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Dual specificity mitogen-activated protein kinase kinase 7 (MAP kinase kinase 7) (MAPKK 7) (EC 2.7.12.2) (JNK-activating kinase 2) (MAPK/ERK kinase 7) (MEK 7) (Stress-activated protein kinase kinase 4) (SAPK kinase 4) (SAPKK-4) (SAPKK4) (c-Jun N-terminal kinase kinase 2) (JNK kinase 2) (JNKK 2)

 MP2K7_HUMAN             Reviewed;         419 AA.
O14733; B2R9S5; D6W659; O14648; O14816; O60452; O60453; Q1PG43;
Q8IY10;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
30-MAY-2000, sequence version 2.
05-DEC-2018, entry version 186.
RecName: Full=Dual specificity mitogen-activated protein kinase kinase 7;
Short=MAP kinase kinase 7;
Short=MAPKK 7;
EC=2.7.12.2;
AltName: Full=JNK-activating kinase 2;
AltName: Full=MAPK/ERK kinase 7;
Short=MEK 7;
AltName: Full=Stress-activated protein kinase kinase 4;
Short=SAPK kinase 4;
Short=SAPKK-4;
Short=SAPKK4;
AltName: Full=c-Jun N-terminal kinase kinase 2;
Short=JNK kinase 2;
Short=JNKK 2;
Name=MAP2K7; Synonyms=JNKK2, MEK7, MKK7, PRKMK7, SKK4;
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), FUNCTION, AND TISSUE
SPECIFICITY.
TISSUE=Heart, and Skeletal muscle;
PubMed=9372971; DOI=10.1128/MCB.17.12.7407;
Wu Z., Wu J., Jacinto E., Karin M.;
"Molecular cloning and characterization of human JNKK2, a novel jun
NH2-terminal kinase-specific kinase.";
Mol. Cell. Biol. 17:7407-7416(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND ACTIVITY
REGULATION.
PubMed=9312068; DOI=10.1074/jbc.272.40.24751;
Lu X., Nemoto S., Lin A.;
"Identification of c-Jun NH2-terminal protein kinase (JNK)-activating
kinase 2 as an activator of JNK but not p38.";
J. Biol. Chem. 272:24751-24754(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE
SPECIFICITY, AND VARIANT PHE-259.
TISSUE=Fetal kidney;
PubMed=9535930; DOI=10.1074/jbc.273.15.9344;
Foltz I.N., Gerl R.E., Wieler J.S., Luckach M., Salmon R.A.,
Schrader J.W.;
"Human mitogen-activated protein kinase kinase 7 (MKK7) is a highly
conserved c-Jun N-terminal kinase/stress-activated protein kinase
(JNK/SAPK) activated by environmental stresses and physiological
stimuli.";
J. Biol. Chem. 273:9344-9351(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ACTIVITY REGULATION, AND
TISSUE SPECIFICITY.
PubMed=16442502; DOI=10.1016/j.bbrc.2005.12.223;
Michael L., Swantek J., Robinson M.J.;
"Cloning and expression of human mitogen-activated protein kinase
kinase 7gamma1.";
Biochem. Biophys. Res. Commun. 341:679-683(2006).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION IN
PHOSPHORYLATION OF MAPK8/JNK1 AND MAPK9/JNK2.
Yang J., New L., Yong J., Han J., Su B.;
"Molecular cloning of human JNKK2 reveals a novel kinase module for c-
Jun N-terminal kinase activation.";
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
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 [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.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=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).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-260 (ISOFORMS 1/4).
PubMed=9207092; DOI=10.1073/pnas.94.14.7337;
Tournier C., Whitmarsh A.J., Cavanagh J., Barrett T., Davis R.J.;
"Mitogen-activated protein kinase kinase 7 is an activator of the c-
Jun NH2-terminal kinase.";
Proc. Natl. Acad. Sci. U.S.A. 94:7337-7342(1997).
[10]
INTERACTION WITH MAPK8IP1/JIP1 AND MAPK8IP2/JIP2.
PubMed=10490659; DOI=10.1128/MCB.19.10.7245;
Yasuda J., Whitmarsh A.J., Cavanagh J., Sharma M., Davis R.J.;
"The JIP group of mitogen-activated protein kinase scaffold
proteins.";
Mol. Cell. Biol. 19:7245-7254(1999).
[11]
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).
[12]
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).
[13]
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).
