Q9GRU1 · MPK4_LEIME

  • Protein
    Mitogen-activated protein kinase 4
  • Gene
    MPK4
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Essential for the two main proliferating life stages, the promastigotes and amastigotes, of the parasite.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

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.

TypeIDPosition(s)Description
Binding site36-44ATP (UniProtKB | ChEBI)
Binding site59ATP (UniProtKB | ChEBI)
Active site156Proton acceptor

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular FunctionMAP kinase activity
Molecular Functionmetal ion binding
Molecular Functionprotein serine kinase activity
Molecular Functionprotein serine/threonine kinase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Mitogen-activated protein kinase 4
  • EC number
  • Alternative names
    • LmxMPK4

Gene names

    • Name
      MPK4

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • MNYC/BZ/62/M379
  • Taxonomic lineage
    Eukaryota > Discoba > Euglenozoa > Kinetoplastea > Metakinetoplastina > Trypanosomatida > Trypanosomatidae > Leishmaniinae > Leishmania

Accessions

  • Primary accession
    Q9GRU1

Organism-specific databases

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis59Loss of catalytic activity.

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00004492931-363Mitogen-activated protein kinase 4
Modified residue186Phosphoserine
Modified residue187Phosphoserine
Modified residue190Phosphothreonine; by MKK5
Modified residue192Phosphotyrosine; by MKK5

Post-translational modification

Dually phosphorylated on Thr-190 and Tyr-192, which activates the enzyme.

Keywords

PTM databases

Expression

Developmental stage

Expressed in promastigotes and to a lower extent in axenic amastigotes (at protein level) (PubMed:14636673, PubMed:16384531).
Low expression levels in lesion-derived amastigotes (at protein level) (PubMed:14636673, PubMed:16384531).

Structure

Family & Domains

Features

Showing features for domain, motif.

TypeIDPosition(s)Description
Domain30-318Protein kinase
Motif190-192TQY

Domain

The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    363
  • Mass (Da)
    41,548
  • Last updated
    2001-03-01 v1
  • Checksum
    D320FBF13B3A87D6
MTQLVPLAELPSGKKIYSVRGQRFEVDRQYDLVKVVGFGACGTVCSAVVNGSGERVAIKRLSRVFGDLREGKRILREMEIMTSLKHNNLIRLHHFMRPQSKETFEDIYLVMDLYDTDLNRIIRSRQKLTDEHLQYFMIQAFRGLHYLHSAKVMHRDLKPSNLLVNADCALAICDFGLARDDQVMSSSDLTQYVVTRWYRPPEVLGMGSNQYTSAVDVWSLGLIFAELMVGRALLPGTDYIGQLVMIVNLLGSPSIDDMEFLSSEAKAFILSQPHRPALSFRDLFPMATEEATDLLSKLLVFHPARRLTAKQVMEHPYFSKYRDAAEEADAPDPFVWNHSHIETKEQLREDLWRVVEAHSQLNE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ293282
EMBL· GenBank· DDBJ
CAC07958.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any 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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp