O09110 · MP2K3_MOUSE
- ProteinDual specificity mitogen-activated protein kinase kinase 3
- GeneMap2k3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids347 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Dual specificity kinase. Is activated by cytokines and environmental stress in vivo. Catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in the MAP kinase p38. Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation of MAPK14.
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Activity regulation
Activated by dual phosphorylation on Ser-218 and Thr-222.
Features
Showing features for binding site, active site.
GO annotations
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDual specificity mitogen-activated protein kinase kinase 3
- EC number
- Short namesMAP kinase kinase 3; MAPKK 3
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionO09110
- Secondary accessions
Proteomes
Organism-specific databases
Phenotypes & Variants
Variants
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The viewer provides 15 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000086379 | 1-347 | Dual specificity mitogen-activated protein kinase kinase 3 | |||
Sequence: MESPAASPPASLPQTKGKSKRKKDLRISCVSKPPVSNPTPPRNLDSRTFITIGDRNFEVEADDLVTISELGRGAYGVVEKVRHAQSGTIMAVKRIRATVNTQEQKRLLMDLDINMRTVDCFYTVTFYGALFREGDVWICMELMDTSLDKFYRKVLEKNMKIPEDILGEIAVSIVRALEHLHSKLSVIHRDVKPSNVLINKEGHVKMCDFGISGYLVDSVAKTMDAGCKPYMAPERINPELNQKGYNVKSDVWSLGITMIEMAILRFPYESWGTPFQQLKQVVEEPSPQLPADQFSPEFVDFTSQCLRKNPAERMSYLELMEHPFFTLHKTKKTDIAAFVKEILGEDS | ||||||
Modified residue | 3 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 218 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 222 | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Autophosphorylated. Phosphorylation on Ser-218 and Thr-222 by MAP kinase kinase kinases positively regulates the kinase activity. Phosphorylated by TAOK2.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Component of a signaling complex containing at least AKAP13, PKN1, MAPK14, ZAK and MAP2K3. Within this complex, AKAP13 interacts directly with PKN1, which in turn recruits MAPK14, MAP2K3 and ZAK. Binds to DYRK1B/MIRK and increases its kinase activity (By similarity).
Part of a complex with MAP3K3, RAC1 and CCM2 (PubMed:14634666).
Interacts with ARRB1 (By similarity).
Part of a complex with MAP3K3, RAC1 and CCM2 (PubMed:14634666).
Interacts with ARRB1 (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-45 | Disordered | ||||
Sequence: MESPAASPPASLPQTKGKSKRKKDLRISCVSKPPVSNPTPPRNLD | ||||||
Domain | 64-325 | Protein kinase | ||||
Sequence: LVTISELGRGAYGVVEKVRHAQSGTIMAVKRIRATVNTQEQKRLLMDLDINMRTVDCFYTVTFYGALFREGDVWICMELMDTSLDKFYRKVLEKNMKIPEDILGEIAVSIVRALEHLHSKLSVIHRDVKPSNVLINKEGHVKMCDFGISGYLVDSVAKTMDAGCKPYMAPERINPELNQKGYNVKSDVWSLGITMIEMAILRFPYESWGTPFQQLKQVVEEPSPQLPADQFSPEFVDFTSQCLRKNPAERMSYLELMEHPFF |
Sequence similarities
Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
O09110-1
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.
- Name2
- Synonyms3b
- Length347
- Mass (Da)39,296
- Last updated2002-11-01 v2
- Checksum4A2A420EDCA8A2BC
O09110-2
- Name1
- Differences from canonical
- 1-37: MESPAASPPASLPQTKGKSKRKKDLRISCVSKPPVSN → MSKP
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0R4J1Q6 | A0A0R4J1Q6_MOUSE | Map2k3 | 173 |
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_004879 | 1-37 | in isoform 1 | |||
Sequence: MESPAASPPASLPQTKGKSKRKKDLRISCVSKPPVSN → MSKP | ||||||
Sequence conflict | 39 | in Ref. 1 | ||||
Sequence: T → A | ||||||
Sequence conflict | 60 | in Ref. 1; CAA63649 | ||||
Sequence: E → K | ||||||
Sequence conflict | 173-347 | in Ref. 4 | ||||
Sequence: IVRALEHLHSKLSVIHRDVKPSNVLINKEGHVKMCDFGISGYLVDSVAKTMDAGCKPYMAPERINPELNQKGYNVKSDVWSLGITMIEMAILRFPYESWGTPFQQLKQVVEEPSPQLPADQFSPEFVDFTSQCLRKNPAERMSYLELMEHPFFTLHKTKKTDIAAFVKEILGEDS → M | ||||||
Sequence conflict | 216 | in Ref. 1; CAA63649 | ||||
Sequence: V → E | ||||||
Sequence conflict | 292 | in Ref. 1; CAA63649 | ||||
Sequence: D → Y |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X93150 EMBL· GenBank· DDBJ | CAA63649.1 EMBL· GenBank· DDBJ | mRNA | ||
D87115 EMBL· GenBank· DDBJ | BAA13247.1 EMBL· GenBank· DDBJ | mRNA | ||
AK011002 EMBL· GenBank· DDBJ | BAB27321.1 EMBL· GenBank· DDBJ | mRNA | ||
AK008141 EMBL· GenBank· DDBJ | BAB25489.1 EMBL· GenBank· DDBJ | mRNA | ||
BC007467 EMBL· GenBank· DDBJ | AAH07467.1 EMBL· GenBank· DDBJ | mRNA |