PKN2

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

PKN2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesPKN2, PAK2, PRK2, PRKCL2, PRO2042, Pak-2, STK7, protein kinase N2
External IDsOMIM: 602549 MGI: 109211 HomoloGene: 2054 GeneCards: PKN2
Gene location (Human)
Chr.Chromosome 1 (human)[1]
Band1p22.2Start88,684,222 bp[1]
End88,836,255 bp[1]
RNA expression pattern




More reference expression data
Orthologs
SpeciesHumanMouse
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 MbChr 3: 142.79 – 142.88 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Interactions

PKN2 has been shown to interact with:

Further reading

References

  1. GRCh38: Ensembl release 89: ENSG00000065243 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000004591 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. 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.
  6. 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.
  7. "Entrez Gene: PKN2 protein kinase N2".
  8. 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.
  9. 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.
  10. 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.
  11. 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.
  12. 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.
  13. 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.
  14. 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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