STRINGSTRING
SRP72 protein (Latimeria chalumnae) - STRING interaction network
"SRP72" - Signal recognition particle 72kDa in Latimeria chalumnae
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.
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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:
some 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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
SRP72Signal recognition particle 72kDa (239 aa)    
Predicted Functional Partners:
SRP68
Signal recognition particle 68kDa; Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane (607 aa)
     
  0.992
SRP19
Signal recognition particle 19kDa (154 aa)
     
  0.979
SRP54
Signal recognition particle 54kDa (504 aa)
     
  0.931
FTSJ3
FtsJ homolog 3 (E. coli) (710 aa)
     
      0.808
GNL3L
Guanine nucleotide binding protein-like 3 (nucleolar)-like (331 aa)
     
      0.797
GNL3
Guanine nucleotide binding protein-like 3 (nucleolar) (564 aa)
     
      0.797
DDX27
DEAD (Asp-Glu-Ala-Asp) box polypeptide 27 (785 aa)
     
      0.794
SSB
Sjogren syndrome antigen B (autoantigen La) (409 aa)
     
      0.791
SRP9
Signal recognition particle 9kDa; 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 (86 aa)
     
 
  0.708
NOC3L
Nucleolar complex associated 3 homolog (S. cerevisiae) (795 aa)
     
      0.686
Your Current Organism:
Latimeria chalumnae
NCBI taxonomy Id: 7897
Other names: Actinistia, Choanichthyes, Coelacanthidae, Coelacanthiformes, Coelacanthimorpha, Crossopterygii, L. chalumnae, Latimeria, Latimeria chalumnae, Latimeriidae, coelacanth, coelacanths, lobe-finned fishes
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