STRINGSTRING
PP1S130_78V6.2 protein (Physcomitrella patens) - STRING interaction network
"PP1S130_78V6.2" - Predicted protein in Physcomitrella patens
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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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
Cooccurence
Coexpression
Experiments
Databases
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[Homology]
Score
PP1S130_78V6.2Predicted protein (450 aa)    
Predicted Functional Partners:
PP1S229_38V6.1
Predicted protein (927 aa)
     
 
  0.967
PP1S62_215V6.1
Annotation not available (1149 aa)
     
 
  0.967
PP1S43_137V6.1
Predicted protein; Subunit of clathrin-associated adaptor protein complex that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules (900 aa)
     
 
  0.875
PP1S42_100V6.1
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 (953 aa)
     
 
  0.875
PP1S338_11V6.1
Predicted protein; Subunit of clathrin-associated adaptor protein complex that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules (899 aa)
     
 
  0.875
PP1S309_15V6.1
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 (956 aa)
     
 
  0.875
PP1S281_58V6.1
Predicted protein; Subunit of clathrin-associated adaptor protein complex that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules (900 aa)
     
 
  0.875
PP1S168_28V6.1
Beta-coat protein ; 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 (954 aa)
     
 
  0.875
PP1S138_133V6.1
Annotation not available (463 aa)
     
 
  0.875
PP1S138_132V6.1
Annotation not available (161 aa)
     
 
  0.875
Your Current Organism:
Physcomitrella patens
NCBI taxonomy Id: 3218
Other names: Bryophyta, Bryophytina, Bryopsida, Funariaceae, Funariales, Funariidae, Moss Superclass V, Musci, P. patens, Physcomitrella, Physcomitrella Bruch & Schimp, Physcomitrella patens, Physcomitrella patens (Hedw.) Bruch & Schimp., Physcomitrium patens, Physcomitrium patens (Hedw.) Mitt., bryophytes, mosses
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