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Dual specificity mitogen-activated protein kinase kinase 6 (MAP kinase kinase 6) (MAPKK 6) (EC 2.7.12.2) (MAPK/ERK kinase 6) (MEK 6) (Stress-activated protein kinase kinase 3) (SAPK kinase 3) (SAPKK-3) (SAPKK3)

 MP2K6_HUMAN             Reviewed;         334 AA.
P52564;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
12-AUG-2020, entry version 200.
RecName: Full=Dual specificity mitogen-activated protein kinase kinase 6;
Short=MAP kinase kinase 6;
Short=MAPKK 6;
EC=2.7.12.2;
AltName: Full=MAPK/ERK kinase 6;
Short=MEK 6;
AltName: Full=Stress-activated protein kinase kinase 3;
Short=SAPK kinase 3;
Short=SAPKK-3;
Short=SAPKK3;
Name=MAP2K6; Synonyms=MEK6, MKK6, PRKMK6, SKK3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS, AND FUNCTION.
TISSUE=Skeletal muscle;
PubMed=8622669; DOI=10.1128/mcb.16.3.1247;
Raingeaud J., Whitmarsh A.J., Barrett T., Derijard B., Davis R.J.;
"MKK3- and MKK6-regulated gene expression is mediated by the p38 mitogen-
activated protein kinase signal transduction pathway.";
Mol. Cell. Biol. 16:1247-1255(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND ACTIVITY REGULATION.
TISSUE=T-cell;
PubMed=8626699; DOI=10.1074/jbc.271.19.11427;
Stein B., Brady H., Yang M.X., Young D.B., Barbosa M.S.;
"Cloning and characterization of MEK6, a novel member of the mitogen-
activated protein kinase kinase cascade.";
J. Biol. Chem. 271:11427-11433(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
MUTAGENESIS.
TISSUE=Placenta;
PubMed=8621675; DOI=10.1074/jbc.271.6.2886;
Han J., Lee J.-D., Jiang Y., Li Z., Feng L., Ulevitch R.J.;
"Characterization of the structure and function of a novel MAP kinase
kinase (MKK6).";
J. Biol. Chem. 271:2886-2891(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION, ACTIVITY
REGULATION, AND FUNCTION.
PubMed=8663074; DOI=10.1074/jbc.271.23.13675;
Moriguchi T., Kuroyanagi N., Yamaguchi K., Gotoh Y., Irie K., Kano T.,
Shirakabe K., Muro Y., Shibuya H., Matsumoto K., Nishida E., Hagiwara M.;
"A novel kinase cascade mediated by mitogen-activated protein kinase kinase
6 and MKK3.";
J. Biol. Chem. 271:13675-13679(1996).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8861944; DOI=10.1002/j.1460-2075.1996.tb00790.x;
Cuenda A., Alonso G., Morrice N., Jones M., Meier R., Cohen P.,
Nebreda A.R.;
"Purification and cDNA cloning of SAPKK3, the major activator of RK/p38 in
stress- and cytokine-stimulated monocytes and epithelial cells.";
EMBO J. 15:4156-4164(1996).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Urinary bladder;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION IN ACTIVATION OF MAPK13.
PubMed=9218798; DOI=10.1093/emboj/16.12.3563;
Goedert M., Cuenda A., Craxton M., Jakes R., Cohen P.;
"Activation of the novel stress-activated protein kinase SAPK4 by cytokines
and cellular stresses is mediated by SKK3 (MKK6); comparison of its
substrate specificity with that of other SAP kinases.";
EMBO J. 16:3563-3571(1997).
[8]
SUBCELLULAR LOCATION.
PubMed=9768359; DOI=10.1016/s0960-9822(98)70442-7;
Ben-Levy R., Hooper S., Wilson R., Paterson H.F., Marshall C.J.;
"Nuclear export of the stress-activated protein kinase p38 mediated by its
substrate MAPKAP kinase-2.";
Curr. Biol. 8:1049-1057(1998).
[9]
PHOSPHORYLATION BY MAP3K4.
PubMed=9841871; DOI=10.1042/bj3360599;
Chan-Hui P.Y., Weaver R.;
"Human mitogen-activated protein kinase kinase kinase mediates the stress-
induced activation of mitogen-activated protein kinase cascades.";
Biochem. J. 336:599-609(1998).
[10]
PHOSPHORYLATION BY MAP3K2/MEKK2 AND MAP3K3/MEK3.
PubMed=10347227; DOI=10.1074/jbc.274.23.16604;
Deacon K., Blank J.L.;
"MEK kinase 3 directly activates MKK6 and MKK7, specific activators of the
p38 and c-Jun NH2-terminal kinases.";
J. Biol. Chem. 274:16604-16610(1999).
[11]
INTERACTION WITH TAOK2, AND PHOSPHORYLATION BY TAOK2.
