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PP1S220_70V6.1 protein (Physcomitrella patens) - STRING interaction network
"PP1S220_70V6.1" - AP complex subunit sigma 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
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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
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textmining
co-expression
protein homology
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PP1S220_70V6.1AP complex subunit sigma; Belongs to the adaptor complexes small subunit family (142 aa)    
Predicted Functional Partners:
PP1S54_156V6.1
Predicted protein; Belongs to the adaptor complexes medium subunit family (439 aa)
     
  0.994
PP1S197_28V6.1
Predicted protein; Belongs to the adaptor complexes medium subunit family (439 aa)
     
  0.994
PP1S507_6V6.1
AP-2 complex subunit alpha; Subunit of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome (1055 aa)
     
  0.987
PP1S26_36V6.1
AP-2 complex subunit alpha; Subunit of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome (1036 aa)
     
  0.987
PP1S171_160V6.1
AP-2 complex subunit alpha; Subunit of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome (1051 aa)
     
  0.987
PP1S171_161V6.1
annotation not available (49 aa)
     
 
  0.941
PP1S43_137V6.1
Beta-adaptin-like 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)
     
 
  0.931
PP1S338_11V6.1
Beta-adaptin-like 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)
     
 
  0.931
PP1S281_58V6.1
Beta-adaptin-like 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)
     
 
  0.931
PP1S131_189V6.1
Predicted protein (836 aa)
     
 
  0.931
Your Current Organism:
Physcomitrella patens
NCBI taxonomy Id: 3218
Other names: P. patens, Physcomitrella patens, Physcomitrella patens (Hedw.) Bruch & Schimp., Physcomitrella patens subsp. patens, Physcomitrium patens, Physcomitrium patens (Hedw.) Mitt.
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