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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) (c-Jun N-terminal kinase kinase 2) (JNK kinase 2) (JNKK 2)

 MP2K7_MOUSE             Reviewed;         535 AA.
Q8CE90; O35406; O35720; O35871; O35872; O54780; O70242; O70243;
Q8BSP1; Q9QWG6; Q9R1Z3; Q9R1Z4; Q9R1Z5; Q9R1Z6;
09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
28-MAR-2018, entry version 136.
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=c-Jun N-terminal kinase kinase 2;
Short=JNK kinase 2;
Short=JNKK 2;
Name=Map2k7 {ECO:0000312|MGI:MGI:1346871};
Synonyms=Mkk7 {ECO:0000312|EMBL:AAC16274.1};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000305, ECO:0000312|EMBL:AAB81848.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), FUNCTION, TISSUE SPECIFICITY,
AND DEVELOPMENTAL STAGE.
PubMed=9405446; DOI=10.1074/jbc.272.51.32378;
Yao Z., Diener K., Wang X.S., Zukowski M., Matsumoto G., Zhou G.,
Mo R., Sasaki T., Nishina H., Hui C.C., Tan T.-H., Woodgett J.P.,
Penninger J.M.;
"Activation of stress-activated protein kinases/c-Jun N-terminal
protein kinases (SAPKs/JNKs) by a novel mitogen-activated protein
kinase kinase (MKK7).";
J. Biol. Chem. 272:32378-32383(1997).
[2] {ECO:0000305, ECO:0000312|EMBL:AAC53365.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 5), FUNCTION, AND TISSUE
SPECIFICITY.
PubMed=9312105; DOI=10.1074/jbc.272.40.24994;
Holland P.M., Magali S., Campbell J.S., Noselli S., Cooper J.A.;
"MKK7 is a stress-activated mitogen-activated protein kinase kinase
functionally related to hemipterous.";
J. Biol. Chem. 272:24994-24998(1997).
[3] {ECO:0000305, ECO:0000312|EMBL:BAA24383.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), AND FUNCTION.
PubMed=9384583; DOI=10.1093/emboj/16.23.7045;
Moriguchi T., Toyoshima F., Masuyama N., Hanafusa H., Gotoh Y.,
Nishida E.;
"A novel SAPK/JNK kinase, MKK7, stimulated by TNFalpha and cellular
stresses.";
EMBO J. 16:7045-7053(1997).
[4] {ECO:0000305, ECO:0000312|EMBL:AAC16274.1}
NUCLEOTIDE SEQUENCE [MRNA] OF 1-311 (ISOFORMS 2/6), FUNCTION, AND
TISSUE SPECIFICITY.
TISSUE=B-cell {ECO:0000312|EMBL:AAC16274.1}, and
Thymus {ECO:0000312|EMBL:AAC16275.1};
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).
[5] {ECO:0000305, ECO:0000312|EMBL:AAD15819.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 6; 7 AND 8), NUCLEOTIDE
SEQUENCE [GENOMIC DNA] OF 47-535 (ISOFORM 6), FUNCTION, ENZYME
REGULATION, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
STRAIN=CD-1 {ECO:0000312|EMBL:AAB63447.1};
TISSUE=Testis {ECO:0000312|EMBL:AAB63447.1};
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).
[6] {ECO:0000305, ECO:0000312|EMBL:BAC26111.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC26111.1};
TISSUE=Fetal forelimb {ECO:0000312|EMBL:BAC27272.1},
Fetus {ECO:0000312|EMBL:BAE38066.1}, and
Skin {ECO:0000312|EMBL:BAC26111.1};
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[7] {ECO:0000305, ECO:0000312|EMBL:AAH70467.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH70467.1};
TISSUE=Eye {ECO:0000312|EMBL:AAH70467.1};
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).
[8]
INTERACTION WITH MAPK8IP1/JIP1.
PubMed=9733513; DOI=10.1126/science.281.5383.1671;
Whitmarsh A.J., Cavanagh J., Tournier C., Yasuda J., Davis R.J.;
"A mammalian scaffold complex that selectively mediates MAP kinase
activation.";
Science 281:1671-1674(1998).
