phosphatase and tensin-like protein mutant, partial [Homo sapiens]
Protein Classification
protein-tyrosine phosphatase family protein( domain architecture ID 1000023)
cys-based protein-tyrosine phosphatase (PTP) family protein may be a PTP or a dual-specificity phosphatase (DUSP or DSP), and may catalyze the dephosphorylation of target phosphoproteins at tyrosine or tyrosine and serine/threonine residues, respectively
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| PTP_DSP_cys super family | cl28904 | cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ... |
1-37 | 2.77e-18 | ||
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases. The actual alignment was detected with superfamily member cd14509: Pssm-ID: 475123 [Multi-domain] Cd Length: 158 Bit Score: 71.47 E-value: 2.77e-18
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| Name | Accession | Description | Interval | E-value | ||
| PTP_PTEN | cd14509 | protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ... |
1-37 | 2.77e-18 | ||
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; Phosphatase and tensin homolog (PTEN), also phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN or mutated in multiple advanced cancers 1 (MMAC1), is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It is a critical endogenous inhibitor of phosphoinositide signaling. It dephosphorylates phosphoinositide trisphosphate, and therefore, has the function of negatively regulating Akt. The PTEN/PI3K/AKT pathway regulates the signaling of multiple biological processes such as apoptosis, metabolism, cell proliferation, and cell growth. PTEN contains an N-terminal PIP-binding domain, a protein tyrosine phosphatase (PTP)-like catalytic domain, a regulatory C2 domain responsible for its cellular location, a C-tail containing phosphorylation sites, and a C-terminal PDZ domain. Pssm-ID: 350359 [Multi-domain] Cd Length: 158 Bit Score: 71.47 E-value: 2.77e-18
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| CDC14 | COG2453 | Protein-tyrosine phosphatase [Signal transduction mechanisms]; |
2-32 | 6.82e-03 | ||
Protein-tyrosine phosphatase [Signal transduction mechanisms]; Pssm-ID: 441989 [Multi-domain] Cd Length: 140 Bit Score: 31.09 E-value: 6.82e-03
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| Name | Accession | Description | Interval | E-value | ||
| PTP_PTEN | cd14509 | protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ... |
1-37 | 2.77e-18 | ||
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; Phosphatase and tensin homolog (PTEN), also phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN or mutated in multiple advanced cancers 1 (MMAC1), is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It is a critical endogenous inhibitor of phosphoinositide signaling. It dephosphorylates phosphoinositide trisphosphate, and therefore, has the function of negatively regulating Akt. The PTEN/PI3K/AKT pathway regulates the signaling of multiple biological processes such as apoptosis, metabolism, cell proliferation, and cell growth. PTEN contains an N-terminal PIP-binding domain, a protein tyrosine phosphatase (PTP)-like catalytic domain, a regulatory C2 domain responsible for its cellular location, a C-tail containing phosphorylation sites, and a C-terminal PDZ domain. Pssm-ID: 350359 [Multi-domain] Cd Length: 158 Bit Score: 71.47 E-value: 2.77e-18
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| PTP_VSP_TPTE | cd14510 | protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ... |
1-34 | 5.54e-13 | ||
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase/transmembrane phosphatase with tensin homology; Voltage-sensitive phosphatase (VSP) proteins comprise a family of phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. This family is conserved in deuterostomes; VSP was first identified as a sperm flagellar plasma membrane protein in Ciona intestinalis. Gene duplication events in primates resulted in the presence of paralogs, transmembrane phosphatase with tensin homology (TPTE) and TPTE2, that retain protein domain architecture but, in the case of TPTE, have lost catalytic activity. TPTE, also called cancer/testis antigen 44 (CT44), may play a role in the signal transduction pathways of the endocrine or spermatogenic function of the testis. TPTE2, also called TPTE and PTEN homologous inositol lipid phosphatase (TPIP), occurs in several differentially spliced forms; TPIP alpha displays phosphoinositide 3-phosphatase activity and is localized on the endoplasmic reticulum, while TPIP beta is cytosolic and lacks detectable phosphatase activity. VSP/TPTE proteins contain an N-terminal voltage sensor consisting of four transmembrane segments, a protein tyrosine phosphatase (PTP)-like phosphoinositide phosphatase catalytic domain, followed by a regulatory C2 domain. Pssm-ID: 350360 [Multi-domain] Cd Length: 177 Bit Score: 58.14 E-value: 5.54e-13
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| PTP_PTEN-like | cd14497 | protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ... |
1-37 | 1.99e-12 | ||
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar proteins; Phosphatase and tensin homolog (PTEN) is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It dephosphorylates phosphoinositide trisphosphate. In addition to PTEN, this family includes tensins, voltage-sensitive phosphatases (VSPs), and auxilins. They all contain a protein tyrosine phosphatase-like domain although not all are active phosphatases. Tensins are intracellular proteins that act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility, and they may or may not have phosphatase activity. VSPs are phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. Auxilins are J domain-containing proteins that facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles, and they do not exhibit phosphatase activity. Pssm-ID: 350347 [Multi-domain] Cd Length: 160 Bit Score: 56.43 E-value: 1.99e-12
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| PTP_DSP_cys | cd14494 | cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ... |
1-37 | 5.70e-04 | ||
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases. Pssm-ID: 350344 [Multi-domain] Cd Length: 113 Bit Score: 33.48 E-value: 5.70e-04
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| CDC14 | COG2453 | Protein-tyrosine phosphatase [Signal transduction mechanisms]; |
2-32 | 6.82e-03 | ||
Protein-tyrosine phosphatase [Signal transduction mechanisms]; Pssm-ID: 441989 [Multi-domain] Cd Length: 140 Bit Score: 31.09 E-value: 6.82e-03
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| CDC14_C | cd14499 | C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ... |
2-24 | 8.56e-03 | ||
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif. Pssm-ID: 350349 [Multi-domain] Cd Length: 174 Bit Score: 30.88 E-value: 8.56e-03
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