# MAP2K4

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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)

MAP2K4 Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3ALN, 3ALO, 3VUT Identifiers Aliases MAP2K4, JNKK, JNKK1, MAPKK4, MEK4, MKK4, PRKMK4, SAPKK-1, SAPKK1, SEK1, SERK1, SKK1, mitogen-activated protein kinase kinase 4 External IDs OMIM: 601335; MGI: 1346869; HomoloGene: 48159; GeneCards: MAP2K4; OMA:MAP2K4 - orthologs Gene location (Human) Chr. Chromosome 17 (human)[1] Band 17p12 Start 12,020,829 bp[1] End 12,143,830 bp[1] Gene location (Mouse) Chr. Chromosome 11 (mouse)[2] Band 11 B3|11 40.53 cM Start 65,579,069 bp[2] End 65,679,123 bp[2] RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in lateral nuclear group of thalamus Brodmann area 46 postcentral gyrus orbitofrontal cortex pars compacta middle temporal gyrus superior frontal gyrus prefrontal cortex Achilles tendon Brodmann area 23 Top expressed in dentate gyrus of hippocampal formation granule cell genital tubercle facial motor nucleus superior frontal gyrus primary visual cortex anterior horn of spinal cord secondary oocyte dorsomedial hypothalamic nucleus granulocyte paraventricular nucleus of hypothalamus More reference expression data BioGPS n/a Gene ontology Molecular function transferase activity protein kinase activity nucleotide binding kinase activity protein binding protein tyrosine kinase activity ATP binding MAP kinase kinase activity JUN kinase kinase activity protein serine/threonine kinase activity mitogen-activated protein kinase kinase kinase binding Cellular component cytoplasm nucleus dendrite cytoplasm cytosol perikaryon axon Biological process phosphorylation MAPK cascade protein phosphorylation cellular response to mechanical stimulus response to wounding peptidyl-tyrosine phosphorylation signal transduction negative regulation of motor neuron apoptotic process apoptotic process cell growth involved in cardiac muscle cell development cellular response to sorbitol positive regulation of smooth muscle cell apoptotic process JNK cascade positive regulation of protein phosphorylation positive regulation of neuron apoptotic process positive regulation of DNA replication positive regulation of apoptotic process positive regulation of nitric-oxide synthase biosynthetic process regulation of mitotic cell cycle stress-activated protein kinase signaling cascade activation of protein kinase activity regulation of apoptotic process Fc-epsilon receptor signaling pathway Sources:Amigo / QuickGO Orthologs Species Human Mouse Entrez 6416 26398 Ensembl ENSG00000065559 ENSMUSG00000033352 UniProt P45985 P47809 RefSeq (mRNA) NM_001281435 NM_003010 NM_009157 NM_001316367 NM_001316368 NM_001316369 NM_001362739 NM_001362740 RefSeq (protein) NP_001268364 NP_003001 NP_001303296 NP_001303297 NP_001303298 NP_033183 NP_001349668 NP_001349669 Location (UCSC) Chr 17: 12.02 – 12.14 Mb Chr 11: 65.58 – 65.68 Mb PubMed search [3] [4] Wikidata View/Edit Human View/Edit Mouse

**Dual-specificity mitogen-activated protein kinase kinase 4** is an [enzyme](/source/Enzyme) that in humans is encoded by the *MAP2K4* [gene](/source/Gene).[5]

*MAP2K4* encodes a [dual-specificity kinase](/source/Dual-specificity_kinase) that belongs to the [Ser/Thr protein kinase family](/source/Serine%2Fthreonine-specific_protein_kinase). MAP2K4 phosphorylates [MAP kinases](/source/MAP_kinases) in response to various environmental stresses or mitogenic stimuli. [MAPK8](/source/MAPK8)/JNK1, [MAPK9](/source/MAPK9)/JNK2, and [MAPK14](/source/MAPK14)/p38 are substrates for MAP2K4, but MAPK1/ERK2 and MAPK3/ERK1 are not phosphorylated by MAP2K4. Structurally, MAP2K4 contains a [kinase](/source/Kinase) domain that is phosphorylated and activated by [MAP3K1](/source/MAP3K1)(aka MEKK1).[6] MAP2K4 contains multiple [amino acid](/source/Amino_acid) sites that are [phosphorylated](/source/Phosphorylated) and [ubiquitinated](/source/Ubiquitinated).[7] Genetic studies using *Map2k4* knockout mice revealed embryonic lethality, impaired hepatogenesis and defective liver formation.[8][9] Analysis of chimeric mice identified a role for *Map2k4* in T cell cytokine production and proliferation.[10] *Map2k4*-deficient chimeric mice frequently develop [lymphadenopathy](/source/Lymphadenopathy).[11] MAP2K4 is altered in 1.97% of all human cancers.[12]

