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
A3770_02p16690Heavy chain of dynein. (4045 aa)    
Predicted Functional Partners:
A3770_11p63340
Rab-GAP TBC domain-containing protein.
    
 0.813
A3770_01p06780
Dynein light chain roadblock.
    
 0.757
A3770_01p08480
WD repeat domain-containing protein.
  
 0.713
A3770_02p13330
WD40 repeat domain-containing protein.
  
 0.701
A3770_16p76610
Uncharacterized protein.
  
 0.697
A3770_03p20170
Caltractin.
    
 0.680
A3770_06p42120
Tubulin beta chain; Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.
 
  
 0.678
A3770_05p38430
Epsilon tubulin; Belongs to the tubulin family.
    
 0.678
A3770_07p48380
Tubulin beta chain; Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.
 
  
 0.678
A3770_01p04550
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.
    
  0.669
Your Current Organism:
Chloropicon primus
NCBI taxonomy Id: 1764295
Other names: C. primus, Chlorophyta sp. CCMP1205, Chloropicon primus Lopes dos Santos & Eikrem, 2017, Coccoid green alga CCMP1205, Prasino-clade-7_X-A2 sp. RCC717, Prasino-clade-7_X-A3 sp. RCC1019, Prasino-clade-7_X-A3 sp. RCC1032, Prasino-clade-7_X-A3 sp. RCC1043, Prasinophyceae sp. CCMP1205, Prasinophyceae sp. RCC1019 (clade 7X-A3), Prasinophyceae sp. RCC1032 (clade 7X-A3), Prasinophyceae sp. RCC1032 (clade VIIA), Prasinophyceae sp. RCC1043 (clade 7X-A3), Prasinophyceae sp. RCC717 (clade 7X-A2), coccoid chlorophyte sp. CCMP1205, coccoid prasinophyte sp. CCMP1205, prasinophyte sp. CCMP1205, prasinophyte sp. NIES-3671, prasinophyte sp. NIES-3671 (clade VIIA3), prasinophyte sp. RCC1019, prasinophyte sp. RCC1019 (clade VIIA3), prasinophyte sp. RCC1032, prasinophyte sp. RCC1032 (clade VIIA), prasinophyte sp. RCC1032 (clade VIIA3), prasinophyte sp. RCC1043, prasinophyte sp. RCC1043 (clade VIIA3), prasinophyte sp. RCC717, prasinophyte sp. RCC717 (clade VIIA2)
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