Mitogen-activated protein (MAP) kinase phosphatase
IPR008343
Definition
MAP Kinase Phosphatases (MKPs) are members of the dual specificity phosphatase family [[cite:PMID:17057753], [cite: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 α/β-architecture. The catalytic mechanism involves a general acid (Asp92 in 1VHR) and a catalytic cysteine (130 in 1VHR), which acts as a nucleophile.
10 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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