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
RPS8BProtein component of the small (40S) ribosomal subunit; homologous to mammalian ribosomal protein S8, no bacterial homolog; RPS8B has a paralog, RPS8A, that arose from the whole genome duplication. (200 aa)    
Predicted Functional Partners:
RPS11B
Protein component of the small (40S) ribosomal subunit; homologous to mammalian ribosomal protein S11 and bacterial S17; RPS11B has a paralog, RPS11A, that arose from the whole genome duplication.
   
 0.999
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.
   
 0.999
RPS9B
Protein component of the small (40S) ribosomal subunit; homologous to mammalian ribosomal protein S9 and bacterial S4; RPS9B has a paralog, RPS9A, that arose from the whole genome duplication.
   
 0.999
RPS14A
Protein component of the small (40S) ribosomal subunit; required for ribosome assembly and 20S pre-rRNA processing; mutations confer cryptopleurine resistance; homologous to mammalian ribosomal protein S14 and bacterial S11; RPS14A has a paralog, RPS14B, that arose from the whole genome duplication.
   
 0.999
RPS29B
Protein component of the small (40S) ribosomal subunit; homologous to mammalian ribosomal protein S29 and bacterial S14; RPS29B has a paralog, RPS29A, that arose from the whole genome duplication.
   
 0.999
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.
   
 0.999
RPS11A
Protein 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.
   
 0.999
RPS13
Protein component of the small (40S) ribosomal subunit; homologous to mammalian ribosomal protein S13 and bacterial S15.
   
 0.999
RPS17B
Ribosomal protein 51 (rp51) of the small (40s) subunit; homologous to mammalian ribosomal protein S17, no bacterial homolog; RPS17B has a paralog, RPS17A, that arose from the whole genome duplication; protein abundance increases in response to DNA replication stress.
   
 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
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.