PKN2

Protein kinase N2

Identifiers

PKN2; MGC150606; MGC71074; PAK2; PRK2; PRKCL2; PRO2042; Pak-2

External IDs

OMIM: 602549 MGI: 109211 HomoloGene: 2054 GeneCards: PKN2 Gene

2.7.11.13

Gene Ontology
Molecular function	• nucleotide binding • protein kinase activity • protein serine/threonine kinase activity • protein kinase C activity • ATP binding • histone deacetylase binding
Cellular component	• intracellular • nucleus • cytoplasm
Biological process	• protein phosphorylation • signal transduction
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
89.15 – 89.3 Mb

Chr 3:
142.45 – 142.54 Mb

PubMed search

[1]

[2]

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 Phosphoinositide-dependent kinase-1,^[4]^[5] AKT1,^[6] NCK1,^[7]^[8] PTPN13^[9] and RHOA.^[7]^[10]

References

^ Palmer RH, Ridden J, Parker PJ (Jan 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.
^ Palmer RH, Ridden J, Parker PJ (Mar 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.
^ "Entrez Gene: PKN2 protein kinase N2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5586.
^ Hodgkinson, Conrad P; Sale Graham J (Jan. 2002). "Regulation of both PDK1 and the phosphorylation of PKC-zeta and -delta by a C-terminal PRK2 fragment". Biochemistry (United States) 41 (2): 561–569. doi:10.1021/bi010719z. ISSN 0006-2960. PMID 11781095.
^ Balendran, A; Biondi R M, Cheung P C, Casamayor A, Deak M, Alessi D R (Jul. 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. (UNITED STATES) 275 (27): 20806–20813. doi:10.1074/jbc.M000421200. ISSN 0021-9258. PMID 10764742.
^ Koh, H; Lee K H, Kim D, Kim S, Kim J W, Chung J (Nov. 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. (UNITED STATES) 275 (44): 34451–34458. doi:10.1074/jbc.M001753200. ISSN 0021-9258. PMID 10926925.
^ ^a ^b Quilliam, L A; Lambert Q T, Mickelson-Young L A, Westwick J K, Sparks A B, Kay B K, Jenkins N A, Gilbert D J, Copeland N G, Der C J (Nov. 1996). "Isolation of a NCK-associated kinase, PRK2, an SH3-binding protein and potential effector of Rho protein signaling". J. Biol. Chem. (UNITED STATES) 271 (46): 28772–28776. doi:10.1074/jbc.271.46.28772. ISSN 0021-9258. PMID 8910519.
^ Braverman, L E; Quilliam L A (Feb. 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. (UNITED STATES) 274 (9): 5542–5549. doi:10.1074/jbc.274.9.5542. ISSN 0021-9258. PMID 10026169.
^ Gross, C; Heumann R, Erdmann K S (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. (Netherlands) 496 (2–3): 101–104. doi:10.1016/S0014-5793(01)02401-2. ISSN 0014-5793. PMID 11356191.
^ Flynn, P; Mellor H, Palmer R, Panayotou G, Parker P J (Jan. 1998). "Multiple interactions of PRK1 with RhoA. Functional assignment of the Hr1 repeat motif". J. Biol. Chem. (UNITED STATES) 273 (5): 2698–2705. doi:10.1074/jbc.273.5.2698. ISSN 0021-9258. PMID 9446575.

Quilliam LA, Lambert QT, Mickelson-Young LA et al. (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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=232074.
Cryns VL, Byun Y, Rana A et al. (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 et al. (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.
Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–16903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
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 et al. (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 et al. (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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=514446.
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 et al. (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 et al. (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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1356129.
Gregory SG, Barlow KF, McLay KE et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature 441 (7091): 315–321. doi:10.1038/nature04727. PMID 16710414.

Kinases: Serine/threonine-specific protein kinases (EC 2.7.11-12)

Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20)

Non-specific serine/threonine protein kinases (EC 2.7.11.1)	LATS1, LATS2, MAST1, MAST2, STK38, STK38L, CIT, ROCK1, SGK, SGK2, SGK3, Protein kinase B (AKT1, AKT2, AKT3), Ataxia telangiectasia mutated, Mammalian target of rapamycin, EIF-2 kinases (PKR, HRI, EIF2AK3, EIF2AK4), Wee1 (WEE1)

Pyruvate dehydrogenase kinase (EC 2.7.11.2)	PDK1, PDK2, PDK3

Dephospho-(reductase kinase) kinase (EC 2.7.11.3)	AMP-activated protein kinase α (PRKAA1, PRKAA2) · β (PRKAB1, PRKAB2) · γ (PRKAG1, PRKAG2, PRKAG3)

(3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)) (EC 2.7.11.4)	BCKDK, BCKDHA, BCKDHB