PubMed=10497253; DOI=10.1074/jbc.274.40.28803;
Chen Z., Hutchison M., Cobb M.H.;
"Isolation of the protein kinase TAO2 and identification of its mitogen-
activated protein kinase/extracellular signal-regulated kinase kinase
binding domain.";
J. Biol. Chem. 274:28803-28807(1999).
[12]
PHOSPHORYLATION BY MAP3K7/TAK1.
PubMed=10094049; DOI=10.1038/18465;
Ninomiya-Tsuji J., Kishimoto K., Hiyama A., Inoue J., Cao Z., Matsumoto K.;
"The kinase TAK1 can activate the NIK-I kappaB as well as the MAP kinase
cascade in the IL-1 signalling pathway.";
Nature 398:252-256(1999).
[13]
CLEAVAGE BY ANTHRAX LETHAL FACTOR.
PubMed=11104681; DOI=10.1042/bj3520739;
Vitale G., Bernardi L., Napolitani G., Mock M., Montecucco C.;
"Susceptibility of mitogen-activated protein kinase kinase family members
to proteolysis by anthrax lethal factor.";
Biochem. J. 352:739-745(2000).
[14]
FUNCTION.
PubMed=10961885;
Visconti R., Gadina M., Chiariello M., Chen E.H., Stancato L.F.,
Gutkind J.S., O'Shea J.J.;
"Importance of the MKK6/p38 pathway for interleukin-12-induced STAT4 serine
phosphorylation and transcriptional activity.";
Blood 96:1844-1852(2000).
[15]
FUNCTION.
PubMed=11727828; DOI=10.1515/bc.2001.178;
Bode J.G., Ludwig S., Freitas C.A., Schaper F., Ruhl M., Melmed S.,
Heinrich P.C., Haussinger D.;
"The MKK6/p38 mitogen-activated protein kinase pathway is capable of
inducing SOCS3 gene expression and inhibits IL-6-induced transcription.";
Biol. Chem. 382:1447-1453(2001).
[16]
PHOSPHORYLATION BY MAP3K5/ASK1.
PubMed=11689443; DOI=10.1093/emboj/20.21.6028;
Morita K., Saitoh M., Tobiume K., Matsuura H., Enomoto S., Nishitoh H.,
Ichijo H.;
"Negative feedback regulation of ASK1 by protein phosphatase 5 (PP5) in
response to oxidative stress.";
EMBO J. 20:6028-6036(2001).
[17]
PHOSPHORYLATION BY TAOK2.
PubMed=11279118; DOI=10.1074/jbc.m100681200;
Chen Z., Cobb M.H.;
"Regulation of stress-responsive mitogen-activated protein (MAP) kinase
pathways by TAO2.";
J. Biol. Chem. 276:16070-16075(2001).
[18]
PHOSPHORYLATION BY MAP3K7/TAK1.
PubMed=11460167; DOI=10.1038/35085597;
Wang C., Deng L., Hong M., Akkaraju G.R., Inoue J., Chen Z.J.;
"TAK1 is a ubiquitin-dependent kinase of MKK and IKK.";
Nature 412:346-351(2001).
[19]
INTERACTION WITH EIF2AK2, AND PHOSPHORYLATION.
PubMed=15229216; DOI=10.1074/jbc.m406554200;
Silva A.M., Whitmore M., Xu Z., Jiang Z., Li X., Williams B.R.;
"Protein kinase R (PKR) interacts with and activates mitogen-activated
protein kinase kinase 6 (MKK6) in response to double-stranded RNA
stimulation.";
J. Biol. Chem. 279:37670-37676(2004).
[20]
INTERACTION WITH DCTN1, AND MICROTUBULE-BINDING.
PubMed=15375157; DOI=10.1074/jbc.c400333200;
Cheung P.Y., Zhang Y., Long J., Lin S., Zhang M., Jiang Y., Wu Z.;
"p150(Glued), Dynein, and microtubules are specifically required for
activation of MKK3/6 and p38 MAPKs.";
J. Biol. Chem. 279:45308-45311(2004).
[21]
FUNCTION IN PHOSPHORYLATION OF PAK6.
PubMed=15550393; DOI=10.1074/jbc.m406701200;
Kaur R., Liu X., Gjoerup O., Zhang A., Yuan X., Balk S.P., Schneider M.C.,
Lu M.L.;
"Activation of p21-activated kinase 6 by MAP kinase kinase 6 and p38 MAP
kinase.";
J. Biol. Chem. 280:3323-3330(2005).
[22]
DOMAIN.
PubMed=15866172; DOI=10.1016/j.molcel.2005.04.001;
Takekawa M., Tatebayashi K., Saito H.;
"Conserved docking site is essential for activation of mammalian MAP kinase
kinases by specific MAP kinase kinase kinases.";
Mol. Cell 18:295-306(2005).
