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STRINGSTRING
PTPRD PTPRD PPFIBP2 PPFIBP2 TRAF7 TRAF7 GRIP1 GRIP1 PPFIA3 PPFIA3 PPFIA1 PPFIA1 PPFIA4 PPFIA4 PPFIA2 PPFIA2 PTPRF PTPRF PTPRS PTPRS KALRN KALRN HSF4 HSF4 PLEKHG4B PLEKHG4B TRIO TRIO PTPRC PTPRC KAZN KAZN
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:
KALRNKalirin; Promotes the exchange of GDP by GTP. Activates specific Rho GTPase family members, thereby inducing various signaling mechanisms that regulate neuronal shape, growth, and plasticity, through their effects on the actin cytoskeleton. Induces lamellipodia independent of its GEF activity; Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family (1663 aa)
PPFIA1Liprin-alpha-1; May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates; Sterile alpha motif domain containing (1202 aa)
HSF4Heat shock factor protein 4; DNA-binding protein that specifically binds heat shock promoter elements (HSE). Isoform HSF4A represses transcription while the isoform HSF4B activates transcription (492 aa)
PPFIA4Liprin-alpha-4; May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates (By similarity); Belongs to the liprin family. Liprin-alpha subfamily (701 aa)
PLEKHG4BPleckstrin homology and RhoGEF domain containing G4B (1271 aa)
PPFIBP2Liprin-beta-2; May regulate the disassembly of focal adhesions. Did not bind receptor-like tyrosine phosphatases type 2A; Sterile alpha motif domain containing (876 aa)
TRAF7E3 ubiquitin-protein ligase TRAF7; E3 ubiquitin ligase capable of auto-ubiquitination, following phosphorylation by MAP3K3. Potentiates MEKK3-mediated activation of the NF-kappa-B, JUN/AP1 and DDIT3 transcriptional regulators. Induces apoptosis when overexpressed; Belongs to the WD repeat TRAF7 family (670 aa)
PPFIA3Liprin-alpha-3; May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates; Belongs to the liprin family. Liprin-alpha subfamily (1194 aa)
TRIOTriple functional domain protein; Guanine nucleotide exchange factor (GEF) for RHOA and RAC1 GTPases. Involved in coordinating actin remodeling, which is necessary for cell migration and growth. In developing hippocampal neurons, limits dendrite formation, without affecting the establishment of axon polarity. Once dendrites are formed, involved in the control of synaptic function by regulating the endocytosis of AMPA-selective glutamate receptors (AMPARs) at CA1 excitatory synapses (By similarity). May act as a regulator of adipogenesis (By similarity); Belongs to the protein kinase su [...] (3097 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)
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)
KAZNKazrin; Component of the cornified envelope of keratinocytes. May be involved in the interplay between adherens junctions and desmosomes. The function in the nucleus is not known; Sterile alpha motif domain containing (775 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)
GRIP1Glutamate receptor-interacting protein 1; May play a role as a localized scaffold for the assembly of a multiprotein signaling complex and as mediator of the trafficking of its binding partners at specific subcellular location in neurons. Through complex formation with NSG1, GRIA2 and STX12 controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting (By similarity); PDZ domain containing (1076 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)
PPFIA2Liprin-alpha-2; Alters PTPRF cellular localization and induces PTPRF clustering. May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates; Belongs to the liprin family. Liprin-alpha subfamily (1257 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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