[14]
INTERACTION WITH VRK2.
PubMed=18286207; DOI=10.1371/journal.pone.0001660;
Blanco S., Sanz-Garcia M., Santos C.R., Lazo P.A.;
"Modulation of interleukin-1 transcriptional response by the
interaction between VRK2 and the JIP1 scaffold protein.";
PLoS ONE 3:E1660-E1660(2008).
[15]
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).
[16]
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).
[17]
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).
[18]
INTERACTION WITH RASSF7.
PubMed=21278800; DOI=10.1038/cdd.2010.137;
Takahashi S., Ebihara A., Kajiho H., Kontani K., Nishina H.,
Katada T.;
"RASSF7 negatively regulates pro-apoptotic JNK signaling by inhibiting
the activity of phosphorylated-MKK7.";
Cell Death Differ. 18:645-655(2011).
[19]
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).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
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).
[22]
FUNCTION.
PubMed=28111074; DOI=10.1016/j.cell.2016.12.044;
Huang Y.A., Zhou B., Wernig M., Suedhof T.C.;
"ApoE2, ApoE3, and ApoE4 Differentially Stimulate APP Transcription
and Abeta Secretion.";
Cell 168:427-441(2017).
[23]
X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 101-405.
RIKEN structural genomics initiative (RSGI);
"Crystal structure of human mitogen-activated protein kinase kinase 7
activated mutant (s287d, t291d).";
Submitted (FEB-2009) to the PDB data bank.
[24]
VARIANTS [LARGE SCALE ANALYSIS] SER-118; CYS-138; CYS-162; HIS-162 AND
THR-195.
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 MAP2K4/MKK4,
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/MKK4 shows preference for
phosphorylation of the Tyr residue and MAP2K7/MKK7 for the Thr
residue. The monophosphorylation of JNKs on the Thr residue is
sufficient to increase JNK activity indicating that MAP2K7/MKK7 is
important to trigger JNK activity, while the additional
phosphorylation of the Tyr residue by MAP2K4/MKK4 ensures optimal
JNK activation. Has a specific role in JNK signal transduction
pathway activated by proinflammatory cytokines. The MKK/JNK
signaling pathway is also involved in mitochondrial death
signaling pathway, including the release cytochrome c, leading to
apoptosis. Part of a non-canonical MAPK signaling pathway,
composed of the upstream MAP3K12 kinase and downstream MAP kinases
MAPK1/ERK2 and MAPK3/ERK1, that enhances the AP-1-mediated
transcription of APP in response to APOE (PubMed:28111074).
{ECO:0000269|PubMed:28111074, ECO:0000269|PubMed:9312068,
ECO:0000269|PubMed:9372971, ECO:0000269|PubMed:9535930,
ECO:0000269|Ref.5}.
-!- 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;
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ACTIVITY REGULATION: Activated by phosphorylation by specific MAP
kinase kinase kinases such as MAP3K1/MEKK1, MAP3K3/MEKK3,
MAP3K11/MLK3 and MAP3K12/DLK. {ECO:0000269|PubMed:16442502,
ECO:0000269|PubMed:9312068}.
-!- SUBUNIT: Interacts with isoform 1 of VRK2. Interacts (via its D
domain) with its substrates MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3
(By similarity). Interacts (via its DVD domain) with MAP3Ks
activators like MAP3K5/ASK1 and MAP3K1/MEKK1 (By similarity).
Interacts with MAPK8IP1/JIP1, MAPK8IP2/JIP2 and MAPK8IP3/JIP3
scaffold proteins. Interacts with RASSF7, the interaction promotes
phosphorylation. Found in a complex with SH3RF1, RAC1,
MAP3K11/MLK3, MAPK8IP1/JIP1 and MAPK8/JNK1. Found in a complex
with SH3RF1, RAC2, MAP3K7/TAK1, MAPK8IP1/JIP1, MAPK8/JNK1 and
MAPK9/JNK2 (By similarity). {ECO:0000250|UniProtKB:Q8CE90,
ECO:0000269|PubMed:10490659, ECO:0000269|PubMed:12189133,
ECO:0000269|PubMed:18286207, ECO:0000269|PubMed:21278800}.
