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  • 11.0 [archived version]
STRINGSTRING
PTPRN2 PTPRN2 PTPRE PTPRE PTPRN PTPRN PTPN23 PTPN23 PTPRK PTPRK PTPRS PTPRS PTPN18 PTPN18 PTPRO PTPRO PTPRU PTPRU PTPN14 PTPN14 PTPN5 PTPN5 PTPRF PTPRF PTPRB PTPRB PTPN7 PTPN7 PTPRR PTPRR PTPN11 PTPN11 RESP18 RESP18 PTPN2 PTPN2 PTPN6 PTPN6 KLRD1 KLRD1 PTPN12 PTPN12 PTPN4 PTPN4 TYROBP TYROBP KLRC3 KLRC3 PTPRC PTPRC PTPN22 PTPN22
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
PTPN18Tyrosine-protein phosphatase non-receptor type 18; Differentially dephosphorylate autophosphorylated tyrosine kinases which are known to be overexpressed in tumor tissues; Protein tyrosine phosphatases, non-receptor type (460 aa)
PTPN12Tyrosine-protein phosphatase non-receptor type 12; Dephosphorylates a range of proteins, and thereby regulates cellular signaling cascades. Dephosphorylates cellular tyrosine kinases, such as ERBB2 and PTK2B/PYK2, and thereby regulates signaling via ERBB2 and PTK2B/PYK2. Selectively dephosphorylates ERBB2 phosphorylated at ’Tyr-1112’, ’Tyr-1196’, and/or ’Tyr-1248’; Protein tyrosine phosphatases, non-receptor type (780 aa)
PTPREReceptor-type tyrosine-protein phosphatase epsilon; Isoform 1 plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells. May play a role in osteoclast formation and function (By similarity); Protein tyrosine phosphatases, receptor type (700 aa)
TYROBPTYRO protein tyrosine kinase-binding protein; Non-covalently associates with activating receptors of the CD300 family. Cross-linking of CD300-TYROBP complexes results in cellular activation. Involved for instance in neutrophil activation mediated by integrin (113 aa)
PTPN4Tyrosine-protein phosphatase non-receptor type 4; May act at junctions between the membrane and the cytoskeleton; Belongs to the protein-tyrosine phosphatase family. Non-receptor class subfamily (926 aa)
PTPN23Tyrosine-protein phosphatase non-receptor type 23; Plays a role in sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs) via its interaction with the ESCRT-I complex (endosomal sorting complex required for transport I), and possibly also other ESCRT complexes. May act as a negative regulator of Ras-mediated mitogenic activity. Plays a role in ciliogenesis; Protein tyrosine phosphatases, non-receptor type (1636 aa)
PTPROReceptor-type tyrosine-protein phosphatase O; Possesses tyrosine phosphatase activity. Plays a role in regulating the glomerular pressure/filtration rate relationship through an effect on podocyte structure and function (By similarity); Fibronectin type III domain containing (1216 aa)
PTPRRReceptor-type tyrosine-protein phosphatase R; Sequesters mitogen-activated protein kinases (MAPKs) such as MAPK1, MAPK3 and MAPK14 in the cytoplasm in an inactive form. The MAPKs bind to a dephosphorylated kinase interacting motif, phosphorylation of which by the protein kinase A complex releases the MAPKs for activation and translocation into the nucleus (By similarity); Protein tyrosine phosphatases, receptor type (657 aa)
PTPRNReceptor-type tyrosine-protein phosphatase-like N; Plays a role in vesicle-mediated secretory processes. Required for normal accumulation of secretory vesicles in hippocampus, pituitary and pancreatic islets (By similarity). Required for the accumulation of normal levels of insulin-containing vesicles and preventing their degradation. Plays a role in insulin secretion in response to glucose stimuli. Required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain (By similarity). In females, but not in males, required for normal accumulation [...] (979 aa)
PTPN7Tyrosine-protein phosphatase non-receptor type 7; Protein phosphatase that acts preferentially on tyrosine-phosphorylated MAPK1. Plays a role in the regulation of T and B-lymphocyte development and signal transduction; Belongs to the protein-tyrosine phosphatase family. Non-receptor class subfamily (465 aa)
PTPN2Tyrosine-protein phosphatase non-receptor type 2; Non-receptor type tyrosine-specific phosphatase that dephosphorylates receptor protein tyrosine kinases including INSR, EGFR, CSF1R, PDGFR. Also dephosphorylates non-receptor protein tyrosine kinases like JAK1, JAK2, JAK3, Src family kinases, STAT1, STAT3 and STAT6 either in the nucleus or the cytoplasm. Negatively regulates numerous signaling pathways and biological processes like hematopoiesis, inflammatory response, cell proliferation and differentiation, and glucose homeostasis. Plays a multifaceted and important role in the develop [...] (415 aa)
RESP18Regulated endocrine-specific protein 18; May play an important regulatory role in corticotrophs; Belongs to the RESP18 family (228 aa)
PTPRBReceptor-type tyrosine-protein phosphatase beta; Plays an important role in blood vessel remodeling and angiogenesis. Not necessary for the initial formation of blood vessels, but is essential for their maintenance and remodeling. Can induce dephosphorylation of TEK/TIE2, CDH5/VE-cadherin and KDR/VEGFR-2. Regulates angiopoietin-TIE2 signaling in endothelial cells. Acts as a negative regulator of TIE2, and controls TIE2 driven endothelial cell proliferation, which in turn affects blood vessel remodeling during embryonic development and determines blood vessel size during perinatal growt [...] (2215 aa)
