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
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[Homology]
Score
RRD2Serine/threonine-protein phosphatase 2A activator 2; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A- phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity). (360 aa)    
Predicted Functional Partners:
KLLA0_F07689g
KLLA0F07689p.
   
 0.871
RRD1
Serine/threonine-protein phosphatase 2A activator 1; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A- phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity).
  
0.865
PPH3
Serine/threonine-protein phosphatase 4 catalytic subunit; Forms the histone H2A phosphatase complex in association with the regulatory subunits PSY2 and PSY4, which dephosphorylates H2AS128ph (gamma-H2A) that has been displaced from sites of DNA lesions in the double-stranded DNA break repair process. Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint (By similarity); Belongs to the PPP phosphatase family. PP-4 (PP-X) subfamily.
    
 0.839
KLLA0_F05357g
Serine/threonine-protein phosphatase.
    
 
 0.820
PSY2
Serine/threonine-protein phosphatase 4 regulatory subunit 3; Core regulatory subunit of the histone H2A phosphatase complex, which dephosphorylates H2AS128ph (gamma-H2A) that has been displaced from sites of DNA lesions in the double-stranded DNA break repair process. Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint (By similarity).
    
 0.797
KLLA0_C12793g
KLLA0C12793p.
    
 0.758
COQ7
5-demethoxyubiquinone hydroxylase, mitochondrial; Catalyzes the hydroxylation of 2-polyprenyl-3-methyl-6- methoxy-1,4-benzoquinol (DMQH2) during ubiquinone biosynthesis. Has also a structural role in the COQ enzyme complex, stabilizing other COQ polypeptides.
      
 0.664
PPM1
Leucine carboxyl methyltransferase 1; Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha- leucine ester residues; Belongs to the methyltransferase superfamily. LCMT family.
    
 
 0.653
KLLA0_D19316g
KLLA0D19316p.
    
 
 0.643
KLLA0_F08085g
Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit; The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.
    
 0.602
Your Current Organism:
Kluyveromyces lactis
NCBI taxonomy Id: 284590
Other names: K. lactis NRRL Y-1140, Kluyveromyces lactis NRRL Y-1140
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