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Protein

Dual specificity mitogen-activated protein kinase kinase 7

Gene

Map2k7

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.7 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.2 Publications

Cofactori

Mg2+2 Publications

Enzyme regulationi

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 8.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei165 – 1651ATPPROSITE-ProRule annotationBy similarity
Active sitei259 – 2591Proton acceptorPROSITE-ProRule annotationBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi142 – 1509ATPPROSITE-ProRule annotationBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • enzyme binding Source: MGI
  • magnesium ion binding Source: UniProtKB
  • MAP kinase kinase activity Source: UniProtKB
  • protein kinase binding Source: MGI
  • protein phosphatase binding Source: BHF-UCL
  • protein serine/threonine kinase activity Source: UniProtKB-KW
  • protein tyrosine kinase activity Source: UniProtKB-KW

GO - Biological processi

  • activation of JUN kinase activity Source: BHF-UCL
  • apoptotic process Source: UniProtKB-KW
  • positive regulation of telomerase activity Source: MGI
  • positive regulation of telomere capping Source: MGI
  • positive regulation of telomere maintenance via telomerase Source: MGI
  • regulation of motor neuron apoptotic process Source: MGI
  • response to heat Source: MGI
  • response to osmotic stress Source: MGI
  • response to stress Source: UniProtKB
  • response to tumor necrosis factor Source: MGI
  • response to UV Source: MGI
  • response to wounding Source: MGI
  • stress-activated MAPK cascade Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Apoptosis, Stress response

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.12.2. 3474.
ReactomeiR-MMU-2559580. Oxidative Stress Induced Senescence.
R-MMU-2871796. FCERI mediated MAPK activation.
R-MMU-450321. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity mitogen-activated protein kinase kinase 7 (EC:2.7.12.2)
Short name:
MAP kinase kinase 7
Short name:
MAPKK 7
Alternative name(s):
JNK-activating kinase 2
MAPK/ERK kinase 7
Short name:
MEK 7
c-Jun N-terminal kinase kinase 2
Short name:
JNK kinase 2
Short name:
JNKK 2
Gene namesi
Name:Map2k7Imported
Synonyms:Mkk7Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1346871. Map2k7.

Subcellular locationi

  • Nucleus 1 Publication
  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 535534Dual specificity mitogen-activated protein kinase kinase 7PRO_0000271406Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei287 – 2871Phosphoserine; by MAP3KBy similarity
Modified residuei291 – 2911Phosphothreonine; by MAP3KBy similarity

Post-translational modificationi

Activated by phosphorylation on Ser-287 and Thr-291 by MAP kinase kinase kinases (MAP3Ks).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei60 – 612Cleavage; by anthrax lethal factorBy similarity
Sitei92 – 932Cleavage; by anthrax lethal factorBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8CE90.
MaxQBiQ8CE90.
PaxDbiQ8CE90.
PRIDEiQ8CE90.

PTM databases

iPTMnetiQ8CE90.
PhosphoSiteiQ8CE90.

Expressioni

Tissue specificityi

Expressed at high levels in brain, lung, liver, skeletal muscle, kidney, and testis and at lower levels in the heart and spleen.3 Publications

Developmental stagei

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.1 Publication

Gene expression databases

BgeeiQ8CE90.
CleanExiMM_MAP2K7.
GenevisibleiQ8CE90. MM.

Interactioni

Subunit structurei

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.By similarity2 Publications

GO - Molecular functioni

  • enzyme binding Source: MGI
  • protein kinase binding Source: MGI
  • protein phosphatase binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi204954. 8 interactions.
IntActiQ8CE90. 2 interactions.
STRINGi10090.ENSMUSP00000003027.

Structurei

3D structure databases

ProteinModelPortaliQ8CE90.
SMRiQ8CE90. Positions 80-418.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini136 – 396261Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni37 – 7337D domainBy similarityAdd
BLAST
Regioni393 – 41624DVD domainBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili2 – 3029Sequence analysisAdd
BLAST

Domaini

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.
The D domain (residues 37-73) contains a conserved docking site and is required for the binding to MAPK substrates.

