Mitogen-activated protein (MAP) kinase phosphatase (IPR008343)

Short name: MKP

Overlapping homologous superfamilies


Family relationships


MAP Kinase Phosphatases (MKPs) are members of the dual specificity phosphatase family [PMID: 17057753, PMID: 15186772]. MKPs constitute a class of phosphatases that reverse the activation of MAP (mitogen activated protein) kinases by dephosphorylating critical tyrosine and threonine residues [PMID: 8221888]. This regulation is mediated via interaction of a Kinase Interaction Motif (KIM) with the common docking domain of the kinase - this motif is shared with a number of other protein families that interact with MAP kinases: these include kinases (MEKs), phosphatases (PTP-SL) and transcription factors (Elk1). MKPs also share an active site motif with the protein tyrosine phosphatases (PTPs). Different MKPs exhibit specificity towards different members of the MAP kinase family [PMID: 8910287].

The structure of the MPK catalytic domain is similar to that of the PTPs - the fold exhibits a complex mixed alpha-/beta-architecture. The catalytic mechanism involves a general acid (Asp92 in 1VHR) and a catalytic cysteine (130 in 1VHR), which acts as a nucleophile.

GO terms

Biological Process

GO:0006470 protein dephosphorylation

Molecular Function

GO:0017017 MAP kinase tyrosine/serine/threonine phosphatase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.