# MAP2K2

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Protein-coding gene in the species Homo sapiens

Main article: [Mitogen-activated protein kinase kinase](/source/Mitogen-activated_protein_kinase_kinase)

MAP2K2 Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1S9I, 4H3Q Identifiers Aliases MAP2K2, CFC4, MAPKK2, MEK2, MKK2, PRKMK2, mitogen-activated protein kinase kinase 2 External IDs OMIM: 601263; MGI: 1346867; HomoloGene: 48591; GeneCards: MAP2K2; OMA:MAP2K2 - orthologs Gene location (Human) Chr. Chromosome 19 (human)[1] Band 19p13.3 Start 4,090,321 bp[1] End 4,124,122 bp[1] Gene location (Mouse) Chr. Chromosome 10 (mouse)[2] Band 10 C1|10 39.72 cM Start 80,941,749 bp[2] End 80,969,809 bp[2] RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in mucosa of transverse colon right testis left testis apex of heart muscle of thigh gastrocnemius muscle right frontal lobe anterior pituitary right hemisphere of cerebellum prefrontal cortex Top expressed in muscle of thigh lip right kidney yolk sac neural tube ventricular zone duodenum esophagus superior frontal gyrus Rostral migratory stream More reference expression data BioGPS More reference expression data Gene ontology Molecular function transferase activity nucleotide binding protein kinase activity PDZ domain binding scaffold protein binding protein serine/threonine kinase activator activity metal ion binding kinase activity protein binding protein serine/threonine/tyrosine kinase activity protein tyrosine kinase activity ATP binding MAP kinase kinase activity protein serine/threonine kinase activity Cellular component late endosome Golgi apparatus membrane focal adhesion cell-cell junction peroxisomal membrane extracellular region early endosome endoplasmic reticulum mitochondrion perinuclear region of cytoplasm cytoplasmic side of plasma membrane microtubule nucleus cytoplasm cytosol plasma membrane Biological process phosphorylation regulation of early endosome to late endosome transport peptidyl-serine autophosphorylation negative regulation of gene expression positive regulation of protein serine/threonine kinase activity protein phosphorylation peptidyl-tyrosine phosphorylation regulation of Golgi inheritance regulation of stress-activated MAPK cascade MAPK cascade ERK1 and ERK2 cascade positive regulation of production of miRNAs involved in gene silencing by miRNA positive regulation of transcription, DNA-templated positive regulation of ERK1 and ERK2 cascade regulation of mitotic cell cycle regulation of apoptotic process signal transduction stress-activated protein kinase signaling cascade activation of protein kinase activity Sources:Amigo / QuickGO Orthologs Species Human Mouse Entrez 5605 26396 Ensembl ENSG00000126934 ENSMUSG00000035027 UniProt P36507 Q63932 RefSeq (mRNA) NM_030662 NM_023138 NM_001347144 NM_001358539 RefSeq (protein) NP_109587 NP_001334073 NP_075627 NP_001345468 Location (UCSC) Chr 19: 4.09 – 4.12 Mb Chr 10: 80.94 – 80.97 Mb PubMed search [3] [4] Wikidata View/Edit Human View/Edit Mouse

**Dual specificity mitogen-activated protein kinase kinase 2** is an [enzyme](/source/Enzyme) that in humans is encoded by the *MAP2K2* [gene](/source/Gene).[5] It is more commonly known as MEK2, but has many alternative names including CFC4, MKK2, MAPKK2 and PRKMK2.[6]

## Function

The protein encoded by this gene is a dual specificity protein kinase that belongs to the MAP kinase kinase family. This kinase is known to play a critical role in [mitogen growth factor signal transduction](/source/MAPK%2FERK_pathway). It phosphorylates and thus activates [MAPK1](/source/MAPK1)/ERK2 and [MAPK3](/source/MAPK3)/ERK1.

The activation of this kinase itself is dependent on the Ser/Thr phosphorylation by [MAP kinase kinase kinases](/source/MAP_kinase_kinase_kinase).

