Gene Report
Basic Information
| Approved Symbol | PTPN1 |
|---|---|
| Approved Name | protein tyrosine phosphatase, non-receptor type 1 |
| Previous Symbol | PTP1B |
| Location | 20q13.1-q13.2 |
| Position | chr20:49126891-49201088 (+) |
| External Links |
Entrez Gene: 5770 Ensembl: ENSG00000196396 UCSC: uc002xvl.3 HGNC ID: 9642 |
| No. of Studies (Positive/Negative) | 1(1/0)
|
| Type | Literature-origin |
Positive relationships between PTPN1 and MDD (count: 1)
| Name in Literature | Reference | Research Type | Statistical Result | Relation Description | |
|---|---|---|---|---|---|
| Protein tyrosine phosphatase, non-receptor type 1 | Tochigi, 2008 | patients and normal controls | Genes differentially expressed in major depression Genes differentially expressed in major depression |
Positive relationships between PTPN1 and other components at different levels (count: 0)
Positive relationship network of PTPN1 in MK4MDD
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Note:
1. The different color of the nodes denotes the level of the nodes.
| Genetic/Epigenetic Locus | Protein and Other Molecule | Cell and Molecular Pathway | Neural System | Cognition and Behavior | Symptoms and Signs | Environment | MDD |
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2. User can drag the nodes to rearrange the layout of the network. Click the node will enter the report page of the node. Right-click will show also the menus to link to the report page of the node and remove the node and related edges. Hover the node will show the level of the node and hover the edge will show the evidence/description of the edge.
3. The network is generated using Cytoscape Web
Negative relationships between PTPN1 and MDD (count: 0)
Negative relationships between PTPN1 and other components at different levels (count: 0)
PTPN1 related SNPs in MK4MDD (count: 0)
PTPN1 related proteins in MK4MDD (count: 1)
| Approved Name | UniportKB | No. of Studies (Positive/Negative) | Source | |
|---|---|---|---|---|
| Tyrosine-protein phosphatase non-receptor type 1 | P18031 | 0(0/0) | Gene mapped |
PTPN1 related GO terms (count: 28)
Gene mapped GO terms | ||||
| ID | Name | Type | Evidence | |
|---|---|---|---|---|
| GO:0030100 | regulation of endocytosis | biological process | IDA | |
| GO:0046627 | negative regulation of insulin receptor signaling pathway | biological process | NAS[11742412] | |
| GO:0009966 | regulation of signal transduction | biological process | IMP | |
| GO:0005789 | endoplasmic reticulum membrane | cellular component | IEA | |
| GO:0060334 | regulation of interferon-gamma-mediated signaling pathway | biological process | TAS | |
| GO:0019221 | cytokine-mediated signaling pathway | biological process | TAS | |
| GO:0060333 | interferon-gamma-mediated signaling pathway | biological process | TAS | |
| GO:0005886 | plasma membrane | cellular component | IDA | |
| GO:0031410 | cytoplasmic vesicle | cellular component | IEA | |
| GO:0019899 | enzyme binding | molecular function | IPI | |
| GO:0005515 | protein binding | molecular function | IPI[17159996] | |
| GO:0060337 | type I interferon-mediated signaling pathway | biological process | TAS | |
| GO:0005769 | early endosome | cellular component | IDA | |
| GO:0004725 | protein tyrosine phosphatase activity | molecular function | IDA; TAS | |
| GO:0060338 | regulation of type I interferon-mediated signaling pathway | biological process | TAS | |
| GO:0008286 | insulin receptor signaling pathway | biological process | IEA | |
| GO:0060397 | JAK-STAT cascade involved in growth hormone signaling pathway | biological process | TAS | |
| GO:0005783 | endoplasmic reticulum | cellular component | IDA | |
| GO:0007596 | blood coagulation | biological process | TAS | |
| GO:0031532 | actin cytoskeleton reorganization | biological process | IMP | |
| GO:0005158 | insulin receptor binding | molecular function | IEA | |
| GO:0030968 | endoplasmic reticulum unfolded protein response | biological process | IDA | |
| GO:0005829 | cytosol | cellular component | TAS | |
| GO:0019901 | protein kinase binding | molecular function | IPI | |
| GO:0035335 | peptidyl-tyrosine dephosphorylation | biological process | IDA | |
| GO:0008270 | zinc ion binding | molecular function | IDA[18074158] | |
| GO:0030168 | platelet activation | biological process | TAS | |
| GO:0046875 | ephrin receptor binding | molecular function | IPI | |
PTPN1 related KEGG pathways (count: 2)
Gene mapped KEGG pathways | ||||
| ID | Name | Brief Description | Full Description | |
|---|---|---|---|---|
