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Dual specificity mitogen-activated protein kinase kinase 4 (MAP kinase kinase 4) (MAPKK 4) (EC 2.7.12.2) (JNK-activating kinase 1) (MAPK/ERK kinase 4) (MEK 4) (SAPK/ERK kinase 1) (SEK1) (Stress-activated protein kinase kinase 1) (SAPK kinase 1) (SAPKK-1) (SAPKK1) (c-Jun N-terminal kinase kinase 1) (JNKK)

 MP2K4_HUMAN             Reviewed;         399 AA.
P45985; B2R7N7; B3KYB2; D3DTS5; Q5U0B8; Q6FHX4; Q6P9H2; Q6PIE6;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
05-DEC-2018, entry version 190.
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=JNK-activating kinase 1;
AltName: Full=MAPK/ERK kinase 4;
Short=MEK 4;
AltName: Full=SAPK/ERK kinase 1;
Short=SEK1;
AltName: Full=Stress-activated protein kinase kinase 1;
Short=SAPK kinase 1;
Short=SAPKK-1;
Short=SAPKK1;
AltName: Full=c-Jun N-terminal kinase kinase 1;
Short=JNKK;
Name=MAP2K4; Synonyms=JNKK1, MEK4, MKK4, PRKMK4, SEK1, SERK1, SKK1;
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).
TISSUE=Brain;
PubMed=7839144; DOI=10.1126/science.7839144;
Derijard B., Raingeaud J., Barrett T., Wu I.-H., Han J.,
Ulevitch R.J., Davis R.J.;
"Independent human MAP-kinase signal transduction pathways defined by
MEK and MKK isoforms.";
Science 267:682-685(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
PubMed=7716521; DOI=10.1126/science.7716521;
Lin A., Minden A., Martinetto H., Claret F.-X., Lange-Carter C.,
Mercurio F., Johnson G.L., Karin M.;
"Identification of a dual specificity kinase that activates the Jun
kinases and p38-Mpk2.";
Science 268:286-290(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9622070;
Su G.H., Hilgers W., Shekher M.C., Tang D.J., Yeo C.J., Hruban R.H.,
Kern S.E.;
"Alterations in pancreatic, biliary, and breast carcinomas support
MKK4 as a genetically targeted tumor suppressor gene.";
Cancer Res. 58:2339-2342(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain, and Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ARG-16.
TISSUE=Brain, and Testis;
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).
[11]
PHOSPHORYLATION AT THR-261, ACTIVITY REGULATION, AND INTERACTION WITH
MAP3K11/MLK3.
PubMed=9003778;
Tibbles L.A., Ing Y.L., Kiefer F., Chan J., Iscove N., Woodgett J.R.,
Lassam N.J.;
"MLK-3 activates the SAPK/JNK and p38/RK pathways via SEK1 and
MKK3/6.";
EMBO J. 15:7026-7035(1996).
[12]
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).
[13]
INTERACTION WITH ARRB2.
PubMed=11090355; DOI=10.1126/science.290.5496.1574;
McDonald P.H., Chow C.W., Miller W.E., Laporte S.A., Field M.E.,
Lin F.-T., Davis R.J., Lefkowitz R.J.;
"Beta-arrestin 2: a receptor-regulated MAPK scaffold for the
activation of JNK3.";
Science 290:1574-1577(2000).
[14]
INTERACTION WITH MAPK8IP3/JIP3.
PubMed=12189133; DOI=10.1074/jbc.M202004200;
Matsuura H., Nishitoh H., Takeda K., Matsuzawa A., Amagasa T., Ito M.,
Yoshioka K., Ichijo H.;
"Phosphorylation-dependent scaffolding role of JSAP1/JIP3 in the ASK1-
JNK signaling pathway. A new mode of regulation of the MAP kinase
cascade.";
J. Biol. Chem. 277:40703-40709(2002).
[15]
DOMAIN, AND INTERACTION WITH MAPK8/JNK1; MAPK9/JNK2; MAPK10/JNK3;
MAPK11 AND MAPK14.
PubMed=12788955; DOI=10.1074/jbc.M304229200;
Ho D.T., Bardwell A.J., Abdollahi M., Bardwell L.;
"A docking site in MKK4 mediates high affinity binding to JNK MAPKs
and competes with similar docking sites in JNK substrates.";
J. Biol. Chem. 278:32662-32672(2003).
[16]
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).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND 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).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[19]
INTERACTION WITH ARRB1 AND ARRB2.
