Dual specificity protein phosphatase domain (IPR020422)


Overlapping homologous superfamilies

Domain relationships


Tyrosine specific protein phosphatases (PTPases) contain two conserved cysteines, the second one has been shown to be absolutely required for activity. This entry represents the PTPase domain that centre on the active site cysteine. A number of conserved residues in its immediate vicinity have also been shown to be important. This domain can be found in dual specificity phosphatases.

Dual specificity phosphatases (DUSPs) are members of the superfamily of protein tyrosine phosphatases [PMID: 17057753, PMID: 15186772]. They remove the phosphate group from both phospho-tyrosine and phospho-serine/threonine residues. They are structurally similar to tyrosine-specific phosphatases but with a shallower active site cleft and a distinctive active site signature motif, HCxxGxxR [PMID: 8987394,PMID: 7961745,PMID: 8154323]. They are characterized as VHR- [PMID: 9571625,PMID: 8650541] or Cdc25-like [PMID: 7601801,PMID: 8701088].

In general, DUSPs are classified into the following subgroups [PMID: 19228121]:

  • Slingshot phosphatases
  • Phosphatase of regenerating liver (PRL)
  • Cdc14 phosphatases
  • Phosphatase and tensin homologue deleted on chromosome 10 (PTEN)-like and myotubularin phosphatases
  • Mitogen-activated protein kinase phosphatases (MKPs)
  • Atypical DUSPs

GO terms

Biological Process

GO:0006470 protein dephosphorylation

Molecular Function

GO:0008138 protein 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.
PROSITE profiles