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0983. Eukaryota.
ENOG410XTNQ. LUCA.
GeneTreeiENSGT00760000119199.
HOVERGENiHBG108518.
InParanoidiQ8CE90.
KOiK04431.
OMAiHPVIVIT.
OrthoDBiEOG7J9VPW.
PhylomeDBiQ8CE90.
TreeFamiTF350701.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (8)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 8 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 11 Publication (identifier: Q8CE90-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAASSLEQKL SRLEAKLKQE NREARRRIDL NLDISPQRPR PIIVITLSPA
60 70 80 90 100
PAPSQRAALQ LPLANDGGSR SPSSESSPQH PTPPTRPRHM LGLPSTLFTP
110 120 130 140 150
RSMESIEIDQ KLQEIMKQTG YLTIGGQRYQ AEINDLENLG EMGSGTCGQV
160 170 180 190 200
WKMRFRKTGH IIAVKQMRRS GNKEENKRIL MDLDVVLKSH DCPYIVQCFG
210 220 230 240 250
TFITNTDVFI AMELMGTCAE KLKKRMQGPI PERILGKMTV AIVKALYYLK
260 270 280 290 300
EKHGVIHRDV KPSNILLDER GQIKLCDFGI SGRLVDSKAK TRSAGCAAYM
310 320 330 340 350
APERIDPPDP TKPDYDIRAD VWSLGISLVE LATGQFPYKN CKTDFEVLTK
360 370 380 390 400
VLQEEPPLLP GHMGFSGDFQ SFVKDCLTKD HRKRPKYNKL LEHSFIKHYE
410 420 430 440 450
ILEVDVASWF KDVMAKTESP RTSGVLSQHH LPFFSTSVTW GAWPLAAQTP
460 470 480 490 500
FQSGVIRCRG RVPSPRRATG GSGGQPCVCA GGPGPSFTEM GPSPSPMLSN
510 520 530
TFFTPDPGAC PGASTWGLPR RRLCQLLTTS TPGCC
Note: No experimental confirmation available.Curated
Length:535
Mass (Da):59,312
Last modified:March 1, 2003 - v1
Checksum:iA96DA75565E3CD0F
GO
Isoform 23 Publications (identifier: Q8CE90-2) [UniParc]FASTAAdd to basket

Also known as: a1 Publication

, beta 11 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     42-58: IIVITLSPAPAPSQRAA → T
     435-435: S → R
     436-535: Missing.

Show »
Length:419
Mass (Da):47,562
Checksum:iB12F5CE8364CE6F5
GO
Isoform 32 Publications (identifier: Q8CE90-3) [UniParc]FASTAAdd to basket

Also known as: alpha 21 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-89: Missing.
     436-519: TSVTWGAWPL...CPGASTWGLP → GSLEESPTSPPSPKSFPLSPAIPQAQAEWVSGR
     520-535: Missing.

Show »
Length:379
Mass (Da):42,725
Checksum:iD7CFD1B827C90015
GO
Isoform 41 Publication (identifier: Q8CE90-4) [UniParc]FASTAAdd to basket

Also known as: alpha 11 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-89: Missing.
     435-435: S → R
     436-535: Missing.

Show »
Length:346
Mass (Da):39,377
Checksum:i15A41F9077C40EAB
GO
Isoform 51 Publication (identifier: Q8CE90-5) [UniParc]FASTAAdd to basket

Also known as: b1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-45: Missing.
     46-57: TLSPAPAPSQRA → MLTPFMPLVFNSP
     435-435: S → R
     436-535: Missing.

Note: No experimental confirmation available.Curated
Show »
Length:391
Mass (Da):44,210
Checksum:i0ABA468DBB8255F7
GO
Isoform 63 Publications (identifier: Q8CE90-6) [UniParc]FASTAAdd to basket

Also known as: b1 Publication

, gamma 11 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     435-435: S → R
     436-535: Missing.

Show »
Length:435
Mass (Da):49,148
Checksum:iC88FDA908B97E34D
GO
Isoform 71 Publication (identifier: Q8CE90-7) [UniParc]FASTAAdd to basket

Also known as: gamma 21 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     436-519: TSVTWGAWPL...CPGASTWGLP → GSLEESPTSPPSPKSFPLSPAIPQAQAEWVSGR
     520-535: Missing.

Show »
Length:468
Mass (Da):52,497
Checksum:iA71A286EE0AF99FF
GO
Isoform 81 Publication (identifier: Q8CE90-8) [UniParc]FASTAAdd to basket

Also known as: beta 21 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     42-58: IIVITLSPAPAPSQRAA → T
     436-519: TSVTWGAWPL...CPGASTWGLP → GSLEESPTSPPSPKSFPLSPAIPQAQAEWVSGR
     520-535: Missing.

