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PKN2

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(Redirected from Pkn2)
Protein-coding gene in the species Homo sapiens
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 IDsOMIM: 602549; MGI: 109211; HomoloGene: 2054; GeneCards: PKN2; OMA:PKN2 - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr. Chromosome 1 (human) [1]
Band 1p22.2Start88,684,222 bp [1]
End88,836,255 bp [1]
Gene location (Mouse)
Chromosome 3 (mouse)
Chr. Chromosome 3 (mouse)[2]
Band 3 H1|3 66.69 cMStart142,496,663 bp [2]
End142,587,765 bp [2]
RNA expression pattern
Bgee
Human Mouse (ortholog)
  • nipple

  • secondary oocyte

  • parotid gland

  • pylorus

  • jejunal mucosa

  • Achilles tendon

  • visceral pleura

  • amniotic fluid

  • cardia

  • trabecular bone
  • superior cervical ganglion

  • medullary collecting duct

  • spermatid

  • tail of embryo

  • spermatocyte

  • genital tubercle

  • renal corpuscle

  • secondary oocyte

  • zygote

  • urothelium
More reference expression data
BioGPS




Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
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 Mb Chr 3: 142.5 – 142.59 Mb
PubMed search[3] [4]
Wikidata

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

Interactions

[edit ]

PKN2 has been shown to interact with:

Further reading

[edit ]

References

[edit ]
  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000065243Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000004591Ensembl, 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. ^ a b 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.
Non-specific serine/threonine protein kinases (EC 2.7.11.1)
Pyruvate dehydrogenase kinase (EC 2.7.11.2)
Dephospho-(reductase kinase) kinase (EC 2.7.11.3)
3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)
(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)
(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)
Myosin-heavy-chain kinase (EC 2.7.11.7)
Fas-activated serine/threonine kinase (EC 2.7.11.8)
Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)
  • -
IκB kinase (EC 2.7.11.10)
cAMP-dependent protein kinase (EC 2.7.11.11)
cGMP-dependent protein kinase (EC 2.7.11.12)
Protein kinase C (EC 2.7.11.13)
Rhodopsin kinase (EC 2.7.11.14)
Beta adrenergic receptor kinase (EC 2.7.11.15)
G-protein coupled receptor kinases (EC 2.7.11.16)
Ca2+/calmodulin-dependent (EC 2.7.11.17)
Myosin light-chain kinase (EC 2.7.11.18)
Phosphorylase kinase (EC 2.7.11.19)
Elongation factor 2 kinase (EC 2.7.11.20)
Polo kinase (EC 2.7.11.21)
Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)
Polo kinase (EC 2.7.11.21)
Cyclin-dependent kinase (EC 2.7.11.22)
(RNA-polymerase)-subunit kinase (EC 2.7.11.23)
Mitogen-activated protein kinase (EC 2.7.11.24)
MAP3K (EC 2.7.11.25)
Tau-protein kinase (EC 2.7.11.26)
(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)
MAP2K


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