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Dual specificity mitogen-activated protein kinase kinase 4 (MAP kinase kinase 4) (MAPKK 4) (EC 2.7.12.2) (C-JUN N-terminal kinase kinase 1) (JNK kinase 1) (JNKK 1) (JNK-activating kinase 1) (MAPK/ERK kinase 4) (MEK 4) (SAPK/ERK kinase 1) (SEK1)

 MP2K4_MOUSE             Reviewed;         397 AA.
P47809;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
12-SEP-2018, entry version 158.
RecName: Full=Dual specificity mitogen-activated protein kinase kinase 4;
Short=MAP kinase kinase 4;
Short=MAPKK 4;
EC=2.7.12.2;
AltName: Full=C-JUN N-terminal kinase kinase 1;
Short=JNK kinase 1;
Short=JNKK 1;
AltName: Full=JNK-activating kinase 1;
AltName: Full=MAPK/ERK kinase 4;
Short=MEK 4;
AltName: Full=SAPK/ERK kinase 1;
Short=SEK1;
Name=Map2k4; Synonyms=Jnkk1, Mek4, Mkk4, Prkmk4, Sek1, Serk1, Skk1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF LYS-129.
TISSUE=Embryo;
PubMed=7997269; DOI=10.1038/372794a0;
Sanchez I., Hughes R.T., Mayer B.J., Yee K., Woodgett J.R., Avruch J.,
Kyriakis J.M., Zon L.I.;
"Role of SAPK/ERK kinase-1 in the stress-activated pathway regulating
transcription factor c-Jun.";
Nature 372:794-798(1994).
[2]
SEQUENCE REVISION.
Zon L.I.;
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION.
PubMed=9620683; DOI=10.1016/S1074-7613(00)80567-1;
Swat W., Fujikawa K., Ganiatsas S., Yang D., Xavier R.J., Harris N.L.,
Davidson L., Ferrini R., Davis R.J., Labow M.A., Flavell R.A.,
Zon L.I., Alt F.W.;
"SEK1/MKK4 is required for maintenance of a normal peripheral lymphoid
compartment but not for lymphocyte development.";
Immunity 8:625-634(1998).
[4]
ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND FUNCTION OF THE MKK/JNK
PATHWAY.
PubMed=9891090; DOI=10.1128/MCB.19.2.1569;
Tournier C., Whitmarsh A.J., Cavanagh J., Barrett T., Davis R.J.;
"The MKK7 gene encodes a group of c-Jun NH2-terminal kinase kinases.";
Mol. Cell. Biol. 19:1569-1581(1999).
[5]
TISSUE SPECIFICITY.
PubMed=10095085; DOI=10.1016/S0169-328X(99)00035-2;
Lee J.K., Hwang W.S., Lee Y.D., Han P.L.;
"Dynamic expression of SEK1 suggests multiple roles of the gene during
embryogenesis and in adult brain of mice.";
Brain Res. Mol. Brain Res. 66:133-140(1999).
[6]
FUNCTION.
PubMed=11390361; DOI=10.1101/gad.888501;
Tournier C., Dong C., Turner T.K., Jones S.N., Flavell R.A.,
Davis R.J.;
"MKK7 is an essential component of the JNK signal transduction pathway
activated by proinflammatory cytokines.";
Genes Dev. 15:1419-1426(2001).
[7]
PHOSPHORYLATION, AND INTERACTION WITH MAP3K1/MEKK1.
PubMed=12401521; DOI=10.1016/S0898-6568(02)00056-6;
Tu Z., Mooney S.M., Lee F.S.;
"A subdomain of MEKK1 that is critical for binding to MKK4.";
Cell. Signal. 15:65-77(2003).
[8]
FUNCTION.