[9]
INTERACTION WITH MAPK8IP3/JIP3.
PubMed=10629060; DOI=10.1128/MCB.20.3.1030-1043.2000;
Kelkar N., Gupta S., Dickens M., Davis R.J.;
"Interaction of a mitogen-activated protein kinase signaling module
with the neuronal protein JIP3.";
Mol. Cell. Biol. 20:1030-1043(2000).
[10]
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).
[11]
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).
[12]
REVIEW ON ENZYME 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).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[14]
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).
[15]
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).
-!- 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. {ECO:0000269|PubMed:11390361,
ECO:0000269|PubMed:12624093, ECO:0000269|PubMed:9312105,
ECO:0000269|PubMed:9384583, ECO:0000269|PubMed:9405446,
ECO:0000269|PubMed:9535930, ECO:0000269|PubMed:9891090}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:9535930, ECO:0000269|PubMed:9891090}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:9535930,
ECO:0000269|PubMed:9891090};
-!- ENZYME REGULATION: Activated by phosphorylation by specific MAP
kinase kinase kinases such as MAP3K1/MEKK1, MAP3K3/MEKK3,
MAP3K11/MLK3 and MAP3K12/DLK. Isoforms 3 and 4 have lower basal
activity but a higher level of inducible activation, than isoforms
2, 6, 7 and 8. {ECO:0000269|PubMed:9891090}.
-!- SUBUNIT: Interacts with RASSF7, the interaction promotes
phosphorylation. Interacts with VRK2 (By similarity). 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. {ECO:0000250,
ECO:0000269|PubMed:10629060, ECO:0000269|PubMed:9733513}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9891090}.
Cytoplasm {ECO:0000269|PubMed:9891090}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Name=1 {ECO:0000269|PubMed:16141072};
IsoId=Q8CE90-1; Sequence=Displayed;
Note=No experimental confirmation available. {ECO:0000305};
Name=2 {ECO:0000269|PubMed:16141072, ECO:0000269|PubMed:9312105,
ECO:0000269|PubMed:9891090}; Synonyms=a
{ECO:0000269|PubMed:9312105}, beta 1 {ECO:0000269|PubMed:9891090};
IsoId=Q8CE90-2; Sequence=VSP_052266, VSP_052268, VSP_052269;
Name=3 {ECO:0000269|PubMed:9384583, ECO:0000269|PubMed:9891090};
Synonyms=alpha 2 {ECO:0000269|PubMed:9891090};
IsoId=Q8CE90-3; Sequence=VSP_052265, VSP_052270, VSP_052271;
Name=4 {ECO:0000269|PubMed:9891090}; Synonyms=alpha 1
{ECO:0000269|PubMed:9891090};
IsoId=Q8CE90-4; Sequence=VSP_052265, VSP_052268, VSP_052269;
Name=5 {ECO:0000269|PubMed:9312105}; Synonyms=b
{ECO:0000269|PubMed:9312105};
IsoId=Q8CE90-5; Sequence=VSP_052264, VSP_052267, VSP_052268,
VSP_052269;
Note=No experimental confirmation available. {ECO:0000305};
Name=6 {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9405446,
ECO:0000269|PubMed:9891090}; Synonyms=b
{ECO:0000269|PubMed:15489334}, gamma 1
{ECO:0000269|PubMed:9891090};
IsoId=Q8CE90-6; Sequence=VSP_052268, VSP_052269;
Name=7 {ECO:0000269|PubMed:9891090}; Synonyms=gamma 2
{ECO:0000269|PubMed:9891090};
IsoId=Q8CE90-7; Sequence=VSP_052270, VSP_052271;
Name=8 {ECO:0000269|PubMed:9891090}; Synonyms=beta 2
{ECO:0000269|PubMed:9891090};
IsoId=Q8CE90-8; Sequence=VSP_052266, VSP_052270, VSP_052271;
-!- TISSUE SPECIFICITY: Expressed at high levels in brain, lung,
liver, skeletal muscle, kidney, and testis and at lower levels in
the heart and spleen. {ECO:0000269|PubMed:9312105,
ECO:0000269|PubMed:9405446, ECO:0000269|PubMed:9535930}.
