erdmann KS |title=The protein kinase C-related kinase PRK2 interacts with the protein tyrosine phosphatase PTP-BL via a novel PDZ domain binding motif. |journal=FEBS Lett. |volume=496 |issue= 2-3 |pages= 101-4 |year= 2001 |pmid= 11356191 |doi= }}
* {{cite journal | vauthors = Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP | title = Large-scale characterization of HeLa cell nuclear phosphoproteins | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 101 | issue = 33 | pages = 12130–12135 | year = 2004 | pmid = 15302935 | pmc = 514446 | doi = 10.1073/pnas.0404720101 }}
*{{cite journal | author=Hodgkinson CP, Sale GJ |title=Regulation of both PDK1 and the phosphorylation of PKC-zeta and -delta by a C-terminal PRK2 fragment. |journal=Biochemistry |volume=41 |issue= 2 |pages= 561-9 |year= 2002 |pmid= 11781095 |doi= }}
* {{cite journal | vauthors = Yarrow JC, Totsukawa G, Charras GT, Mitchison TJ | title = Screening for cell migration inhibitors via automated microscopy reveals a Rho-kinase inhibitor | journal = Chem. Biol. | volume = 12 | issue = 3 | pages = 385–395 | year = 2005 | pmid = 15797222 | doi = 10.1016/j.chembiol.2005.01.015 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{cite journal | vauthors = DeGiorgis JA, Jaffe H, Moreira JE, Carlotti CG, Leite JP, Pant HC, Dosemeci A | title = Phosphoproteomic analysis of synaptosomes from human cerebral cortex | journal = J. Proteome Res. | volume = 4 | issue = 2 | pages = 306–315 | year = 2005 | pmid = 15822905 | doi = 10.1021/pr0498436 }}
*{{cite journal | author=McDonald C, Vacratsis PO, Bliska JB, Dixon JE |title=The yersinia virulence factor YopM forms a novel protein complex with two cellular kinases. |journal=J. Biol. Chem. |volume=278 |issue= 20 |pages= 18514-23 |year= 2003 |pmid= 12626518 |doi= 10.1074/jbc.M301226200 }}
* {{cite journal | vauthors = Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S | title = Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes | journal = Genome Res. | volume = 16 | issue = 1 | pages = 55–65 | year = 2006 | pmid = 16344560 | pmc = 1356129 | doi = 10.1101/gr.4039406 }}
*{{cite journal | author=Anderson NL, Polanski M, Pieper R, ''et al.'' |title=The human plasma proteome: a nonredundant list developed by combination of four separate sources. |journal=Mol. Cell Proteomics |volume=3 |issue= 4 |pages= 311-26 |year= 2004 |pmid= 14718574 |doi= 10.1074/mcp.M300127-MCP200 }}
*{{cite journal | author=Beausoleil SA, Jedrychowski M, Schwartz D, ''et al.'' |title=Large-scale characterization of HeLa cell nuclear phosphoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130-5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101 }}
*{{cite journal  | author=Yarrow JC, Totsukawa G, Charras GT, Mitchison TJ |title=Screening for cell migration inhibitors via automated microscopy reveals a Rho-kinase inhibitor. |journal=Chem. Biol. |volume=12 |issue= 3 |pages= 385-95 |year= 2005 |pmid= 15797222 |doi= 10.1016/j.chembiol.2005.01.015 }}
*{{cite journal  | author=DeGiorgis JA, Jaffe H, Moreira JE, ''et al.'' |title=Phosphoproteomic analysis of synaptosomes from human cerebral cortex. |journal=J. Proteome Res. |volume=4 |issue= 2 |pages= 306-15 |year= 2005 |pmid= 15822905 |doi= 10.1021/pr0498436 }}
*{{cite journal  | author=Kimura K, Wakamatsu A, Suzuki Y, ''et al.'' |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55-65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406 }}
*{{cite journal  | author=Gregory SG, Barlow KF, McLay KE, ''et al.'' |title=The DNA sequence and biological annotation of human chromosome 1. |journal=Nature |volume=441 |issue= 7091 |pages= 315-21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
==References==
{{WikiDoc Sources}}
{{Reflist}}
 
