MAP3K2

From Wikipedia, the free encyclopedia

Mitogen-activated protein kinase kinase kinase 2

PDB rendering based on 2cu1.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
2CU1, 2NPT

Identifiers

Symbols

MAP3K2; MEKK2; MEKK2B

External IDs

OMIM: 609487 MGI: 1346873 HomoloGene: 74576 ChEMBL: 5914 GeneCards: MAP3K2 Gene

EC number

2.7.11.25

Gene Ontology
Molecular function	• protein kinase activity • protein serine/threonine kinase activity • MAP kinase kinase kinase activity • ATP binding • protein kinase binding • metal ion binding
Cellular component	• nucleus • cytoplasm
Biological process	• activation of MAPK activity • protein phosphorylation • activation of JUN kinase activity • positive regulation of transcription, DNA-dependent • cellular response to mechanical stimulus
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 2:
128.06 – 128.15 Mb

Chr 18:
32.16 – 32.24 Mb

PubMed search

Mitogen-activated protein kinase kinase kinase 2 is an enzyme that in humans is encoded by the MAP3K2 gene.^[1]^[2]^[3]

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 IkappaB 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.^[3]

Interactions

MAP3K2 has been shown to interact with SH2D2A,^[4] MAP2K7,^[5] MAP2K5,^[4] XIAP^[6] and MAPK8.^[5]

References

↑ Blank JL, Gerwins P, Elliott EM, Sather S, Johnson GL (June 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. doi:10.1074/jbc.271.10.5361. PMID 8621389.
↑ Zhao Q, Lee FS (April 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. doi:10.1074/jbc.274.13.8355. PMID 10085062.
↑ 3.0 3.1 "Entrez Gene: MAP3K2 mitogen-activated protein kinase kinase kinase 2".
↑ 4.0 4.1 Sun, W; Kesavan K, Schaefer B C, Garrington T P, Ware M, Johnson N L, Gelfand E W, Johnson G L (February 2001). "MEKK2 associates with the adapter protein Lad/RIBP and regulates the MEK5-BMK1/ERK5 pathway". J. Biol. Chem. (United States) 276 (7): 5093–100. doi:10.1074/jbc.M003719200. ISSN 0021-9258. PMID 11073940. Cite uses deprecated parameters (help)
↑ 5.0 5.1 Cheng, J; Yang J, Xia Y, Karin M, Su B (April 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. (UNITED STATES) 20 (7): 2334–42. doi:10.1128/MCB.20.7.2334-2342.2000. ISSN 0270-7306. PMC 85399. PMID 10713157. Cite uses deprecated parameters (help)
↑ Winsauer, Gabriele; Resch Ulrike, Hofer-Warbinek Renate, Schichl Yvonne M, de Martin Rainer (November 2008). "XIAP regulates bi-phasic NF-kappaB induction involving physical interaction and ubiquitination of MEKK2". Cell. Signal. (England) 20 (11): 2107–12. doi:10.1016/j.cellsig.2008.08.004. ISSN 0898-6568. PMID 18761086. Cite uses deprecated parameters (help)

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. doi:10.1038/372798a0. PMID 7997270.
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. PMC 232596. 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. doi:10.1074/jbc.273.6.3476. PMID 9452471.
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. doi:10.1128/MCB.20.7.2334-2342.2000. PMC 85399. 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. PMC 314024. 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. PMC 139241. 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. doi:10.1016/S0006-291X(03)00387-5. 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. PMC 1168836. 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.

PDB gallery

2cu1: Solution structure of the PB1 domain of human protein kinase MEKK2b

2npt: Crystal Structure of the complex of human mitogen activated protein kinase kinase 5 phox domain (MAP2K5-phox) with human mitogen activated protein kinase kinase kinase 2 phox domain (MAP3K2-phox)

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MAP3K2

Interactions

References

Further reading