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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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Textmining
[Homology]
Score
RRD1Serine/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). (424 aa)    
Predicted Functional Partners:
PPH21
Serine/threonine-protein phosphatase.
    
 0.967
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.
   
 0.935
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.
   
 
 0.910
RRD2
Serine/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).
  
0.857
Q6FNB2_CANGA
Serine/threonine-protein phosphatase.
   
 0.856
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).
    
 0.819
TPD3
Uncharacterized protein.
   
 
 0.814
Q6FJC3_CANGA
Uncharacterized protein.
    
 0.809
Q6FRS6_CANGA
Uncharacterized protein.
   
 0.765
Q6FK70_CANGA
V-type proton ATPase subunit; Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. The active enzyme consists of a catalytic V1 domain attached to an integral membrane V0 proton pore complex. This subunit is a non-integral membrane component of the membrane pore domain and is required for proper assembly of the V0 sector. Might be involved in the regulated assembly of V1 subunits onto the membrane sector or alternatively may prevent the passage of protons through V0 pores; Belongs to the V-ATPase V0D/AC39 subunit family.
   
  
 0.757
Your Current Organism:
Candida glabrata
NCBI taxonomy Id: 284593
Other names: Candida glabrata ATCC 2001, Candida glabrata ATCC2001, Candida glabrata CBS 138, Candida glabrata CBS138, [. glabrata CBS 138, [Candida] glabrata CBS 138
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.