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
TIF6Eukaryotic translation initiation factor 6; Constituent of 66S pre-ribosomal particles; has similarity to human translation initiation factor 6 (eIF6); may be involved in the biogenesis and or stability of 60S ribosomal subunits; Belongs to the eIF-6 family. (245 aa)    
Predicted Functional Partners:
RPL23A
Ribosomal 60S subunit protein L23A; homologous to mammalian ribosomal protein L23 and bacterial L14; RPL23A has a paralog, RPL23B, that arose from the whole genome duplication.
  
 
 0.999
REI1
Cytoplasmic pre-60S factor; required for the correct recycling of shuttling factors Alb1, Arx1 and Tif6 at the end of the ribosomal large subunit biogenesis; involved in bud growth in the mitotic signaling network.
   
 0.999
SPB1
27S pre-rRNA (guanosine(2922)-2'-O)-methyltransferase; AdoMet-dependent methyltransferase; involved in rRNA processing and 60S ribosomal subunit maturation; methylates G2922 in the tRNA docking site of the large subunit rRNA and in the absence of snR52, U2921; suppressor of PAB1 mutants.
   
 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
ARX1
Probable metalloprotease ARX1; Nuclear export factor for the ribosomal pre-60S subunit; shuttling factor which directly binds FG rich nucleoporins and facilities translocation through the nuclear pore complex; interacts directly with Alb1p; responsible for Tif6p recycling defects in the absence of Rei1; associated with the ribosomal export complex.
   
 0.999
NUG1
Nuclear GTP-binding protein NUG1; GTPase that associates with nuclear 60S pre-ribosomes; required for export of 60S ribosomal subunits from the nucleus.
   
 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
NSA2
Ribosome biogenesis protein NSA2; Protein constituent of 66S pre-ribosomal particles; contributes to processing of the 27S pre-rRNA; recruited by ribosomal proteins L17, L35, and L37 to assembling ribosomes after 27SB pre-rRNA is generated, immediately preceding removal of ITS2.
   
 0.999
RPL24A
Ribosomal 60S subunit protein L24A; not essential for translation but may be required for normal translation rate; homologous to mammalian ribosomal protein L24, no bacterial homolog; RPL24A has a paralog, RPL24B, 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
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.