Q9GRU1 · MPK4_LEIME
- ProteinMitogen-activated protein kinase 4
- GeneMPK4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids363 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Essential for the two main proliferating life stages, the promastigotes and amastigotes, of the parasite.
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Cofactor
Note: Can use both Mg2+ and Mn2+ in vitro and shows higher activity with Mn2+ but Mg2+ is likely to be the in vivo cofactor.
pH Dependence
Optimum pH is 6-7.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | MAP kinase activity | |
Molecular Function | metal ion binding | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMitogen-activated protein kinase 4
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Discoba > Euglenozoa > Kinetoplastea > Metakinetoplastina > Trypanosomatida > Trypanosomatidae > Leishmaniinae > Leishmania
Accessions
- Primary accessionQ9GRU1
Organism-specific databases
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 59 | Loss of catalytic activity. | ||||
Sequence: K → M |
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000449293 | 1-363 | Mitogen-activated protein kinase 4 | |||
Sequence: MTQLVPLAELPSGKKIYSVRGQRFEVDRQYDLVKVVGFGACGTVCSAVVNGSGERVAIKRLSRVFGDLREGKRILREMEIMTSLKHNNLIRLHHFMRPQSKETFEDIYLVMDLYDTDLNRIIRSRQKLTDEHLQYFMIQAFRGLHYLHSAKVMHRDLKPSNLLVNADCALAICDFGLARDDQVMSSSDLTQYVVTRWYRPPEVLGMGSNQYTSAVDVWSLGLIFAELMVGRALLPGTDYIGQLVMIVNLLGSPSIDDMEFLSSEAKAFILSQPHRPALSFRDLFPMATEEATDLLSKLLVFHPARRLTAKQVMEHPYFSKYRDAAEEADAPDPFVWNHSHIETKEQLREDLWRVVEAHSQLNE | ||||||
Modified residue | 186 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 187 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 190 | Phosphothreonine; by MKK5 | ||||
Sequence: T | ||||||
Modified residue | 192 | Phosphotyrosine; by MKK5 | ||||
Sequence: Y |
Post-translational modification
Dually phosphorylated on Thr-190 and Tyr-192, which activates the enzyme.
Keywords
- PTM
PTM databases
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 30-318 | Protein kinase | ||||
Sequence: YDLVKVVGFGACGTVCSAVVNGSGERVAIKRLSRVFGDLREGKRILREMEIMTSLKHNNLIRLHHFMRPQSKETFEDIYLVMDLYDTDLNRIIRSRQKLTDEHLQYFMIQAFRGLHYLHSAKVMHRDLKPSNLLVNADCALAICDFGLARDDQVMSSSDLTQYVVTRWYRPPEVLGMGSNQYTSAVDVWSLGLIFAELMVGRALLPGTDYIGQLVMIVNLLGSPSIDDMEFLSSEAKAFILSQPHRPALSFRDLFPMATEEATDLLSKLLVFHPARRLTAKQVMEHPYF | ||||||
Motif | 190-192 | TQY | ||||
Sequence: TQY |
Domain
The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.
Sequence similarities
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length363
- Mass (Da)41,548
- Last updated2001-03-01 v1
- ChecksumD320FBF13B3A87D6