Dual specificity protein phosphatase domain
IPR020422
Definition
Tyrosine specific protein phosphatases (PTPases) ([ec:3.1.3.48]) 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 [[cite:PMID:17057753], [cite: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 [[cite:PMID:8987394], [cite:PMID:7961745], [cite:PMID:8154323]]. They are characterised as VHR- [[cite:PMID:9571625], [cite:PMID:8650541]] or Cdc25-like [[cite:PMID:7601801], [cite: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
41 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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