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EFB1 protein (Saccharomyces cerevisiae) - STRING interaction network
"EFB1" - Translation elongation factor 1 beta in Saccharomyces cerevisiae
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second shell of interactors
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proteins of unknown 3D structure
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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EFB1Translation elongation factor 1 beta; stimulates nucleotide exchange to regenerate EF-1 alpha-GTP for the next elongation cycle; part of the EF-1 complex, which facilitates binding of aminoacyl-tRNA to the ribosomal A site; Catalytic subunit of the guanine nucleotide exchange factor (GEF) (eEF1B subcomplex) of the eukaryotic elongation factor 1 complex (eEF1). Stimulates the exchange of GDP for GTP on elongation factor 1A (eEF1A), probably by displacing GDP from the nucleotide binding pocket in eEF1A. The 30-fold higher concentration of GTP compared to GDP in cells favors the formation [...] (206 aa)    
Predicted Functional Partners:
TEF4
Gamma subunit of translational elongation factor eEF1B, stimulates the binding of aminoacyl-tRNA (AA-tRNA) to ribosomes by releasing eEF1A (Tef1p/Tef2p) from the ribosomal complex; Subunit of the eukaryotic elongation factor 1 complex (eEF1). Probably plays a role in anchoring the complex to other cellular components (By similarity) (412 aa)
     
  0.999
CAM1
Nuclear protein required for transcription of MXR1; binds the MXR1 promoter in the presence of other nuclear factors; binds calcium and phospholipids; has similarity to translational cofactor EF-1 gamma; Subunit of the eukaryotic elongation factor 1 complex (eEF1). Probably plays a role in anchoring the complex to other cellular components. May be involved in transcriptional regulation of MXR1 (415 aa)
     
  0.999
TEF1
Translational elongation factor EF-1 alpha; also encoded by TEF2; functions in the binding reaction of aminoacyl-tRNA (AA-tRNA) to ribosomes; may also have a role in tRNA re-export from the nucleus; GTP-binding component of the eukaryotic elongation factor 1 complex (eEF1). In its active GTP-bound form, binds to and delivers aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. In the presence of a correct codon-anticodon match between the aminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, the ribosome acts as a GTPase activator and the GTP is hydrolyzed. [...] (458 aa)
     
  0.999
TEF2
Translational elongation factor EF-1 alpha; also encoded by TEF1; functions in the binding reaction of aminoacyl-tRNA (AA-tRNA) to ribosomes; may also have a role in tRNA re-export from the nucleus (458 aa)
     
  0.999
RPL15A
Protein component of the large (60S) ribosomal subunit, nearly identical to Rpl15Bp and has similarity to rat L15 ribosomal protein; binds to 5.8 S rRNA (204 aa)
     
      0.992
RPP0
Conserved ribosomal protein P0 of the ribosomal stalk, which is involved in interaction between translational elongation factors and the ribosome; similar to rat P0, human P0, and E. coli L10e; phosphorylated on serine 302; Ribosomal protein P0 is the functional equivalent of E.coli protein L10 (312 aa)
   
   
  0.988
RPL1B
N-terminally acetylated protein component of the large (60S) ribosomal subunit, nearly identical to Rpl1Ap and has similarity to E. coli L1 and rat L10a ribosomal proteins; rpl1a rpl1b double null mutation is lethal (217 aa)
   
 
  0.987
RPL31A
Protein component of the large (60S) ribosomal subunit, nearly identical to Rpl31Bp and has similarity to rat L31 ribosomal protein; associates with the karyopherin Sxm1p; loss of both Rpl31p and Rpl39p confers lethality (113 aa)
     
   
  0.986
RPL31B
Protein component of the large (60S) ribosomal subunit, nearly identical to Rpl31Ap and has similarity to rat L31 ribosomal protein; associates with the karyopherin Sxm1p; loss of both Rpl31p and Rpl39p confers lethality (113 aa)
     
   
  0.983
RPL1A
N-terminally acetylated protein component of the large (60S) ribosomal subunit, nearly identical to Rpl1Bp and has similarity to E. coli L1 and rat L10a ribosomal proteins; rpl1a rpl1b double null mutation is lethal (217 aa)
   
 
  0.983
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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