The inhibition or degradation of this kinase is found to be involved in the pathogenesis of Yersinia and anthrax.[7]

## Interactions

MAP2K2 has been shown to [interact](/source/Protein-protein_interaction) with [MAPK3](/source/MAPK3)[8][9][10] and [ARAF](/source/ARAF).[11]

## References

1. ^ [***a***](#cite_ref-refGRCh38Ensembl_1-0) [***b***](#cite_ref-refGRCh38Ensembl_1-1) [***c***](#cite_ref-refGRCh38Ensembl_1-2) [GRCh38: Ensembl release 89: ENSG00000126934](http://May2017.archive.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000126934) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. ^ [***a***](#cite_ref-refGRCm38Ensembl_2-0) [***b***](#cite_ref-refGRCm38Ensembl_2-1) [***c***](#cite_ref-refGRCm38Ensembl_2-2) [GRCm38: Ensembl release 89: ENSMUSG00000035027](http://May2017.archive.ensembl.org/Mus_musculus/Gene/Summary?db=core;g=ENSMUSG00000035027) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. **[^](#cite_ref-3)** ["Human PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=5605). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-4)** ["Mouse PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=26396). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-pmid8388392_5-0)** Zheng CF, Guan KL (Jun 1993). ["Cloning and characterization of two distinct human extracellular signal-regulated kinase activator kinases, MEK1 and MEK2"](https://doi.org/10.1016%2FS0021-9258%2818%2982142-1). *J Biol Chem*. **268** (15): 11435–9. [doi](/source/Doi_(identifier)):[10.1016/S0021-9258(18)82142-1](https://doi.org/10.1016%2FS0021-9258%2818%2982142-1). [PMID](/source/PMID_(identifier)) [8388392](https://pubmed.ncbi.nlm.nih.gov/8388392).

1. **[^](#cite_ref-6)** ["MAP2K2 mitogen-activated protein kinase kinase 2 \[Homo sapiens (human)\] - Gene - NCBI"](https://www.ncbi.nlm.nih.gov/gene/5605). *www.ncbi.nlm.nih.gov*. Retrieved 2015-10-16.

1. **[^](#cite_ref-7)** ["Entrez Gene: MAP2K2 mitogen-activated protein kinase kinase 2"](https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=5605).

1. **[^](#cite_ref-pmid9006895_8-0)** Marti A, Luo Z, Cunningham C, Ohta Y, Hartwig J, Stossel T P, Kyriakis J M, Avruch J (Jan 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"](https://doi.org/10.1074%2Fjbc.272.5.2620). *J. Biol. Chem*. **272** (5). UNITED STATES: 2620–8. [doi](/source/Doi_(identifier)):[10.1074/jbc.272.5.2620](https://doi.org/10.1074%2Fjbc.272.5.2620). [ISSN](/source/ISSN_(identifier)) [0021-9258](https://search.worldcat.org/issn/0021-9258). [PMID](/source/PMID_(identifier)) [9006895](https://pubmed.ncbi.nlm.nih.gov/9006895).

1. **[^](#cite_ref-pmid8626767_9-0)** Butch ER, Guan K L (Feb 1996). ["Characterization of ERK1 activation site mutants and the effect on recognition by MEK1 and MEK2"](https://doi.org/10.1074%2Fjbc.271.8.4230). *J. Biol. Chem*. **271** (8). UNITED STATES: 4230–5. [doi](/source/Doi_(identifier)):[10.1074/jbc.271.8.4230](https://doi.org/10.1074%2Fjbc.271.8.4230). [ISSN](/source/ISSN_(identifier)) [0021-9258](https://search.worldcat.org/issn/0021-9258). [PMID](/source/PMID_(identifier)) [8626767](https://pubmed.ncbi.nlm.nih.gov/8626767).

