Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Dual specificity mitogen-activated protein kinase kinase 4  

UniProtKB / Swiss-Prot ID :  MP2K4_MOUSE

Gene Name (Synonyms) : 
Map2k4, Jnkk1, Mek4, Mkk4, Prkmk4, Sek1, Serk1, Skk1  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Cytoplasm. Nucleus. 

Protein 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 MAP2K7/MKK7, 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 shows preference for phosphorylation of the Tyr residue and MAP2K7/MKK7 for the Thr residue. The phosphorylation of the Thr residue by MAP2K7/MKK7 seems to be the prerequisite for JNK activation at least in response to proinflammatory cytokines, while other stimuli activate both MAP2K4/MKK4 and MAP2K7/MKK7 which synergistically phosphorylate JNKs. MAP2K4 is required for maintaining peripheral lymphoid homeostasis. The MKK/JNK signaling pathway is also involved in mitochondrial death signaling pathway, including the release cytochrome c, leading to apoptosis. Whereas MAP2K7/MKK7 exclusively activates JNKs, MAP2K4/MKK4 additionally activates the p38 MAPKs MAPK11, MAPK12, MAPK13 and MAPK14. 

Protein Sequence MAAPSPSGGGGSGGGGGTPGPIGPPASGHPAVSSMQGKRKALKLNFANPPVKSTARFTLNPNTTGVQNPH...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
78PhosphoserineLRTHSIESS
CCCCCCCCC
27.69Phosphositeplus
Link-
78PhosphoserineLRTHSIESS
CCCCCCCCC
27.69SysPTM
Link-
82PhosphoserineSIESSGKLK
CCCCCCCCC
27.44Phosphositeplus
Link-
88PhosphoserineKLKISPEQH
CCCCCCCCC
22.31Phosphositeplus
Link-
88PhosphoserineKLKISPEQH
CCCCCCCCC
22.31SysPTM
Link-
244S-nitrosocysteineNIKLCDFGI
CEEEEECEE
3.28dbSNO
Link-
255PhosphoserineQLVDSIAKT
EECCCCEEE
19.57PhosphoELM
Link-
255PhosphoserineQLVDSIAKT
EECCCCEEE
19.57Phosphositeplus
Link-
255PhosphoserineQLVDSIAKT
EECCCCEEE
19.57SysPTM
Link-
259PhosphothreonineSIAKTRDAG
CCEEEEEEE
25.43PhosphoELM
Link-
259PhosphothreonineSIAKTRDAG
CCEEEEEEE
25.43Phosphositeplus
Link-
389PhosphothreonineQMPATPSSP
CCCCCCCCC
20.17Phosphositeplus
Link-
392PhosphoserineATPSSPMYV
CCCCCCCCC
18.19Phosphositeplus
Link-
395PhosphotyrosineSSPMYVD
CCCCCCC
12.59Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures