paladin isoform X1 [Homo sapiens]
Protein Classification
PTP_paladin_1 and PTP_DSP_cys domain-containing protein( domain architecture ID 13026115)
PTP_paladin_1 and PTP_DSP_cys domain-containing protein
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 ... |
477-733 | 6.51e-117 | |||||
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 cd17660: Pssm-ID: 475123 Cd Length: 216 Bit Score: 353.70 E-value: 6.51e-117
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| PTP_paladin_1 | cd17659 | protein tyrosine phosphatase-like domain of paladin, repeat 1; Paladin is a putative ... |
91-382 | 9.02e-99 | |||||
protein tyrosine phosphatase-like domain of paladin, repeat 1; Paladin is a putative phosphatase, which in mouse is expressed in endothelial cells during embryonic development and in arterial smooth muscle cells in adults. It has been suggested to be an antiphosphatase that regulates the activity of specific neural crest regulatory factors and thus, modulates neural crest cell formation and migration. Paladin contains two tyrosine-protein phosphatase domains. This model represents repeat 1. : Pssm-ID: 350497 Cd Length: 220 Bit Score: 306.78 E-value: 9.02e-99
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| Name | Accession | Description | Interval | E-value | |||||
| PTP_paladin_2 | cd17660 | protein tyrosine phosphatase-like domain of paladin, repeat 2; Paladin is a putative ... |
477-733 | 6.51e-117 | |||||
protein tyrosine phosphatase-like domain of paladin, repeat 2; Paladin is a putative phosphatase, which in mouse is expressed in endothelial cells during embryonic development and in arterial smooth muscle cells in adults. It has been suggested to be an antiphosphatase that regulates the activity of specific neural crest regulatory factors and thus, modulates neural crest cell formation and migration. Paladin contains two tyrosine-protein phosphatase domains. This model represents repeat 2. Pssm-ID: 350498 Cd Length: 216 Bit Score: 353.70 E-value: 6.51e-117
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| PTP_paladin_1 | cd17659 | protein tyrosine phosphatase-like domain of paladin, repeat 1; Paladin is a putative ... |
91-382 | 9.02e-99 | |||||
protein tyrosine phosphatase-like domain of paladin, repeat 1; Paladin is a putative phosphatase, which in mouse is expressed in endothelial cells during embryonic development and in arterial smooth muscle cells in adults. It has been suggested to be an antiphosphatase that regulates the activity of specific neural crest regulatory factors and thus, modulates neural crest cell formation and migration. Paladin contains two tyrosine-protein phosphatase domains. This model represents repeat 1. Pssm-ID: 350497 Cd Length: 220 Bit Score: 306.78 E-value: 9.02e-99
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| PTPlike_phytase | pfam14566 | Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in ... |
161-330 | 1.37e-50 | |||||
Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in abundance in seeds and acting as an inorganic phosphate reservoir. Phytases are phosphatases that hydrolyze phytate to less-phosphorylated myo-inositol derivatives and inorganic phosphate. The active-site sequence (HCXXGXGR) of the phytase identified from the gut micro-organizm Selenomonas ruminantium forms a loop (P loop) at the base of a substrate binding pocket that is characteriztic of protein tyrosine phosphatases (PTPs). The depth of this pocket is an important determinant of the substrate specificity of PTPs. In humans this enzyme is thought to aid bone mineralization and salvage the inositol moiety prior to apoptosis. Pssm-ID: 464208 [Multi-domain] Cd Length: 157 Bit Score: 174.81 E-value: 1.37e-50
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| PTPlike_phytase | pfam14566 | Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in ... |
545-677 | 5.24e-31 | |||||
Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in abundance in seeds and acting as an inorganic phosphate reservoir. Phytases are phosphatases that hydrolyze phytate to less-phosphorylated myo-inositol derivatives and inorganic phosphate. The active-site sequence (HCXXGXGR) of the phytase identified from the gut micro-organizm Selenomonas ruminantium forms a loop (P loop) at the base of a substrate binding pocket that is characteriztic of protein tyrosine phosphatases (PTPs). The depth of this pocket is an important determinant of the substrate specificity of PTPs. In humans this enzyme is thought to aid bone mineralization and salvage the inositol moiety prior to apoptosis. Pssm-ID: 464208 [Multi-domain] Cd Length: 157 Bit Score: 118.95 E-value: 5.24e-31
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| CDC14 | COG2453 | Protein-tyrosine phosphatase [Signal transduction mechanisms]; |
618-677 | 3.13e-09 | |||||
Protein-tyrosine phosphatase [Signal transduction mechanisms]; Pssm-ID: 441989 [Multi-domain] Cd Length: 140 Bit Score: 56.13 E-value: 3.13e-09
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| Name | Accession | Description | Interval | E-value | |||||
| PTP_paladin_2 | cd17660 | protein tyrosine phosphatase-like domain of paladin, repeat 2; Paladin is a putative ... |
477-733 | 6.51e-117 | |||||
