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
N300_09001Dynactin subunit 1. (120 aa)    
Predicted Functional Partners:
N300_14526
Dynactin subunit 3.
   
 0.979
N300_01610
Actin-related protein 10; Belongs to the actin family.
    
 0.975
N300_10578
Dynactin subunit 4.
    
 0.972
N300_12484
Alpha-centractin; Belongs to the actin family.
   
 0.971
N300_14220
Dynactin subunit 5.
    
 0.970
N300_02073
Dynactin subunit 6.
    
 0.970
N300_15853
Cytoplasmic dynein 1 heavy chain 1.
   
 0.961
N300_04557
Cytoplasmic dynein 1 intermediate chain 2.
    
 0.954
N300_07610
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.
   
 0.943
N300_10473
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.
    
 0.935
Your Current Organism:
Calypte anna
NCBI taxonomy Id: 9244
Other names: C. anna
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