Show »
Length:452
Mass (Da):50,911
Checksum:i7243158357786C2A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti47 – 471L → T in AAB63448 (PubMed:9891090).Curated
Sequence conflicti166 – 1661Q → K in BAC27272 (PubMed:16141072).Curated
Sequence conflicti211 – 2111A → V in AAC16274 (PubMed:9535930).Curated
Sequence conflicti217 – 2171T → I in AAB81848 (PubMed:9405446).Curated
Sequence conflicti396 – 3961I → II in AAD15819 (PubMed:9891090).Curated
Sequence conflicti396 – 3961I → II in AAD15821 (PubMed:9891090).Curated
Sequence conflicti396 – 3961I → II in AAD15823 (PubMed:9891090).Curated
Sequence conflicti418 – 4181E → D in AAB81848 (PubMed:9405446).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8989Missing in isoform 3 and isoform 4. 1 PublicationVSP_052265Add
BLAST
Alternative sequencei1 – 4545Missing in isoform 5. 1 PublicationVSP_052264Add
BLAST
Alternative sequencei42 – 5817IIVIT…SQRAA → T in isoform 2 and isoform 8. 3 PublicationsVSP_052266Add
BLAST
Alternative sequencei46 – 5712TLSPA…PSQRA → MLTPFMPLVFNSP in isoform 5. 1 PublicationVSP_052267Add
BLAST
Alternative sequencei435 – 4351S → R in isoform 2, isoform 4, isoform 5 and isoform 6. 5 PublicationsVSP_052268
Alternative sequencei436 – 535100Missing in isoform 2, isoform 4, isoform 5 and isoform 6. 5 PublicationsVSP_052269Add
BLAST
Alternative sequencei436 – 51984TSVTW…TWGLP → GSLEESPTSPPSPKSFPLSP AIPQAQAEWVSGR in isoform 3, isoform 7 and isoform 8. 2 PublicationsVSP_052270Add
BLAST
Alternative sequencei520 – 53516Missing in isoform 3, isoform 7 and isoform 8. 2 PublicationsVSP_052271Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF026216 mRNA. Translation: AAB81848.1.
U74463 mRNA. Translation: AAC53364.1.
U74464 mRNA. Translation: AAC53365.1.
AB005654 mRNA. Translation: BAA24383.1.
AF022112 mRNA. Translation: AAC16274.1.
AF022113 mRNA. Translation: AAC16275.1.
U93030 mRNA. Translation: AAB63447.1.
U93031 Genomic DNA. Translation: AAB63448.1.
AF060943 mRNA. Translation: AAD15819.1.
AF060944 mRNA. Translation: AAD15820.1.
AF060945 mRNA. Translation: AAD15821.1.
AF060946 mRNA. Translation: AAD15822.1.
AF060947 mRNA. Translation: AAD15823.1.
AK028772 mRNA. Translation: BAC26111.1.
AK031137 mRNA. Translation: BAC27272.1.
AK165184 mRNA. Translation: BAE38066.1.
BC070467 mRNA. Translation: AAH70467.1.
CCDSiCCDS40208.1. [Q8CE90-7]
CCDS40209.1. [Q8CE90-2]
CCDS52474.1. [Q8CE90-6]
CCDS80852.1. [Q8CE90-8]
CCDS80853.1. [Q8CE90-3]
CCDS80854.1. [Q8CE90-4]
RefSeqiNP_001036022.1. NM_001042557.2. [Q8CE90-7]
NP_001157644.1. NM_001164172.1. [Q8CE90-6]
NP_001278706.1. NM_001291777.1. [Q8CE90-8]
NP_001278707.1. NM_001291778.1. [Q8CE90-3]
NP_001278712.1. NM_001291783.1. [Q8CE90-4]
NP_036074.2. NM_011944.3. [Q8CE90-2]
UniGeneiMm.3906.

