Atypical dual specificity phosphatase, subfamily A
IPR020405
Definition
This entry represents atypical dual specificity phosphatase subfamily A. 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 The atypical DUSPs share a high degree of similarity with the MKP subgroup, but lack the N-terminal regulatory domain, which provides the substrate specificity towards the MAP kinases. These atypical-DUSPs form a heterogeneous group and have in common the presence of a single catalytic PTP domain. VHR was the first characterised member of this subfamily; its crystal structure is known [[cite:PMID:1281549], [cite:PMID:8650541]]. The function of many atypical DUSPs remains unknown, although some have been related to regulation of MAP kinase pathways [[cite:PMID:10224087], [cite:PMID:11971192], [cite:PMID:15796912]]. VHR has also been related to the control of cell-senescence PMID:16604064.
6 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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