-!- DEVELOPMENTAL STAGE: Expressed at high levels in the brain, spinal
cord, eyes, muscle, lungs, vertebrae, and intestine and at lower
levels in the heart and livers at E12.5. At later stages of
embryogenesis (E14.5, E16.5, and E18.5) high levels were found in
the brain, retina, bone marrow, skin, intestine, lung epithelium
and the epithelial layers lining the olfactory cavity and
developing teeth and whiskers. {ECO:0000269|PubMed:9405446}.
-!- DOMAIN: The DVD domain (residues 393-413) 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 37-73) contains a conserved docking
site and is required for the binding to MAPK substrates.
-!- PTM: Activated by phosphorylation on Ser-287 and Thr-291 by MAP
kinase kinase kinases (MAP3Ks). {ECO:0000269|PubMed:9891090}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
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EMBL; AF026216; AAB81848.1; -; mRNA.
EMBL; U74463; AAC53364.1; -; mRNA.
EMBL; U74464; AAC53365.1; -; mRNA.
EMBL; AB005654; BAA24383.1; -; mRNA.
EMBL; AF022112; AAC16274.1; -; mRNA.
EMBL; AF022113; AAC16275.1; -; mRNA.
EMBL; U93030; AAB63447.1; -; mRNA.
EMBL; U93031; AAB63448.1; -; Genomic_DNA.
EMBL; AF060943; AAD15819.1; -; mRNA.
EMBL; AF060944; AAD15820.1; -; mRNA.
EMBL; AF060945; AAD15821.1; -; mRNA.
EMBL; AF060946; AAD15822.1; -; mRNA.
EMBL; AF060947; AAD15823.1; -; mRNA.
EMBL; AK028772; BAC26111.1; -; mRNA.
EMBL; AK031137; BAC27272.1; -; mRNA.
EMBL; AK165184; BAE38066.1; -; mRNA.
EMBL; BC070467; AAH70467.1; -; mRNA.
CCDS; CCDS40208.1; -. [Q8CE90-7]
CCDS; CCDS40209.1; -. [Q8CE90-2]
CCDS; CCDS52474.1; -. [Q8CE90-6]
CCDS; CCDS80852.1; -. [Q8CE90-8]
CCDS; CCDS80853.1; -. [Q8CE90-3]
CCDS; CCDS80854.1; -. [Q8CE90-4]
RefSeq; NP_001036022.1; NM_001042557.2. [Q8CE90-7]
RefSeq; NP_001157644.1; NM_001164172.1. [Q8CE90-6]
RefSeq; NP_001278706.1; NM_001291777.1. [Q8CE90-8]
RefSeq; NP_001278707.1; NM_001291778.1. [Q8CE90-3]
RefSeq; NP_001278712.1; NM_001291783.1. [Q8CE90-4]
RefSeq; NP_036074.2; NM_011944.3. [Q8CE90-2]
UniGene; Mm.3906; -.
ProteinModelPortal; Q8CE90; -.
SMR; Q8CE90; -.
BioGrid; 204954; 9.
CORUM; Q8CE90; -.
IntAct; Q8CE90; 2.
STRING; 10090.ENSMUSP00000003027; -.
iPTMnet; Q8CE90; -.
PhosphoSitePlus; Q8CE90; -.
PaxDb; Q8CE90; -.
PeptideAtlas; Q8CE90; -.
PRIDE; Q8CE90; -.
Ensembl; ENSMUST00000003027; ENSMUSP00000003027; ENSMUSG00000002948. [Q8CE90-7]
Ensembl; ENSMUST00000062686; ENSMUSP00000054512; ENSMUSG00000002948. [Q8CE90-6]
Ensembl; ENSMUST00000110994; ENSMUSP00000106622; ENSMUSG00000002948. [Q8CE90-4]
Ensembl; ENSMUST00000110995; ENSMUSP00000106623; ENSMUSG00000002948. [Q8CE90-3]
Ensembl; ENSMUST00000110996; ENSMUSP00000106624; ENSMUSG00000002948. [Q8CE90-5]
Ensembl; ENSMUST00000110998; ENSMUSP00000106626; ENSMUSG00000002948. [Q8CE90-2]
Ensembl; ENSMUST00000110999; ENSMUSP00000106627; ENSMUSG00000002948. [Q8CE90-8]
Ensembl; ENSMUST00000145165; ENSMUSP00000117418; ENSMUSG00000109061. [Q8CE90-1]
GeneID; 26400; -.