[23]
ACETYLATION AT SER-207 AND THR-211, PHOSPHORYLATION AT SER-207 AND THR-211,
INACTIVATION BY YERSINIA YOPJ, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16728640; DOI=10.1126/science.1126867;
Mukherjee S., Keitany G., Li Y., Wang Y., Ball H.L., Goldsmith E.J.,
Orth K.;
"Yersinia YopJ acetylates and inhibits kinase activation by blocking
phosphorylation.";
Science 312:1211-1214(2006).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[25]
PHOSPHORYLATION BY MAP3K5/ASK1, ACTIVITY REGULATION, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=20364819; DOI=10.1021/bi100010j;
Sturchler E., Feurstein D., McDonald P., Duckett D.;
"Mechanism of oxidative stress-induced ASK1-catalyzed MKK6
phosphorylation.";
Biochemistry 49:4094-4102(2010).
[26]
FUNCTION.
PubMed=20869211; DOI=10.1016/j.jdermsci.2010.08.006;
Kim M.Y., Choi T.Y., Kim J.H., Lee J.H., Kim J.G., Sohn K.C., Yoon K.S.,
Kim C.D., Lee J.H., Yoon T.J.;
"MKK6 increases the melanocyte dendricity through the regulation of Rho
family GTPases.";
J. Dermatol. Sci. 60:114-119(2010).
[27]
REVIEW ON ACTIVITY REGULATION, AND REVIEW ON FUNCTION.
PubMed=9779990; DOI=10.1038/sj.onc.1202251;
Dhanasekaran N., Premkumar Reddy E.;
"Signaling by dual specificity kinases.";
Oncogene 17:1447-1455(1998).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[30]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 45-332 OF MUTANT ASP-207 AND
ASP-211, AND SUBUNIT.
PubMed=19141286; DOI=10.1016/j.str.2008.11.007;
Min X., Akella R., He H., Humphreys J.M., Tsutakawa S.E., Lee S.J.,
Tainer J.A., Cobb M.H., Goldsmith E.J.;
"The structure of the MAP2K MEK6 reveals an autoinhibitory dimer.";
Structure 17:96-104(2009).
[31]
X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) OF 47-334.
Structural genomics consortium (SGC);
"Crystal structure of human mitogen-activated protein kinase kinase 6
(mek6) activated mutant (s207d, t211d).";
Submitted (JUL-2011) to the PDB data bank.
-!- FUNCTION: Dual specificity protein kinase which acts as an essential
component of the MAP kinase signal transduction pathway. With
MAP3K3/MKK3, catalyzes the concomitant phosphorylation of a threonine
and a tyrosine residue in the MAP kinases p38 MAPK11, MAPK12, MAPK13
and MAPK14 and plays an important role in the regulation of cellular
responses to cytokines and all kinds of stresses. Especially,
MAP2K3/MKK3 and MAP2K6/MKK6 are both essential for the activation of
MAPK11 and MAPK13 induced by environmental stress, whereas MAP2K6/MKK6
is the major MAPK11 activator in response to TNF. MAP2K6/MKK6 also
phosphorylates and activates PAK6. The p38 MAP kinase signal
transduction pathway leads to direct activation of transcription
factors. Nuclear targets of p38 MAP kinase include the transcription
factors ATF2 and ELK1. Within the p38 MAPK signal transduction pathway,
MAP3K6/MKK6 mediates phosphorylation of STAT4 through MAPK14
activation, and is therefore required for STAT4 activation and STAT4-
regulated gene expression in response to IL-12 stimulation. The pathway
is also crucial for IL-6-induced SOCS3 expression and down-regulation
of IL-6-mediated gene induction; and for IFNG-dependent gene
transcription. Has a role in osteoclast differentiation through NF-
kappa-B transactivation by TNFSF11, and in endochondral ossification
and since SOX9 is another likely downstream target of the p38 MAPK
pathway. MAP2K6/MKK6 mediates apoptotic cell death in thymocytes. Acts
also as a regulator for melanocytes dendricity, through the modulation
of Rho family GTPases. {ECO:0000269|PubMed:10961885,
ECO:0000269|PubMed:11727828, ECO:0000269|PubMed:15550393,
ECO:0000269|PubMed:20869211, ECO:0000269|PubMed:8622669,
ECO:0000269|PubMed:8626699, ECO:0000269|PubMed:8663074,
ECO:0000269|PubMed:9218798}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.2;
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.12.2;
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2;
-!- ACTIVITY REGULATION: Activated by dual phosphorylation on Ser-207 and
Thr-211 in response to a variety of cellular stresses, including UV
radiation, osmotic shock, hypoxia, inflammatory cytokines, interferon
gamma (IFNG), and less often by growth factors. MAP2K6/MKK6 is
activated by the majority of M3Ks, such as MAP3K5/ASK1, MAP3K1/MEKK1,
MAP3K2/MEKK2, MAP3K3/MEKK3, MAP3K4/MEKK4, MAP3K7/TAK1, MAP3K11/MLK3 and
MAP3K17/TAOK2. {ECO:0000269|PubMed:20364819,
ECO:0000269|PubMed:8626699, ECO:0000269|PubMed:8663074}.