## Interactions

MAP2K4 has been shown to [interact](/source/Protein-protein_interaction) with:

- [MAP3K1](/source/MAP3K1),[13]

- [FLNC](/source/FLNC_(gene)),[14]

- [MAPK8](/source/MAPK8),[15][16][17][18][19]

- [MAPK8IP3](/source/MAPK8IP3)[20][21] and

- [AKT1](/source/AKT1).[16]

- [ITCH](/source/ITCH).[22]

## References

1. ^ [***a***](#cite_ref-refGRCh38Ensembl_1-0) [***b***](#cite_ref-refGRCh38Ensembl_1-1) [***c***](#cite_ref-refGRCh38Ensembl_1-2) [GRCh38: Ensembl release 89: ENSG00000065559](http://May2017.archive.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000065559) – [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: ENSMUSG00000033352](http://May2017.archive.ensembl.org/Mus_musculus/Gene/Summary?db=core;g=ENSMUSG00000033352) – [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=6416). *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=26398). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-pmid7716521_5-0)** Lin A, Minden A, Martinetto H, Claret FX, Lange-Carter C, Mercurio F, et al. (April 1995). "Identification of a dual specificity kinase that activates the Jun kinases and p38-Mpk2". *Science*. **268** (5208): 286–90. [Bibcode](/source/Bibcode_(identifier)):[1995Sci...268..286L](https://ui.adsabs.harvard.edu/abs/1995Sci...268..286L). [doi](/source/Doi_(identifier)):[10.1126/science.7716521](https://doi.org/10.1126%2Fscience.7716521). [PMID](/source/PMID_(identifier)) [7716521](https://pubmed.ncbi.nlm.nih.gov/7716521).

1. **[^](#cite_ref-6)** ["P45985 | SWISS-MODEL Repository"](https://swissmodel.expasy.org/repository/uniprot/P45985).

1. **[^](#cite_ref-7)** ["MKK4 (human)"](https://www.phosphosite.org/proteinAction.action?id=659&showAllSites=true). *www.phosphosite.org*. Retrieved 2020-10-28.

1. **[^](#cite_ref-8)** Nishina H, Vaz C, Billia P, Nghiem M, Sasaki T, De la Pompa JL, et al. (February 1999). "Defective liver formation and liver cell apoptosis in mice lacking the stress signaling kinase SEK1/MKK4". *Development*. **126** (3): 505–16. [doi](/source/Doi_(identifier)):[10.1242/dev.126.3.505](https://doi.org/10.1242%2Fdev.126.3.505). [PMID](/source/PMID_(identifier)) [9876179](https://pubmed.ncbi.nlm.nih.gov/9876179).

1. **[^](#cite_ref-9)** Ganiatsas S, Kwee L, Fujiwara Y, Perkins A, Ikeda T, Labow MA, Zon LI (June 1998). ["SEK1 deficiency reveals mitogen-activated protein kinase cascade crossregulation and leads to abnormal hepatogenesis"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC22670). *Proceedings of the National Academy of Sciences of the United States of America*. **95** (12): 6881–6. [Bibcode](/source/Bibcode_(identifier)):[1998PNAS...95.6881G](https://ui.adsabs.harvard.edu/abs/1998PNAS...95.6881G). [doi](/source/Doi_(identifier)):[10.1073/pnas.95.12.6881](https://doi.org/10.1073%2Fpnas.95.12.6881). [PMC](/source/PMC_(identifier)) [22670](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC22670). [PMID](/source/PMID_(identifier)) [9618507](https://pubmed.ncbi.nlm.nih.gov/9618507).

1. **[^](#cite_ref-10)** Nishina H, Bachmann M, Oliveira-dos-Santos AJ, Kozieradzki I, Fischer KD, Odermatt B, et al. (September 1997). ["Impaired CD28-mediated interleukin 2 production and proliferation in stress kinase SAPK/ERK1 kinase (SEK1)/mitogen-activated protein kinase kinase 4 (MKK4)-deficient T lymphocytes"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2199046). *The Journal of Experimental Medicine*. **186** (6): 941–53. [doi](/source/Doi_(identifier)):[10.1084/jem.186.6.941](https://doi.org/10.1084%2Fjem.186.6.941). [PMC](/source/PMC_(identifier)) [2199046](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2199046). [PMID](/source/PMID_(identifier)) [9294148](https://pubmed.ncbi.nlm.nih.gov/9294148).

