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
CCDC115Coiled-coil domain containing 115. (239 aa)    
Predicted Functional Partners:
ATP6V1H
V-type proton ATPase subunit H; Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit H activates ATPase activity of the enzyme and couples ATPase activity to proton flow. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system.
    
 
 0.706
ATP6V1C1
V-type proton ATPase subunit C; Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
      
 0.699
SERGEF
Secretion regulating guanine nucleotide exchange factor.
      
 0.698
SUSD1
Sushi domain containing 1.
    
 
 0.692
MED10
Mediator of RNA polymerase II transcription subunit 10; Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
    
 0.658
MED17
Mediator of RNA polymerase II transcription subunit 17; Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
    
 0.650
ATP6AP1
ATPase H+ transporting accessory protein 1.
     
 0.649
LOC102358523
Uncharacterized protein.
     
 0.649
ATP6V0D2
V-type proton ATPase subunit; Subunit of the integral membrane V0 complex of vacuolar ATPase. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system. Belongs to the V-ATPase V0D/AC39 subunit family.
    
 
 0.640
ATP6V0D1
V-type proton ATPase subunit; Subunit of the integral membrane V0 complex of vacuolar ATPase. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system. Belongs to the V-ATPase V0D/AC39 subunit family.
    
 
 0.640
Your Current Organism:
Latimeria chalumnae
NCBI taxonomy Id: 7897
Other names: L. chalumnae, coelacanth
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