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
RPL17BRibosomal 60S subunit protein L17B; required for processing of 27SB pre-rRNA and formation of stable 66S assembly intermediates; homologous to mammalian ribosomal protein L17 and bacterial L22; RPL17B has a paralog, RPL17A, that arose from the whole genome duplication. (184 aa)    
Predicted Functional Partners:
RPL32
Ribosomal 60S subunit protein L32; overexpression disrupts telomeric silencing; homologous to mammalian ribosomal protein L32, no bacterial homolog.
  
 
 0.999
RPL35B
Ribosomal 60S subunit protein L35B; homologous to mammalian ribosomal protein L35 and bacterial L29; RPL35B has a paralog, RPL35A, that arose from the whole genome duplication.
  
 0.999
RPL35A
Ribosomal 60S subunit protein L35A; homologous to mammalian ribosomal protein L35 and bacterial L29; RPL35A has a paralog, RPL35B, that arose from the whole genome duplication.
  
 0.999
RPS13
Protein component of the small (40S) ribosomal subunit; homologous to mammalian ribosomal protein S13 and bacterial S15.
   
 
 0.999
RPL37B
Ribosomal 60S subunit protein L37B; required for processing of 27SB pre-rRNA and formation of stable 66S assembly intermediates; protein abundance increases in response to DNA replication stress; homologous to mammalian ribosomal protein L37, no bacterial homolog; RPL37B has a paralog, RPL37A, that arose from the whole genome duplication.
 
 
 0.999
RPL34A
Ribosomal 60S subunit protein L34A; homologous to mammalian ribosomal protein L34, no bacterial homolog; RPL34A has a paralog, RPL34B, that arose from the whole genome duplication.
  
 0.999
RPS2
Protein component of the small (40S) subunit; essential for control of translational accuracy; phosphorylation by C-terminal domain kinase I (CTDK-I) enhances translational accuracy; methylated on one or more arginine residues by Hmt1p; homologous to mammalian ribosomal protein S2 and bacterial S5.
  
 
 0.999
RPL26B
Ribosomal 60S subunit protein L26B; binds to 5.8S rRNA; non-essential even when paralog is also deleted; deletion has minimal affections on ribosome biosynthesis; homologous to mammalian ribosomal protein L26 and bacterial L24; RPL26B has a paralog, RPL26A, that arose from the whole genome duplication.
  
 
 0.999
RPS5
Protein component of the small (40S) ribosomal subunit; least basic of non-acidic ribosomal proteins; phosphorylated in vivo; essential for viability; homologous to mammalian ribosomal protein S5 and bacterial S7.
  
 
 0.999
RPL37A
Ribosomal 60S subunit protein L37A; required for processing of 27SB pre-rRNA and formation of stable 66S assembly intermediates; homologous to mammalian ribosomal protein L37, no bacterial homolog; RPL37A has a paralog, RPL37B, that arose from the whole genome duplication.
 
 
 0.999
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: ATCC 18824, Candida robusta, Mycoderma cerevisiae, NRRL Y-12632, S. cerevisiae, Saccharomyces capensis, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, yeast
Server load: medium (66%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.