| hsa04520 | adherens junction | Adherens junction | Cell-cell adherens junctions (AJs), the most common type of ...... Cell-cell adherens junctions (AJs), the most common type of intercellular adhesions, are important for maintaining tissue architecture and cell polarity and can limit cell movement and proliferation. At AJs, E-cadherin serves as an essential cell adhesion molecules (CAMs). The cytoplasmic tail binds beta-catenin, which in turn binds alpha-catenin. Alpha-catenin is associated with F-actin bundles directly and indirectly. The integrity of the cadherin-catenin complex is negatively regulated by phosphorylation of beta-catenin by receptor tyrosine kinases (RTKs) and cytoplasmic tyrosine kinases (Fer, Fyn, Yes, and Src), which leads to dissociation of the cadherin-catenin complex. Integrity of this complex is positively regulated by beta -catenin phosphorylation by casein kinase II, and dephosphorylation by protein tyrosine phosphatases. Changes in the phosphorylation state of beta-catenin affect cell-cell adhesion, cell migration and the level of signaling beta-catenin. Wnt signaling acts as a positive regulator of beta-catenin by inhibiting beta-catenin degradation, which stabilizes beta-catenin, and causes its accumulation. Cadherin may acts as a negative regulator of signaling beta-catenin as it binds beta-catenin at the cell surface and thereby sequesters it from the nucleus. Nectins also function as CAMs at AJs, but are more highly concentrated at AJs than E-cadherin. Nectins transduce signals through Cdc42 and Rac, which reorganize the actin cytoskeleton, regulate the formation of AJs, and strengthen cell-cell adhesion. More... | |
| hsa04910 | insulin signaling_pathway | Insulin signaling pathway | Insulin binding to its receptor results in the tyrosine phos...... Insulin binding to its receptor results in the tyrosine phosphorylation of insulin receptor substrates (IRS) by the insulin receptor tyrosine kinase (INSR). This allows association of IRSs with the regulatory subunit of phosphoinositide 3-kinase (PI3K). PI3K activates 3-phosphoinositide-dependent protein kinase 1 (PDK1), which activates Akt, a serine kinase. Akt in turn deactivates glycogen synthase kinase 3 (GSK-3), leading to activation of glycogen synthase (GYS) and thus glycogen synthesis. Activation of Akt also results in the translocation of GLUT4 vesicles from their intracellular pool to the plasma membrane, where they allow uptake of glucose into the cell. Akt also leads to mTOR-mediated activation of protein synthesis by eIF4 and p70S6K. The translocation of GLUT4 protein is also elicited through the CAP/Cbl/TC10 pathway, once Cbl is phosphorylated by INSR. Other signal transduction proteins interact with IRS including GRB2. GRB2 is part of the cascade including SOS, RAS, RAF and MEK that leads to activation of mitogen-activated protein kinase (MAPK) and mitogenic responses in the form of gene transcription. SHC is another substrate of INSR. When tyrosine phosphorylated, SHC associates with GRB2 and can thus activate the RAS/MAPK pathway independently of IRS-1. More... | |
PTPN1 related BioCarta pathways (count: 0)
PTPN1 related Reactome pathways (count: 5)
Gene mapped Reactome pathways | |||
| ID | Name | Description | |
|---|---|---|---|
| REACT_278 | platelet aggregation_plug_formation | The tethering of platelets to the site of vascular injury is...... The tethering of platelets to the site of vascular injury is the first step in the formation of a platelet thrombus. Firm adhesion of these tethered platelets, as well as the additional recruitment of others onto their surface leads to the formation of large platelet aggregates. The formation of a thrombus is strictly dependent on the formation of interplatelet bonds. More... | |
| REACT_13552 | integrin cell_surface_interactions | The extracellular matrix (ECM) is a network of macro-molecul...... The extracellular matrix (ECM) is a network of macro-molecules that underlies all epithelia and endothelia and that surrounds all connective tissue cells. This matrix provides the mechanical strength and also influences the behavior and differentiation state of cells in contact with it. The ECM are diverse in composition, but they generally comprise a mixture of fibrillar proteins, polysaccharides synthesized, secreted and organized by neighboring cells. Collagens, fibronectin, and laminins are the principal components involved in cell matrix interactions; other components, such as vitronectin, thrombospondin, and osteopontin, although less abundant, are also important adhesive molecules. Integrins are the receptors that mediate cell adhesion to ECM. Integrins consists of one alpha and one beta subunit forming a noncovalently bound heterodimer. 