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MAPK3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2ZOQ, 4QTB
Identifiers
Aliases	MAPK3, ERK-1, ERK1, ERT2, HS44KDAP, HUMKER1A, P44ERK1, P44MAPK, PRKM3, p44-ERK1, p44-MAPK, mitogen-activated protein kinase 3
External IDs	OMIM: 601795; MGI: 1346859; HomoloGene: 55682; GeneCards: MAPK3; OMA:MAPK3 - orthologs
Gene location (Human) Chr. Chromosome 16 (human) Band 16p11.2 Start 30,114,105 bp End 30,123,506 bp
Gene location (Mouse) Chr. Chromosome 7 (mouse) Band 7 F3|7 69.25 cM Start 126,358,773 bp End 126,364,991 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right frontal lobe mucosa of transverse colon Amygdala cingulate gyrus anterior cingulate cortex gastric mucosa nucleus accumbens ectocervix rectum C1 segment Top expressed in granulocyte dentate gyrus of hippocampal formation granule cell yolk sac pyloric antrum lip entorhinal cortex large intestine colon epithelium of stomach duodenum More reference expression data BioGPS More reference expression data
Gene ontology Molecular function phosphatase binding ATP binding protein kinase activity MAP kinase activity transferase activity phosphotyrosine residue binding scaffold protein binding protein binding nucleotide binding kinase activity protein serine/threonine kinase activity MAP kinase kinase activity identical protein binding Cellular component cytosol nuclear envelope focal adhesion mitochondrion cytoskeleton nucleus late endosome Golgi apparatus early endosome pseudopodium nucleoplasm cytoplasm plasma membrane caveola membrane protein-containing complex Biological process caveolin-mediated endocytosis positive regulation of protein phosphorylation positive regulation of telomere capping response to exogenous dsRNA cardiac neural crest cell development involved in heart development positive regulation of xenophagy positive regulation of translation cellular response to DNA damage stimulus platelet activation Fc-epsilon receptor signaling pathway protein phosphorylation cellular response to mechanical stimulus face development positive regulation of histone modification regulation of DNA-binding transcription factor activity DNA damage induced protein phosphorylation positive regulation of ERK1 and ERK2 cascade animal organ morphogenesis cell cycle apoptotic process Fc-gamma receptor signaling pathway involved in phagocytosis thymus development ERK1 and ERK2 cascade negative regulation of apolipoprotein binding transcription, DNA-templated cartilage development viral process response to toxic substance regulation of stress-activated MAPK cascade phosphorylation outer ear morphogenesis BMP signaling pathway response to lipopolysaccharide thyroid gland development response to epidermal growth factor positive regulation of MAP kinase activity positive regulation of telomerase activity peptidyl-tyrosine autophosphorylation sensory perception of pain positive regulation of cyclase activity trachea formation lipopolysaccharide-mediated signaling pathway intracellular signal transduction lung morphogenesis neural crest cell development transcription initiation from RNA polymerase I promoter regulation of early endosome to late endosome transport positive regulation of telomere maintenance via telomerase MAPK cascade positive regulation of histone acetylation axon guidance interleukin-1-mediated signaling pathway fibroblast growth factor receptor signaling pathway peptidyl-serine phosphorylation regulation of cellular response to heat Bergmann glial cell differentiation regulation of Golgi inheritance arachidonic acid metabolic process regulation of cytoskeleton organization positive regulation of transcription by RNA polymerase II regulation of phosphatidylinositol 3-kinase signaling regulation of ossification positive regulation of gene expression positive regulation of macrophage chemotaxis cellular response to amino acid starvation cellular response to reactive oxygen species stress-activated MAPK cascade cellular response to cadmium ion cellular response to dopamine positive regulation of metallopeptidase activity regulation of cellular pH protein-containing complex assembly cellular response to tumor necrosis factor regulation of gene expression cellular response to organic substance ageing decidualization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5595 26417 Ensembl ENSG00000102882 ENSMUSG00000063065 UniProt P27361 Q63844 RefSeq (mRNA) NM_001040056 NM_001109891 NM_002746 NM_011952 RefSeq (protein) NP_001035145 NP_001103361 NP_002737 NP_036082 Location (UCSC) Chr 16: 30.11 – 30.12 Mb Chr 7: 126.36 – 126.36 Mb PubMed search
Wikidata
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Mitogen-activated protein kinase 3, also known as p44MAPK and ERK1, is an enzyme that in humans is encoded by the MAPK3 gene.

