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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.
22-NOV-2017, entry version 181.
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 ENZYME
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, ENZYME
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;
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, ENZYME 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 ENZYME 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: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME 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:
P24522:GADD45A; NbExp=2; IntAct=EBI-448135, EBI-448167;
Q5S007:LRRK2; NbExp=4; IntAct=EBI-448135, EBI-5323863;
Q9Y6R4:MAP3K4; NbExp=2; IntAct=EBI-448135, EBI-448104;
-!- 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]
UniGene; Hs.463978; -.
UniGene; Hs.49329; -.
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; -.
ProteinModelPortal; P52564; -.
SMR; P52564; -.
BioGrid; 111594; 27.
DIP; DIP-31346N; -.
ELM; P52564; -.
IntAct; P52564; 12.
MINT; MINT-3019559; -.
STRING; 9606.ENSP00000468348; -.
BindingDB; P52564; -.
ChEMBL; CHEMBL2171; -.
GuidetoPHARMACOLOGY; 2067; -.
iPTMnet; P52564; -.
PhosphoSitePlus; P52564; -.
BioMuta; MAP2K6; -.
DMDM; 1709088; -.
EPD; P52564; -.
MaxQB; P52564; -.
PaxDb; P52564; -.
PeptideAtlas; P52564; -.
PRIDE; P52564; -.
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; CAB007744; -.
HPA; HPA031134; -.
MIM; 601254; gene.
neXtProt; NX_P52564; -.
OpenTargets; ENSG00000108984; -.
PharmGKB; PA30591; -.
eggNOG; KOG0984; Eukaryota.
eggNOG; ENOG410XT3F; LUCA.
GeneTree; ENSGT00760000119199; -.
HOGENOM; HOG000234206; -.
HOVERGEN; HBG108518; -.
InParanoid; P52564; -.
KO; K04433; -.
OMA; WGTPFEQ; -.
OrthoDB; EOG091G0A9H; -.
PhylomeDB; P52564; -.
BRENDA; 2.7.12.2; 2681.
Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-375170; CDO in myogenesis.
Reactome; R-HSA-446652; Interleukin-1 family signaling.
Reactome; R-HSA-450302; activated TAK1 mediates p38 MAPK activation.
Reactome; R-HSA-5210891; Uptake and function of anthrax toxins.
Reactome; R-HSA-6811555; PI5P Regulates TP53 Acetylation.
SignaLink; P52564; -.
SIGNOR; P52564; -.
ChiTaRS; MAP2K6; human.
EvolutionaryTrace; P52564; -.
GeneWiki; MAP2K6; -.
GenomeRNAi; 5608; -.
PMAP-CutDB; P52564; -.
PRO; PR:P52564; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000108984; -.
CleanEx; HS_MAP2K6; -.
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; TAS:Reactome.
GO; GO:0005634; C:nucleus; 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; TAS:Reactome.
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; TAS:Reactome.
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: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:0035897; P:proteolysis in other organism; TAS:Reactome.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
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.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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; Complete proteome; 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 Dual specificity mitogen-activated
protein kinase kinase 6.
/FTId=PRO_0000086386.
DOMAIN 53 314 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 59 67 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 4 19 D domain. {ECO:0000250}.
REGION 311 334 DVD domain.
ACT_SITE 179 179 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 82 82 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 14 15 Cleavage; by anthrax lethal factor.
MOD_RES 207 207 O-acetylserine; by Yersinia yopJ;
alternate. {ECO:0000269|PubMed:16728640}.
MOD_RES 207 207 Phosphoserine; by MAP3K; alternate.
{ECO:0000269|PubMed:16728640}.
MOD_RES 211 211 O-acetylthreonine; by Yersinia yopJ;
alternate. {ECO:0000269|PubMed:16728640}.
MOD_RES 211 211 Phosphothreonine; by MAP3K; alternate.
{ECO:0000269|PubMed:16728640}.
VAR_SEQ 1 56 Missing (in isoform 2).
{ECO:0000303|PubMed:8621675}.
/FTId=VSP_004882.
MUTAGEN 207 207 S->A: Inactivation.
MUTAGEN 207 207 S->E: Constitutive activation according
to PubMed:8622669, but not to
PubMed:8621675.
MUTAGEN 211 211 T->A: Inactivation.
MUTAGEN 211 211 T->E: Constitutive activation according
to PubMed:8622669, but not to
PubMed:8621675.
CONFLICT 125 125 V -> M (in Ref. 3; AAB03705/AAB03708).
{ECO:0000305}.
HELIX 50 52 {ECO:0000244|PDB:3FME}.
STRAND 53 61 {ECO:0000244|PDB:3FME}.
STRAND 63 72 {ECO:0000244|PDB:3FME}.
TURN 73 76 {ECO:0000244|PDB:3FME}.
STRAND 77 84 {ECO:0000244|PDB:3FME}.
HELIX 90 104 {ECO:0000244|PDB:3FME}.
TURN 110 112 {ECO:0000244|PDB:3VN9}.
STRAND 115 120 {ECO:0000244|PDB:3FME}.
STRAND 122 130 {ECO:0000244|PDB:3FME}.
STRAND 133 135 {ECO:0000244|PDB:3FME}.
HELIX 136 145 {ECO:0000244|PDB:3FME}.
HELIX 152 172 {ECO:0000244|PDB:3FME}.
HELIX 182 184 {ECO:0000244|PDB:3FME}.
STRAND 185 187 {ECO:0000244|PDB:3ENM}.
STRAND 193 195 {ECO:0000244|PDB:3FME}.
HELIX 201 203 {ECO:0000244|PDB:3ENM}.
HELIX 207 212 {ECO:0000244|PDB:3VN9}.
HELIX 222 225 {ECO:0000244|PDB:3FME}.
HELIX 236 252 {ECO:0000244|PDB:3FME}.
HELIX 263 272 {ECO:0000244|PDB:3FME}.
TURN 280 282 {ECO:0000244|PDB:3FME}.
HELIX 285 294 {ECO:0000244|PDB:3FME}.
HELIX 299 301 {ECO:0000244|PDB:3FME}.
HELIX 305 308 {ECO:0000244|PDB:3FME}.
HELIX 312 319 {ECO:0000244|PDB:3FME}.
HELIX 324 332 {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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