MAP3K2

MAP3K2

Mitogen-activated protein kinase kinase kinase 2, also known as MAP3K2, is a human gene.cite web | title = Entrez Gene: MAP3K2 mitogen-activated protein kinase kinase kinase 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10746| accessdate = ]

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: MAP3K2 mitogen-activated protein kinase kinase kinase 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10746| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Yan M, Dai T, Deak JC, "et al." |title=Activation of stress-activated protein kinase by MEKK1 phosphorylation of its activator SEK1. |journal=Nature |volume=372 |issue= 6508 |pages= 798–800 |year= 1995 |pmid= 7997270 |doi=
*cite journal | author=Blank JL, Gerwins P, Elliott EM, "et al." |title=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. |journal=J. Biol. Chem. |volume=271 |issue= 10 |pages= 5361–8 |year= 1996 |pmid= 8621389 |doi=
*cite journal | author=Wu Z, Wu J, Jacinto E, Karin M |title=Molecular cloning and characterization of human JNKK2, a novel Jun NH2-terminal kinase-specific kinase. |journal=Mol. Cell. Biol. |volume=17 |issue= 12 |pages= 7407–16 |year= 1997 |pmid= 9372971 |doi=
*cite journal | author=Fanger GR, Widmann C, Porter AC, "et al." |title=14-3-3 proteins interact with specific MEK kinases. |journal=J. Biol. Chem. |volume=273 |issue= 6 |pages= 3476–83 |year= 1998 |pmid= 9452471 |doi=
*cite journal | author=Zhao Q, Lee FS |title=Mitogen-activated protein kinase/ERK kinase kinases 2 and 3 activate nuclear factor-kappaB through IkappaB kinase-alpha and IkappaB kinase-beta. |journal=J. Biol. Chem. |volume=274 |issue= 13 |pages= 8355–8 |year= 1999 |pmid= 10085062 |doi=
*cite journal | author=Cheng J, Yang J, Xia Y, "et al." |title=Synergistic interaction of MEK kinase 2, c-Jun N-terminal kinase (JNK) kinase 2, and JNK1 results in efficient and specific JNK1 activation. |journal=Mol. Cell. Biol. |volume=20 |issue= 7 |pages= 2334–42 |year= 2000 |pmid= 10713157 |doi=
*cite journal | author=Sun W, Vincent S, Settleman J, Johnson GL |title=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. |journal=J. Biol. Chem. |volume=275 |issue= 32 |pages= 24421–8 |year= 2000 |pmid= 10818102 |doi= 10.1074/jbc.M003148200
*cite journal | author=Garrington TP, Ishizuka T, Papst PJ, "et al." |title=MEKK2 gene disruption causes loss of cytokine production in response to IgE and c-Kit ligand stimulation of ES cell-derived mast cells. |journal=EMBO J. |volume=19 |issue= 20 |pages= 5387–95 |year= 2000 |pmid= 11032806 |doi= 10.1093/emboj/19.20.5387
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Huang J, Tu Z, Lee FS |title=Mutations in protein kinase subdomain X differentially affect MEKK2 and MEKK1 activity. |journal=Biochem. Biophys. Res. Commun. |volume=303 |issue= 2 |pages= 532–40 |year= 2003 |pmid= 12659851 |doi=
*cite journal | author=Nakamura K, Johnson GL |title=PB1 domains of MEKK2 and MEKK3 interact with the MEK5 PB1 domain for activation of the ERK5 pathway. |journal=J. Biol. Chem. |volume=278 |issue= 39 |pages= 36989–92 |year= 2003 |pmid= 12912994 |doi= 10.1074/jbc.C300313200
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Hammaker DR, Boyle DL, Chabaud-Riou M, Firestein GS |title=Regulation of c-Jun N-terminal kinase by MEKK-2 and mitogen-activated protein kinase kinase kinases in rheumatoid arthritis. |journal=J. Immunol. |volume=172 |issue= 3 |pages= 1612–8 |year= 2004 |pmid= 14734742 |doi=
*cite journal | author=Raviv Z, Kalie E, Seger R |title=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. |journal=J. Cell. Sci. |volume=117 |issue= Pt 9 |pages= 1773–84 |year= 2004 |pmid= 15075238 |doi= 10.1242/jcs.01040
*cite journal | author=Jin J, Smith FD, Stark C, "et al." |title=Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization. |journal=Curr. Biol. |volume=14 |issue= 16 |pages= 1436–50 |year= 2004 |pmid= 15324660 |doi= 10.1016/j.cub.2004.07.051
*cite journal | author=Benzinger A, Muster N, Koch HB, "et al." |title=Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer. |journal=Mol. Cell Proteomics |volume=4 |issue= 6 |pages= 785–95 |year= 2005 |pmid= 15778465 |doi= 10.1074/mcp.M500021-MCP200
*cite journal | author=Hillier LW, Graves TA, Fulton RS, "et al." |title=Generation and annotation of the DNA sequences of human chromosomes 2 and 4. |journal=Nature |volume=434 |issue= 7034 |pages= 724–31 |year= 2005 |pmid= 15815621 |doi= 10.1038/nature03466
*cite journal | author=Cheng J, Zhang D, Kim K, "et al." |title=Mip1, an MEKK2-interacting protein, controls MEKK2 dimerization and activation. |journal=Mol. Cell. Biol. |volume=25 |issue= 14 |pages= 5955–64 |year= 2005 |pmid= 15988011 |doi= 10.1128/MCB.25.14.5955-5964.2005
*cite journal | author=Pelkmans L, Zerial M |title=Kinase-regulated quantal assemblies and kiss-and-run recycling of caveolae. |journal=Nature |volume=436 |issue= 7047 |pages= 128–33 |year= 2005 |pmid= 16001074 |doi= 10.1038/nature03866
*cite journal | author=Wissing J, Jänsch L, Nimtz M, "et al." |title=Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry. |journal=Mol. Cell Proteomics |volume=6 |issue= 3 |pages= 537–47 |year= 2007 |pmid= 17192257 |doi= 10.1074/mcp.T600062-MCP200

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