Genome annotation databases

EnsembliENSMUST00000003027; ENSMUSP00000003027; ENSMUSG00000002948. [Q8CE90-7]
ENSMUST00000062686; ENSMUSP00000054512; ENSMUSG00000002948. [Q8CE90-6]
ENSMUST00000110994; ENSMUSP00000106622; ENSMUSG00000002948. [Q8CE90-4]
ENSMUST00000110995; ENSMUSP00000106623; ENSMUSG00000002948. [Q8CE90-3]
ENSMUST00000110996; ENSMUSP00000106624; ENSMUSG00000002948. [Q8CE90-5]
ENSMUST00000110998; ENSMUSP00000106626; ENSMUSG00000002948. [Q8CE90-2]
ENSMUST00000110999; ENSMUSP00000106627; ENSMUSG00000002948. [Q8CE90-8]
ENSMUST00000145165; ENSMUSP00000117418; ENSMUSG00000109061. [Q8CE90-1]
GeneIDi26400.
KEGGimmu:26400.
UCSCiuc009kti.2. mouse. [Q8CE90-2]
uc009ktj.2. mouse. [Q8CE90-6]
uc009ktk.2. mouse. [Q8CE90-7]
uc009ktm.2. mouse. [Q8CE90-4]
uc009ktn.2. mouse. [Q8CE90-5]
uc057ake.1. mouse. [Q8CE90-8]
uc057akf.1. mouse. [Q8CE90-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF026216 mRNA. Translation: AAB81848.1.
U74463 mRNA. Translation: AAC53364.1.
U74464 mRNA. Translation: AAC53365.1.
AB005654 mRNA. Translation: BAA24383.1.
AF022112 mRNA. Translation: AAC16274.1.
AF022113 mRNA. Translation: AAC16275.1.
U93030 mRNA. Translation: AAB63447.1.
U93031 Genomic DNA. Translation: AAB63448.1.
AF060943 mRNA. Translation: AAD15819.1.
AF060944 mRNA. Translation: AAD15820.1.
AF060945 mRNA. Translation: AAD15821.1.
AF060946 mRNA. Translation: AAD15822.1.
AF060947 mRNA. Translation: AAD15823.1.
AK028772 mRNA. Translation: BAC26111.1.
AK031137 mRNA. Translation: BAC27272.1.
AK165184 mRNA. Translation: BAE38066.1.
BC070467 mRNA. Translation: AAH70467.1.
CCDSiCCDS40208.1. [Q8CE90-7]
CCDS40209.1. [Q8CE90-2]
CCDS52474.1. [Q8CE90-6]
CCDS80852.1. [Q8CE90-8]
CCDS80853.1. [Q8CE90-3]
CCDS80854.1. [Q8CE90-4]
RefSeqiNP_001036022.1. NM_001042557.2. [Q8CE90-7]
NP_001157644.1. NM_001164172.1. [Q8CE90-6]
NP_001278706.1. NM_001291777.1. [Q8CE90-8]
NP_001278707.1. NM_001291778.1. [Q8CE90-3]
NP_001278712.1. NM_001291783.1. [Q8CE90-4]
NP_036074.2. NM_011944.3. [Q8CE90-2]
UniGeneiMm.3906.

3D structure databases

ProteinModelPortaliQ8CE90.
SMRiQ8CE90. Positions 80-418.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204954. 8 interactions.
IntActiQ8CE90. 2 interactions.
STRINGi10090.ENSMUSP00000003027.

PTM databases

iPTMnetiQ8CE90.
PhosphoSiteiQ8CE90.

Proteomic databases

EPDiQ8CE90.
MaxQBiQ8CE90.
PaxDbiQ8CE90.
PRIDEiQ8CE90.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000003027; ENSMUSP00000003027; ENSMUSG00000002948. [Q8CE90-7]
ENSMUST00000062686; ENSMUSP00000054512; ENSMUSG00000002948. [Q8CE90-6]
ENSMUST00000110994; ENSMUSP00000106622; ENSMUSG00000002948. [Q8CE90-4]
ENSMUST00000110995; ENSMUSP00000106623; ENSMUSG00000002948. [Q8CE90-3]
ENSMUST00000110996; ENSMUSP00000106624; ENSMUSG00000002948. [Q8CE90-5]
ENSMUST00000110998; ENSMUSP00000106626; ENSMUSG00000002948. [Q8CE90-2]
ENSMUST00000110999; ENSMUSP00000106627; ENSMUSG00000002948. [Q8CE90-8]
ENSMUST00000145165; ENSMUSP00000117418; ENSMUSG00000109061. [Q8CE90-1]
GeneIDi26400.
KEGGimmu:26400.
UCSCiuc009kti.2. mouse. [Q8CE90-2]
uc009ktj.2. mouse. [Q8CE90-6]
uc009ktk.2. mouse. [Q8CE90-7]
uc009ktm.2. mouse. [Q8CE90-4]
uc009ktn.2. mouse. [Q8CE90-5]
uc057ake.1. mouse. [Q8CE90-8]
uc057akf.1. mouse. [Q8CE90-3]

Organism-specific databases

CTDi5609.
MGIiMGI:1346871. Map2k7.