-!- SUBUNIT: Dimer. Interacts with Yersinia yopJ. Interacts (via its D
domain) with its substrates MAPK11, MAPK12, MAPK13 and MAPK14 (By
similarity). Interacts (via its DVD domain) with MAP3Ks activators like
MAP3K5/ASK1, MAP3K1/MEKK1, MAP3K2/MEKK2, MAP3K3/MEKK3, MAP3K4/MEKK4,
MAP3K7/TAK1, MAP3K11/MLK3 and MAP3K17/TAOK2 (By similarity). Interacts
with DCTN1. Interacts with EIF2AK2/PKR. {ECO:0000250,
ECO:0000269|PubMed:10497253, ECO:0000269|PubMed:15229216,
ECO:0000269|PubMed:15375157, ECO:0000269|PubMed:19141286}.
-!- INTERACTION:
P52564; P24522: GADD45A; NbExp=2; IntAct=EBI-448135, EBI-448167;
P52564; Q5S007: LRRK2; NbExp=4; IntAct=EBI-448135, EBI-5323863;
P52564; Q9Y6R4: MAP3K4; NbExp=2; IntAct=EBI-448135, EBI-448104;
P52564; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-448135, EBI-79165;
P52564-1; P52564-1: MAP2K6; NbExp=3; IntAct=EBI-15750978, EBI-15750978;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9768359}. Cytoplasm
{ECO:0000269|PubMed:9768359}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:9768359}. Note=Binds to microtubules.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=MKK6b;
IsoId=P52564-1; Sequence=Displayed;
Name=2; Synonyms=MKK6;
IsoId=P52564-2; Sequence=VSP_004882;
-!- TISSUE SPECIFICITY: Isoform 2 is only expressed in skeletal muscle.
Isoform 1 is expressed in skeletal muscle, heart, and in lesser extent
in liver or pancreas. {ECO:0000269|PubMed:8621675}.
-!- INDUCTION: Strongly activated by UV, anisomycin, and osmotic shock but
not by phorbol esters, NGF or EGF.
-!- DOMAIN: The DVD domain (residues 311-334) contains a conserved docking
site and is found in the mammalian MAP kinase kinases (MAP2Ks). The DVD
sites bind to their specific upstream MAP kinase kinase kinases
(MAP3Ks) and are essential for activation.
{ECO:0000269|PubMed:15866172}.
-!- DOMAIN: The D domain (residues 4-19) contains a conserved docking site
and is required for the binding to MAPK substrates. {ECO:0000250}.
-!- PTM: Weakly autophosphorylated. Phosphorylated at Ser-207 and Thr-211
by the majority of M3Ks, such as MAP3K5/ASK1, MAP3K1/MEKK1,
MAP3K2/MEKK2, MAP3K3/MEKK3, MAP3K4/MEKK4, MAP3K7/TAK1, MAP3K11/MLK3 and
MAP3K17/TAOK2. {ECO:0000269|PubMed:16728640}.
-!- PTM: Acetylation of Ser-207 and Thr-211 by Yersinia yopJ prevents
phosphorylation and activation, thus blocking the MAPK signaling
pathway. {ECO:0000269|PubMed:16728640}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
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EMBL; U39657; AAC50389.1; -; mRNA.
EMBL; U39656; AAC50388.1; -; mRNA.
EMBL; U49732; AAB05035.1; -; mRNA.
EMBL; U39065; AAB03705.1; -; mRNA.
EMBL; U39064; AAB03708.1; -; mRNA.
EMBL; D87905; BAA13496.1; -; mRNA.
EMBL; X96757; CAA65532.1; -; mRNA.
EMBL; BC012009; AAH12009.1; -; mRNA.
CCDS; CCDS11686.1; -. [P52564-1]
CCDS; CCDS82194.1; -. [P52564-2]
PIR; S71631; S71631.
RefSeq; NP_002749.2; NM_002758.3. [P52564-1]
PDB; 2Y8O; X-ray; 1.95 A; B=4-17.
PDB; 3ENM; X-ray; 2.35 A; A/B/C/D=45-332.
PDB; 3FME; X-ray; 2.26 A; A=47-334.
PDB; 3VN9; X-ray; 2.60 A; A=1-334.
PDB; 5ETF; X-ray; 2.40 A; B=4-17.
PDBsum; 2Y8O; -.
PDBsum; 3ENM; -.
PDBsum; 3FME; -.
PDBsum; 3VN9; -.
PDBsum; 5ETF; -.
SMR; P52564; -.
BioGRID; 111594; 45.
DIP; DIP-31346N; -.
ELM; P52564; -.
IntAct; P52564; 13.
MINT; P52564; -.
STRING; 9606.ENSP00000468348; -.
BindingDB; P52564; -.