-!- INTERACTION:
O15519-1:CFLAR; NbExp=2; IntAct=EBI-492605, EBI-4567563;
O75293:GADD45B; NbExp=8; IntAct=EBI-492605, EBI-448187;
Q5S007:LRRK2; NbExp=3; IntAct=EBI-492605, EBI-5323863;
O43318:MAP3K7; NbExp=3; IntAct=EBI-492605, EBI-358684;
P45983:MAPK8; NbExp=4; IntAct=EBI-492605, EBI-286483;
Q9UQF2:MAPK8IP1; NbExp=5; IntAct=EBI-492605, EBI-78404;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=A;
IsoId=O14733-1; Sequence=Displayed;
Name=2; Synonyms=B;
IsoId=O14733-2; Sequence=VSP_004883;
Note=May be due to intron retention.;
Name=3; Synonyms=gamma1;
IsoId=O14733-3; Sequence=VSP_022309;
Name=4;
IsoId=O14733-4; Sequence=VSP_022310;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous; with highest level of expression
in skeletal muscle. Isoform 3 is found at low levels in placenta,
fetal liver, and skeletal muscle. {ECO:0000269|PubMed:16442502,
ECO:0000269|PubMed:9372971, ECO:0000269|PubMed:9535930}.
-!- DOMAIN: The DVD domain (residues 377-400) 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 37-57) contains a conserved docking
site and is required for the binding to MAPK substrates.
{ECO:0000269|PubMed:15866172}.
-!- PTM: Activated by phosphorylation on Ser-271 and Thr-275 by MAP
kinase kinase kinases (MAP3Ks). {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB97813.1; Type=Erroneous termination; Positions=420; Note=Translated as stop.; Evidence={ECO:0000305};
Sequence=AAB97813.1; Type=Frameshift; Positions=402, 410; Evidence={ECO:0000305};
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EMBL; AF014401; AAB88048.1; -; mRNA.
EMBL; AF006689; AAB97813.1; ALT_SEQ; mRNA.
EMBL; AF013588; AAC16272.1; -; mRNA.
EMBL; AF013589; AAC16273.1; -; mRNA.
EMBL; DQ445915; ABE03013.1; -; mRNA.
EMBL; AF022805; AAC26142.1; -; mRNA.
EMBL; AK313899; BAG36622.1; -; mRNA.
EMBL; CH471139; EAW68964.1; -; Genomic_DNA.
EMBL; CH471139; EAW68968.1; -; Genomic_DNA.
EMBL; BC038295; AAH38295.1; -; mRNA.
EMBL; AF003199; AAB63374.1; -; mRNA.
CCDS; CCDS42491.1; -. [O14733-1]
CCDS; CCDS74277.1; -. [O14733-3]
CCDS; CCDS74278.1; -. [O14733-4]
RefSeq; NP_001284484.1; NM_001297555.1. [O14733-3]
RefSeq; NP_001284485.1; NM_001297556.1. [O14733-4]
RefSeq; NP_660186.1; NM_145185.3. [O14733-1]
UniGene; Hs.531754; -.
PDB; 2DYL; X-ray; 2.45 A; A=101-405.
PDB; 3WZU; X-ray; 3.01 A; A=103-419.
PDB; 4UX9; X-ray; 2.34 A; F/G/H/I=37-48.
PDB; 5B2K; X-ray; 2.75 A; A=103-419.
PDB; 5B2L; X-ray; 2.10 A; A=103-419.
PDB; 5B2M; X-ray; 3.06 A; A=103-419.
PDB; 5Y8U; X-ray; 2.92 A; A=103-419.
PDB; 5Y90; X-ray; 1.30 A; A=103-419.
PDBsum; 2DYL; -.
PDBsum; 3WZU; -.
PDBsum; 4UX9; -.
PDBsum; 5B2K; -.
PDBsum; 5B2L; -.
PDBsum; 5B2M; -.
PDBsum; 5Y8U; -.
PDBsum; 5Y90; -.
DisProt; DP00841; -.
ProteinModelPortal; O14733; -.
SMR; O14733; -.
BioGrid; 111595; 63.
IntAct; O14733; 26.
MINT; O14733; -.
STRING; 9606.ENSP00000381066; -.
BindingDB; O14733; -.
ChEMBL; CHEMBL3530; -.
GuidetoPHARMACOLOGY; 2068; -.
iPTMnet; O14733; -.
PhosphoSitePlus; O14733; -.
BioMuta; MAP2K7; -.
EPD; O14733; -.
MaxQB; O14733; -.
PaxDb; O14733; -.
PeptideAtlas; O14733; -.
PRIDE; O14733; -.