Function

The protein encoded by this gene is a member of the mitogen-activated protein kinase (MAP kinase) family. MAP kinases, also known as extracellular signal-regulated kinases (ERKs), act in a signaling cascade that regulates various cellular processes such as proliferation, differentiation, and cell cycle progression in response to a variety of extracellular signals. This kinase is activated by upstream kinases, resulting in its translocation to the nucleus where it phosphorylates nuclear targets. Alternatively spliced transcript variants encoding different protein isoforms have been described.

Clinical significance

It has been suggested that MAPK3, along with the gene IRAK1, is turned off by two microRNAs that were activated after the influenza A virus had been made to infect human lung cells.

Signaling pathways

Pharmacological inhibition of ERK1/2 restores GSK3β activity and protein synthesis levels in a model of tuberous sclerosis.

Interactions

MAPK3 has been shown to interact with:

• DUSP3,
• DUSP6
• GTF2I,
• HDAC4,
• MAP2K1,
• MAP2K2,
• PTPN7,
• RPS6KA2, and
• SPIB.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000102882 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000063065 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Thomas, Gareth M.; Huganir, Richard L. (1 March 2004). "MAPK cascade signalling and synaptic plasticity". Nature Reviews Neuroscience. 5 (3): 173–183. doi:10.1038/nrn1346. ISSN 1471-003X. PMID 14976517. S2CID 205499891.
6. García F, Zalba G, Páez G, Encío I, de Miguel C (15 May 1998). "Molecular cloning and characterization of the human p44 mitogen-activated protein kinase gene". Genomics. 50 (1): 69–78. doi:10.1006/geno.1998.5315. PMID 9628824.
7. "Entrez Gene: MAPK3 mitogen-activated protein kinase 3".
8. Buggele WA, Johnson KE, Horvath CM (2012). "Influenza A virus infection of human respiratory cells induces primary microRNA expression". J. Biol. Chem. 287 (37): 31027–40. doi:10.1074/jbc.M112.387670. PMC 3438935. PMID 22822053.
9. Pal R, Bondar VV, Adamski CJ, Rodney GG, Sardiello M (2017). "Inhibition of ERK1/2 Restores GSK3β Activity and Protein Synthesis Levels in a Model of Tuberous Sclerosis". Sci. Rep. 7 (1): 4174. Bibcode:2017NatSR...7.4174P. doi:10.1038/s41598-017-04528-5. PMC 5482840. PMID 28646232.
10. Todd JL, Tanner KG, Denu JM (May 1999). "Extracellular regulated kinases (ERK) 1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR. A novel role in down-regulating the ERK pathway". J. Biol. Chem. 274 (19): 13271–80. doi:10.1074/jbc.274.19.13271. PMID 10224087.
11. Muda M, Theodosiou A, Gillieron C, Smith A, Chabert C, Camps M, Boschert U, Rodrigues N, Davies K, Ashworth A, Arkinstall S (April 1998). "The mitogen-activated protein kinase phosphatase-3 N-terminal noncatalytic region is responsible for tight substrate binding and enzymatic specificity". J. Biol. Chem. 273 (15): 9323–9. doi:10.1074/jbc.273.15.9323. PMID 9535927.
12. Kim DW, Cochran BH (February 2000). "Extracellular signal-regulated kinase binds to TFII-I and regulates its activation of the c-fos promoter". Mol. Cell. Biol. 20 (4): 1140–8. doi:10.1128/mcb.20.4.1140-1148.2000. PMC 85232. PMID 10648599.
13. Zhou X, Richon VM, Wang AH, Yang XJ, Rifkind RA, Marks PA (December 2000). "Histone deacetylase 4 associates with extracellular signal-regulated kinases 1 and 2, and its cellular localization is regulated by oncogenic Ras". Proc. Natl. Acad. Sci. U.S.A. 97 (26): 14329–33. Bibcode:2000PNAS...9714329Z. doi:10.1073/pnas.250494697. PMC 18918. PMID 11114188.
