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O14733

- MP2K7_HUMAN

UniProt

O14733 - MP2K7_HUMAN

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Protein

Dual specificity mitogen-activated protein kinase kinase 7

Gene
MAP2K7, JNKK2, MEK7, MKK7, PRKMK7, SKK4
Organism
Homo sapiens (Human)
Status
Reviewed - 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.4 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium.

Enzyme regulationi

Activated by phosphorylation by specific MAP kinase kinase kinases such as MAP3K1/MEKK1, MAP3K3/MEKK3, MAP3K11/MLK3 and MAP3K12/DLK.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei44 – 452Cleavage; by anthrax lethal factor
Sitei76 – 772Cleavage; by anthrax lethal factor
Binding sitei149 – 1491ATP By similarity
Active sitei243 – 2431Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi126 – 1349ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. JUN kinase kinase activity Source: Ensembl
  3. magnesium ion binding Source: UniProtKB
  4. MAP kinase kinase activity Source: UniProtKB
  5. protein binding Source: IntAct
  6. protein kinase binding Source: UniProtKB
  7. protein phosphatase binding Source: BHF-UCL
  8. protein serine/threonine kinase activity Source: UniProtKB-KW
  9. protein tyrosine kinase activity Source: UniProtKB-KW

GO - Biological processi

  1. activation of JUN kinase activity Source: BHF-UCL
  2. apoptotic process Source: UniProtKB-KW
  3. cellular response to sorbitol Source: Ensembl
  4. Fc-epsilon receptor signaling pathway Source: Reactome
  5. innate immune response Source: Reactome
  6. JNK cascade Source: Reactome
  7. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
  8. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  9. positive regulation of neuron apoptotic process Source: Ensembl
  10. response to stress Source: UniProtKB
  11. signal transduction Source: ProtInc
  12. stress-activated MAPK cascade Source: UniProtKB
  13. toll-like receptor 10 signaling pathway Source: Reactome
  14. toll-like receptor 2 signaling pathway Source: Reactome
  15. toll-like receptor 3 signaling pathway Source: Reactome
  16. toll-like receptor 4 signaling pathway Source: Reactome
  17. toll-like receptor 5 signaling pathway Source: Reactome
  18. toll-like receptor 9 signaling pathway Source: Reactome
  19. toll-like receptor signaling pathway Source: Reactome
  20. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
  21. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
  22. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
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. 2681.
ReactomeiREACT_163701. FCERI mediated MAPK activation.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_21368. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
SignaLinkiO14733.

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
Stress-activated protein kinase kinase 4
Short name:
SAPK kinase 4
Short name:
SAPKK-4
Short name:
SAPKK4
c-Jun N-terminal kinase kinase 2
Short name:
JNK kinase 2
Short name:
JNKK 2
Gene namesi
Name:MAP2K7
Synonyms:JNKK2, MEK7, MKK7, PRKMK7, SKK4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:6847. MAP2K7.

Subcellular locationi

Nucleus. Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA284.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 419418Dual specificity mitogen-activated protein kinase kinase 7PRO_0000086388Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei271 – 2711Phosphoserine; by MAP3K By similarity
Modified residuei275 – 2751Phosphothreonine; by MAP3K By similarity

Post-translational modificationi

Activated by phosphorylation on Ser-271 and Thr-275 by MAP kinase kinase kinases (MAP3Ks) By similarity.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO14733.
PaxDbiO14733.
PRIDEiO14733.

PTM databases

PhosphoSiteiO14733.

Miscellaneous databases

PMAP-CutDBO14733.

Expressioni

Tissue specificityi

Ubiquitous; with highest level of expression in skeletal muscle. Isoform 3 is found at low levels in placenta, fetal liver, and skeletal muscle.3 Publications

Gene expression databases

ArrayExpressiO14733.
BgeeiO14733.
CleanExiHS_MAP2K7.
GenevestigatoriO14733.

Organism-specific databases

HPAiCAB004262.
HPA001633.

Interactioni

Subunit structurei

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.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CFLARO15519-12EBI-492605,EBI-4567563
LRRK2Q5S0073EBI-492605,EBI-5323863
MAP3K7O433182EBI-492605,EBI-358684
MAPK8P459833EBI-492627,EBI-286483
MAPK8IP1Q9UQF25EBI-492605,EBI-78404

Protein-protein interaction databases

BioGridi111595. 34 interactions.
IntActiO14733. 18 interactions.
MINTiMINT-1378223.
STRINGi9606.ENSP00000381066.