Phylogenomic databases

eggNOGiKOG0983. Eukaryota.
ENOG410XTNQ. LUCA.
GeneTreeiENSGT00760000119199.
HOVERGENiHBG108518.
InParanoidiQ8CE90.
KOiK04431.
OMAiHPVIVIT.
OrthoDBiEOG7J9VPW.
PhylomeDBiQ8CE90.
TreeFamiTF350701.

Enzyme and pathway databases

BRENDAi2.7.12.2. 3474.
ReactomeiR-MMU-2559580. Oxidative Stress Induced Senescence.
R-MMU-2871796. FCERI mediated MAPK activation.
R-MMU-450321. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.

Miscellaneous databases

ChiTaRSiMap2k7. mouse.
PROiQ8CE90.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CE90.
CleanExiMM_MAP2K7.
GenevisibleiQ8CE90. MM.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Activation of stress-activated protein kinases/c-Jun N-terminal protein kinases (SAPKs/JNKs) by a novel mitogen-activated protein kinase kinase (MKK7)."
    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.
    J. Biol. Chem. 272:32378-32383(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  2. "MKK7 is a stress-activated mitogen-activated protein kinase kinase functionally related to hemipterous."
    Holland P.M., Magali S., Campbell J.S., Noselli S., Cooper J.A.
    J. Biol. Chem. 272:24994-24998(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 5), FUNCTION, TISSUE SPECIFICITY.
  3. "A novel SAPK/JNK kinase, MKK7, stimulated by TNFalpha and cellular stresses."
    Moriguchi T., Toyoshima F., Masuyama N., Hanafusa H., Gotoh Y., Nishida E.
    EMBO J. 16:7045-7053(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), FUNCTION.
  4. "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."
    Foltz I.N., Gerl R.E., Wieler J.S., Luckach M., Salmon R.A., Schrader J.W.
    J. Biol. Chem. 273:9344-9351(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-311 (ISOFORMS 2/6), FUNCTION, TISSUE SPECIFICITY.
    Tissue: B-cellImported and ThymusImported.
  5. "The MKK7 gene encodes a group of c-Jun NH2-terminal kinase kinases."
    Tournier C., Whitmarsh A.J., Cavanagh J., Barrett T., Davis R.J.
    Mol. Cell. Biol. 19:1569-1581(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 6; 7 AND 8), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 47-535 (ISOFORM 6), FUNCTION, ENZYME REGULATION, PHOSPHORYLATION, SUBCELLULAR LOCATION.
    Strain: CD-1Imported.
    Tissue: TestisImported.
  6. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6JImported.
    Tissue: Fetal forelimbImported, FetusImported and SkinImported.
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
    Strain: C57BL/6JImported.
    Tissue: EyeImported.
  8. "A mammalian scaffold complex that selectively mediates MAP kinase activation."
    Whitmarsh A.J., Cavanagh J., Tournier C., Yasuda J., Davis R.J.
    Science 281:1671-1674(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAPK8IP1/JIP1.
  9. "Interaction of a mitogen-activated protein kinase signaling module with the neuronal protein JIP3."
    Kelkar N., Gupta S., Dickens M., Davis R.J.
    Mol. Cell. Biol. 20:1030-1043(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAPK8IP3/JIP3.
  10. "MKK7 is an essential component of the JNK signal transduction pathway activated by proinflammatory cytokines."
    Tournier C., Dong C., Turner T.K., Jones S.N., Flavell R.A., Davis R.J.
    Genes Dev. 15:1419-1426(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Different properties of SEK1 and MKK7 in dual phosphorylation of stress-induced activated protein kinase SAPK/JNK in embryonic stem cells."
    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.
    J. Biol. Chem. 278:16595-16601(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Differential regulation and properties of MAPKs."
    Raman M., Chen W., Cobb M.H.
    Oncogene 26:3100-3112(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON ENZYME REGULATION.
  13. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Diverse physiological functions of MKK4 and MKK7 during early embryogenesis."
    Asaoka Y., Nishina H.
    J. Biochem. 148:393-401(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  15. "The bottleneck of JNK signaling: molecular and functional characteristics of MKK4 and MKK7."
    Haeusgen W., Herdegen T., Waetzig V.
    Eur. J. Cell Biol. 90:536-544(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON REGULATION, REVIEW ON FUNCTION.

Entry informationi

Entry nameiMP2K7_MOUSE
AccessioniPrimary (citable) accession number: Q8CE90
Secondary accession number(s): O35406
, O35720, O35871, O35872, O54780, O70242, O70243, Q8BSP1, Q9QWG6, Q9R1Z3, Q9R1Z4, Q9R1Z5, Q9R1Z6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.