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:
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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
SRP101Signal recognition particle (SRP) receptor alpha subunit; contain GTPase domains; involved in SRP-dependent protein targeting; interacts with the beta subunit, Srp102p (621 aa)    
Predicted Functional Partners:
SRP102
Signal recognition particle (SRP) receptor beta subunit; involved in SRP-dependent protein targeting; anchors the alpha subunit, Srp101p to the ER membrane
   
 0.999
SEC65
Subunit of the signal recognition particle (SRP); involved in protein targeting to the ER; interacts with Srp54p; homolog of mammalian SRP19
   
 
 0.997
SRP54
Signal recognition particle (SRP) subunit (homolog of mammalian SRP54); contains the signal sequence-binding activity of SRP, interacts with the SRP RNA, and mediates binding of SRP to signal receptor; contains GTPase domain
 
 
0.987
SRP72
Signal recognition particle subunit srp72; Core component of the signal recognition particle (SRP); the SRP is a ribonucleoprotein (RNP) complex that functions in targeting nascent secretory proteins to the endoplasmic reticulum (ER) membrane
   
 
 0.984
PUF6
Pumilio-homology domain protein; binds the 3' UTR of ASH1 mRNA and represses its translation, resulting in proper asymmetric localization of ASH1 mRNA; required at post-transcriptional step for efficient retrotransposition; absence results in decreased Ty1 Gag:GFP protein levels; co-sediments with the 60S ribosomal subunit and is required for its biogenesis; Belongs to the PUF6 family
    
 
 0.983
SRP68
Core component of the signal recognition particle (SRP) complex; SRP complex functions in targeting nascent secretory proteins to the endoplasmic reticulum (ER) membrane; relocalizes from cytoplasm to the nuclear periphery upon DNA replication stress; Belongs to the SRP68 family
   
 
 0.972
SEC61
Conserved ER protein translocation channel; essential subunit of Sec61 complex (Sec61p, Sbh1p, and Sss1p); forms channel for SRP-dependent protein import; with Sec63 complex allows SRP-independent protein import into ER; involved in posttranslational soluble protein import into the ER, ERAD of soluble substrates, and misfolded soluble protein export from the ER
  
 
 0.938
SRP14
Signal recognition particle (SRP) subunit; interacts with the RNA component of SRP to form the Alu domain, which is the region of SRP responsible for arrest of nascent chain elongation during membrane targeting; homolog of mammalian SRP14
   
 
 0.916
RPL5
Ribosomal 60S subunit protein L5; nascent Rpl5p is bound by specific chaperone Syo1p during translation; homologous to mammalian ribosomal protein L5 and bacterial L18; binds 5S rRNA and is required for 60S subunit assembly; Belongs to the universal ribosomal protein uL18 family
  
 
 0.879
RPL25
Ribosomal 60S subunit protein L25; primary rRNA-binding ribosomal protein component of large ribosomal subunit; binds to 25S rRNA via a conserved C-terminal motif; homologous to mammalian ribosomal protein L23A and bacterial L23; Belongs to the universal ribosomal protein uL23 family
  
 
 0.872
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: ATCC 18824, Candida robusta, NRRL Y-12632, S. cerevisiae, Saccharomyces capensis, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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