ProteomicsDB; 48192; -.
ProteomicsDB; 48193; -. [O14733-2]
ProteomicsDB; 48194; -. [O14733-3]
ProteomicsDB; 48195; -. [O14733-4]
DNASU; 5609; -.
Ensembl; ENST00000397979; ENSP00000381066; ENSG00000076984. [O14733-1]
Ensembl; ENST00000397981; ENSP00000381068; ENSG00000076984. [O14733-4]
Ensembl; ENST00000397983; ENSP00000381070; ENSG00000076984. [O14733-3]
GeneID; 5609; -.
KEGG; hsa:5609; -.
UCSC; uc002mit.4; human. [O14733-1]
CTD; 5609; -.
DisGeNET; 5609; -.
EuPathDB; HostDB:ENSG00000076984.17; -.
GeneCards; MAP2K7; -.
HGNC; HGNC:6847; MAP2K7.
HPA; CAB004262; -.
HPA; HPA001633; -.
HPA; HPA064711; -.
MIM; 603014; gene.
neXtProt; NX_O14733; -.
OpenTargets; ENSG00000076984; -.
PharmGKB; PA284; -.
eggNOG; KOG0983; Eukaryota.
eggNOG; ENOG410XTNQ; LUCA.
GeneTree; ENSGT00940000158914; -.
HOVERGEN; HBG108518; -.
InParanoid; O14733; -.
KO; K04431; -.
OMA; SSQCYSH; -.
OrthoDB; EOG091G0A9H; -.
PhylomeDB; O14733; -.
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.
SignaLink; O14733; -.
SIGNOR; O14733; -.
ChiTaRS; MAP2K7; human.
EvolutionaryTrace; O14733; -.
GeneWiki; MAP2K7; -.
GenomeRNAi; 5609; -.
PMAP-CutDB; O14733; -.
PRO; PR:O14733; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000076984; Expressed in 225 organ(s), highest expression level in buccal mucosa cell.
CleanEx; HS_MAP2K7; -.
Genevisible; O14733; HS.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0008545; F:JUN kinase kinase activity; IBA:GO_Central.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0004708; F:MAP kinase kinase activity; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0019903; F:protein phosphatase binding; ISS:BHF-UCL.
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; ISS:BHF-UCL.
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:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
GO; GO:0051973; P:positive regulation of telomerase activity; IMP:BHF-UCL.
GO; GO:1904355; P:positive regulation of telomere capping; IMP:BHF-UCL.
GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IMP:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0009408; P:response to heat; IDA:UniProtKB.
GO; GO:0006970; P:response to osmotic stress; IDA:UniProtKB.
GO; GO:0034612; P:response to tumor necrosis factor; IDA:UniProtKB.
GO; GO:0009411; P:response to UV; IDA:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0023014; P:signal transduction by protein phosphorylation; IBA:GO_Central.
GO; GO:0051403; P:stress-activated MAPK cascade; IDA:UniProtKB.
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; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 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; Coiled coil; Complete proteome; Cytoplasm; Kinase;
Magnesium; Metal-binding; 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,
ECO:0000244|PubMed:22814378}.
CHAIN 2 419 Dual specificity mitogen-activated
protein kinase kinase 7.
/FTId=PRO_0000086388.
DOMAIN 120 380 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 126 134 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 37 57 D domain. {ECO:0000250}.
REGION 377 400 DVD domain.
COILED 2 30 {ECO:0000255}.
ACT_SITE 243 243 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 149 149 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 44 45 Cleavage; by anthrax lethal factor.
SITE 76 77 Cleavage; by anthrax lethal factor.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
MOD_RES 271 271 Phosphoserine; by MAP3K. {ECO:0000250}.
MOD_RES 275 275 Phosphothreonine; by MAP3K.
{ECO:0000250}.
MOD_RES 411 411 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 42 42 T -> IIVITLSPAPAPSQRAA (in isoform 3).
{ECO:0000303|PubMed:16442502}.
/FTId=VSP_022309.
VAR_SEQ 111 111 Q -> QVPPSLWRGEGGGPARLDPSWERQWGAGGGGRAPGT
LQPSLSSQ (in isoform 2).
{ECO:0000303|PubMed:9535930}.
/FTId=VSP_004883.
VAR_SEQ 312 312 L -> LPCPSPSQ (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_022310.
VARIANT 118 118 N -> S (in dbSNP:rs56316660).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040825.