KEGG; mmu:26400; -.
UCSC; uc009kti.2; mouse. [Q8CE90-2]
UCSC; uc009ktj.2; mouse. [Q8CE90-6]
UCSC; uc009ktk.2; mouse. [Q8CE90-7]
UCSC; uc009ktm.2; mouse. [Q8CE90-4]
UCSC; uc009ktn.2; mouse. [Q8CE90-5]
UCSC; uc057ake.1; mouse. [Q8CE90-8]
UCSC; uc057akf.1; mouse. [Q8CE90-3]
CTD; 5609; -.
MGI; MGI:1346871; Map2k7.
eggNOG; KOG0983; Eukaryota.
eggNOG; ENOG410XTNQ; LUCA.
GeneTree; ENSGT00760000119199; -.
HOVERGEN; HBG108518; -.
InParanoid; Q8CE90; -.
KO; K04431; -.
OMA; HIVYSAI; -.
OrthoDB; EOG091G0A9H; -.
PhylomeDB; Q8CE90; -.
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.
ChiTaRS; Map2k7; mouse.
PRO; PR:Q8CE90; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000002948; -.
CleanEx; MM_MAP2K7; -.
ExpressionAtlas; Q8CE90; baseline and differential.
Genevisible; Q8CE90; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0008545; F:JUN kinase kinase activity; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0004708; F:MAP kinase kinase activity; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0019903; F:protein phosphatase binding; IPI: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:0016909; F:SAP kinase activity; IDA:UniProtKB.
GO; GO:0007257; P:activation of JUN kinase activity; IDA:BHF-UCL.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0071347; P:cellular response to interleukin-1; IMP:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:UniProtKB.
GO; GO:0046330; P:positive regulation of JNK cascade; IDA:UniProtKB.
GO; GO:0051973; P:positive regulation of telomerase activity; ISO:MGI.
GO; GO:1904355; P:positive regulation of telomere capping; ISO:MGI.
GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:MGI.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:2000671; P:regulation of motor neuron apoptotic process; IMP:MGI.
GO; GO:0009408; P:response to heat; ISO:MGI.
GO; GO:0006970; P:response to osmotic stress; ISO:MGI.
GO; GO:0034612; P:response to tumor necrosis factor; ISO:MGI.
GO; GO:0009411; P:response to UV; ISO:MGI.
GO; GO:0009611; P:response to wounding; IMP:MGI.
GO; GO:0051403; P:stress-activated MAPK cascade; ISO:MGI.
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;
Acetylation; Alternative splicing; Apoptosis; ATP-binding;
Coiled coil; Complete proteome; Cytoplasm; Kinase; Magnesium;
Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Stress response;
Transferase; Tyrosine-protein kinase.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:O14733}.
CHAIN 2 535 Dual specificity mitogen-activated
protein kinase kinase 7.
/FTId=PRO_0000271406.
DOMAIN 136 396 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 142 150 ATP. {ECO:0000250|UniProtKB:Q13131,
ECO:0000255|PROSITE-ProRule:PRU00159}.
REGION 37 73 D domain. {ECO:0000250}.
REGION 393 416 DVD domain. {ECO:0000250}.
COILED 2 30 {ECO:0000255}.
ACT_SITE 259 259 Proton acceptor.
{ECO:0000250|UniProtKB:Q13131,
ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10027}.
BINDING 165 165 ATP. {ECO:0000250|UniProtKB:Q13131,
ECO:0000255|PROSITE-ProRule:PRU00159}.
SITE 60 61 Cleavage; by anthrax lethal factor.
{ECO:0000250}.
SITE 92 93 Cleavage; by anthrax lethal factor.
{ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:O14733}.
MOD_RES 287 287 Phosphoserine; by MAP3K. {ECO:0000250}.
MOD_RES 291 291 Phosphothreonine; by MAP3K.
