tyrosine-protein phosphatase non-receptor type 20 isoform X13 [Homo sapiens]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| PTPc super family | cl33376 | Protein tyrosine phosphatase, catalytic domain; |
159-195 | 2.36e-04 | ||
Protein tyrosine phosphatase, catalytic domain; The actual alignment was detected with superfamily member smart00194: Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 41.11 E-value: 2.36e-04
|
||||||
| Name | Accession | Description | Interval | E-value | ||
| PTPc | smart00194 | Protein tyrosine phosphatase, catalytic domain; |
159-195 | 2.36e-04 | ||
Protein tyrosine phosphatase, catalytic domain; Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 41.11 E-value: 2.36e-04
|
||||||
| PTPc-N9 | cd14543 | catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ... |
159-196 | 3.92e-04 | ||
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein phosphatase non-receptor type 9 (PTPN9), also called protein-tyrosine phosphatase MEG2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN9 plays an important role in promoting intracellular secretary vesicle fusion in hematopoietic cells and promotes the dephosphorylation of ErbB2 and EGFR in breast cancer cells, leading to impaired activation of STAT5 and STAT3. It also directly dephosphorylates STAT3 at the Tyr705 residue, resulting in its inactivation. PTPN9 has been found to be dysregulated in various human cancers, including breast, colorectal, and gastric cancer. Pssm-ID: 350391 [Multi-domain] Cd Length: 271 Bit Score: 40.81 E-value: 3.92e-04
|
||||||
| Name | Accession | Description | Interval | E-value | ||
| PTPc | smart00194 | Protein tyrosine phosphatase, catalytic domain; |
159-195 | 2.36e-04 | ||
Protein tyrosine phosphatase, catalytic domain; Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 41.11 E-value: 2.36e-04
|
||||||
| PTPc-N9 | cd14543 | catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ... |
159-196 | 3.92e-04 | ||
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein phosphatase non-receptor type 9 (PTPN9), also called protein-tyrosine phosphatase MEG2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN9 plays an important role in promoting intracellular secretary vesicle fusion in hematopoietic cells and promotes the dephosphorylation of ErbB2 and EGFR in breast cancer cells, leading to impaired activation of STAT5 and STAT3. It also directly dephosphorylates STAT3 at the Tyr705 residue, resulting in its inactivation. PTPN9 has been found to be dysregulated in various human cancers, including breast, colorectal, and gastric cancer. Pssm-ID: 350391 [Multi-domain] Cd Length: 271 Bit Score: 40.81 E-value: 3.92e-04
|
||||||
| PTPc-N14 | cd14599 | catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ... |
148-207 | 4.45e-03 | ||
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein phosphatase non-receptor type 14 (PTPN14), also called protein-tyrosine phosphatase pez, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN14 is a potential tumor suppressor and plays a regulatory role in the Hippo and Wnt/beta-catenin signaling pathways. It contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence. Pssm-ID: 350447 [Multi-domain] Cd Length: 287 Bit Score: 37.67 E-value: 4.45e-03
|
||||||
| Blast search parameters | ||||
|
