PKN2

Serine/threonine-protein kinase N2 is an enzyme that in humans and Strongylocentrotus purpuratus is encoded by the PKN2 gene.^[5][6][7]

PKN2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4CRS, 4RRV
Identifiers
Aliases	PKN2, PAK2, PRK2, PRKCL2, PRO2042, Pak-2, STK7, protein kinase N2
External IDs	OMIM: 602549; MGI: 109211; HomoloGene: 2054; GeneCards: PKN2; OMA:PKN2 - orthologs
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1p22.2 Start 88,684,222 bp[1] End 88,836,255 bp[1]
Gene location (Mouse) Chr. Chromosome 3 (mouse)[2] Band 3 H1|3 66.69 cM Start 142,496,663 bp[2] End 142,587,765 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in nipple secondary oocyte parotid gland pylorus jejunal mucosa Achilles tendon visceral pleura amniotic fluid cardia trabecular bone Top expressed in superior cervical ganglion medullary collecting duct spermatid tail of embryo spermatocyte genital tubercle renal corpuscle secondary oocyte zygote urothelium More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity protein kinase activity nucleotide binding protein kinase C activity histone deacetylase binding kinase activity protein serine/threonine kinase activity protein binding RNA polymerase binding ATP binding RNA binding cadherin binding Cellular component cytoplasm cytosol cell projection membrane midbody perinuclear region of cytoplasm cleavage furrow cytoskeleton apical junction complex nucleus lamellipodium cell junction nucleoplasm centrosome plasma membrane nuclear body protein-containing complex intermediate filament cytoskeleton Biological process intracellular signal transduction regulation of transcription, DNA-templated phosphorylation positive regulation of mitotic cell cycle transcription, DNA-templated positive regulation of cytokinesis cell division regulation of cell motility protein phosphorylation cell adhesion peptidyl-serine phosphorylation epithelial cell migration cell cycle positive regulation of viral genome replication apical junction assembly signal transduction apoptotic process cell projection organization viral process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5586 109333 Ensembl ENSG00000065243 ENSMUSG00000004591 UniProt Q16513 Q8BWW9 RefSeq (mRNA) NM_006256 NM_001320707 NM_001320708 NM_001320709 NM_178654 RefSeq (protein) NP_001307636 NP_001307637 NP_001307638 NP_006247 NP_848769 Location (UCSC) Chr 1: 88.68 – 88.84 Mb Chr 3: 142.5 – 142.59 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Interactions

PKN2 has been shown to interact with:

• AKT1,^[8]
• NCK1,^[9][10]
• PTPN13,^[11]
• Phosphoinositide-dependent kinase-1,^[12][13] and
• RHOA.^[9][14]

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. doi:10.1128/MCB.17.4.2247. 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. Bibcode:2004PNAS..10112130B. 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.