VARIANT 138 138 R -> C (in dbSNP:rs56106612).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040826.
VARIANT 162 162 R -> C (in a colorectal adenocarcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040827.
VARIANT 162 162 R -> H (in a colorectal adenocarcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040828.
VARIANT 195 195 A -> T (in dbSNP:rs55800262).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040829.
VARIANT 259 259 L -> F (in dbSNP:rs1053566).
{ECO:0000269|PubMed:9535930}.
/FTId=VAR_029890.
CONFLICT 94 94 Q -> H (in Ref. 2; AAB97813).
{ECO:0000305}.
CONFLICT 106 106 L -> P (in Ref. 4; ABE03013).
{ECO:0000305}.
CONFLICT 133 133 Q -> P (in Ref. 2; AAB97813).
{ECO:0000305}.
CONFLICT 142 142 T -> N (in Ref. 1; AAB88048).
{ECO:0000305}.
CONFLICT 407 407 S -> N (in Ref. 2; AAB97813).
{ECO:0000305}.
CONFLICT 415 415 L -> LG (in Ref. 2; AAB97813).
{ECO:0000305}.
STRAND 104 108 {ECO:0000244|PDB:5Y90}.
STRAND 111 115 {ECO:0000244|PDB:5Y90}.
HELIX 117 119 {ECO:0000244|PDB:5Y90}.
STRAND 120 126 {ECO:0000244|PDB:5Y90}.
STRAND 129 138 {ECO:0000244|PDB:5Y90}.
TURN 140 142 {ECO:0000244|PDB:5Y90}.
STRAND 145 152 {ECO:0000244|PDB:5Y90}.
HELIX 157 171 {ECO:0000244|PDB:5Y90}.
TURN 173 175 {ECO:0000244|PDB:5B2L}.
STRAND 182 187 {ECO:0000244|PDB:5Y90}.
STRAND 189 196 {ECO:0000244|PDB:5Y90}.
STRAND 200 202 {ECO:0000244|PDB:5Y90}.
HELIX 203 210 {ECO:0000244|PDB:5Y90}.
HELIX 216 237 {ECO:0000244|PDB:5Y90}.
HELIX 246 248 {ECO:0000244|PDB:5Y90}.
STRAND 249 251 {ECO:0000244|PDB:5Y90}.
STRAND 257 259 {ECO:0000244|PDB:5Y90}.
TURN 262 265 {ECO:0000244|PDB:5Y90}.
HELIX 281 283 {ECO:0000244|PDB:5Y90}.
HELIX 286 289 {ECO:0000244|PDB:5Y90}.
STRAND 292 297 {ECO:0000244|PDB:5B2L}.
HELIX 302 317 {ECO:0000244|PDB:5Y90}.
TURN 321 324 {ECO:0000244|PDB:2DYL}.
HELIX 328 337 {ECO:0000244|PDB:5Y90}.
STRAND 345 347 {ECO:0000244|PDB:5Y90}.
HELIX 351 360 {ECO:0000244|PDB:5Y90}.
HELIX 365 367 {ECO:0000244|PDB:5Y90}.
HELIX 371 374 {ECO:0000244|PDB:5Y90}.
HELIX 378 385 {ECO:0000244|PDB:5Y90}.
HELIX 390 401 {ECO:0000244|PDB:5Y90}.
SEQUENCE 419 AA; 47485 MW; F1B22E050F54299A CRC64;
MAASSLEQKL SRLEAKLKQE NREARRRIDL NLDISPQRPR PTLQLPLAND GGSRSPSSES
SPQHPTPPAR PRHMLGLPST LFTPRSMESI EIDQKLQEIM KQTGYLTIGG QRYQAEINDL
ENLGEMGSGT CGQVWKMRFR KTGHVIAVKQ MRRSGNKEEN KRILMDLDVV LKSHDCPYIV
QCFGTFITNT DVFIAMELMG TCAEKLKKRM QGPIPERILG KMTVAIVKAL YYLKEKHGVI
HRDVKPSNIL LDERGQIKLC DFGISGRLVD SKAKTRSAGC AAYMAPERID PPDPTKPDYD
IRADVWSLGI SLVELATGQF PYKNCKTDFE VLTKVLQEEP PLLPGHMGFS GDFQSFVKDC
LTKDHRKRPK YNKLLEHSFI KRYETLEVDV ASWFKDVMAK TESPRTSGVL SQPHLPFFR


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