InterPro : IPR016130

Name  Protein-tyrosine phosphatase, active site Short Name  Tyr_Pase_AS
Type  Active_site Description  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.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

0 Contains

16 Found In

Id Name Short Name Type
IPR000340 Dual specificity phosphatase, catalytic domain Dual-sp_phosphatase_cat-dom Domain
IPR000242 Protein-tyrosine phosphatase, receptor/non-receptor type Tyr_Pase_rcpt/non-rcpt Domain
IPR000387 Protein-tyrosine/Dual specificity phosphatase Tyr/Dual-sp_Pase Domain
IPR003595 Protein-tyrosine phosphatase, catalytic Tyr_Pase_cat Domain
IPR020422 Dual specificity phosphatase, subgroup, catalytic domain Dual-sp_phosphatase_subgr_cat Domain
IPR020417 Atypical dual specificity phosphatase Atypical_DUSP Family
IPR008356 Protein-tyrosine phosphatase, KIM-containing Tyr_Pase_KIM-con Family
IPR020428 Protein-tyrosine phosphatase, dual specificity phosphatase, eukaryotic Tyr_Pase_dualsp-Pase_euk 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

0 Parent Features

1 Publications

First Author Title Year Journal Volume Pages
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)