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MAP2 protein (Saccharomyces cerevisiae) - STRING interaction network
"MAP2" - Methionine aminopeptidase, catalyzes the cotranslational removal of N-terminal methionine from nascent polypeptides in Saccharomyces cerevisiae
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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MAP2Methionine aminopeptidase, catalyzes the cotranslational removal of N-terminal methionine from nascent polypeptides; function is partially redundant with that of Map1p; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Plays only a minor role in N-terminal methionine removal. Less efficient when the second residue is Val, Gly, Cys or Thr (421 aa)    
Predicted Functional Partners:
MAP1
Methionine aminopeptidase, catalyzes the cotranslational removal of N-terminal methionine from nascent polypeptides; function is partially redundant with that of Map2p; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Plays the major role in N-terminal methionine removal. Less efficient when the second residue is Val (387 aa)
     
 
  0.943
GPA2
Nucleotide binding alpha subunit of the heterotrimeric G protein; interacts with the receptor Gpr1p, has signaling role in response to nutrients; required for the recruitment of Ras-GTP at the plasma membrane and in the nucleus; Alpha subunit of the heterotrimeric guanine nucleotide- binding protein (G protein) involved in glucose-induced cAMP signaling. Binds to its cognate transmembrane receptor GPR1, which senses extracellular carbon sources, and activates cAMP-PKA signaling and governs diploid pseudohyphal differentiation and haploid invasive growth. The G protein beta-mimic protei [...] (449 aa)
         
  0.901
ICP55
Mitochondrial aminopeptidase; cleaves the N termini of at least 38 imported proteins after cleavage by the mitochondrial processing peptidase (MPP), thereby increasing their stability; member of the aminopeptidase P family; Aminopeptidase which cleaves preprotein intermediates that carry destabilizing N-ter amino acid residues after the mitochondrial processing peptidase (MPP) cleavage site and is thus critical for stabilization of the mitochondrial proteome (511 aa)
   
   
  0.843
MSF1
Mitochondrial phenylalanyl-tRNA synthetase, active as a monomer, unlike the cytoplasmic subunit which is active as a dimer complexed to a beta subunit dimer; similar to the alpha subunit of E. coli phenylalanyl-tRNA synthetase; Is responsible for the charging of tRNA(Phe) with phenylalanine in mitochondrial translation (469 aa)
   
   
  0.815
YNR029C
Putative protein of unknown function, deletion confers reduced fitness in saline (429 aa)
     
 
  0.801
ADE6
Formylglycinamidine-ribonucleotide (FGAM)-synthetase, catalyzes a step in the ’de novo’ purine nucleotide biosynthetic pathway; Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate (By similarity) (1358 aa)
   
   
  0.729
URA2
Bifunctional carbamoylphosphate synthetase/aspartate transcarbamylase; catalyzes the first two enzymatic steps in the de novo biosynthesis of pyrimidines; both activities are subject to feedback inhibition by UTP; This protein is a "fusion" protein encoding three enzymatic activities of the pyrimidine pathway (GATase, CPSase, and ATCase) (2214 aa)
   
   
  0.691
TMA46
Protein of unknown function that associates with translating ribosomes; interacts with GTPase Rbg1p (345 aa)
     
      0.671
RPL16A
N-terminally acetylated protein component of the large (60S) ribosomal subunit, binds to 5.8 S rRNA; has similarity to Rpl16Bp, E. coli L13 and rat L13a ribosomal proteins; transcriptionally regulated by Rap1p (199 aa)
   
 
  0.645
TUF1
Mitochondrial translation elongation factor Tu; comprises both GTPase and guanine nucleotide exchange factor activities, while these activities are found in separate proteins in S. pombe and humans; G-protein that, in its active GTP-bound form, binds to and delivers aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. In the presence of a correct codon-anticodon match between the aminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, the ribosome acts as a GTPase activator and the GTP is hydrolyzed. The inactive GDP-bound form leaves the ribosome and must be [...] (437 aa)
   
   
  0.614
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: Candida robusta, Pachytichospora, S. cerevisiae, Saccharomyces, Saccharomyces capensis, Saccharomyces cerevisiae, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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