1. **[^](#cite_ref-pmid8226933_10-0)** Zheng CF, Guan K L (Nov 1993). ["Properties of MEKs, the kinases that phosphorylate and activate the extracellular signal-regulated kinases"](https://doi.org/10.1016%2FS0021-9258%2820%2980474-8). *J. Biol. Chem*. **268** (32). UNITED STATES: 23933–9. [doi](/source/Doi_(identifier)):[10.1016/S0021-9258(20)80474-8](https://doi.org/10.1016%2FS0021-9258%2820%2980474-8). [ISSN](/source/ISSN_(identifier)) [0021-9258](https://search.worldcat.org/issn/0021-9258). [PMID](/source/PMID_(identifier)) [8226933](https://pubmed.ncbi.nlm.nih.gov/8226933).

1. **[^](#cite_ref-pmid11909642_11-0)** Yin XL, Chen She, Yan Jun, Hu Yun, Gu Jian X (Feb 2002). ["Identification of interaction between MEK2 and A-Raf-1"](https://doi.org/10.1016%2FS0167-4889%2801%2900188-4). *Biochim. Biophys. Acta*. **1589** (1). Netherlands: 71–6. [doi](/source/Doi_(identifier)):[10.1016/S0167-4889(01)00188-4](https://doi.org/10.1016%2FS0167-4889%2801%2900188-4). [ISSN](/source/ISSN_(identifier)) [0006-3002](https://search.worldcat.org/issn/0006-3002). [PMID](/source/PMID_(identifier)) [11909642](https://pubmed.ncbi.nlm.nih.gov/11909642).

## Further reading

- Joseph AM, Kumar M, Mitra D (2005). "Nef: "necessary and enforcing factor" in HIV infection". *Curr. HIV Res*. **3** (1): 87–94. [doi](/source/Doi_(identifier)):[10.2174/1570162052773013](https://doi.org/10.2174%2F1570162052773013). [PMID](/source/PMID_(identifier)) [15638726](https://pubmed.ncbi.nlm.nih.gov/15638726).

- Stove V, Verhasselt B (2006). "Modelling thymic HIV-1 Nef effects". *Curr. HIV Res*. **4** (1): 57–64. [doi](/source/Doi_(identifier)):[10.2174/157016206775197583](https://doi.org/10.2174%2F157016206775197583). [PMID](/source/PMID_(identifier)) [16454711](https://pubmed.ncbi.nlm.nih.gov/16454711).

- Charest DL, Mordret G, Harder KW, et al. (1993). ["Molecular cloning, expression, and characterization of the human mitogen-activated protein kinase p44erk1"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC360094). *Mol. Cell. Biol*. **13** (8): 4679–90. [doi](/source/Doi_(identifier)):[10.1128/mcb.13.8.4679](https://doi.org/10.1128%2Fmcb.13.8.4679). [PMC](/source/PMC_(identifier)) [360094](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC360094). [PMID](/source/PMID_(identifier)) [7687743](https://pubmed.ncbi.nlm.nih.gov/7687743).

- Dérijard B, Raingeaud J, Barrett T, et al. (1995). "Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms". *Science*. **267** (5198): 682–5. [Bibcode](/source/Bibcode_(identifier)):[1995Sci...267..682D](https://ui.adsabs.harvard.edu/abs/1995Sci...267..682D). [doi](/source/Doi_(identifier)):[10.1126/science.7839144](https://doi.org/10.1126%2Fscience.7839144). [PMID](/source/PMID_(identifier)) [7839144](https://pubmed.ncbi.nlm.nih.gov/7839144). [S2CID](/source/S2CID_(identifier)) [9153074](https://api.semanticscholar.org/CorpusID:9153074).

- Alessi DR, Saito Y, Campbell DG, et al. (1994). ["Identification of the sites in MAP kinase kinase-1 phosphorylated by p74raf-1"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC394991). *EMBO J*. **13** (7): 1610–9. [doi](/source/Doi_(identifier)):[10.1002/j.1460-2075.1994.tb06424.x](https://doi.org/10.1002%2Fj.1460-2075.1994.tb06424.x). [PMC](/source/PMC_(identifier)) [394991](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC394991). [PMID](/source/PMID_(identifier)) [8157000](https://pubmed.ncbi.nlm.nih.gov/8157000).

