STRINGSTRING
RPL24B protein (Saccharomyces cerevisiae) - STRING interaction network
"RPL24B" - Ribosomal protein L30 of the large in Saccharomyces cerevisiae
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 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
RPL24BRibosomal protein L30 of the large (60S) ribosomal subunit, nearly identical to Rpl24Ap and has similarity to rat L24 ribosomal protein; not essential for translation but may be required for normal translation rate (155 aa)    
Predicted Functional Partners:
RPL11B
Protein component of the large (60S) ribosomal subunit, nearly identical to Rpl11Ap; involved in ribosomal assembly; depletion causes degradation of proteins and RNA of the 60S subunit; has similarity to E. coli L5 and rat L11; Binds to 5S ribosomal RNA (174 aa)
     
 
  0.999
RPL19B
Protein component of the large (60S) ribosomal subunit, nearly identical to Rpl19Ap and has similarity to rat L19 ribosomal protein; rpl19a and rpl19b single null mutations result in slow growth, while the double null mutation is lethal (189 aa)
     
 
  0.999
RPL11A
Protein of the large 60S ribosomal subunit, nearly identical to Rpl11Bp but expressed at twice the level; involved in ribosomal assembly; depletion causes degradation of 60S proteins and RNA; similar to E. coli L5 and rat L11; Binds to 5S ribosomal RNA (174 aa)
     
 
  0.999
RPL9A
Protein component of the large (60S) ribosomal subunit, nearly identical to Rpl9Bp and has similarity to E. coli L6 and rat L9 ribosomal proteins (191 aa)
     
 
  0.999
RPS26A
Protein component of the small (40S) ribosomal subunit; nearly identical to Rps26Bp and has similarity to rat S26 ribosomal protein (119 aa)
     
 
  0.999
RPL18A
Protein component of the large (60S) ribosomal subunit, identical to Rpl18Bp and has similarity to rat L18 ribosomal protein; intron of RPL18A pre-mRNA forms stem-loop structures that are a target for Rnt1p cleavage leading to degradation (186 aa)
     
 
  0.999
RPS18B
Protein component of the small (40S) ribosomal subunit; nearly identical to Rps18Ap and has similarity to E. coli S13 and rat S18 ribosomal proteins; Located at the top of the head of the 40S subunit, it contacts several helices of the 18S rRNA (146 aa)
     
 
  0.999
RPL19A
Protein component of the large (60S) ribosomal subunit, nearly identical to Rpl19Bp and has similarity to rat L19 ribosomal protein; rpl19a and rpl19b single null mutations result in slow growth, while the double null mutation is lethal (189 aa)
     
 
  0.999
RPL21A
Protein component of the large (60S) ribosomal subunit, nearly identical to Rpl21Bp and has similarity to rat L21 ribosomal protein (160 aa)
     
 
  0.999
RPS3
Protein component of the small (40S) ribosomal subunit, has apurinic/apyrimidinic (AP) endonuclease activity; essential for viability; has similarity to E. coli S3 and rat S3 ribosomal proteins (240 aa)
     
 
  0.999
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
Server load: low (4%) [HD]