Q39027 · MPK7_ARATH

Function

function

MKK3-MPK7 module acts as a positive regulator of PR1 gene expression.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Activity regulation

Activated by threonine and tyrosine phosphorylation (By similarity).
Activated in response to hydrogen peroxide. Activation is triggered by MAPKKK17 and MAPKKK18 in a MKK3-dependent manner (PubMed:25720833).

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site38-46ATP (UniProtKB | ChEBI)
Binding site61ATP (UniProtKB | ChEBI)
Active site158Proton acceptor

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular FunctionMAP kinase activity
Molecular Functionprotein serine kinase activity
Biological Processdefense response
Biological Processresponse to hydrogen peroxide

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Mitogen-activated protein kinase 7
  • EC number
  • Short names
    AtMPK7; MAP kinase 7

Gene names

    • Name
      MPK7
    • ORF names
      F8D23
    • Ordered locus names
      At2g18170
Community curation (1)

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q39027
  • Secondary accessions
    • Q56W33
    • Q9SI14

Proteomes

Organism-specific databases

Genome annotation databases

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001863161-368Mitogen-activated protein kinase 7
Modified residue191Phosphothreonine
Modified residue193Phosphotyrosine
Modified residue196Phosphothreonine

Post-translational modification

Dually phosphorylated on Thr-191 and Tyr-193, which activates the enzyme.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Interacts with MKK3.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, motif.

TypeIDPosition(s)Description
Domain32-319Protein kinase
Motif191-193TXY

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
    368
  • Mass (Da)
    42,299
  • Last updated
    2002-06-06 v2
  • Checksum
    64587E4CA40C1418
MAMLVEPPNGIKQQGKHYYSMWQTLFEIDTKYVPIKPIGRGAYGVVCSSINRETNERVAIKKIHNVFENRVDALRTLRELKLLRHVRHENVIALKDVMLPANRSSFKDVYLVYELMDTDLHQIIKSSQSLSDDHCKYFLFQLLRGLKYLHSANILHRDLKPGNLLVNANCDLKICDFGLARTSQGNEQFMTEYVVTRWYRAPELLLCCDNYGTSIDVWSVGCIFAEILGRKPIFPGTECLNQLKLIINVVGSQQESDIRFIDNPKARRFIKSLPYSRGTHLSNLYPQANPLAIDLLQRMLVFDPTKRISVTDALLHPYMAGLFDPGSNPPAHVPISLDIDENMEEPVIREMMWNEMLYYHPEAEISNA

Sequence caution

The sequence BAD95376.1 differs from that shown. Reason: Frameshift

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict104in Ref. 1; BAA04870
Sequence conflict303in Ref. 1; BAA04870
Sequence conflict324in Ref. 1; BAA04870
Sequence conflict327in Ref. 1; BAA04870
Sequence conflict366in Ref. 1; BAA04870

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
D21843
EMBL· GenBank· DDBJ
BAA04870.1
EMBL· GenBank· DDBJ
mRNA
AC007212
EMBL· GenBank· DDBJ
AAD31349.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002685
EMBL· GenBank· DDBJ
AEC06734.1
EMBL· GenBank· DDBJ
Genomic DNA
AK222214
EMBL· GenBank· DDBJ
BAD95376.1
EMBL· GenBank· DDBJ
mRNA Frameshift

Genome annotation databases

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