MAPKAPK3

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

MAPKAPK3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3FHR, 3FXW, 3R1N, 3SHE
Identifiers
Aliases	MAPKAPK3, 3PK, MAPKAP-K3, MAPKAP3, MAPKAPK-3, MK-3, mitogen-activated protein kinase-activated protein kinase 3, MDPT3, MAPK activated protein kinase 3, MK3
External IDs	OMIM: 602130; MGI: 2143163; HomoloGene: 55836; GeneCards: MAPKAPK3; OMA:MAPKAPK3 - orthologs
Gene location (Human) Chr. Chromosome 3 (human) Band 3p21.2 Start 50,611,520 bp End 50,649,291 bp
Gene location (Mouse) Chr. Chromosome 9 (mouse) Band 9|9 F1 Start 107,132,126 bp End 107,167,076 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in apex of heart left ventricle body of tongue gastrocnemius muscle myocardium of left ventricle monocyte right auricle right ventricle granulocyte tibialis anterior muscle Top expressed in hair follicle granulocyte conjunctival fornix lip skin of external ear Paneth cell semi-lunar valve temporal muscle esophagus aortic valve More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity nucleotide binding protein kinase activity calcium-dependent protein serine/threonine kinase activity calmodulin binding kinase activity protein binding calmodulin-dependent protein kinase activity ATP binding MAP kinase kinase activity protein serine/threonine kinase activity mitogen-activated protein kinase binding Cellular component cytoplasm cytosol nucleoplasm nucleus Biological process response to cytokine phosphorylation protein phosphorylation cell surface receptor signaling pathway response to lipopolysaccharide vascular endothelial growth factor receptor signaling pathway macropinocytosis peptidyl-serine phosphorylation protein autophosphorylation signal transduction toll-like receptor signaling pathway MAPK cascade intracellular signal transduction Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 7867 102626 Ensembl ENSG00000114738 ENSMUSG00000032577 UniProt Q16644 Q3UMW7 RefSeq (mRNA) NM_001243925 NM_001243926 NM_004635 NM_178907 NM_001316691 RefSeq (protein) NP_001230854 NP_001230855 NP_004626 NP_001303620 NP_849238 Location (UCSC) Chr 3: 50.61 – 50.65 Mb Chr 9: 107.13 – 107.17 Mb PubMed search
Wikidata
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Function

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.

Interactions

MAPKAPK3 has been shown to interact with MAPK14 and TCF3.

Further reading

• Wei MH, Latif F, Bader S, Kashuba V, Chen JY, Duh FM, Sekido Y, Lee CC, Geil L, Kuzmin I, Zabarovsky E, Klein G, Zbar B, Minna JD, Lerman MI (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. S2CID 45549489.
• Ludwig S, Engel K, Hoffmeyer A, Sithanandam G, Neufeld B, Palm D, Gaestel M, Rapp UR (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. doi:10.1128/mcb.16.12.6687. PMC 231671. PMID 8943323.
• Kumar S, McDonnell PC, Gum RJ, Hand AT, Lee JC, Young PR (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, Jordan BW, Chen P, Dinev D, Ludwig S, Rapp UR (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. PMC 133461. PMID 11157753.
• Simkhovich BZ, Abdishoo S, Poizat C, Hale SL, Kedes LH, Kloner RA (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. PMC 1222910. PMID 12171600.
• Zakowski V, Keramas G, Kilian K, Rapp UR, Ludwig S (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.
• Voncken JW, Niessen H, Neufeld B, Rennefahrt U, Dahlmans V, Kubben N, Holzer B, Ludwig S, Rapp UR (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, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.