D
IPR020422

Dual specificity protein phosphatase domain

InterPro entry
Short nameTYR_PHOSPHATASE_DUAL_dom
Overlapping
homologous
superfamilies
 
domain relationships

Description

Tyrosine specific protein phosphatases (PTPases) (
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
[8, 7]
. 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
[1, 9, 4]
. They are characterized as VHR-
[5, 3]
or Cdc25-like
[2, 6]
.

In general, DUSPs are classified into the following subgroups
[10]
:


 * 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

References

1.Structure and function of the protein tyrosine phosphatases. Fauman EB, Saper MA. Trends Biochem. Sci. 21, 413-7, (1996). View articlePMID: 8987394

2.Cloning and sequencing of a pig cdc25 tyrosine phosphatase cDNA. Cui H, Xu WX, Powell D, Newman B. J. Anim. Sci. 73, 630, (1995). PMID: 7601801

3.Crystal structure of the dual specificity protein phosphatase VHR. Yuvaniyama J, Denu JM, Dixon JE, Saper MA. Science 272, 1328-31, (1996). View articlePMID: 8650541

4.Protein tyrosine phosphatases: mechanism of catalysis and substrate specificity. Zhang ZY, Dixon JE. Adv. Enzymol. Relat. Areas Mol. Biol. 68, 1-36, (1994). PMID: 8154323

5.The "VH1-like" dual-specificity protein tyrosine phosphatases. Martell KJ, Angelotti T, Ullrich A. Mol. Cells 8, 2-11, (1998). PMID: 9571625

6.Protein tyrosine phosphatases: their roles in signal transduction. Dixon JE. Recent Prog. Horm. Res. 51, 405-14; discussion 415, (1996). PMID: 8701088

7.Protein tyrosine phosphatases in the human genome. Alonso A, Sasin J, Bottini N, Friedberg I, Friedberg I, Osterman A, Godzik A, Hunter T, Dixon J, Mustelin T. Cell 117, 699-711, (2004). View articlePMID: 15186772

8.Protein tyrosine phosphatases: from genes, to function, to disease. Tonks NK. Nat. Rev. Mol. Cell Biol. 7, 833-46, (2006). View articlePMID: 17057753

9.The catalytic role of Cys124 in the dual specificity phosphatase VHR. Zhou G, Denu JM, Wu L, Dixon JE. J. Biol. Chem. 269, 28084-90, (1994). PMID: 7961745

10.Dual-specificity phosphatases: critical regulators with diverse cellular targets. Patterson KI, Brummer T, O'Brien PM, Daly RJ. Biochem. J. 418, 475-89, (2009). PMID: 19228121

GO terms

molecular function

  • None

cellular component

  • None

Cross References

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