PubMed=12624093; DOI=10.1074/jbc.M213182200;
Kishimoto H., Nakagawa K., Watanabe T., Kitagawa D., Momose H.,
Seo J., Nishitai G., Shimizu N., Ohata S., Tanemura S., Asaka S.,
Goto T., Fukushi H., Yoshida H., Suzuki A., Sasaki T., Wada T.,
Penninger J.M., Nishina H., Katada T.;
"Different properties of SEK1 and MKK7 in dual phosphorylation of
stress-induced activated protein kinase SAPK/JNK in embryonic stem
cells.";
J. Biol. Chem. 278:16595-16601(2003).
[9]
DISRUPTION PHENOTYPE.
PubMed=17875933; DOI=10.1128/MCB.00226-07;
Wang X., Nadarajah B., Robinson A.C., McColl B.W., Jin J.W.,
Dajas-Bailador F., Boot-Handford R.P., Tournier C.;
"Targeted deletion of the mitogen-activated protein kinase kinase 4
gene in the nervous system causes severe brain developmental defects
and premature death.";
Mol. Cell. Biol. 27:7935-7946(2007).
[10]
DISRUPTION PHENOTYPE.
PubMed=19265040; DOI=10.1161/CIRCRESAHA.108.188292;
Liu W., Zi M., Jin J., Prehar S., Oceandy D., Kimura T.E., Lei M.,
Neyses L., Weston A.H., Cartwright E.J., Wang X.;
"Cardiac-specific deletion of mkk4 reveals its role in pathological
hypertrophic remodeling but not in physiological cardiac growth.";
Circ. Res. 104:905-914(2009).
[11]
REVIEW ON ACTIVITY REGULATION.
PubMed=17496909; DOI=10.1038/sj.onc.1210392;
Raman M., Chen W., Cobb M.H.;
"Differential regulation and properties of MAPKs.";
Oncogene 26:3100-3112(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-255 AND THR-259,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[13]
REVIEW ON FUNCTION.
PubMed=20801953; DOI=10.1093/jb/mvq098;
Asaoka Y., Nishina H.;
"Diverse physiological functions of MKK4 and MKK7 during early
embryogenesis.";
J. Biochem. 148:393-401(2010).
[14]
REVIEW ON REGULATION, AND REVIEW ON FUNCTION.
PubMed=21333379; DOI=10.1016/j.ejcb.2010.11.008;
Haeusgen W., Herdegen T., Waetzig V.;
"The bottleneck of JNK signaling: molecular and functional
characteristics of MKK4 and MKK7.";
Eur. J. Cell Biol. 90:536-544(2011).
[15]
INTERACTION WITH SPAG9.
PubMed=12391307; DOI=10.1073/pnas.232310199;
Lee C.M., Onesime D., Reddy C.D., Dhanasekaran N., Reddy E.P.;
"JLP: a scaffolding protein that tethers JNK/p38MAPK signaling modules
and transcription factors.";
Proc. Natl. Acad. Sci. U.S.A. 99:14189-14194(2002).
[16]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-56, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Dual specificity protein kinase which acts as an
essential component of the MAP kinase signal transduction pathway.
Essential component of the stress-activated protein kinase/c-Jun
N-terminal kinase (SAP/JNK) signaling pathway. With MAP2K7/MKK7,
is the one of the only known kinase to directly activate the
stress-activated protein kinase/c-Jun N-terminal kinases
MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3. MAP2K4/MKK4 and
MAP2K7/MKK7 both activate the JNKs by phosphorylation, but they
differ in their preference for the phosphorylation site in the
Thr-Pro-Tyr motif. MAP2K4 shows preference for phosphorylation of
the Tyr residue and MAP2K7/MKK7 for the Thr residue. The
phosphorylation of the Thr residue by MAP2K7/MKK7 seems to be the
prerequisite for JNK activation at least in response to
proinflammatory cytokines, while other stimuli activate both
MAP2K4/MKK4 and MAP2K7/MKK7 which synergistically phosphorylate
JNKs. MAP2K4 is required for maintaining peripheral lymphoid
homeostasis. The MKK/JNK signaling pathway is also involved in
mitochondrial death signaling pathway, including the release
cytochrome c, leading to apoptosis. Whereas MAP2K7/MKK7
exclusively activates JNKs, MAP2K4/MKK4 additionally activates the
p38 MAPKs MAPK11, MAPK12, MAPK13 and MAPK14.