{ECO:0000250}.
MOD_RES 427 427 Phosphoserine.
{ECO:0000250|UniProtKB:O14733}.
VAR_SEQ 1 89 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:9891090}.
/FTId=VSP_052265.
VAR_SEQ 1 45 Missing (in isoform 5).
{ECO:0000303|PubMed:9312105}.
/FTId=VSP_052264.
VAR_SEQ 42 58 IIVITLSPAPAPSQRAA -> T (in isoform 2 and
isoform 8). {ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:9312105,
ECO:0000303|PubMed:9891090}.
/FTId=VSP_052266.
VAR_SEQ 46 57 TLSPAPAPSQRA -> MLTPFMPLVFNSP (in isoform
5). {ECO:0000303|PubMed:9312105}.
/FTId=VSP_052267.
VAR_SEQ 435 435 S -> R (in isoform 2, isoform 4, isoform
5 and isoform 6).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:9312105,
ECO:0000303|PubMed:9405446,
ECO:0000303|PubMed:9891090}.
/FTId=VSP_052268.
VAR_SEQ 436 535 Missing (in isoform 2, isoform 4, isoform
5 and isoform 6).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:9312105,
ECO:0000303|PubMed:9405446,
ECO:0000303|PubMed:9891090}.
/FTId=VSP_052269.
VAR_SEQ 436 519 TSVTWGAWPLAAQTPFQSGVIRCRGRVPSPRRATGGSGGQP
CVCAGGPGPSFTEMGPSPSPMLSNTFFTPDPGACPGASTWG
LP -> GSLEESPTSPPSPKSFPLSPAIPQAQAEWVSGR
(in isoform 3, isoform 7 and isoform 8).
{ECO:0000303|PubMed:9384583,
ECO:0000303|PubMed:9891090}.
/FTId=VSP_052270.
VAR_SEQ 520 535 Missing (in isoform 3, isoform 7 and
isoform 8). {ECO:0000303|PubMed:9384583,
ECO:0000303|PubMed:9891090}.
/FTId=VSP_052271.
CONFLICT 47 47 L -> T (in Ref. 5; AAB63448).
{ECO:0000305}.
CONFLICT 166 166 Q -> K (in Ref. 6; BAC27272).
{ECO:0000305}.
CONFLICT 211 211 A -> V (in Ref. 4; AAC16274).
{ECO:0000305}.
CONFLICT 217 217 T -> I (in Ref. 1; AAB81848).
{ECO:0000305}.
CONFLICT 396 396 I -> II (in Ref. 5; AAD15819/AAD15821/
AAD15823). {ECO:0000305}.
CONFLICT 418 418 E -> D (in Ref. 1; AAB81848).
{ECO:0000305}.
SEQUENCE 535 AA; 59312 MW; A96DA75565E3CD0F CRC64;
MAASSLEQKL SRLEAKLKQE NREARRRIDL NLDISPQRPR PIIVITLSPA PAPSQRAALQ
LPLANDGGSR SPSSESSPQH PTPPTRPRHM LGLPSTLFTP RSMESIEIDQ KLQEIMKQTG
YLTIGGQRYQ AEINDLENLG EMGSGTCGQV WKMRFRKTGH IIAVKQMRRS GNKEENKRIL
MDLDVVLKSH DCPYIVQCFG TFITNTDVFI AMELMGTCAE KLKKRMQGPI PERILGKMTV
AIVKALYYLK EKHGVIHRDV KPSNILLDER GQIKLCDFGI SGRLVDSKAK TRSAGCAAYM
APERIDPPDP TKPDYDIRAD VWSLGISLVE LATGQFPYKN CKTDFEVLTK VLQEEPPLLP
GHMGFSGDFQ SFVKDCLTKD HRKRPKYNKL LEHSFIKHYE ILEVDVASWF KDVMAKTESP
RTSGVLSQHH LPFFSTSVTW GAWPLAAQTP FQSGVIRCRG RVPSPRRATG GSGGQPCVCA
GGPGPSFTEM GPSPSPMLSN TFFTPDPGAC PGASTWGLPR RRLCQLLTTS TPGCC


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