ChEMBL; CHEMBL2171; -.
DrugBank; DB12010; Fostamatinib.
DrugCentral; P52564; -.
GuidetoPHARMACOLOGY; 2067; -.
iPTMnet; P52564; -.
MetOSite; P52564; -.
PhosphoSitePlus; P52564; -.
BioMuta; MAP2K6; -.
DMDM; 1709088; -.
CPTAC; CPTAC-820; -.
CPTAC; CPTAC-821; -.
EPD; P52564; -.
jPOST; P52564; -.
MassIVE; P52564; -.
MaxQB; P52564; -.
PaxDb; P52564; -.
PeptideAtlas; P52564; -.
PRIDE; P52564; -.
ProteomicsDB; 56487; -. [P52564-1]
ProteomicsDB; 56488; -. [P52564-2]
Antibodypedia; 3570; 838 antibodies.
DNASU; 5608; -.
Ensembl; ENST00000589647; ENSP00000467213; ENSG00000108984. [P52564-2]
Ensembl; ENST00000590474; ENSP00000468348; ENSG00000108984. [P52564-1]
Ensembl; ENST00000613873; ENSP00000477701; ENSG00000108984. [P52564-2]
GeneID; 5608; -.
KEGG; hsa:5608; -.
UCSC; uc002jij.4; human. [P52564-1]
CTD; 5608; -.
DisGeNET; 5608; -.
EuPathDB; HostDB:ENSG00000108984.13; -.
GeneCards; MAP2K6; -.
HGNC; HGNC:6846; MAP2K6.
HPA; ENSG00000108984; Tissue enhanced (blood, skeletal muscle).
MIM; 601254; gene.
neXtProt; NX_P52564; -.
OpenTargets; ENSG00000108984; -.
PharmGKB; PA30591; -.
eggNOG; KOG0984; Eukaryota.
GeneTree; ENSGT00940000157836; -.
HOGENOM; CLU_000288_63_23_1; -.
InParanoid; P52564; -.
KO; K04433; -.
OMA; WGTPFEQ; -.
PhylomeDB; P52564; -.
BRENDA; 2.7.12.2; 2681.
PathwayCommons; P52564; -.
Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-450302; activated TAK1 mediates p38 MAPK activation.
Reactome; R-HSA-5210891; Uptake and function of anthrax toxins. [P52564-1]
Reactome; R-HSA-525793; Myogenesis.
Reactome; R-HSA-6811555; PI5P Regulates TP53 Acetylation.
Reactome; R-HSA-9020702; Interleukin-1 signaling.
SignaLink; P52564; -.
SIGNOR; P52564; -.
BioGRID-ORCS; 5608; 4 hits in 902 CRISPR screens.
ChiTaRS; MAP2K6; human.
EvolutionaryTrace; P52564; -.
GeneWiki; MAP2K6; -.
GenomeRNAi; 5608; -.
Pharos; P52564; Tchem.
PRO; PR:P52564; -.
Proteomes; UP000005640; Chromosome 17.
RNAct; P52564; protein.
Bgee; ENSG00000108984; Expressed in quadriceps femoris and 218 other tissues.
ExpressionAtlas; P52564; baseline and differential.
Genevisible; P52564; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004708; F:MAP kinase kinase activity; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
GO; GO:0000187; P:activation of MAPK activity; IDA:UniProtKB.
GO; GO:0032147; P:activation of protein kinase activity; IBA:GO_Central.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0060048; P:cardiac muscle contraction; IEA:Ensembl.
GO; GO:0007050; P:cell cycle arrest; TAS:ProtInc.
GO; GO:0072709; P:cellular response to sorbitol; IEA:Ensembl.
GO; GO:0006975; P:DNA damage induced protein phosphorylation; TAS:ProtInc.
GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
GO; GO:0070423; P:nucleotide-binding oligomerization domain containing signaling pathway; TAS:Reactome.
GO; GO:0022602; P:ovulation cycle process; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IEA:Ensembl.
GO; GO:0032308; P:positive regulation of prostaglandin secretion; IEA:Ensembl.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0023014; P:signal transduction by protein phosphorylation; IBA:GO_Central.
GO; GO:0031098; P:stress-activated protein kinase signaling cascade; IBA:GO_Central.
DisProt; DP01342; -.
IDEAL; IID00455; -.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis; ATP-binding;
Cytoplasm; Cytoskeleton; Kinase; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
Stress response; Transcription; Transcription regulation; Transferase;
Tyrosine-protein kinase.