14. ^ Marti A, Luo Z, Cunningham C, Ohta Y, Hartwig J, Stossel TP, Kyriakis JM, Avruch J (January 1997). "Actin-binding protein-280 binds the stress-activated protein kinase (SAPK) activator SEK-1 and is required for tumor necrosis factor-alpha activation of SAPK in melanoma cells". J. Biol. Chem. 272 (5): 2620–8. doi:10.1074/jbc.272.5.2620. PMID 9006895.
15. ^ Butch ER, Guan KL (February 1996). "Characterization of ERK1 activation site mutants and the effect on recognition by MEK1 and MEK2". J. Biol. Chem. 271 (8): 4230–5. doi:10.1074/jbc.271.8.4230. PMID 8626767.
16. Elion EA (September 1998). "Routing MAP kinase cascades". Science. 281 (5383): 1625–6. doi:10.1126/science.281.5383.1625. PMID 9767029. S2CID 28868990.
17. ^ Zheng CF, Guan KL (November 1993). "Properties of MEKs, the kinases that phosphorylate and activate the extracellular signal-regulated kinases". J. Biol. Chem. 268 (32): 23933–9. doi:10.1016/S0021-9258(20)80474-8. PMID 8226933.
18. Pettiford SM, Herbst R (February 2000). "The MAP-kinase ERK2 is a specific substrate of the protein tyrosine phosphatase HePTP". Oncogene. 19 (7): 858–69. doi:10.1038/sj.onc.1203408. PMID 10702794.
19. Saxena M, Williams S, Taskén K, Mustelin T (September 1999). "Crosstalk between cAMP-dependent kinase and MAP kinase through a protein tyrosine phosphatase". Nat. Cell Biol. 1 (5): 305–11. doi:10.1038/13024. PMID 10559944. S2CID 40413956.
20. Saxena M, Williams S, Brockdorff J, Gilman J, Mustelin T (April 1999). "Inhibition of T cell signaling by mitogen-activated protein kinase-targeted hematopoietic tyrosine phosphatase (HePTP)". J. Biol. Chem. 274 (17): 11693–700. doi:10.1074/jbc.274.17.11693. PMID 10206983.
21. Roux PP, Richards SA, Blenis J (July 2003). "Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity". Mol. Cell. Biol. 23 (14): 4796–804. doi:10.1128/mcb.23.14.4796-4804.2003. PMC 162206. PMID 12832467.
22. Zhao Y, Bjorbaek C, Moller DE (November 1996). "Regulation and interaction of pp90(rsk) isoforms with mitogen-activated protein kinases". J. Biol. Chem. 271 (47): 29773–9. doi:10.1074/jbc.271.47.29773. PMID 8939914.
23. Mao C, Ray-Gallet D, Tavitian A, Moreau-Gachelin F (February 1996). "Differential phosphorylations of Spi-B and Spi-1 transcription factors". Oncogene. 12 (4): 863–73. PMID 8632909.

Further reading

• Peruzzi F, Gordon J, Darbinian N, Amini S (2002). "Tat-induced deregulation of neuronal differentiation and survival by nerve growth factor pathway". J. Neurovirol. 8 Suppl 2 (2): 91–6. doi:10.1080/13550280290167885. PMID 12491158.
• Meloche S, Pouysségur J (2007). "The ERK1/2 mitogen-activated protein kinase pathway as a master regulator of the G1- to S-phase transition". Oncogene. 26 (22): 3227–39. doi:10.1038/sj.onc.1210414. PMID 17496918.
• Ruscica M, Dozio E, Motta M, Magni P (2007), "Modulatory Actions of Neuropeptide y on Prostate Cancer Growth: Role of MAP Kinase/ERK 1/2 Activatio", Modulatory actions of neuropeptide Y on prostate cancer growth: role of MAP kinase/ERK 1/2 activation, Advances In Experimental Medicine And Biology, vol. 604, Springer, pp. 96–100, doi:10.1007/978-0-387-69116-9_7, ISBN 978-0-387-69114-5, PMID 17695723

External links

• MAP Kinase Resource Archived 2021-04-15 at the Wayback Machine.

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