PubMed=19782076; DOI=10.1016/j.febslet.2009.09.035;
Li X., MacLeod R., Dunlop A.J., Edwards H.V., Advant N., Gibson L.C.,
Devine N.M., Brown K.M., Adams D.R., Houslay M.D., Baillie G.S.;
"A scanning peptide array approach uncovers association sites within
the JNK/beta arrestin signalling complex.";
FEBS Lett. 583:3310-3316(2009).
[20]
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).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[22]
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).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[24]
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).
[25]
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).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[27]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-58, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
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).
[28]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 80-399.
PubMed=20732303; DOI=10.1016/j.bbrc.2010.08.071;
Matsumoto T., Kinoshita T., Kirii Y., Yokota K., Hamada K., Tada T.;
"Crystal structures of MKK4 kinase domain reveal that substrate
peptide binds to an allosteric site and induces an auto-inhibition
state.";
Biochem. Biophys. Res. Commun. 400:369-373(2010).
[29]
VARIANTS [LARGE SCALE ANALYSIS] LEU-142; TRP-154; ILE-234; ASN-251 AND
THR-279.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- 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:7716521}.
-!- 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;
-!- 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:9003778}.
-!- SUBUNIT: Interacts with SPAG9 (By similarity). Interacts (via its
D domain) with its substrates MAPK8/JNK1, MAPK9/JNK2, MAPK10/JNK3,
MAPK11 and MAPK14. Interacts (via its DVD domain) with MAP3Ks
activators like MAP3K1/MEKK1 and MAP3K11/MLK3. Interacts with
ARRB1, ARRB2 and MAPK8IP3/JIP3. {ECO:0000250,
ECO:0000269|PubMed:11090355, ECO:0000269|PubMed:12189133,
ECO:0000269|PubMed:12788955, ECO:0000269|PubMed:19782076,
ECO:0000269|PubMed:9003778}.
-!- INTERACTION:
Q13233:MAP3K1; NbExp=3; IntAct=EBI-447868, EBI-49776;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P45985-1; Sequence=Displayed;
Name=2;
IsoId=P45985-2; Sequence=VSP_038838;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Abundant expression is seen in the skeletal
muscle. It is also widely expressed in other tissues.
-!- DOMAIN: The DVD domain (residues 364-387) 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.
-!- DOMAIN: The D domain (residues 34-52) contains a conserved docking
site and is required for the binding to MAPK substrates.
-!- PTM: Activated by phosphorylation on Ser-257 and Thr-261 by MAP
kinase kinase kinases (MAP3Ks). {ECO:0000269|PubMed:9003778}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/map2k4/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MAP2K4ID244ch17p12.html";
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EMBL; L36870; AAC41719.1; -; mRNA.
EMBL; U17743; AAC50127.1; -; mRNA.
EMBL; AF070090; AAC24130.1; -; Genomic_DNA.
EMBL; AF070080; AAC24130.1; JOINED; Genomic_DNA.
EMBL; AF070081; AAC24130.1; JOINED; Genomic_DNA.
EMBL; AF070082; AAC24130.1; JOINED; Genomic_DNA.
EMBL; AF070083; AAC24130.1; JOINED; Genomic_DNA.
EMBL; AF070084; AAC24130.1; JOINED; Genomic_DNA.
EMBL; AF070085; AAC24130.1; JOINED; Genomic_DNA.
EMBL; AF070086; AAC24130.1; JOINED; Genomic_DNA.
EMBL; AF070087; AAC24130.1; JOINED; Genomic_DNA.
EMBL; AF070088; AAC24130.1; JOINED; Genomic_DNA.
EMBL; AF070089; AAC24130.1; JOINED; Genomic_DNA.
EMBL; CR536564; CAG38801.1; -; mRNA.
EMBL; BT019676; AAV38482.1; -; mRNA.
EMBL; AK131544; BAG54774.1; -; mRNA.
EMBL; AK313053; BAG35884.1; -; mRNA.
EMBL; DQ015703; AAY22176.1; -; Genomic_DNA.
EMBL; AC005244; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC005410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471108; EAW89975.1; -; Genomic_DNA.
EMBL; CH471108; EAW89974.1; -; Genomic_DNA.
EMBL; CH471108; EAW89976.1; -; Genomic_DNA.
EMBL; BC036032; AAH36032.1; -; mRNA.
EMBL; BC060764; AAH60764.1; -; mRNA.
CCDS; CCDS11162.1; -. [P45985-1]
CCDS; CCDS62095.1; -. [P45985-2]
PIR; I38901; I38901.
RefSeq; NP_001268364.1; NM_001281435.1. [P45985-2]
RefSeq; NP_003001.1; NM_003010.3. [P45985-1]
UniGene; Hs.514681; -.
