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
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Co-expression
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[Homology]
Score
G1L2S8_AILMENbas_N domain-containing protein. (376 aa)    
Predicted Functional Partners:
ZW10
Zw10 kinetochore protein.
   
 0.969
RINT1
RAD50 interactor 1.
    
 0.968
STX18
Syntaxin 18.
    
 0.946
BNIP1
BCL2 interacting protein 1.
    
 0.939
LOC100466252
Neuroblastoma amplified sequence.
 
     0.938
USE1
Unconventional SNARE in the ER 1.
    
 0.931
NAPG
NSF attachment protein gamma.
    
 0.913
SEC22B
SEC22 homolog B, vesicle trafficking protein (gene/pseudogene); Belongs to the synaptobrevin family.
    
 0.902
SCFD2
Sec1 family domain containing 2; Belongs to the STXBP/unc-18/SEC1 family.
   
 
 0.874
COPB2
Coatomer subunit beta; The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin- coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.
    
 0.819
Your Current Organism:
Ailuropoda melanoleuca
NCBI taxonomy Id: 9646
Other names: A. melanoleuca, giant panda
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