- Zheng CF, Guan KL (1993). ["Properties of MEKs, the kinases that phosphorylate and activate the extracellular signal-regulated kinases"](https://doi.org/10.1016%2FS0021-9258%2820%2980474-8). *J. Biol. Chem*. **268** (32): 23933–9. [doi](/source/Doi_(identifier)):[10.1016/S0021-9258(20)80474-8](https://doi.org/10.1016%2FS0021-9258%2820%2980474-8). [PMID](/source/PMID_(identifier)) [8226933](https://pubmed.ncbi.nlm.nih.gov/8226933).

- Wu J, Harrison JK, Dent P, et al. (1993). ["Identification and characterization of a new mammalian mitogen-activated protein kinase kinase, MKK2"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC360070). *Mol. Cell. Biol*. **13** (8): 4539–48. [doi](/source/Doi_(identifier)):[10.1128/mcb.13.8.4539](https://doi.org/10.1128%2Fmcb.13.8.4539). [PMC](/source/PMC_(identifier)) [360070](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC360070). [PMID](/source/PMID_(identifier)) [8393135](https://pubmed.ncbi.nlm.nih.gov/8393135).

- Moriguchi T, Gotoh Y, Nishida E (1996). ["Activation of two isoforms of mitogen-activated protein kinase kinase in response to epidermal growth factor and nerve growth factor"](https://doi.org/10.1111%2Fj.1432-1033.1995.032_c.x). *Eur. J. Biochem*. **234** (1): 32–8. [doi](/source/Doi_(identifier)):[10.1111/j.1432-1033.1995.032_c.x](https://doi.org/10.1111%2Fj.1432-1033.1995.032_c.x). [PMID](/source/PMID_(identifier)) [8529659](https://pubmed.ncbi.nlm.nih.gov/8529659).

- Butch ER, Guan KL (1996). ["Characterization of ERK1 activation site mutants and the effect on recognition by MEK1 and MEK2"](https://doi.org/10.1074%2Fjbc.271.8.4230). *J. Biol. Chem*. **271** (8): 4230–5. [doi](/source/Doi_(identifier)):[10.1074/jbc.271.8.4230](https://doi.org/10.1074%2Fjbc.271.8.4230). [PMID](/source/PMID_(identifier)) [8626767](https://pubmed.ncbi.nlm.nih.gov/8626767).

- Papin C, Denouel A, Calothy G, Eychène A (1996). "Identification of signalling proteins interacting with B-Raf in the yeast two-hybrid system". *Oncogene*. **12** (10): 2213–21. [PMID](/source/PMID_(identifier)) [8668348](https://pubmed.ncbi.nlm.nih.gov/8668348).

- Downey GP, Butler JR, Brumell J, et al. (1996). ["Chemotactic peptide-induced activation of MEK-2, the predominant isoform in human neutrophils. Inhibition by wortmannin"](https://doi.org/10.1074%2Fjbc.271.35.21005). *J. Biol. Chem*. **271** (35): 21005–1011. [doi](/source/Doi_(identifier)):[10.1074/jbc.271.35.21005](https://doi.org/10.1074%2Fjbc.271.35.21005). [PMID](/source/PMID_(identifier)) [8702863](https://pubmed.ncbi.nlm.nih.gov/8702863).

- Khoo S, Cobb MH (1997). ["Activation of mitogen-activating protein kinase by glucose is not required for insulin secretion"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC20824). *Proc. Natl. Acad. Sci. U.S.A*. **94** (11): 5599–604. [Bibcode](/source/Bibcode_(identifier)):[1997PNAS...94.5599K](https://ui.adsabs.harvard.edu/abs/1997PNAS...94.5599K). [doi](/source/Doi_(identifier)):[10.1073/pnas.94.11.5599](https://doi.org/10.1073%2Fpnas.94.11.5599). [PMC](/source/PMC_(identifier)) [20824](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC20824). [PMID](/source/PMID_(identifier)) [9159118](https://pubmed.ncbi.nlm.nih.gov/9159118).

