| Primary Identifier | IPR029021 | Type | Homologous_superfamily |
| Short Name | Prot-tyrosine_phosphatase-like |
| description | This superfamily represents a domain found in some protein-tyrosine phosphatases, including dual specificity phosphatases, myotubularin-like phosphatases [], receptor-type tyrosine-protein phosphatases and non receptor-type tyrosine-protein phosphatases. This domain also shares structure similarity with the lipid phosphatase domain in tensin []and tensin like proteins, such as cyclin G-associated kinase (GAK) []and phoshphoinositide phosphatase PTEN (phosphatase and tensin homologue) [].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 β-sheet with flanking α-helices containing a β-loop-α-loop that encompasses the PTP signature motif []. Functional diversity between PTPases is endowed by regulatory domains and subunits. |
