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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
A0A484CBV0CAP-ZIP_m domain-containing protein. (2721 aa)    
Predicted Functional Partners:
A0A484C5K9
Vacuolar protein sorting-associated protein 29; Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway.
    
 
 0.977
A0A484BZW0
Uncharacterized protein.
    
 
 0.975
A0A484D1Y9
Uncharacterized protein.
   
 
 0.971
A0A484DA18
Uncharacterized protein.
   
 
 0.970
A0A484D334
WASH_WAHD domain-containing protein.
    
 
 0.969
A0A484DP30
Vacuolar protein sorting-associated protein 35; Plays a role in vesicular protein sorting.
    
 
 0.958
A0A484DB07
Uncharacterized protein.
    
 
 0.941
A0A484CIZ7
Uncharacterized protein.
    
 
 0.925
A0A484D900
Uncharacterized protein.
    
 
 0.925
A0A484DG39
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.
    
 
 0.911
Your Current Organism:
Perca flavescens
NCBI taxonomy Id: 8167
Other names: Morone flavescens, P. flavescens, yellow perch
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