MAPKAPK3

From Wikipedia, the free encyclopedia

Mitogen-activated protein kinase-activated protein kinase 3

Identifiers

MAPKAPK3; 3PK; MAPKAP3

External IDs

OMIM: 602130 MGI: 2143163 HomoloGene: 55836

Gene ontology
Molecular Function:	• nucleotide binding • protein serine/threonine kinase activity • MAP kinase kinase activity • ATP binding • transferase activity
Cellular Component:	• nucleus
Biological Process:	• protein amino acid phosphorylation • response to stress • signal transduction

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_004635 (mRNA)
NP_004626 (protein)

NM_178907 (mRNA)
NP_849238 (protein)

Location

Chr 3: 50.62 - 50.66 Mb

Chr 9: 107.11 - 107.15 Mb

Pubmed search

[1]

[2]

Mitogen-activated protein kinase-activated protein kinase 3, also known as MAPKAPK3, is a human gene.^[1]

This gene encodes a member of the Ser/Thr protein kinase family. This kinase functions as a mitogen-activated protein kinase (MAP kinase)- activated protein kinase. MAP kinases are also known as extracellular signal-regulated kinases (ERKs), act as an integration point for multiple biochemical signals. This kinase was shown to be activated by growth inducers and stress stimulation of cells. In vitro studies demonstrated that ERK, p38 MAP kinase and Jun N-terminal kinase were all able to phosphorylate and activate this kinase, which suggested the role of this kinase as an integrative element of signaling in both mitogen and stress responses. This kinase was reported to interact with, phosphorylate and repress the activity of E47, which is a basic helix-loop-helix transcription factor known to be involved in the regulation of tissue-specific gene expression and cell differentiation.^[1]

[edit] References

^ ^a ^b Entrez Gene: MAPKAPK3 mitogen-activated protein kinase-activated protein kinase 3.

[edit] Further reading

Wei MH, Latif F, Bader S, et al. (1996). "Construction of a 600-kilobase cosmid clone contig and generation of a transcriptional map surrounding the lung cancer tumor suppressor gene (TSG) locus on human chromosome 3p21.3: progress toward the isolation of a lung cancer TSG.". Cancer Res. 56 (7): 1487-92. PMID 8603390.
Sithanandam G, Latif F, Duh FM, et al. (1996). "3pK, a new mitogen-activated protein kinase-activated protein kinase located in the small cell lung cancer tumor suppressor gene region.". Mol. Cell. Biol. 16 (3): 868-76. PMID 8622688.
McLaughlin MM, Kumar S, McDonnell PC, et al. (1996). "Identification of mitogen-activated protein (MAP) kinase-activated protein kinase-3, a novel substrate of CSBP p38 MAP kinase.". J. Biol. Chem. 271 (14): 8488-92. PMID 8626550.
Clifton AD, Young PR, Cohen P (1996). "A comparison of the substrate specificity of MAPKAP kinase-2 and MAPKAP kinase-3 and their activation by cytokines and cellular stress.". FEBS Lett. 392 (3): 209-14. PMID 8774846.
Ludwig S, Engel K, Hoffmeyer A, et al. (1997). "3pK, a novel mitogen-activated protein (MAP) kinase-activated protein kinase, is targeted by three MAP kinase pathways.". Mol. Cell. Biol. 16 (12): 6687-97. PMID 8943323.
Kumar S, McDonnell PC, Gum RJ, et al. (1997). "Novel homologues of CSBP/p38 MAP kinase: activation, substrate specificity and sensitivity to inhibition by pyridinyl imidazoles.". Biochem. Biophys. Res. Commun. 235 (3): 533-8. doi:10.1006/bbrc.1997.6849. PMID 9207191.
Neufeld B, Grosse-Wilde A, Hoffmeyer A, et al. (2000). "Serine/Threonine kinases 3pK and MAPK-activated protein kinase 2 interact with the basic helix-loop-helix transcription factor E47 and repress its transcriptional activity.". J. Biol. Chem. 275 (27): 20239-42. doi:10.1074/jbc.C901040199. PMID 10781029.
Tanoue T, Maeda R, Adachi M, Nishida E (2001). "Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions.". EMBO J. 20 (3): 466-79. doi:10.1093/emboj/20.3.466. PMID 11157753.
Simkhovich BZ, Abdishoo S, Poizat C, et al. (2002). "Gene activity changes in ischemically preconditioned rabbit heart gene: discovery array study.". Heart disease (Hagerstown, Md.) 4 (2): 63-9. PMID 11975836.
Knebel A, Haydon CE, Morrice N, Cohen P (2002). "Stress-induced regulation of eukaryotic elongation factor 2 kinase by SB 203580-sensitive and -insensitive pathways.". Biochem. J. 367 (Pt 2): 525-32. doi:10.1042/BJ20020916. PMID 12171600.
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.
Zakowski V, Keramas G, Kilian K, et al. (2004). "Mitogen-activated 3p kinase is active in the nucleus.". Exp. Cell Res. 299 (1): 101-9. doi:10.1016/j.yexcr.2004.05.027. PMID 15302577.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi:10.1101/gr.2596504. PMID 15489334.
Voncken JW, Niessen H, Neufeld B, et al. (2005). "MAPKAP kinase 3pK phosphorylates and regulates chromatin association of the polycomb group protein Bmi1.". J. Biol. Chem. 280 (7): 5178-87. doi:10.1074/jbc.M407155200. PMID 15563468.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173-8. doi:10.1038/nature04209. PMID 16189514.