MAP3K2

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Mitogen-activated protein kinase kinase kinase 2
File:PBB Protein MAP3K2 image.jpg
PDB rendering based on 2cu1.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols MAP3K2 ; MEKK2; MEKK2B
External IDs Template:OMIM5 Template:MGI HomoloGene74576
RNA expression pattern
File:PBB GE MAP3K2 221695 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
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 n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Mitogen-activated protein kinase kinase kinase 2, also known as MAP3K2, is a human gene.[1]

The protein encoded by this gene is a member of serine/threonine protein kinase family. This kinase preferentially activates other kinases involved in the MAP kinase signaling pathway. This kinase has been shown to directly phosphorylate and activate Ikappa B kinases, and thus plays a role in NF-kappa B signaling pathway. This kinase has also been found to bind and activate protein kinase C-related kinase 2, which suggests its involvement in a regulated signaling process.[1]

References

  1. 1.0 1.1 "Entrez Gene: MAP3K2 mitogen-activated protein kinase kinase kinase 2".

Further reading

  • Yan M, Dai T, Deak JC; et al. (1995). "Activation of stress-activated protein kinase by MEKK1 phosphorylation of its activator SEK1". Nature. 372 (6508): 798–800. PMID 7997270.
  • Blank JL, Gerwins P, Elliott EM; et al. (1996). "Molecular cloning of mitogen-activated protein/ERK kinase kinases (MEKK) 2 and 3. Regulation of sequential phosphorylation pathways involving mitogen-activated protein kinase and c-Jun kinase". J. Biol. Chem. 271 (10): 5361–8. PMID 8621389.
  • Wu Z, Wu J, Jacinto E, Karin M (1997). "Molecular cloning and characterization of human JNKK2, a novel Jun NH2-terminal kinase-specific kinase". Mol. Cell. Biol. 17 (12): 7407–16. PMID 9372971.
  • Fanger GR, Widmann C, Porter AC; et al. (1998). "14-3-3 proteins interact with specific MEK kinases". J. Biol. Chem. 273 (6): 3476–83. PMID 9452471.
  • Zhao Q, Lee FS (1999). "Mitogen-activated protein kinase/ERK kinase kinases 2 and 3 activate nuclear factor-kappaB through IkappaB kinase-alpha and IkappaB kinase-beta". J. Biol. Chem. 274 (13): 8355–8. PMID 10085062.
  • Cheng J, Yang J, Xia Y; et al. (2000). "Synergistic interaction of MEK kinase 2, c-Jun N-terminal kinase (JNK) kinase 2, and JNK1 results in efficient and specific JNK1 activation". Mol. Cell. Biol. 20 (7): 2334–42. PMID 10713157.
  • 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): 24421–8. doi:10.1074/jbc.M003148200. PMID 10818102.
  • Garrington TP, Ishizuka T, Papst PJ; et al. (2000). "MEKK2 gene disruption causes loss of cytokine production in response to IgE and c-Kit ligand stimulation of ES cell-derived mast cells". EMBO J. 19 (20): 5387–95. doi:10.1093/emboj/19.20.5387. PMID 11032806.
  • 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): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Huang J, Tu Z, Lee FS (2003). "Mutations in protein kinase subdomain X differentially affect MEKK2 and MEKK1 activity". Biochem. Biophys. Res. Commun. 303 (2): 532–40. PMID 12659851.
  • Nakamura K, Johnson GL (2003). "PB1 domains of MEKK2 and MEKK3 interact with the MEK5 PB1 domain for activation of the ERK5 pathway". J. Biol. Chem. 278 (39): 36989–92. doi:10.1074/jbc.C300313200. PMID 12912994.
  • Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Hammaker DR, Boyle DL, Chabaud-Riou M, Firestein GS (2004). "Regulation of c-Jun N-terminal kinase by MEKK-2 and mitogen-activated protein kinase kinase kinases in rheumatoid arthritis". J. Immunol. 172 (3): 1612–8. PMID 14734742.
  • Raviv Z, Kalie E, Seger R (2004). "MEK5 and ERK5 are localized in the nuclei of resting as well as stimulated cells, while MEKK2 translocates from the cytosol to the nucleus upon stimulation". J. Cell. Sci. 117 (Pt 9): 1773–84. doi:10.1242/jcs.01040. PMID 15075238.
  • Jin J, Smith FD, Stark C; et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.
  • Benzinger A, Muster N, Koch HB; et al. (2005). "Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer". Mol. Cell Proteomics. 4 (6): 785–95. doi:10.1074/mcp.M500021-MCP200. PMID 15778465.
  • Hillier LW, Graves TA, Fulton RS; et al. (2005). "Generation and annotation of the DNA sequences of human chromosomes 2 and 4". Nature. 434 (7034): 724–31. doi:10.1038/nature03466. PMID 15815621.
  • Cheng J, Zhang D, Kim K; et al. (2005). "Mip1, an MEKK2-interacting protein, controls MEKK2 dimerization and activation". Mol. Cell. Biol. 25 (14): 5955–64. doi:10.1128/MCB.25.14.5955-5964.2005. PMID 15988011.
  • Pelkmans L, Zerial M (2005). "Kinase-regulated quantal assemblies and kiss-and-run recycling of caveolae". Nature. 436 (7047): 128–33. doi:10.1038/nature03866. PMID 16001074.
  • Wissing J, Jänsch L, Nimtz M; et al. (2007). "Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry". Mol. Cell Proteomics. 6 (3): 537–47. doi:10.1074/mcp.T600062-MCP200. PMID 17192257.

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