PDB; 3ALN; X-ray; 2.30 A; A/B/C=80-399.
PDB; 3ALO; X-ray; 2.60 A; A=80-399.
PDB; 3VUT; X-ray; 3.50 A; A/B=80-399.
PDBsum; 3ALN; -.
PDBsum; 3ALO; -.
PDBsum; 3VUT; -.
ProteinModelPortal; P45985; -.
SMR; P45985; -.
BioGrid; 112315; 43.
CORUM; P45985; -.
IntAct; P45985; 17.
MINT; P45985; -.
STRING; 9606.ENSP00000262445; -.
BindingDB; P45985; -.
ChEMBL; CHEMBL2897; -.
GuidetoPHARMACOLOGY; 2065; -.
iPTMnet; P45985; -.
PhosphoSitePlus; P45985; -.
BioMuta; MAP2K4; -.
DMDM; 1170596; -.
EPD; P45985; -.
MaxQB; P45985; -.
PaxDb; P45985; -.
PeptideAtlas; P45985; -.
PRIDE; P45985; -.
ProteomicsDB; 55703; -.
ProteomicsDB; 55704; -. [P45985-2]
DNASU; 6416; -.
Ensembl; ENST00000353533; ENSP00000262445; ENSG00000065559. [P45985-1]
Ensembl; ENST00000415385; ENSP00000410402; ENSG00000065559. [P45985-2]
GeneID; 6416; -.
KEGG; hsa:6416; -.
UCSC; uc002gnj.5; human. [P45985-1]
CTD; 6416; -.
DisGeNET; 6416; -.
EuPathDB; HostDB:ENSG00000065559.14; -.
GeneCards; MAP2K4; -.
HGNC; HGNC:6844; MAP2K4.
HPA; CAB007751; -.
HPA; HPA060074; -.
MIM; 601335; gene.
neXtProt; NX_P45985; -.
OpenTargets; ENSG00000065559; -.
PharmGKB; PA30589; -.
eggNOG; KOG0984; Eukaryota.
eggNOG; ENOG410XT3F; LUCA.
GeneTree; ENSGT00940000154744; -.
HOVERGEN; HBG108518; -.
InParanoid; P45985; -.
KO; K04430; -.
OMA; TCLIKDE; -.
OrthoDB; EOG091G0A9H; -.
PhylomeDB; P45985; -.
TreeFam; TF350701; -.
BRENDA; 2.7.12.2; 2681.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
Reactome; R-HSA-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
Reactome; R-HSA-5210891; Uptake and function of anthrax toxins.
Reactome; R-HSA-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation.
SignaLink; P45985; -.
SIGNOR; P45985; -.
ChiTaRS; MAP2K4; human.
EvolutionaryTrace; P45985; -.
GeneWiki; MAP2K4; -.
GenomeRNAi; 6416; -.
PMAP-CutDB; P45985; -.
PRO; PR:P45985; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000065559; Expressed in 227 organ(s), highest expression level in frontal cortex.
CleanEx; HS_MAP2K4; -.
ExpressionAtlas; P45985; baseline and differential.
Genevisible; P45985; HS.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0032839; C:dendrite cytoplasm; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0043204; C:perikaryon; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008545; F:JUN kinase kinase activity; IBA:GO_Central.
GO; GO:0004708; F:MAP kinase kinase activity; IBA:GO_Central.
GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IEA:Ensembl.
GO; GO:0004672; F:protein kinase activity; TAS:ProtInc.
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; IBA:GO_Central.
GO; GO:0000187; P:activation of MAPK activity; IBA:GO_Central.
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; IEA:Ensembl.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
GO; GO:0072709; P:cellular response to sorbitol; IEA:Ensembl.
GO; GO:0007254; P:JNK cascade; TAS:ProtInc.
GO; GO:2000672; P:negative regulation of motor neuron apoptotic process; IEA:Ensembl.
GO; GO:0045740; P:positive regulation of DNA replication; IEA:Ensembl.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IEA:Ensembl.
GO; GO:0034393; P:positive regulation of smooth muscle cell apoptotic process; IEA:Ensembl.
GO; GO:0009611; P:response to wounding; 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.
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; Kinase; Methylation;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Serine/threonine-protein kinase; Stress response;
Transferase; Tyrosine-protein kinase.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 399 Dual specificity mitogen-activated
protein kinase kinase 4.
/FTId=PRO_0000086381.
DOMAIN 102 367 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 108 116 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 37 52 D domain.
REGION 364 387 DVD domain.
COMPBIAS 5 19 Gly/Ser-rich.