{ECO:0000269|PubMed:11390361, ECO:0000269|PubMed:12624093,
ECO:0000269|PubMed:7997269, ECO:0000269|PubMed:9620683,
ECO:0000269|PubMed:9891090}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ACTIVITY REGULATION: Activated in response to a variety of
cellular stresses, including UV and gamma-irradiation, heat shock,
hyperosmolarity, T-cell receptor stimulation, peroxide and
inflammatory cytokines. Also activated by developmental cues.
MAP2K4/MKK4 is activated by the majority of MKKKs, such as
MAP3K5/ASK1, MAP3K1/MEKK1, MAP3K7/TAK1, MAP3K10/MLK2,
MAP3K11/MLK3, MAP3K12/DLK and MAP3K13/LZK.
{ECO:0000269|PubMed:9891090}.
-!- SUBUNIT: Interacts with SPAG9. Interacts (via its D domain) with
its substrates MAPK8/JNK1, MAPK9/JNK2, MAPK10/JNK3, MAPK11 and
MAPK14 (By similarity). Interacts (via its DVD domain) with MAP3Ks
activators like MAP3K1/MEKK1 and MAP3K11/MLK3. Interacts with
ARRB1, ARRB2 and MAPK8IP3/JIP3 (By similarity). {ECO:0000250}.
-!- INTERACTION:
P53349:Map3k1; NbExp=2; IntAct=EBI-447934, EBI-447913;
Q9ESN9-2:Mapk8ip3; NbExp=3; IntAct=EBI-447934, EBI-9549291;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9891090}.
Nucleus {ECO:0000269|PubMed:9891090}.
-!- TISSUE SPECIFICITY: Strong expression is detected in most of the
central nervous system and in liver and thymus during early stages
of development. While expression in nervous system increases over
time, expression in fetal liver and thymus gradually decreases as
embryogenesis proceeds. High level of expression in the central
nervous system persists throughout postnatal development and
remained at a stable level in adult brain.
{ECO:0000269|PubMed:10095085}.
-!- DOMAIN: The DVD domain (residues 362-385) 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 (By
similarity). {ECO:0000250}.
-!- DOMAIN: The D domain (residues 35-50) contains a conserved docking
site and is required for the binding to MAPk substrates.
-!- PTM: Activated by phosphorylation on Ser-255 and Thr-259 by MAP
kinase kinase kinases (MAP3Ks). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Causes irregular alignment of Purkinje cells
in the cerebellum and delayed radial migration in the cortex
during brain development. The cardiac-specific deletion prevents
pathological cardiac hypertrophy. {ECO:0000269|PubMed:17875933,
ECO:0000269|PubMed:19265040}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U18310; AAB81554.1; -; mRNA.
CCDS; CCDS24844.1; -.
PIR; S52423; S52423.
RefSeq; NP_033183.1; NM_009157.5.
UniGene; Mm.412922; -.
ProteinModelPortal; P47809; -.
SMR; P47809; -.
BioGrid; 204952; 8.
CORUM; P47809; -.
DIP; DIP-869N; -.
IntAct; P47809; 5.
MINT; P47809; -.
STRING; 10090.ENSMUSP00000041282; -.
ChEMBL; CHEMBL2201; -.
iPTMnet; P47809; -.
PhosphoSitePlus; P47809; -.
EPD; P47809; -.
PaxDb; P47809; -.
PeptideAtlas; P47809; -.
PRIDE; P47809; -.
DNASU; 26398; -.
Ensembl; ENSMUST00000046963; ENSMUSP00000041282; ENSMUSG00000033352.
GeneID; 26398; -.
KEGG; mmu:26398; -.
UCSC; uc007jlb.1; mouse.
CTD; 6416; -.
MGI; MGI:1346869; Map2k4.
eggNOG; KOG0984; Eukaryota.
eggNOG; ENOG410XT3F; LUCA.