- Li CJ, Ueda Y, Shi B (1997). ["Tat protein induces self-perpetuating permissivity for productive HIV-1 infection"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC21566). *Proc. Natl. Acad. Sci. U.S.A*. **94** (15): 8116–20. [Bibcode](/source/Bibcode_(identifier)):[1997PNAS...94.8116L](https://ui.adsabs.harvard.edu/abs/1997PNAS...94.8116L). [doi](/source/Doi_(identifier)):[10.1073/pnas.94.15.8116](https://doi.org/10.1073%2Fpnas.94.15.8116). [PMC](/source/PMC_(identifier)) [21566](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC21566). [PMID](/source/PMID_(identifier)) [9223324](https://pubmed.ncbi.nlm.nih.gov/9223324).

- Menegon A, Leoni C, Benfenati F, Valtorta F (1997). "Tat protein from HIV-1 activates MAP kinase in granular neurons and glial cells from rat cerebellum". *Biochem. Biophys. Res. Commun*. **238** (3): 800–5. [Bibcode](/source/Bibcode_(identifier)):[1997BBRC..238..800M](https://ui.adsabs.harvard.edu/abs/1997BBRC..238..800M). [doi](/source/Doi_(identifier)):[10.1006/bbrc.1997.7393](https://doi.org/10.1006%2Fbbrc.1997.7393). [PMID](/source/PMID_(identifier)) [9325171](https://pubmed.ncbi.nlm.nih.gov/9325171).

- Denouel-Galy A, Douville EM, Warne PH (1998). ["Murine Ksr interacts with MEK and inhibits Ras-induced transformation"](https://doi.org/10.1016%2FS0960-9822%2898%2970019-3). *Curr. Biol*. **8** (1): 46–55. [Bibcode](/source/Bibcode_(identifier)):[1998CBio....8...46D](https://ui.adsabs.harvard.edu/abs/1998CBio....8...46D). [doi](/source/Doi_(identifier)):[10.1016/S0960-9822(98)70019-3](https://doi.org/10.1016%2FS0960-9822%2898%2970019-3). [PMID](/source/PMID_(identifier)) [9427625](https://pubmed.ncbi.nlm.nih.gov/9427625). [S2CID](/source/S2CID_(identifier)) [15524760](https://api.semanticscholar.org/CorpusID:15524760).

- Gibellini D, Bassini A, Pierpaoli S (1998). "Extracellular HIV-1 Tat protein induces the rapid Ser133 phosphorylation and activation of CREB transcription factor in both Jurkat lymphoblastoid T cells and primary peripheral blood mononuclear cells". *J. Immunol*. **160** (8): 3891–8. [doi](/source/Doi_(identifier)):[10.4049/jimmunol.160.8.3891](https://doi.org/10.4049%2Fjimmunol.160.8.3891). [PMID](/source/PMID_(identifier)) [9558095](https://pubmed.ncbi.nlm.nih.gov/9558095). [S2CID](/source/S2CID_(identifier)) [31628194](https://api.semanticscholar.org/CorpusID:31628194).

- Duesbery NS, Webb CP, Leppla SH (1998). "Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor". *Science*. **280** (5364): 734–7. [Bibcode](/source/Bibcode_(identifier)):[1998Sci...280..734D](https://ui.adsabs.harvard.edu/abs/1998Sci...280..734D). [doi](/source/Doi_(identifier)):[10.1126/science.280.5364.734](https://doi.org/10.1126%2Fscience.280.5364.734). [PMID](/source/PMID_(identifier)) [9563949](https://pubmed.ncbi.nlm.nih.gov/9563949).