protein tyrosine phosphatase-like domain of paladin, repeat 2; Paladin is a putative phosphatase, which in mouse is expressed in endothelial cells during embryonic development and in arterial smooth muscle cells in adults. It has been suggested to be an antiphosphatase that regulates the activity of specific neural crest regulatory factors and thus, modulates neural crest cell formation and migration. Paladin contains two tyrosine-protein phosphatase domains. This model represents repeat 2. Pssm-ID: 350498 Cd Length: 216 Bit Score: 353.70 E-value: 6.51e-117
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| PTP_paladin_1 | cd17659 | protein tyrosine phosphatase-like domain of paladin, repeat 1; Paladin is a putative ... |
91-382 | 9.02e-99 | |||||
protein tyrosine phosphatase-like domain of paladin, repeat 1; Paladin is a putative phosphatase, which in mouse is expressed in endothelial cells during embryonic development and in arterial smooth muscle cells in adults. It has been suggested to be an antiphosphatase that regulates the activity of specific neural crest regulatory factors and thus, modulates neural crest cell formation and migration. Paladin contains two tyrosine-protein phosphatase domains. This model represents repeat 1. Pssm-ID: 350497 Cd Length: 220 Bit Score: 306.78 E-value: 9.02e-99
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| PTPlike_phytase | pfam14566 | Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in ... |
161-330 | 1.37e-50 | |||||
Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in abundance in seeds and acting as an inorganic phosphate reservoir. Phytases are phosphatases that hydrolyze phytate to less-phosphorylated myo-inositol derivatives and inorganic phosphate. The active-site sequence (HCXXGXGR) of the phytase identified from the gut micro-organizm Selenomonas ruminantium forms a loop (P loop) at the base of a substrate binding pocket that is characteriztic of protein tyrosine phosphatases (PTPs). The depth of this pocket is an important determinant of the substrate specificity of PTPs. In humans this enzyme is thought to aid bone mineralization and salvage the inositol moiety prior to apoptosis. Pssm-ID: 464208 [Multi-domain] Cd Length: 157 Bit Score: 174.81 E-value: 1.37e-50
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| PTP_paladin | cd14496 | protein tyrosine phosphatase-like domains of paladin; Paladin is a putative phosphatase, which ... |
91-382 | 1.46e-50 | |||||
protein tyrosine phosphatase-like domains of paladin; Paladin is a putative phosphatase, which in mouse is expressed in endothelial cells during embryonic development and in arterial smooth muscle cells in adults. It has been suggested to be an antiphosphatase that regulates the activity of specific neural crest regulatory factors and thus, modulates neural crest cell formation and migration. Paladin contains two protein tyrosine phosphatase (PTP)-like domains. This model represents both repeats. Pssm-ID: 350346 [Multi-domain] Cd Length: 185 Bit Score: 175.51 E-value: 1.46e-50
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| PTP_paladin | cd14496 | protein tyrosine phosphatase-like domains of paladin; Paladin is a putative phosphatase, which ... |
497-733 | 3.00e-49 | |||||
protein tyrosine phosphatase-like domains of paladin; Paladin is a putative phosphatase, which in mouse is expressed in endothelial cells during embryonic development and in arterial smooth muscle cells in adults. It has been suggested to be an antiphosphatase that regulates the activity of specific neural crest regulatory factors and thus, modulates neural crest cell formation and migration. Paladin contains two protein tyrosine phosphatase (PTP)-like domains. This model represents both repeats. Pssm-ID: 350346 [Multi-domain] Cd Length: 185 Bit Score: 172.04 E-value: 3.00e-49
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| PTPlike_phytase | pfam14566 | Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in ... |
545-677 | 5.24e-31 | |||||
Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in abundance in seeds and acting as an inorganic phosphate reservoir. Phytases are phosphatases that hydrolyze phytate to less-phosphorylated myo-inositol derivatives and inorganic phosphate. The active-site sequence (HCXXGXGR) of the phytase identified from the gut micro-organizm Selenomonas ruminantium forms a loop (P loop) at the base of a substrate binding pocket that is characteriztic of protein tyrosine phosphatases (PTPs). The depth of this pocket is an important determinant of the substrate specificity of PTPs. In humans this enzyme is thought to aid bone mineralization and salvage the inositol moiety prior to apoptosis. Pssm-ID: 464208 [Multi-domain] Cd Length: 157 Bit Score: 118.95 E-value: 5.24e-31
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| PTP_paladin_2 | cd17660 | protein tyrosine phosphatase-like domain of paladin, repeat 2; Paladin is a putative ... |
94-379 | 1.64e-22 | |||||