1. **[^](#cite_ref-11)** Swat W, Fujikawa K, Ganiatsas S, Yang D, Xavier RJ, Harris NL, et al. (May 1998). ["SEK1/MKK4 is required for maintenance of a normal peripheral lymphoid compartment but not for lymphocyte development"](https://doi.org/10.1016%2Fs1074-7613%2800%2980567-1). *Immunity*. **8** (5): 625–34. [doi](/source/Doi_(identifier)):[10.1016/s1074-7613(00)80567-1](https://doi.org/10.1016%2Fs1074-7613%2800%2980567-1). [PMID](/source/PMID_(identifier)) [9620683](https://pubmed.ncbi.nlm.nih.gov/9620683).

1. **[^](#cite_ref-12)** ["MAP2K4 - My Cancer Genome"](https://www.mycancergenome.org/content/gene/map2k4/). *www.mycancergenome.org*. Retrieved 2020-12-26.

1. **[^](#cite_ref-pmid9808624_13-0)** Xia Y, Wu Z, Su B, Murray B, Karin M (November 1998). ["JNKK1 organizes a MAP kinase module through specific and sequential interactions with upstream and downstream components mediated by its amino-terminal extension"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC317229). *Genes & Development*. **12** (21): 3369–81. [doi](/source/Doi_(identifier)):[10.1101/gad.12.21.3369](https://doi.org/10.1101%2Fgad.12.21.3369). [PMC](/source/PMC_(identifier)) [317229](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC317229). [PMID](/source/PMID_(identifier)) [9808624](https://pubmed.ncbi.nlm.nih.gov/9808624).

1. **[^](#cite_ref-pmid9006895_14-0)** Marti A, Luo Z, Cunningham C, Ohta Y, Hartwig J, Stossel TP, et al. (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"](https://doi.org/10.1074%2Fjbc.272.5.2620). *The Journal of Biological Chemistry*. **272** (5): 2620–8. [doi](/source/Doi_(identifier)):[10.1074/jbc.272.5.2620](https://doi.org/10.1074%2Fjbc.272.5.2620). [PMID](/source/PMID_(identifier)) [9006895](https://pubmed.ncbi.nlm.nih.gov/9006895).

1. **[^](#cite_ref-pmid12391307_15-0)** Lee CM, Onésime D, Reddy CD, Dhanasekaran N, Reddy EP (October 2002). ["JLP: A scaffolding protein that tethers JNK/p38MAPK signaling modules and transcription factors"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC137859). *Proceedings of the National Academy of Sciences of the United States of America*. **99** (22): 14189–94. [Bibcode](/source/Bibcode_(identifier)):[2002PNAS...9914189L](https://ui.adsabs.harvard.edu/abs/2002PNAS...9914189L). [doi](/source/Doi_(identifier)):[10.1073/pnas.232310199](https://doi.org/10.1073%2Fpnas.232310199). [PMC](/source/PMC_(identifier)) [137859](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC137859). [PMID](/source/PMID_(identifier)) [12391307](https://pubmed.ncbi.nlm.nih.gov/12391307).

1. ^ [***a***](#cite_ref-pmid11707464_16-0) [***b***](#cite_ref-pmid11707464_16-1) Park HS, Kim MS, Huh SH, Park J, Chung J, Kang SS, Choi EJ (January 2002). ["Akt (protein kinase B) negatively regulates SEK1 by means of protein phosphorylation"](https://doi.org/10.1074%2Fjbc.M110299200). *The Journal of Biological Chemistry*. **277** (4): 2573–8. [doi](/source/Doi_(identifier)):[10.1074/jbc.M110299200](https://doi.org/10.1074%2Fjbc.M110299200). [PMID](/source/PMID_(identifier)) [11707464](https://pubmed.ncbi.nlm.nih.gov/11707464).

1. **[^](#cite_ref-pmid11279118_17-0)** Chen Z, Cobb MH (May 2001). ["Regulation of stress-responsive mitogen-activated protein (MAP) kinase pathways by TAO2"](https://doi.org/10.1074%2Fjbc.M100681200). *The Journal of Biological Chemistry*. **276** (19): 16070–5. [doi](/source/Doi_(identifier)):[10.1074/jbc.M100681200](https://doi.org/10.1074%2Fjbc.M100681200). [PMID](/source/PMID_(identifier)) [11279118](https://pubmed.ncbi.nlm.nih.gov/11279118).

