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
C34B2.10Probable signal peptidase complex subunit 1; Microsomal signal peptidase is a membrane-bound endoproteinase that removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. (105 aa)    
Predicted Functional Partners:
hpo-21
Probable signal peptidase complex subunit 2; Component of the microsomal signal peptidase complex which removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum.
   
 0.997
K12H4.4
Probable signal peptidase complex subunit 3; Component of the microsomal signal peptidase complex which removes signal peptides and other N-terminal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum.
   
 0.985
Y54E10BR.5
Signal peptidase complex catalytic subunit SEC11.
   
 0.983
dad-1
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit dad-1; Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol- pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across th [...]
   
    0.851
Y38F2AR.9
Protein transport protein Sec61 subunit beta; Necessary for protein translocation in the endoplasmic reticulum.
   
 
 0.836
emo-1
Protein transport protein Sec61 subunit gamma; Required for oocyte development and ovulation. Required for the translocation of secretory and transmembrane proteins into the endoplasmic reticulum in vitro ; Belongs to the SecE/SEC61-gamma family.
   
  
 0.802
immp-1
Peptidase_S24 domain-containing protein.
   
 
 0.784
immp-2
Inner Mitochondrial Membrane Protease.
   
 
 0.784
Y57E12AM.1
Transmembrane protein 258; Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol- pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are requ [...]
   
    0.756
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).
   
  
 0.749
Your Current Organism:
Caenorhabditis elegans
NCBI taxonomy Id: 6239
Other names: C. elegans, Rhabditis elegans, roundworm
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