Structurei

Secondary structure

1
419
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi105 – 11410
Helixi117 – 1193
Beta strandi120 – 1256
Beta strandi134 – 1396
Turni140 – 1423
Beta strandi145 – 1528
Helixi157 – 17216
Turni173 – 1753
Beta strandi182 – 1876
Beta strandi189 – 1968
Beta strandi200 – 2023
Helixi203 – 2108
Helixi216 – 23722
Helixi246 – 2483
Beta strandi249 – 2513
Beta strandi257 – 2593
Helixi286 – 2894
Helixi302 – 31716
Turni321 – 3244
Helixi328 – 33710
Beta strandi345 – 3473
Helixi351 – 36010
Turni365 – 3673
Helixi371 – 3744
Helixi378 – 3858
Helixi390 – 39910

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DYLX-ray2.45A101-405[»]
ProteinModelPortaliO14733.
SMRiO14733. Positions 53-402.

Miscellaneous databases

EvolutionaryTraceiO14733.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini120 – 380261Protein kinaseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni37 – 5721D domain By similarityAdd
BLAST
Regioni377 – 40024DVD domainAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili2 – 3029 Reviewed predictionAdd
BLAST

Domaini

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.1 Publication
The D domain (residues 37-57) contains a conserved docking site and is required for the binding to MAPK substrates.1 Publication

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG0515.
HOVERGENiHBG108518.
KOiK04431.
OrthoDBiEOG7J9VPW.
PhylomeDBiO14733.
TreeFamiTF350701.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_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 (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O14733-1) [UniParc]FASTAAdd to Basket

Also known as: A

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

MAASSLEQKL SRLEAKLKQE NREARRRIDL NLDISPQRPR PTLQLPLAND    50
GGSRSPSSES SPQHPTPPAR PRHMLGLPST LFTPRSMESI EIDQKLQEIM 100
KQTGYLTIGG QRYQAEINDL ENLGEMGSGT CGQVWKMRFR KTGHVIAVKQ 150
MRRSGNKEEN KRILMDLDVV LKSHDCPYIV QCFGTFITNT DVFIAMELMG 200
TCAEKLKKRM QGPIPERILG KMTVAIVKAL YYLKEKHGVI HRDVKPSNIL 250
LDERGQIKLC DFGISGRLVD SKAKTRSAGC AAYMAPERID PPDPTKPDYD 300
IRADVWSLGI SLVELATGQF PYKNCKTDFE VLTKVLQEEP PLLPGHMGFS 350
GDFQSFVKDC LTKDHRKRPK YNKLLEHSFI KRYETLEVDV ASWFKDVMAK 400
TESPRTSGVL SQPHLPFFR 419
Length:419
Mass (Da):47,485
Last modified:May 30, 2000 - v2
Checksum:iF1B22E050F54299A
GO
Isoform 2 (identifier: O14733-2) [UniParc]FASTAAdd to Basket

Also known as: B

The sequence of this isoform differs from the canonical sequence as follows:
     111-111: Q → QVPPSLWRGEGGGPARLDPSWERQWGAGGGGRAPGTLQPSLSSQ

Note: May be due to intron retention.

Show »
Length:462
Mass (Da):51,881
Checksum:iDF3496066961B0C7
GO
Isoform 3 (identifier: O14733-3) [UniParc]FASTAAdd to Basket

Also known as: gamma1

The sequence of this isoform differs from the canonical sequence as follows:
     42-42: T → IIVITLSPAPAPSQRAA

Show »
Length:435
Mass (Da):49,071
Checksum:i8812A87DB28F2C22
GO
Isoform 4 (identifier: O14733-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     312-312: L → LPCPSPSQ

Note: No experimental confirmation available.

Show »
Length:426
Mass (Da):48,182
Checksum:i7934E29217D8A137
GO

Sequence cautioni

The sequence AAB97813.1 differs from that shown. Reason: Frameshift at positions 402 and 410.
The sequence AAB97813.1 differs from that shown. Reason: Erroneous termination at position 420. Translated as stop.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti118 – 1181N → S.1 Publication
Corresponds to variant rs56316660 [ dbSNP | Ensembl ].
VAR_040825
Natural varianti138 – 1381R → C.1 Publication
Corresponds to variant rs56106612 [ dbSNP | Ensembl ].
VAR_040826
Natural varianti162 – 1621R → C in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
VAR_040827
Natural varianti162 – 1621R → H in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
VAR_040828
Natural varianti195 – 1951A → T.1 Publication
Corresponds to variant rs55800262 [ dbSNP | Ensembl ].
VAR_040829
Natural varianti259 – 2591L → F.1 Publication
Corresponds to variant rs1053566 [ dbSNP | Ensembl ].
VAR_029890