CHAIN 1..334
/note="Dual specificity mitogen-activated protein kinase
kinase 6"
/id="PRO_0000086386"
DOMAIN 53..314
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 59..67
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
REGION 4..19
/note="D domain"
/evidence="ECO:0000250"
REGION 311..334
/note="DVD domain"
ACT_SITE 179
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10027"
BINDING 82
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SITE 14..15
/note="Cleavage; by anthrax lethal factor"
MOD_RES 207
/note="O-acetylserine; by Yersinia yopJ; alternate"
/evidence="ECO:0000269|PubMed:16728640"
MOD_RES 207
/note="Phosphoserine; by MAP3K; alternate"
/evidence="ECO:0000269|PubMed:16728640"
MOD_RES 211
/note="O-acetylthreonine; by Yersinia yopJ; alternate"
/evidence="ECO:0000269|PubMed:16728640"
MOD_RES 211
/note="Phosphothreonine; by MAP3K; alternate"
/evidence="ECO:0000269|PubMed:16728640"
VAR_SEQ 1..56
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:8621675"
/id="VSP_004882"
MUTAGEN 207
/note="S->A: Inactivation."
MUTAGEN 207
/note="S->E: Constitutive activation according to
PubMed:8622669, but not to PubMed:8621675."
MUTAGEN 211
/note="T->A: Inactivation."
MUTAGEN 211
/note="T->E: Constitutive activation according to
PubMed:8622669, but not to PubMed:8621675."
CONFLICT 125
/note="V -> M (in Ref. 3; AAB03705/AAB03708)"
/evidence="ECO:0000305"
HELIX 50..52
/evidence="ECO:0000244|PDB:3FME"
STRAND 53..61
/evidence="ECO:0000244|PDB:3FME"
STRAND 63..72
/evidence="ECO:0000244|PDB:3FME"
TURN 73..76
/evidence="ECO:0000244|PDB:3FME"
STRAND 77..84
/evidence="ECO:0000244|PDB:3FME"
HELIX 90..104
/evidence="ECO:0000244|PDB:3FME"
TURN 110..112
/evidence="ECO:0000244|PDB:3VN9"
STRAND 115..120
/evidence="ECO:0000244|PDB:3FME"
STRAND 122..130
/evidence="ECO:0000244|PDB:3FME"
STRAND 133..135
/evidence="ECO:0000244|PDB:3FME"
HELIX 136..145
/evidence="ECO:0000244|PDB:3FME"
HELIX 152..172
/evidence="ECO:0000244|PDB:3FME"
HELIX 182..184
/evidence="ECO:0000244|PDB:3FME"
STRAND 185..187
/evidence="ECO:0000244|PDB:3ENM"
STRAND 193..195
/evidence="ECO:0000244|PDB:3FME"
HELIX 201..203
/evidence="ECO:0000244|PDB:3ENM"
HELIX 207..212
/evidence="ECO:0000244|PDB:3VN9"
HELIX 222..225
/evidence="ECO:0000244|PDB:3FME"
HELIX 236..252
/evidence="ECO:0000244|PDB:3FME"
HELIX 263..272
/evidence="ECO:0000244|PDB:3FME"
TURN 280..282
/evidence="ECO:0000244|PDB:3FME"
HELIX 285..294
/evidence="ECO:0000244|PDB:3FME"
HELIX 299..301
/evidence="ECO:0000244|PDB:3FME"
HELIX 305..308
/evidence="ECO:0000244|PDB:3FME"
HELIX 312..319
/evidence="ECO:0000244|PDB:3FME"
HELIX 324..332
/evidence="ECO:0000244|PDB:3FME"
SEQUENCE 334 AA; 37492 MW; 4ECA8014522216AF CRC64;
MSQSKGKKRN PGLKIPKEAF EQPQTSSTPP RDLDSKACIS IGNQNFEVKA DDLEPIMELG
RGAYGVVEKM RHVPSGQIMA VKRIRATVNS QEQKRLLMDL DISMRTVDCP FTVTFYGALF
REGDVWICME LMDTSLDKFY KQVIDKGQTI PEDILGKIAV SIVKALEHLH SKLSVIHRDV
KPSNVLINAL GQVKMCDFGI SGYLVDSVAK TIDAGCKPYM APERINPELN QKGYSVKSDI
WSLGITMIEL AILRFPYDSW GTPFQQLKQV VEEPSPQLPA DKFSAEFVDF TSQCLKKNSK
ERPTYPELMQ HPFFTLHESK GTDVASFVKL ILGD


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Pathways :
WP1493: Carbon assimilation C4 pathway
WP1703: Streptomycin biosynthesis
WP253: Glycolysis
WP1567: Glycolysis and Gluconeogenesis
WP1619: Amino sugar and nucleotide sugar metabolism
WP1701: Starch and sucrose metabolism
WP1653: Galactose metabolism
WP1946: Cori Cycle
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP1844: MAP kinase cascade