(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)	IDH2, IDH3A, IDH3B, IDH3G

(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)	STK4

Myosin-heavy-chain kinase (EC 2.7.11.7)	Aurora kinase (Aurora A kinase, Aurora B kinase)

Fas-activated serine/threonine kinase (EC 2.7.11.8)	FASTK, STK10

Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)	-

IκB kinase (EC 2.7.11.10)	CHUK, IKK2, TBK1, IKBKE, IKBKG, IKBKAP

cAMP-dependent protein kinase (EC 2.7.11.11)	Protein kinase A, PRKACG, PRKACB, PRKACA, PRKY

cGMP-dependent protein kinase (EC 2.7.11.12)	Protein kinase G, PRKG1

Protein kinase C (EC 2.7.11.13)	Protein kinase C, Protein kinase Cζ, PKC alpha, PRKCB1, PRKCD, PRKCE, PRKCH, PRKCG, PRKCI, PRKCQ, Protein kinase N1, PKN2, PKN3,

Rhodopsin kinase (EC 2.7.11.14)	Rhodopsin kinase

Beta adrenergic receptor kinase (EC 2.7.11.15)	Beta adrenergic receptor kinase, Beta adrenergic receptor kinase-2

G-protein coupled receptor kinases (EC 2.7.11.16)	GRK4, GRK5, GRK6

Ca2+/calmodulin-dependent (EC 2.7.11.17)	BRSK2, CAMK1, CAMK2A, CAMK2B, CAMK2D, CAMK2G, CAMK4, MLCK, CASK, CHEK1, CHEK2, DAPK1, DAPK2, DAPK3, STK11, MAPKAPK2, MAPKAPK3, MAPKAPK5, MARK1, MARK2, MARK3, MARK4, MELK, MKNK1, MKNK2, NUAK1, NUAK2, OBSCN, PASK, PHKG1, PHKG2, PIM1, PIM2, PKD1, PRKD2, PRKD3, PSKH1, SNF1LK2, KIAA0999, STK40, SNF1LK, SNRK, SPEG, TSSK2, Kalirin, TRIB1, TRIB2, TRIB3, TRIO, Titin, DCLK1

Myosin light-chain kinase (EC 2.7.11.18)	MYLK, MYLK2, MYLK3, MYLK4

Phosphorylase kinase (EC 2.7.11.19)	PHKA1, PHKA2, PHKB, PHKG1, PHKG2

Elongation factor 2 kinase (EC 2.7.11.20)	EEF2K, STK19

Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)

Polo kinase (EC 2.7.11.21)	PLK1, PLK2, PLK3, PLK4

Cyclin-dependent kinase (EC 2.7.11.22)	CDK1, CDK2, CDKL2, CDK3, CDK4, CDK5, CDKL5, CDK6, CDK7, CDK8, CDK9, CDK10, CDC2L5, CRKRS, PCTK1, PCTK2, PCTK3, PFTK1, CDC2L1

(RNA-polymerase)-subunit kinase (EC 2.7.11.23)	RPS6KA5, RPS6KA4, P70S6 kinase, P70-S6 Kinase 1, RPS6KB2, RPS6KA2, RPS6KA3, RPS6KA1, RPS6KC1

Mitogen-activated protein kinase (EC 2.7.11.24)	Extracellular signal-regulated (MAPK1, MAPK3, MAPK4, MAPK6, MAPK7, MAPK12, MAPK15), C-Jun N-terminal (MAPK8, MAPK9, MAPK10), P38 mitogen-activated protein (MAPK11, MAPK13, MAPK14)

MAP3K (EC 2.7.11.25)	MAP kinase kinase kinases (MAP3K1, MAP3K2, MAP3K3, MAP3K4, MAP3K5, MAP3K6, MAP3K7, MAP3K8) RAFs (ARAF, BRAF, KSR1, KSR2), MLKs (MAP3K12, MAP3K13, MAP3K9, MAP3K10, MAP3K11, MAP3K7, ZAK), CDC7, MAP3K14

Tau-protein kinase (EC 2.7.11.26)	TPK1, TTK, GSK-3

(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)	-

Tropomyosin kinase (EC 2.7.11.28)	-

Low-density-lipoprotein receptor kinase (EC 2.7.11.29)	-

Receptor protein serine/threonine kinase (EC 2.7.11.30)	Bone morphogenetic protein receptors (BMPR1, BMPR1A, BMPR1B, BMPR2), ACVR1, ACVR1B, ACVR1C, ACVR2A, ACVR2B, ACVRL1, Anti-Müllerian hormone receptor

Dual-specificity kinases (EC 2.7.12)

MAP2K	MAP2K1, MAP2K2, MAP2K3, MAP2K4, MAP2K5, MAP2K6, MAP2K7

B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6

PKN2

Interactions

References

Further reading