- Ganju RK, Munshi N, Nair BC (1998). ["Human Immunodeficiency Virus Tat Modulates the Flk-1/KDR Receptor, Mitogen-Activated Protein Kinases, and Components of Focal Adhesion in Kaposi's Sarcoma Cells"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC110419). *J. Virol*. **72** (7): 6131–7. [doi](/source/Doi_(identifier)):[10.1128/JVI.72.7.6131-6137.1998](https://doi.org/10.1128%2FJVI.72.7.6131-6137.1998). [PMC](/source/PMC_(identifier)) [110419](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC110419). [PMID](/source/PMID_(identifier)) [9621077](https://pubmed.ncbi.nlm.nih.gov/9621077).

- Tanimura S, Chatani Y, Hoshino R (1998). "Activation of the 41/43 kDa mitogen-activated protein kinase signaling pathway is required for hepatocyte growth factor-induced cell scattering". *Oncogene*. **17** (1): 57–65. [doi](/source/Doi_(identifier)):[10.1038/sj.onc.1201905](https://doi.org/10.1038%2Fsj.onc.1201905). [PMID](/source/PMID_(identifier)) [9671314](https://pubmed.ncbi.nlm.nih.gov/9671314). [S2CID](/source/S2CID_(identifier)) [7117056](https://api.semanticscholar.org/CorpusID:7117056).

## External links

- [GeneReviews/NCBI/NIH/UW entry on Cardiofaciocutaneous Syndrome](https://www.ncbi.nlm.nih.gov/books/NBK1186/)

- Overview of all the structural information available in the [PDB](/source/Protein_Data_Bank) for [UniProt](/source/UniProt): *[P36507](https://www.ebi.ac.uk/pdbe/pdbe-kb/proteins/P36507)* (Dual specificity mitogen-activated protein kinase kinase 2) at the [PDBe-KB](/source/PDBe-KB).

v t e PDB gallery 1s9i: X-ray structure of the human mitogen-activated protein kinase kinase 2 (MEK2)in a complex with ligand and MgATP