WP32: Translation Factors
WP1681: Pantothenate and CoA biosynthesis
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP2199: Seed Development
WP2292: Chemokine signaling pathway
WP1663: Homologous recombination
WP1531: Vitamin D synthesis
WP1673: Naphthalene and anthracene degradation
WP2272: Pathogenic Escherichia coli infection
WP1888: Post-translational protein modification
WP35: G Protein Signaling Pathways
WP1678: Nucleotide excision repair
WP1689: Porphyrin and chlorophyll metabolism
WP2324: AGE/RAGE pathway
WP1644: DNA replication

Related Genes :
[MAP2K6 MEK6 MKK6 PRKMK6 SKK3] Dual specificity mitogen-activated protein kinase kinase 6 (MAP kinase kinase 6) (MAPKK 6) (EC 2.7.12.2) (MAPK/ERK kinase 6) (MEK 6) (Stress-activated protein kinase kinase 3) (SAPK kinase 3) (SAPKK-3) (SAPKK3)
[Map2k1 Mek1 Prkmk1] Dual specificity mitogen-activated protein kinase kinase 1 (MAP kinase kinase 1) (MAPKK 1) (EC 2.7.12.2) (ERK activator kinase 1) (MAPK/ERK kinase 1) (MEK 1)
[Map2k2 Mek2 Mkk2 Prkmk2] Dual specificity mitogen-activated protein kinase kinase 2 (MAP kinase kinase 2) (MAPKK 2) (EC 2.7.12.2) (ERK activator kinase 2) (MAPK/ERK kinase 2) (MEK 2)
[Mapk12 Sapk3] Mitogen-activated protein kinase 12 (MAP kinase 12) (MAPK 12) (EC 2.7.11.24) (Extracellular signal-regulated kinase 6) (ERK-6) (Mitogen-activated protein kinase p38 gamma) (MAP kinase p38 gamma) (Stress-activated protein kinase 3)
[Map2k5 Mek5 Mkk5 Prkmk5] Dual specificity mitogen-activated protein kinase kinase 5 (MAP kinase kinase 5) (MAPKK 5) (EC 2.7.12.2) (MAPK/ERK kinase 5) (MEK 5)
[MAPK12 ERK6 SAPK3] Mitogen-activated protein kinase 12 (MAP kinase 12) (MAPK 12) (EC 2.7.11.24) (Extracellular signal-regulated kinase 6) (ERK-6) (Mitogen-activated protein kinase p38 gamma) (MAP kinase p38 gamma) (Stress-activated protein kinase 3)
[MAP2K1 MEK1 PRKMK1] Dual specificity mitogen-activated protein kinase kinase 1 (MAP kinase kinase 1) (MAPKK 1) (MKK1) (EC 2.7.12.2) (ERK activator kinase 1) (MAPK/ERK kinase 1) (MEK 1)
[Map2k1 Mek1 Prkmk1] Dual specificity mitogen-activated protein kinase kinase 1 (MAP kinase kinase 1) (MAPKK 1) (EC 2.7.12.2) (ERK activator kinase 1) (MAPK/ERK kinase 1) (MEK 1)
[MAP2K1 MEK1 PRKMK1] Dual specificity mitogen-activated protein kinase kinase 1 (MAP kinase kinase 1) (MAPKK 1) (EC 2.7.12.2) (ERK activator kinase 1) (MAPK/ERK kinase 1) (MEK 1)
[MAP2K2 MEK2 MKK2 PRKMK2] Dual specificity mitogen-activated protein kinase kinase 2 (MAP kinase kinase 2) (MAPKK 2) (EC 2.7.12.2) (ERK activator kinase 2) (MAPK/ERK kinase 2) (MEK 2)
[Mapk12 Sapk3] Mitogen-activated protein kinase 12 (MAP kinase 12) (MAPK 12) (EC 2.7.11.24) (Extracellular signal-regulated kinase 6) (ERK-6) (Mitogen-activated protein kinase p38 gamma) (MAP kinase p38 gamma) (Stress-activated protein kinase 3)
[MAP2K1 MEK1 PRKMK1] Dual specificity mitogen-activated protein kinase kinase 1 (MAP kinase kinase 1) (MAPKK 1) (EC 2.7.12.2) (ERK activator kinase 1) (MAPK/ERK kinase 1) (MEK 1)
[Map2k2 Mek2 Mkk2 Prkmk2] Dual specificity mitogen-activated protein kinase kinase 2 (MAP kinase kinase 2) (MAPKK 2) (EC 2.7.12.2) (ERK activator kinase 2) (MAPK/ERK kinase 2) (MEK 2)
[Map2k5 Mek5 Mkk5 Prkmk5] Dual specificity mitogen-activated protein kinase kinase 5 (MAP kinase kinase 5) (MAPKK 5) (EC 2.7.12.2) (MAPK/ERK kinase 5) (MEK 5)
[MAP2K1 MEK1 PRKMK1] Dual specificity mitogen-activated protein kinase kinase 1 (MAP kinase kinase 1) (MAPKK 1) (EC 2.7.12.2) (ERK activator kinase 1) (MAPK/ERK kinase 1) (MEK 1)
