InterPro : IPR000387

Name  Protein-tyrosine/Dual specificity phosphatase Short Name  Tyr/Dual-sp_Pase
Type  Domain Description  Protein tyrosine (pTyr) phosphorylation is a common post-translational modification which can create novel recognition motifs for protein interactions and cellular localisation, affect protein stability, and regulate enzyme activity. Consequently, maintaining an appropriate level of protein tyrosine phosphorylation is essential for many cellular functions. Tyrosine-specific protein phosphatases (PTPase; ) catalyse the removal of a phosphate group attached to a tyrosine residue, using a cysteinyl-phosphate enzyme intermediate. These enzymes are key regulatory components in signal transduction pathways (such as the MAP kinase pathway) and cell cycle control, and are important in the control of cell growth, proliferation, differentiation and transformation [, ]. The PTP superfamily can be divided into four subfamilies []:(1) pTyr-specific phosphatases(2) dual specificity phosphatases (dTyr and dSer/dThr)(3) Cdc25 phosphatases (dTyr and/or dThr)(4) LMW (low molecular weight) phosphatasesBased on their cellular localisation, PTPases are also classified as:Receptor-like, which are transmembrane receptors that contain PTPase domains []Non-receptor (intracellular) PTPases []All PTPases carry the highly conserved active site motif C(X)5R (PTP signature motif), employ a common catalytic mechanism, and share a similar core structure made of a central parallel beta-sheet with flanking alpha-helices containing a beta-loop-alpha-loop that encompasses the PTP signature motif []. Functional diversity between PTPases is endowed by regulatory domains and subunits. This entry includes proteins of two subfamilies: Ser/Thr () and Tyr dual specificity protein phosphatase and tyrosine specific protein phosphatase (). Both of these subfamilies may also have inactive phosphatase domains, and dependent on the domain composition this loss of catalytic activity has different effects on protein function. Inactive single domain phosphatases can still specifically bind substrates, and protect against dephosphorylation, while the inactive domains of tandem phosphatases can be further subdivided into two classes. Those which bind phosphorylated tyrosine residues may recruit multi-phosphorylated substrates for the adjacent active domains and are more conserved, while the other class have accumulated several variable amino acid substitutions and have a complete loss of tyrosine binding capability. The second class shows a release of evolutionary constraint for the sites around the catalytic centre, which emphasises a difference in function from the first group. There is a region of higher conservation common to both classes, suggesting a regulatory centre [].Ser/Thr and Tyr dual specificity phosphatases are a group of enzymes with both Ser/Thr () and tyrosine specific proteinphosphatase () activity able to remove both the serine/threonine or tyrosine-bound phosphate group from a widerange of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase. Dual specificity protein phosphatases (DSPs) regulate mitogenic signal transduction and control the cell cycle. Tyrosine specific protein phosphatases catalyze the removal of a phosphate group attached to a tyrosine residue. They are also very important in the control of cell growth, proliferation, differentiation and transformation.This domain is common to both dual-specificity protein phosphatases and protein-tyrosine phosphatase.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



2 Child Features

Id Name Short Name Type
IPR000242 Protein-tyrosine phosphatase, receptor/non-receptor type Tyr_Pase_rcpt/non-rcpt Domain
IPR020422 Dual specificity phosphatase, subgroup, catalytic domain Dual-sp_phosphatase_subgr_cat Domain

1 Contains

Id Name Short Name Type
IPR016130 Protein-tyrosine phosphatase, active site Tyr_Pase_AS Active_site

20 Found In

Id Name Short Name Type
IPR000340 Dual specificity phosphatase, catalytic domain Dual-sp_phosphatase_cat-dom Domain
IPR020417 Atypical dual specificity phosphatase Atypical_DUSP Family
IPR008356 Protein-tyrosine phosphatase, KIM-containing Tyr_Pase_KIM-con Family
IPR012153 Tyrosine-protein phosphatase non-receptor type 13 PTPN13 Family
IPR003546 Type III secreted modular tyrosine phosphatase, SptP/YopH Tyr_Pase_SptP/YopH Family
IPR012151 Protein-tyrosine phosphatase, non-receptor type-3, -4 Tyr_Pase_non-rcpt_typ-3/4 Family
IPR012152 Protein-tyrosine phosphatase, non-receptor type-6, -11 Tyr_Pase_non-rcpt_typ-6/11 Family
IPR020405 Atypical dual specificity phosphatase, subfamily A Atypical_DUSP_famA Family
IPR012265 Protein-tyrosine phosphatase, non-receptor type-1/2 Ptpn1/Ptpn2 Family
IPR012266 Protein-tyrosine phosphatase, non-receptor type-12 Ptpn_12 Family
IPR020420 Atypical dual specificity phosphatase, subfamily B Atypical_DUSP_famB Family
IPR014392 Protein-tyrosine phosphatase, non-receptor type-14, -21 Tyr_Pase_non-rcpt_typ-14/21 Family
IPR016336 Receptor tyrosine-protein phosphatase, alpha/epsilon-type Tyr_Pase_rcpt_a/e-type Family
IPR016335 Leukocyte common antigen Leukocyte_common_ag Family
IPR016334 Protein-tyrosine phosphatase, receptor type R/non-receptor type 5 Tyr_Pase_rcpt_R/non-rcpt_5 Family
IPR016276 Non-receptor tyrosine-protein phosphatase 22 PTPN22 Family
IPR016278 Dual specificity protein phosphatase 12 DUSP12 Family
IPR016277 Non-receptor tyrosine-protein phosphatase type 1, yeast Non-rcpt_Tyr_Pase_T1_fun Family
IPR017074 mRNA capping enzyme, bifunctional mRNA_cap_enz_bifunc Family
IPR008425 Cyclin-dependent kinase inhibitor 3 CDK_inhib_3 Family

1 Parent Features

Id Name Short Name Type
IPR029021 Protein-tyrosine phosphatase-like Prot-tyrosine_phosphatase-like Domain

7 Publications

First Author Title Year Journal Volume Pages
Denu JM Protein tyrosine phosphatases: mechanisms of catalysis and regulation. 1998 Curr Opin Chem Biol 2 633-41
Paul S Receptor and nonreceptor protein tyrosine phosphatases in the nervous system. 2003 Cell Mol Life Sci 60 2465-82
Wang WQ An overview of the protein tyrosine phosphatase superfamily. 2003 Curr Top Med Chem 3 739-48
Eswaran J The crystal structure of human receptor protein tyrosine phosphatase kappa phosphatase domain 1. 2006 Protein Sci 15 1500-5
Perkins LA The nonreceptor protein tyrosine phosphatase corkscrew functions in multiple receptor tyrosine kinase pathways in Drosophila. 1996 Dev Biol 180 63-81
Barford D The structure and mechanism of protein phosphatases: insights into catalysis and regulation. 1998 Annu Rev Biophys Biomol Struct 27 133-64
Pils B Evolution of the multifunctional protein tyrosine phosphatase family. 2004 Mol Biol Evol 21 625-31

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)