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
srpa-72Signal recognition particle subunit SRP72; Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. Binds the 7S RNA only in presence of SRP68. This ribonucleoprotein complex might interact directly with the docking protein in the ER membrane and possibly participate in the elongation arrest function (By similarity). (635 aa)    
Predicted Functional Partners:
F21D5.7
Signal recognition particle 54 kDa protein; Binds to the signal sequence of presecretory protein when they emerge from the ribosomes and transfers them to TRAM (translocating chain-associating membrane protein). Belongs to the GTP-binding SRP family. SRP54 subfamily.
   
 0.999
F25G6.8
Signal recognition particle 14 kDa protein; Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding (By similarity).
    
 0.999
F37F2.2
Probable signal recognition particle 19 kDa protein; Signal-recognition-particle assembly, binds directly to 7S RNA and mediates binding of the 54 kDa subunit of the SRP.
   
 0.999
srpa-68
Probable signal recognition particle subunit SRP68; Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP68 binds the 7S RNA, SRP72 binds to this complex subsequently. This ribonucleoprotein complex might interact directly with the docking protein in the ER membrane and possibly participate in the elongation arrest function (By similarity).
   
 0.999
ZK512.4
Signal recognition particle 9 kDa protein; Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding (By similarity).
    
 0.999
F38A1.8
SRP54 domain-containing protein.
   
 
 0.986
F25G6.9
Uncharacterized protein.
    
 0.942
R186.3
Uncharacterized protein.
   
 
 0.942
rpl-16
60S ribosomal protein L13a; Belongs to the universal ribosomal protein uL13 family.
   
 
 0.927
rpl-39
60S ribosomal protein L39.
   
 
 0.893
Your Current Organism:
Caenorhabditis elegans
NCBI taxonomy Id: 6239
Other names: C. elegans, Rhabditis elegans, roundworm
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.