{{Serine/threonine-specific protein kinases}}
{{Enzymes}}
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{{gene-1-stub}}

Latest revision as of 18:13, 7 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
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

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Serine/threonine-protein kinase N2 is an enzyme that in humans is encoded by the PKN2 gene.[1][2][3]

Interactions

PKN2 has been shown to interact with:

Further reading

  • Quilliam LA, Lambert QT, Mickelson-Young LA, Westwick JK, Sparks AB, Kay BK, Jenkins NA, Gilbert DJ, Copeland NG, Der CJ (1997). "Isolation of a NCK-associated kinase, PRK2, an SH3-binding protein and potential effector of Rho protein signaling". J. Biol. Chem. 271 (46): 28772–28776. doi:10.1074/jbc.271.46.28772. PMID 8910519.
  • Yu W, Liu J, Morrice NA, Wettenhall RE (1997). "Isolation and characterization of a structural homologue of human PRK2 from rat liver. Distinguishing substrate and lipid activator specificities". J. Biol. Chem. 272 (15): 10030–10034. doi:10.1074/jbc.272.15.10030. PMID 9092545.
  • Vincent S, Settleman J (1997). "The PRK2 kinase is a potential effector target of both Rho and Rac GTPases and regulates actin cytoskeletal organization". Mol. Cell. Biol. 17 (4): 2247–56. PMC 232074. PMID 9121475.
  • Cryns VL, Byun Y, Rana A, Mellor H, Lustig KD, Ghanem L, Parker PJ, Kirschner MW, Yuan J (1997). "Specific proteolysis of the kinase protein kinase C-related kinase 2 by caspase-3 during apoptosis. Identification by a novel, small pool expression cloning strategy". J. Biol. Chem. 272 (47): 29449–29453. doi:10.1074/jbc.272.47.29449. PMID 9368003.
  • Braverman LE, Quilliam LA (1999). "Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing adapter protein having similar binding and biological properties to Nck". J. Biol. Chem. 274 (9): 5542–5549. doi:10.1074/jbc.274.9.5542. PMID 10026169.
  • Flynn P, Mellor H, Casamassima A, Parker PJ (2000). "Rho GTPase control of protein kinase C-related protein kinase activation by 3-phosphoinositide-dependent protein kinase". J. Biol. Chem. 275 (15): 11064–11070. doi:10.1074/jbc.275.15.11064. PMID 10753910.
  • Sun W, Vincent S, Settleman J, Johnson GL (2000). "MEK kinase 2 binds and activates protein kinase C-related kinase 2. Bifurcation of kinase regulatory pathways at the level of an MAPK kinase kinase". J. Biol. Chem. 275 (32): 24421–24428. doi:10.1074/jbc.M003148200. PMID 10818102.
  • Koh H, Lee KH, Kim D, Kim S, Kim JW, Chung J (2000). "Inhibition of Akt and its anti-apoptotic activities by tumor necrosis factor-induced protein kinase C-related kinase 2 (PRK2) cleavage". J. Biol. Chem. 275 (44): 34451–34458. doi:10.1074/jbc.M001753200. PMID 10926925.
  • Gross C, Heumann R, Erdmann KS (2001). "The protein kinase C-related kinase PRK2 interacts with the protein tyrosine phosphatase PTP-BL via a novel PDZ domain binding motif". FEBS Lett. 496 (2–3): 101–104. doi:10.1016/S0014-5793(01)02401-2. PMID 11356191.
  • Hodgkinson CP, Sale GJ (2002). "Regulation of both PDK1 and the phosphorylation of PKC-zeta and -delta by a C-terminal PRK2 fragment". Biochemistry. 41 (2): 561–569. doi:10.1021/bi010719z. PMID 11781095.
  • McDonald C, Vacratsis PO, Bliska JB, Dixon JE (2003). "The yersinia virulence factor YopM forms a novel protein complex with two cellular kinases". J. Biol. Chem. 278 (20): 18514–18523. doi:10.1074/jbc.M301226200. PMID 12626518.
  • Anderson NL, Polanski M, Pieper R, Gatlin T, Tirumalai RS, Conrads TP, Veenstra TD, Adkins JN, Pounds JG, Fagan R, Lobley A (2004). "The human plasma proteome: a nonredundant list developed by combination of four separate sources". Mol. Cell. Proteomics. 3 (4): 311–326. doi:10.1074/mcp.M300127-MCP200. PMID 14718574.
  • Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–12135. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
  • Yarrow JC, Totsukawa G, Charras GT, Mitchison TJ (2005). "Screening for cell migration inhibitors via automated microscopy reveals a Rho-kinase inhibitor". Chem. Biol. 12 (3): 385–395. doi:10.1016/j.chembiol.2005.01.015. PMID 15797222.
  • DeGiorgis JA, Jaffe H, Moreira JE, Carlotti CG, Leite JP, Pant HC, Dosemeci A (2005). "Phosphoproteomic analysis of synaptosomes from human cerebral cortex". J. Proteome Res. 4 (2): 306–315. doi:10.1021/pr0498436. PMID 15822905.
  • Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.

