MAP3K10

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2RF0

Identifiers

Aliases

MAP3K10, MEKK10, MLK2, MST, mitogen-activated protein kinase kinase kinase 10

External IDs

MGI: 1346879 HomoloGene: 1834 GeneCards: MAP3K10

Gene ontology
Molecular function	• transferase activity • protein kinase activity • nucleotide binding • protein homodimerization activity • transcription corepressor activity • JUN kinase kinase kinase activity • kinase activity • protein serine/threonine kinase activity • bHLH transcription factor binding • ATP binding • MAP kinase kinase kinase activity
Cellular component	• cytoplasm • intracellular
Biological process	• activation of JUN kinase activity • phosphorylation • activation of MAPKK activity • positive regulation of JUN kinase activity • cell death • positive regulation of JNK cascade • negative regulation of sequence-specific DNA binding transcription factor activity • protein phosphorylation • JNK cascade • peptidyl-serine phosphorylation • positive regulation of apoptotic process • protein autophosphorylation • smoothened signaling pathway • peptidyl-threonine phosphorylation • negative regulation of transcription, DNA-templated • signal transduction • apoptotic process • activation of JNKK activity • MAPK cascade
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


4294


269881

Ensembl


ENSG00000130758


ENSMUSG00000040390

UniProt


Q02779


Q66L42

RefSeq (mRNA)


NM_002446


NM_001081292 NM_001290528

RefSeq (protein)


NP_002437.2


NP_001277457.1

Location (UCSC)

Chr 19: 40.19 – 40.22 Mb

Chr 7: 27.66 – 27.67 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Mitogen-activated protein kinase kinase kinase 10 is an enzyme that in humans is encoded by the MAP3K10 gene.^[3]^[4]^[5]

Function

The protein encoded by this gene is a member of the serine/threonine kinase family. This kinase has been shown to activate MAPK8/JNK and MKK4/SEK1, and this kinase itself can be phoshorylated, and thus activated by JNK kinases. This kinase functions preferentially on the JNK signaling pathway, and is reported to be involved in nerve growth factor (NGF) induced neuronal apoptosis.^[5]

Interactions

MAP3K10 has been shown to interact with:

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Dorow DS, Devereux L, Tu GF, Price G, Nicholl JK, Sutherland GR, Simpson RJ (February 1996). "Complete nucleotide sequence, expression, and chromosomal localisation of human mixed-lineage kinase 2". Eur J Biochem. 234 (2): 492–500. doi:10.1111/j.1432-1033.1995.492_b.x. PMID 8536694.
↑ Katoh M, Hirai M, Sugimura T, Terada M (May 1995). "Cloning and characterization of MST, a novel (putative) serine/threonine kinase with SH3 domain". Oncogene. 10 (7): 1447–51. PMID 7731697.
1 2 "Entrez Gene: MAP3K10 mitogen-activated protein kinase kinase kinase 10".
1 2 Nagata Ki, Puls A, Futter C, Aspenstrom P, Schaefer E, Nakata T, Hirokawa N, Hall A (January 1998). "The MAP kinase kinase kinase MLK2 co-localizes with activated JNK along microtubules and associates with kinesin superfamily motor KIF3". EMBO J. 17 (1): 149–58. doi:10.1093/emboj/17.1.149. PMC 1170366. PMID 9427749.
↑ Liu YF, Dorow D, Marshall J (June 2000). "Activation of MLK2-mediated signaling cascades by polyglutamine-expanded huntingtin". J. Biol. Chem. 275 (25): 19035–40. doi:10.1074/jbc.C000180200. PMID 10801775.
1 2 Yasuda J, Whitmarsh AJ, Cavanagh J, Sharma M, Davis RJ (October 1999). "The JIP group of mitogen-activated protein kinase scaffold proteins". Mol. Cell. Biol. 19 (10): 7245–54. doi:10.1128/mcb.19.10.7245. PMC 84717. PMID 10490659.
↑ Marcora E, Gowan K, Lee JE (August 2003). "Stimulation of NeuroD activity by huntingtin and huntingtin-associated proteins HAP1 and MLK2". Proc. Natl. Acad. Sci. U.S.A. 100 (16): 9578–83. doi:10.1073/pnas.1133382100. PMC 170960. PMID 12881483.

