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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_RAT               Reviewed;         419 AA.
Q4KSH7;
09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
02-AUG-2005, sequence version 1.
12-SEP-2018, entry version 107.
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|EMBL:AAX61178.1};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1] {ECO:0000312|EMBL:AAX61178.1}
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAX61178.1};
Itoh T., Horiuchi M., Itoh A.;
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000305}
FUNCTION.
PubMed=10051439; DOI=10.1042/bj3380681;
Butterfield L., Zentrich E., Beekman A., Heasley L.E.;
"Stress- and cell type-dependent regulation of transfected c-Jun N-
terminal kinase and mitogen-activated protein kinase kinase
isoforms.";
Biochem. J. 338:681-686(1999).
[3]
PHOSPHORYLATION, AND INTERACTION WITH MAPK8/JNK1; MAPK9/JNK2;
MAPK10/JNK3; MAP3K11/MLK3 AND MAP3K5/ASK1.
PubMed=14575811; DOI=10.1016/j.lfs.2003.06.025;
Zhang Q., Tian H., Fu X., Zhang G.;
"Delayed activation and regulation of MKK7 in hippocampal CA1 region
following global cerebral ischemia in rats.";
Life Sci. 74:37-45(2003).
[4]
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).
[5]
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).
[6]
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:10051439}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:10051439}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:10051439};
-!- ACTIVITY REGULATION: Activated by phosphorylation by specific MAP
kinase kinase kinases such as MAP3K1/MEKK1, MAP3K3/MEKK3,
MAP3K11/MLK3 and MAP3K12/DLK.
-!- SUBUNIT: Interacts with VRK2 (By similarity). Interacts (via its D
domain) with its substrates MAPK8/JNK1, MAPK9/JNK2 and
MAPK10/JNK3. Interacts (via its DVD domain) with MAP3Ks activators
like MAP3K5/ASK1 and MAP3K1/MEKK1. 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:O14733, ECO:0000250|UniProtKB:Q8CE90}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8CE90}.
Cytoplasm {ECO:0000250|UniProtKB:Q8CE90}.
-!- 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.
-!- DOMAIN: The D domain (residues 37-57) contains a conserved docking
site and is required for the binding to MAPK substrates.
-!- PTM: Activated by phosphorylation on Ser-271 and Thr-275 by MAP
kinase kinase kinases (MAP3Ks). {ECO:0000269|PubMed:14575811}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AY879265; AAX61178.1; -; mRNA.
RefSeq; NP_001020596.1; NM_001025425.1.
UniGene; Rn.162081; -.
ProteinModelPortal; Q4KSH7; -.
SMR; Q4KSH7; -.
STRING; 10116.ENSRNOP00000058535; -.
PaxDb; Q4KSH7; -.
PeptideAtlas; Q4KSH7; -.
PRIDE; Q4KSH7; -.
Ensembl; ENSRNOT00000061821; ENSRNOP00000058535; ENSRNOG00000001047.
GeneID; 363855; -.
KEGG; rno:363855; -.
UCSC; RGD:1560043; rat.
CTD; 5609; -.
RGD; 1560043; Map2k7.
eggNOG; KOG0983; Eukaryota.
eggNOG; ENOG410XTNQ; LUCA.
GeneTree; ENSGT00760000119199; -.
HOGENOM; HOG000234206; -.
HOVERGEN; HBG108518; -.
InParanoid; Q4KSH7; -.
KO; K04431; -.
Reactome; R-RNO-2559580; Oxidative Stress Induced Senescence.
Reactome; R-RNO-2871796; FCERI mediated MAPK activation.
Reactome; R-RNO-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
PRO; PR:Q4KSH7; -.
Proteomes; UP000002494; Chromosome 12.
Bgee; ENSRNOG00000001047; Expressed in 9 organ(s), highest expression level in skeletal muscle tissue.
ExpressionAtlas; Q4KSH7; baseline and differential.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005524; F:ATP binding; IDA:RGD.
GO; GO:0008545; F:JUN kinase kinase activity; IDA:RGD.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0004708; F:MAP kinase kinase activity; IDA:UniProtKB.
GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IPI:RGD.
GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
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; IDA:RGD.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0072709; P:cellular response to sorbitol; IEP:RGD.
GO; GO:0007254; P:JNK cascade; IDA:RGD.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:RGD.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:RGD.
GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:0006970; P:response to osmotic stress; IDA:UniProtKB.
GO; GO:0051403; P:stress-activated MAPK cascade; IDA:UniProtKB.
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; 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 2 419 Dual specificity mitogen-activated
protein kinase kinase 7.
/FTId=PRO_0000271407.
DOMAIN 120 380 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 126 134 ATP. {ECO:0000250|UniProtKB:Q13131,
ECO:0000255|PROSITE-ProRule:PRU00159}.
REGION 37 57 D Domain. {ECO:0000250}.
REGION 377 400 DVD domain. {ECO:0000250}.
COILED 2 30 {ECO:0000255}.
ACT_SITE 243 243 Proton acceptor.
{ECO:0000250|UniProtKB:Q13131,
ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10027}.
BINDING 149 149 ATP. {ECO:0000250|UniProtKB:Q13131,
ECO:0000255|PROSITE-ProRule:PRU00159}.
SITE 44 45 Cleavage; by anthrax lethal factor.
{ECO:0000250}.
SITE 76 77 Cleavage; by anthrax lethal factor.
{ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:O14733}.
MOD_RES 271 271 Phosphoserine; by MAP3K. {ECO:0000250}.
MOD_RES 275 275 Phosphothreonine; by MAP3K.
{ECO:0000250}.
MOD_RES 411 411 Phosphoserine.
{ECO:0000250|UniProtKB:O14733}.
SEQUENCE 419 AA; 47536 MW; 60405BF7111E294B CRC64;
MAASSLEQKL SRLEAKLKQE NREARRRIDL NLDISPQRPR PTLQLPLAND GGSRSPSSES
SPQHPTPPSR PRHMLGLPST LFTPRSMESI EIDQKLQEIM KQTGYLTIGG QRYQAEINDL
ENLGEMGSGT CGQVWKMRFR KTGHIIAVKQ MRRSGNKEEN KRILMDLDVV LKSHDCPYIV
QCFGTFITNT DVFIAMELMG TCAEKLKKRM QGPIPERILG KMTVAIVKAL YYLKEKHGVI
HRDVKPSNIL LDERGQIKLC DFGISGRLVD SKAKTRSAGC AAYMAPERID PPDPTKPDYD
IRADVWSLGI SLVELATGQF PYKNCKTDFE VLTKVLQEEP PLLPGHMGFS GDFQSFVKDC
LTKDHRKRPK YNKLLEHSFI KHYETLEVDV ASWFKDVMAK TESPRTSGVL SQHHLPFFR


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