PTPRUReceptor-type tyrosine-protein phosphatase U; Tyrosine-protein phosphatase which dephosphorylates CTNNB1. Regulates CTNNB1 function both in cell adhesion and signaling. May function in cell proliferation and migration and play a role in the maintenance of epithelial integrity. May play a role in megakaryocytopoiesis; Belongs to the protein-tyrosine phosphatase family. Receptor class 2B subfamily (1446 aa)
PTPN11Tyrosine-protein phosphatase non-receptor type 11; Acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus. Positively regulates MAPK signal transduction pathway. Dephosphorylates GAB1, ARHGAP35 and EGFR. Dephosphorylates ROCK2 at ’Tyr-722’ resulting in stimulatation of its RhoA binding activity. Dephosphorylates CDC73; Protein tyrosine phosphatases, non-receptor type (593 aa)
PTPRSReceptor-type tyrosine-protein phosphatase S; Cell surface receptor that binds to glycosaminoglycans, including chondroitin sulfate proteoglycans and heparan sulfate proteoglycan. Binding to chondroitin sulfate and heparan sulfate proteoglycans has opposite effects on PTPRS oligomerization and regulation of neurite outgrowth. Contributes to the inhibition of neurite and axonal outgrowth by chondroitin sulfate proteoglycans, also after nerve transection. Plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. Required for normal brain developm [...] (1948 aa)
PTPN5Tyrosine-protein phosphatase non-receptor type 5; May regulate the activity of several effector molecules involved in synaptic plasticity and neuronal cell survival, including MAPKs, Src family kinases and NMDA receptors; Belongs to the protein-tyrosine phosphatase family. Non-receptor class subfamily (565 aa)
PTPN22Tyrosine-protein phosphatase non-receptor type 22; Acts as negative regulator of T-cell receptor (TCR) signaling by direct dephosphorylation of the Src family kinases LCK and FYN, ITAMs of the TCRz/CD3 complex, as well as ZAP70, VAV, VCP and other key signaling molecules. Associates with and probably dephosphorylates CBL. Dephosphorylates LCK at its activating ’Tyr-394’ residue. Dephosphorylates ZAP70 at its activating ’Tyr- 493’ residue. Dephosphorylates the immune system activator SKAP2. Positively regulates toll-like receptor (TLR)-induced type 1 interferon production. Promotes host [...] (807 aa)
PTPRFReceptor-type tyrosine-protein phosphatase F; Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase) and dephosphorylates EPHA2 regulating its activity; Fibronectin type III domain containing (1907 aa)
PTPN14Tyrosine-protein phosphatase non-receptor type 14; Protein tyrosine phosphatase which may play a role in the regulation of lymphangiogenesis, cell-cell adhesion, cell- matrix adhesion, cell migration, cell growth and also regulates TGF-beta gene expression, thereby modulating epithelial- mesenchymal transition. Mediates beta-catenin dephosphorylation at adhesion junctions. Acts as a negative regulator of the oncogenic property of YAP, a downstream target of the hippo pathway, in a cell density-dependent manner. May function as a tumor suppressor; Belongs to the protein-tyrosine phospha [...] (1187 aa)
PTPRKReceptor-type tyrosine-protein phosphatase kappa; Regulation of processes involving cell contact and adhesion such as growth control, tumor invasion, and metastasis. Negative regulator of EGFR signaling pathway. Forms complexes with beta-catenin and gamma-catenin/plakoglobin. Beta-catenin may be a substrate for the catalytic activity of PTPRK/PTP-kappa; Fibronectin type III domain containing (1446 aa)
KLRC3Killer cell lectin-like receptor subfamily C, member 3; Plays a role as a receptor for the recognition of MHC class I HLA-E molecules by NK cells and some cytotoxic T-cells; C-type lectin domain containing (257 aa)
KLRD1Natural killer cells antigen CD94; Plays a role as a receptor for the recognition of MHC class I HLA-E molecules by NK cells and some cytotoxic T-cells; C-type lectin domain containing (179 aa)
PTPRN2Receptor-type tyrosine-protein phosphatase N2; Plays a role in vesicle-mediated secretory processes. Required for normal accumulation of secretory vesicles in hippocampus, pituitary and pancreatic islets. Required for the accumulation of normal levels of insulin-containing vesicles and preventing their degradation. Plays a role in insulin secretion in response to glucose stimuli. Required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain. In females, but not in males, required for normal accumulation and secretion of pituitary hormones [...] (1015 aa)
PTPN6Tyrosine-protein phosphatase non-receptor type 6; Modulates signaling by tyrosine phosphorylated cell surface receptors such as KIT and the EGF receptor/EGFR. The SH2 regions may interact with other cellular components to modulate its own phosphatase activity against interacting substrates. Together with MTUS1, induces UBE2V2 expression upon angiotensin II stimulation. Plays a key role in hematopoiesis; Protein tyrosine phosphatases, non-receptor type (624 aa)
PTPRCReceptor-type tyrosine-protein phosphatase C; Protein tyrosine-protein phosphatase required for T-cell activation through the antigen receptor. Acts as a positive regulator of T-cell coactivation upon binding to DPP4. The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one. Upon T-cell activation, recruits and dephosphorylates SKAP1 and FYN. Dephosphorylates LYN, and thereby modulates LYN activity (By similarity); Belongs to the protein-tyrosine phosphatase family. Receptor class 1/6 subfamily (1306 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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