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
K5XTM4_AGABUCoatomer 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. (967 aa)    
Predicted Functional Partners:
K5WN90_AGABU
WD_REPEATS_REGION domain-containing protein.
   
 0.999
K5WWA5_AGABU
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.
   
 0.999
K5Y7T8_AGABU
Coatomer subunit delta; 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.
   
 0.999
K5XKF3_AGABU
Coatomer subunit gamma; 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.
   
 0.998
K5X075_AGABU
Coatomer subunit zeta; The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex.
   
 0.997
K5XEG6_AGABU
Coatomer subunit epsilon; 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. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. Belongs to the COPE family.
   
 0.990
K5XLU1_AGABU
Arf-GAP domain-containing protein.
    
 0.976
K5XXN0_AGABU
Uncharacterized protein; Belongs to the small GTPase superfamily. Arf family.
   
 0.959
K5Y0E3_AGABU
Uncharacterized protein.
   
 0.883
K5XD45_AGABU
ER lumen protein-retaining receptor.
   
 0.864
Your Current Organism:
Agaricus bisporus
NCBI taxonomy Id: 597362
Other names: A. bisporus var. burnettii JB137-S8, Agaricus bisporus var. burnettii JB137-S8
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.