EC Number   |
General Information |
Reference |
|---|
   3.1.3.48 | evolution |
among the 36 PTP genes, gene ptp-h, which is proposed to be the origin of baculovirus ptp, belongs to atypical VH1-like dual-specific PTP subset and encodes a catalytic active protein. PTP variants and subfamilies in Bombyx mori, overview |
750382 |
| 3.1.3.48 | evolution |
analysis of molecular basis of substrate specificity in the FERM-containing subfamily of nonreceptor PTPs, overview. These enzymes are characterized by the presence of an N-terminal FERM plasma-membrane-localization domain and a C-terminal catalytic domain |
752276 |
| 3.1.3.48 | evolution |
enzyme Siw14 is a member of the protein tyrosine-phosphatase (PTP) superfamily. Siw14 has a cysteine-based, class I CX5R(S/T) motif that defines the family of protein-tyrosine phosphatases (PTPs). Bioinformatic studies lead to Siw14 being classified as belonging within a specialist subgroup of PTPs, the dual specific protein-tyrosine phosphatases (DUSPs). The DUSPs themselves include a distinct class of proteins that appears not to have substantial activity against phosphoproteins. These are usually described as nonprotein-specific or atypical phosphatases. The inclusion of Siw14 in this category is supported by biochemical analysis, the enzyme's catalytic activity against 5-diphosphoinositol 1,2,3,4,6-pentakisphosphate (5-InsP7) is several orders of magnitude greater than that against 4-nitrophenyl phosphate, a generic protein phosphatase substrate. Other members of this atypical DUSP subgroup preferentially hydrolyze either phosphorylated carbohydrates, inositol lipids, or triphosphate groups in mRNA. Thus, this DUSP subfamily exhibits catalytic site diversity that is not observed for classical PTPs |
-, 751120 |
| 3.1.3.48 | evolution |
group A Streptococcus (GAS) Streptococcus pyogenes is a human pathogen that causes high morbidity and mortality. GAS lacks a gene encoding tyrosine kinase but contains one encoding tyrosine phosphatase (SP-PTP). SP-PTP falls into the category of low-molecular weight PTPases (LMW PTPases) |
-, 751599 |
| 3.1.3.48 | evolution |
osteoclastic protein tyrosine phosphatase (PTP-oc) belongs to the receptor PTP family |
752091 |
| 3.1.3.48 | evolution |
protein tyrosine phosphatase 1B (PTP1B) belongs to class I of the cysteine-based protein tyrosine phosphatases |
750465 |
| 3.1.3.48 | evolution |
protein tyrosine phosphatase N3 (PTPN3/PTPH1) belongs to a subfamily of five PTPs that contain an N-terminal 4.1 protein, ezrin, radixin, and moesin (FERM) plasma membrane-localization domain and a C-terminal catalytic domain. PTPs in this subfamily can be further divided into two types based on the presence of a PDZ domain |
752277 |
| 3.1.3.48 | evolution |
Protein tyrosine phosphatases form a large family of enzymes involved in the regulation of numerous cellular functions in eukaryotes |
-, 714058 |
| 3.1.3.48 | evolution |
protein tyrosine phosphatases share a common catalytic mechanism that utilizes a highly reactive nucleophilic Cys residue |
750056 |
| 3.1.3.48 | evolution |
receptor protein tyrosine phosphatases (PTPRs) are a family of cell surface receptor proteins that antagonize tyrosine kinase signaling |
749850 |
