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  • 11.0 [archived version]
STRINGSTRING
PTPRR PTPRR PTPN7 PTPN7 PTPN5 PTPN5 PTPRK PTPRK RESP18 RESP18 PTPRQ PTPRQ PTPRT PTPRT PTPRM PTPRM PTPN18 PTPN18 PTPRN2 PTPRN2 PTPRN PTPRN PTPRZ1 PTPRZ1 SLITRK1 SLITRK1 PTPRS PTPRS PTPRD PTPRD YWHAB YWHAB PTPRE PTPRE PTPRF PTPRF PTPRU PTPRU PTPRA PTPRA PTPRC PTPRC PTPN9 PTPN9 FRMPD2 FRMPD2 PTPN13 PTPN13 PTPRO PTPRO PTPRG PTPRG
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.
Node Color
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)
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)
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)
RESP18Regulated endocrine-specific protein 18; May play an important regulatory role in corticotrophs; Belongs to the RESP18 family (228 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)
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)
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)
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)
YWHAB14-3-3 protein beta/alpha; Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negative regulator of osteogenesis. Blocks the nuclear translocation of the phosphorylated form (by AKT1) of SRPK2 and antagonizes its stimulatory effect on cyclin D1 expression resulting in blockage of neuronal apoptosis elicited by SRPK2. Negative regulato [...] (246 aa)
PTPRTReceptor-type tyrosine-protein phosphatase T; May be involved in both signal transduction and cellular adhesion in the CNS; Belongs to the protein-tyrosine phosphatase family. Receptor class 2B subfamily (1460 aa)
FRMPD2FERM and PDZ domain-containing protein 2; May play a role in the regulation of tight junction formation. Binds phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2); FERM domain containing (1309 aa)
SLITRK1SLIT and NTRK-like protein 1; It is involved in synaptogenesis and promotes excitatory synapse differentiation. Enhances neuronal dendrite outgrowth (696 aa)
PTPRAReceptor-type tyrosine-protein phosphatase alpha; Protein tyrosine phosphatase, receptor type A; Belongs to the protein-tyrosine phosphatase family. Receptor class 4 subfamily (802 aa)
PTPRDReceptor-type tyrosine-protein phosphatase delta; Can bidirectionally induce pre- and post-synaptic differentiation of neurons by mediating interaction with IL1RAP and IL1RAPL1 trans-synaptically. Involved in pre-synaptic differentiation through interaction with SLITRK2; Belongs to the protein-tyrosine phosphatase family. Receptor class 2A subfamily (1912 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)
PTPRZ1Receptor-type tyrosine-protein phosphatase zeta; Protein tyrosine phosphatase that negatively regulates oligodendrocyte precursor proliferation in the embryonic spinal cord. Required for normal differentiation of the precursor cells into mature, fully myelinating oligodendrocytes. May play a role in protecting oligondendrocytes against apoptosis. May play a role in the establishment of contextual memory, probably via the dephosphorylation of proteins that are part of important signaling cascades (By similarity); Belongs to the protein-tyrosine phosphatase family. Receptor class 5 subfamily (2315 aa)
PTPN13Tyrosine-protein phosphatase non-receptor type 13; Tyrosine phosphatase which regulates negatively FAS- induced apoptosis and NGFR-mediated pro-apoptotic signaling. May regulate phosphoinositide 3-kinase (PI3K) signaling through dephosphorylation of PIK3R2; FERM domain containing (2490 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)
PTPRGReceptor-type tyrosine-protein phosphatase gamma; Possesses tyrosine phosphatase activity; Fibronectin type III domain containing (1445 aa)
PTPRMReceptor-type tyrosine-protein phosphatase mu; Involved in cell-cell adhesion through homophilic interactions. May play a key role in signal transduction and growth control; Fibronectin type III domain containing (1465 aa)
PTPN9Tyrosine-protein phosphatase non-receptor type 9; Protein-tyrosine phosphatase that could participate in the transfer of hydrophobic ligands or in functions of the Golgi apparatus; Belongs to the protein-tyrosine phosphatase family. Non-receptor class 3 subfamily (593 aa)
PTPRQPhosphatidylinositol phosphatase PTPRQ; Phosphatidylinositol phosphatase required for auditory function. May act by regulating the level of phosphatidylinositol 4,5-bisphosphate (PIP2) level in the basal region of hair bundles. Can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates. Phosphate can be hydrolyzed from the D3 and D5 positions in the inositol ring. Has low tyrosine-protein phosphatase activity; however, the relevance of such activity in vivo is unc [...] (2299 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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