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SRP54 protein (Saccharomyces cerevisiae) - STRING interaction network
"SRP54" - Signal recognition particle in Saccharomyces cerevisiae
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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
filled nodes:
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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[Homology]
Score
SRP54Signal 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; Signal-recognition-particle (SRP) assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum (ER) membrane. SRP is required for the cotranslational protein translocation for ER import and preferentially recognizes strongly hydrophobic signal sequences. It is involved in targeting the nascent chain-ribosome (RNC) complex to the E [...] (541 aa)    
Predicted Functional Partners:
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; Signal-recognition-particle (SRP) assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum (ER) membrane. SRP is required for the cotranslational protein translocation for ER import and preferentially recognizes strongly hydrophobic signal sequences. It is involved in targeting the nascent chain-ribosome (RNC) co [...] (146 aa)
       
 
  0.999
SEC65
Subunit of the signal recognition particle (SRP), involved in protein targeting to the ER; interacts with Srp54p; homolog of mammalian SRP19; Signal-recognition-particle (SRP) assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum (ER) membrane. SRP is required for the cotranslational protein translocation for ER import and preferentially recognizes strongly hydrophobic signal sequences. It is involved in targeting the nascent chain-ribosome (RNC) complex to the ER and is proposed to participate in the arrest of nascent chain elongation during me [...] (273 aa)
     
 
  0.999
SRP68
Core component of the signal recognition particle (SRP) ribonucleoprotein (RNP) complex that functions in targeting nascent secretory proteins to the endoplasmic reticulum (ER) membrane; Signal-recognition-particle (SRP) assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum (ER) membrane. SRP is required for the cotranslational protein translocation for ER import and preferentially recognizes strongly hydrophobic signal sequences. It is involved in targeting the nascent chain-ribosome (RNC) complex to the ER and is proposed to participate in the [...] (599 aa)
     
 
  0.999
SRP72
Core component of the signal recognition particle (SRP) ribonucleoprotein (RNP) complex that functions in targeting nascent secretory proteins to the endoplasmic reticulum (ER) membrane; Signal-recognition-particle (SRP) assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum (ER) membrane. SRP is required for the cotranslational protein translocation for ER import and preferentially recognizes strongly hydrophobic signal sequences. It is involved in targeting the nascent chain-ribosome (RNC) complex to the ER and is proposed to participate in the [...] (640 aa)
     
 
  0.993
SRP101
Signal recognition particle (SRP) receptor alpha subunit; contain GTPase domains; involved in SRP-dependent protein targeting; interacts with the beta subunit, Srp102p; Component of the SRP (signal recognition particle) receptor. Ensures, in conjunction with the signal recognition particle, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system. GTP hydrolysis may enhance the fidelity of and provide unidirectionality to the targeting reaction. It is important but not essential for cell growth. May be directly involved in mitochondrial prote [...] (621 aa)
 
 
0.977
SRP21
Subunit of the signal recognition particle (SRP); SRP functions in protein targeting to the endoplasmic reticulum membrane; not found in mammalian SRP; forms a pre-SRP structure in the nucleolus that is translocated to the cytoplasm; Signal-recognition-particle (SRP) assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum (ER) membrane. SRP is required for the cotranslational protein translocation for ER import and preferentially recognizes strongly hydrophobic signal sequences. It is involved in targeting the nascent chain-ribosome (RNC) complex [...] (167 aa)
       
 
  0.962
RPL2A
Protein component of the large (60S) ribosomal subunit, identical to Rpl2Bp and has similarity to E. coli L2 and rat L8 ribosomal proteins (254 aa)
     
 
  0.958
RPL25
Primary rRNA-binding ribosomal protein component of the large (60S) ribosomal subunit, has similarity to E. coli L23 and rat L23a ribosomal proteins; binds to 25S rRNA via a conserved C-terminal motif; This protein binds to a specific region on the 26S rRNA (142 aa)
     
 
  0.956
IMG1
Mitochondrial ribosomal protein of the large subunit, required for respiration and for maintenance of the mitochondrial genome; Essential for respiration (169 aa)
   
 
  0.953
MRPL8
Mitochondrial ribosomal protein of the large subunit (238 aa)
   
 
  0.948
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: Candida robusta, Pachytichospora, S. cerevisiae, Saccharomyces, Saccharomyces capensis, Saccharomyces cerevisiae, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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