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
T1HAE1_RHOPRWD_REPEATS_REGION domain-containing protein. (760 aa)    
Predicted Functional Partners:
R4FMK9_RHOPR
Dynein light chain roadblock.
    
 0.852
R4FM50_RHOPR
Putative dynein light chain.
    
 0.846
T1HXD9_RHOPR
Uncharacterized protein.
    
 0.809
T1HPU2_RHOPR
Dynein light intermediate chain; Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes.
    
 0.748
T1I551_RHOPR
Uncharacterized protein.
    
 0.737
T1IFZ1_RHOPR
Uncharacterized protein.
    
 0.711
T1I355_RHOPR
CAP-Gly domain-containing protein.
   
 0.695
T1I6F7_RHOPR
Uncharacterized protein.
    
 0.695
T1IG42_RHOPR
Uncharacterized protein.
    
  0.695
T1HIQ8_RHOPR
F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.
    
  0.690
Your Current Organism:
Rhodnius prolixus
NCBI taxonomy Id: 13249
Other names: R. prolixus
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