v t e Kinases: Serine/threonine-specific protein kinases (EC 2.7.11-12) Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20) Non-specific serine/threonine protein kinases (EC 2.7.11.1) LATS1 LATS2 MAST1 MAST2 STK38 STK38L CIT ROCK1 SGK SGK2 SGK3 Protein kinase B AKT1 AKT2 AKT3 Ataxia telangiectasia mutated mTOR EIF-2 kinases PKR HRI EIF2AK3 EIF2AK4 Wee1 WEE1 Pyruvate dehydrogenase kinase (EC 2.7.11.2) PDK1 PDK2 PDK3 PDK4 Dephospho-(reductase kinase) kinase (EC 2.7.11.3) AMP-activated protein kinase α PRKAA1 PRKAA2 β PRKAB1 PRKAB2 γ PRKAG1 PRKAG2 PRKAG3 3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4) BCKDK BCKDHA BCKDHB (isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5) IDH2 IDH3A IDH3B IDH3G (tyrosine 3-monooxygenase) kinase (EC 2.7.11.6) STK4 Myosin-heavy-chain kinase (EC 2.7.11.7) Aurora kinase Aurora kinase A Aurora kinase B Aurora kinase C Fas-activated serine/threonine kinase (EC 2.7.11.8) FASTK STK10 Goodpasture-antigen-binding protein kinase (EC 2.7.11.9) - IκB kinase (EC 2.7.11.10) CHUK IKK2 TBK1 IKBKE IKBKG IKBKAP cAMP-dependent protein kinase (EC 2.7.11.11) Protein kinase A PRKACG PRKACB PRKACA PRKY cGMP-dependent protein kinase (EC 2.7.11.12) Protein kinase G PRKG1 Protein kinase C (EC 2.7.11.13) Protein kinase C Protein kinase Cζ PKC alpha PRKCB1 PRKCD PRKCE PRKCH PRKCG PRKCI PRKCQ Protein kinase N1 PKN2 PKN3 Rhodopsin kinase (EC 2.7.11.14) Rhodopsin kinase Beta adrenergic receptor kinase (EC 2.7.11.15) Beta adrenergic receptor kinase Beta adrenergic receptor kinase-2 G-protein coupled receptor kinases (EC 2.7.11.16) GRK4 GRK5 GRK6 Ca2+/calmodulin-dependent (EC 2.7.11.17) BRSK2 CAMK1 CAMK1A CAMK1B CAMK1D CAMK1G CAMK2 CAMK2A CAMK2B CAMK2D CAMK2G CAMK4 MLCK CASK CHEK1 CHEK2 DAPK1 DAPK2 DAPK3 STK11 MAPKAPK2 MAPKAPK3 MAPKAPK5 MARK1 MARK2 MARK3 MARK4 MELK MKNK1 MKNK2 NUAK1 NUAK2 OBSCN PASK PHKG1 PHKG2 PIM1 PIM2 PKD1 PRKD2 PRKD3 PSKH1 SNF1LK2 KIAA0999 STK40 SNF1LK SNRK SPEG TSSK2 Kalirin TRIB1 TRIB2 TRIB3 TRIO Titin DCLK1 Myosin light-chain kinase (EC 2.7.11.18) MYLK MYLK2 MYLK3 MYLK4 Phosphorylase kinase (EC 2.7.11.19) PHKA1 PHKA2 PHKB PHKG1 PHKG2 Elongation factor 2 kinase (EC 2.7.11.20) EEF2K STK19 Polo kinase (EC 2.7.11.21) PLK1 PLK2 PLK3 PLK4 Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30) Polo kinase (EC 2.7.11.21) PLK1 PLK2 PLK3 PLK4 Cyclin-dependent kinase (EC 2.7.11.22) CDK1 CDK2 CDKL2 CDK3 CDK4 CDK5 CDKL5 CDK6 CDK7 CDK8 CDK9 CDK10 CDK12 CDC2L5 PCTK1 PCTK2 PCTK3 PFTK1 CDC2L1 (RNA-polymerase)-subunit kinase (EC 2.7.11.23) RPS6KA5 RPS6KA4 P70-S6 Kinase 1 RPS6KB2 RPS6KA2 RPS6KA3 RPS6KA1 RPS6KC1 Mitogen-activated protein kinase (EC 2.7.11.24) Extracellular signal-regulated MAPK1 MAPK3 MAPK4 MAPK6 MAPK7 MAPK12 MAPK15 C-Jun N-terminal MAPK8 MAPK9 MAPK10 P38 mitogen-activated protein MAPK11 MAPK13 MAPK14 MAP3K (EC 2.7.11.25) MAP kinase kinase kinases MAP3K1 MAP3K2 MAP3K3 MAP3K4 MAP3K5 MAP3K6 MAP3K7 MAP3K8 RAFs ARAF BRAF KSR1 KSR2 MLKs MAP3K12 MAP3K13 MAP3K9 MAP3K10 MAP3K11 MAP3K7 ZAK CDC7 MAP3K14 Tau-protein kinase (EC 2.7.11.26) TPK1 TTK GSK-3 (acetyl-CoA carboxylase) kinase (EC 2.7.11.27) - Tropomyosin kinase (EC 2.7.11.28) - Low-density-lipoprotein receptor kinase (EC 2.7.11.29) - Receptor protein serine/threonine kinase (EC 2.7.11.30) Bone morphogenetic protein receptors BMPR1 BMPR1A BMPR1B BMPR2 ACVR1 ACVR1B ACVR1C ACVR2A ACVR2B ACVRL1 Anti-Müllerian hormone receptor Dual-specificity kinases (EC 2.7.12) MAP2K MAP2K1 MAP2K2 MAP2K3 MAP2K4 MAP2K5 MAP2K6 MAP2K7

v t e Enzymes Activity Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis Regulation Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator Classification EC number Enzyme superfamily Enzyme family List of enzymes Kinetics Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics Types EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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Adapted from the Wikipedia article [MAP2K2](https://en.wikipedia.org/wiki/MAP2K2) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/MAP2K2?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.