ACT_SITE 229 229 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 131 131 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 45 46 Cleavage; by anthrax lethal factor.
SITE 58 59 Cleavage; by anthrax lethal factor.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 58 58 Asymmetric dimethylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 58 58 Omega-N-methylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 90 90 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 257 257 Phosphoserine; by MAP3K.
{ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:24275569}.
MOD_RES 261 261 Phosphothreonine; by MAP3K.
{ECO:0000269|PubMed:9003778}.
VAR_SEQ 39 39 G -> GFQINFCEKAQS (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038838.
VARIANT 16 16 S -> R (in dbSNP:rs17855590).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_062963.
VARIANT 142 142 Q -> L (in a lung squamous cell carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040818.
VARIANT 154 154 R -> W (in a colorectal adenocarcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040819.
VARIANT 234 234 N -> I (in an ovarian serous carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040820.
VARIANT 251 251 S -> N (in a metastatic melanoma sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040821.
VARIANT 279 279 A -> T (in a colorectal adenocarcinoma
sample; somatic mutation;
dbSNP:rs753665559).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040822.
CONFLICT 118 118 K -> R (in Ref. 4; CAG38801).
{ECO:0000305}.
CONFLICT 179 179 E -> G (in Ref. 6; BAG35884).
{ECO:0000305}.
CONFLICT 356 356 P -> L (in Ref. 10; AAH60764).
{ECO:0000305}.
STRAND 81 83 {ECO:0000244|PDB:3VUT}.
STRAND 85 88 {ECO:0000244|PDB:3ALN}.
STRAND 93 95 {ECO:0000244|PDB:3ALN}.
STRAND 101 103 {ECO:0000244|PDB:3ALN}.
STRAND 107 110 {ECO:0000244|PDB:3ALN}.
STRAND 112 121 {ECO:0000244|PDB:3ALN}.
TURN 122 124 {ECO:0000244|PDB:3ALN}.
STRAND 127 134 {ECO:0000244|PDB:3ALN}.
HELIX 139 153 {ECO:0000244|PDB:3ALN}.
STRAND 164 169 {ECO:0000244|PDB:3ALN}.
STRAND 171 178 {ECO:0000244|PDB:3ALN}.
STRAND 182 184 {ECO:0000244|PDB:3ALN}.
HELIX 185 194 {ECO:0000244|PDB:3ALN}.
HELIX 202 223 {ECO:0000244|PDB:3ALN}.
HELIX 232 234 {ECO:0000244|PDB:3ALN}.
STRAND 235 237 {ECO:0000244|PDB:3ALN}.
STRAND 243 245 {ECO:0000244|PDB:3ALN}.
STRAND 249 251 {ECO:0000244|PDB:3ALN}.
STRAND 255 259 {ECO:0000244|PDB:3VUT}.
STRAND 267 270 {ECO:0000244|PDB:3ALO}.
HELIX 272 274 {ECO:0000244|PDB:3ALO}.
HELIX 287 302 {ECO:0000244|PDB:3ALN}.
STRAND 312 314 {ECO:0000244|PDB:3ALO}.
STRAND 316 321 {ECO:0000244|PDB:3ALO}.
HELIX 338 347 {ECO:0000244|PDB:3ALN}.
HELIX 352 354 {ECO:0000244|PDB:3ALN}.
HELIX 358 361 {ECO:0000244|PDB:3ALN}.
HELIX 365 372 {ECO:0000244|PDB:3ALN}.
HELIX 377 387 {ECO:0000244|PDB:3ALN}.
SEQUENCE 399 AA; 44288 MW; A472537F2F26770B CRC64;
MAAPSPSGGG GSGGGSGSGT PGPVGSPAPG HPAVSSMQGK RKALKLNFAN PPFKSTARFT
LNPNPTGVQN PHIERLRTHS IESSGKLKIS PEQHWDFTAE DLKDLGEIGR GAYGSVNKMV
HKPSGQIMAV KRIRSTVDEK EQKQLLMDLD VVMRSSDCPY IVQFYGALFR EGDCWICMEL
MSTSFDKFYK YVYSVLDDVI PEEILGKITL ATVKALNHLK ENLKIIHRDI KPSNILLDRS
GNIKLCDFGI SGQLVDSIAK TRDAGCRPYM APERIDPSAS RQGYDVRSDV WSLGITLYEL
ATGRFPYPKW NSVFDQLTQV VKGDPPQLSN SEEREFSPSF INFVNLCLTK DESKRPKYKE
LLKHPFILMY EERAVEVACY VCKILDQMPA TPSSPMYVD


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