Gallo KA, Mark MR, Scadden DT, Wang Z, Gu Q, Godowski PJ (1994). "Identification and characterization of SPRK, a novel src-homology 3 domain-containing proline-rich kinase with serine/threonine kinase activity". J. Biol. Chem. 269 (21): 15092–100. PMID 8195146.
Dorow DS, Devereux L, Dietzsch E, De Kretser T (1993). "Identification of a new family of human epithelial protein kinases containing two leucine/isoleucine-zipper domains". Eur. J. Biochem. 213 (2): 701–10. doi:10.1111/j.1432-1033.1993.tb17810.x. PMID 8477742.
Hirai Si, Katoh M, Terada M, Kyriakis JM, Zon LI, Rana A, Avruch J, Ohno S (1997). "MST/MLK2, a member of the mixed lineage kinase family, directly phosphorylates and activates SEK1, an activator of c-Jun N-terminal kinase/stress-activated protein kinase". J. Biol. Chem. 272 (24): 15167–73. doi:10.1074/jbc.272.24.15167. PMID 9182538.
Hirai Si, Noda K, Moriguchi T, Nishida E, Yamashita A, Deyama T, Fukuyama K, Ohno S (1998). "Differential activation of two JNK activators, MKK7 and SEK1, by MKN28-derived nonreceptor serine/threonine kinase/mixed lineage kinase 2". J. Biol. Chem. 273 (13): 7406–12. doi:10.1074/jbc.273.13.7406. PMID 9516438.
Rasmussen RK, Ji H, Eddes JS, Moritz RL, Reid GE, Simpson RJ, Dorow DS (1998). "Two-dimensional electrophoretic analysis of mixed lineage kinase 2 N-terminal domain binding proteins". Electrophoresis. 19 (5): 809–17. doi:10.1002/elps.1150190535. PMID 9629920.
Rasmussen RK, Rusak J, Price G, Robinson PJ, Simpson RJ, Dorow DS (1998). "Mixed-lineage kinase 2-SH3 domain binds dynamin and greatly enhances activation of GTPase by phospholipid". Biochem. J. 335 (Pt 1): 119–24. doi:10.1042/bj3350119. PMC 1219759. PMID 9742220.
Liu YF, Dorow D, Marshall J (2000). "Activation of MLK2-mediated signaling cascades by polyglutamine-expanded huntingtin". J. Biol. Chem. 275 (25): 19035–40. doi:10.1074/jbc.C000180200. PMID 10801775.
Hartley JL, Temple GF, Brasch MA (2001). "DNA Cloning Using In Vitro Site-Specific Recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
Savinainen A, Garcia EP, Dorow D, Marshall J, Liu YF (2001). "Kainate receptor activation induces mixed lineage kinase-mediated cellular signaling cascades via post-synaptic density protein 95". J. Biol. Chem. 276 (14): 11382–6. doi:10.1074/jbc.M100190200. PMID 11152698.
Xu Z, Maroney AC, Dobrzanski P, Kukekov NV, Greene LA (2001). "The MLK Family Mediates c-Jun N-Terminal Kinase Activation in Neuronal Apoptosis". Mol. Cell. Biol. 21 (14): 4713–24. doi:10.1128/MCB.21.14.4713-4724.2001. PMC 87148. PMID 11416147.
Poy MN, Yang Y, Rezaei K, Fernström MA, Lee AD, Kido Y, Erickson SK, Najjar SM (2002). "CEACAM1 regulates insulin clearance in liver". Nat. Genet. 30 (3): 270–6. doi:10.1038/ng840. PMID 11850617.
Akbarzadeh S, Ji H, Frecklington D, Marmy-Conus N, Mok YF, Bowes L, Devereux L, Linsenmeyer M, Simpson RJ, Dorow DS (2002). "Mixed lineage kinase 2 interacts with clathrin and influences clathrin-coated vesicle trafficking". J. Biol. Chem. 277 (39): 36280–7. doi:10.1074/jbc.M204626200. PMID 12105200.
Figueroa C, Tarras S, Taylor J, Vojtek AB (2004). "Akt2 negatively regulates assembly of the POSH-MLK-JNK signaling complex". J. Biol. Chem. 278 (48): 47922–7. doi:10.1074/jbc.M307357200. PMID 14504284.
Eckey M, Tenbaum SP, Muñoz A, Baniahmad A (2004). "Mixed lineage kinase 2 enhances trans-repression of Alien and nuclear receptors". Mol. Cell. Endocrinol. 213 (1): 71–8. doi:10.1016/j.mce.2003.10.035. PMID 15062575.
Jaffe AB, Hall A, Schmidt A (2005). "Association of CNK1 with Rho guanine nucleotide exchange factors controls signaling specificity downstream of Rho". Curr. Biol. 15 (5): 405–12. doi:10.1016/j.cub.2004.12.082. PMID 15753034.
Kollers S, Musilova P, Rubes J, Rocha D (2007). "Comparative mapping reveals multiple rearrangements between pig chromosome 6 and human 19q13". Anim. Genet. 37 (6): 595–6. doi:10.1111/j.1365-2052.2006.01516.x. PMID 17121608.

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 Mammalian target of rapamycin EIF-2 kinases PKR HRI EIF2AK3 EIF2AK4 Wee1 WEE1

Pyruvate dehydrogenase kinase (EC 2.7.11.2)	PDK1 PDK2 PDK3

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 A kinase Aurora B kinase

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 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 P70S6 kinase 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

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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MAP3K10

Function

Interactions

References

Further reading