18 alpha and 8 beta subunits have been identified in humans that combine to form 24 different receptors. The integrin dimers can be broadly divided into three families consisting of the beta1, beta2/beta7, and beta3/alphaV integrins. beta1 associates with 12 alpha-subunits and can be further divided into RGD-, collagen-, or laminin binding and the related alpha4/alpha9 integrins that recognise both matrix and vascular ligands. beta2/beta7 integrins are restricted to leukocytes and mediate cell-cell rather than cell-matrix interactions, although some recognize fibrinogen. The beta3/alphaV family members are all RGD receptors and comprise aIIbb3, an important receptor on platelets, and the remaining b-subunits, which all associate with alphaV. It is the collagen receptors and leukocyte-specific integrins that contain alpha A-domains. More... | |
| REACT_604 | hemostasis | Two principal mechanisms limit blood loss after vascular inj...... Two principal mechanisms limit blood loss after vascular injury. Initially, platelets are activated, adhere to the site of the injury, and aggregate into a plug that limits blood loss. Proteins and small molecules released from activated platelets stimulate the plug formation process, and fibrinogen from the plasma forms bridges between activated platelets. These events allow the initiation of the clotting cascade, the second mechanism to limit blood loss. Negatively charged phospholipids exposed on cell surfaces at the site of injury and on activated platelets interact with tissue factor, setting off a cascade of reactions leading to generation of fibrin and the formation of an insoluble fibrin clot that strengthens the platelet plug. More... | |
| REACT_15523 | integrin alphaiibbeta3_signaling | At the sites of vascular injury bioactive molecules such as ...... At the sites of vascular injury bioactive molecules such as thrombin, ADP, collagen, fibrinogen and thrombospondin are generated, secreted or exposed. These stimuli activate platelets, converting the major platelet integrin alphaIIbbeta3 from a resting state to an active conformation, in a process termed integrin priming or inside-out signalling. Integrin activation refers to the change required to enhance ligand-binding activity. The activated alphaIIbbeta3 interacts with the fibrinogen and links platelets together in an aggregate to form a platelet plug. AlphaIIbbeta3 bound to fibrin generates more intracellular signals (outside-in signalling), causing further platelet activation and platelet-plug retraction. In the resting state the alpha and beta tails are close together. This interaction keeps the membrane proximal regions in a bent conformation that maintains alphaIIbbeta3 in a low affinity state. Integrin alphaIIbbeta3 is released from its inactive state by interaction with the protein talin. Talin interacts with the beta3 cytoplasmic domain and disrupts the salt bridge between the alpha and beta chains. This separation in the cytoplasmic regions triggers the conformational change in the extracellular domain that increases its affinity to fibrinogen. Much of talin exists in an inactive cytosolic pool, and the Rap1 interacting adaptor molecule (RIAM) is implicated in talin activation and translocation to beta3 integrin cytoplasmic domain. More... | |
| REACT_20 | formation of_platelet_plug | Hemostasis is a physiological response that culminates in th...... Hemostasis is a physiological response that culminates in the arrest of bleeding from an injured vessel. Acute vessel injury results in its constriction to reduce the loss of blood. Under normal conditions vascular endothelium supports vasodilation, inhibits platelet adhesion and activation, suppresses coagulation, enhances fibrin cleavage and is anti-inflammatory in character. Under acute vascular trauma vasoconstrictor mechanisms predominate and the endothelium becomes prothrombotic, procoagulatory and proinflammatory in nature. This is achieved by a reduction of endothelial dilating agents: adenosine, NO and prostacyclin; and the direct action of ADP, serotonin and thromboxane on vascular smooth muscle cells to elicit their contraction. The chief trigger for the change in endothelial function that leads to the formation of haemostatic thrombus is the loss of the endothelial cell barrier between blood and ECM components. Circulating platelets identify and discriminate areas of endothelial lesions; here, they adhere to the exposed sub endothelium. Their interaction with the various thrombogenic substrates and locally generated or released agonists results in platelet activation. This process is described as possessing two stages, firstly, adhesion - the initial tethering to a surface, and secondly aggregation - the platelet-platelet cohesion. More... | |
PTPN1 related interactors from protein-protein interaction data in HPRD (count: 38)