close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING • newly available directed regulatory networks • a new typed view showing functional, physical, and regulatory edges in one network • new clustering options and cluster-based layouts • … and much more!
Explore STRING v12.5 →
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
Rsad1Radical S-adenosyl methionine domain-containing protein 1, mitochondrial; May be a heme chaperone, appears to bind heme. Homologous bacterial proteins do not have oxygen-independent coproporphyrinogen- III oxidase activity (By similarity). Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl- L-methionine (By similarity). (442 aa)    
Predicted Functional Partners:
Fau
Ubiquitin-like protein FUBI; Belongs to the ubiquitin family.
   
 
 0.998
Rpl31
60S ribosomal protein L31; Belongs to the eukaryotic ribosomal protein eL31 family.
   
 
 0.976
Rpl35a
60S ribosomal protein L35a; Required for the proliferation and viability of hematopoietic cells. Plays a role in 60S ribosomal subunit formation. The protein was found to bind to both initiator and elongator tRNAs and consequently was assigned to the P site or P and A site.
   
 
 0.976
Rps11
40S ribosomal protein S11.
  
 
 0.974
Rps15
40S ribosomal protein S15; Belongs to the universal ribosomal protein uS19 family.
  
 
 0.974
Rpl5
60S ribosomal protein L5; Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through [...]
  
 
 0.973
Rpl34
60S ribosomal protein L34; Component of the large ribosomal subunit.
  
 
 0.973
Rpl23a
60S ribosomal protein L23a; Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. Binds a specific region on the 26S rRNA (By similarity). May promote p53/TP53 degradation possibly through the stimulation of MDM2-mediated TP53 polyubiquitination (By similarity); Belongs to the universal ribosomal protein uL23 family.
  
 
 0.973
Rps19
40S ribosomal protein S19; Required for pre-rRNA processing and maturation of 40S ribosomal subunits; Belongs to the eukaryotic ribosomal protein eS19 family.
   
 
 0.973
Rpl14
60S ribosomal protein L14; Component of the large ribosomal subunit. Belongs to the eukaryotic ribosomal protein eL14 family.
  
 
 0.973
Your Current Organism:
Mus musculus
NCBI taxonomy Id: 10090
Other names: LK3 transgenic mice, M. musculus, Mus sp. 129SV, house mouse, mouse, nude mice, transgenic mice
Server load: low (24%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.