The domain within your query sequence starts at position 45 and ends at position 190; the E-value for the DSPc domain shown below is 9.29e-31.

All catalytic sites are present in this domain. Check the literature (PubMed 96243129 ) for details.



Dual specificity phosphatase, catalytic domain
SMART accession number:SM00195
Description: -
Interpro abstract (IPR020422):

Dual specificity phosphatases (DUSPs) are members of the superfamily of protein tyrosine phosphatases [ (PUBMED:17057753) (PUBMED: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 [ (PUBMED:8987394) (PUBMED:7961745) (PUBMED:8154323) ]. They are characterized as VHR- [ (PUBMED:9571625) (PUBMED:8650541) ] or Cdc25-like [ (PUBMED:7601801) (PUBMED:8701088) ].

In general, DUSPs are classified into the following subgroups [ (PUBMED: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

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.

GO process:protein dephosphorylation (GO:0006470)
GO function:protein tyrosine/serine/threonine phosphatase activity (GO:0008138)
Family alignment:
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There are 17170 DSPc domains in 17099 proteins in SMART's nrdb database.

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