STRINGSTRING
STRING protein interaction network
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:
a 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 to 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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
TJP2Tight junction protein ZO-2; Plays a role in tight junctions and adherens junctions; Belongs to the MAGUK family. (1256 aa)    
Predicted Functional Partners:
TJP1
Tight junction protein ZO-1; TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton. The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Necessary for lumenogenesis, and particularly efficient epithelial polarization and barrier formation. Plays a role in the regulation [...]
  
0.989
AFDN
Afadin, adherens junction formation factor.
   
 0.985
F11R
F11 receptor.
   
 0.974
OCLN
Occludin; May play a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier. Interacts with ZO-1.
   
 
 0.967
RAPGEF2
Rap guanine nucleotide exchange factor 2; Functions as a guanine nucleotide exchange factor (GEF), which activates Rap and Ras family of small GTPases by exchanging bound GDP for free GTP in a cAMP-dependent manner. Serves as a link between cell surface receptors and Rap/Ras GTPases in intracellular signaling cascades. Acts also as an effector for Rap1 by direct association with Rap1-GTP thereby leading to the amplification of Rap1-mediated signaling. Shows weak activity on HRAS. It is controversial whether RAPGEF2 binds cAMP and cGMP or not. Its binding to ligand-activated beta-1 adre [...]
   
 0.944
WWTR1
WW domain containing transcription regulator 1.
   
 0.925
CLDN1
Claudin; Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity; Belongs to the claudin family.
   
 
 0.795
CLDN5
Claudin; Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity; Belongs to the claudin family.
   
 
 0.775
GJA1
Gap junction alpha-1 protein; Gap junction protein that acts as a regulator of bladder capacity. A gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. May play a critical role in the physiology of hearing by participating in the recycling of potassium to the cochlear endolymph. Negative regulator of bladder functional capacity: acts by enhancing intercellular electrical and chemical transmission, thus sensitizing bladder muscles to cholinergic neural stimuli a [...]
   
 
 0.728
CLDN4
Claudin; Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity; Belongs to the claudin family.
   
 
 0.723
Your Current Organism:
Canis lupus familiaris
NCBI taxonomy Id: 9615
Other names: C. lupus familiaris, Canis canis, Canis domesticus, Canis familiaris, beagle dog, beagle dogs, dog, dogs
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