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei42 – 421T → IIVITLSPAPAPSQRAA in isoform 3. VSP_022309
Alternative sequencei111 – 1111Q → QVPPSLWRGEGGGPARLDPS WERQWGAGGGGRAPGTLQPS LSSQ in isoform 2. VSP_004883
Alternative sequencei312 – 3121L → LPCPSPSQ in isoform 4. VSP_022310

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 941Q → H in AAB97813. 1 Publication
Sequence conflicti106 – 1061L → P in ABE03013. 1 Publication
Sequence conflicti133 – 1331Q → P in AAB97813. 1 Publication
Sequence conflicti142 – 1421T → N in AAB88048. 1 Publication
Sequence conflicti407 – 4071S → N in AAB97813. 1 Publication
Sequence conflicti415 – 4151L → LG in AAB97813. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF014401 mRNA. Translation: AAB88048.1.
AF006689 mRNA. Translation: AAB97813.1. Sequence problems.
AF013588 mRNA. Translation: AAC16272.1.
AF013589 mRNA. Translation: AAC16273.1.
DQ445915 mRNA. Translation: ABE03013.1.
AF022805 mRNA. Translation: AAC26142.1.
AK313899 mRNA. Translation: BAG36622.1.
CH471139 Genomic DNA. Translation: EAW68964.1.
CH471139 Genomic DNA. Translation: EAW68968.1.
BC038295 mRNA. Translation: AAH38295.1.
AF003199 mRNA. Translation: AAB63374.1.
CCDSiCCDS42491.1. [O14733-1]
RefSeqiNP_660186.1. NM_145185.2. [O14733-1]
XP_005272546.1. XM_005272489.1. [O14733-3]
XP_005272547.1. XM_005272490.1. [O14733-4]
UniGeneiHs.531754.

Genome annotation databases

EnsembliENST00000397979; ENSP00000381066; ENSG00000076984. [O14733-1]
ENST00000397981; ENSP00000381068; ENSG00000076984. [O14733-4]
ENST00000397983; ENSP00000381070; ENSG00000076984. [O14733-3]
GeneIDi5609.
KEGGihsa:5609.
UCSCiuc002mit.3. human. [O14733-1]
uc002miv.2. human. [O14733-4]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF014401 mRNA. Translation: AAB88048.1 .
AF006689 mRNA. Translation: AAB97813.1 . Sequence problems.
AF013588 mRNA. Translation: AAC16272.1 .
AF013589 mRNA. Translation: AAC16273.1 .
DQ445915 mRNA. Translation: ABE03013.1 .
AF022805 mRNA. Translation: AAC26142.1 .
AK313899 mRNA. Translation: BAG36622.1 .
CH471139 Genomic DNA. Translation: EAW68964.1 .
CH471139 Genomic DNA. Translation: EAW68968.1 .
BC038295 mRNA. Translation: AAH38295.1 .
AF003199 mRNA. Translation: AAB63374.1 .
CCDSi CCDS42491.1. [O14733-1 ]
RefSeqi NP_660186.1. NM_145185.2. [O14733-1 ]
XP_005272546.1. XM_005272489.1. [O14733-3 ]
XP_005272547.1. XM_005272490.1. [O14733-4 ]
UniGenei Hs.531754.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DYL X-ray 2.45 A 101-405 [» ]
ProteinModelPortali O14733.
SMRi O14733. Positions 53-402.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111595. 34 interactions.
IntActi O14733. 18 interactions.
MINTi MINT-1378223.
STRINGi 9606.ENSP00000381066.

Chemistry

BindingDBi O14733.
ChEMBLi CHEMBL3530.
DrugBanki DB00773. Etoposide.
GuidetoPHARMACOLOGYi 2068.

PTM databases

PhosphoSitei O14733.

Proteomic databases

MaxQBi O14733.
PaxDbi O14733.
PRIDEi O14733.

Protocols and materials databases

DNASUi 5609.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000397979 ; ENSP00000381066 ; ENSG00000076984 . [O14733-1 ]
ENST00000397981 ; ENSP00000381068 ; ENSG00000076984 . [O14733-4 ]
ENST00000397983 ; ENSP00000381070 ; ENSG00000076984 . [O14733-3 ]
GeneIDi 5609.
KEGGi hsa:5609.
UCSCi uc002mit.3. human. [O14733-1 ]
uc002miv.2. human. [O14733-4 ]

Organism-specific databases

CTDi 5609.
GeneCardsi GC19P007968.
HGNCi HGNC:6847. MAP2K7.
HPAi CAB004262.
HPA001633.
MIMi 603014. gene.
neXtProti NX_O14733.
PharmGKBi PA284.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOVERGENi HBG108518.
KOi K04431.
OrthoDBi EOG7J9VPW.
PhylomeDBi O14733.
TreeFami TF350701.

