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:
some 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
MAP1Methionine aminopeptidase; catalyzes the cotranslational removal of N-terminal methionine from nascent polypeptides; function is partially redundant with that of Map2p (387 aa)    
Predicted Functional Partners:
MAP2
Methionine aminopeptidase; catalyzes the cotranslational removal of N-terminal methionine from nascent polypeptides; function is partially redundant with that of Map1p; Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily
   
 
 0.999
YNR029C
Uncharacterized protein YNR029C; Putative protein of unknown function; deletion confers reduced fitness in saline
   
 
 0.979
ARD1
Subunit of protein N-terminal acetyltransferase NatA; NatA comprises Nat1p, Ard1p, Nat5p; acetylates many proteins to influence telomeric silencing, cell cycle, heat-shock resistance, mating, sporulation, early stages of mitophagy; protein abundance increases under DNA replication stress; mutations in human homolog X-linked NAA10 lead to Ogden syndrome (S37P) and intellectual disability (R116W); expression of human NAA10 and NAA15 can complement ard1 nat1 double mutant
   
 
 0.964
NAT5
N-alpha-acetyltransferase NAT5; Subunit of protein N-terminal acetyltransferase NatA; NatA is comprised of Nat1p, Ard1p, and Nat5p; N-terminally acetylates many proteins, which influences multiple processes such as the cell cycle, heat-shock resistance, mating, sporulation, and telomeric silencing; Belongs to the acetyltransferase family
   
 
 0.932
NAT1
Subunit of protein N-terminal acetyltransferase NatA; NatA comprised of Nat1p, Ard1p, and Nat5p; N-terminally acetylates many proteins to influence multiple processes such as cell cycle progression, heat-shock resistance, mating, sporulation, telomeric silencing and early stages of mitophagy; orthologous to human NAA15; expression of both human NAA10 and NAA15 functionally complements ard1 nat1 double mutant although single mutations are not complemented by their orthologs
   
 
 0.928
YHR112C
Uncharacterized trans-sulfuration enzyme YHR112C; Protein of unknown function; localizes to the cytoplasm and nucleus; overexpression affects protein trafficking through the endocytic pathway; Belongs to the trans-sulfuration enzymes family
  
  
 0.901
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
  
 
 0.765
RPL31A
Ribosomal 60S subunit protein L31A; associates with karyopherin Sxm1p; loss of both Rpl31p and Rpl39p confers lethality; homologous to mammalian ribosomal protein L31, no bacterial homolog; RPL31A has a paralog, RPL31B, that arose from the whole genome duplication
   
 
 0.721
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
  
 
 0.717
TCP1
Alpha subunit of chaperonin-containing T-complex; complex mediates protein folding in the cytosol; involved in actin cytoskeleton maintenance; overexpression in neurons suppresses formation of pathogenic conformations of huntingtin protein
  
  
 0.717
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: ATCC 18824, Candida robusta, NRRL Y-12632, S. cerevisiae, Saccharomyces capensis, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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