protein tyrosine phosphatase-like domain of paladin, repeat 2; Paladin is a putative phosphatase, which in mouse is expressed in endothelial cells during embryonic development and in arterial smooth muscle cells in adults. It has been suggested to be an antiphosphatase that regulates the activity of specific neural crest regulatory factors and thus, modulates neural crest cell formation and migration. Paladin contains two tyrosine-protein phosphatase domains. This model represents repeat 2. Pssm-ID: 350498 Cd Length: 216 Bit Score: 96.77 E-value: 1.64e-22
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| PTP_paladin_1 | cd17659 | protein tyrosine phosphatase-like domain of paladin, repeat 1; Paladin is a putative ... |
493-750 | 3.82e-13 | |||||
protein tyrosine phosphatase-like domain of paladin, repeat 1; Paladin is a putative phosphatase, which in mouse is expressed in endothelial cells during embryonic development and in arterial smooth muscle cells in adults. It has been suggested to be an antiphosphatase that regulates the activity of specific neural crest regulatory factors and thus, modulates neural crest cell formation and migration. Paladin contains two tyrosine-protein phosphatase domains. This model represents repeat 1. Pssm-ID: 350497 Cd Length: 220 Bit Score: 69.50 E-value: 3.82e-13
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| PTPLP-like | cd14495 | Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily ... |
516-673 | 1.00e-09 | |||||
Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily contains the tandem protein tyrosine phosphatase (PTP)-like domains of protein tyrosine phosphatase-like phytases (PTPLPs) and similar domains including the PTP domain of Pseudomonas syringae tyrosine-protein phosphatase hopPtoD2. PTPLPs, also known as cysteine phytases, are one of four known classes of phytases, enzymes that degrade phytate (inositol hexakisphosphate [InsP(6)]) to less-phosphorylated myo-inositol derivatives. Phytate is the most abundant cellular inositol phosphate and plays important roles in a broad scope of cellular processes, including DNA repair, RNA processing and export, development, apoptosis, and pathogenicity. PTPLPs adopt a PTP fold, including the active-site signature sequence (CX5R(S/T)) and utilize a classical PTP reaction mechanism. However, these enzymes display no catalytic activity against classical PTP substrates due to several unique structural features that confer specificity for myo-inositol polyphosphates. Pssm-ID: 350345 Cd Length: 278 Bit Score: 60.47 E-value: 1.00e-09
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| CDC14 | COG2453 | Protein-tyrosine phosphatase [Signal transduction mechanisms]; |
618-677 | 3.13e-09 | |||||
Protein-tyrosine phosphatase [Signal transduction mechanisms]; Pssm-ID: 441989 [Multi-domain] Cd Length: 140 Bit Score: 56.13 E-value: 3.13e-09
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| DUSP23 | cd14504 | dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ... |
617-672 | 4.90e-08 | |||||
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as VH1-like phosphatase Z (VHZ) or low molecular mass dual specificity phosphatase 3 (LDP-3), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP23 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is able to enhance activation of JNK and p38 MAPK, and has been shown to dephosphorylate p44-ERK1 (MAPK3) in vitro. It has been associated with cell growth and human primary cancers. It has also been identified as a cell-cell adhesion regulatory protein; it promotes the dephosphorylation of beta-catenin at Tyr 142 and enhances the interaction between alpha- and beta-catenin. Pssm-ID: 350354 [Multi-domain] Cd Length: 142 Bit Score: 52.66 E-value: 4.90e-08
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| CDKN3-like | cd14505 | cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ... |
619-670 | 1.12e-03 | |||||
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of eukaryotic cyclin-dependent kinase inhibitor 3 (CDKN3) and related archaeal and bacterial proteins. CDKN3 is also known as kinase-associated phosphatase (KAP), CDK2-associated dual-specificity phosphatase, cyclin-dependent kinase interactor 1 (CDI1), or cyclin-dependent kinase-interacting protein 2 (CIP2). It has been characterized as dual-specificity phosphatase, which function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and protein-tyrosine-phosphatase (EC 3.1.3.48). It dephosphorylates CDK2 at a threonine residue in a cyclin-dependent manner, resulting in the inhibition of G1/S cell cycle progression. It also interacts with CDK1 and controls progression through mitosis by dephosphorylating CDC2. CDKN3 may also function as a tumor suppressor; its loss of function was found in a variety of cancers including glioblastoma and hepatocellular carcinoma. However, it has also been found over-expressed in many cancers such as breast, cervical, lung and prostate cancers, and may also have an oncogenic function. Pssm-ID: 350355 [Multi-domain] Cd Length: 163 Bit Score: 40.71 E-value: 1.12e-03
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| PTP_DSP_cys | cd14494 | cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ... |
279-336 | 1.76e-03 | |||||
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: 38.87 E-value: 1.76e-03
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| Blast search parameters | ||||
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