InterPro : IPR000242

Name  Protein-tyrosine phosphatase, receptor/non-receptor type Short Name  Tyr_Pase_rcpt/non-rcpt
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 repesents several receptor and non-receptor protein-tyrosine phosphatases.Structurally, all known receptor PTPases, are made up of a variable lengthextracellular domain, followed by a transmembrane region and a C-terminalcatalytic cytoplasmic domain. Some of the receptor PTPases contain fibronectintype III (FN-III) repeats, immunoglobulin-like domains, MAM domains orcarbonic anhydrase-like domains in their extracellular region. The cytoplasmicregion generally contains two copies of the PTPase domain. The first seems tohave enzymatic activity, while the second is inactive. The inactive domains of tandem phosphatases can be divided 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 new regulatory centre []. PTPase domains consist of about 300 amino acids. There are two conserved cysteines, the second one has been shown to be absolutely required for activity. Furthermore, a number of conserved residues in its immediate vicinity have also been shownto be important.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



1 Child Features

Id Name Short Name Type
IPR003595 Protein-tyrosine phosphatase, catalytic Tyr_Pase_cat Domain

1 Contains

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

11 Found In

Id Name Short Name Type
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
IPR012265 Protein-tyrosine phosphatase, non-receptor type-1/2 Ptpn1/Ptpn2 Family
IPR012266 Protein-tyrosine phosphatase, non-receptor type-12 Ptpn_12 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

1 Parent Features

Id Name Short Name Type
IPR000387 Protein-tyrosine/Dual specificity phosphatase Tyr/Dual-sp_Pase 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)