References

  1. ↑ Palmer RH, Ridden J, Parker PJ (January 1995). "Identification of multiple, novel, protein kinase C-related gene products". FEBS Lett. 356 (1): 5–8. doi:10.1016/0014-5793(94)01202-4. PMID 7988719.
  2. ↑ Palmer RH, Ridden J, Parker PJ (March 1995). "Cloning and expression patterns of two members of a novel protein-kinase-C-related kinase family". Eur J Biochem. 227 (1–2): 344–351. doi:10.1111/j.1432-1033.1995.tb20395.x. PMID 7851406.
  3. ↑ "Entrez Gene: PKN2 protein kinase N2".
  4. ↑ Koh H, Lee KH, Kim D, Kim S, Kim JW, Chung J (November 2000). "Inhibition of Akt and its anti-apoptotic activities by tumor necrosis factor-induced protein kinase C-related kinase 2 (PRK2) cleavage". J. Biol. Chem. 275 (44): 34451–8. doi:10.1074/jbc.M001753200. PMID 10926925.
  5. ↑ 5.0 5.1 Quilliam LA, Lambert QT, Mickelson-Young LA, Westwick JK, Sparks AB, Kay BK, Jenkins NA, Gilbert DJ, Copeland NG, Der CJ (November 1996). "Isolation of a NCK-associated kinase, PRK2, an SH3-binding protein and potential effector of Rho protein signaling". J. Biol. Chem. 271 (46): 28772–6. doi:10.1074/jbc.271.46.28772. PMID 8910519.
  6. ↑ Braverman LE, Quilliam LA (February 1999). "Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing adapter protein having similar binding and biological properties to Nck". J. Biol. Chem. 274 (9): 5542–9. doi:10.1074/jbc.274.9.5542. PMID 10026169.
  7. ↑ Gross C, Heumann R, Erdmann KS (May 2001). "The protein kinase C-related kinase PRK2 interacts with the protein tyrosine phosphatase PTP-BL via a novel PDZ domain binding motif". FEBS Lett. 496 (2–3): 101–4. doi:10.1016/s0014-5793(01)02401-2. PMID 11356191.
  8. ↑ Hodgkinson CP, Sale GJ (January 2002). "Regulation of both PDK1 and the phosphorylation of PKC-zeta and -delta by a C-terminal PRK2 fragment". Biochemistry. 41 (2): 561–9. doi:10.1021/bi010719z. PMID 11781095.
  9. ↑ Balendran A, Biondi RM, Cheung PC, Casamayor A, Deak M, Alessi DR (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. 275 (27): 20806–13. doi:10.1074/jbc.M000421200. PMID 10764742.
  10. ↑ Flynn P, Mellor H, Palmer R, Panayotou G, Parker PJ (January 1998). "Multiple interactions of PRK1 with RhoA. Functional assignment of the Hr1 repeat motif". J. Biol. Chem. 273 (5): 2698–705. doi:10.1074/jbc.273.5.2698. PMID 9446575.


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