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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
RPS11AProtein component of the small (40S) ribosomal subunit; homologous to mammalian ribosomal protein S11 and bacterial S17; N-terminally propionylated in vivo; RPS11A has a paralog, RPS11B, that arose from the whole genome duplication. (156 aa)    
Predicted Functional Partners:
RPS13
Protein component of the small (40S) ribosomal subunit; homologous to mammalian ribosomal protein S13 and bacterial S15.
   
 
 0.999
RPS18A
Protein component of the small (40S) ribosomal subunit; homologous to mammalian ribosomal protein S18 and bacterial S13; RPS18A has a paralog, RPS18B, that arose from the whole genome duplication; protein increases in abundance and relocalizes from cytoplasm to nuclear foci upon DNA replication stress.
  
 
 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
RPS3
Protein component of the small (40S) ribosomal subunit; has apurinic/apyrimidinic (AP) endonuclease activity; essential for viability; nascent Rps3p is bound by specific chaperone Yar1p during translation; homologous to mammalian ribosomal protein S3 and bacterial S3.
  
 
 0.999
RPS15
Protein component of the small (40S) ribosomal subunit; homologous to mammalian ribosomal protein S15 and bacterial S19.
  
 
 0.999
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.
  
 
 0.999
RPS8A
Protein component of the small (40S) ribosomal subunit; homologous to mammalian ribosomal protein S8, no bacterial homolog; RPS8A has a paralog, RPS8B, that arose from the whole genome duplication.
   
 
 0.998
RPL32
Ribosomal 60S subunit protein L32; overexpression disrupts telomeric silencing; homologous to mammalian ribosomal protein L32, no bacterial homolog.
  
 
 0.998
RPS6B
Protein component of the small (40S) ribosomal subunit; homologous to mammalian ribosomal protein S6, no bacterial homolog; phosphorylated on S233 by Ypk3p in a TORC1-dependent manner, and on S232 in a TORC1/2-dependent manner by Ypk1/2/3p; RPS6B has a paralog, RPS6A, that arose from the whole genome duplication.
   
 
 0.998
RPS16B
Protein component of the small (40S) ribosomal subunit; homologous to mammalian ribosomal protein S16 and bacterial S9; RPS16B has a paralog, RPS16A, that arose from the whole genome duplication.
  
 
 0.998
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
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.