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Mitogen-activated protein kinase-activated protein kinase 3
External IDs OMIM602130 MGI2143163 HomoloGene55836 GeneCards: MAPKAPK3 Gene
RNA expression pattern
PBB GE MAPKAPK3 202787 s at tn.png
PBB GE MAPKAPK3 202788 at tn.png
More reference expression data
Species Human Mouse
Entrez 7867 102626
Ensembl ENSG00000114738 ENSMUSG00000032577
UniProt Q16644 Q3UMW7
RefSeq (mRNA) NM_004635 NM_178907
RefSeq (protein) NP_004626 NP_849238
Location (UCSC) Chr 3:
50.62 - 50.66 Mb
Chr 9:
107.11 - 107.15 Mb
PubMed search [1] [2]

MAP kinase-activated protein kinase 3 is an enzyme that in humans is encoded by the MAPKAPK3 gene.[1][2][3]

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.[3]


MAPKAPK3 has been shown to interact with MAPK14[4] and TCF3.[5]


  1. ^ McLaughlin MM, Kumar S, McDonnell PC, Van Horn S, Lee JC, Livi GP, Young PR (Jun 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.  
  2. ^ Sithanandam G, Latif F, Duh FM, Bernal R, Smola U, Li H, Kuzmin I, Wixler V, Geil L, Shrestha S (Jun 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.  
  3. ^ a b "Entrez Gene: MAPKAPK3 mitogen-activated protein kinase-activated protein kinase 3".  
  4. ^ Tanoue, T; Maeda R, Adachi M, Nishida E (Feb. 2001). "Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions". EMBO J. (England) 20 (3): 466–79. doi:10.1093/emboj/20.3.466. ISSN 0261-4189. PMID 11157753.  
  5. ^ Neufeld, B; Grosse-Wilde A, Hoffmeyer A, Jordan B W, Chen P, Dinev D, Ludwig S, Rapp U R (Jul. 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. (UNITED STATES) 275 (27): 20239–42. doi:10.1074/jbc.C901040199. ISSN 0021-9258. PMID 10781029.  

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.  
  • 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. doi:10.1016/0014-5793(96)00816-2. 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. doi:10.1097/00132580-200203000-00002. 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.  


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