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
bma-arp-1BMA-ARP-1. (376 aa)    
Predicted Functional Partners:
Bm1_02805
BMA-DNC-2, isoform e.
   
 0.995
Bma-dnc-4
BMA-DNC-4, isoform a; BMA-DNC-4, isoform c.
   
 0.990
bma-dnc-6
BMA-DNC-6.
    
 0.987
Bm1_17985
BMA-DNC-5.
 
 
 0.983
bma-cap-2
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.
   
 0.971
A0A5S6PY10
Bm9824.
   
 0.949
A0A5S6PY57
Bm9824.
   
 0.949
Bma-cap-1
F-actin-capping protein subunit alpha; 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.
   
 0.880
Bm1_39440
F-actin-capping protein subunit alpha.
   
 0.880
bma-dli-1
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.
   
 0.863
Your Current Organism:
Brugia malayi
NCBI taxonomy Id: 6279
Other names: B. malayi, agent of lymphatic filariasis
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.