1. **[^](#cite_ref-pmid9207092_18-0)** Tournier C, Whitmarsh AJ, Cavanagh J, Barrett T, Davis RJ (July 1997). ["Mitogen-activated protein kinase kinase 7 is an activator of the c-Jun NH2-terminal kinase"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC23822). *Proceedings of the National Academy of Sciences of the United States of America*. **94** (14): 7337–42. [Bibcode](/source/Bibcode_(identifier)):[1997PNAS...94.7337T](https://ui.adsabs.harvard.edu/abs/1997PNAS...94.7337T). [doi](/source/Doi_(identifier)):[10.1073/pnas.94.14.7337](https://doi.org/10.1073%2Fpnas.94.14.7337). [PMC](/source/PMC_(identifier)) [23822](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC23822). [PMID](/source/PMID_(identifier)) [9207092](https://pubmed.ncbi.nlm.nih.gov/9207092).

1. **[^](#cite_ref-pmid10713157_19-0)** Cheng J, Yang J, Xia Y, Karin M, Su B (April 2000). ["Synergistic interaction of MEK kinase 2, c-Jun N-terminal kinase (JNK) kinase 2, and JNK1 results in efficient and specific JNK1 activation"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC85399). *Molecular and Cellular Biology*. **20** (7): 2334–42. [doi](/source/Doi_(identifier)):[10.1128/MCB.20.7.2334-2342.2000](https://doi.org/10.1128%2FMCB.20.7.2334-2342.2000). [PMC](/source/PMC_(identifier)) [85399](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC85399). [PMID](/source/PMID_(identifier)) [10713157](https://pubmed.ncbi.nlm.nih.gov/10713157).

1. **[^](#cite_ref-pmid10523642_20-0)** Ito M, Yoshioka K, Akechi M, Yamashita S, Takamatsu N, Sugiyama K, et al. (November 1999). ["JSAP1, a novel jun N-terminal protein kinase (JNK)-binding protein that functions as a Scaffold factor in the JNK signaling pathway"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC84763). *Molecular and Cellular Biology*. **19** (11): 7539–48. [doi](/source/Doi_(identifier)):[10.1128/mcb.19.11.7539](https://doi.org/10.1128%2Fmcb.19.11.7539). [PMC](/source/PMC_(identifier)) [84763](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC84763). [PMID](/source/PMID_(identifier)) [10523642](https://pubmed.ncbi.nlm.nih.gov/10523642).

1. **[^](#cite_ref-pmid12189133_21-0)** Matsuura H, Nishitoh H, Takeda K, Matsuzawa A, Amagasa T, Ito M, et al. (October 2002). ["Phosphorylation-dependent scaffolding role of JSAP1/JIP3 in the ASK1-JNK signaling pathway. A new mode of regulation of the MAP kinase cascade"](https://doi.org/10.1074%2Fjbc.M202004200). *The Journal of Biological Chemistry*. **277** (43): 40703–9. [doi](/source/Doi_(identifier)):[10.1074/jbc.M202004200](https://doi.org/10.1074%2Fjbc.M202004200). [hdl](/source/Hdl_(identifier)):[2297/2692](https://hdl.handle.net/2297%2F2692). [PMID](/source/PMID_(identifier)) [12189133](https://pubmed.ncbi.nlm.nih.gov/12189133).

1. **[^](#cite_ref-22)** Ahn YH, Kurie JM (October 2009). ["MKK4/SEK1 is negatively regulated through a feedback loop involving the E3 ubiquitin ligase itch"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2785572). *The Journal of Biological Chemistry*. **284** (43): 29399–29404. [doi](/source/Doi_(identifier)):[10.1074/jbc.M109.044958](https://doi.org/10.1074%2Fjbc.M109.044958). [PMC](/source/PMC_(identifier)) [2785572](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2785572). [PMID](/source/PMID_(identifier)) [19737936](https://pubmed.ncbi.nlm.nih.gov/19737936).

## Further reading

- Lin, A (2006). "The JNK Signaling Pathway (Molecular Biology Intelligence Unit)". *Landes Bioscience*. **1**: 1–97. [ISBN](/source/ISBN_(identifier)) [978-1587061202](https://en.wikipedia.org/wiki/Special:BookSources/978-1587061202).

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)

[Portal](https://en.wikipedia.org/wiki/Wikipedia:Contents/Portals):
- [Biology](https://en.wikipedia.org/wiki/Portal:Biology)

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Adapted from the Wikipedia article [MAP2K4](https://en.wikipedia.org/wiki/MAP2K4) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/MAP2K4?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.