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PPH3 protein (Candida glabrata) - STRING interaction network
"PPH3" - Hypothetical protein in Candida glabrata
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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:
some 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
Others
textmining
co-expression
protein homology
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[Homology]
Score
PPH3Hypothetical protein; 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) (309 aa)    
Predicted Functional Partners:
XP_446032.1
Hypothetical protein (729 aa)
     
  0.970
XP_449044.1
Hypothetical protein (495 aa)
     
  0.968
XP_447068.1
Hypothetical protein (606 aa)
     
  0.962
TPD3
Hypothetical protein (611 aa)
     
  0.962
XP_449671.1
Hypothetical protein (375 aa)
     
 
  0.942
XP_445554.1
Hypothetical protein (2082 aa)
     
 
  0.940
PSY2
Hypothetical protein; 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) (842 aa)
       
  0.911
XP_448929.1
Hypothetical protein (1123 aa)
       
  0.891
XP_445269.1
Hypothetical protein (777 aa)
       
  0.891
RRD2
Hypothetical protein; 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) (358 aa)
     
  0.890
Your Current Organism:
Candida glabrata
NCBI taxonomy Id: 284593
Other names: C. glabrata, C. glabrata CBS 138, Candida glabrata, Candida glabrata ATCC 2001, Candida glabrata ATCC2001, Candida glabrata CBS 138, Candida glabrata CBS138, Nakaseomyces, Torulopsis glabrata, m. Nakaseomyces, mitosporic Nakaseomyces
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