STRINGSTRING
PTC5 PTC5 PTC7 PTC7 PTC6 PTC6 PDA1 PDA1 PKP2 PKP2 PKP1 PKP1 PTP1 PTP1 PTC1 PTC1 SDP1 SDP1 PPZ1 PPZ1 FMT1 FMT1
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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PTC5[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial; Mitochondrial type 2C protein phosphatase (PP2C); involved in regulation of pyruvate dehydrogenase activity by dephosphorylating the serine 133 of the Pda1p subunit; localizes to the intermembrane space and is imported via the presequence pathway and processed by the inner membrane protease (Imp1p-Imp2p); acts in concert with kinases Pkp1p and Pkp2p and phosphatase Ptc6p. (572 aa)    
Predicted Functional Partners:
PTC7
Type 2C serine/threonine protein phosphatase (PP2C); alternatively spliced to create two mRNA isoforms; protein from spliced form localizes to the mitochondria while the one from the unspliced form is localized to the nuclear envelope; activates coenzyme Q6 biosynthesis by dephosphorylation of demethoxy-Q6 hydroxylase Coq7p.
   
 
 0.922
PTC6
[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 2, mitochondrial; Mitochondrial type 2C protein phosphatase (PP2C); has similarity to mammalian PP1Ks; involved in mitophagy; null mutant is sensitive to rapamycin and has decreased phosphorylation of the Pda1 subunit of pyruvate dehydrogenase.
      
 0.914
PDA1
E1 alpha subunit of the pyruvate dehydrogenase (PDH) complex; catalyzes the direct oxidative decarboxylation of pyruvate to acetyl-CoA; phosphorylated; regulated by glucose; PDH complex is concentrated in spots within the mitochondrial matrix, often near the ERMES complex and near peroxisomes.
    
 
 0.871
PKP2
Mitochondrial protein kinase; negatively regulates activity of the pyruvate dehydrogenase complex by phosphorylating the ser-133 residue of the Pda1p subunit; acts in concert with kinase Pkp1p and phosphatases Ptc5p and Ptc6p; relocalizes from mitochondrion to cytoplasm upon DNA replication stress.
   
 
 0.734
PKP1
Mitochondrial protein kinase; involved in negative regulation of pyruvate dehydrogenase complex activity by phosphorylating the ser-133 residue of the Pda1p subunit; acts in concert with kinase Pkp2p and phosphatases Ptc5p and Ptc6p.
   
 
 0.689
PTP1
Tyrosine-protein phosphatase 1; Phosphotyrosine-specific protein phosphatase; dephosphorylates a broad range of substrates in vivo, including Fpr3p; localized to the cytoplasm and the mitochondria; proposed to be a negative regulator of filamentation; Belongs to the protein-tyrosine phosphatase family. Non- receptor class subfamily.
    
 
 0.676
PTC1
Type 2C protein phosphatase (PP2C); dephosphorylates Hog1p, inactivating osmosensing MAPK cascade; involved in Fus3p activation during pheromone response; deletion affects precursor tRNA splicing, mitochondrial inheritance, and sporulation.
    
 
 0.649
SDP1
Stress-inducible dual-specificity MAP kinase phosphatase; negatively regulates Slt2p MAP kinase by direct dephosphorylation, diffuse localization under normal conditions shifts to punctate localization after heat shock; SDP1 has a paralog, MSG5, that arose from the whole genome duplication; Belongs to the protein-tyrosine phosphatase family. Non- receptor class dual specificity subfamily.
   
 
 0.639
PPZ1
Serine/threonine-protein phosphatase PP-Z1; Serine/threonine protein phosphatase Z, isoform of Ppz2p; involved in regulation of potassium transport, which affects osmotic stability, cell cycle progression, and halotolerance; Belongs to the PPP phosphatase family. PP-Z subfamily.
    
 
 0.577
FMT1
Methionyl-tRNA formyltransferase, mitochondrial; Methionyl-tRNA formyltransferase; catalyzes the formylation of initiator Met-tRNA in mitochondria; potential Cdc28p substrate.
  
   0.575
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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