Enzyme and pathway databases

BRENDAi 2.7.12.2. 2681.
Reactomei REACT_163701. FCERI mediated MAPK activation.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_21368. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
SignaLinki O14733.

Miscellaneous databases

EvolutionaryTracei O14733.
GeneWikii MAP2K7.
GenomeRNAii 5609.
NextBioi 21802.
PMAP-CutDB O14733.
PROi O14733.
SOURCEi Search...

Gene expression databases

ArrayExpressi O14733.
Bgeei O14733.
CleanExi HS_MAP2K7.
Genevestigatori O14733.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of human JNKK2, a novel jun NH2-terminal kinase-specific kinase."
    Wu Z., Wu J., Jacinto E., Karin M.
    Mol. Cell. Biol. 17:7407-7416(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
    Tissue: Heart and Skeletal muscle.
  2. "Identification of c-Jun NH2-terminal protein kinase (JNK)-activating kinase 2 as an activator of JNK but not p38."
    Lu X., Nemoto S., Lin A.
    J. Biol. Chem. 272:24751-24754(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION.
  3. "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] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY, VARIANT PHE-259.
    Tissue: Fetal kidney.
  4. "Cloning and expression of human mitogen-activated protein kinase kinase 7gamma1."
    Michael L., Swantek J., Robinson M.J.
    Biochem. Biophys. Res. Commun. 341:679-683(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ENZYME REGULATION, TISSUE SPECIFICITY.
  5. "Molecular cloning of human JNKK2 reveals a novel kinase module for c-Jun N-terminal kinase activation."
    Yang J., New L., Yong J., Han J., Su B.
    Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN PHOSPHORYLATION OF MAPK8/JNK1 AND MAPK9/JNK2.
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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 4).
    Tissue: Testis.
  9. "Mitogen-activated protein kinase kinase 7 is an activator of the c-Jun NH2-terminal kinase."
    Tournier C., Whitmarsh A.J., Cavanagh J., Barrett T., Davis R.J.
    Proc. Natl. Acad. Sci. U.S.A. 94:7337-7342(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-260 (ISOFORMS 1/4).
  10. "The JIP group of mitogen-activated protein kinase scaffold proteins."
    Yasuda J., Whitmarsh A.J., Cavanagh J., Sharma M., Davis R.J.
    Mol. Cell. Biol. 19:7245-7254(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAPK8IP1/JIP1 AND MAPK8IP2/JIP2.
  11. "Susceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factor."
    Vitale G., Bernardi L., Napolitani G., Mock M., Montecucco C.
    Biochem. J. 352:739-745(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE BY ANTHRAX LETHAL FACTOR.
  12. "Phosphorylation-dependent scaffolding role of JSAP1/JIP3 in the ASK1-JNK signaling pathway. A new mode of regulation of the MAP kinase cascade."
    Matsuura H., Nishitoh H., Takeda K., Matsuzawa A., Amagasa T., Ito M., Yoshioka K., Ichijo H.
    J. Biol. Chem. 277:40703-40709(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAPK8IP3/JIP3.
  13. "Conserved docking site is essential for activation of mammalian MAP kinase kinases by specific MAP kinase kinase kinases."
    Takekawa M., Tatebayashi K., Saito H.
    Mol. Cell 18:295-306(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN.
  14. "Modulation of interleukin-1 transcriptional response by the interaction between VRK2 and the JIP1 scaffold protein."
    Blanco S., Sanz-Garcia M., Santos C.R., Lazo P.A.
    PLoS ONE 3:E1660-E1660(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VRK2.
  15. "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.
  16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  17. "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.
  18. "RASSF7 negatively regulates pro-apoptotic JNK signaling by inhibiting the activity of phosphorylated-MKK7."
    Takahashi S., Ebihara A., Kajiho H., Kontani K., Nishina H., Katada T.
    Cell Death Differ. 18:645-655(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RASSF7.
  19. "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.
  20. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Crystal structure of human mitogen-activated protein kinase kinase 7 activated mutant (s287d, t291d)."
    RIKEN structural genomics initiative (RSGI)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 101-405.
  22. "Patterns of somatic mutation in human cancer genomes."
    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.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-118; CYS-138; CYS-162; HIS-162 AND THR-195.

Entry informationi

Entry nameiMP2K7_HUMAN
AccessioniPrimary (citable) accession number: O14733
Secondary accession number(s): B2R9S5
, D6W659, O14648, O14816, O60452, O60453, Q1PG43, Q8IY10
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: September 3, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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