[MAP2K5 MEK5 MKK5 PRKMK5] Dual specificity mitogen-activated protein kinase kinase 5 (MAP kinase kinase 5) (MAPKK 5) (EC 2.7.12.2) (MAPK/ERK kinase 5) (MEK 5)
[mekA MEK1 DDB_G0269152] Dual specificity mitogen-activated protein kinase kinase 1 (MAP kinase kinase 1) (MAPKK 1) (EC 2.7.12.2) (ERK activator kinase 1) (MAPK/ERK kinase 1) (DdMEK1) (MEK1) (MAPK/ERK kinase A) (MEKA)
[Mapk1 Erk2 Mapk Prkm1] Mitogen-activated protein kinase 1 (MAP kinase 1) (MAPK 1) (EC 2.7.11.24) (ERT1) (Extracellular signal-regulated kinase 2) (ERK-2) (MAP kinase isoform p42) (p42-MAPK) (Mitogen-activated protein kinase 2) (MAP kinase 2) (MAPK 2)
[MAP3K5 ASK1 MAPKKK5 MEKK5] Mitogen-activated protein kinase kinase kinase 5 (EC 2.7.11.25) (Apoptosis signal-regulating kinase 1) (ASK-1) (MAPK/ERK kinase kinase 5) (MEK kinase 5) (MEKK 5)
[MAPK10 JNK3 JNK3A PRKM10 SAPK1B] Mitogen-activated protein kinase 10 (MAP kinase 10) (MAPK 10) (EC 2.7.11.24) (MAP kinase p49 3F12) (Stress-activated protein kinase 1b) (SAPK1b) (Stress-activated protein kinase JNK3) (c-Jun N-terminal kinase 3)
[MAPK1 ERK2 PRKM1 PRKM2] Mitogen-activated protein kinase 1 (MAP kinase 1) (MAPK 1) (EC 2.7.11.24) (ERT1) (Extracellular signal-regulated kinase 2) (ERK-2) (MAP kinase isoform p42) (p42-MAPK) (Mitogen-activated protein kinase 2) (MAP kinase 2) (MAPK 2)
[Mapk7 Bmk1 Erk5] Mitogen-activated protein kinase 7 (MAP kinase 7) (MAPK 7) (EC 2.7.11.24) (Big MAP kinase 1) (BMK-1) (Extracellular signal-regulated kinase 5) (ERK-5)
[MAPK14 CSBP CSBP1 CSBP2 CSPB1 MXI2 SAPK2A] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (Cytokine suppressive anti-inflammatory drug-binding protein) (CSAID-binding protein) (CSBP) (MAP kinase MXI2) (MAX-interacting protein 2) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha) (Stress-activated protein kinase 2a) (SAPK2a)
[MAPK3 ERK1 PRKM3] Mitogen-activated protein kinase 3 (MAP kinase 3) (MAPK 3) (EC 2.7.11.24) (ERT2) (Extracellular signal-regulated kinase 1) (ERK-1) (Insulin-stimulated MAP2 kinase) (MAP kinase isoform p44) (p44-MAPK) (Microtubule-associated protein 2 kinase) (p44-ERK1)
[Rps6ka3 Mapkapk1b Rps6ka-rs1 Rsk2] Ribosomal protein S6 kinase alpha-3 (S6K-alpha-3) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 3) (p90-RSK 3) (p90RSK3) (MAP kinase-activated protein kinase 1b) (MAPK-activated protein kinase 1b) (MAPKAP kinase 1b) (MAPKAPK-1b) (Ribosomal S6 kinase 2) (RSK-2) (pp90RSK2)
[Mapk14 Crk1 Csbp1 Csbp2] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (CRK1) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha)
[Map3k1 Mekk Mekk1] Mitogen-activated protein kinase kinase kinase 1 (EC 2.7.11.25) (MAPK/ERK kinase kinase 1) (MEK kinase 1) (MEKK 1)
[MAP2K2 MEK2] Dual specificity mitogen-activated protein kinase kinase 2 (MAP kinase kinase 2) (MAPKK 2) (EC 2.7.12.2) (ERK activator kinase 2) (MAPK/ERK kinase 2) (MEK 2)
[MAPK8 JNK1 PRKM8 SAPK1 SAPK1C] Mitogen-activated protein kinase 8 (MAP kinase 8) (MAPK 8) (EC 2.7.11.24) (JNK-46) (Stress-activated protein kinase 1c) (SAPK1c) (Stress-activated protein kinase JNK1) (c-Jun N-terminal kinase 1)
[Rps6ka2 Mapkapk1c Rsk3] Ribosomal protein S6 kinase alpha-2 (S6K-alpha-2) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 2) (p90-RSK 2) (p90RSK2) (MAP kinase-activated protein kinase 1c) (MAPK-activated protein kinase 1c) (MAPKAP kinase 1c) (MAPKAPK-1c) (Protein-tyrosine kinase Mpk-9) (Ribosomal S6 kinase 3) (RSK-3) (pp90RSK3)

Bibliography :