GeneTree; ENSGT00760000119199; -.
HOGENOM; HOG000234206; -.
HOVERGEN; HBG108518; -.
InParanoid; P47809; -.
KO; K04430; -.
OMA; VMKSNDC; -.
OrthoDB; EOG091G0A9H; -.
PhylomeDB; P47809; -.
TreeFam; TF350701; -.
BRENDA; 2.7.12.2; 3474.
Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
Reactome; R-MMU-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
PRO; PR:P47809; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000033352; Expressed in 312 organ(s), highest expression level in secondary oocyte.
CleanEx; MM_MAP2K4; -.
ExpressionAtlas; P47809; baseline and differential.
Genevisible; P47809; MM.
GO; GO:0030424; C:axon; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0032839; C:dendrite cytoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0043204; C:perikaryon; ISO:MGI.
GO; GO:0005524; F:ATP binding; ISO:MGI.
GO; GO:0008545; F:JUN kinase kinase activity; ISO:MGI.
GO; GO:0004708; F:MAP kinase kinase activity; ISO:MGI.
GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; ISO:MGI.
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:0007257; P:activation of JUN kinase activity; ISO:MGI.
GO; GO:0032147; P:activation of protein kinase activity; IBA:GO_Central.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; ISO:MGI.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0072709; P:cellular response to sorbitol; IEA:Ensembl.
GO; GO:0007254; P:JNK cascade; ISO:MGI.
GO; GO:0000165; P:MAPK cascade; IPI:MGI.
GO; GO:2000672; P:negative regulation of motor neuron apoptotic process; IMP:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
GO; GO:0045740; P:positive regulation of DNA replication; ISO:MGI.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; ISO:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
GO; GO:0034393; P:positive regulation of smooth muscle cell apoptotic process; IDA:BHF-UCL.
GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:0009611; P:response to wounding; IMP:MGI.
GO; GO:0031098; P:stress-activated protein kinase signaling cascade; IBA:GO_Central.
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;
Acetylation; Apoptosis; ATP-binding; Complete proteome; Cytoplasm;
Kinase; Methylation; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Stress response;
Transferase; Tyrosine-protein kinase.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P45985}.
CHAIN 2 397 Dual specificity mitogen-activated
protein kinase kinase 4.
/FTId=PRO_0000086382.
DOMAIN 100 366 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 106 114 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 35 50 D domain. {ECO:0000250}.
REGION 362 385 DVD domain. {ECO:0000250}.
COMPBIAS 5 17 Gly/Ser-rich.
ACT_SITE 227 227 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 129 129 ATP.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P45985}.
MOD_RES 56 56 Asymmetric dimethylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 56 56 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:P45985}.
MOD_RES 88 88 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 255 255 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 259 259 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MUTAGEN 129 129 K->R: Loss of ATP-binding.
{ECO:0000269|PubMed:7997269}.
SEQUENCE 397 AA; 44114 MW; B99C6688184E5B3D CRC64;
MAAPSPSGGG GSGGGGGTPG PIGPPASGHP AVSSMQGKRK ALKLNFANPP VKSTARFTLN
PNTTGVQNPH IERLRTHSIE SSGKLKISPE QHWDFTAEDL KDLGEIGRGA YGSVNKMVHK
PSGQIMAVKR IRSTVDEKEQ KQLLMDLDVV MRSSDCPYIV QFYGALFREG DCWICMELMS
TSFDKFYKYV YSVLDDVIPE EILGKITLAT VKALNHLKEN LKIIHRDIKP SNILLDRSGN
IKLCDFGISG QLVDSIAKTR DAGCRPYMAP ERIDPSASRQ GYDVRSDVWS LGITLYELAT
GRFPYPKWNS VFDQLTQVVK GDPPQLSNSE EREFSPSFIN FVNLCLTKDE SKRPKYKELL
KHPFILMYEE RTVEVACYVC KILDQMPATP SSPMYVD


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